data_4K29
# 
_entry.id   4K29 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4K29         pdb_00004k29 10.2210/pdb4k29/pdb 
RCSB  RCSB078799   ?            ?                   
WWPDB D_1000078799 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2013-04-24 
2 'Structure model' 1 1 2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'      
2 2 'Structure model' 'Database references'  
3 2 'Structure model' 'Derived calculations' 
4 2 'Structure model' 'Structure summary'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom            
2 2 'Structure model' chem_comp_bond            
3 2 'Structure model' database_2                
4 2 'Structure model' pdbx_entry_details        
5 2 'Structure model' pdbx_modification_feature 
6 2 'Structure model' struct_conn               
7 2 'Structure model' struct_ref_seq_dif        
8 2 'Structure model' struct_site               
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_database_2.pdbx_DOI'                
2 2 'Structure model' '_database_2.pdbx_database_accession' 
3 2 'Structure model' '_struct_conn.pdbx_leaving_atom_flag' 
4 2 'Structure model' '_struct_ref_seq_dif.details'         
5 2 'Structure model' '_struct_site.pdbx_auth_asym_id'      
6 2 'Structure model' '_struct_site.pdbx_auth_comp_id'      
7 2 'Structure model' '_struct_site.pdbx_auth_seq_id'       
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4K29 
_pdbx_database_status.recvd_initial_deposition_date   2013-04-08 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_database_related.db_name        TargetTrack 
_pdbx_database_related.db_id          NYSGRC-028229 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Eswaramoorthy, S.'                                         1  
'Chamala, S.'                                               2  
'Evans, B.'                                                 3  
'Foti, F.'                                                  4  
'Gizzi, A.'                                                 5  
'Hillerich, B.'                                             6  
'Kar, A.'                                                   7  
'Lafleur, J.'                                               8  
'Seidel, R.'                                                9  
'Villigas, G.'                                              10 
'Zencheck, W.'                                              11 
'Al Obaidi, N.'                                             12 
'Almo, S.C.'                                                13 
'Swaminathan, S.'                                           14 
'New York Structural Genomics Research Consortium (NYSGRC)' 15 
# 
_citation.id                        primary 
_citation.title                     'Crystal structure of an enoyl-CoA hydratase/isomerase from Xanthobacter autotrophicus Py2' 
_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.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Eswaramoorthy, S.' 1 ? 
primary 'Almo, S.C.'        2 ? 
primary 'Swaminathan, S.'   3 ? 
# 
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 'Enoyl-CoA hydratase/isomerase' 32567.848 3   ? ? ? ? 
2 non-polymer syn 'L(+)-TARTARIC ACID'            150.087   3   ? ? ? ? 
3 non-polymer syn GLYCEROL                        92.094    2   ? ? ? ? 
4 water       nat water                           18.015    564 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;(MSE)HHHHHHSSGVDLGTENLYFQS(MSE)TYSKILYETLHGVARITLNRPERTNALDQE(MSE)LGEINAA(MSE)DA
AEADAGVKAVIVRGAGNAFSSGFDLKAQ(MSE)EARPAGVDAWRPLLRKDFDTV(MSE)RFWHCPKPTIAAVRGPCLAGA
CELALACD(MSE)TIATEDAFFGEPELKFGAGIVV(MSE)LLPWIVGPKIAKEIILLGEDRVPARRAAEIG(MSE)VNRV
VDGDGLDAEALRIARHIGAIDPGLVKETKRALNRALETQG(MSE)LQALESALEIDLAIEGAGSPDKIAFFEVARRDGLR
AAIAWRDARFPARDA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHSSGVDLGTENLYFQSMTYSKILYETLHGVARITLNRPERTNALDQEMLGEINAAMDAAEADAGVKAVIVRGAG
NAFSSGFDLKAQMEARPAGVDAWRPLLRKDFDTVMRFWHCPKPTIAAVRGPCLAGACELALACDMTIATEDAFFGEPELK
FGAGIVVMLLPWIVGPKIAKEIILLGEDRVPARRAAEIGMVNRVVDGDGLDAEALRIARHIGAIDPGLVKETKRALNRAL
ETQGMLQALESALEIDLAIEGAGSPDKIAFFEVARRDGLRAAIAWRDARFPARDA
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         NYSGRC-028229 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'L(+)-TARTARIC ACID' TLA 
3 GLYCEROL             GOL 
4 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MSE n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   SER n 
1 9   SER n 
1 10  GLY n 
1 11  VAL n 
1 12  ASP n 
1 13  LEU n 
1 14  GLY n 
1 15  THR n 
1 16  GLU n 
1 17  ASN n 
1 18  LEU n 
1 19  TYR n 
1 20  PHE n 
1 21  GLN n 
1 22  SER n 
1 23  MSE n 
1 24  THR n 
1 25  TYR n 
1 26  SER n 
1 27  LYS n 
1 28  ILE n 
1 29  LEU n 
1 30  TYR n 
1 31  GLU n 
1 32  THR n 
1 33  LEU n 
1 34  HIS n 
1 35  GLY n 
1 36  VAL n 
1 37  ALA n 
1 38  ARG n 
1 39  ILE n 
1 40  THR n 
1 41  LEU n 
1 42  ASN n 
1 43  ARG n 
1 44  PRO n 
1 45  GLU n 
1 46  ARG n 
1 47  THR n 
1 48  ASN n 
1 49  ALA n 
1 50  LEU n 
1 51  ASP n 
1 52  GLN n 
1 53  GLU n 
1 54  MSE n 
1 55  LEU n 
1 56  GLY n 
1 57  GLU n 
1 58  ILE n 
1 59  ASN n 
1 60  ALA n 
1 61  ALA n 
1 62  MSE n 
1 63  ASP n 
1 64  ALA n 
1 65  ALA n 
1 66  GLU n 
1 67  ALA n 
1 68  ASP n 
1 69  ALA n 
1 70  GLY n 
1 71  VAL n 
1 72  LYS n 
1 73  ALA n 
1 74  VAL n 
1 75  ILE n 
1 76  VAL n 
1 77  ARG n 
1 78  GLY n 
1 79  ALA n 
1 80  GLY n 
1 81  ASN n 
1 82  ALA n 
1 83  PHE n 
1 84  SER n 
1 85  SER n 
1 86  GLY n 
1 87  PHE n 
1 88  ASP n 
1 89  LEU n 
1 90  LYS n 
1 91  ALA n 
1 92  GLN n 
1 93  MSE n 
1 94  GLU n 
1 95  ALA n 
1 96  ARG n 
1 97  PRO n 
1 98  ALA n 
1 99  GLY n 
1 100 VAL n 
1 101 ASP n 
1 102 ALA n 
1 103 TRP n 
1 104 ARG n 
1 105 PRO n 
1 106 LEU n 
1 107 LEU n 
1 108 ARG n 
1 109 LYS n 
1 110 ASP n 
1 111 PHE n 
1 112 ASP n 
1 113 THR n 
1 114 VAL n 
1 115 MSE n 
1 116 ARG n 
1 117 PHE n 
1 118 TRP n 
1 119 HIS n 
1 120 CYS n 
1 121 PRO n 
1 122 LYS n 
1 123 PRO n 
1 124 THR n 
1 125 ILE n 
1 126 ALA n 
1 127 ALA n 
1 128 VAL n 
1 129 ARG n 
1 130 GLY n 
1 131 PRO n 
1 132 CYS n 
1 133 LEU n 
1 134 ALA n 
1 135 GLY n 
1 136 ALA n 
1 137 CYS n 
1 138 GLU n 
1 139 LEU n 
1 140 ALA n 
1 141 LEU n 
1 142 ALA n 
1 143 CYS n 
1 144 ASP n 
1 145 MSE n 
1 146 THR n 
1 147 ILE n 
1 148 ALA n 
1 149 THR n 
1 150 GLU n 
1 151 ASP n 
1 152 ALA n 
1 153 PHE n 
1 154 PHE n 
1 155 GLY n 
1 156 GLU n 
1 157 PRO n 
1 158 GLU n 
1 159 LEU n 
1 160 LYS n 
1 161 PHE n 
1 162 GLY n 
1 163 ALA n 
1 164 GLY n 
1 165 ILE n 
1 166 VAL n 
1 167 VAL n 
1 168 MSE n 
1 169 LEU n 
1 170 LEU n 
1 171 PRO n 
1 172 TRP n 
1 173 ILE n 
1 174 VAL n 
1 175 GLY n 
1 176 PRO n 
1 177 LYS n 
1 178 ILE n 
1 179 ALA n 
1 180 LYS n 
1 181 GLU n 
1 182 ILE n 
1 183 ILE n 
1 184 LEU n 
1 185 LEU n 
1 186 GLY n 
1 187 GLU n 
1 188 ASP n 
1 189 ARG n 
1 190 VAL n 
1 191 PRO n 
1 192 ALA n 
1 193 ARG n 
1 194 ARG n 
1 195 ALA n 
1 196 ALA n 
1 197 GLU n 
1 198 ILE n 
1 199 GLY n 
1 200 MSE n 
1 201 VAL n 
1 202 ASN n 
1 203 ARG n 
1 204 VAL n 
1 205 VAL n 
1 206 ASP n 
1 207 GLY n 
1 208 ASP n 
1 209 GLY n 
1 210 LEU n 
1 211 ASP n 
1 212 ALA n 
1 213 GLU n 
1 214 ALA n 
1 215 LEU n 
1 216 ARG n 
1 217 ILE n 
1 218 ALA n 
1 219 ARG n 
1 220 HIS n 
1 221 ILE n 
1 222 GLY n 
1 223 ALA n 
1 224 ILE n 
1 225 ASP n 
1 226 PRO n 
1 227 GLY n 
1 228 LEU n 
1 229 VAL n 
1 230 LYS n 
1 231 GLU n 
1 232 THR n 
1 233 LYS n 
1 234 ARG n 
1 235 ALA n 
1 236 LEU n 
1 237 ASN n 
1 238 ARG n 
1 239 ALA n 
1 240 LEU n 
1 241 GLU n 
1 242 THR n 
1 243 GLN n 
1 244 GLY n 
1 245 MSE n 
1 246 LEU n 
1 247 GLN n 
1 248 ALA n 
1 249 LEU n 
1 250 GLU n 
1 251 SER n 
1 252 ALA n 
1 253 LEU n 
1 254 GLU n 
1 255 ILE n 
1 256 ASP n 
1 257 LEU n 
1 258 ALA n 
1 259 ILE n 
1 260 GLU n 
1 261 GLY n 
1 262 ALA n 
1 263 GLY n 
1 264 SER n 
1 265 PRO n 
1 266 ASP n 
1 267 LYS n 
1 268 ILE n 
1 269 ALA n 
1 270 PHE n 
1 271 PHE n 
1 272 GLU n 
1 273 VAL n 
1 274 ALA n 
1 275 ARG n 
1 276 ARG n 
1 277 ASP n 
1 278 GLY n 
1 279 LEU n 
1 280 ARG n 
1 281 ALA n 
1 282 ALA n 
1 283 ILE n 
1 284 ALA n 
1 285 TRP n 
1 286 ARG n 
1 287 ASP n 
1 288 ALA n 
1 289 ARG n 
1 290 PHE n 
1 291 PRO n 
1 292 ALA n 
1 293 ARG n 
1 294 ASP n 
1 295 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Xaut_3350 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    Py2 
_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      'Xanthobacter autotrophicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     78245 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_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               BL21 
_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                       pET3A 
_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 
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  
GOL non-polymer         . GLYCEROL             'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
MSE 'L-peptide linking' n SELENOMETHIONINE     ?                               'C5 H11 N O2 Se' 196.106 
PHE 'L-peptide linking' y PHENYLALANINE        ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE              ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE               ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE            ?                               'C4 H9 N O3'     119.119 
TLA non-polymer         . 'L(+)-TARTARIC ACID' ?                               'C4 H6 O6'       150.087 
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   MSE 1   -21 ?   ?   ?   A . n 
A 1 2   HIS 2   -20 ?   ?   ?   A . n 
A 1 3   HIS 3   -19 ?   ?   ?   A . n 
A 1 4   HIS 4   -18 ?   ?   ?   A . n 
A 1 5   HIS 5   -17 ?   ?   ?   A . n 
A 1 6   HIS 6   -16 ?   ?   ?   A . n 
A 1 7   HIS 7   -15 ?   ?   ?   A . n 
A 1 8   SER 8   -14 ?   ?   ?   A . n 
A 1 9   SER 9   -13 ?   ?   ?   A . n 
A 1 10  GLY 10  -12 ?   ?   ?   A . n 
A 1 11  VAL 11  -11 ?   ?   ?   A . n 
A 1 12  ASP 12  -10 ?   ?   ?   A . n 
A 1 13  LEU 13  -9  ?   ?   ?   A . n 
A 1 14  GLY 14  -8  ?   ?   ?   A . n 
A 1 15  THR 15  -7  ?   ?   ?   A . n 
A 1 16  GLU 16  -6  ?   ?   ?   A . n 
A 1 17  ASN 17  -5  ?   ?   ?   A . n 
A 1 18  LEU 18  -4  ?   ?   ?   A . n 
A 1 19  TYR 19  -3  ?   ?   ?   A . n 
A 1 20  PHE 20  -2  ?   ?   ?   A . n 
A 1 21  GLN 21  -1  ?   ?   ?   A . n 
A 1 22  SER 22  0   ?   ?   ?   A . n 
A 1 23  MSE 23  1   ?   ?   ?   A . n 
A 1 24  THR 24  2   2   THR THR A . n 
A 1 25  TYR 25  3   3   TYR TYR A . n 
A 1 26  SER 26  4   4   SER SER A . n 
A 1 27  LYS 27  5   5   LYS LYS A . n 
A 1 28  ILE 28  6   6   ILE ILE A . n 
A 1 29  LEU 29  7   7   LEU LEU A . n 
A 1 30  TYR 30  8   8   TYR TYR A . n 
A 1 31  GLU 31  9   9   GLU GLU A . n 
A 1 32  THR 32  10  10  THR THR A . n 
A 1 33  LEU 33  11  11  LEU LEU A . n 
A 1 34  HIS 34  12  12  HIS HIS A . n 
A 1 35  GLY 35  13  13  GLY GLY A . n 
A 1 36  VAL 36  14  14  VAL VAL A . n 
A 1 37  ALA 37  15  15  ALA ALA A . n 
A 1 38  ARG 38  16  16  ARG ARG A . n 
A 1 39  ILE 39  17  17  ILE ILE A . n 
A 1 40  THR 40  18  18  THR THR A . n 
A 1 41  LEU 41  19  19  LEU LEU A . n 
A 1 42  ASN 42  20  20  ASN ASN A . n 
A 1 43  ARG 43  21  21  ARG ARG A . n 
A 1 44  PRO 44  22  22  PRO PRO A . n 
A 1 45  GLU 45  23  23  GLU GLU A . n 
A 1 46  ARG 46  24  24  ARG ARG A . n 
A 1 47  THR 47  25  25  THR THR A . n 
A 1 48  ASN 48  26  26  ASN ASN A . n 
A 1 49  ALA 49  27  27  ALA ALA A . n 
A 1 50  LEU 50  28  28  LEU LEU A . n 
A 1 51  ASP 51  29  29  ASP ASP A . n 
A 1 52  GLN 52  30  30  GLN GLN A . n 
A 1 53  GLU 53  31  31  GLU GLU A . n 
A 1 54  MSE 54  32  32  MSE MSE A . n 
A 1 55  LEU 55  33  33  LEU LEU A . n 
A 1 56  GLY 56  34  34  GLY GLY A . n 
A 1 57  GLU 57  35  35  GLU GLU A . n 
A 1 58  ILE 58  36  36  ILE ILE A . n 
A 1 59  ASN 59  37  37  ASN ASN A . n 
A 1 60  ALA 60  38  38  ALA ALA A . n 
A 1 61  ALA 61  39  39  ALA ALA A . n 
A 1 62  MSE 62  40  40  MSE MSE A . n 
A 1 63  ASP 63  41  41  ASP ASP A . n 
A 1 64  ALA 64  42  42  ALA ALA A . n 
A 1 65  ALA 65  43  43  ALA ALA A . n 
A 1 66  GLU 66  44  44  GLU GLU A . n 
A 1 67  ALA 67  45  45  ALA ALA A . n 
A 1 68  ASP 68  46  46  ASP ASP A . n 
A 1 69  ALA 69  47  47  ALA ALA A . n 
A 1 70  GLY 70  48  48  GLY GLY A . n 
A 1 71  VAL 71  49  49  VAL VAL A . n 
A 1 72  LYS 72  50  50  LYS LYS A . n 
A 1 73  ALA 73  51  51  ALA ALA A . n 
A 1 74  VAL 74  52  52  VAL VAL A . n 
A 1 75  ILE 75  53  53  ILE ILE A . n 
A 1 76  VAL 76  54  54  VAL VAL A . n 
A 1 77  ARG 77  55  55  ARG ARG A . n 
A 1 78  GLY 78  56  56  GLY GLY A . n 
A 1 79  ALA 79  57  57  ALA ALA A . n 
A 1 80  GLY 80  58  58  GLY GLY A . n 
A 1 81  ASN 81  59  59  ASN ASN A . n 
A 1 82  ALA 82  60  60  ALA ALA A . n 
A 1 83  PHE 83  61  61  PHE PHE A . n 
A 1 84  SER 84  62  62  SER SER A . n 
A 1 85  SER 85  63  63  SER SER A . n 
A 1 86  GLY 86  64  64  GLY GLY A . n 
A 1 87  PHE 87  65  65  PHE PHE A . n 
A 1 88  ASP 88  66  66  ASP ASP A . n 
A 1 89  LEU 89  67  67  LEU LEU A . n 
A 1 90  LYS 90  68  68  LYS LYS A . n 
A 1 91  ALA 91  69  69  ALA ALA A . n 
A 1 92  GLN 92  70  70  GLN GLN A . n 
A 1 93  MSE 93  71  71  MSE MSE A . n 
A 1 94  GLU 94  72  72  GLU GLU A . n 
A 1 95  ALA 95  73  73  ALA ALA A . n 
A 1 96  ARG 96  74  74  ARG ARG A . n 
A 1 97  PRO 97  75  75  PRO PRO A . n 
A 1 98  ALA 98  76  76  ALA ALA A . n 
A 1 99  GLY 99  77  77  GLY GLY A . n 
A 1 100 VAL 100 78  78  VAL VAL A . n 
A 1 101 ASP 101 79  79  ASP ASP A . n 
A 1 102 ALA 102 80  80  ALA ALA A . n 
A 1 103 TRP 103 81  81  TRP TRP A . n 
A 1 104 ARG 104 82  82  ARG ARG A . n 
A 1 105 PRO 105 83  83  PRO PRO A . n 
A 1 106 LEU 106 84  84  LEU LEU A . n 
A 1 107 LEU 107 85  85  LEU LEU A . n 
A 1 108 ARG 108 86  86  ARG ARG A . n 
A 1 109 LYS 109 87  87  LYS LYS A . n 
A 1 110 ASP 110 88  88  ASP ASP A . n 
A 1 111 PHE 111 89  89  PHE PHE A . n 
A 1 112 ASP 112 90  90  ASP ASP A . n 
A 1 113 THR 113 91  91  THR THR A . n 
A 1 114 VAL 114 92  92  VAL VAL A . n 
A 1 115 MSE 115 93  93  MSE MSE A . n 
A 1 116 ARG 116 94  94  ARG ARG A . n 
A 1 117 PHE 117 95  95  PHE PHE A . n 
A 1 118 TRP 118 96  96  TRP TRP A . n 
A 1 119 HIS 119 97  97  HIS HIS A . n 
A 1 120 CYS 120 98  98  CYS CYS A . n 
A 1 121 PRO 121 99  99  PRO PRO A . n 
A 1 122 LYS 122 100 100 LYS LYS A . n 
A 1 123 PRO 123 101 101 PRO PRO A . n 
A 1 124 THR 124 102 102 THR THR A . n 
A 1 125 ILE 125 103 103 ILE ILE A . n 
A 1 126 ALA 126 104 104 ALA ALA A . n 
A 1 127 ALA 127 105 105 ALA ALA A . n 
A 1 128 VAL 128 106 106 VAL VAL A . n 
A 1 129 ARG 129 107 107 ARG ARG A . n 
A 1 130 GLY 130 108 108 GLY GLY A . n 
A 1 131 PRO 131 109 109 PRO PRO A . n 
A 1 132 CYS 132 110 110 CYS CYS A . n 
A 1 133 LEU 133 111 111 LEU LEU A . n 
A 1 134 ALA 134 112 112 ALA ALA A . n 
A 1 135 GLY 135 113 113 GLY GLY A . n 
A 1 136 ALA 136 114 114 ALA ALA A . n 
A 1 137 CYS 137 115 115 CYS CYS A . n 
A 1 138 GLU 138 116 116 GLU GLU A . n 
A 1 139 LEU 139 117 117 LEU LEU A . n 
A 1 140 ALA 140 118 118 ALA ALA A . n 
A 1 141 LEU 141 119 119 LEU LEU A . n 
A 1 142 ALA 142 120 120 ALA ALA A . n 
A 1 143 CYS 143 121 121 CYS CYS A . n 
A 1 144 ASP 144 122 122 ASP ASP A . n 
A 1 145 MSE 145 123 123 MSE MSE A . n 
A 1 146 THR 146 124 124 THR THR A . n 
A 1 147 ILE 147 125 125 ILE ILE A . n 
A 1 148 ALA 148 126 126 ALA ALA A . n 
A 1 149 THR 149 127 127 THR THR A . n 
A 1 150 GLU 150 128 128 GLU GLU A . n 
A 1 151 ASP 151 129 129 ASP ASP A . n 
A 1 152 ALA 152 130 130 ALA ALA A . n 
A 1 153 PHE 153 131 131 PHE PHE A . n 
A 1 154 PHE 154 132 132 PHE PHE A . n 
A 1 155 GLY 155 133 133 GLY GLY A . n 
A 1 156 GLU 156 134 134 GLU GLU A . n 
A 1 157 PRO 157 135 135 PRO PRO A . n 
A 1 158 GLU 158 136 136 GLU GLU A . n 
A 1 159 LEU 159 137 137 LEU LEU A . n 
A 1 160 LYS 160 138 138 LYS LYS A . n 
A 1 161 PHE 161 139 139 PHE PHE A . n 
A 1 162 GLY 162 140 140 GLY GLY A . n 
A 1 163 ALA 163 141 141 ALA ALA A . n 
A 1 164 GLY 164 142 142 GLY GLY A . n 
A 1 165 ILE 165 143 143 ILE ILE A . n 
A 1 166 VAL 166 144 144 VAL VAL A . n 
A 1 167 VAL 167 145 145 VAL VAL A . n 
A 1 168 MSE 168 146 146 MSE MSE A . n 
A 1 169 LEU 169 147 147 LEU LEU A . n 
A 1 170 LEU 170 148 148 LEU LEU A . n 
A 1 171 PRO 171 149 149 PRO PRO A . n 
A 1 172 TRP 172 150 150 TRP TRP A . n 
A 1 173 ILE 173 151 151 ILE ILE A . n 
A 1 174 VAL 174 152 152 VAL VAL A . n 
A 1 175 GLY 175 153 153 GLY GLY A . n 
A 1 176 PRO 176 154 154 PRO PRO A . n 
A 1 177 LYS 177 155 155 LYS LYS A . n 
A 1 178 ILE 178 156 156 ILE ILE A . n 
A 1 179 ALA 179 157 157 ALA ALA A . n 
A 1 180 LYS 180 158 158 LYS LYS A . n 
A 1 181 GLU 181 159 159 GLU GLU A . n 
A 1 182 ILE 182 160 160 ILE ILE A . n 
A 1 183 ILE 183 161 161 ILE ILE A . n 
A 1 184 LEU 184 162 162 LEU LEU A . n 
A 1 185 LEU 185 163 163 LEU LEU A . n 
A 1 186 GLY 186 164 164 GLY GLY A . n 
A 1 187 GLU 187 165 165 GLU GLU A . n 
A 1 188 ASP 188 166 166 ASP ASP A . n 
A 1 189 ARG 189 167 167 ARG ARG A . n 
A 1 190 VAL 190 168 168 VAL VAL A . n 
A 1 191 PRO 191 169 169 PRO PRO A . n 
A 1 192 ALA 192 170 170 ALA ALA A . n 
A 1 193 ARG 193 171 171 ARG ARG A . n 
A 1 194 ARG 194 172 172 ARG ARG A . n 
A 1 195 ALA 195 173 173 ALA ALA A . n 
A 1 196 ALA 196 174 174 ALA ALA A . n 
A 1 197 GLU 197 175 175 GLU GLU A . n 
A 1 198 ILE 198 176 176 ILE ILE A . n 
A 1 199 GLY 199 177 177 GLY GLY A . n 
A 1 200 MSE 200 178 178 MSE MSE A . n 
A 1 201 VAL 201 179 179 VAL VAL A . n 
A 1 202 ASN 202 180 180 ASN ASN A . n 
A 1 203 ARG 203 181 181 ARG ARG A . n 
A 1 204 VAL 204 182 182 VAL VAL A . n 
A 1 205 VAL 205 183 183 VAL VAL A . n 
A 1 206 ASP 206 184 184 ASP ASP A . n 
A 1 207 GLY 207 185 185 GLY GLY A . n 
A 1 208 ASP 208 186 186 ASP ASP A . n 
A 1 209 GLY 209 187 187 GLY GLY A . n 
A 1 210 LEU 210 188 188 LEU LEU A . n 
A 1 211 ASP 211 189 189 ASP ASP A . n 
A 1 212 ALA 212 190 190 ALA ALA A . n 
A 1 213 GLU 213 191 191 GLU GLU A . n 
A 1 214 ALA 214 192 192 ALA ALA A . n 
A 1 215 LEU 215 193 193 LEU LEU A . n 
A 1 216 ARG 216 194 194 ARG ARG A . n 
A 1 217 ILE 217 195 195 ILE ILE A . n 
A 1 218 ALA 218 196 196 ALA ALA A . n 
A 1 219 ARG 219 197 197 ARG ARG A . n 
A 1 220 HIS 220 198 198 HIS HIS A . n 
A 1 221 ILE 221 199 199 ILE ILE A . n 
A 1 222 GLY 222 200 200 GLY GLY A . n 
A 1 223 ALA 223 201 201 ALA ALA A . n 
A 1 224 ILE 224 202 202 ILE ILE A . n 
A 1 225 ASP 225 203 203 ASP ASP A . n 
A 1 226 PRO 226 204 204 PRO PRO A . n 
A 1 227 GLY 227 205 205 GLY GLY A . n 
A 1 228 LEU 228 206 206 LEU LEU A . n 
A 1 229 VAL 229 207 207 VAL VAL A . n 
A 1 230 LYS 230 208 208 LYS LYS A . n 
A 1 231 GLU 231 209 209 GLU GLU A . n 
A 1 232 THR 232 210 210 THR THR A . n 
A 1 233 LYS 233 211 211 LYS LYS A . n 
A 1 234 ARG 234 212 212 ARG ARG A . n 
A 1 235 ALA 235 213 213 ALA ALA A . n 
A 1 236 LEU 236 214 214 LEU LEU A . n 
A 1 237 ASN 237 215 215 ASN ASN A . n 
A 1 238 ARG 238 216 216 ARG ARG A . n 
A 1 239 ALA 239 217 217 ALA ALA A . n 
A 1 240 LEU 240 218 218 LEU LEU A . n 
A 1 241 GLU 241 219 219 GLU GLU A . n 
A 1 242 THR 242 220 220 THR THR A . n 
A 1 243 GLN 243 221 221 GLN GLN A . n 
A 1 244 GLY 244 222 222 GLY GLY A . n 
A 1 245 MSE 245 223 223 MSE MSE A . n 
A 1 246 LEU 246 224 224 LEU LEU A . n 
A 1 247 GLN 247 225 225 GLN GLN A . n 
A 1 248 ALA 248 226 226 ALA ALA A . n 
A 1 249 LEU 249 227 227 LEU LEU A . n 
A 1 250 GLU 250 228 228 GLU GLU A . n 
A 1 251 SER 251 229 229 SER SER A . n 
A 1 252 ALA 252 230 230 ALA ALA A . n 
A 1 253 LEU 253 231 231 LEU LEU A . n 
A 1 254 GLU 254 232 232 GLU GLU A . n 
A 1 255 ILE 255 233 233 ILE ILE A . n 
A 1 256 ASP 256 234 234 ASP ASP A . n 
A 1 257 LEU 257 235 235 LEU LEU A . n 
A 1 258 ALA 258 236 236 ALA ALA A . n 
A 1 259 ILE 259 237 237 ILE ILE A . n 
A 1 260 GLU 260 238 238 GLU GLU A . n 
A 1 261 GLY 261 239 239 GLY GLY A . n 
A 1 262 ALA 262 240 240 ALA ALA A . n 
A 1 263 GLY 263 241 241 GLY GLY A . n 
A 1 264 SER 264 242 242 SER SER A . n 
A 1 265 PRO 265 243 243 PRO PRO A . n 
A 1 266 ASP 266 244 244 ASP ASP A . n 
A 1 267 LYS 267 245 245 LYS LYS A . n 
A 1 268 ILE 268 246 246 ILE ILE A . n 
A 1 269 ALA 269 247 247 ALA ALA A . n 
A 1 270 PHE 270 248 248 PHE PHE A . n 
A 1 271 PHE 271 249 249 PHE PHE A . n 
A 1 272 GLU 272 250 250 GLU GLU A . n 
A 1 273 VAL 273 251 251 VAL VAL A . n 
A 1 274 ALA 274 252 252 ALA ALA A . n 
A 1 275 ARG 275 253 253 ARG ARG A . n 
A 1 276 ARG 276 254 254 ARG ARG A . n 
A 1 277 ASP 277 255 255 ASP ASP A . n 
A 1 278 GLY 278 256 256 GLY GLY A . n 
A 1 279 LEU 279 257 257 LEU LEU A . n 
A 1 280 ARG 280 258 258 ARG ARG A . n 
A 1 281 ALA 281 259 259 ALA ALA A . n 
A 1 282 ALA 282 260 260 ALA ALA A . n 
A 1 283 ILE 283 261 261 ILE ILE A . n 
A 1 284 ALA 284 262 262 ALA ALA A . n 
A 1 285 TRP 285 263 263 TRP TRP A . n 
A 1 286 ARG 286 264 264 ARG ARG A . n 
A 1 287 ASP 287 265 265 ASP ASP A . n 
A 1 288 ALA 288 266 266 ALA ALA A . n 
A 1 289 ARG 289 267 267 ARG ARG A . n 
A 1 290 PHE 290 268 268 PHE PHE A . n 
A 1 291 PRO 291 269 269 PRO PRO A . n 
A 1 292 ALA 292 270 270 ALA ALA A . n 
A 1 293 ARG 293 271 ?   ?   ?   A . n 
A 1 294 ASP 294 272 ?   ?   ?   A . n 
A 1 295 ALA 295 273 ?   ?   ?   A . n 
B 1 1   MSE 1   -21 ?   ?   ?   B . n 
B 1 2   HIS 2   -20 ?   ?   ?   B . n 
B 1 3   HIS 3   -19 ?   ?   ?   B . n 
B 1 4   HIS 4   -18 ?   ?   ?   B . n 
B 1 5   HIS 5   -17 ?   ?   ?   B . n 
B 1 6   HIS 6   -16 ?   ?   ?   B . n 
B 1 7   HIS 7   -15 ?   ?   ?   B . n 
B 1 8   SER 8   -14 ?   ?   ?   B . n 
B 1 9   SER 9   -13 ?   ?   ?   B . n 
B 1 10  GLY 10  -12 ?   ?   ?   B . n 
B 1 11  VAL 11  -11 ?   ?   ?   B . n 
B 1 12  ASP 12  -10 ?   ?   ?   B . n 
B 1 13  LEU 13  -9  ?   ?   ?   B . n 
B 1 14  GLY 14  -8  ?   ?   ?   B . n 
B 1 15  THR 15  -7  ?   ?   ?   B . n 
B 1 16  GLU 16  -6  ?   ?   ?   B . n 
B 1 17  ASN 17  -5  ?   ?   ?   B . n 
B 1 18  LEU 18  -4  ?   ?   ?   B . n 
B 1 19  TYR 19  -3  ?   ?   ?   B . n 
B 1 20  PHE 20  -2  ?   ?   ?   B . n 
B 1 21  GLN 21  -1  ?   ?   ?   B . n 
B 1 22  SER 22  0   ?   ?   ?   B . n 
B 1 23  MSE 23  1   ?   ?   ?   B . n 
B 1 24  THR 24  2   ?   ?   ?   B . n 
B 1 25  TYR 25  3   3   TYR TYR B . n 
B 1 26  SER 26  4   4   SER SER B . n 
B 1 27  LYS 27  5   5   LYS LYS B . n 
B 1 28  ILE 28  6   6   ILE ILE B . n 
B 1 29  LEU 29  7   7   LEU LEU B . n 
B 1 30  TYR 30  8   8   TYR TYR B . n 
B 1 31  GLU 31  9   9   GLU GLU B . n 
B 1 32  THR 32  10  10  THR THR B . n 
B 1 33  LEU 33  11  11  LEU LEU B . n 
B 1 34  HIS 34  12  12  HIS HIS B . n 
B 1 35  GLY 35  13  13  GLY GLY B . n 
B 1 36  VAL 36  14  14  VAL VAL B . n 
B 1 37  ALA 37  15  15  ALA ALA B . n 
B 1 38  ARG 38  16  16  ARG ARG B . n 
B 1 39  ILE 39  17  17  ILE ILE B . n 
B 1 40  THR 40  18  18  THR THR B . n 
B 1 41  LEU 41  19  19  LEU LEU B . n 
B 1 42  ASN 42  20  20  ASN ASN B . n 
B 1 43  ARG 43  21  21  ARG ARG B . n 
B 1 44  PRO 44  22  22  PRO PRO B . n 
B 1 45  GLU 45  23  23  GLU GLU B . n 
B 1 46  ARG 46  24  24  ARG ARG B . n 
B 1 47  THR 47  25  25  THR THR B . n 
B 1 48  ASN 48  26  26  ASN ASN B . n 
B 1 49  ALA 49  27  27  ALA ALA B . n 
B 1 50  LEU 50  28  28  LEU LEU B . n 
B 1 51  ASP 51  29  29  ASP ASP B . n 
B 1 52  GLN 52  30  30  GLN GLN B . n 
B 1 53  GLU 53  31  31  GLU GLU B . n 
B 1 54  MSE 54  32  32  MSE MSE B . n 
B 1 55  LEU 55  33  33  LEU LEU B . n 
B 1 56  GLY 56  34  34  GLY GLY B . n 
B 1 57  GLU 57  35  35  GLU GLU B . n 
B 1 58  ILE 58  36  36  ILE ILE B . n 
B 1 59  ASN 59  37  37  ASN ASN B . n 
B 1 60  ALA 60  38  38  ALA ALA B . n 
B 1 61  ALA 61  39  39  ALA ALA B . n 
B 1 62  MSE 62  40  40  MSE MSE B . n 
B 1 63  ASP 63  41  41  ASP ASP B . n 
B 1 64  ALA 64  42  42  ALA ALA B . n 
B 1 65  ALA 65  43  43  ALA ALA B . n 
B 1 66  GLU 66  44  44  GLU GLU B . n 
B 1 67  ALA 67  45  45  ALA ALA B . n 
B 1 68  ASP 68  46  46  ASP ASP B . n 
B 1 69  ALA 69  47  47  ALA ALA B . n 
B 1 70  GLY 70  48  48  GLY GLY B . n 
B 1 71  VAL 71  49  49  VAL VAL B . n 
B 1 72  LYS 72  50  50  LYS LYS B . n 
B 1 73  ALA 73  51  51  ALA ALA B . n 
B 1 74  VAL 74  52  52  VAL VAL B . n 
B 1 75  ILE 75  53  53  ILE ILE B . n 
B 1 76  VAL 76  54  54  VAL VAL B . n 
B 1 77  ARG 77  55  55  ARG ARG B . n 
B 1 78  GLY 78  56  56  GLY GLY B . n 
B 1 79  ALA 79  57  57  ALA ALA B . n 
B 1 80  GLY 80  58  58  GLY GLY B . n 
B 1 81  ASN 81  59  59  ASN ASN B . n 
B 1 82  ALA 82  60  60  ALA ALA B . n 
B 1 83  PHE 83  61  61  PHE PHE B . n 
B 1 84  SER 84  62  62  SER SER B . n 
B 1 85  SER 85  63  63  SER SER B . n 
B 1 86  GLY 86  64  64  GLY GLY B . n 
B 1 87  PHE 87  65  65  PHE PHE B . n 
B 1 88  ASP 88  66  66  ASP ASP B . n 
B 1 89  LEU 89  67  67  LEU LEU B . n 
B 1 90  LYS 90  68  68  LYS LYS B . n 
B 1 91  ALA 91  69  69  ALA ALA B . n 
B 1 92  GLN 92  70  70  GLN GLN B . n 
B 1 93  MSE 93  71  71  MSE MSE B . n 
B 1 94  GLU 94  72  72  GLU GLU B . n 
B 1 95  ALA 95  73  73  ALA ALA B . n 
B 1 96  ARG 96  74  74  ARG ARG B . n 
B 1 97  PRO 97  75  75  PRO PRO B . n 
B 1 98  ALA 98  76  76  ALA ALA B . n 
B 1 99  GLY 99  77  77  GLY GLY B . n 
B 1 100 VAL 100 78  78  VAL VAL B . n 
B 1 101 ASP 101 79  79  ASP ASP B . n 
B 1 102 ALA 102 80  80  ALA ALA B . n 
B 1 103 TRP 103 81  81  TRP TRP B . n 
B 1 104 ARG 104 82  82  ARG ARG B . n 
B 1 105 PRO 105 83  83  PRO PRO B . n 
B 1 106 LEU 106 84  84  LEU LEU B . n 
B 1 107 LEU 107 85  85  LEU LEU B . n 
B 1 108 ARG 108 86  86  ARG ARG B . n 
B 1 109 LYS 109 87  87  LYS LYS B . n 
B 1 110 ASP 110 88  88  ASP ASP B . n 
B 1 111 PHE 111 89  89  PHE PHE B . n 
B 1 112 ASP 112 90  90  ASP ASP B . n 
B 1 113 THR 113 91  91  THR THR B . n 
B 1 114 VAL 114 92  92  VAL VAL B . n 
B 1 115 MSE 115 93  93  MSE MSE B . n 
B 1 116 ARG 116 94  94  ARG ARG B . n 
B 1 117 PHE 117 95  95  PHE PHE B . n 
B 1 118 TRP 118 96  96  TRP TRP B . n 
B 1 119 HIS 119 97  97  HIS HIS B . n 
B 1 120 CYS 120 98  98  CYS CYS B . n 
B 1 121 PRO 121 99  99  PRO PRO B . n 
B 1 122 LYS 122 100 100 LYS LYS B . n 
B 1 123 PRO 123 101 101 PRO PRO B . n 
B 1 124 THR 124 102 102 THR THR B . n 
B 1 125 ILE 125 103 103 ILE ILE B . n 
B 1 126 ALA 126 104 104 ALA ALA B . n 
B 1 127 ALA 127 105 105 ALA ALA B . n 
B 1 128 VAL 128 106 106 VAL VAL B . n 
B 1 129 ARG 129 107 107 ARG ARG B . n 
B 1 130 GLY 130 108 108 GLY GLY B . n 
B 1 131 PRO 131 109 109 PRO PRO B . n 
B 1 132 CYS 132 110 110 CYS CYS B . n 
B 1 133 LEU 133 111 111 LEU LEU B . n 
B 1 134 ALA 134 112 112 ALA ALA B . n 
B 1 135 GLY 135 113 113 GLY GLY B . n 
B 1 136 ALA 136 114 114 ALA ALA B . n 
B 1 137 CYS 137 115 115 CYS CYS B . n 
B 1 138 GLU 138 116 116 GLU GLU B . n 
B 1 139 LEU 139 117 117 LEU LEU B . n 
B 1 140 ALA 140 118 118 ALA ALA B . n 
B 1 141 LEU 141 119 119 LEU LEU B . n 
B 1 142 ALA 142 120 120 ALA ALA B . n 
B 1 143 CYS 143 121 121 CYS CYS B . n 
B 1 144 ASP 144 122 122 ASP ASP B . n 
B 1 145 MSE 145 123 123 MSE MSE B . n 
B 1 146 THR 146 124 124 THR THR B . n 
B 1 147 ILE 147 125 125 ILE ILE B . n 
B 1 148 ALA 148 126 126 ALA ALA B . n 
B 1 149 THR 149 127 127 THR THR B . n 
B 1 150 GLU 150 128 128 GLU GLU B . n 
B 1 151 ASP 151 129 129 ASP ASP B . n 
B 1 152 ALA 152 130 130 ALA ALA B . n 
B 1 153 PHE 153 131 131 PHE PHE B . n 
B 1 154 PHE 154 132 132 PHE PHE B . n 
B 1 155 GLY 155 133 133 GLY GLY B . n 
B 1 156 GLU 156 134 134 GLU GLU B . n 
B 1 157 PRO 157 135 135 PRO PRO B . n 
B 1 158 GLU 158 136 136 GLU GLU B . n 
B 1 159 LEU 159 137 137 LEU LEU B . n 
B 1 160 LYS 160 138 138 LYS LYS B . n 
B 1 161 PHE 161 139 139 PHE PHE B . n 
B 1 162 GLY 162 140 140 GLY GLY B . n 
B 1 163 ALA 163 141 141 ALA ALA B . n 
B 1 164 GLY 164 142 142 GLY GLY B . n 
B 1 165 ILE 165 143 143 ILE ILE B . n 
B 1 166 VAL 166 144 144 VAL VAL B . n 
B 1 167 VAL 167 145 145 VAL VAL B . n 
B 1 168 MSE 168 146 146 MSE MSE B . n 
B 1 169 LEU 169 147 147 LEU LEU B . n 
B 1 170 LEU 170 148 148 LEU LEU B . n 
B 1 171 PRO 171 149 149 PRO PRO B . n 
B 1 172 TRP 172 150 150 TRP TRP B . n 
B 1 173 ILE 173 151 151 ILE ILE B . n 
B 1 174 VAL 174 152 152 VAL VAL B . n 
B 1 175 GLY 175 153 153 GLY GLY B . n 
B 1 176 PRO 176 154 154 PRO PRO B . n 
B 1 177 LYS 177 155 155 LYS LYS B . n 
B 1 178 ILE 178 156 156 ILE ILE B . n 
B 1 179 ALA 179 157 157 ALA ALA B . n 
B 1 180 LYS 180 158 158 LYS LYS B . n 
B 1 181 GLU 181 159 159 GLU GLU B . n 
B 1 182 ILE 182 160 160 ILE ILE B . n 
B 1 183 ILE 183 161 161 ILE ILE B . n 
B 1 184 LEU 184 162 162 LEU LEU B . n 
B 1 185 LEU 185 163 163 LEU LEU B . n 
B 1 186 GLY 186 164 164 GLY GLY B . n 
B 1 187 GLU 187 165 165 GLU GLU B . n 
B 1 188 ASP 188 166 166 ASP ASP B . n 
B 1 189 ARG 189 167 167 ARG ARG B . n 
B 1 190 VAL 190 168 168 VAL VAL B . n 
B 1 191 PRO 191 169 169 PRO PRO B . n 
B 1 192 ALA 192 170 170 ALA ALA B . n 
B 1 193 ARG 193 171 171 ARG ARG B . n 
B 1 194 ARG 194 172 172 ARG ARG B . n 
B 1 195 ALA 195 173 173 ALA ALA B . n 
B 1 196 ALA 196 174 174 ALA ALA B . n 
B 1 197 GLU 197 175 175 GLU GLU B . n 
B 1 198 ILE 198 176 176 ILE ILE B . n 
B 1 199 GLY 199 177 177 GLY GLY B . n 
B 1 200 MSE 200 178 178 MSE MSE B . n 
B 1 201 VAL 201 179 179 VAL VAL B . n 
B 1 202 ASN 202 180 180 ASN ASN B . n 
B 1 203 ARG 203 181 181 ARG ARG B . n 
B 1 204 VAL 204 182 182 VAL VAL B . n 
B 1 205 VAL 205 183 183 VAL VAL B . n 
B 1 206 ASP 206 184 184 ASP ASP B . n 
B 1 207 GLY 207 185 185 GLY GLY B . n 
B 1 208 ASP 208 186 186 ASP ASP B . n 
B 1 209 GLY 209 187 187 GLY GLY B . n 
B 1 210 LEU 210 188 188 LEU LEU B . n 
B 1 211 ASP 211 189 189 ASP ASP B . n 
B 1 212 ALA 212 190 190 ALA ALA B . n 
B 1 213 GLU 213 191 191 GLU GLU B . n 
B 1 214 ALA 214 192 192 ALA ALA B . n 
B 1 215 LEU 215 193 193 LEU LEU B . n 
B 1 216 ARG 216 194 194 ARG ARG B . n 
B 1 217 ILE 217 195 195 ILE ILE B . n 
B 1 218 ALA 218 196 196 ALA ALA B . n 
B 1 219 ARG 219 197 197 ARG ARG B . n 
B 1 220 HIS 220 198 198 HIS HIS B . n 
B 1 221 ILE 221 199 199 ILE ILE B . n 
B 1 222 GLY 222 200 200 GLY GLY B . n 
B 1 223 ALA 223 201 201 ALA ALA B . n 
B 1 224 ILE 224 202 202 ILE ILE B . n 
B 1 225 ASP 225 203 203 ASP ASP B . n 
B 1 226 PRO 226 204 204 PRO PRO B . n 
B 1 227 GLY 227 205 205 GLY GLY B . n 
B 1 228 LEU 228 206 206 LEU LEU B . n 
B 1 229 VAL 229 207 207 VAL VAL B . n 
B 1 230 LYS 230 208 208 LYS LYS B . n 
B 1 231 GLU 231 209 209 GLU GLU B . n 
B 1 232 THR 232 210 210 THR THR B . n 
B 1 233 LYS 233 211 211 LYS LYS B . n 
B 1 234 ARG 234 212 212 ARG ARG B . n 
B 1 235 ALA 235 213 213 ALA ALA B . n 
B 1 236 LEU 236 214 214 LEU LEU B . n 
B 1 237 ASN 237 215 215 ASN ASN B . n 
B 1 238 ARG 238 216 216 ARG ARG B . n 
B 1 239 ALA 239 217 217 ALA ALA B . n 
B 1 240 LEU 240 218 218 LEU LEU B . n 
B 1 241 GLU 241 219 219 GLU GLU B . n 
B 1 242 THR 242 220 220 THR THR B . n 
B 1 243 GLN 243 221 221 GLN GLN B . n 
B 1 244 GLY 244 222 222 GLY GLY B . n 
B 1 245 MSE 245 223 223 MSE MSE B . n 
B 1 246 LEU 246 224 224 LEU LEU B . n 
B 1 247 GLN 247 225 225 GLN GLN B . n 
B 1 248 ALA 248 226 226 ALA ALA B . n 
B 1 249 LEU 249 227 227 LEU LEU B . n 
B 1 250 GLU 250 228 228 GLU GLU B . n 
B 1 251 SER 251 229 229 SER SER B . n 
B 1 252 ALA 252 230 230 ALA ALA B . n 
B 1 253 LEU 253 231 231 LEU LEU B . n 
B 1 254 GLU 254 232 232 GLU GLU B . n 
B 1 255 ILE 255 233 233 ILE ILE B . n 
B 1 256 ASP 256 234 234 ASP ASP B . n 
B 1 257 LEU 257 235 235 LEU LEU B . n 
B 1 258 ALA 258 236 236 ALA ALA B . n 
B 1 259 ILE 259 237 237 ILE ILE B . n 
B 1 260 GLU 260 238 238 GLU GLU B . n 
B 1 261 GLY 261 239 239 GLY GLY B . n 
B 1 262 ALA 262 240 240 ALA ALA B . n 
B 1 263 GLY 263 241 241 GLY GLY B . n 
B 1 264 SER 264 242 242 SER SER B . n 
B 1 265 PRO 265 243 243 PRO PRO B . n 
B 1 266 ASP 266 244 244 ASP ASP B . n 
B 1 267 LYS 267 245 245 LYS LYS B . n 
B 1 268 ILE 268 246 246 ILE ILE B . n 
B 1 269 ALA 269 247 247 ALA ALA B . n 
B 1 270 PHE 270 248 248 PHE PHE B . n 
B 1 271 PHE 271 249 249 PHE PHE B . n 
B 1 272 GLU 272 250 250 GLU GLU B . n 
B 1 273 VAL 273 251 251 VAL VAL B . n 
B 1 274 ALA 274 252 252 ALA ALA B . n 
B 1 275 ARG 275 253 253 ARG ARG B . n 
B 1 276 ARG 276 254 254 ARG ARG B . n 
B 1 277 ASP 277 255 255 ASP ASP B . n 
B 1 278 GLY 278 256 256 GLY GLY B . n 
B 1 279 LEU 279 257 257 LEU LEU B . n 
B 1 280 ARG 280 258 258 ARG ARG B . n 
B 1 281 ALA 281 259 259 ALA ALA B . n 
B 1 282 ALA 282 260 260 ALA ALA B . n 
B 1 283 ILE 283 261 261 ILE ILE B . n 
B 1 284 ALA 284 262 262 ALA ALA B . n 
B 1 285 TRP 285 263 263 TRP TRP B . n 
B 1 286 ARG 286 264 264 ARG ARG B . n 
B 1 287 ASP 287 265 265 ASP ASP B . n 
B 1 288 ALA 288 266 266 ALA ALA B . n 
B 1 289 ARG 289 267 267 ARG ARG B . n 
B 1 290 PHE 290 268 268 PHE PHE B . n 
B 1 291 PRO 291 269 269 PRO PRO B . n 
B 1 292 ALA 292 270 270 ALA ALA B . n 
B 1 293 ARG 293 271 ?   ?   ?   B . n 
B 1 294 ASP 294 272 ?   ?   ?   B . n 
B 1 295 ALA 295 273 ?   ?   ?   B . n 
C 1 1   MSE 1   -21 ?   ?   ?   C . n 
C 1 2   HIS 2   -20 ?   ?   ?   C . n 
C 1 3   HIS 3   -19 ?   ?   ?   C . n 
C 1 4   HIS 4   -18 ?   ?   ?   C . n 
C 1 5   HIS 5   -17 ?   ?   ?   C . n 
C 1 6   HIS 6   -16 ?   ?   ?   C . n 
C 1 7   HIS 7   -15 ?   ?   ?   C . n 
C 1 8   SER 8   -14 ?   ?   ?   C . n 
C 1 9   SER 9   -13 ?   ?   ?   C . n 
C 1 10  GLY 10  -12 ?   ?   ?   C . n 
C 1 11  VAL 11  -11 ?   ?   ?   C . n 
C 1 12  ASP 12  -10 ?   ?   ?   C . n 
C 1 13  LEU 13  -9  ?   ?   ?   C . n 
C 1 14  GLY 14  -8  ?   ?   ?   C . n 
C 1 15  THR 15  -7  ?   ?   ?   C . n 
C 1 16  GLU 16  -6  ?   ?   ?   C . n 
C 1 17  ASN 17  -5  ?   ?   ?   C . n 
C 1 18  LEU 18  -4  ?   ?   ?   C . n 
C 1 19  TYR 19  -3  ?   ?   ?   C . n 
C 1 20  PHE 20  -2  ?   ?   ?   C . n 
C 1 21  GLN 21  -1  ?   ?   ?   C . n 
C 1 22  SER 22  0   ?   ?   ?   C . n 
C 1 23  MSE 23  1   ?   ?   ?   C . n 
C 1 24  THR 24  2   ?   ?   ?   C . n 
C 1 25  TYR 25  3   3   TYR TYR C . n 
C 1 26  SER 26  4   4   SER SER C . n 
C 1 27  LYS 27  5   5   LYS LYS C . n 
C 1 28  ILE 28  6   6   ILE ILE C . n 
C 1 29  LEU 29  7   7   LEU LEU C . n 
C 1 30  TYR 30  8   8   TYR TYR C . n 
C 1 31  GLU 31  9   9   GLU GLU C . n 
C 1 32  THR 32  10  10  THR THR C . n 
C 1 33  LEU 33  11  11  LEU LEU C . n 
C 1 34  HIS 34  12  12  HIS HIS C . n 
C 1 35  GLY 35  13  13  GLY GLY C . n 
C 1 36  VAL 36  14  14  VAL VAL C . n 
C 1 37  ALA 37  15  15  ALA ALA C . n 
C 1 38  ARG 38  16  16  ARG ARG C . n 
C 1 39  ILE 39  17  17  ILE ILE C . n 
C 1 40  THR 40  18  18  THR THR C . n 
C 1 41  LEU 41  19  19  LEU LEU C . n 
C 1 42  ASN 42  20  20  ASN ASN C . n 
C 1 43  ARG 43  21  21  ARG ARG C . n 
C 1 44  PRO 44  22  22  PRO PRO C . n 
C 1 45  GLU 45  23  23  GLU GLU C . n 
C 1 46  ARG 46  24  24  ARG ARG C . n 
C 1 47  THR 47  25  25  THR THR C . n 
C 1 48  ASN 48  26  26  ASN ASN C . n 
C 1 49  ALA 49  27  27  ALA ALA C . n 
C 1 50  LEU 50  28  28  LEU LEU C . n 
C 1 51  ASP 51  29  29  ASP ASP C . n 
C 1 52  GLN 52  30  30  GLN GLN C . n 
C 1 53  GLU 53  31  31  GLU GLU C . n 
C 1 54  MSE 54  32  32  MSE MSE C . n 
C 1 55  LEU 55  33  33  LEU LEU C . n 
C 1 56  GLY 56  34  34  GLY GLY C . n 
C 1 57  GLU 57  35  35  GLU GLU C . n 
C 1 58  ILE 58  36  36  ILE ILE C . n 
C 1 59  ASN 59  37  37  ASN ASN C . n 
C 1 60  ALA 60  38  38  ALA ALA C . n 
C 1 61  ALA 61  39  39  ALA ALA C . n 
C 1 62  MSE 62  40  40  MSE MSE C . n 
C 1 63  ASP 63  41  41  ASP ASP C . n 
C 1 64  ALA 64  42  42  ALA ALA C . n 
C 1 65  ALA 65  43  43  ALA ALA C . n 
C 1 66  GLU 66  44  44  GLU GLU C . n 
C 1 67  ALA 67  45  45  ALA ALA C . n 
C 1 68  ASP 68  46  46  ASP ASP C . n 
C 1 69  ALA 69  47  47  ALA ALA C . n 
C 1 70  GLY 70  48  48  GLY GLY C . n 
C 1 71  VAL 71  49  49  VAL VAL C . n 
C 1 72  LYS 72  50  50  LYS LYS C . n 
C 1 73  ALA 73  51  51  ALA ALA C . n 
C 1 74  VAL 74  52  52  VAL VAL C . n 
C 1 75  ILE 75  53  53  ILE ILE C . n 
C 1 76  VAL 76  54  54  VAL VAL C . n 
C 1 77  ARG 77  55  55  ARG ARG C . n 
C 1 78  GLY 78  56  56  GLY GLY C . n 
C 1 79  ALA 79  57  57  ALA ALA C . n 
C 1 80  GLY 80  58  58  GLY GLY C . n 
C 1 81  ASN 81  59  59  ASN ASN C . n 
C 1 82  ALA 82  60  60  ALA ALA C . n 
C 1 83  PHE 83  61  61  PHE PHE C . n 
C 1 84  SER 84  62  62  SER SER C . n 
C 1 85  SER 85  63  63  SER SER C . n 
C 1 86  GLY 86  64  64  GLY GLY C . n 
C 1 87  PHE 87  65  65  PHE PHE C . n 
C 1 88  ASP 88  66  66  ASP ASP C . n 
C 1 89  LEU 89  67  67  LEU LEU C . n 
C 1 90  LYS 90  68  68  LYS LYS C . n 
C 1 91  ALA 91  69  69  ALA ALA C . n 
C 1 92  GLN 92  70  70  GLN GLN C . n 
C 1 93  MSE 93  71  71  MSE MSE C . n 
C 1 94  GLU 94  72  72  GLU GLU C . n 
C 1 95  ALA 95  73  73  ALA ALA C . n 
C 1 96  ARG 96  74  74  ARG ARG C . n 
C 1 97  PRO 97  75  75  PRO PRO C . n 
C 1 98  ALA 98  76  76  ALA ALA C . n 
C 1 99  GLY 99  77  77  GLY GLY C . n 
C 1 100 VAL 100 78  78  VAL VAL C . n 
C 1 101 ASP 101 79  79  ASP ASP C . n 
C 1 102 ALA 102 80  80  ALA ALA C . n 
C 1 103 TRP 103 81  81  TRP TRP C . n 
C 1 104 ARG 104 82  82  ARG ARG C . n 
C 1 105 PRO 105 83  83  PRO PRO C . n 
C 1 106 LEU 106 84  84  LEU LEU C . n 
C 1 107 LEU 107 85  85  LEU LEU C . n 
C 1 108 ARG 108 86  86  ARG ARG C . n 
C 1 109 LYS 109 87  87  LYS LYS C . n 
C 1 110 ASP 110 88  88  ASP ASP C . n 
C 1 111 PHE 111 89  89  PHE PHE C . n 
C 1 112 ASP 112 90  90  ASP ASP C . n 
C 1 113 THR 113 91  91  THR THR C . n 
C 1 114 VAL 114 92  92  VAL VAL C . n 
C 1 115 MSE 115 93  93  MSE MSE C . n 
C 1 116 ARG 116 94  94  ARG ARG C . n 
C 1 117 PHE 117 95  95  PHE PHE C . n 
C 1 118 TRP 118 96  96  TRP TRP C . n 
C 1 119 HIS 119 97  97  HIS HIS C . n 
C 1 120 CYS 120 98  98  CYS CYS C . n 
C 1 121 PRO 121 99  99  PRO PRO C . n 
C 1 122 LYS 122 100 100 LYS LYS C . n 
C 1 123 PRO 123 101 101 PRO PRO C . n 
C 1 124 THR 124 102 102 THR THR C . n 
C 1 125 ILE 125 103 103 ILE ILE C . n 
C 1 126 ALA 126 104 104 ALA ALA C . n 
C 1 127 ALA 127 105 105 ALA ALA C . n 
C 1 128 VAL 128 106 106 VAL VAL C . n 
C 1 129 ARG 129 107 107 ARG ARG C . n 
C 1 130 GLY 130 108 108 GLY GLY C . n 
C 1 131 PRO 131 109 109 PRO PRO C . n 
C 1 132 CYS 132 110 110 CYS CYS C . n 
C 1 133 LEU 133 111 111 LEU LEU C . n 
C 1 134 ALA 134 112 112 ALA ALA C . n 
C 1 135 GLY 135 113 113 GLY GLY C . n 
C 1 136 ALA 136 114 114 ALA ALA C . n 
C 1 137 CYS 137 115 115 CYS CYS C . n 
C 1 138 GLU 138 116 116 GLU GLU C . n 
C 1 139 LEU 139 117 117 LEU LEU C . n 
C 1 140 ALA 140 118 118 ALA ALA C . n 
C 1 141 LEU 141 119 119 LEU LEU C . n 
C 1 142 ALA 142 120 120 ALA ALA C . n 
C 1 143 CYS 143 121 121 CYS CYS C . n 
C 1 144 ASP 144 122 122 ASP ASP C . n 
C 1 145 MSE 145 123 123 MSE MSE C . n 
C 1 146 THR 146 124 124 THR THR C . n 
C 1 147 ILE 147 125 125 ILE ILE C . n 
C 1 148 ALA 148 126 126 ALA ALA C . n 
C 1 149 THR 149 127 127 THR THR C . n 
C 1 150 GLU 150 128 128 GLU GLU C . n 
C 1 151 ASP 151 129 129 ASP ASP C . n 
C 1 152 ALA 152 130 130 ALA ALA C . n 
C 1 153 PHE 153 131 131 PHE PHE C . n 
C 1 154 PHE 154 132 132 PHE PHE C . n 
C 1 155 GLY 155 133 133 GLY GLY C . n 
C 1 156 GLU 156 134 134 GLU GLU C . n 
C 1 157 PRO 157 135 135 PRO PRO C . n 
C 1 158 GLU 158 136 136 GLU GLU C . n 
C 1 159 LEU 159 137 137 LEU LEU C . n 
C 1 160 LYS 160 138 138 LYS LYS C . n 
C 1 161 PHE 161 139 139 PHE PHE C . n 
C 1 162 GLY 162 140 140 GLY GLY C . n 
C 1 163 ALA 163 141 141 ALA ALA C . n 
C 1 164 GLY 164 142 142 GLY GLY C . n 
C 1 165 ILE 165 143 143 ILE ILE C . n 
C 1 166 VAL 166 144 144 VAL VAL C . n 
C 1 167 VAL 167 145 145 VAL VAL C . n 
C 1 168 MSE 168 146 146 MSE MSE C . n 
C 1 169 LEU 169 147 147 LEU LEU C . n 
C 1 170 LEU 170 148 148 LEU LEU C . n 
C 1 171 PRO 171 149 149 PRO PRO C . n 
C 1 172 TRP 172 150 150 TRP TRP C . n 
C 1 173 ILE 173 151 151 ILE ILE C . n 
C 1 174 VAL 174 152 152 VAL VAL C . n 
C 1 175 GLY 175 153 153 GLY GLY C . n 
C 1 176 PRO 176 154 154 PRO PRO C . n 
C 1 177 LYS 177 155 155 LYS LYS C . n 
C 1 178 ILE 178 156 156 ILE ILE C . n 
C 1 179 ALA 179 157 157 ALA ALA C . n 
C 1 180 LYS 180 158 158 LYS LYS C . n 
C 1 181 GLU 181 159 159 GLU GLU C . n 
C 1 182 ILE 182 160 160 ILE ILE C . n 
C 1 183 ILE 183 161 161 ILE ILE C . n 
C 1 184 LEU 184 162 162 LEU LEU C . n 
C 1 185 LEU 185 163 163 LEU LEU C . n 
C 1 186 GLY 186 164 164 GLY GLY C . n 
C 1 187 GLU 187 165 165 GLU GLU C . n 
C 1 188 ASP 188 166 166 ASP ASP C . n 
C 1 189 ARG 189 167 167 ARG ARG C . n 
C 1 190 VAL 190 168 168 VAL VAL C . n 
C 1 191 PRO 191 169 169 PRO PRO C . n 
C 1 192 ALA 192 170 170 ALA ALA C . n 
C 1 193 ARG 193 171 171 ARG ARG C . n 
C 1 194 ARG 194 172 172 ARG ARG C . n 
C 1 195 ALA 195 173 173 ALA ALA C . n 
C 1 196 ALA 196 174 174 ALA ALA C . n 
C 1 197 GLU 197 175 175 GLU GLU C . n 
C 1 198 ILE 198 176 176 ILE ILE C . n 
C 1 199 GLY 199 177 177 GLY GLY C . n 
C 1 200 MSE 200 178 178 MSE MSE C . n 
C 1 201 VAL 201 179 179 VAL VAL C . n 
C 1 202 ASN 202 180 180 ASN ASN C . n 
C 1 203 ARG 203 181 181 ARG ARG C . n 
C 1 204 VAL 204 182 182 VAL VAL C . n 
C 1 205 VAL 205 183 183 VAL VAL C . n 
C 1 206 ASP 206 184 184 ASP ASP C . n 
C 1 207 GLY 207 185 185 GLY GLY C . n 
C 1 208 ASP 208 186 186 ASP ASP C . n 
C 1 209 GLY 209 187 187 GLY GLY C . n 
C 1 210 LEU 210 188 188 LEU LEU C . n 
C 1 211 ASP 211 189 189 ASP ASP C . n 
C 1 212 ALA 212 190 190 ALA ALA C . n 
C 1 213 GLU 213 191 191 GLU GLU C . n 
C 1 214 ALA 214 192 192 ALA ALA C . n 
C 1 215 LEU 215 193 193 LEU LEU C . n 
C 1 216 ARG 216 194 194 ARG ARG C . n 
C 1 217 ILE 217 195 195 ILE ILE C . n 
C 1 218 ALA 218 196 196 ALA ALA C . n 
C 1 219 ARG 219 197 197 ARG ARG C . n 
C 1 220 HIS 220 198 198 HIS HIS C . n 
C 1 221 ILE 221 199 199 ILE ILE C . n 
C 1 222 GLY 222 200 200 GLY GLY C . n 
C 1 223 ALA 223 201 201 ALA ALA C . n 
C 1 224 ILE 224 202 202 ILE ILE C . n 
C 1 225 ASP 225 203 203 ASP ASP C . n 
C 1 226 PRO 226 204 204 PRO PRO C . n 
C 1 227 GLY 227 205 205 GLY GLY C . n 
C 1 228 LEU 228 206 206 LEU LEU C . n 
C 1 229 VAL 229 207 207 VAL VAL C . n 
C 1 230 LYS 230 208 208 LYS LYS C . n 
C 1 231 GLU 231 209 209 GLU GLU C . n 
C 1 232 THR 232 210 210 THR THR C . n 
C 1 233 LYS 233 211 211 LYS LYS C . n 
C 1 234 ARG 234 212 212 ARG ARG C . n 
C 1 235 ALA 235 213 213 ALA ALA C . n 
C 1 236 LEU 236 214 214 LEU LEU C . n 
C 1 237 ASN 237 215 215 ASN ASN C . n 
C 1 238 ARG 238 216 216 ARG ARG C . n 
C 1 239 ALA 239 217 217 ALA ALA C . n 
C 1 240 LEU 240 218 218 LEU LEU C . n 
C 1 241 GLU 241 219 219 GLU GLU C . n 
C 1 242 THR 242 220 220 THR THR C . n 
C 1 243 GLN 243 221 221 GLN GLN C . n 
C 1 244 GLY 244 222 222 GLY GLY C . n 
C 1 245 MSE 245 223 223 MSE MSE C . n 
C 1 246 LEU 246 224 224 LEU LEU C . n 
C 1 247 GLN 247 225 225 GLN GLN C . n 
C 1 248 ALA 248 226 226 ALA ALA C . n 
C 1 249 LEU 249 227 227 LEU LEU C . n 
C 1 250 GLU 250 228 228 GLU GLU C . n 
C 1 251 SER 251 229 229 SER SER C . n 
C 1 252 ALA 252 230 230 ALA ALA C . n 
C 1 253 LEU 253 231 231 LEU LEU C . n 
C 1 254 GLU 254 232 232 GLU GLU C . n 
C 1 255 ILE 255 233 233 ILE ILE C . n 
C 1 256 ASP 256 234 234 ASP ASP C . n 
C 1 257 LEU 257 235 235 LEU LEU C . n 
C 1 258 ALA 258 236 236 ALA ALA C . n 
C 1 259 ILE 259 237 237 ILE ILE C . n 
C 1 260 GLU 260 238 238 GLU GLU C . n 
C 1 261 GLY 261 239 239 GLY GLY C . n 
C 1 262 ALA 262 240 240 ALA ALA C . n 
C 1 263 GLY 263 241 241 GLY GLY C . n 
C 1 264 SER 264 242 242 SER SER C . n 
C 1 265 PRO 265 243 243 PRO PRO C . n 
C 1 266 ASP 266 244 244 ASP ASP C . n 
C 1 267 LYS 267 245 245 LYS LYS C . n 
C 1 268 ILE 268 246 246 ILE ILE C . n 
C 1 269 ALA 269 247 247 ALA ALA C . n 
C 1 270 PHE 270 248 248 PHE PHE C . n 
C 1 271 PHE 271 249 249 PHE PHE C . n 
C 1 272 GLU 272 250 250 GLU GLU C . n 
C 1 273 VAL 273 251 251 VAL VAL C . n 
C 1 274 ALA 274 252 252 ALA ALA C . n 
C 1 275 ARG 275 253 253 ARG ARG C . n 
C 1 276 ARG 276 254 254 ARG ARG C . n 
C 1 277 ASP 277 255 255 ASP ASP C . n 
C 1 278 GLY 278 256 256 GLY GLY C . n 
C 1 279 LEU 279 257 257 LEU LEU C . n 
C 1 280 ARG 280 258 258 ARG ARG C . n 
C 1 281 ALA 281 259 259 ALA ALA C . n 
C 1 282 ALA 282 260 260 ALA ALA C . n 
C 1 283 ILE 283 261 261 ILE ILE C . n 
C 1 284 ALA 284 262 262 ALA ALA C . n 
C 1 285 TRP 285 263 263 TRP TRP C . n 
C 1 286 ARG 286 264 264 ARG ARG C . n 
C 1 287 ASP 287 265 265 ASP ASP C . n 
C 1 288 ALA 288 266 266 ALA ALA C . n 
C 1 289 ARG 289 267 267 ARG ARG C . n 
C 1 290 PHE 290 268 268 PHE PHE C . n 
C 1 291 PRO 291 269 269 PRO PRO C . n 
C 1 292 ALA 292 270 270 ALA ALA C . n 
C 1 293 ARG 293 271 ?   ?   ?   C . n 
C 1 294 ASP 294 272 ?   ?   ?   C . n 
C 1 295 ALA 295 273 ?   ?   ?   C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 TLA 1   301 602 TLA TLA A . 
E 3 GOL 1   302 605 GOL GOL A . 
F 2 TLA 1   601 601 TLA TLA C . 
G 2 TLA 1   602 603 TLA TLA C . 
H 3 GOL 1   603 604 GOL GOL C . 
I 4 HOH 1   401 2   HOH HOH A . 
I 4 HOH 2   402 5   HOH HOH A . 
I 4 HOH 3   403 7   HOH HOH A . 
I 4 HOH 4   404 9   HOH HOH A . 
I 4 HOH 5   405 13  HOH HOH A . 
I 4 HOH 6   406 15  HOH HOH A . 
I 4 HOH 7   407 16  HOH HOH A . 
I 4 HOH 8   408 19  HOH HOH A . 
I 4 HOH 9   409 20  HOH HOH A . 
I 4 HOH 10  410 21  HOH HOH A . 
I 4 HOH 11  411 23  HOH HOH A . 
I 4 HOH 12  412 26  HOH HOH A . 
I 4 HOH 13  413 27  HOH HOH A . 
I 4 HOH 14  414 31  HOH HOH A . 
I 4 HOH 15  415 37  HOH HOH A . 
I 4 HOH 16  416 39  HOH HOH A . 
I 4 HOH 17  417 40  HOH HOH A . 
I 4 HOH 18  418 43  HOH HOH A . 
I 4 HOH 19  419 46  HOH HOH A . 
I 4 HOH 20  420 54  HOH HOH A . 
I 4 HOH 21  421 56  HOH HOH A . 
I 4 HOH 22  422 58  HOH HOH A . 
I 4 HOH 23  423 69  HOH HOH A . 
I 4 HOH 24  424 70  HOH HOH A . 
I 4 HOH 25  425 73  HOH HOH A . 
I 4 HOH 26  426 81  HOH HOH A . 
I 4 HOH 27  427 92  HOH HOH A . 
I 4 HOH 28  428 97  HOH HOH A . 
I 4 HOH 29  429 101 HOH HOH A . 
I 4 HOH 30  430 104 HOH HOH A . 
I 4 HOH 31  431 106 HOH HOH A . 
I 4 HOH 32  432 111 HOH HOH A . 
I 4 HOH 33  433 112 HOH HOH A . 
I 4 HOH 34  434 113 HOH HOH A . 
I 4 HOH 35  435 116 HOH HOH A . 
I 4 HOH 36  436 117 HOH HOH A . 
I 4 HOH 37  437 118 HOH HOH A . 
I 4 HOH 38  438 122 HOH HOH A . 
I 4 HOH 39  439 125 HOH HOH A . 
I 4 HOH 40  440 129 HOH HOH A . 
I 4 HOH 41  441 131 HOH HOH A . 
I 4 HOH 42  442 133 HOH HOH A . 
I 4 HOH 43  443 136 HOH HOH A . 
I 4 HOH 44  444 145 HOH HOH A . 
I 4 HOH 45  445 146 HOH HOH A . 
I 4 HOH 46  446 147 HOH HOH A . 
I 4 HOH 47  447 149 HOH HOH A . 
I 4 HOH 48  448 154 HOH HOH A . 
I 4 HOH 49  449 156 HOH HOH A . 
I 4 HOH 50  450 157 HOH HOH A . 
I 4 HOH 51  451 158 HOH HOH A . 
I 4 HOH 52  452 159 HOH HOH A . 
I 4 HOH 53  453 160 HOH HOH A . 
I 4 HOH 54  454 161 HOH HOH A . 
I 4 HOH 55  455 163 HOH HOH A . 
I 4 HOH 56  456 171 HOH HOH A . 
I 4 HOH 57  457 174 HOH HOH A . 
I 4 HOH 58  458 177 HOH HOH A . 
I 4 HOH 59  459 178 HOH HOH A . 
I 4 HOH 60  460 179 HOH HOH A . 
I 4 HOH 61  461 182 HOH HOH A . 
I 4 HOH 62  462 190 HOH HOH A . 
I 4 HOH 63  463 193 HOH HOH A . 
I 4 HOH 64  464 196 HOH HOH A . 
I 4 HOH 65  465 199 HOH HOH A . 
I 4 HOH 66  466 205 HOH HOH A . 
I 4 HOH 67  467 209 HOH HOH A . 
I 4 HOH 68  468 210 HOH HOH A . 
I 4 HOH 69  469 212 HOH HOH A . 
I 4 HOH 70  470 218 HOH HOH A . 
I 4 HOH 71  471 220 HOH HOH A . 
I 4 HOH 72  472 222 HOH HOH A . 
I 4 HOH 73  473 226 HOH HOH A . 
I 4 HOH 74  474 227 HOH HOH A . 
I 4 HOH 75  475 235 HOH HOH A . 
I 4 HOH 76  476 236 HOH HOH A . 
I 4 HOH 77  477 237 HOH HOH A . 
I 4 HOH 78  478 241 HOH HOH A . 
I 4 HOH 79  479 258 HOH HOH A . 
I 4 HOH 80  480 260 HOH HOH A . 
I 4 HOH 81  481 262 HOH HOH A . 
I 4 HOH 82  482 264 HOH HOH A . 
I 4 HOH 83  483 266 HOH HOH A . 
I 4 HOH 84  484 267 HOH HOH A . 
I 4 HOH 85  485 272 HOH HOH A . 
I 4 HOH 86  486 279 HOH HOH A . 
I 4 HOH 87  487 281 HOH HOH A . 
I 4 HOH 88  488 284 HOH HOH A . 
I 4 HOH 89  489 286 HOH HOH A . 
I 4 HOH 90  490 291 HOH HOH A . 
I 4 HOH 91  491 292 HOH HOH A . 
I 4 HOH 92  492 296 HOH HOH A . 
I 4 HOH 93  493 298 HOH HOH A . 
I 4 HOH 94  494 300 HOH HOH A . 
I 4 HOH 95  495 302 HOH HOH A . 
I 4 HOH 96  496 311 HOH HOH A . 
I 4 HOH 97  497 313 HOH HOH A . 
I 4 HOH 98  498 317 HOH HOH A . 
I 4 HOH 99  499 321 HOH HOH A . 
I 4 HOH 100 500 328 HOH HOH A . 
I 4 HOH 101 501 333 HOH HOH A . 
I 4 HOH 102 502 334 HOH HOH A . 
I 4 HOH 103 503 338 HOH HOH A . 
I 4 HOH 104 504 341 HOH HOH A . 
I 4 HOH 105 505 343 HOH HOH A . 
I 4 HOH 106 506 345 HOH HOH A . 
I 4 HOH 107 507 348 HOH HOH A . 
I 4 HOH 108 508 358 HOH HOH A . 
I 4 HOH 109 509 360 HOH HOH A . 
I 4 HOH 110 510 362 HOH HOH A . 
I 4 HOH 111 511 368 HOH HOH A . 
I 4 HOH 112 512 369 HOH HOH A . 
I 4 HOH 113 513 370 HOH HOH A . 
I 4 HOH 114 514 372 HOH HOH A . 
I 4 HOH 115 515 376 HOH HOH A . 
I 4 HOH 116 516 379 HOH HOH A . 
I 4 HOH 117 517 385 HOH HOH A . 
I 4 HOH 118 518 386 HOH HOH A . 
I 4 HOH 119 519 387 HOH HOH A . 
I 4 HOH 120 520 388 HOH HOH A . 
I 4 HOH 121 521 390 HOH HOH A . 
I 4 HOH 122 522 397 HOH HOH A . 
I 4 HOH 123 523 398 HOH HOH A . 
I 4 HOH 124 524 401 HOH HOH A . 
I 4 HOH 125 525 402 HOH HOH A . 
I 4 HOH 126 526 404 HOH HOH A . 
I 4 HOH 127 527 407 HOH HOH A . 
I 4 HOH 128 528 413 HOH HOH A . 
I 4 HOH 129 529 414 HOH HOH A . 
I 4 HOH 130 530 415 HOH HOH A . 
I 4 HOH 131 531 416 HOH HOH A . 
I 4 HOH 132 532 418 HOH HOH A . 
I 4 HOH 133 533 424 HOH HOH A . 
I 4 HOH 134 534 426 HOH HOH A . 
I 4 HOH 135 535 427 HOH HOH A . 
I 4 HOH 136 536 429 HOH HOH A . 
I 4 HOH 137 537 430 HOH HOH A . 
I 4 HOH 138 538 432 HOH HOH A . 
I 4 HOH 139 539 436 HOH HOH A . 
I 4 HOH 140 540 438 HOH HOH A . 
I 4 HOH 141 541 439 HOH HOH A . 
I 4 HOH 142 542 440 HOH HOH A . 
I 4 HOH 143 543 441 HOH HOH A . 
I 4 HOH 144 544 442 HOH HOH A . 
I 4 HOH 145 545 449 HOH HOH A . 
I 4 HOH 146 546 455 HOH HOH A . 
I 4 HOH 147 547 457 HOH HOH A . 
I 4 HOH 148 548 458 HOH HOH A . 
I 4 HOH 149 549 459 HOH HOH A . 
I 4 HOH 150 550 460 HOH HOH A . 
I 4 HOH 151 551 463 HOH HOH A . 
I 4 HOH 152 552 465 HOH HOH A . 
I 4 HOH 153 553 467 HOH HOH A . 
I 4 HOH 154 554 473 HOH HOH A . 
I 4 HOH 155 555 475 HOH HOH A . 
I 4 HOH 156 556 476 HOH HOH A . 
I 4 HOH 157 557 478 HOH HOH A . 
I 4 HOH 158 558 480 HOH HOH A . 
I 4 HOH 159 559 486 HOH HOH A . 
I 4 HOH 160 560 488 HOH HOH A . 
I 4 HOH 161 561 490 HOH HOH A . 
I 4 HOH 162 562 491 HOH HOH A . 
I 4 HOH 163 563 492 HOH HOH A . 
I 4 HOH 164 564 493 HOH HOH A . 
I 4 HOH 165 565 496 HOH HOH A . 
I 4 HOH 166 566 498 HOH HOH A . 
I 4 HOH 167 567 503 HOH HOH A . 
I 4 HOH 168 568 505 HOH HOH A . 
I 4 HOH 169 569 517 HOH HOH A . 
I 4 HOH 170 570 529 HOH HOH A . 
I 4 HOH 171 571 537 HOH HOH A . 
I 4 HOH 172 572 541 HOH HOH A . 
I 4 HOH 173 573 544 HOH HOH A . 
I 4 HOH 174 574 545 HOH HOH A . 
I 4 HOH 175 575 546 HOH HOH A . 
I 4 HOH 176 576 548 HOH HOH A . 
I 4 HOH 177 577 551 HOH HOH A . 
I 4 HOH 178 578 553 HOH HOH A . 
I 4 HOH 179 579 567 HOH HOH A . 
I 4 HOH 180 580 570 HOH HOH A . 
I 4 HOH 181 581 574 HOH HOH A . 
I 4 HOH 182 582 576 HOH HOH A . 
I 4 HOH 183 583 582 HOH HOH A . 
I 4 HOH 184 584 584 HOH HOH A . 
I 4 HOH 185 585 590 HOH HOH A . 
I 4 HOH 186 586 592 HOH HOH A . 
I 4 HOH 187 587 595 HOH HOH A . 
J 4 HOH 1   301 12  HOH HOH B . 
J 4 HOH 2   302 18  HOH HOH B . 
J 4 HOH 3   303 22  HOH HOH B . 
J 4 HOH 4   304 28  HOH HOH B . 
J 4 HOH 5   305 32  HOH HOH B . 
J 4 HOH 6   306 35  HOH HOH B . 
J 4 HOH 7   307 36  HOH HOH B . 
J 4 HOH 8   308 38  HOH HOH B . 
J 4 HOH 9   309 47  HOH HOH B . 
J 4 HOH 10  310 48  HOH HOH B . 
J 4 HOH 11  311 49  HOH HOH B . 
J 4 HOH 12  312 50  HOH HOH B . 
J 4 HOH 13  313 51  HOH HOH B . 
J 4 HOH 14  314 53  HOH HOH B . 
J 4 HOH 15  315 55  HOH HOH B . 
J 4 HOH 16  316 61  HOH HOH B . 
J 4 HOH 17  317 64  HOH HOH B . 
J 4 HOH 18  318 65  HOH HOH B . 
J 4 HOH 19  319 66  HOH HOH B . 
J 4 HOH 20  320 68  HOH HOH B . 
J 4 HOH 21  321 71  HOH HOH B . 
J 4 HOH 22  322 75  HOH HOH B . 
J 4 HOH 23  323 80  HOH HOH B . 
J 4 HOH 24  324 82  HOH HOH B . 
J 4 HOH 25  325 84  HOH HOH B . 
J 4 HOH 26  326 85  HOH HOH B . 
J 4 HOH 27  327 86  HOH HOH B . 
J 4 HOH 28  328 91  HOH HOH B . 
J 4 HOH 29  329 93  HOH HOH B . 
J 4 HOH 30  330 96  HOH HOH B . 
J 4 HOH 31  331 98  HOH HOH B . 
J 4 HOH 32  332 99  HOH HOH B . 
J 4 HOH 33  333 100 HOH HOH B . 
J 4 HOH 34  334 102 HOH HOH B . 
J 4 HOH 35  335 103 HOH HOH B . 
J 4 HOH 36  336 105 HOH HOH B . 
J 4 HOH 37  337 114 HOH HOH B . 
J 4 HOH 38  338 115 HOH HOH B . 
J 4 HOH 39  339 120 HOH HOH B . 
J 4 HOH 40  340 130 HOH HOH B . 
J 4 HOH 41  341 137 HOH HOH B . 
J 4 HOH 42  342 138 HOH HOH B . 
J 4 HOH 43  343 139 HOH HOH B . 
J 4 HOH 44  344 141 HOH HOH B . 
J 4 HOH 45  345 142 HOH HOH B . 
J 4 HOH 46  346 144 HOH HOH B . 
J 4 HOH 47  347 148 HOH HOH B . 
J 4 HOH 48  348 155 HOH HOH B . 
J 4 HOH 49  349 162 HOH HOH B . 
J 4 HOH 50  350 166 HOH HOH B . 
J 4 HOH 51  351 167 HOH HOH B . 
J 4 HOH 52  352 168 HOH HOH B . 
J 4 HOH 53  353 169 HOH HOH B . 
J 4 HOH 54  354 170 HOH HOH B . 
J 4 HOH 55  355 175 HOH HOH B . 
J 4 HOH 56  356 181 HOH HOH B . 
J 4 HOH 57  357 184 HOH HOH B . 
J 4 HOH 58  358 185 HOH HOH B . 
J 4 HOH 59  359 186 HOH HOH B . 
J 4 HOH 60  360 188 HOH HOH B . 
J 4 HOH 61  361 194 HOH HOH B . 
J 4 HOH 62  362 197 HOH HOH B . 
J 4 HOH 63  363 200 HOH HOH B . 
J 4 HOH 64  364 202 HOH HOH B . 
J 4 HOH 65  365 204 HOH HOH B . 
J 4 HOH 66  366 207 HOH HOH B . 
J 4 HOH 67  367 211 HOH HOH B . 
J 4 HOH 68  368 215 HOH HOH B . 
J 4 HOH 69  369 219 HOH HOH B . 
J 4 HOH 70  370 221 HOH HOH B . 
J 4 HOH 71  371 223 HOH HOH B . 
J 4 HOH 72  372 224 HOH HOH B . 
J 4 HOH 73  373 225 HOH HOH B . 
J 4 HOH 74  374 228 HOH HOH B . 
J 4 HOH 75  375 229 HOH HOH B . 
J 4 HOH 76  376 230 HOH HOH B . 
J 4 HOH 77  377 231 HOH HOH B . 
J 4 HOH 78  378 240 HOH HOH B . 
J 4 HOH 79  379 242 HOH HOH B . 
J 4 HOH 80  380 244 HOH HOH B . 
J 4 HOH 81  381 245 HOH HOH B . 
J 4 HOH 82  382 248 HOH HOH B . 
J 4 HOH 83  383 254 HOH HOH B . 
J 4 HOH 84  384 255 HOH HOH B . 
J 4 HOH 85  385 265 HOH HOH B . 
J 4 HOH 86  386 268 HOH HOH B . 
J 4 HOH 87  387 269 HOH HOH B . 
J 4 HOH 88  388 270 HOH HOH B . 
J 4 HOH 89  389 271 HOH HOH B . 
J 4 HOH 90  390 273 HOH HOH B . 
J 4 HOH 91  391 276 HOH HOH B . 
J 4 HOH 92  392 277 HOH HOH B . 
J 4 HOH 93  393 278 HOH HOH B . 
J 4 HOH 94  394 287 HOH HOH B . 
J 4 HOH 95  395 289 HOH HOH B . 
J 4 HOH 96  396 293 HOH HOH B . 
J 4 HOH 97  397 294 HOH HOH B . 
J 4 HOH 98  398 308 HOH HOH B . 
J 4 HOH 99  399 309 HOH HOH B . 
J 4 HOH 100 400 319 HOH HOH B . 
J 4 HOH 101 401 320 HOH HOH B . 
J 4 HOH 102 402 322 HOH HOH B . 
J 4 HOH 103 403 323 HOH HOH B . 
J 4 HOH 104 404 324 HOH HOH B . 
J 4 HOH 105 405 326 HOH HOH B . 
J 4 HOH 106 406 329 HOH HOH B . 
J 4 HOH 107 407 331 HOH HOH B . 
J 4 HOH 108 408 339 HOH HOH B . 
J 4 HOH 109 409 340 HOH HOH B . 
J 4 HOH 110 410 344 HOH HOH B . 
J 4 HOH 111 411 346 HOH HOH B . 
J 4 HOH 112 412 353 HOH HOH B . 
J 4 HOH 113 413 354 HOH HOH B . 
J 4 HOH 114 414 357 HOH HOH B . 
J 4 HOH 115 415 359 HOH HOH B . 
J 4 HOH 116 416 361 HOH HOH B . 
J 4 HOH 117 417 365 HOH HOH B . 
J 4 HOH 118 418 367 HOH HOH B . 
J 4 HOH 119 419 373 HOH HOH B . 
J 4 HOH 120 420 375 HOH HOH B . 
J 4 HOH 121 421 380 HOH HOH B . 
J 4 HOH 122 422 382 HOH HOH B . 
J 4 HOH 123 423 383 HOH HOH B . 
J 4 HOH 124 424 389 HOH HOH B . 
J 4 HOH 125 425 395 HOH HOH B . 
J 4 HOH 126 426 396 HOH HOH B . 
J 4 HOH 127 427 399 HOH HOH B . 
J 4 HOH 128 428 403 HOH HOH B . 
J 4 HOH 129 429 405 HOH HOH B . 
J 4 HOH 130 430 408 HOH HOH B . 
J 4 HOH 131 431 412 HOH HOH B . 
J 4 HOH 132 432 417 HOH HOH B . 
J 4 HOH 133 433 422 HOH HOH B . 
J 4 HOH 134 434 423 HOH HOH B . 
J 4 HOH 135 435 425 HOH HOH B . 
J 4 HOH 136 436 431 HOH HOH B . 
J 4 HOH 137 437 433 HOH HOH B . 
J 4 HOH 138 438 434 HOH HOH B . 
J 4 HOH 139 439 437 HOH HOH B . 
J 4 HOH 140 440 443 HOH HOH B . 
J 4 HOH 141 441 445 HOH HOH B . 
J 4 HOH 142 442 448 HOH HOH B . 
J 4 HOH 143 443 452 HOH HOH B . 
J 4 HOH 144 444 453 HOH HOH B . 
J 4 HOH 145 445 456 HOH HOH B . 
J 4 HOH 146 446 461 HOH HOH B . 
J 4 HOH 147 447 462 HOH HOH B . 
J 4 HOH 148 448 468 HOH HOH B . 
J 4 HOH 149 449 469 HOH HOH B . 
J 4 HOH 150 450 472 HOH HOH B . 
J 4 HOH 151 451 474 HOH HOH B . 
J 4 HOH 152 452 477 HOH HOH B . 
J 4 HOH 153 453 479 HOH HOH B . 
J 4 HOH 154 454 481 HOH HOH B . 
J 4 HOH 155 455 482 HOH HOH B . 
J 4 HOH 156 456 487 HOH HOH B . 
J 4 HOH 157 457 495 HOH HOH B . 
J 4 HOH 158 458 502 HOH HOH B . 
J 4 HOH 159 459 506 HOH HOH B . 
J 4 HOH 160 460 508 HOH HOH B . 
J 4 HOH 161 461 510 HOH HOH B . 
J 4 HOH 162 462 511 HOH HOH B . 
J 4 HOH 163 463 512 HOH HOH B . 
J 4 HOH 164 464 514 HOH HOH B . 
J 4 HOH 165 465 516 HOH HOH B . 
J 4 HOH 166 466 518 HOH HOH B . 
J 4 HOH 167 467 519 HOH HOH B . 
J 4 HOH 168 468 520 HOH HOH B . 
J 4 HOH 169 469 522 HOH HOH B . 
J 4 HOH 170 470 523 HOH HOH B . 
J 4 HOH 171 471 524 HOH HOH B . 
J 4 HOH 172 472 527 HOH HOH B . 
J 4 HOH 173 473 528 HOH HOH B . 
J 4 HOH 174 474 530 HOH HOH B . 
J 4 HOH 175 475 534 HOH HOH B . 
J 4 HOH 176 476 538 HOH HOH B . 
J 4 HOH 177 477 539 HOH HOH B . 
J 4 HOH 178 478 540 HOH HOH B . 
J 4 HOH 179 479 543 HOH HOH B . 
J 4 HOH 180 480 556 HOH HOH B . 
J 4 HOH 181 481 559 HOH HOH B . 
J 4 HOH 182 482 561 HOH HOH B . 
J 4 HOH 183 483 564 HOH HOH B . 
J 4 HOH 184 484 571 HOH HOH B . 
J 4 HOH 185 485 572 HOH HOH B . 
J 4 HOH 186 486 575 HOH HOH B . 
J 4 HOH 187 487 578 HOH HOH B . 
J 4 HOH 188 488 579 HOH HOH B . 
J 4 HOH 189 489 583 HOH HOH B . 
J 4 HOH 190 490 585 HOH HOH B . 
J 4 HOH 191 491 588 HOH HOH B . 
J 4 HOH 192 492 589 HOH HOH B . 
J 4 HOH 193 493 591 HOH HOH B . 
J 4 HOH 194 494 593 HOH HOH B . 
J 4 HOH 195 495 594 HOH HOH B . 
J 4 HOH 196 496 596 HOH HOH B . 
K 4 HOH 1   701 1   HOH HOH C . 
K 4 HOH 2   702 3   HOH HOH C . 
K 4 HOH 3   703 6   HOH HOH C . 
K 4 HOH 4   704 8   HOH HOH C . 
K 4 HOH 5   705 10  HOH HOH C . 
K 4 HOH 6   706 14  HOH HOH C . 
K 4 HOH 7   707 17  HOH HOH C . 
K 4 HOH 8   708 25  HOH HOH C . 
K 4 HOH 9   709 30  HOH HOH C . 
K 4 HOH 10  710 33  HOH HOH C . 
K 4 HOH 11  711 34  HOH HOH C . 
K 4 HOH 12  712 41  HOH HOH C . 
K 4 HOH 13  713 42  HOH HOH C . 
K 4 HOH 14  714 44  HOH HOH C . 
K 4 HOH 15  715 45  HOH HOH C . 
K 4 HOH 16  716 52  HOH HOH C . 
K 4 HOH 17  717 59  HOH HOH C . 
K 4 HOH 18  718 62  HOH HOH C . 
K 4 HOH 19  719 63  HOH HOH C . 
K 4 HOH 20  720 67  HOH HOH C . 
K 4 HOH 21  721 74  HOH HOH C . 
K 4 HOH 22  722 76  HOH HOH C . 
K 4 HOH 23  723 77  HOH HOH C . 
K 4 HOH 24  724 78  HOH HOH C . 
K 4 HOH 25  725 83  HOH HOH C . 
K 4 HOH 26  726 87  HOH HOH C . 
K 4 HOH 27  727 88  HOH HOH C . 
K 4 HOH 28  728 89  HOH HOH C . 
K 4 HOH 29  729 90  HOH HOH C . 
K 4 HOH 30  730 94  HOH HOH C . 
K 4 HOH 31  731 95  HOH HOH C . 
K 4 HOH 32  732 107 HOH HOH C . 
K 4 HOH 33  733 108 HOH HOH C . 
K 4 HOH 34  734 109 HOH HOH C . 
K 4 HOH 35  735 110 HOH HOH C . 
K 4 HOH 36  736 119 HOH HOH C . 
K 4 HOH 37  737 121 HOH HOH C . 
K 4 HOH 38  738 123 HOH HOH C . 
K 4 HOH 39  739 124 HOH HOH C . 
K 4 HOH 40  740 126 HOH HOH C . 
K 4 HOH 41  741 127 HOH HOH C . 
K 4 HOH 42  742 128 HOH HOH C . 
K 4 HOH 43  743 132 HOH HOH C . 
K 4 HOH 44  744 134 HOH HOH C . 
K 4 HOH 45  745 135 HOH HOH C . 
K 4 HOH 46  746 140 HOH HOH C . 
K 4 HOH 47  747 143 HOH HOH C . 
K 4 HOH 48  748 150 HOH HOH C . 
K 4 HOH 49  749 151 HOH HOH C . 
K 4 HOH 50  750 152 HOH HOH C . 
K 4 HOH 51  751 153 HOH HOH C . 
K 4 HOH 52  752 164 HOH HOH C . 
K 4 HOH 53  753 165 HOH HOH C . 
K 4 HOH 54  754 172 HOH HOH C . 
K 4 HOH 55  755 173 HOH HOH C . 
K 4 HOH 56  756 176 HOH HOH C . 
K 4 HOH 57  757 180 HOH HOH C . 
K 4 HOH 58  758 183 HOH HOH C . 
K 4 HOH 59  759 187 HOH HOH C . 
K 4 HOH 60  760 189 HOH HOH C . 
K 4 HOH 61  761 191 HOH HOH C . 
K 4 HOH 62  762 192 HOH HOH C . 
K 4 HOH 63  763 195 HOH HOH C . 
K 4 HOH 64  764 198 HOH HOH C . 
K 4 HOH 65  765 201 HOH HOH C . 
K 4 HOH 66  766 203 HOH HOH C . 
K 4 HOH 67  767 206 HOH HOH C . 
K 4 HOH 68  768 208 HOH HOH C . 
K 4 HOH 69  769 213 HOH HOH C . 
K 4 HOH 70  770 214 HOH HOH C . 
K 4 HOH 71  771 217 HOH HOH C . 
K 4 HOH 72  772 233 HOH HOH C . 
K 4 HOH 73  773 234 HOH HOH C . 
K 4 HOH 74  774 238 HOH HOH C . 
K 4 HOH 75  775 239 HOH HOH C . 
K 4 HOH 76  776 243 HOH HOH C . 
K 4 HOH 77  777 246 HOH HOH C . 
K 4 HOH 78  778 247 HOH HOH C . 
K 4 HOH 79  779 249 HOH HOH C . 
K 4 HOH 80  780 250 HOH HOH C . 
K 4 HOH 81  781 251 HOH HOH C . 
K 4 HOH 82  782 253 HOH HOH C . 
K 4 HOH 83  783 256 HOH HOH C . 
K 4 HOH 84  784 257 HOH HOH C . 
K 4 HOH 85  785 259 HOH HOH C . 
K 4 HOH 86  786 263 HOH HOH C . 
K 4 HOH 87  787 274 HOH HOH C . 
K 4 HOH 88  788 275 HOH HOH C . 
K 4 HOH 89  789 280 HOH HOH C . 
K 4 HOH 90  790 282 HOH HOH C . 
K 4 HOH 91  791 283 HOH HOH C . 
K 4 HOH 92  792 285 HOH HOH C . 
K 4 HOH 93  793 288 HOH HOH C . 
K 4 HOH 94  794 299 HOH HOH C . 
K 4 HOH 95  795 301 HOH HOH C . 
K 4 HOH 96  796 303 HOH HOH C . 
K 4 HOH 97  797 304 HOH HOH C . 
K 4 HOH 98  798 305 HOH HOH C . 
K 4 HOH 99  799 306 HOH HOH C . 
K 4 HOH 100 800 307 HOH HOH C . 
K 4 HOH 101 801 312 HOH HOH C . 
K 4 HOH 102 802 314 HOH HOH C . 
K 4 HOH 103 803 315 HOH HOH C . 
K 4 HOH 104 804 316 HOH HOH C . 
K 4 HOH 105 805 318 HOH HOH C . 
K 4 HOH 106 806 325 HOH HOH C . 
K 4 HOH 107 807 327 HOH HOH C . 
K 4 HOH 108 808 332 HOH HOH C . 
K 4 HOH 109 809 335 HOH HOH C . 
K 4 HOH 110 810 336 HOH HOH C . 
K 4 HOH 111 811 337 HOH HOH C . 
K 4 HOH 112 812 342 HOH HOH C . 
K 4 HOH 113 813 349 HOH HOH C . 
K 4 HOH 114 814 350 HOH HOH C . 
K 4 HOH 115 815 351 HOH HOH C . 
K 4 HOH 116 816 352 HOH HOH C . 
K 4 HOH 117 817 356 HOH HOH C . 
K 4 HOH 118 818 363 HOH HOH C . 
K 4 HOH 119 819 364 HOH HOH C . 
K 4 HOH 120 820 366 HOH HOH C . 
K 4 HOH 121 821 371 HOH HOH C . 
K 4 HOH 122 822 374 HOH HOH C . 
K 4 HOH 123 823 377 HOH HOH C . 
K 4 HOH 124 824 378 HOH HOH C . 
K 4 HOH 125 825 381 HOH HOH C . 
K 4 HOH 126 826 384 HOH HOH C . 
K 4 HOH 127 827 391 HOH HOH C . 
K 4 HOH 128 828 392 HOH HOH C . 
K 4 HOH 129 829 393 HOH HOH C . 
K 4 HOH 130 830 394 HOH HOH C . 
K 4 HOH 131 831 400 HOH HOH C . 
K 4 HOH 132 832 406 HOH HOH C . 
K 4 HOH 133 833 409 HOH HOH C . 
K 4 HOH 134 834 410 HOH HOH C . 
K 4 HOH 135 835 411 HOH HOH C . 
K 4 HOH 136 836 419 HOH HOH C . 
K 4 HOH 137 837 420 HOH HOH C . 
K 4 HOH 138 838 421 HOH HOH C . 
K 4 HOH 139 839 428 HOH HOH C . 
K 4 HOH 140 840 444 HOH HOH C . 
K 4 HOH 141 841 450 HOH HOH C . 
K 4 HOH 142 842 451 HOH HOH C . 
K 4 HOH 143 843 454 HOH HOH C . 
K 4 HOH 144 844 464 HOH HOH C . 
K 4 HOH 145 845 466 HOH HOH C . 
K 4 HOH 146 846 470 HOH HOH C . 
K 4 HOH 147 847 471 HOH HOH C . 
K 4 HOH 148 848 483 HOH HOH C . 
K 4 HOH 149 849 484 HOH HOH C . 
K 4 HOH 150 850 485 HOH HOH C . 
K 4 HOH 151 851 489 HOH HOH C . 
K 4 HOH 152 852 494 HOH HOH C . 
K 4 HOH 153 853 497 HOH HOH C . 
K 4 HOH 154 854 499 HOH HOH C . 
K 4 HOH 155 855 501 HOH HOH C . 
K 4 HOH 156 856 504 HOH HOH C . 
K 4 HOH 157 857 507 HOH HOH C . 
K 4 HOH 158 858 509 HOH HOH C . 
K 4 HOH 159 859 513 HOH HOH C . 
K 4 HOH 160 860 525 HOH HOH C . 
K 4 HOH 161 861 526 HOH HOH C . 
K 4 HOH 162 862 532 HOH HOH C . 
K 4 HOH 163 863 536 HOH HOH C . 
K 4 HOH 164 864 542 HOH HOH C . 
K 4 HOH 165 865 547 HOH HOH C . 
K 4 HOH 166 866 549 HOH HOH C . 
K 4 HOH 167 867 552 HOH HOH C . 
K 4 HOH 168 868 554 HOH HOH C . 
K 4 HOH 169 869 555 HOH HOH C . 
K 4 HOH 170 870 557 HOH HOH C . 
K 4 HOH 171 871 558 HOH HOH C . 
K 4 HOH 172 872 562 HOH HOH C . 
K 4 HOH 173 873 563 HOH HOH C . 
K 4 HOH 174 874 566 HOH HOH C . 
K 4 HOH 175 875 568 HOH HOH C . 
K 4 HOH 176 876 569 HOH HOH C . 
K 4 HOH 177 877 577 HOH HOH C . 
K 4 HOH 178 878 580 HOH HOH C . 
K 4 HOH 179 879 581 HOH HOH C . 
K 4 HOH 180 880 586 HOH HOH C . 
K 4 HOH 181 881 587 HOH HOH C . 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CBASS    'data collection' .        ? 1 
SHELXS   phasing           .        ? 2 
REFMAC   refinement        5.7.0032 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
_cell.entry_id           4K29 
_cell.length_a           115.052 
_cell.length_b           144.576 
_cell.length_c           129.568 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              24 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4K29 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
# 
_exptl.entry_id          4K29 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.76 
_exptl_crystal.density_percent_sol   55.39 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pdbx_details    
'0.8M Potassium Sodium Tartrate, 0.1M TRIS, 0.5% PEGMME 5000, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315' 
_diffrn_detector.pdbx_collection_date   2013-04-03 
_diffrn_detector.details                mirrors 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si 111 CHANNEL' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9793 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'NSLS BEAMLINE X29A' 
_diffrn_source.pdbx_synchrotron_site       NSLS 
_diffrn_source.pdbx_synchrotron_beamline   X29A 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9793 
# 
_reflns.entry_id                     4K29 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   0.0 
_reflns.d_resolution_low             50.0 
_reflns.d_resolution_high            1.66 
_reflns.number_obs                   126795 
_reflns.number_all                   126795 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.115 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.3 
_reflns.B_iso_Wilson_estimate        13.8 
_reflns.pdbx_redundancy              13.9 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.66 
_reflns_shell.d_res_low              1.69 
_reflns_shell.percent_possible_all   98.0 
_reflns_shell.Rmerge_I_obs           0.260 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        12.3 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      6165 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 4K29 
_refine.ls_number_reflns_obs                     120222 
_refine.ls_number_reflns_all                     126555 
_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                             44.49 
_refine.ls_d_res_high                            1.66 
_refine.ls_percent_reflns_obs                    99.63 
_refine.ls_R_factor_obs                          0.18207 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.18122 
_refine.ls_R_factor_R_free                       0.19799 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  6351 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.947 
_refine.correlation_coeff_Fo_to_Fc_free          0.939 
_refine.B_iso_mean                               11.405 
_refine.aniso_B[1][1]                            0.00 
_refine.aniso_B[2][2]                            0.07 
_refine.aniso_B[3][3]                            -0.07 
_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          SAD 
_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                       0.082 
_refine.pdbx_overall_ESU_R_Free                  0.079 
_refine.overall_SU_ML                            0.045 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.282 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_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        6097 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             564 
_refine_hist.number_atoms_total               6703 
_refine_hist.d_res_high                       1.66 
_refine_hist.d_res_low                        44.49 
# 
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_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       0.005  0.019  ? 6239  ? 'X-RAY DIFFRACTION' 
r_bond_other_d         0.001  0.020  ? 6165  ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    1.069  1.991  ? 8438  ? 'X-RAY DIFFRACTION' 
r_angle_other_deg      0.701  3.000  ? 14124 ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 5.198  5.000  ? 802   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 27.091 22.921 ? 267   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 11.927 15.000 ? 976   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 16.600 15.000 ? 66    ? 'X-RAY DIFFRACTION' 
r_chiral_restr         0.061  0.200  ? 955   ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   0.004  0.021  ? 7075  ? 'X-RAY DIFFRACTION' 
r_gen_planes_other     0.001  0.020  ? 1369  ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.660 
_refine_ls_shell.d_res_low                        1.703 
_refine_ls_shell.number_reflns_R_work             8696 
_refine_ls_shell.R_factor_R_work                  0.193 
_refine_ls_shell.percent_reflns_obs               98.04 
_refine_ls_shell.R_factor_R_free                  0.211 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             424 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                9120 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_database_PDB_matrix.entry_id          4K29 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_struct.entry_id                  4K29 
_struct.title                     'Crystal structure of an enoyl-CoA hydratase/isomerase from Xanthobacter autotrophicus Py2' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4K29 
_struct_keywords.pdbx_keywords   ISOMERASE 
_struct_keywords.text            
;PSI-Biology, NYSGRC, Structural Genomics, New York Structural Genomics Research Consortium, dimer of trimers, crotonase superfamily, oxyanion hole, ISOMERASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A7IKN6_XANP2 
_struct_ref.pdbx_db_accession          A7IKN6 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTYSKILYETLHGVARITLNRPERTNALDQEMLGEINAAMDAAEADAGVKAVIVRGAGNAFSSGFDLKAQMEARPAGVDA
WRPLLRKDFDTVMRFWHCPKPTIAAVRGPCLAGACELALACDMTIATEDAFFGEPELKFGAGIVVMLLPWIVGPKIAKEI
ILLGEDRVPARRAAEIGMVNRVVDGDGLDAEALRIARHIGAIDPGLVKETKRALNRALETQGMLQALESALEIDLAIEGA
GSPDKIAFFEVARRDGLRAAIAWRDARFPARDA
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 4K29 A 23 ? 295 ? A7IKN6 1 ? 273 ? 1 273 
2 1 4K29 B 23 ? 295 ? A7IKN6 1 ? 273 ? 1 273 
3 1 4K29 C 23 ? 295 ? A7IKN6 1 ? 273 ? 1 273 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4K29 MSE A 1  ? UNP A7IKN6 ? ? 'expression tag' -21 1  
1 4K29 HIS A 2  ? UNP A7IKN6 ? ? 'expression tag' -20 2  
1 4K29 HIS A 3  ? UNP A7IKN6 ? ? 'expression tag' -19 3  
1 4K29 HIS A 4  ? UNP A7IKN6 ? ? 'expression tag' -18 4  
1 4K29 HIS A 5  ? UNP A7IKN6 ? ? 'expression tag' -17 5  
1 4K29 HIS A 6  ? UNP A7IKN6 ? ? 'expression tag' -16 6  
1 4K29 HIS A 7  ? UNP A7IKN6 ? ? 'expression tag' -15 7  
1 4K29 SER A 8  ? UNP A7IKN6 ? ? 'expression tag' -14 8  
1 4K29 SER A 9  ? UNP A7IKN6 ? ? 'expression tag' -13 9  
1 4K29 GLY A 10 ? UNP A7IKN6 ? ? 'expression tag' -12 10 
1 4K29 VAL A 11 ? UNP A7IKN6 ? ? 'expression tag' -11 11 
1 4K29 ASP A 12 ? UNP A7IKN6 ? ? 'expression tag' -10 12 
1 4K29 LEU A 13 ? UNP A7IKN6 ? ? 'expression tag' -9  13 
1 4K29 GLY A 14 ? UNP A7IKN6 ? ? 'expression tag' -8  14 
1 4K29 THR A 15 ? UNP A7IKN6 ? ? 'expression tag' -7  15 
1 4K29 GLU A 16 ? UNP A7IKN6 ? ? 'expression tag' -6  16 
1 4K29 ASN A 17 ? UNP A7IKN6 ? ? 'expression tag' -5  17 
1 4K29 LEU A 18 ? UNP A7IKN6 ? ? 'expression tag' -4  18 
1 4K29 TYR A 19 ? UNP A7IKN6 ? ? 'expression tag' -3  19 
1 4K29 PHE A 20 ? UNP A7IKN6 ? ? 'expression tag' -2  20 
1 4K29 GLN A 21 ? UNP A7IKN6 ? ? 'expression tag' -1  21 
1 4K29 SER A 22 ? UNP A7IKN6 ? ? 'expression tag' 0   22 
2 4K29 MSE B 1  ? UNP A7IKN6 ? ? 'expression tag' -21 23 
2 4K29 HIS B 2  ? UNP A7IKN6 ? ? 'expression tag' -20 24 
2 4K29 HIS B 3  ? UNP A7IKN6 ? ? 'expression tag' -19 25 
2 4K29 HIS B 4  ? UNP A7IKN6 ? ? 'expression tag' -18 26 
2 4K29 HIS B 5  ? UNP A7IKN6 ? ? 'expression tag' -17 27 
2 4K29 HIS B 6  ? UNP A7IKN6 ? ? 'expression tag' -16 28 
2 4K29 HIS B 7  ? UNP A7IKN6 ? ? 'expression tag' -15 29 
2 4K29 SER B 8  ? UNP A7IKN6 ? ? 'expression tag' -14 30 
2 4K29 SER B 9  ? UNP A7IKN6 ? ? 'expression tag' -13 31 
2 4K29 GLY B 10 ? UNP A7IKN6 ? ? 'expression tag' -12 32 
2 4K29 VAL B 11 ? UNP A7IKN6 ? ? 'expression tag' -11 33 
2 4K29 ASP B 12 ? UNP A7IKN6 ? ? 'expression tag' -10 34 
2 4K29 LEU B 13 ? UNP A7IKN6 ? ? 'expression tag' -9  35 
2 4K29 GLY B 14 ? UNP A7IKN6 ? ? 'expression tag' -8  36 
2 4K29 THR B 15 ? UNP A7IKN6 ? ? 'expression tag' -7  37 
2 4K29 GLU B 16 ? UNP A7IKN6 ? ? 'expression tag' -6  38 
2 4K29 ASN B 17 ? UNP A7IKN6 ? ? 'expression tag' -5  39 
2 4K29 LEU B 18 ? UNP A7IKN6 ? ? 'expression tag' -4  40 
2 4K29 TYR B 19 ? UNP A7IKN6 ? ? 'expression tag' -3  41 
2 4K29 PHE B 20 ? UNP A7IKN6 ? ? 'expression tag' -2  42 
2 4K29 GLN B 21 ? UNP A7IKN6 ? ? 'expression tag' -1  43 
2 4K29 SER B 22 ? UNP A7IKN6 ? ? 'expression tag' 0   44 
3 4K29 MSE C 1  ? UNP A7IKN6 ? ? 'expression tag' -21 45 
3 4K29 HIS C 2  ? UNP A7IKN6 ? ? 'expression tag' -20 46 
3 4K29 HIS C 3  ? UNP A7IKN6 ? ? 'expression tag' -19 47 
3 4K29 HIS C 4  ? UNP A7IKN6 ? ? 'expression tag' -18 48 
3 4K29 HIS C 5  ? UNP A7IKN6 ? ? 'expression tag' -17 49 
3 4K29 HIS C 6  ? UNP A7IKN6 ? ? 'expression tag' -16 50 
3 4K29 HIS C 7  ? UNP A7IKN6 ? ? 'expression tag' -15 51 
3 4K29 SER C 8  ? UNP A7IKN6 ? ? 'expression tag' -14 52 
3 4K29 SER C 9  ? UNP A7IKN6 ? ? 'expression tag' -13 53 
3 4K29 GLY C 10 ? UNP A7IKN6 ? ? 'expression tag' -12 54 
3 4K29 VAL C 11 ? UNP A7IKN6 ? ? 'expression tag' -11 55 
3 4K29 ASP C 12 ? UNP A7IKN6 ? ? 'expression tag' -10 56 
3 4K29 LEU C 13 ? UNP A7IKN6 ? ? 'expression tag' -9  57 
3 4K29 GLY C 14 ? UNP A7IKN6 ? ? 'expression tag' -8  58 
3 4K29 THR C 15 ? UNP A7IKN6 ? ? 'expression tag' -7  59 
3 4K29 GLU C 16 ? UNP A7IKN6 ? ? 'expression tag' -6  60 
3 4K29 ASN C 17 ? UNP A7IKN6 ? ? 'expression tag' -5  61 
3 4K29 LEU C 18 ? UNP A7IKN6 ? ? 'expression tag' -4  62 
3 4K29 TYR C 19 ? UNP A7IKN6 ? ? 'expression tag' -3  63 
3 4K29 PHE C 20 ? UNP A7IKN6 ? ? 'expression tag' -2  64 
3 4K29 GLN C 21 ? UNP A7IKN6 ? ? 'expression tag' -1  65 
3 4K29 SER C 22 ? UNP A7IKN6 ? ? 'expression tag' 0   66 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA hexameric 6 
2 software_defined_assembly            PISA trimeric  3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 25330 ? 
1 MORE         -142  ? 
1 'SSA (A^2)'  49820 ? 
2 'ABSA (A^2)' 10130 ? 
2 MORE         -69   ? 
2 'SSA (A^2)'  27450 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2 A,B,C,D,E,F,G,H,I,J,K 
2 1   A,B,C,D,E,F,G,H,I,J,K 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 3_555 -x,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 64.7840000000 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ARG A 43  ? THR A 47  ? ARG A 21  THR A 25  5 ? 5  
HELX_P HELX_P2  2  ASP A 51  ? ASP A 68  ? ASP A 29  ASP A 46  1 ? 18 
HELX_P HELX_P3  3  ASP A 88  ? ARG A 96  ? ASP A 66  ARG A 74  1 ? 9  
HELX_P HELX_P4  4  GLY A 99  ? CYS A 120 ? GLY A 77  CYS A 98  1 ? 22 
HELX_P HELX_P5  5  ALA A 134 ? CYS A 143 ? ALA A 112 CYS A 121 1 ? 10 
HELX_P HELX_P6  6  PRO A 157 ? GLY A 162 ? PRO A 135 GLY A 140 5 ? 6  
HELX_P HELX_P7  7  LEU A 169 ? GLY A 175 ? LEU A 147 GLY A 153 1 ? 7  
HELX_P HELX_P8  8  GLY A 175 ? GLY A 186 ? GLY A 153 GLY A 164 1 ? 12 
HELX_P HELX_P9  9  ALA A 192 ? ILE A 198 ? ALA A 170 ILE A 176 1 ? 7  
HELX_P HELX_P10 10 ASP A 206 ? ASP A 208 ? ASP A 184 ASP A 186 5 ? 3  
HELX_P HELX_P11 11 GLY A 209 ? ALA A 223 ? GLY A 187 ALA A 201 1 ? 15 
HELX_P HELX_P12 12 ASP A 225 ? GLN A 243 ? ASP A 203 GLN A 221 1 ? 19 
HELX_P HELX_P13 13 GLY A 244 ? GLY A 263 ? GLY A 222 GLY A 241 1 ? 20 
HELX_P HELX_P14 14 SER A 264 ? GLY A 278 ? SER A 242 GLY A 256 1 ? 15 
HELX_P HELX_P15 15 GLY A 278 ? ARG A 289 ? GLY A 256 ARG A 267 1 ? 12 
HELX_P HELX_P16 16 ARG B 43  ? THR B 47  ? ARG B 21  THR B 25  5 ? 5  
HELX_P HELX_P17 17 ASP B 51  ? ASP B 68  ? ASP B 29  ASP B 46  1 ? 18 
HELX_P HELX_P18 18 ASP B 88  ? ARG B 96  ? ASP B 66  ARG B 74  1 ? 9  
HELX_P HELX_P19 19 GLY B 99  ? CYS B 120 ? GLY B 77  CYS B 98  1 ? 22 
HELX_P HELX_P20 20 ALA B 134 ? CYS B 143 ? ALA B 112 CYS B 121 1 ? 10 
HELX_P HELX_P21 21 PRO B 157 ? GLY B 162 ? PRO B 135 GLY B 140 5 ? 6  
HELX_P HELX_P22 22 LEU B 169 ? VAL B 174 ? LEU B 147 VAL B 152 1 ? 6  
HELX_P HELX_P23 23 GLY B 175 ? GLY B 186 ? GLY B 153 GLY B 164 1 ? 12 
HELX_P HELX_P24 24 ALA B 192 ? ILE B 198 ? ALA B 170 ILE B 176 1 ? 7  
HELX_P HELX_P25 25 ASP B 206 ? ASP B 208 ? ASP B 184 ASP B 186 5 ? 3  
HELX_P HELX_P26 26 GLY B 209 ? ALA B 223 ? GLY B 187 ALA B 201 1 ? 15 
HELX_P HELX_P27 27 ASP B 225 ? GLN B 243 ? ASP B 203 GLN B 221 1 ? 19 
HELX_P HELX_P28 28 GLY B 244 ? GLY B 263 ? GLY B 222 GLY B 241 1 ? 20 
HELX_P HELX_P29 29 SER B 264 ? GLY B 278 ? SER B 242 GLY B 256 1 ? 15 
HELX_P HELX_P30 30 GLY B 278 ? ARG B 289 ? GLY B 256 ARG B 267 1 ? 12 
HELX_P HELX_P31 31 ARG C 43  ? THR C 47  ? ARG C 21  THR C 25  5 ? 5  
HELX_P HELX_P32 32 ASP C 51  ? ASP C 68  ? ASP C 29  ASP C 46  1 ? 18 
HELX_P HELX_P33 33 ASP C 88  ? ARG C 96  ? ASP C 66  ARG C 74  1 ? 9  
HELX_P HELX_P34 34 GLY C 99  ? CYS C 120 ? GLY C 77  CYS C 98  1 ? 22 
HELX_P HELX_P35 35 ALA C 134 ? CYS C 143 ? ALA C 112 CYS C 121 1 ? 10 
HELX_P HELX_P36 36 PRO C 157 ? GLY C 162 ? PRO C 135 GLY C 140 5 ? 6  
HELX_P HELX_P37 37 LEU C 169 ? VAL C 174 ? LEU C 147 VAL C 152 1 ? 6  
HELX_P HELX_P38 38 GLY C 175 ? GLY C 186 ? GLY C 153 GLY C 164 1 ? 12 
HELX_P HELX_P39 39 ALA C 192 ? ILE C 198 ? ALA C 170 ILE C 176 1 ? 7  
HELX_P HELX_P40 40 ASP C 206 ? ASP C 208 ? ASP C 184 ASP C 186 5 ? 3  
HELX_P HELX_P41 41 GLY C 209 ? ALA C 223 ? GLY C 187 ALA C 201 1 ? 15 
HELX_P HELX_P42 42 ASP C 225 ? GLN C 243 ? ASP C 203 GLN C 221 1 ? 19 
HELX_P HELX_P43 43 GLY C 244 ? GLY C 263 ? GLY C 222 GLY C 241 1 ? 20 
HELX_P HELX_P44 44 SER C 264 ? GLY C 278 ? SER C 242 GLY C 256 1 ? 15 
HELX_P HELX_P45 45 GLY C 278 ? ARG C 289 ? GLY C 256 ARG C 267 1 ? 12 
# 
_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 
covale1  covale both ? A GLU 53  C ? ? ? 1_555 A MSE 54  N ? ? A GLU 31  A MSE 32  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale2  covale both ? A MSE 54  C ? ? ? 1_555 A LEU 55  N ? ? A MSE 32  A LEU 33  1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale3  covale both ? A ALA 61  C ? ? ? 1_555 A MSE 62  N ? ? A ALA 39  A MSE 40  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale4  covale both ? A MSE 62  C ? ? ? 1_555 A ASP 63  N ? ? A MSE 40  A ASP 41  1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale5  covale both ? A GLN 92  C ? ? ? 1_555 A MSE 93  N ? ? A GLN 70  A MSE 71  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale6  covale both ? A MSE 93  C ? ? ? 1_555 A GLU 94  N ? ? A MSE 71  A GLU 72  1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale7  covale both ? A VAL 114 C ? ? ? 1_555 A MSE 115 N ? ? A VAL 92  A MSE 93  1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale8  covale both ? A MSE 115 C ? ? ? 1_555 A ARG 116 N ? ? A MSE 93  A ARG 94  1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale9  covale both ? A ASP 144 C ? ? ? 1_555 A MSE 145 N ? ? A ASP 122 A MSE 123 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale10 covale both ? A MSE 145 C ? ? ? 1_555 A THR 146 N ? ? A MSE 123 A THR 124 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale11 covale both ? A VAL 167 C ? ? ? 1_555 A MSE 168 N ? ? A VAL 145 A MSE 146 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale12 covale both ? A MSE 168 C ? ? ? 1_555 A LEU 169 N ? ? A MSE 146 A LEU 147 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale13 covale both ? A GLY 199 C ? ? ? 1_555 A MSE 200 N ? ? A GLY 177 A MSE 178 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale14 covale both ? A MSE 200 C ? ? ? 1_555 A VAL 201 N ? ? A MSE 178 A VAL 179 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale15 covale both ? A GLY 244 C ? ? ? 1_555 A MSE 245 N ? ? A GLY 222 A MSE 223 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale16 covale both ? A MSE 245 C ? ? ? 1_555 A LEU 246 N ? ? A MSE 223 A LEU 224 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale17 covale both ? B GLU 53  C ? ? ? 1_555 B MSE 54  N ? ? B GLU 31  B MSE 32  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale18 covale both ? B MSE 54  C ? ? ? 1_555 B LEU 55  N ? ? B MSE 32  B LEU 33  1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale19 covale both ? B ALA 61  C ? ? ? 1_555 B MSE 62  N ? ? B ALA 39  B MSE 40  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale20 covale both ? B MSE 62  C ? ? ? 1_555 B ASP 63  N ? ? B MSE 40  B ASP 41  1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale21 covale both ? B GLN 92  C ? ? ? 1_555 B MSE 93  N ? ? B GLN 70  B MSE 71  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale22 covale both ? B MSE 93  C ? ? ? 1_555 B GLU 94  N ? ? B MSE 71  B GLU 72  1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale23 covale both ? B VAL 114 C ? ? ? 1_555 B MSE 115 N ? ? B VAL 92  B MSE 93  1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale24 covale both ? B MSE 115 C ? ? ? 1_555 B ARG 116 N ? ? B MSE 93  B ARG 94  1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale25 covale both ? B ASP 144 C ? ? ? 1_555 B MSE 145 N ? ? B ASP 122 B MSE 123 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale26 covale both ? B MSE 145 C ? ? ? 1_555 B THR 146 N ? ? B MSE 123 B THR 124 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale27 covale both ? B VAL 167 C ? ? ? 1_555 B MSE 168 N ? ? B VAL 145 B MSE 146 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale28 covale both ? B MSE 168 C ? ? ? 1_555 B LEU 169 N ? ? B MSE 146 B LEU 147 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale29 covale both ? B GLY 199 C ? ? ? 1_555 B MSE 200 N ? ? B GLY 177 B MSE 178 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale30 covale both ? B MSE 200 C ? ? ? 1_555 B VAL 201 N ? ? B MSE 178 B VAL 179 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale31 covale both ? B GLY 244 C ? ? ? 1_555 B MSE 245 N ? ? B GLY 222 B MSE 223 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale32 covale both ? B MSE 245 C ? ? ? 1_555 B LEU 246 N ? ? B MSE 223 B LEU 224 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale33 covale both ? C GLU 53  C ? ? ? 1_555 C MSE 54  N ? ? C GLU 31  C MSE 32  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale34 covale both ? C MSE 54  C ? ? ? 1_555 C LEU 55  N ? ? C MSE 32  C LEU 33  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale35 covale both ? C ALA 61  C ? ? ? 1_555 C MSE 62  N ? ? C ALA 39  C MSE 40  1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale36 covale both ? C MSE 62  C ? ? ? 1_555 C ASP 63  N ? ? C MSE 40  C ASP 41  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale37 covale both ? C GLN 92  C ? ? ? 1_555 C MSE 93  N ? ? C GLN 70  C MSE 71  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale38 covale both ? C MSE 93  C ? ? ? 1_555 C GLU 94  N ? ? C MSE 71  C GLU 72  1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale39 covale both ? C VAL 114 C ? ? ? 1_555 C MSE 115 N ? ? C VAL 92  C MSE 93  1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale40 covale both ? C MSE 115 C ? ? ? 1_555 C ARG 116 N ? ? C MSE 93  C ARG 94  1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale41 covale both ? C ASP 144 C ? ? ? 1_555 C MSE 145 N ? ? C ASP 122 C MSE 123 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale42 covale both ? C MSE 145 C ? ? ? 1_555 C THR 146 N ? ? C MSE 123 C THR 124 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale43 covale both ? C VAL 167 C ? ? ? 1_555 C MSE 168 N ? ? C VAL 145 C MSE 146 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale44 covale both ? C MSE 168 C ? ? ? 1_555 C LEU 169 N ? ? C MSE 146 C LEU 147 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale45 covale both ? C GLY 199 C ? ? ? 1_555 C MSE 200 N ? ? C GLY 177 C MSE 178 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale46 covale both ? C MSE 200 C ? ? ? 1_555 C VAL 201 N ? ? C MSE 178 C VAL 179 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale47 covale both ? C GLY 244 C ? ? ? 1_555 C MSE 245 N ? ? C GLY 222 C MSE 223 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale48 covale both ? C MSE 245 C ? ? ? 1_555 C LEU 246 N ? ? C MSE 223 C LEU 224 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  MSE A 54  ? . . . . MSE A 32  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
2  MSE A 62  ? . . . . MSE A 40  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
3  MSE A 93  ? . . . . MSE A 71  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
4  MSE A 115 ? . . . . MSE A 93  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
5  MSE A 145 ? . . . . MSE A 123 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
6  MSE A 168 ? . . . . MSE A 146 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
7  MSE A 200 ? . . . . MSE A 178 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
8  MSE A 245 ? . . . . MSE A 223 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
9  MSE B 54  ? . . . . MSE B 32  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
10 MSE B 62  ? . . . . MSE B 40  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
11 MSE B 93  ? . . . . MSE B 71  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
12 MSE B 115 ? . . . . MSE B 93  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
13 MSE B 145 ? . . . . MSE B 123 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
14 MSE B 168 ? . . . . MSE B 146 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
15 MSE B 200 ? . . . . MSE B 178 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
16 MSE B 245 ? . . . . MSE B 223 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
17 MSE C 54  ? . . . . MSE C 32  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
18 MSE C 62  ? . . . . MSE C 40  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
19 MSE C 93  ? . . . . MSE C 71  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
20 MSE C 115 ? . . . . MSE C 93  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
21 MSE C 145 ? . . . . MSE C 123 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
22 MSE C 168 ? . . . . MSE C 146 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
23 MSE C 200 ? . . . . MSE C 178 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
24 MSE C 245 ? . . . . MSE C 223 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 6 ? 
B ? 3 ? 
C ? 6 ? 
D ? 3 ? 
E ? 6 ? 
F ? 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 
A 1 2 ? anti-parallel 
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
A 5 6 ? parallel      
B 1 2 ? parallel      
B 2 3 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
D 1 2 ? parallel      
D 2 3 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? parallel      
E 3 4 ? parallel      
E 4 5 ? parallel      
E 5 6 ? parallel      
F 1 2 ? parallel      
F 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 
A 1 ILE A 28  ? LEU A 33  ? ILE A 6   LEU A 11  
A 2 VAL A 36  ? LEU A 41  ? VAL A 14  LEU A 19  
A 3 ALA A 73  ? GLY A 78  ? ALA A 51  GLY A 56  
A 4 THR A 124 ? VAL A 128 ? THR A 102 VAL A 106 
A 5 MSE A 145 ? THR A 149 ? MSE A 123 THR A 127 
A 6 ARG A 203 ? VAL A 205 ? ARG A 181 VAL A 183 
B 1 PRO A 131 ? LEU A 133 ? PRO A 109 LEU A 111 
B 2 PHE A 153 ? GLY A 155 ? PHE A 131 GLY A 133 
B 3 VAL A 190 ? PRO A 191 ? VAL A 168 PRO A 169 
C 1 ILE B 28  ? LEU B 33  ? ILE B 6   LEU B 11  
C 2 VAL B 36  ? LEU B 41  ? VAL B 14  LEU B 19  
C 3 ALA B 73  ? GLY B 78  ? ALA B 51  GLY B 56  
C 4 THR B 124 ? VAL B 128 ? THR B 102 VAL B 106 
C 5 MSE B 145 ? THR B 149 ? MSE B 123 THR B 127 
C 6 ARG B 203 ? VAL B 205 ? ARG B 181 VAL B 183 
D 1 PRO B 131 ? LEU B 133 ? PRO B 109 LEU B 111 
D 2 PHE B 153 ? GLY B 155 ? PHE B 131 GLY B 133 
D 3 VAL B 190 ? PRO B 191 ? VAL B 168 PRO B 169 
E 1 ILE C 28  ? LEU C 33  ? ILE C 6   LEU C 11  
E 2 VAL C 36  ? LEU C 41  ? VAL C 14  LEU C 19  
E 3 VAL C 74  ? GLY C 78  ? VAL C 52  GLY C 56  
E 4 THR C 124 ? VAL C 128 ? THR C 102 VAL C 106 
E 5 MSE C 145 ? THR C 149 ? MSE C 123 THR C 127 
E 6 ARG C 203 ? VAL C 205 ? ARG C 181 VAL C 183 
F 1 PRO C 131 ? LEU C 133 ? PRO C 109 LEU C 111 
F 2 PHE C 153 ? GLY C 155 ? PHE C 131 GLY C 133 
F 3 VAL C 190 ? PRO C 191 ? VAL C 168 PRO C 169 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N GLU A 31  ? N GLU A 9   O ARG A 38  ? O ARG A 16  
A 2 3 N ILE A 39  ? N ILE A 17  O ILE A 75  ? O ILE A 53  
A 3 4 N VAL A 76  ? N VAL A 54  O ALA A 127 ? O ALA A 105 
A 4 5 N ALA A 126 ? N ALA A 104 O ILE A 147 ? O ILE A 125 
A 5 6 N ALA A 148 ? N ALA A 126 O VAL A 205 ? O VAL A 183 
B 1 2 N CYS A 132 ? N CYS A 110 O PHE A 153 ? O PHE A 131 
B 2 3 N PHE A 154 ? N PHE A 132 O VAL A 190 ? O VAL A 168 
C 1 2 N GLU B 31  ? N GLU B 9   O ARG B 38  ? O ARG B 16  
C 2 3 N ILE B 39  ? N ILE B 17  O ILE B 75  ? O ILE B 53  
C 3 4 N VAL B 76  ? N VAL B 54  O ALA B 127 ? O ALA B 105 
C 4 5 N ALA B 126 ? N ALA B 104 O ILE B 147 ? O ILE B 125 
C 5 6 N ALA B 148 ? N ALA B 126 O VAL B 205 ? O VAL B 183 
D 1 2 N CYS B 132 ? N CYS B 110 O PHE B 153 ? O PHE B 131 
D 2 3 N PHE B 154 ? N PHE B 132 O VAL B 190 ? O VAL B 168 
E 1 2 N GLU C 31  ? N GLU C 9   O ARG C 38  ? O ARG C 16  
E 2 3 N ILE C 39  ? N ILE C 17  O ILE C 75  ? O ILE C 53  
E 3 4 N VAL C 76  ? N VAL C 54  O ALA C 127 ? O ALA C 105 
E 4 5 N ALA C 126 ? N ALA C 104 O ILE C 147 ? O ILE C 125 
E 5 6 N ALA C 148 ? N ALA C 126 O VAL C 205 ? O VAL C 183 
F 1 2 N CYS C 132 ? N CYS C 110 O PHE C 153 ? O PHE C 131 
F 2 3 N PHE C 154 ? N PHE C 132 O VAL C 190 ? O VAL C 168 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A TLA 301 ? 6  'BINDING SITE FOR RESIDUE TLA A 301' 
AC2 Software A GOL 302 ? 5  'BINDING SITE FOR RESIDUE GOL A 302' 
AC3 Software C TLA 601 ? 14 'BINDING SITE FOR RESIDUE TLA C 601' 
AC4 Software C TLA 602 ? 7  'BINDING SITE FOR RESIDUE TLA C 602' 
AC5 Software C GOL 603 ? 7  'BINDING SITE FOR RESIDUE GOL C 603' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 6  LYS A 90  ? LYS A 68  . ? 1_555 ? 
2  AC1 6  GLY A 278 ? GLY A 256 . ? 1_555 ? 
3  AC1 6  LEU A 279 ? LEU A 257 . ? 1_555 ? 
4  AC1 6  ARG A 280 ? ARG A 258 . ? 1_555 ? 
5  AC1 6  HOH I .   ? HOH A 507 . ? 1_555 ? 
6  AC1 6  HOH I .   ? HOH A 523 . ? 1_555 ? 
7  AC2 5  ARG A 203 ? ARG A 181 . ? 1_555 ? 
8  AC2 5  ARG A 216 ? ARG A 194 . ? 1_555 ? 
9  AC2 5  HIS A 220 ? HIS A 198 . ? 1_555 ? 
10 AC2 5  GLU C 187 ? GLU C 165 . ? 1_555 ? 
11 AC2 5  PRO C 291 ? PRO C 269 . ? 1_555 ? 
12 AC3 14 GLY C 99  ? GLY C 77  . ? 1_555 ? 
13 AC3 14 GLY C 99  ? GLY C 77  . ? 3_555 ? 
14 AC3 14 VAL C 100 ? VAL C 78  . ? 1_555 ? 
15 AC3 14 VAL C 100 ? VAL C 78  . ? 3_555 ? 
16 AC3 14 GLY C 261 ? GLY C 239 . ? 3_555 ? 
17 AC3 14 GLY C 261 ? GLY C 239 . ? 1_555 ? 
18 AC3 14 ALA C 262 ? ALA C 240 . ? 1_555 ? 
19 AC3 14 ALA C 262 ? ALA C 240 . ? 3_555 ? 
20 AC3 14 HOH K .   ? HOH C 720 . ? 1_555 ? 
21 AC3 14 HOH K .   ? HOH C 720 . ? 3_555 ? 
22 AC3 14 HOH K .   ? HOH C 727 . ? 3_555 ? 
23 AC3 14 HOH K .   ? HOH C 727 . ? 1_555 ? 
24 AC3 14 HOH K .   ? HOH C 873 . ? 1_555 ? 
25 AC3 14 HOH K .   ? HOH C 873 . ? 3_555 ? 
26 AC4 7  GLY A 80  ? GLY A 58  . ? 6_555 ? 
27 AC4 7  ASN A 81  ? ASN A 59  . ? 6_555 ? 
28 AC4 7  HIS C 34  ? HIS C 12  . ? 1_555 ? 
29 AC4 7  ARG C 219 ? ARG C 197 . ? 1_555 ? 
30 AC4 7  HOH K .   ? HOH C 802 . ? 1_555 ? 
31 AC4 7  HOH K .   ? HOH C 825 . ? 1_555 ? 
32 AC4 7  HOH K .   ? HOH C 871 . ? 1_555 ? 
33 AC5 7  GLN C 52  ? GLN C 30  . ? 1_555 ? 
34 AC5 7  PHE C 87  ? PHE C 65  . ? 1_555 ? 
35 AC5 7  GLN C 92  ? GLN C 70  . ? 1_555 ? 
36 AC5 7  TRP C 103 ? TRP C 81  . ? 1_555 ? 
37 AC5 7  ASP C 110 ? ASP C 88  . ? 1_555 ? 
38 AC5 7  HOH K .   ? HOH C 714 . ? 1_555 ? 
39 AC5 7  HOH K .   ? HOH C 822 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   4K29 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 61  ? ? -80.51  -74.98  
2  1 SER A 62  ? ? -172.65 145.51  
3  1 ALA A 112 ? ? 58.37   -128.31 
4  1 ASN B 59  ? ? 72.16   30.18   
5  1 PHE B 61  ? ? -84.09  -75.18  
6  1 SER B 62  ? ? -170.07 146.56  
7  1 ALA B 112 ? ? 58.76   -126.83 
8  1 PHE C 61  ? ? -80.59  -74.19  
9  1 SER C 62  ? ? -172.56 146.94  
10 1 ALA C 112 ? ? 55.37   -125.23 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          PSI:Biology 
_pdbx_SG_project.full_name_of_center   'New York Structural Genomics Research Consortium' 
_pdbx_SG_project.initial_of_center     NYSGRC 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A MSE 54  A MSE 32  ? MET SELENOMETHIONINE 
2  A MSE 62  A MSE 40  ? MET SELENOMETHIONINE 
3  A MSE 93  A MSE 71  ? MET SELENOMETHIONINE 
4  A MSE 115 A MSE 93  ? MET SELENOMETHIONINE 
5  A MSE 145 A MSE 123 ? MET SELENOMETHIONINE 
6  A MSE 168 A MSE 146 ? MET SELENOMETHIONINE 
7  A MSE 200 A MSE 178 ? MET SELENOMETHIONINE 
8  A MSE 245 A MSE 223 ? MET SELENOMETHIONINE 
9  B MSE 54  B MSE 32  ? MET SELENOMETHIONINE 
10 B MSE 62  B MSE 40  ? MET SELENOMETHIONINE 
11 B MSE 93  B MSE 71  ? MET SELENOMETHIONINE 
12 B MSE 115 B MSE 93  ? MET SELENOMETHIONINE 
13 B MSE 145 B MSE 123 ? MET SELENOMETHIONINE 
14 B MSE 168 B MSE 146 ? MET SELENOMETHIONINE 
15 B MSE 200 B MSE 178 ? MET SELENOMETHIONINE 
16 B MSE 245 B MSE 223 ? MET SELENOMETHIONINE 
17 C MSE 54  C MSE 32  ? MET SELENOMETHIONINE 
18 C MSE 62  C MSE 40  ? MET SELENOMETHIONINE 
19 C MSE 93  C MSE 71  ? MET SELENOMETHIONINE 
20 C MSE 115 C MSE 93  ? MET SELENOMETHIONINE 
21 C MSE 145 C MSE 123 ? MET SELENOMETHIONINE 
22 C MSE 168 C MSE 146 ? MET SELENOMETHIONINE 
23 C MSE 200 C MSE 178 ? MET SELENOMETHIONINE 
24 C MSE 245 C MSE 223 ? MET SELENOMETHIONINE 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 465 ? I HOH . 
2 1 B HOH 360 ? J HOH . 
3 1 B HOH 430 ? J HOH . 
# 
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 MSE -21 ? A MSE 1   
2  1 Y 1 A HIS -20 ? A HIS 2   
3  1 Y 1 A HIS -19 ? A HIS 3   
4  1 Y 1 A HIS -18 ? A HIS 4   
5  1 Y 1 A HIS -17 ? A HIS 5   
6  1 Y 1 A HIS -16 ? A HIS 6   
7  1 Y 1 A HIS -15 ? A HIS 7   
8  1 Y 1 A SER -14 ? A SER 8   
9  1 Y 1 A SER -13 ? A SER 9   
10 1 Y 1 A GLY -12 ? A GLY 10  
11 1 Y 1 A VAL -11 ? A VAL 11  
12 1 Y 1 A ASP -10 ? A ASP 12  
13 1 Y 1 A LEU -9  ? A LEU 13  
14 1 Y 1 A GLY -8  ? A GLY 14  
15 1 Y 1 A THR -7  ? A THR 15  
16 1 Y 1 A GLU -6  ? A GLU 16  
17 1 Y 1 A ASN -5  ? A ASN 17  
18 1 Y 1 A LEU -4  ? A LEU 18  
19 1 Y 1 A TYR -3  ? A TYR 19  
20 1 Y 1 A PHE -2  ? A PHE 20  
21 1 Y 1 A GLN -1  ? A GLN 21  
22 1 Y 1 A SER 0   ? A SER 22  
23 1 Y 1 A MSE 1   ? A MSE 23  
24 1 Y 1 A ARG 271 ? A ARG 293 
25 1 Y 1 A ASP 272 ? A ASP 294 
26 1 Y 1 A ALA 273 ? A ALA 295 
27 1 Y 1 B MSE -21 ? B MSE 1   
28 1 Y 1 B HIS -20 ? B HIS 2   
29 1 Y 1 B HIS -19 ? B HIS 3   
30 1 Y 1 B HIS -18 ? B HIS 4   
31 1 Y 1 B HIS -17 ? B HIS 5   
32 1 Y 1 B HIS -16 ? B HIS 6   
33 1 Y 1 B HIS -15 ? B HIS 7   
34 1 Y 1 B SER -14 ? B SER 8   
35 1 Y 1 B SER -13 ? B SER 9   
36 1 Y 1 B GLY -12 ? B GLY 10  
37 1 Y 1 B VAL -11 ? B VAL 11  
38 1 Y 1 B ASP -10 ? B ASP 12  
39 1 Y 1 B LEU -9  ? B LEU 13  
40 1 Y 1 B GLY -8  ? B GLY 14  
41 1 Y 1 B THR -7  ? B THR 15  
42 1 Y 1 B GLU -6  ? B GLU 16  
43 1 Y 1 B ASN -5  ? B ASN 17  
44 1 Y 1 B LEU -4  ? B LEU 18  
45 1 Y 1 B TYR -3  ? B TYR 19  
46 1 Y 1 B PHE -2  ? B PHE 20  
47 1 Y 1 B GLN -1  ? B GLN 21  
48 1 Y 1 B SER 0   ? B SER 22  
49 1 Y 1 B MSE 1   ? B MSE 23  
50 1 Y 1 B THR 2   ? B THR 24  
51 1 Y 1 B ARG 271 ? B ARG 293 
52 1 Y 1 B ASP 272 ? B ASP 294 
53 1 Y 1 B ALA 273 ? B ALA 295 
54 1 Y 1 C MSE -21 ? C MSE 1   
55 1 Y 1 C HIS -20 ? C HIS 2   
56 1 Y 1 C HIS -19 ? C HIS 3   
57 1 Y 1 C HIS -18 ? C HIS 4   
58 1 Y 1 C HIS -17 ? C HIS 5   
59 1 Y 1 C HIS -16 ? C HIS 6   
60 1 Y 1 C HIS -15 ? C HIS 7   
61 1 Y 1 C SER -14 ? C SER 8   
62 1 Y 1 C SER -13 ? C SER 9   
63 1 Y 1 C GLY -12 ? C GLY 10  
64 1 Y 1 C VAL -11 ? C VAL 11  
65 1 Y 1 C ASP -10 ? C ASP 12  
66 1 Y 1 C LEU -9  ? C LEU 13  
67 1 Y 1 C GLY -8  ? C GLY 14  
68 1 Y 1 C THR -7  ? C THR 15  
69 1 Y 1 C GLU -6  ? C GLU 16  
70 1 Y 1 C ASN -5  ? C ASN 17  
71 1 Y 1 C LEU -4  ? C LEU 18  
72 1 Y 1 C TYR -3  ? C TYR 19  
73 1 Y 1 C PHE -2  ? C PHE 20  
74 1 Y 1 C GLN -1  ? C GLN 21  
75 1 Y 1 C SER 0   ? C SER 22  
76 1 Y 1 C MSE 1   ? C MSE 23  
77 1 Y 1 C THR 2   ? C THR 24  
78 1 Y 1 C ARG 271 ? C ARG 293 
79 1 Y 1 C ASP 272 ? C ASP 294 
80 1 Y 1 C ALA 273 ? C ALA 295 
# 
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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
GOL C1   C  N N 137 
GOL O1   O  N N 138 
GOL C2   C  N N 139 
GOL O2   O  N N 140 
GOL C3   C  N N 141 
GOL O3   O  N N 142 
GOL H11  H  N N 143 
GOL H12  H  N N 144 
GOL HO1  H  N N 145 
GOL H2   H  N N 146 
GOL HO2  H  N N 147 
GOL H31  H  N N 148 
GOL H32  H  N N 149 
GOL HO3  H  N N 150 
HIS N    N  N N 151 
HIS CA   C  N S 152 
HIS C    C  N N 153 
HIS O    O  N N 154 
HIS CB   C  N N 155 
HIS CG   C  Y N 156 
HIS ND1  N  Y N 157 
HIS CD2  C  Y N 158 
HIS CE1  C  Y N 159 
HIS NE2  N  Y N 160 
HIS OXT  O  N N 161 
HIS H    H  N N 162 
HIS H2   H  N N 163 
HIS HA   H  N N 164 
HIS HB2  H  N N 165 
HIS HB3  H  N N 166 
HIS HD1  H  N N 167 
HIS HD2  H  N N 168 
HIS HE1  H  N N 169 
HIS HE2  H  N N 170 
HIS HXT  H  N N 171 
HOH O    O  N N 172 
HOH H1   H  N N 173 
HOH H2   H  N N 174 
ILE N    N  N N 175 
ILE CA   C  N S 176 
ILE C    C  N N 177 
ILE O    O  N N 178 
ILE CB   C  N S 179 
ILE CG1  C  N N 180 
ILE CG2  C  N N 181 
ILE CD1  C  N N 182 
ILE OXT  O  N N 183 
ILE H    H  N N 184 
ILE H2   H  N N 185 
ILE HA   H  N N 186 
ILE HB   H  N N 187 
ILE HG12 H  N N 188 
ILE HG13 H  N N 189 
ILE HG21 H  N N 190 
ILE HG22 H  N N 191 
ILE HG23 H  N N 192 
ILE HD11 H  N N 193 
ILE HD12 H  N N 194 
ILE HD13 H  N N 195 
ILE HXT  H  N N 196 
LEU N    N  N N 197 
LEU CA   C  N S 198 
LEU C    C  N N 199 
LEU O    O  N N 200 
LEU CB   C  N N 201 
LEU CG   C  N N 202 
LEU CD1  C  N N 203 
LEU CD2  C  N N 204 
LEU OXT  O  N N 205 
LEU H    H  N N 206 
LEU H2   H  N N 207 
LEU HA   H  N N 208 
LEU HB2  H  N N 209 
LEU HB3  H  N N 210 
LEU HG   H  N N 211 
LEU HD11 H  N N 212 
LEU HD12 H  N N 213 
LEU HD13 H  N N 214 
LEU HD21 H  N N 215 
LEU HD22 H  N N 216 
LEU HD23 H  N N 217 
LEU HXT  H  N N 218 
LYS N    N  N N 219 
LYS CA   C  N S 220 
LYS C    C  N N 221 
LYS O    O  N N 222 
LYS CB   C  N N 223 
LYS CG   C  N N 224 
LYS CD   C  N N 225 
LYS CE   C  N N 226 
LYS NZ   N  N N 227 
LYS OXT  O  N N 228 
LYS H    H  N N 229 
LYS H2   H  N N 230 
LYS HA   H  N N 231 
LYS HB2  H  N N 232 
LYS HB3  H  N N 233 
LYS HG2  H  N N 234 
LYS HG3  H  N N 235 
LYS HD2  H  N N 236 
LYS HD3  H  N N 237 
LYS HE2  H  N N 238 
LYS HE3  H  N N 239 
LYS HZ1  H  N N 240 
LYS HZ2  H  N N 241 
LYS HZ3  H  N N 242 
LYS HXT  H  N N 243 
MSE N    N  N N 244 
MSE CA   C  N S 245 
MSE C    C  N N 246 
MSE O    O  N N 247 
MSE OXT  O  N N 248 
MSE CB   C  N N 249 
MSE CG   C  N N 250 
MSE SE   SE N N 251 
MSE CE   C  N N 252 
MSE H    H  N N 253 
MSE H2   H  N N 254 
MSE HA   H  N N 255 
MSE HXT  H  N N 256 
MSE HB2  H  N N 257 
MSE HB3  H  N N 258 
MSE HG2  H  N N 259 
MSE HG3  H  N N 260 
MSE HE1  H  N N 261 
MSE HE2  H  N N 262 
MSE HE3  H  N N 263 
PHE N    N  N N 264 
PHE CA   C  N S 265 
PHE C    C  N N 266 
PHE O    O  N N 267 
PHE CB   C  N N 268 
PHE CG   C  Y N 269 
PHE CD1  C  Y N 270 
PHE CD2  C  Y N 271 
PHE CE1  C  Y N 272 
PHE CE2  C  Y N 273 
PHE CZ   C  Y N 274 
PHE OXT  O  N N 275 
PHE H    H  N N 276 
PHE H2   H  N N 277 
PHE HA   H  N N 278 
PHE HB2  H  N N 279 
PHE HB3  H  N N 280 
PHE HD1  H  N N 281 
PHE HD2  H  N N 282 
PHE HE1  H  N N 283 
PHE HE2  H  N N 284 
PHE HZ   H  N N 285 
PHE HXT  H  N N 286 
PRO N    N  N N 287 
PRO CA   C  N S 288 
PRO C    C  N N 289 
PRO O    O  N N 290 
PRO CB   C  N N 291 
PRO CG   C  N N 292 
PRO CD   C  N N 293 
PRO OXT  O  N N 294 
PRO H    H  N N 295 
PRO HA   H  N N 296 
PRO HB2  H  N N 297 
PRO HB3  H  N N 298 
PRO HG2  H  N N 299 
PRO HG3  H  N N 300 
PRO HD2  H  N N 301 
PRO HD3  H  N N 302 
PRO HXT  H  N N 303 
SER N    N  N N 304 
SER CA   C  N S 305 
SER C    C  N N 306 
SER O    O  N N 307 
SER CB   C  N N 308 
SER OG   O  N N 309 
SER OXT  O  N N 310 
SER H    H  N N 311 
SER H2   H  N N 312 
SER HA   H  N N 313 
SER HB2  H  N N 314 
SER HB3  H  N N 315 
SER HG   H  N N 316 
SER HXT  H  N N 317 
THR N    N  N N 318 
THR CA   C  N S 319 
THR C    C  N N 320 
THR O    O  N N 321 
THR CB   C  N R 322 
THR OG1  O  N N 323 
THR CG2  C  N N 324 
THR OXT  O  N N 325 
THR H    H  N N 326 
THR H2   H  N N 327 
THR HA   H  N N 328 
THR HB   H  N N 329 
THR HG1  H  N N 330 
THR HG21 H  N N 331 
THR HG22 H  N N 332 
THR HG23 H  N N 333 
THR HXT  H  N N 334 
TLA O1   O  N N 335 
TLA O11  O  N N 336 
TLA C1   C  N N 337 
TLA C2   C  N R 338 
TLA O2   O  N N 339 
TLA C3   C  N R 340 
TLA O3   O  N N 341 
TLA C4   C  N N 342 
TLA O4   O  N N 343 
TLA O41  O  N N 344 
TLA H11  H  N N 345 
TLA H2   H  N N 346 
TLA HA   H  N N 347 
TLA H3   H  N N 348 
TLA HB   H  N N 349 
TLA H41  H  N N 350 
TRP N    N  N N 351 
TRP CA   C  N S 352 
TRP C    C  N N 353 
TRP O    O  N N 354 
TRP CB   C  N N 355 
TRP CG   C  Y N 356 
TRP CD1  C  Y N 357 
TRP CD2  C  Y N 358 
TRP NE1  N  Y N 359 
TRP CE2  C  Y N 360 
TRP CE3  C  Y N 361 
TRP CZ2  C  Y N 362 
TRP CZ3  C  Y N 363 
TRP CH2  C  Y N 364 
TRP OXT  O  N N 365 
TRP H    H  N N 366 
TRP H2   H  N N 367 
TRP HA   H  N N 368 
TRP HB2  H  N N 369 
TRP HB3  H  N N 370 
TRP HD1  H  N N 371 
TRP HE1  H  N N 372 
TRP HE3  H  N N 373 
TRP HZ2  H  N N 374 
TRP HZ3  H  N N 375 
TRP HH2  H  N N 376 
TRP HXT  H  N N 377 
TYR N    N  N N 378 
TYR CA   C  N S 379 
TYR C    C  N N 380 
TYR O    O  N N 381 
TYR CB   C  N N 382 
TYR CG   C  Y N 383 
TYR CD1  C  Y N 384 
TYR CD2  C  Y N 385 
TYR CE1  C  Y N 386 
TYR CE2  C  Y N 387 
TYR CZ   C  Y N 388 
TYR OH   O  N N 389 
TYR OXT  O  N N 390 
TYR H    H  N N 391 
TYR H2   H  N N 392 
TYR HA   H  N N 393 
TYR HB2  H  N N 394 
TYR HB3  H  N N 395 
TYR HD1  H  N N 396 
TYR HD2  H  N N 397 
TYR HE1  H  N N 398 
TYR HE2  H  N N 399 
TYR HH   H  N N 400 
TYR HXT  H  N N 401 
VAL N    N  N N 402 
VAL CA   C  N S 403 
VAL C    C  N N 404 
VAL O    O  N N 405 
VAL CB   C  N N 406 
VAL CG1  C  N N 407 
VAL CG2  C  N N 408 
VAL OXT  O  N N 409 
VAL H    H  N N 410 
VAL H2   H  N N 411 
VAL HA   H  N N 412 
VAL HB   H  N N 413 
VAL HG11 H  N N 414 
VAL HG12 H  N N 415 
VAL HG13 H  N N 416 
VAL HG21 H  N N 417 
VAL HG22 H  N N 418 
VAL HG23 H  N N 419 
VAL HXT  H  N N 420 
# 
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 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MSE N   CA   sing N N 231 
MSE N   H    sing N N 232 
MSE N   H2   sing N N 233 
MSE CA  C    sing N N 234 
MSE CA  CB   sing N N 235 
MSE CA  HA   sing N N 236 
MSE C   O    doub N N 237 
MSE C   OXT  sing N N 238 
MSE OXT HXT  sing N N 239 
MSE CB  CG   sing N N 240 
MSE CB  HB2  sing N N 241 
MSE CB  HB3  sing N N 242 
MSE CG  SE   sing N N 243 
MSE CG  HG2  sing N N 244 
MSE CG  HG3  sing N N 245 
MSE SE  CE   sing N N 246 
MSE CE  HE1  sing N N 247 
MSE CE  HE2  sing N N 248 
MSE CE  HE3  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TLA O1  C1   doub N N 319 
TLA O11 C1   sing N N 320 
TLA O11 H11  sing N N 321 
TLA C1  C2   sing N N 322 
TLA C2  O2   sing N N 323 
TLA C2  C3   sing N N 324 
TLA C2  H2   sing N N 325 
TLA O2  HA   sing N N 326 
TLA C3  O3   sing N N 327 
TLA C3  C4   sing N N 328 
TLA C3  H3   sing N N 329 
TLA O3  HB   sing N N 330 
TLA C4  O4   doub N N 331 
TLA C4  O41  sing N N 332 
TLA O41 H41  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
# 
_atom_sites.entry_id                    4K29 
_atom_sites.fract_transf_matrix[1][1]   0.008692 
_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]   0.006917 
_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]   0.007718 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
SE 
# 
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   . THR A 1 24  ? 12.952 23.678 -6.307  1.00 26.18 ? 2   THR A N   1 
ATOM   2    C  CA  . THR A 1 24  ? 11.653 24.333 -6.648  1.00 25.75 ? 2   THR A CA  1 
ATOM   3    C  C   . THR A 1 24  ? 11.589 25.819 -6.263  1.00 23.90 ? 2   THR A C   1 
ATOM   4    O  O   . THR A 1 24  ? 10.747 26.550 -6.783  1.00 24.90 ? 2   THR A O   1 
ATOM   5    C  CB  . THR A 1 24  ? 10.459 23.608 -5.985  1.00 27.04 ? 2   THR A CB  1 
ATOM   6    O  OG1 . THR A 1 24  ? 10.582 23.663 -4.556  1.00 28.10 ? 2   THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 24  ? 10.388 22.150 -6.433  1.00 27.53 ? 2   THR A CG2 1 
ATOM   8    N  N   . TYR A 1 25  ? 12.463 26.265 -5.361  1.00 21.11 ? 3   TYR A N   1 
ATOM   9    C  CA  . TYR A 1 25  ? 12.467 27.663 -4.924  1.00 18.97 ? 3   TYR A CA  1 
ATOM   10   C  C   . TYR A 1 25  ? 13.391 28.538 -5.767  1.00 18.44 ? 3   TYR A C   1 
ATOM   11   O  O   . TYR A 1 25  ? 14.431 28.090 -6.250  1.00 18.34 ? 3   TYR A O   1 
ATOM   12   C  CB  . TYR A 1 25  ? 12.876 27.768 -3.455  1.00 18.01 ? 3   TYR A CB  1 
ATOM   13   C  CG  . TYR A 1 25  ? 11.975 27.002 -2.519  1.00 16.87 ? 3   TYR A CG  1 
ATOM   14   C  CD1 . TYR A 1 25  ? 10.666 27.408 -2.299  1.00 16.58 ? 3   TYR A CD1 1 
ATOM   15   C  CD2 . TYR A 1 25  ? 12.436 25.876 -1.841  1.00 16.47 ? 3   TYR A CD2 1 
ATOM   16   C  CE1 . TYR A 1 25  ? 9.835  26.711 -1.441  1.00 16.23 ? 3   TYR A CE1 1 
ATOM   17   C  CE2 . TYR A 1 25  ? 11.614 25.174 -0.979  1.00 16.16 ? 3   TYR A CE2 1 
ATOM   18   C  CZ  . TYR A 1 25  ? 10.317 25.595 -0.783  1.00 16.15 ? 3   TYR A CZ  1 
ATOM   19   O  OH  . TYR A 1 25  ? 9.499  24.902 0.072   1.00 15.95 ? 3   TYR A OH  1 
ATOM   20   N  N   . SER A 1 26  ? 12.997 29.799 -5.912  1.00 18.10 ? 4   SER A N   1 
ATOM   21   C  CA  . SER A 1 26  ? 13.723 30.780 -6.704  1.00 17.65 ? 4   SER A CA  1 
ATOM   22   C  C   . SER A 1 26  ? 14.657 31.662 -5.871  1.00 16.58 ? 4   SER A C   1 
ATOM   23   O  O   . SER A 1 26  ? 15.720 32.067 -6.344  1.00 16.77 ? 4   SER A O   1 
ATOM   24   C  CB  . SER A 1 26  ? 12.718 31.664 -7.443  1.00 18.54 ? 4   SER A CB  1 
ATOM   25   O  OG  . SER A 1 26  ? 13.351 32.783 -8.020  1.00 19.87 ? 4   SER A OG  1 
ATOM   26   N  N   . LYS A 1 27  ? 14.248 31.976 -4.644  1.00 14.99 ? 5   LYS A N   1 
ATOM   27   C  CA  . LYS A 1 27  ? 14.955 32.966 -3.824  1.00 14.22 ? 5   LYS A CA  1 
ATOM   28   C  C   . LYS A 1 27  ? 15.505 32.399 -2.516  1.00 12.96 ? 5   LYS A C   1 
ATOM   29   O  O   . LYS A 1 27  ? 16.133 33.127 -1.747  1.00 12.31 ? 5   LYS A O   1 
ATOM   30   C  CB  . LYS A 1 27  ? 14.021 34.141 -3.531  1.00 14.81 ? 5   LYS A CB  1 
ATOM   31   C  CG  . LYS A 1 27  ? 13.635 34.948 -4.761  1.00 15.60 ? 5   LYS A CG  1 
ATOM   32   C  CD  . LYS A 1 27  ? 14.711 35.942 -5.156  1.00 16.34 ? 5   LYS A CD  1 
ATOM   33   C  CE  . LYS A 1 27  ? 14.388 36.623 -6.479  1.00 16.84 ? 5   LYS A CE  1 
ATOM   34   N  NZ  . LYS A 1 27  ? 13.070 37.314 -6.481  1.00 17.07 ? 5   LYS A NZ  1 
ATOM   35   N  N   . ILE A 1 28  ? 15.255 31.118 -2.260  1.00 11.88 ? 6   ILE A N   1 
ATOM   36   C  CA  . ILE A 1 28  ? 15.899 30.409 -1.162  1.00 11.53 ? 6   ILE A CA  1 
ATOM   37   C  C   . ILE A 1 28  ? 16.390 29.048 -1.636  1.00 11.31 ? 6   ILE A C   1 
ATOM   38   O  O   . ILE A 1 28  ? 16.024 28.584 -2.714  1.00 11.48 ? 6   ILE A O   1 
ATOM   39   C  CB  . ILE A 1 28  ? 14.950 30.197 0.040   1.00 11.44 ? 6   ILE A CB  1 
ATOM   40   C  CG1 . ILE A 1 28  ? 13.757 29.311 -0.337  1.00 11.48 ? 6   ILE A CG1 1 
ATOM   41   C  CG2 . ILE A 1 28  ? 14.472 31.537 0.575   1.00 11.42 ? 6   ILE A CG2 1 
ATOM   42   C  CD1 . ILE A 1 28  ? 12.950 28.838 0.859   1.00 11.53 ? 6   ILE A CD1 1 
ATOM   43   N  N   . LEU A 1 29  ? 17.222 28.419 -0.819  1.00 10.95 ? 7   LEU A N   1 
ATOM   44   C  CA  . LEU A 1 29  ? 17.527 27.002 -0.968  1.00 11.04 ? 7   LEU A CA  1 
ATOM   45   C  C   . LEU A 1 29  ? 16.979 26.294 0.263   1.00 11.00 ? 7   LEU A C   1 
ATOM   46   O  O   . LEU A 1 29  ? 16.970 26.858 1.363   1.00 10.64 ? 7   LEU A O   1 
ATOM   47   C  CB  . LEU A 1 29  ? 19.032 26.758 -1.094  1.00 11.28 ? 7   LEU A CB  1 
ATOM   48   C  CG  . LEU A 1 29  ? 19.751 27.491 -2.228  1.00 11.55 ? 7   LEU A CG  1 
ATOM   49   C  CD1 . LEU A 1 29  ? 21.255 27.338 -2.080  1.00 11.83 ? 7   LEU A CD1 1 
ATOM   50   C  CD2 . LEU A 1 29  ? 19.285 26.985 -3.585  1.00 11.65 ? 7   LEU A CD2 1 
ATOM   51   N  N   . TYR A 1 30  ? 16.495 25.075 0.063   1.00 10.99 ? 8   TYR A N   1 
ATOM   52   C  CA  . TYR A 1 30  ? 16.006 24.235 1.148   1.00 11.33 ? 8   TYR A CA  1 
ATOM   53   C  C   . TYR A 1 30  ? 16.685 22.873 1.066   1.00 11.80 ? 8   TYR A C   1 
ATOM   54   O  O   . TYR A 1 30  ? 16.677 22.236 0.007   1.00 11.58 ? 8   TYR A O   1 
ATOM   55   C  CB  . TYR A 1 30  ? 14.493 24.077 1.053   1.00 11.25 ? 8   TYR A CB  1 
ATOM   56   C  CG  . TYR A 1 30  ? 13.883 23.228 2.149   1.00 11.21 ? 8   TYR A CG  1 
ATOM   57   C  CD1 . TYR A 1 30  ? 13.616 23.766 3.406   1.00 11.29 ? 8   TYR A CD1 1 
ATOM   58   C  CD2 . TYR A 1 30  ? 13.571 21.892 1.933   1.00 11.42 ? 8   TYR A CD2 1 
ATOM   59   C  CE1 . TYR A 1 30  ? 13.057 22.999 4.408   1.00 11.27 ? 8   TYR A CE1 1 
ATOM   60   C  CE2 . TYR A 1 30  ? 13.001 21.120 2.931   1.00 11.31 ? 8   TYR A CE2 1 
ATOM   61   C  CZ  . TYR A 1 30  ? 12.748 21.675 4.167   1.00 11.30 ? 8   TYR A CZ  1 
ATOM   62   O  OH  . TYR A 1 30  ? 12.186 20.906 5.167   1.00 11.44 ? 8   TYR A OH  1 
ATOM   63   N  N   . GLU A 1 31  ? 17.286 22.451 2.176   1.00 12.36 ? 9   GLU A N   1 
ATOM   64   C  CA  . GLU A 1 31  ? 17.967 21.159 2.272   1.00 13.20 ? 9   GLU A CA  1 
ATOM   65   C  C   . GLU A 1 31  ? 17.498 20.446 3.521   1.00 13.17 ? 9   GLU A C   1 
ATOM   66   O  O   . GLU A 1 31  ? 17.171 21.090 4.514   1.00 12.51 ? 9   GLU A O   1 
ATOM   67   C  CB  . GLU A 1 31  ? 19.481 21.337 2.437   1.00 14.20 ? 9   GLU A CB  1 
ATOM   68   C  CG  . GLU A 1 31  ? 20.174 22.258 1.455   1.00 15.42 ? 9   GLU A CG  1 
ATOM   69   C  CD  . GLU A 1 31  ? 21.568 22.623 1.930   1.00 16.48 ? 9   GLU A CD  1 
ATOM   70   O  OE1 . GLU A 1 31  ? 22.501 21.813 1.743   1.00 18.56 ? 9   GLU A OE1 1 
ATOM   71   O  OE2 . GLU A 1 31  ? 21.733 23.709 2.510   1.00 16.75 ? 9   GLU A OE2 1 
ATOM   72   N  N   . THR A 1 32  ? 17.496 19.119 3.484   1.00 13.32 ? 10  THR A N   1 
ATOM   73   C  CA  . THR A 1 32  ? 17.455 18.336 4.717   1.00 13.67 ? 10  THR A CA  1 
ATOM   74   C  C   . THR A 1 32  ? 18.685 17.440 4.783   1.00 13.75 ? 10  THR A C   1 
ATOM   75   O  O   . THR A 1 32  ? 19.108 16.863 3.775   1.00 13.60 ? 10  THR A O   1 
ATOM   76   C  CB  . THR A 1 32  ? 16.165 17.506 4.860   1.00 14.16 ? 10  THR A CB  1 
ATOM   77   O  OG1 . THR A 1 32  ? 16.028 16.631 3.737   1.00 14.68 ? 10  THR A OG1 1 
ATOM   78   C  CG2 . THR A 1 32  ? 14.946 18.411 4.950   1.00 14.28 ? 10  THR A CG2 1 
ATOM   79   N  N   . LEU A 1 33  ? 19.272 17.355 5.971   1.00 13.82 ? 11  LEU A N   1 
ATOM   80   C  CA  . LEU A 1 33  ? 20.469 16.552 6.200   1.00 14.00 ? 11  LEU A CA  1 
ATOM   81   C  C   . LEU A 1 33  ? 20.596 16.262 7.692   1.00 13.86 ? 11  LEU A C   1 
ATOM   82   O  O   . LEU A 1 33  ? 20.368 17.145 8.516   1.00 13.44 ? 11  LEU A O   1 
ATOM   83   C  CB  . LEU A 1 33  ? 21.724 17.266 5.677   1.00 14.30 ? 11  LEU A CB  1 
ATOM   84   C  CG  . LEU A 1 33  ? 22.263 18.515 6.391   1.00 14.65 ? 11  LEU A CG  1 
ATOM   85   C  CD1 . LEU A 1 33  ? 23.619 18.900 5.817   1.00 14.98 ? 11  LEU A CD1 1 
ATOM   86   C  CD2 . LEU A 1 33  ? 21.289 19.681 6.295   1.00 14.90 ? 11  LEU A CD2 1 
ATOM   87   N  N   . HIS A 1 34  ? 20.933 15.021 8.032   1.00 13.87 ? 12  HIS A N   1 
ATOM   88   C  CA  . HIS A 1 34  ? 21.134 14.615 9.424   1.00 14.11 ? 12  HIS A CA  1 
ATOM   89   C  C   . HIS A 1 34  ? 19.954 14.952 10.335  1.00 13.36 ? 12  HIS A C   1 
ATOM   90   O  O   . HIS A 1 34  ? 20.147 15.272 11.507  1.00 12.98 ? 12  HIS A O   1 
ATOM   91   C  CB  . HIS A 1 34  ? 22.403 15.253 9.989   1.00 15.03 ? 12  HIS A CB  1 
ATOM   92   C  CG  . HIS A 1 34  ? 23.626 15.004 9.165   1.00 16.07 ? 12  HIS A CG  1 
ATOM   93   N  ND1 . HIS A 1 34  ? 24.211 13.760 9.060   1.00 16.96 ? 12  HIS A ND1 1 
ATOM   94   C  CD2 . HIS A 1 34  ? 24.385 15.842 8.421   1.00 16.81 ? 12  HIS A CD2 1 
ATOM   95   C  CE1 . HIS A 1 34  ? 25.276 13.843 8.283   1.00 17.04 ? 12  HIS A CE1 1 
ATOM   96   N  NE2 . HIS A 1 34  ? 25.402 15.094 7.879   1.00 17.18 ? 12  HIS A NE2 1 
ATOM   97   N  N   . GLY A 1 35  ? 18.740 14.869 9.796   1.00 12.81 ? 13  GLY A N   1 
ATOM   98   C  CA  . GLY A 1 35  ? 17.529 15.182 10.551  1.00 12.58 ? 13  GLY A CA  1 
ATOM   99   C  C   . GLY A 1 35  ? 17.322 16.662 10.831  1.00 12.30 ? 13  GLY A C   1 
ATOM   100  O  O   . GLY A 1 35  ? 16.572 17.027 11.747  1.00 12.39 ? 13  GLY A O   1 
ATOM   101  N  N   . VAL A 1 36  ? 17.978 17.505 10.042  1.00 11.76 ? 14  VAL A N   1 
ATOM   102  C  CA  . VAL A 1 36  ? 17.929 18.961 10.186  1.00 11.71 ? 14  VAL A CA  1 
ATOM   103  C  C   . VAL A 1 36  ? 17.492 19.583 8.864   1.00 11.20 ? 14  VAL A C   1 
ATOM   104  O  O   . VAL A 1 36  ? 17.883 19.114 7.793   1.00 11.69 ? 14  VAL A O   1 
ATOM   105  C  CB  . VAL A 1 36  ? 19.327 19.523 10.552  1.00 11.80 ? 14  VAL A CB  1 
ATOM   106  C  CG1 . VAL A 1 36  ? 19.314 21.049 10.620  1.00 12.14 ? 14  VAL A CG1 1 
ATOM   107  C  CG2 . VAL A 1 36  ? 19.813 18.920 11.862  1.00 12.02 ? 14  VAL A CG2 1 
ATOM   108  N  N   . ALA A 1 37  ? 16.684 20.637 8.930   1.00 10.39 ? 15  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 37  ? 16.342 21.403 7.741   1.00 9.84  ? 15  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 37  ? 17.214 22.649 7.712   1.00 9.52  ? 15  ALA A C   1 
ATOM   111  O  O   . ALA A 1 37  ? 17.476 23.253 8.747   1.00 9.26  ? 15  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 37  ? 14.871 21.779 7.740   1.00 9.79  ? 15  ALA A CB  1 
ATOM   113  N  N   . ARG A 1 38  ? 17.680 23.023 6.528   1.00 9.14  ? 16  ARG A N   1 
ATOM   114  C  CA  . ARG A 1 38  ? 18.506 24.212 6.384   1.00 9.10  ? 16  ARG A CA  1 
ATOM   115  C  C   . ARG A 1 38  ? 17.945 25.087 5.272   1.00 8.59  ? 16  ARG A C   1 
ATOM   116  O  O   . ARG A 1 38  ? 17.790 24.638 4.133   1.00 8.47  ? 16  ARG A O   1 
ATOM   117  C  CB  . ARG A 1 38  ? 19.963 23.841 6.112   1.00 9.51  ? 16  ARG A CB  1 
ATOM   118  C  CG  . ARG A 1 38  ? 20.905 25.032 6.113   1.00 10.01 ? 16  ARG A CG  1 
ATOM   119  C  CD  . ARG A 1 38  ? 22.347 24.605 6.301   1.00 10.50 ? 16  ARG A CD  1 
ATOM   120  N  NE  . ARG A 1 38  ? 22.840 23.781 5.197   1.00 11.13 ? 16  ARG A NE  1 
ATOM   121  C  CZ  . ARG A 1 38  ? 23.984 23.099 5.217   1.00 11.85 ? 16  ARG A CZ  1 
ATOM   122  N  NH1 . ARG A 1 38  ? 24.768 23.107 6.293   1.00 12.19 ? 16  ARG A NH1 1 
ATOM   123  N  NH2 . ARG A 1 38  ? 24.345 22.383 4.159   1.00 12.46 ? 16  ARG A NH2 1 
ATOM   124  N  N   . ILE A 1 39  ? 17.630 26.332 5.627   1.00 8.10  ? 17  ILE A N   1 
ATOM   125  C  CA  . ILE A 1 39  ? 17.109 27.319 4.699   1.00 7.90  ? 17  ILE A CA  1 
ATOM   126  C  C   . ILE A 1 39  ? 18.207 28.337 4.420   1.00 7.78  ? 17  ILE A C   1 
ATOM   127  O  O   . ILE A 1 39  ? 18.783 28.905 5.346   1.00 7.55  ? 17  ILE A O   1 
ATOM   128  C  CB  . ILE A 1 39  ? 15.876 28.044 5.289   1.00 7.93  ? 17  ILE A CB  1 
ATOM   129  C  CG1 . ILE A 1 39  ? 14.720 27.058 5.468   1.00 7.98  ? 17  ILE A CG1 1 
ATOM   130  C  CG2 . ILE A 1 39  ? 15.456 29.216 4.406   1.00 8.07  ? 17  ILE A CG2 1 
ATOM   131  C  CD1 . ILE A 1 39  ? 13.602 27.576 6.351   1.00 7.95  ? 17  ILE A CD1 1 
ATOM   132  N  N   . THR A 1 40  ? 18.494 28.561 3.141   1.00 7.63  ? 18  THR A N   1 
ATOM   133  C  CA  . THR A 1 40  ? 19.488 29.536 2.729   1.00 7.71  ? 18  THR A CA  1 
ATOM   134  C  C   . THR A 1 40  ? 18.787 30.682 2.011   1.00 7.80  ? 18  THR A C   1 
ATOM   135  O  O   . THR A 1 40  ? 18.113 30.468 1.003   1.00 7.88  ? 18  THR A O   1 
ATOM   136  C  CB  . THR A 1 40  ? 20.531 28.901 1.786   1.00 7.66  ? 18  THR A CB  1 
ATOM   137  O  OG1 . THR A 1 40  ? 21.155 27.781 2.437   1.00 7.67  ? 18  THR A OG1 1 
ATOM   138  C  CG2 . THR A 1 40  ? 21.603 29.914 1.381   1.00 7.73  ? 18  THR A CG2 1 
ATOM   139  N  N   . LEU A 1 41  ? 18.948 31.895 2.533   1.00 7.95  ? 19  LEU A N   1 
ATOM   140  C  CA  . LEU A 1 41  ? 18.405 33.100 1.897   1.00 8.21  ? 19  LEU A CA  1 
ATOM   141  C  C   . LEU A 1 41  ? 19.291 33.377 0.692   1.00 8.65  ? 19  LEU A C   1 
ATOM   142  O  O   . LEU A 1 41  ? 20.486 33.646 0.851   1.00 8.54  ? 19  LEU A O   1 
ATOM   143  C  CB  . LEU A 1 41  ? 18.426 34.280 2.872   1.00 8.18  ? 19  LEU A CB  1 
ATOM   144  C  CG  . LEU A 1 41  ? 17.823 34.009 4.253   1.00 8.18  ? 19  LEU A CG  1 
ATOM   145  C  CD1 . LEU A 1 41  ? 18.026 35.207 5.164   1.00 8.24  ? 19  LEU A CD1 1 
ATOM   146  C  CD2 . LEU A 1 41  ? 16.351 33.639 4.131   1.00 8.16  ? 19  LEU A CD2 1 
ATOM   147  N  N   . ASN A 1 42  ? 18.721 33.282 -0.508  1.00 9.35  ? 20  ASN A N   1 
ATOM   148  C  CA  . ASN A 1 42  ? 19.533 33.142 -1.720  1.00 10.07 ? 20  ASN A CA  1 
ATOM   149  C  C   . ASN A 1 42  ? 19.314 34.217 -2.789  1.00 10.48 ? 20  ASN A C   1 
ATOM   150  O  O   . ASN A 1 42  ? 18.679 33.968 -3.812  1.00 10.67 ? 20  ASN A O   1 
ATOM   151  C  CB  . ASN A 1 42  ? 19.315 31.749 -2.326  1.00 10.32 ? 20  ASN A CB  1 
ATOM   152  C  CG  . ASN A 1 42  ? 20.336 31.412 -3.400  1.00 10.76 ? 20  ASN A CG  1 
ATOM   153  O  OD1 . ASN A 1 42  ? 21.470 31.878 -3.352  1.00 11.11 ? 20  ASN A OD1 1 
ATOM   154  N  ND2 . ASN A 1 42  ? 19.937 30.602 -4.374  1.00 11.05 ? 20  ASN A ND2 1 
ATOM   155  N  N   . ARG A 1 43  ? 19.848 35.410 -2.543  1.00 11.06 ? 21  ARG A N   1 
ATOM   156  C  CA  . ARG A 1 43  ? 19.969 36.430 -3.586  1.00 11.68 ? 21  ARG A CA  1 
ATOM   157  C  C   . ARG A 1 43  ? 21.287 37.167 -3.406  1.00 11.26 ? 21  ARG A C   1 
ATOM   158  O  O   . ARG A 1 43  ? 21.317 38.324 -2.987  1.00 10.61 ? 21  ARG A O   1 
ATOM   159  C  CB  . ARG A 1 43  ? 18.798 37.397 -3.590  1.00 12.70 ? 21  ARG A CB  1 
ATOM   160  C  CG  . ARG A 1 43  ? 18.769 38.206 -4.871  1.00 13.92 ? 21  ARG A CG  1 
ATOM   161  C  CD  . ARG A 1 43  ? 17.426 38.833 -5.112  1.00 14.99 ? 21  ARG A CD  1 
ATOM   162  N  NE  . ARG A 1 43  ? 17.284 39.311 -6.484  1.00 16.02 ? 21  ARG A NE  1 
ATOM   163  C  CZ  . ARG A 1 43  ? 16.232 39.993 -6.923  1.00 17.06 ? 21  ARG A CZ  1 
ATOM   164  N  NH1 . ARG A 1 43  ? 15.238 40.295 -6.094  1.00 17.28 ? 21  ARG A NH1 1 
ATOM   165  N  NH2 . ARG A 1 43  ? 16.180 40.389 -8.188  1.00 17.45 ? 21  ARG A NH2 1 
ATOM   166  N  N   . PRO A 1 44  ? 22.391 36.481 -3.725  1.00 11.53 ? 22  PRO A N   1 
ATOM   167  C  CA  . PRO A 1 44  ? 23.734 36.990 -3.441  1.00 11.52 ? 22  PRO A CA  1 
ATOM   168  C  C   . PRO A 1 44  ? 24.030 38.361 -4.037  1.00 11.41 ? 22  PRO A C   1 
ATOM   169  O  O   . PRO A 1 44  ? 24.790 39.116 -3.451  1.00 11.47 ? 22  PRO A O   1 
ATOM   170  C  CB  . PRO A 1 44  ? 24.666 35.930 -4.054  1.00 11.81 ? 22  PRO A CB  1 
ATOM   171  C  CG  . PRO A 1 44  ? 23.828 34.738 -4.302  1.00 11.71 ? 22  PRO A CG  1 
ATOM   172  C  CD  . PRO A 1 44  ? 22.416 35.188 -4.431  1.00 11.65 ? 22  PRO A CD  1 
ATOM   173  N  N   . GLU A 1 45  ? 23.438 38.681 -5.186  1.00 11.47 ? 23  GLU A N   1 
ATOM   174  C  CA  . GLU A 1 45  ? 23.677 39.964 -5.842  1.00 11.68 ? 23  GLU A CA  1 
ATOM   175  C  C   . GLU A 1 45  ? 22.943 41.140 -5.184  1.00 11.52 ? 23  GLU A C   1 
ATOM   176  O  O   . GLU A 1 45  ? 23.201 42.290 -5.525  1.00 11.36 ? 23  GLU A O   1 
ATOM   177  C  CB  . GLU A 1 45  ? 23.331 39.879 -7.338  1.00 12.14 ? 23  GLU A CB  1 
ATOM   178  C  CG  . GLU A 1 45  ? 21.851 39.989 -7.692  1.00 12.77 ? 23  GLU A CG  1 
ATOM   179  C  CD  . GLU A 1 45  ? 21.059 38.709 -7.487  1.00 13.11 ? 23  GLU A CD  1 
ATOM   180  O  OE1 . GLU A 1 45  ? 21.559 37.767 -6.837  1.00 13.84 ? 23  GLU A OE1 1 
ATOM   181  O  OE2 . GLU A 1 45  ? 19.916 38.644 -7.992  1.00 14.22 ? 23  GLU A OE2 1 
ATOM   182  N  N   . ARG A 1 46  ? 22.023 40.850 -4.264  1.00 11.23 ? 24  ARG A N   1 
ATOM   183  C  CA  . ARG A 1 46  ? 21.326 41.889 -3.506  1.00 11.48 ? 24  ARG A CA  1 
ATOM   184  C  C   . ARG A 1 46  ? 21.531 41.719 -2.002  1.00 10.96 ? 24  ARG A C   1 
ATOM   185  O  O   . ARG A 1 46  ? 20.676 42.113 -1.209  1.00 10.70 ? 24  ARG A O   1 
ATOM   186  C  CB  . ARG A 1 46  ? 19.827 41.872 -3.825  1.00 12.33 ? 24  ARG A CB  1 
ATOM   187  C  CG  . ARG A 1 46  ? 19.474 42.275 -5.242  1.00 13.46 ? 24  ARG A CG  1 
ATOM   188  C  CD  . ARG A 1 46  ? 18.079 42.884 -5.301  1.00 14.53 ? 24  ARG A CD  1 
ATOM   189  N  NE  . ARG A 1 46  ? 17.692 43.235 -6.662  1.00 15.51 ? 24  ARG A NE  1 
ATOM   190  C  CZ  . ARG A 1 46  ? 16.511 43.738 -7.015  1.00 16.07 ? 24  ARG A CZ  1 
ATOM   191  N  NH1 . ARG A 1 46  ? 15.563 43.966 -6.111  1.00 16.20 ? 24  ARG A NH1 1 
ATOM   192  N  NH2 . ARG A 1 46  ? 16.275 44.014 -8.292  1.00 16.59 ? 24  ARG A NH2 1 
ATOM   193  N  N   . THR A 1 47  ? 22.669 41.152 -1.611  1.00 10.42 ? 25  THR A N   1 
ATOM   194  C  CA  . THR A 1 47  ? 22.970 40.886 -0.194  1.00 10.21 ? 25  THR A CA  1 
ATOM   195  C  C   . THR A 1 47  ? 21.822 40.089 0.442   1.00 9.82  ? 25  THR A C   1 
ATOM   196  O  O   . THR A 1 47  ? 21.425 40.334 1.586   1.00 9.63  ? 25  THR A O   1 
ATOM   197  C  CB  . THR A 1 47  ? 23.251 42.199 0.580   1.00 10.51 ? 25  THR A CB  1 
ATOM   198  O  OG1 . THR A 1 47  ? 24.027 43.084 -0.244  1.00 10.88 ? 25  THR A OG1 1 
ATOM   199  C  CG2 . THR A 1 47  ? 24.019 41.928 1.865   1.00 10.63 ? 25  THR A CG2 1 
ATOM   200  N  N   . ASN A 1 48  ? 21.282 39.142 -0.326  1.00 9.31  ? 26  ASN A N   1 
ATOM   201  C  CA  . ASN A 1 48  ? 20.176 38.293 0.115   1.00 9.23  ? 26  ASN A CA  1 
ATOM   202  C  C   . ASN A 1 48  ? 18.999 39.067 0.701   1.00 9.41  ? 26  ASN A C   1 
ATOM   203  O  O   . ASN A 1 48  ? 18.350 38.620 1.653   1.00 9.03  ? 26  ASN A O   1 
ATOM   204  C  CB  . ASN A 1 48  ? 20.693 37.261 1.106   1.00 9.11  ? 26  ASN A CB  1 
ATOM   205  C  CG  . ASN A 1 48  ? 21.863 36.485 0.558   1.00 9.08  ? 26  ASN A CG  1 
ATOM   206  O  OD1 . ASN A 1 48  ? 21.901 36.153 -0.646  1.00 9.22  ? 26  ASN A OD1 1 
ATOM   207  N  ND2 . ASN A 1 48  ? 22.826 36.183 1.417   1.00 8.74  ? 26  ASN A ND2 1 
ATOM   208  N  N   . ALA A 1 49  ? 18.717 40.221 0.103   1.00 9.81  ? 27  ALA A N   1 
ATOM   209  C  CA  . ALA A 1 49  ? 17.618 41.067 0.548   1.00 10.45 ? 27  ALA A CA  1 
ATOM   210  C  C   . ALA A 1 49  ? 16.297 40.310 0.485   1.00 11.09 ? 27  ALA A C   1 
ATOM   211  O  O   . ALA A 1 49  ? 16.039 39.555 -0.457  1.00 11.21 ? 27  ALA A O   1 
ATOM   212  C  CB  . ALA A 1 49  ? 17.546 42.331 -0.298  1.00 10.37 ? 27  ALA A CB  1 
ATOM   213  N  N   . LEU A 1 50  ? 15.466 40.516 1.499   1.00 12.05 ? 28  LEU A N   1 
ATOM   214  C  CA  . LEU A 1 50  ? 14.204 39.802 1.627   1.00 13.19 ? 28  LEU A CA  1 
ATOM   215  C  C   . LEU A 1 50  ? 13.105 40.524 0.849   1.00 13.74 ? 28  LEU A C   1 
ATOM   216  O  O   . LEU A 1 50  ? 12.557 41.514 1.329   1.00 15.10 ? 28  LEU A O   1 
ATOM   217  C  CB  . LEU A 1 50  ? 13.815 39.699 3.109   1.00 13.48 ? 28  LEU A CB  1 
ATOM   218  C  CG  . LEU A 1 50  ? 14.753 38.892 4.019   1.00 13.94 ? 28  LEU A CG  1 
ATOM   219  C  CD1 . LEU A 1 50  ? 14.837 39.519 5.403   1.00 14.27 ? 28  LEU A CD1 1 
ATOM   220  C  CD2 . LEU A 1 50  ? 14.308 37.445 4.121   1.00 14.27 ? 28  LEU A CD2 1 
ATOM   221  N  N   . ASP A 1 51  ? 12.780 40.035 -0.345  1.00 14.29 ? 29  ASP A N   1 
ATOM   222  C  CA  . ASP A 1 51  ? 11.668 40.609 -1.114  1.00 14.49 ? 29  ASP A CA  1 
ATOM   223  C  C   . ASP A 1 51  ? 10.390 39.796 -0.879  1.00 14.52 ? 29  ASP A C   1 
ATOM   224  O  O   . ASP A 1 51  ? 10.400 38.824 -0.123  1.00 13.49 ? 29  ASP A O   1 
ATOM   225  C  CB  . ASP A 1 51  ? 12.015 40.759 -2.605  1.00 14.89 ? 29  ASP A CB  1 
ATOM   226  C  CG  . ASP A 1 51  ? 12.190 39.433 -3.333  1.00 15.07 ? 29  ASP A CG  1 
ATOM   227  O  OD1 . ASP A 1 51  ? 12.113 38.359 -2.707  1.00 15.19 ? 29  ASP A OD1 1 
ATOM   228  O  OD2 . ASP A 1 51  ? 12.411 39.474 -4.568  1.00 16.03 ? 29  ASP A OD2 1 
ATOM   229  N  N   . GLN A 1 52  ? 9.296  40.209 -1.516  1.00 14.99 ? 30  GLN A N   1 
ATOM   230  C  CA  . GLN A 1 52  ? 7.997  39.553 -1.338  1.00 15.86 ? 30  GLN A CA  1 
ATOM   231  C  C   . GLN A 1 52  ? 8.041  38.075 -1.674  1.00 15.32 ? 30  GLN A C   1 
ATOM   232  O  O   . GLN A 1 52  ? 7.497  37.240 -0.942  1.00 14.74 ? 30  GLN A O   1 
ATOM   233  C  CB  . GLN A 1 52  ? 6.939  40.220 -2.225  1.00 16.83 ? 30  GLN A CB  1 
ATOM   234  C  CG  . GLN A 1 52  ? 6.617  41.639 -1.818  1.00 17.91 ? 30  GLN A CG  1 
ATOM   235  C  CD  . GLN A 1 52  ? 6.211  41.714 -0.366  1.00 18.46 ? 30  GLN A CD  1 
ATOM   236  O  OE1 . GLN A 1 52  ? 7.000  42.113 0.486   1.00 20.13 ? 30  GLN A OE1 1 
ATOM   237  N  NE2 . GLN A 1 52  ? 4.993  41.277 -0.068  1.00 19.93 ? 30  GLN A NE2 1 
ATOM   238  N  N   . GLU A 1 53  ? 8.681  37.767 -2.796  1.00 15.43 ? 31  GLU A N   1 
ATOM   239  C  CA  . GLU A 1 53  ? 8.797  36.401 -3.263  1.00 15.77 ? 31  GLU A CA  1 
ATOM   240  C  C   . GLU A 1 53  ? 9.554  35.541 -2.254  1.00 14.88 ? 31  GLU A C   1 
ATOM   241  O  O   . GLU A 1 53  ? 9.125  34.435 -1.942  1.00 14.26 ? 31  GLU A O   1 
ATOM   242  C  CB  . GLU A 1 53  ? 9.489  36.353 -4.627  1.00 17.05 ? 31  GLU A CB  1 
ATOM   243  C  CG  . GLU A 1 53  ? 9.482  34.971 -5.257  1.00 18.40 ? 31  GLU A CG  1 
ATOM   244  C  CD  . GLU A 1 53  ? 10.100 34.930 -6.644  1.00 19.62 ? 31  GLU A CD  1 
ATOM   245  O  OE1 . GLU A 1 53  ? 10.609 35.965 -7.124  1.00 21.68 ? 31  GLU A OE1 1 
ATOM   246  O  OE2 . GLU A 1 53  ? 10.081 33.845 -7.256  1.00 21.04 ? 31  GLU A OE2 1 
HETATM 247  N  N   . MSE A 1 54  ? 10.673 36.051 -1.745  1.00 14.16 ? 32  MSE A N   1 
HETATM 248  C  CA  . MSE A 1 54  ? 11.494 35.287 -0.799  1.00 13.95 ? 32  MSE A CA  1 
HETATM 249  C  C   . MSE A 1 54  ? 10.730 35.024 0.475   1.00 12.73 ? 32  MSE A C   1 
HETATM 250  O  O   . MSE A 1 54  ? 10.803 33.925 1.016   1.00 11.88 ? 32  MSE A O   1 
HETATM 251  C  CB  . MSE A 1 54  ? 12.828 35.973 -0.499  1.00 15.82 ? 32  MSE A CB  1 
HETATM 252  C  CG  . MSE A 1 54  ? 13.788 35.030 0.237   1.00 17.27 ? 32  MSE A CG  1 
HETATM 253  SE SE  . MSE A 1 54  ? 15.362 35.980 0.960   1.00 22.26 ? 32  MSE A SE  1 
HETATM 254  C  CE  . MSE A 1 54  ? 16.240 36.421 -0.756  1.00 20.48 ? 32  MSE A CE  1 
ATOM   255  N  N   . LEU A 1 55  ? 9.988  36.015 0.971   1.00 11.70 ? 33  LEU A N   1 
ATOM   256  C  CA  . LEU A 1 55  ? 9.178  35.810 2.181   1.00 11.27 ? 33  LEU A CA  1 
ATOM   257  C  C   . LEU A 1 55  ? 8.146  34.701 1.977   1.00 10.80 ? 33  LEU A C   1 
ATOM   258  O  O   . LEU A 1 55  ? 7.944  33.863 2.855   1.00 10.56 ? 33  LEU A O   1 
ATOM   259  C  CB  . LEU A 1 55  ? 8.483  37.105 2.612   1.00 11.34 ? 33  LEU A CB  1 
ATOM   260  C  CG  . LEU A 1 55  ? 9.390  38.261 3.028   1.00 11.46 ? 33  LEU A CG  1 
ATOM   261  C  CD1 . LEU A 1 55  ? 8.561  39.520 3.222   1.00 11.82 ? 33  LEU A CD1 1 
ATOM   262  C  CD2 . LEU A 1 55  ? 10.187 37.945 4.286   1.00 11.34 ? 33  LEU A CD2 1 
ATOM   263  N  N   . GLY A 1 56  ? 7.500  34.684 0.814   1.00 10.42 ? 34  GLY A N   1 
ATOM   264  C  CA  . GLY A 1 56  ? 6.560  33.610 0.492   1.00 10.18 ? 34  GLY A CA  1 
ATOM   265  C  C   . GLY A 1 56  ? 7.213  32.236 0.508   1.00 9.91  ? 34  GLY A C   1 
ATOM   266  O  O   . GLY A 1 56  ? 6.659  31.275 1.047   1.00 9.84  ? 34  GLY A O   1 
ATOM   267  N  N   . GLU A 1 57  ? 8.403  32.144 -0.076  1.00 9.78  ? 35  GLU A N   1 
ATOM   268  C  CA  . GLU A 1 57  ? 9.134  30.883 -0.117  1.00 9.75  ? 35  GLU A CA  1 
ATOM   269  C  C   . GLU A 1 57  ? 9.613  30.456 1.273   1.00 9.24  ? 35  GLU A C   1 
ATOM   270  O  O   . GLU A 1 57  ? 9.602  29.268 1.587   1.00 9.20  ? 35  GLU A O   1 
ATOM   271  C  CB  . GLU A 1 57  ? 10.295 30.973 -1.102  1.00 10.29 ? 35  GLU A CB  1 
ATOM   272  C  CG  . GLU A 1 57  ? 9.814  31.168 -2.532  1.00 10.90 ? 35  GLU A CG  1 
ATOM   273  C  CD  . GLU A 1 57  ? 10.926 31.072 -3.552  1.00 11.75 ? 35  GLU A CD  1 
ATOM   274  O  OE1 . GLU A 1 57  ? 12.097 31.274 -3.186  1.00 12.27 ? 35  GLU A OE1 1 
ATOM   275  O  OE2 . GLU A 1 57  ? 10.627 30.775 -4.727  1.00 13.02 ? 35  GLU A OE2 1 
ATOM   276  N  N   . ILE A 1 58  ? 10.003 31.417 2.111   1.00 8.70  ? 36  ILE A N   1 
ATOM   277  C  CA  . ILE A 1 58  ? 10.393 31.098 3.493   1.00 8.31  ? 36  ILE A CA  1 
ATOM   278  C  C   . ILE A 1 58  ? 9.214  30.457 4.227   1.00 8.21  ? 36  ILE A C   1 
ATOM   279  O  O   . ILE A 1 58  ? 9.382  29.475 4.941   1.00 7.96  ? 36  ILE A O   1 
ATOM   280  C  CB  . ILE A 1 58  ? 10.900 32.336 4.272   1.00 8.18  ? 36  ILE A CB  1 
ATOM   281  C  CG1 . ILE A 1 58  ? 12.256 32.796 3.725   1.00 8.16  ? 36  ILE A CG1 1 
ATOM   282  C  CG2 . ILE A 1 58  ? 11.029 32.019 5.761   1.00 8.20  ? 36  ILE A CG2 1 
ATOM   283  C  CD1 . ILE A 1 58  ? 12.656 34.187 4.153   1.00 8.18  ? 36  ILE A CD1 1 
ATOM   284  N  N   . ASN A 1 59  ? 8.019  31.006 4.043   1.00 8.13  ? 37  ASN A N   1 
ATOM   285  C  CA  . ASN A 1 59  ? 6.825  30.435 4.661   1.00 8.21  ? 37  ASN A CA  1 
ATOM   286  C  C   . ASN A 1 59  ? 6.544  29.014 4.170   1.00 8.23  ? 37  ASN A C   1 
ATOM   287  O  O   . ASN A 1 59  ? 6.211  28.138 4.963   1.00 8.01  ? 37  ASN A O   1 
ATOM   288  C  CB  . ASN A 1 59  ? 5.623  31.350 4.442   1.00 8.32  ? 37  ASN A CB  1 
ATOM   289  C  CG  . ASN A 1 59  ? 5.663  32.566 5.337   1.00 8.33  ? 37  ASN A CG  1 
ATOM   290  O  OD1 . ASN A 1 59  ? 5.907  33.692 4.889   1.00 8.88  ? 37  ASN A OD1 1 
ATOM   291  N  ND2 . ASN A 1 59  ? 5.488  32.338 6.616   1.00 8.11  ? 37  ASN A ND2 1 
ATOM   292  N  N   . ALA A 1 60  ? 6.702  28.790 2.868   1.00 8.35  ? 38  ALA A N   1 
ATOM   293  C  CA  . ALA A 1 60  ? 6.556  27.451 2.295   1.00 8.63  ? 38  ALA A CA  1 
ATOM   294  C  C   . ALA A 1 60  ? 7.588  26.464 2.860   1.00 8.63  ? 38  ALA A C   1 
ATOM   295  O  O   . ALA A 1 60  ? 7.253  25.310 3.158   1.00 8.76  ? 38  ALA A O   1 
ATOM   296  C  CB  . ALA A 1 60  ? 6.660  27.518 0.782   1.00 8.72  ? 38  ALA A CB  1 
ATOM   297  N  N   . ALA A 1 61  ? 8.833  26.911 2.997   1.00 8.74  ? 39  ALA A N   1 
ATOM   298  C  CA  . ALA A 1 61  ? 9.904  26.064 3.536   1.00 8.93  ? 39  ALA A CA  1 
ATOM   299  C  C   . ALA A 1 61  ? 9.659  25.724 5.006   1.00 9.24  ? 39  ALA A C   1 
ATOM   300  O  O   . ALA A 1 61  ? 9.871  24.583 5.429   1.00 9.09  ? 39  ALA A O   1 
ATOM   301  C  CB  . ALA A 1 61  ? 11.256 26.740 3.369   1.00 8.86  ? 39  ALA A CB  1 
HETATM 302  N  N   . MSE A 1 62  ? 9.221  26.714 5.780   1.00 9.72  ? 40  MSE A N   1 
HETATM 303  C  CA  . MSE A 1 62  ? 8.898  26.489 7.192   1.00 10.32 ? 40  MSE A CA  1 
HETATM 304  C  C   . MSE A 1 62  ? 7.715  25.559 7.328   1.00 10.00 ? 40  MSE A C   1 
HETATM 305  O  O   . MSE A 1 62  ? 7.697  24.705 8.214   1.00 9.64  ? 40  MSE A O   1 
HETATM 306  C  CB  . MSE A 1 62  ? 8.663  27.806 7.930   1.00 11.47 ? 40  MSE A CB  1 
HETATM 307  C  CG  . MSE A 1 62  ? 9.956  28.612 8.070   1.00 12.67 ? 40  MSE A CG  1 
HETATM 308  SE SE  . MSE A 1 62  ? 11.256 27.726 9.259   1.00 16.24 ? 40  MSE A SE  1 
HETATM 309  C  CE  . MSE A 1 62  ? 10.478 28.340 10.958  1.00 14.65 ? 40  MSE A CE  1 
ATOM   310  N  N   . ASP A 1 63  ? 6.718  25.696 6.458   1.00 9.75  ? 41  ASP A N   1 
ATOM   311  C  CA  . ASP A 1 63  ? 5.611  24.735 6.440   1.00 10.00 ? 41  ASP A CA  1 
ATOM   312  C  C   . ASP A 1 63  ? 6.141  23.313 6.222   1.00 9.84  ? 41  ASP A C   1 
ATOM   313  O  O   . ASP A 1 63  ? 5.750  22.374 6.926   1.00 9.83  ? 41  ASP A O   1 
ATOM   314  C  CB  . ASP A 1 63  ? 4.598  25.063 5.336   1.00 10.31 ? 41  ASP A CB  1 
ATOM   315  C  CG  . ASP A 1 63  ? 3.769  26.301 5.624   1.00 10.66 ? 41  ASP A CG  1 
ATOM   316  O  OD1 . ASP A 1 63  ? 3.773  26.818 6.764   1.00 10.82 ? 41  ASP A OD1 1 
ATOM   317  O  OD2 . ASP A 1 63  ? 3.084  26.754 4.678   1.00 11.47 ? 41  ASP A OD2 1 
ATOM   318  N  N   . ALA A 1 64  ? 7.037  23.154 5.250   1.00 9.68  ? 42  ALA A N   1 
ATOM   319  C  CA  . ALA A 1 64  ? 7.585  21.833 4.925   1.00 9.57  ? 42  ALA A CA  1 
ATOM   320  C  C   . ALA A 1 64  ? 8.393  21.269 6.086   1.00 9.52  ? 42  ALA A C   1 
ATOM   321  O  O   . ALA A 1 64  ? 8.228  20.110 6.452   1.00 9.62  ? 42  ALA A O   1 
ATOM   322  C  CB  . ALA A 1 64  ? 8.445  21.900 3.672   1.00 9.64  ? 42  ALA A CB  1 
ATOM   323  N  N   . ALA A 1 65  ? 9.261  22.095 6.667   1.00 9.34  ? 43  ALA A N   1 
ATOM   324  C  CA  . ALA A 1 65  ? 10.095 21.670 7.795   1.00 9.20  ? 43  ALA A CA  1 
ATOM   325  C  C   . ALA A 1 65  ? 9.239  21.270 8.993   1.00 9.26  ? 43  ALA A C   1 
ATOM   326  O  O   . ALA A 1 65  ? 9.537  20.294 9.675   1.00 9.15  ? 43  ALA A O   1 
ATOM   327  C  CB  . ALA A 1 65  ? 11.073 22.777 8.187   1.00 9.19  ? 43  ALA A CB  1 
ATOM   328  N  N   . GLU A 1 66  ? 8.171  22.024 9.239   1.00 9.36  ? 44  GLU A N   1 
ATOM   329  C  CA  . GLU A 1 66  ? 7.293  21.757 10.381  1.00 9.67  ? 44  GLU A CA  1 
ATOM   330  C  C   . GLU A 1 66  ? 6.465  20.484 10.189  1.00 9.96  ? 44  GLU A C   1 
ATOM   331  O  O   . GLU A 1 66  ? 6.224  19.750 11.153  1.00 9.93  ? 44  GLU A O   1 
ATOM   332  C  CB  . GLU A 1 66  ? 6.421  22.985 10.680  1.00 9.82  ? 44  GLU A CB  1 
ATOM   333  C  CG  . GLU A 1 66  ? 7.245  24.098 11.311  1.00 9.92  ? 44  GLU A CG  1 
ATOM   334  C  CD  . GLU A 1 66  ? 6.555  25.445 11.383  1.00 10.19 ? 44  GLU A CD  1 
ATOM   335  O  OE1 . GLU A 1 66  ? 5.342  25.555 11.102  1.00 10.46 ? 44  GLU A OE1 1 
ATOM   336  O  OE2 . GLU A 1 66  ? 7.258  26.414 11.721  1.00 10.42 ? 44  GLU A OE2 1 
ATOM   337  N  N   . ALA A 1 67  ? 6.093  20.192 8.945   1.00 10.25 ? 45  ALA A N   1 
ATOM   338  C  CA  . ALA A 1 67  ? 5.321  18.981 8.614   1.00 10.65 ? 45  ALA A CA  1 
ATOM   339  C  C   . ALA A 1 67  ? 6.152  17.702 8.537   1.00 10.95 ? 45  ALA A C   1 
ATOM   340  O  O   . ALA A 1 67  ? 5.598  16.600 8.631   1.00 11.61 ? 45  ALA A O   1 
ATOM   341  C  CB  . ALA A 1 67  ? 4.594  19.180 7.296   1.00 10.59 ? 45  ALA A CB  1 
ATOM   342  N  N   . ASP A 1 68  ? 7.459  17.843 8.336   1.00 10.89 ? 46  ASP A N   1 
ATOM   343  C  CA  . ASP A 1 68  ? 8.351  16.701 8.120   1.00 11.03 ? 46  ASP A CA  1 
ATOM   344  C  C   . ASP A 1 68  ? 8.839  16.151 9.458   1.00 11.00 ? 46  ASP A C   1 
ATOM   345  O  O   . ASP A 1 68  ? 9.694  16.753 10.110  1.00 10.82 ? 46  ASP A O   1 
ATOM   346  C  CB  . ASP A 1 68  ? 9.532  17.129 7.236   1.00 11.22 ? 46  ASP A CB  1 
ATOM   347  C  CG  . ASP A 1 68  ? 10.438 15.969 6.832   1.00 11.40 ? 46  ASP A CG  1 
ATOM   348  O  OD1 . ASP A 1 68  ? 10.325 14.855 7.386   1.00 11.76 ? 46  ASP A OD1 1 
ATOM   349  O  OD2 . ASP A 1 68  ? 11.294 16.186 5.946   1.00 11.65 ? 46  ASP A OD2 1 
ATOM   350  N  N   . ALA A 1 69  ? 8.310  14.994 9.857   1.00 11.26 ? 47  ALA A N   1 
ATOM   351  C  CA  . ALA A 1 69  ? 8.690  14.387 11.136  1.00 11.34 ? 47  ALA A CA  1 
ATOM   352  C  C   . ALA A 1 69  ? 10.178 14.026 11.210  1.00 11.40 ? 47  ALA A C   1 
ATOM   353  O  O   . ALA A 1 69  ? 10.726 13.873 12.303  1.00 11.62 ? 47  ALA A O   1 
ATOM   354  C  CB  . ALA A 1 69  ? 7.824  13.168 11.431  1.00 11.51 ? 47  ALA A CB  1 
ATOM   355  N  N   . GLY A 1 70  ? 10.823 13.882 10.054  1.00 11.33 ? 48  GLY A N   1 
ATOM   356  C  CA  . GLY A 1 70  ? 12.258 13.646 9.988   1.00 11.44 ? 48  GLY A CA  1 
ATOM   357  C  C   . GLY A 1 70  ? 13.106 14.875 10.282  1.00 11.33 ? 48  GLY A C   1 
ATOM   358  O  O   . GLY A 1 70  ? 14.315 14.757 10.461  1.00 12.40 ? 48  GLY A O   1 
ATOM   359  N  N   . VAL A 1 71  ? 12.482 16.053 10.321  1.00 10.68 ? 49  VAL A N   1 
ATOM   360  C  CA  . VAL A 1 71  ? 13.177 17.299 10.651  1.00 10.35 ? 49  VAL A CA  1 
ATOM   361  C  C   . VAL A 1 71  ? 12.992 17.598 12.135  1.00 10.00 ? 49  VAL A C   1 
ATOM   362  O  O   . VAL A 1 71  ? 11.863 17.656 12.617  1.00 9.84  ? 49  VAL A O   1 
ATOM   363  C  CB  . VAL A 1 71  ? 12.637 18.477 9.813   1.00 10.36 ? 49  VAL A CB  1 
ATOM   364  C  CG1 . VAL A 1 71  ? 13.173 19.813 10.331  1.00 10.35 ? 49  VAL A CG1 1 
ATOM   365  C  CG2 . VAL A 1 71  ? 12.985 18.280 8.345   1.00 10.39 ? 49  VAL A CG2 1 
ATOM   366  N  N   . LYS A 1 72  ? 14.104 17.784 12.843  1.00 9.84  ? 50  LYS A N   1 
ATOM   367  C  CA  . LYS A 1 72  ? 14.091 18.020 14.289  1.00 9.89  ? 50  LYS A CA  1 
ATOM   368  C  C   . LYS A 1 72  ? 14.449 19.458 14.666  1.00 9.10  ? 50  LYS A C   1 
ATOM   369  O  O   . LYS A 1 72  ? 14.180 19.885 15.789  1.00 8.79  ? 50  LYS A O   1 
ATOM   370  C  CB  . LYS A 1 72  ? 15.080 17.082 14.984  1.00 10.76 ? 50  LYS A CB  1 
ATOM   371  C  CG  . LYS A 1 72  ? 14.911 15.606 14.670  1.00 11.80 ? 50  LYS A CG  1 
ATOM   372  C  CD  . LYS A 1 72  ? 13.617 15.057 15.237  1.00 12.42 ? 50  LYS A CD  1 
ATOM   373  C  CE  . LYS A 1 72  ? 13.402 13.598 14.855  1.00 13.12 ? 50  LYS A CE  1 
ATOM   374  N  NZ  . LYS A 1 72  ? 14.502 12.719 15.329  1.00 13.75 ? 50  LYS A NZ  1 
ATOM   375  N  N   . ALA A 1 73  ? 15.076 20.184 13.745  1.00 8.23  ? 51  ALA A N   1 
ATOM   376  C  CA  . ALA A 1 73  ? 15.502 21.560 13.981  1.00 7.86  ? 51  ALA A CA  1 
ATOM   377  C  C   . ALA A 1 73  ? 15.726 22.241 12.639  1.00 7.61  ? 51  ALA A C   1 
ATOM   378  O  O   . ALA A 1 73  ? 15.867 21.563 11.617  1.00 7.64  ? 51  ALA A O   1 
ATOM   379  C  CB  . ALA A 1 73  ? 16.772 21.593 14.814  1.00 7.85  ? 51  ALA A CB  1 
ATOM   380  N  N   . VAL A 1 74  ? 15.748 23.571 12.651  1.00 7.31  ? 52  VAL A N   1 
ATOM   381  C  CA  . VAL A 1 74  ? 15.892 24.372 11.438  1.00 7.21  ? 52  VAL A CA  1 
ATOM   382  C  C   . VAL A 1 74  ? 17.047 25.362 11.578  1.00 7.03  ? 52  VAL A C   1 
ATOM   383  O  O   . VAL A 1 74  ? 17.123 26.113 12.553  1.00 7.22  ? 52  VAL A O   1 
ATOM   384  C  CB  . VAL A 1 74  ? 14.606 25.174 11.126  1.00 7.27  ? 52  VAL A CB  1 
ATOM   385  C  CG1 . VAL A 1 74  ? 14.757 25.946 9.821   1.00 7.32  ? 52  VAL A CG1 1 
ATOM   386  C  CG2 . VAL A 1 74  ? 13.394 24.256 11.074  1.00 7.34  ? 52  VAL A CG2 1 
ATOM   387  N  N   . ILE A 1 75  ? 17.940 25.350 10.594  1.00 6.73  ? 53  ILE A N   1 
ATOM   388  C  CA  . ILE A 1 75  ? 19.006 26.333 10.470  1.00 6.58  ? 53  ILE A CA  1 
ATOM   389  C  C   . ILE A 1 75  ? 18.622 27.313 9.367   1.00 6.49  ? 53  ILE A C   1 
ATOM   390  O  O   . ILE A 1 75  ? 18.197 26.898 8.282   1.00 6.38  ? 53  ILE A O   1 
ATOM   391  C  CB  . ILE A 1 75  ? 20.338 25.659 10.075  1.00 6.53  ? 53  ILE A CB  1 
ATOM   392  C  CG1 . ILE A 1 75  ? 20.787 24.690 11.173  1.00 6.64  ? 53  ILE A CG1 1 
ATOM   393  C  CG2 . ILE A 1 75  ? 21.407 26.710 9.787   1.00 6.53  ? 53  ILE A CG2 1 
ATOM   394  C  CD1 . ILE A 1 75  ? 21.903 23.769 10.741  1.00 6.66  ? 53  ILE A CD1 1 
ATOM   395  N  N   . VAL A 1 76  ? 18.773 28.606 9.644   1.00 6.46  ? 54  VAL A N   1 
ATOM   396  C  CA  . VAL A 1 76  ? 18.620 29.639 8.623   1.00 6.55  ? 54  VAL A CA  1 
ATOM   397  C  C   . VAL A 1 76  ? 19.940 30.402 8.497   1.00 6.68  ? 54  VAL A C   1 
ATOM   398  O  O   . VAL A 1 76  ? 20.572 30.759 9.490   1.00 6.47  ? 54  VAL A O   1 
ATOM   399  C  CB  . VAL A 1 76  ? 17.398 30.561 8.881   1.00 6.56  ? 54  VAL A CB  1 
ATOM   400  C  CG1 . VAL A 1 76  ? 17.518 31.314 10.195  1.00 6.57  ? 54  VAL A CG1 1 
ATOM   401  C  CG2 . VAL A 1 76  ? 17.189 31.533 7.720   1.00 6.60  ? 54  VAL A CG2 1 
ATOM   402  N  N   . ARG A 1 77  ? 20.353 30.612 7.253   1.00 6.90  ? 55  ARG A N   1 
ATOM   403  C  CA  . ARG A 1 77  ? 21.608 31.273 6.929   1.00 7.14  ? 55  ARG A CA  1 
ATOM   404  C  C   . ARG A 1 77  ? 21.436 31.988 5.600   1.00 7.08  ? 55  ARG A C   1 
ATOM   405  O  O   . ARG A 1 77  ? 20.473 31.738 4.875   1.00 6.99  ? 55  ARG A O   1 
ATOM   406  C  CB  . ARG A 1 77  ? 22.734 30.246 6.802   1.00 7.45  ? 55  ARG A CB  1 
ATOM   407  C  CG  . ARG A 1 77  ? 22.542 29.313 5.615   1.00 7.82  ? 55  ARG A CG  1 
ATOM   408  C  CD  . ARG A 1 77  ? 23.621 28.259 5.477   1.00 8.36  ? 55  ARG A CD  1 
ATOM   409  N  NE  . ARG A 1 77  ? 23.408 27.502 4.248   1.00 8.87  ? 55  ARG A NE  1 
ATOM   410  C  CZ  . ARG A 1 77  ? 24.232 26.569 3.780   1.00 9.54  ? 55  ARG A CZ  1 
ATOM   411  N  NH1 . ARG A 1 77  ? 25.325 26.239 4.453   1.00 9.67  ? 55  ARG A NH1 1 
ATOM   412  N  NH2 . ARG A 1 77  ? 23.947 25.956 2.640   1.00 10.02 ? 55  ARG A NH2 1 
ATOM   413  N  N   . GLY A 1 78  ? 22.378 32.863 5.275   1.00 7.21  ? 56  GLY A N   1 
ATOM   414  C  CA  . GLY A 1 78  ? 22.408 33.478 3.957   1.00 7.33  ? 56  GLY A CA  1 
ATOM   415  C  C   . GLY A 1 78  ? 23.342 32.759 3.002   1.00 7.55  ? 56  GLY A C   1 
ATOM   416  O  O   . GLY A 1 78  ? 24.227 32.010 3.418   1.00 7.79  ? 56  GLY A O   1 
ATOM   417  N  N   . ALA A 1 79  ? 23.137 32.997 1.711   1.00 7.81  ? 57  ALA A N   1 
ATOM   418  C  CA  . ALA A 1 79  ? 24.045 32.509 0.680   1.00 8.05  ? 57  ALA A CA  1 
ATOM   419  C  C   . ALA A 1 79  ? 25.366 33.263 0.756   1.00 8.34  ? 57  ALA A C   1 
ATOM   420  O  O   . ALA A 1 79  ? 25.401 34.472 1.001   1.00 8.28  ? 57  ALA A O   1 
ATOM   421  C  CB  . ALA A 1 79  ? 23.422 32.685 -0.694  1.00 8.03  ? 57  ALA A CB  1 
ATOM   422  N  N   . GLY A 1 80  ? 26.462 32.539 0.548   1.00 8.89  ? 58  GLY A N   1 
ATOM   423  C  CA  . GLY A 1 80  ? 27.780 33.153 0.532   1.00 9.31  ? 58  GLY A CA  1 
ATOM   424  C  C   . GLY A 1 80  ? 28.207 33.647 1.902   1.00 9.79  ? 58  GLY A C   1 
ATOM   425  O  O   . GLY A 1 80  ? 28.050 32.935 2.890   1.00 10.23 ? 58  GLY A O   1 
ATOM   426  N  N   . ASN A 1 81  ? 28.767 34.853 1.972   1.00 10.17 ? 59  ASN A N   1 
ATOM   427  C  CA  . ASN A 1 81  ? 29.219 35.398 3.252   1.00 10.25 ? 59  ASN A CA  1 
ATOM   428  C  C   . ASN A 1 81  ? 28.422 36.600 3.737   1.00 9.48  ? 59  ASN A C   1 
ATOM   429  O  O   . ASN A 1 81  ? 28.965 37.511 4.364   1.00 9.49  ? 59  ASN A O   1 
ATOM   430  C  CB  . ASN A 1 81  ? 30.731 35.663 3.250   1.00 11.20 ? 59  ASN A CB  1 
ATOM   431  C  CG  . ASN A 1 81  ? 31.161 36.725 2.261   1.00 11.93 ? 59  ASN A CG  1 
ATOM   432  O  OD1 . ASN A 1 81  ? 30.348 37.439 1.665   1.00 12.60 ? 59  ASN A OD1 1 
ATOM   433  N  ND2 . ASN A 1 81  ? 32.478 36.837 2.080   1.00 12.88 ? 59  ASN A ND2 1 
ATOM   434  N  N   . ALA A 1 82  ? 27.123 36.574 3.458   1.00 8.77  ? 60  ALA A N   1 
ATOM   435  C  CA  . ALA A 1 82  ? 26.182 37.523 4.041   1.00 8.33  ? 60  ALA A CA  1 
ATOM   436  C  C   . ALA A 1 82  ? 24.965 36.756 4.519   1.00 8.01  ? 60  ALA A C   1 
ATOM   437  O  O   . ALA A 1 82  ? 24.579 35.764 3.906   1.00 8.11  ? 60  ALA A O   1 
ATOM   438  C  CB  . ALA A 1 82  ? 25.761 38.569 3.025   1.00 8.30  ? 60  ALA A CB  1 
ATOM   439  N  N   . PHE A 1 83  ? 24.370 37.211 5.620   1.00 7.62  ? 61  PHE A N   1 
ATOM   440  C  CA  . PHE A 1 83  ? 23.080 36.699 6.050   1.00 7.42  ? 61  PHE A CA  1 
ATOM   441  C  C   . PHE A 1 83  ? 22.018 37.409 5.215   1.00 7.57  ? 61  PHE A C   1 
ATOM   442  O  O   . PHE A 1 83  ? 21.487 36.825 4.275   1.00 7.46  ? 61  PHE A O   1 
ATOM   443  C  CB  . PHE A 1 83  ? 22.892 36.898 7.559   1.00 7.18  ? 61  PHE A CB  1 
ATOM   444  C  CG  . PHE A 1 83  ? 21.644 36.272 8.106   1.00 6.97  ? 61  PHE A CG  1 
ATOM   445  C  CD1 . PHE A 1 83  ? 21.606 34.915 8.388   1.00 6.87  ? 61  PHE A CD1 1 
ATOM   446  C  CD2 . PHE A 1 83  ? 20.509 37.040 8.350   1.00 6.85  ? 61  PHE A CD2 1 
ATOM   447  C  CE1 . PHE A 1 83  ? 20.462 34.330 8.895   1.00 6.84  ? 61  PHE A CE1 1 
ATOM   448  C  CE2 . PHE A 1 83  ? 19.362 36.458 8.860   1.00 6.81  ? 61  PHE A CE2 1 
ATOM   449  C  CZ  . PHE A 1 83  ? 19.339 35.105 9.136   1.00 6.80  ? 61  PHE A CZ  1 
ATOM   450  N  N   . SER A 1 84  ? 21.747 38.675 5.521   1.00 7.78  ? 62  SER A N   1 
ATOM   451  C  CA  . SER A 1 84  ? 20.836 39.487 4.714   1.00 8.03  ? 62  SER A CA  1 
ATOM   452  C  C   . SER A 1 84  ? 20.853 40.936 5.186   1.00 8.40  ? 62  SER A C   1 
ATOM   453  O  O   . SER A 1 84  ? 20.989 41.200 6.377   1.00 8.32  ? 62  SER A O   1 
ATOM   454  C  CB  . SER A 1 84  ? 19.402 38.937 4.765   1.00 8.01  ? 62  SER A CB  1 
ATOM   455  O  OG  . SER A 1 84  ? 18.479 39.816 4.131   1.00 8.05  ? 62  SER A OG  1 
ATOM   456  N  N   . SER A 1 85  ? 20.704 41.866 4.244   1.00 9.03  ? 63  SER A N   1 
ATOM   457  C  CA  . SER A 1 85  ? 20.613 43.290 4.569   1.00 9.60  ? 63  SER A CA  1 
ATOM   458  C  C   . SER A 1 85  ? 19.197 43.699 5.000   1.00 10.04 ? 63  SER A C   1 
ATOM   459  O  O   . SER A 1 85  ? 18.980 44.848 5.392   1.00 10.15 ? 63  SER A O   1 
ATOM   460  C  CB  . SER A 1 85  ? 21.054 44.129 3.369   1.00 9.81  ? 63  SER A CB  1 
ATOM   461  O  OG  . SER A 1 85  ? 20.234 43.854 2.253   1.00 10.06 ? 63  SER A OG  1 
ATOM   462  N  N   . GLY A 1 86  ? 18.245 42.767 4.924   1.00 10.71 ? 64  GLY A N   1 
ATOM   463  C  CA  . GLY A 1 86  ? 16.871 43.002 5.366   1.00 11.52 ? 64  GLY A CA  1 
ATOM   464  C  C   . GLY A 1 86  ? 15.893 43.088 4.211   1.00 12.37 ? 64  GLY A C   1 
ATOM   465  O  O   . GLY A 1 86  ? 16.180 42.629 3.102   1.00 12.69 ? 64  GLY A O   1 
ATOM   466  N  N   . PHE A 1 87  ? 14.730 43.676 4.470   1.00 13.18 ? 65  PHE A N   1 
ATOM   467  C  CA  . PHE A 1 87  ? 13.680 43.756 3.459   1.00 13.83 ? 65  PHE A CA  1 
ATOM   468  C  C   . PHE A 1 87  ? 14.199 44.593 2.277   1.00 14.32 ? 65  PHE A C   1 
ATOM   469  O  O   . PHE A 1 87  ? 14.936 45.562 2.468   1.00 14.39 ? 65  PHE A O   1 
ATOM   470  C  CB  . PHE A 1 87  ? 12.363 44.311 4.047   1.00 13.85 ? 65  PHE A CB  1 
ATOM   471  C  CG  . PHE A 1 87  ? 11.835 43.526 5.233   1.00 13.96 ? 65  PHE A CG  1 
ATOM   472  C  CD1 . PHE A 1 87  ? 11.729 42.141 5.187   1.00 14.06 ? 65  PHE A CD1 1 
ATOM   473  C  CD2 . PHE A 1 87  ? 11.428 44.179 6.395   1.00 14.09 ? 65  PHE A CD2 1 
ATOM   474  C  CE1 . PHE A 1 87  ? 11.247 41.422 6.272   1.00 14.39 ? 65  PHE A CE1 1 
ATOM   475  C  CE2 . PHE A 1 87  ? 10.943 43.468 7.482   1.00 14.31 ? 65  PHE A CE2 1 
ATOM   476  C  CZ  . PHE A 1 87  ? 10.856 42.085 7.423   1.00 14.33 ? 65  PHE A CZ  1 
ATOM   477  N  N   . ASP A 1 88  ? 13.836 44.183 1.062   1.00 15.24 ? 66  ASP A N   1 
ATOM   478  C  CA  . ASP A 1 88  ? 14.446 44.686 -0.181  1.00 15.86 ? 66  ASP A CA  1 
ATOM   479  C  C   . ASP A 1 88  ? 14.024 46.119 -0.514  1.00 16.84 ? 66  ASP A C   1 
ATOM   480  O  O   . ASP A 1 88  ? 12.877 46.360 -0.881  1.00 16.51 ? 66  ASP A O   1 
ATOM   481  C  CB  . ASP A 1 88  ? 14.066 43.740 -1.332  1.00 15.81 ? 66  ASP A CB  1 
ATOM   482  C  CG  . ASP A 1 88  ? 14.871 43.976 -2.608  1.00 15.74 ? 66  ASP A CG  1 
ATOM   483  O  OD1 . ASP A 1 88  ? 15.386 45.088 -2.841  1.00 15.65 ? 66  ASP A OD1 1 
ATOM   484  O  OD2 . ASP A 1 88  ? 14.967 43.020 -3.403  1.00 15.67 ? 66  ASP A OD2 1 
ATOM   485  N  N   . LEU A 1 89  ? 14.963 47.059 -0.399  1.00 17.80 ? 67  LEU A N   1 
ATOM   486  C  CA  . LEU A 1 89  ? 14.670 48.482 -0.621  1.00 18.90 ? 67  LEU A CA  1 
ATOM   487  C  C   . LEU A 1 89  ? 14.608 48.849 -2.100  1.00 18.96 ? 67  LEU A C   1 
ATOM   488  O  O   . LEU A 1 89  ? 13.893 49.779 -2.471  1.00 19.39 ? 67  LEU A O   1 
ATOM   489  C  CB  . LEU A 1 89  ? 15.698 49.372 0.078   1.00 19.56 ? 67  LEU A CB  1 
ATOM   490  C  CG  . LEU A 1 89  ? 15.717 49.375 1.608   1.00 19.94 ? 67  LEU A CG  1 
ATOM   491  C  CD1 . LEU A 1 89  ? 16.576 50.532 2.097   1.00 20.28 ? 67  LEU A CD1 1 
ATOM   492  C  CD2 . LEU A 1 89  ? 14.319 49.461 2.206   1.00 20.07 ? 67  LEU A CD2 1 
ATOM   493  N  N   . LYS A 1 90  ? 15.357 48.135 -2.939  1.00 18.96 ? 68  LYS A N   1 
ATOM   494  C  CA  . LYS A 1 90  ? 15.295 48.359 -4.381  1.00 18.76 ? 68  LYS A CA  1 
ATOM   495  C  C   . LYS A 1 90  ? 13.912 47.965 -4.901  1.00 18.06 ? 68  LYS A C   1 
ATOM   496  O  O   . LYS A 1 90  ? 13.341 48.655 -5.743  1.00 18.19 ? 68  LYS A O   1 
ATOM   497  C  CB  . LYS A 1 90  ? 16.394 47.587 -5.118  1.00 19.55 ? 68  LYS A CB  1 
ATOM   498  C  CG  . LYS A 1 90  ? 16.365 47.790 -6.626  1.00 19.99 ? 68  LYS A CG  1 
ATOM   499  C  CD  . LYS A 1 90  ? 17.646 47.311 -7.292  1.00 20.55 ? 68  LYS A CD  1 
ATOM   500  C  CE  . LYS A 1 90  ? 17.576 47.506 -8.796  1.00 20.73 ? 68  LYS A CE  1 
ATOM   501  N  NZ  . LYS A 1 90  ? 18.770 46.939 -9.483  1.00 21.10 ? 68  LYS A NZ  1 
ATOM   502  N  N   . ALA A 1 91  ? 13.375 46.864 -4.381  1.00 17.25 ? 69  ALA A N   1 
ATOM   503  C  CA  . ALA A 1 91  ? 12.013 46.444 -4.696  1.00 16.76 ? 69  ALA A CA  1 
ATOM   504  C  C   . ALA A 1 91  ? 11.000 47.478 -4.198  1.00 16.65 ? 69  ALA A C   1 
ATOM   505  O  O   . ALA A 1 91  ? 10.016 47.769 -4.875  1.00 16.02 ? 69  ALA A O   1 
ATOM   506  C  CB  . ALA A 1 91  ? 11.728 45.074 -4.097  1.00 16.60 ? 69  ALA A CB  1 
ATOM   507  N  N   . GLN A 1 92  ? 11.251 48.043 -3.019  1.00 16.48 ? 70  GLN A N   1 
ATOM   508  C  CA  . GLN A 1 92  ? 10.379 49.088 -2.477  1.00 16.78 ? 70  GLN A CA  1 
ATOM   509  C  C   . GLN A 1 92  ? 10.428 50.363 -3.327  1.00 17.64 ? 70  GLN A C   1 
ATOM   510  O  O   . GLN A 1 92  ? 9.395  50.997 -3.559  1.00 17.48 ? 70  GLN A O   1 
ATOM   511  C  CB  . GLN A 1 92  ? 10.757 49.407 -1.028  1.00 16.19 ? 70  GLN A CB  1 
ATOM   512  C  CG  . GLN A 1 92  ? 9.767  50.338 -0.345  1.00 15.70 ? 70  GLN A CG  1 
ATOM   513  C  CD  . GLN A 1 92  ? 10.130 50.659 1.091   1.00 15.02 ? 70  GLN A CD  1 
ATOM   514  O  OE1 . GLN A 1 92  ? 10.734 49.848 1.807   1.00 15.61 ? 70  GLN A OE1 1 
ATOM   515  N  NE2 . GLN A 1 92  ? 9.759  51.844 1.522   1.00 13.99 ? 70  GLN A NE2 1 
HETATM 516  N  N   . MSE A 1 93  ? 11.624 50.729 -3.787  1.00 19.08 ? 71  MSE A N   1 
HETATM 517  C  CA  . MSE A 1 93  ? 11.810 51.897 -4.665  1.00 20.71 ? 71  MSE A CA  1 
HETATM 518  C  C   . MSE A 1 93  ? 10.972 51.769 -5.908  1.00 20.08 ? 71  MSE A C   1 
HETATM 519  O  O   . MSE A 1 93  ? 10.362 52.740 -6.358  1.00 19.61 ? 71  MSE A O   1 
HETATM 520  C  CB  . MSE A 1 93  ? 13.273 52.033 -5.092  1.00 23.15 ? 71  MSE A CB  1 
HETATM 521  C  CG  . MSE A 1 93  ? 13.519 53.251 -5.986  1.00 25.64 ? 71  MSE A CG  1 
HETATM 522  SE SE  . MSE A 1 93  ? 15.409 53.350 -6.537  1.00 31.87 ? 71  MSE A SE  1 
HETATM 523  C  CE  . MSE A 1 93  ? 15.431 51.773 -7.719  1.00 30.11 ? 71  MSE A CE  1 
ATOM   524  N  N   . GLU A 1 94  ? 10.944 50.568 -6.476  1.00 19.45 ? 72  GLU A N   1 
ATOM   525  C  CA  . GLU A 1 94  ? 10.225 50.317 -7.725  1.00 19.60 ? 72  GLU A CA  1 
ATOM   526  C  C   . GLU A 1 94  ? 8.714  50.184 -7.525  1.00 18.99 ? 72  GLU A C   1 
ATOM   527  O  O   . GLU A 1 94  ? 7.936  50.673 -8.345  1.00 18.80 ? 72  GLU A O   1 
ATOM   528  C  CB  . GLU A 1 94  ? 10.793 49.070 -8.409  1.00 20.48 ? 72  GLU A CB  1 
ATOM   529  C  CG  . GLU A 1 94  ? 12.227 49.272 -8.880  1.00 21.50 ? 72  GLU A CG  1 
ATOM   530  C  CD  . GLU A 1 94  ? 12.914 47.998 -9.336  1.00 22.52 ? 72  GLU A CD  1 
ATOM   531  O  OE1 . GLU A 1 94  ? 12.347 46.894 -9.176  1.00 23.93 ? 72  GLU A OE1 1 
ATOM   532  O  OE2 . GLU A 1 94  ? 14.043 48.107 -9.853  1.00 24.25 ? 72  GLU A OE2 1 
ATOM   533  N  N   . ALA A 1 95  ? 8.305  49.533 -6.436  1.00 18.28 ? 73  ALA A N   1 
ATOM   534  C  CA  . ALA A 1 95  ? 6.888  49.260 -6.175  1.00 17.89 ? 73  ALA A CA  1 
ATOM   535  C  C   . ALA A 1 95  ? 6.117  50.508 -5.745  1.00 17.61 ? 73  ALA A C   1 
ATOM   536  O  O   . ALA A 1 95  ? 4.940  50.655 -6.077  1.00 17.45 ? 73  ALA A O   1 
ATOM   537  C  CB  . ALA A 1 95  ? 6.743  48.167 -5.126  1.00 17.79 ? 73  ALA A CB  1 
ATOM   538  N  N   . ARG A 1 96  ? 6.783  51.385 -5.001  1.00 17.25 ? 74  ARG A N   1 
ATOM   539  C  CA  . ARG A 1 96  ? 6.199  52.643 -4.530  1.00 17.18 ? 74  ARG A CA  1 
ATOM   540  C  C   . ARG A 1 96  ? 4.841  52.464 -3.849  1.00 15.98 ? 74  ARG A C   1 
ATOM   541  O  O   . ARG A 1 96  ? 3.860  53.092 -4.243  1.00 15.94 ? 74  ARG A O   1 
ATOM   542  C  CB  . ARG A 1 96  ? 6.092  53.644 -5.684  1.00 18.55 ? 74  ARG A CB  1 
ATOM   543  C  CG  . ARG A 1 96  ? 7.429  53.957 -6.327  1.00 19.73 ? 74  ARG A CG  1 
ATOM   544  C  CD  . ARG A 1 96  ? 7.363  55.171 -7.236  1.00 20.91 ? 74  ARG A CD  1 
ATOM   545  N  NE  . ARG A 1 96  ? 7.116  56.408 -6.501  1.00 22.06 ? 74  ARG A NE  1 
ATOM   546  C  CZ  . ARG A 1 96  ? 7.223  57.629 -7.024  1.00 23.18 ? 74  ARG A CZ  1 
ATOM   547  N  NH1 . ARG A 1 96  ? 7.591  57.793 -8.290  1.00 23.99 ? 74  ARG A NH1 1 
ATOM   548  N  NH2 . ARG A 1 96  ? 6.976  58.694 -6.270  1.00 23.84 ? 74  ARG A NH2 1 
ATOM   549  N  N   . PRO A 1 97  ? 4.780  51.604 -2.818  1.00 14.66 ? 75  PRO A N   1 
ATOM   550  C  CA  . PRO A 1 97  ? 3.534  51.465 -2.072  1.00 13.87 ? 75  PRO A CA  1 
ATOM   551  C  C   . PRO A 1 97  ? 3.170  52.786 -1.411  1.00 13.03 ? 75  PRO A C   1 
ATOM   552  O  O   . PRO A 1 97  ? 4.043  53.462 -0.866  1.00 13.49 ? 75  PRO A O   1 
ATOM   553  C  CB  . PRO A 1 97  ? 3.868  50.405 -1.015  1.00 14.07 ? 75  PRO A CB  1 
ATOM   554  C  CG  . PRO A 1 97  ? 5.341  50.480 -0.854  1.00 14.42 ? 75  PRO A CG  1 
ATOM   555  C  CD  . PRO A 1 97  ? 5.885  50.854 -2.197  1.00 14.51 ? 75  PRO A CD  1 
ATOM   556  N  N   . ALA A 1 98  ? 1.896  53.149 -1.474  1.00 12.11 ? 76  ALA A N   1 
ATOM   557  C  CA  . ALA A 1 98  ? 1.436  54.431 -0.965  1.00 11.52 ? 76  ALA A CA  1 
ATOM   558  C  C   . ALA A 1 98  ? 0.164  54.255 -0.151  1.00 10.74 ? 76  ALA A C   1 
ATOM   559  O  O   . ALA A 1 98  ? -0.846 53.777 -0.667  1.00 10.89 ? 76  ALA A O   1 
ATOM   560  C  CB  . ALA A 1 98  ? 1.188  55.388 -2.120  1.00 11.71 ? 76  ALA A CB  1 
ATOM   561  N  N   . GLY A 1 99  ? 0.227  54.644 1.119   1.00 9.88  ? 77  GLY A N   1 
ATOM   562  C  CA  . GLY A 1 99  ? -0.953 54.709 1.970   1.00 9.25  ? 77  GLY A CA  1 
ATOM   563  C  C   . GLY A 1 99  ? -1.102 53.504 2.872   1.00 8.72  ? 77  GLY A C   1 
ATOM   564  O  O   . GLY A 1 99  ? -0.454 52.474 2.676   1.00 8.61  ? 77  GLY A O   1 
ATOM   565  N  N   . VAL A 1 100 ? -1.997 53.637 3.842   1.00 8.23  ? 78  VAL A N   1 
ATOM   566  C  CA  . VAL A 1 100 ? -2.208 52.616 4.868   1.00 8.08  ? 78  VAL A CA  1 
ATOM   567  C  C   . VAL A 1 100 ? -2.641 51.277 4.277   1.00 8.14  ? 78  VAL A C   1 
ATOM   568  O  O   . VAL A 1 100 ? -2.103 50.234 4.633   1.00 7.94  ? 78  VAL A O   1 
ATOM   569  C  CB  . VAL A 1 100 ? -3.252 53.093 5.910   1.00 7.96  ? 78  VAL A CB  1 
ATOM   570  C  CG1 . VAL A 1 100 ? -3.701 51.948 6.810   1.00 7.98  ? 78  VAL A CG1 1 
ATOM   571  C  CG2 . VAL A 1 100 ? -2.679 54.228 6.747   1.00 8.02  ? 78  VAL A CG2 1 
ATOM   572  N  N   . ASP A 1 101 ? -3.620 51.291 3.381   1.00 8.31  ? 79  ASP A N   1 
ATOM   573  C  CA  . ASP A 1 101 ? -4.158 50.037 2.872   1.00 8.51  ? 79  ASP A CA  1 
ATOM   574  C  C   . ASP A 1 101 ? -3.146 49.248 2.028   1.00 8.32  ? 79  ASP A C   1 
ATOM   575  O  O   . ASP A 1 101 ? -3.168 48.021 2.033   1.00 8.24  ? 79  ASP A O   1 
ATOM   576  C  CB  . ASP A 1 101 ? -5.469 50.279 2.112   1.00 8.89  ? 79  ASP A CB  1 
ATOM   577  C  CG  . ASP A 1 101 ? -6.614 50.685 3.034   1.00 9.31  ? 79  ASP A CG  1 
ATOM   578  O  OD1 . ASP A 1 101 ? -6.534 50.473 4.265   1.00 9.72  ? 79  ASP A OD1 1 
ATOM   579  O  OD2 . ASP A 1 101 ? -7.622 51.210 2.528   1.00 10.03 ? 79  ASP A OD2 1 
ATOM   580  N  N   . ALA A 1 102 ? -2.252 49.950 1.336   1.00 8.14  ? 80  ALA A N   1 
ATOM   581  C  CA  . ALA A 1 102 ? -1.181 49.299 0.576   1.00 8.16  ? 80  ALA A CA  1 
ATOM   582  C  C   . ALA A 1 102 ? -0.120 48.725 1.511   1.00 8.06  ? 80  ALA A C   1 
ATOM   583  O  O   . ALA A 1 102 ? 0.388  47.624 1.293   1.00 8.32  ? 80  ALA A O   1 
ATOM   584  C  CB  . ALA A 1 102 ? -0.545 50.283 -0.394  1.00 8.30  ? 80  ALA A CB  1 
ATOM   585  N  N   . TRP A 1 103 ? 0.213  49.475 2.554   1.00 7.78  ? 81  TRP A N   1 
ATOM   586  C  CA  . TRP A 1 103 ? 1.249  49.044 3.493   1.00 7.65  ? 81  TRP A CA  1 
ATOM   587  C  C   . TRP A 1 103 ? 0.813  47.920 4.435   1.00 7.58  ? 81  TRP A C   1 
ATOM   588  O  O   . TRP A 1 103 ? 1.639  47.091 4.823   1.00 7.56  ? 81  TRP A O   1 
ATOM   589  C  CB  . TRP A 1 103 ? 1.789  50.233 4.289   1.00 7.70  ? 81  TRP A CB  1 
ATOM   590  C  CG  . TRP A 1 103 ? 2.912  50.917 3.579   1.00 7.73  ? 81  TRP A CG  1 
ATOM   591  C  CD1 . TRP A 1 103 ? 2.834  52.016 2.769   1.00 7.82  ? 81  TRP A CD1 1 
ATOM   592  C  CD2 . TRP A 1 103 ? 4.288  50.531 3.603   1.00 7.82  ? 81  TRP A CD2 1 
ATOM   593  N  NE1 . TRP A 1 103 ? 4.083  52.342 2.296   1.00 7.89  ? 81  TRP A NE1 1 
ATOM   594  C  CE2 . TRP A 1 103 ? 4.993  51.448 2.797   1.00 7.88  ? 81  TRP A CE2 1 
ATOM   595  C  CE3 . TRP A 1 103 ? 4.998  49.508 4.247   1.00 7.89  ? 81  TRP A CE3 1 
ATOM   596  C  CZ2 . TRP A 1 103 ? 6.369  51.366 2.608   1.00 7.92  ? 81  TRP A CZ2 1 
ATOM   597  C  CZ3 . TRP A 1 103 ? 6.374  49.434 4.060   1.00 7.97  ? 81  TRP A CZ3 1 
ATOM   598  C  CH2 . TRP A 1 103 ? 7.038  50.353 3.245   1.00 8.01  ? 81  TRP A CH2 1 
ATOM   599  N  N   . ARG A 1 104 ? -0.466 47.865 4.792   1.00 7.50  ? 82  ARG A N   1 
ATOM   600  C  CA  . ARG A 1 104 ? -0.917 46.865 5.770   1.00 7.59  ? 82  ARG A CA  1 
ATOM   601  C  C   . ARG A 1 104 ? -0.492 45.424 5.434   1.00 7.60  ? 82  ARG A C   1 
ATOM   602  O  O   . ARG A 1 104 ? 0.117  44.768 6.279   1.00 7.37  ? 82  ARG A O   1 
ATOM   603  C  CB  . ARG A 1 104 ? -2.432 46.944 6.013   1.00 7.72  ? 82  ARG A CB  1 
ATOM   604  C  CG  . ARG A 1 104 ? -2.882 46.032 7.150   1.00 7.88  ? 82  ARG A CG  1 
ATOM   605  C  CD  . ARG A 1 104 ? -4.381 46.047 7.371   1.00 8.06  ? 82  ARG A CD  1 
ATOM   606  N  NE  . ARG A 1 104 ? -4.832 47.229 8.104   1.00 8.26  ? 82  ARG A NE  1 
ATOM   607  C  CZ  . ARG A 1 104 ? -5.414 48.295 7.559   1.00 8.41  ? 82  ARG A CZ  1 
ATOM   608  N  NH1 . ARG A 1 104 ? -5.631 48.375 6.243   1.00 8.64  ? 82  ARG A NH1 1 
ATOM   609  N  NH2 . ARG A 1 104 ? -5.786 49.299 8.342   1.00 8.51  ? 82  ARG A NH2 1 
ATOM   610  N  N   . PRO A 1 105 ? -0.805 44.922 4.222   1.00 7.67  ? 83  PRO A N   1 
ATOM   611  C  CA  . PRO A 1 105 ? -0.415 43.533 3.918   1.00 7.82  ? 83  PRO A CA  1 
ATOM   612  C  C   . PRO A 1 105 ? 1.090  43.309 3.805   1.00 7.94  ? 83  PRO A C   1 
ATOM   613  O  O   . PRO A 1 105 ? 1.572  42.209 4.085   1.00 8.11  ? 83  PRO A O   1 
ATOM   614  C  CB  . PRO A 1 105 ? -1.096 43.257 2.573   1.00 7.85  ? 83  PRO A CB  1 
ATOM   615  C  CG  . PRO A 1 105 ? -1.324 44.600 1.979   1.00 7.85  ? 83  PRO A CG  1 
ATOM   616  C  CD  . PRO A 1 105 ? -1.612 45.505 3.134   1.00 7.78  ? 83  PRO A CD  1 
ATOM   617  N  N   . LEU A 1 106 ? 1.823  44.333 3.383   1.00 7.93  ? 84  LEU A N   1 
ATOM   618  C  CA  . LEU A 1 106 ? 3.276  44.238 3.283   1.00 8.10  ? 84  LEU A CA  1 
ATOM   619  C  C   . LEU A 1 106 ? 3.888  44.013 4.657   1.00 7.99  ? 84  LEU A C   1 
ATOM   620  O  O   . LEU A 1 106 ? 4.692  43.100 4.849   1.00 7.94  ? 84  LEU A O   1 
ATOM   621  C  CB  . LEU A 1 106 ? 3.850  45.510 2.664   1.00 8.25  ? 84  LEU A CB  1 
ATOM   622  C  CG  . LEU A 1 106 ? 3.482  45.752 1.198   1.00 8.54  ? 84  LEU A CG  1 
ATOM   623  C  CD1 . LEU A 1 106 ? 3.929  47.132 0.753   1.00 8.64  ? 84  LEU A CD1 1 
ATOM   624  C  CD2 . LEU A 1 106 ? 4.067  44.674 0.301   1.00 8.74  ? 84  LEU A CD2 1 
ATOM   625  N  N   . LEU A 1 107 ? 3.483  44.844 5.608   1.00 7.86  ? 85  LEU A N   1 
ATOM   626  C  CA  . LEU A 1 107 ? 3.983  44.752 6.981   1.00 7.87  ? 85  LEU A CA  1 
ATOM   627  C  C   . LEU A 1 107 ? 3.504  43.478 7.684   1.00 8.02  ? 85  LEU A C   1 
ATOM   628  O  O   . LEU A 1 107 ? 4.240  42.893 8.470   1.00 7.82  ? 85  LEU A O   1 
ATOM   629  C  CB  . LEU A 1 107 ? 3.560  45.981 7.788   1.00 7.84  ? 85  LEU A CB  1 
ATOM   630  C  CG  . LEU A 1 107 ? 4.075  47.334 7.289   1.00 7.91  ? 85  LEU A CG  1 
ATOM   631  C  CD1 . LEU A 1 107 ? 3.585  48.473 8.179   1.00 7.95  ? 85  LEU A CD1 1 
ATOM   632  C  CD2 . LEU A 1 107 ? 5.591  47.341 7.216   1.00 7.95  ? 85  LEU A CD2 1 
ATOM   633  N  N   . ARG A 1 108 ? 2.277  43.055 7.397   1.00 8.41  ? 86  ARG A N   1 
ATOM   634  C  CA  . ARG A 1 108 ? 1.727  41.824 7.971   1.00 8.82  ? 86  ARG A CA  1 
ATOM   635  C  C   . ARG A 1 108 ? 2.555  40.607 7.566   1.00 8.99  ? 86  ARG A C   1 
ATOM   636  O  O   . ARG A 1 108 ? 2.843  39.731 8.384   1.00 8.55  ? 86  ARG A O   1 
ATOM   637  C  CB  . ARG A 1 108 ? 0.282  41.635 7.500   1.00 9.30  ? 86  ARG A CB  1 
ATOM   638  C  CG  . ARG A 1 108 ? -0.511 40.593 8.265   1.00 9.76  ? 86  ARG A CG  1 
ATOM   639  C  CD  . ARG A 1 108 ? -0.857 41.079 9.666   1.00 10.23 ? 86  ARG A CD  1 
ATOM   640  N  NE  . ARG A 1 108 ? -0.121 40.369 10.691  1.00 10.60 ? 86  ARG A NE  1 
ATOM   641  C  CZ  . ARG A 1 108 ? -0.162 40.665 11.988  1.00 10.77 ? 86  ARG A CZ  1 
ATOM   642  N  NH1 . ARG A 1 108 ? -0.886 41.685 12.443  1.00 10.73 ? 86  ARG A NH1 1 
ATOM   643  N  NH2 . ARG A 1 108 ? 0.539  39.936 12.836  1.00 11.26 ? 86  ARG A NH2 1 
ATOM   644  N  N   . LYS A 1 109 ? 2.929  40.558 6.293   1.00 9.21  ? 87  LYS A N   1 
ATOM   645  C  CA  . LYS A 1 109 ? 3.737  39.464 5.768   1.00 9.79  ? 87  LYS A CA  1 
ATOM   646  C  C   . LYS A 1 109 ? 5.165  39.521 6.317   1.00 9.38  ? 87  LYS A C   1 
ATOM   647  O  O   . LYS A 1 109 ? 5.730  38.486 6.685   1.00 9.13  ? 87  LYS A O   1 
ATOM   648  C  CB  . LYS A 1 109 ? 3.740  39.511 4.239   1.00 10.71 ? 87  LYS A CB  1 
ATOM   649  C  CG  . LYS A 1 109 ? 4.472  38.373 3.553   1.00 11.80 ? 87  LYS A CG  1 
ATOM   650  C  CD  . LYS A 1 109 ? 4.248  38.452 2.050   1.00 12.86 ? 87  LYS A CD  1 
ATOM   651  C  CE  . LYS A 1 109 ? 5.126  37.493 1.269   1.00 13.58 ? 87  LYS A CE  1 
ATOM   652  N  NZ  . LYS A 1 109 ? 4.607  37.217 -0.098  1.00 14.45 ? 87  LYS A NZ  1 
ATOM   653  N  N   . ASP A 1 110 ? 5.740  40.725 6.384   1.00 9.06  ? 88  ASP A N   1 
ATOM   654  C  CA  . ASP A 1 110 ? 7.064  40.915 6.995   1.00 9.12  ? 88  ASP A CA  1 
ATOM   655  C  C   . ASP A 1 110 ? 7.069  40.353 8.413   1.00 8.41  ? 88  ASP A C   1 
ATOM   656  O  O   . ASP A 1 110 ? 7.919  39.544 8.779   1.00 8.35  ? 88  ASP A O   1 
ATOM   657  C  CB  . ASP A 1 110 ? 7.427  42.401 7.101   1.00 9.95  ? 88  ASP A CB  1 
ATOM   658  C  CG  . ASP A 1 110 ? 7.749  43.055 5.768   1.00 10.85 ? 88  ASP A CG  1 
ATOM   659  O  OD1 . ASP A 1 110 ? 8.119  42.377 4.785   1.00 11.87 ? 88  ASP A OD1 1 
ATOM   660  O  OD2 . ASP A 1 110 ? 7.639  44.299 5.721   1.00 12.29 ? 88  ASP A OD2 1 
ATOM   661  N  N   . PHE A 1 111 ? 6.106  40.817 9.205   1.00 7.73  ? 89  PHE A N   1 
ATOM   662  C  CA  . PHE A 1 111 ? 6.010  40.494 10.628  1.00 7.28  ? 89  PHE A CA  1 
ATOM   663  C  C   . PHE A 1 111 ? 5.762  39.008 10.833  1.00 7.15  ? 89  PHE A C   1 
ATOM   664  O  O   . PHE A 1 111 ? 6.461  38.355 11.605  1.00 6.87  ? 89  PHE A O   1 
ATOM   665  C  CB  . PHE A 1 111 ? 4.870  41.312 11.250  1.00 7.10  ? 89  PHE A CB  1 
ATOM   666  C  CG  . PHE A 1 111 ? 4.661  41.077 12.719  1.00 7.02  ? 89  PHE A CG  1 
ATOM   667  C  CD1 . PHE A 1 111 ? 3.872  40.033 13.163  1.00 6.95  ? 89  PHE A CD1 1 
ATOM   668  C  CD2 . PHE A 1 111 ? 5.220  41.929 13.659  1.00 6.92  ? 89  PHE A CD2 1 
ATOM   669  C  CE1 . PHE A 1 111 ? 3.662  39.827 14.515  1.00 6.99  ? 89  PHE A CE1 1 
ATOM   670  C  CE2 . PHE A 1 111 ? 5.012  41.731 15.016  1.00 6.96  ? 89  PHE A CE2 1 
ATOM   671  C  CZ  . PHE A 1 111 ? 4.230  40.677 15.444  1.00 7.02  ? 89  PHE A CZ  1 
ATOM   672  N  N   . ASP A 1 112 ? 4.773  38.466 10.130  1.00 7.18  ? 90  ASP A N   1 
ATOM   673  C  CA  . ASP A 1 112 ? 4.402  37.067 10.336  1.00 7.34  ? 90  ASP A CA  1 
ATOM   674  C  C   . ASP A 1 112 ? 5.504  36.109 9.882   1.00 7.18  ? 90  ASP A C   1 
ATOM   675  O  O   . ASP A 1 112 ? 5.678  35.056 10.481  1.00 7.17  ? 90  ASP A O   1 
ATOM   676  C  CB  . ASP A 1 112 ? 3.077  36.733 9.644   1.00 7.67  ? 90  ASP A CB  1 
ATOM   677  C  CG  . ASP A 1 112 ? 1.860  37.307 10.373  1.00 7.98  ? 90  ASP A CG  1 
ATOM   678  O  OD1 . ASP A 1 112 ? 1.944  37.665 11.569  1.00 8.07  ? 90  ASP A OD1 1 
ATOM   679  O  OD2 . ASP A 1 112 ? 0.795  37.409 9.729   1.00 8.79  ? 90  ASP A OD2 1 
ATOM   680  N  N   . THR A 1 113 ? 6.251  36.476 8.842   1.00 7.09  ? 91  THR A N   1 
ATOM   681  C  CA  . THR A 1 113 ? 7.346  35.633 8.360   1.00 7.07  ? 91  THR A CA  1 
ATOM   682  C  C   . THR A 1 113 ? 8.480  35.590 9.383   1.00 6.97  ? 91  THR A C   1 
ATOM   683  O  O   . THR A 1 113 ? 8.997  34.524 9.703   1.00 6.99  ? 91  THR A O   1 
ATOM   684  C  CB  . THR A 1 113 ? 7.878  36.129 7.005   1.00 7.18  ? 91  THR A CB  1 
ATOM   685  O  OG1 . THR A 1 113 ? 6.796  36.171 6.071   1.00 7.42  ? 91  THR A OG1 1 
ATOM   686  C  CG2 . THR A 1 113 ? 8.969  35.198 6.466   1.00 7.21  ? 91  THR A CG2 1 
ATOM   687  N  N   . VAL A 1 114 ? 8.859  36.754 9.900   1.00 7.01  ? 92  VAL A N   1 
ATOM   688  C  CA  . VAL A 1 114 ? 9.857  36.818 10.971  1.00 7.13  ? 92  VAL A CA  1 
ATOM   689  C  C   . VAL A 1 114 ? 9.416  35.959 12.164  1.00 7.39  ? 92  VAL A C   1 
ATOM   690  O  O   . VAL A 1 114 ? 10.192 35.161 12.701  1.00 7.30  ? 92  VAL A O   1 
ATOM   691  C  CB  . VAL A 1 114 ? 10.106 38.283 11.403  1.00 7.10  ? 92  VAL A CB  1 
ATOM   692  C  CG1 . VAL A 1 114 ? 10.798 38.357 12.763  1.00 7.18  ? 92  VAL A CG1 1 
ATOM   693  C  CG2 . VAL A 1 114 ? 10.912 39.011 10.332  1.00 7.13  ? 92  VAL A CG2 1 
HETATM 694  N  N   . MSE A 1 115 ? 8.162  36.110 12.571  1.00 7.87  ? 93  MSE A N   1 
HETATM 695  C  CA  . MSE A 1 115 ? 7.677  35.415 13.761  1.00 8.56  ? 93  MSE A CA  1 
HETATM 696  C  C   . MSE A 1 115 ? 7.513  33.923 13.565  1.00 7.89  ? 93  MSE A C   1 
HETATM 697  O  O   . MSE A 1 115 ? 7.353  33.208 14.548  1.00 7.63  ? 93  MSE A O   1 
HETATM 698  C  CB  . MSE A 1 115 ? 6.403  36.090 14.276  1.00 9.97  ? 93  MSE A CB  1 
HETATM 699  C  CG  . MSE A 1 115 ? 6.678  37.502 14.815  1.00 11.50 ? 93  MSE A CG  1 
HETATM 700  SE SE  . MSE A 1 115 ? 8.007  37.585 16.279  1.00 16.08 ? 93  MSE A SE  1 
HETATM 701  C  CE  . MSE A 1 115 ? 6.953  36.679 17.672  1.00 14.37 ? 93  MSE A CE  1 
ATOM   702  N  N   . ARG A 1 116 ? 7.578  33.426 12.327  1.00 7.33  ? 94  ARG A N   1 
ATOM   703  C  CA  . ARG A 1 116 ? 7.607  31.968 12.104  1.00 7.05  ? 94  ARG A CA  1 
ATOM   704  C  C   . ARG A 1 116 ? 8.737  31.313 12.898  1.00 6.71  ? 94  ARG A C   1 
ATOM   705  O  O   . ARG A 1 116 ? 8.606  30.178 13.364  1.00 6.57  ? 94  ARG A O   1 
ATOM   706  C  CB  . ARG A 1 116 ? 7.818  31.611 10.627  1.00 7.09  ? 94  ARG A CB  1 
ATOM   707  C  CG  . ARG A 1 116 ? 6.704  31.982 9.665   1.00 7.26  ? 94  ARG A CG  1 
ATOM   708  C  CD  . ARG A 1 116 ? 5.391  31.274 9.942   1.00 7.38  ? 94  ARG A CD  1 
ATOM   709  N  NE  . ARG A 1 116 ? 5.487  29.806 9.913   1.00 7.43  ? 94  ARG A NE  1 
ATOM   710  C  CZ  . ARG A 1 116 ? 5.246  29.027 8.857   1.00 7.49  ? 94  ARG A CZ  1 
ATOM   711  N  NH1 . ARG A 1 116 ? 4.904  29.532 7.682   1.00 7.55  ? 94  ARG A NH1 1 
ATOM   712  N  NH2 . ARG A 1 116 ? 5.342  27.712 8.979   1.00 7.63  ? 94  ARG A NH2 1 
ATOM   713  N  N   . PHE A 1 117 ? 9.855  32.022 13.024  1.00 6.52  ? 95  PHE A N   1 
ATOM   714  C  CA  . PHE A 1 117 ? 11.042 31.464 13.659  1.00 6.52  ? 95  PHE A CA  1 
ATOM   715  C  C   . PHE A 1 117 ? 10.922 31.409 15.176  1.00 6.64  ? 95  PHE A C   1 
ATOM   716  O  O   . PHE A 1 117 ? 11.561 30.577 15.814  1.00 6.74  ? 95  PHE A O   1 
ATOM   717  C  CB  . PHE A 1 117 ? 12.293 32.199 13.172  1.00 6.51  ? 95  PHE A CB  1 
ATOM   718  C  CG  . PHE A 1 117 ? 12.547 31.983 11.714  1.00 6.40  ? 95  PHE A CG  1 
ATOM   719  C  CD1 . PHE A 1 117 ? 13.324 30.918 11.282  1.00 6.36  ? 95  PHE A CD1 1 
ATOM   720  C  CD2 . PHE A 1 117 ? 11.942 32.797 10.766  1.00 6.43  ? 95  PHE A CD2 1 
ATOM   721  C  CE1 . PHE A 1 117 ? 13.516 30.686 9.934   1.00 6.36  ? 95  PHE A CE1 1 
ATOM   722  C  CE2 . PHE A 1 117 ? 12.134 32.572 9.417   1.00 6.48  ? 95  PHE A CE2 1 
ATOM   723  C  CZ  . PHE A 1 117 ? 12.922 31.516 9.000   1.00 6.44  ? 95  PHE A CZ  1 
ATOM   724  N  N   . TRP A 1 118 ? 10.074 32.266 15.741  1.00 6.70  ? 96  TRP A N   1 
ATOM   725  C  CA  . TRP A 1 118 ? 9.769  32.222 17.168  1.00 6.94  ? 96  TRP A CA  1 
ATOM   726  C  C   . TRP A 1 118 ? 8.761  31.109 17.448  1.00 6.99  ? 96  TRP A C   1 
ATOM   727  O  O   . TRP A 1 118 ? 8.980  30.254 18.317  1.00 7.09  ? 96  TRP A O   1 
ATOM   728  C  CB  . TRP A 1 118 ? 9.216  33.576 17.631  1.00 7.08  ? 96  TRP A CB  1 
ATOM   729  C  CG  . TRP A 1 118 ? 8.639  33.555 19.015  1.00 7.25  ? 96  TRP A CG  1 
ATOM   730  C  CD1 . TRP A 1 118 ? 7.333  33.350 19.358  1.00 7.33  ? 96  TRP A CD1 1 
ATOM   731  C  CD2 . TRP A 1 118 ? 9.348  33.741 20.236  1.00 7.44  ? 96  TRP A CD2 1 
ATOM   732  N  NE1 . TRP A 1 118 ? 7.189  33.398 20.716  1.00 7.50  ? 96  TRP A NE1 1 
ATOM   733  C  CE2 . TRP A 1 118 ? 8.410  33.645 21.282  1.00 7.46  ? 96  TRP A CE2 1 
ATOM   734  C  CE3 . TRP A 1 118 ? 10.688 33.985 20.552  1.00 7.55  ? 96  TRP A CE3 1 
ATOM   735  C  CZ2 . TRP A 1 118 ? 8.771  33.769 22.622  1.00 7.54  ? 96  TRP A CZ2 1 
ATOM   736  C  CZ3 . TRP A 1 118 ? 11.041 34.125 21.890  1.00 7.76  ? 96  TRP A CZ3 1 
ATOM   737  C  CH2 . TRP A 1 118 ? 10.083 34.013 22.904  1.00 7.71  ? 96  TRP A CH2 1 
ATOM   738  N  N   . HIS A 1 119 ? 7.662  31.125 16.698  1.00 6.96  ? 97  HIS A N   1 
ATOM   739  C  CA  . HIS A 1 119 ? 6.545  30.198 16.912  1.00 7.06  ? 97  HIS A CA  1 
ATOM   740  C  C   . HIS A 1 119 ? 6.804  28.764 16.461  1.00 7.09  ? 97  HIS A C   1 
ATOM   741  O  O   . HIS A 1 119 ? 6.051  27.859 16.837  1.00 7.42  ? 97  HIS A O   1 
ATOM   742  C  CB  . HIS A 1 119 ? 5.292  30.705 16.201  1.00 7.16  ? 97  HIS A CB  1 
ATOM   743  C  CG  . HIS A 1 119 ? 4.737  31.962 16.788  1.00 7.32  ? 97  HIS A CG  1 
ATOM   744  N  ND1 . HIS A 1 119 ? 4.260  32.030 18.078  1.00 7.53  ? 97  HIS A ND1 1 
ATOM   745  C  CD2 . HIS A 1 119 ? 4.555  33.192 16.252  1.00 7.41  ? 97  HIS A CD2 1 
ATOM   746  C  CE1 . HIS A 1 119 ? 3.829  33.257 18.319  1.00 7.51  ? 97  HIS A CE1 1 
ATOM   747  N  NE2 . HIS A 1 119 ? 3.991  33.978 17.226  1.00 7.53  ? 97  HIS A NE2 1 
ATOM   748  N  N   . CYS A 1 120 ? 7.826  28.557 15.635  1.00 6.94  ? 98  CYS A N   1 
ATOM   749  C  CA  . CYS A 1 120 ? 8.156  27.224 15.146  1.00 6.98  ? 98  CYS A CA  1 
ATOM   750  C  C   . CYS A 1 120 ? 8.159  26.218 16.300  1.00 6.95  ? 98  CYS A C   1 
ATOM   751  O  O   . CYS A 1 120 ? 8.838  26.426 17.304  1.00 6.67  ? 98  CYS A O   1 
ATOM   752  C  CB  . CYS A 1 120 ? 9.520  27.222 14.463  1.00 7.02  ? 98  CYS A CB  1 
ATOM   753  S  SG  . CYS A 1 120 ? 9.892  25.669 13.613  1.00 7.07  ? 98  CYS A SG  1 
ATOM   754  N  N   . PRO A 1 121 ? 7.397  25.121 16.165  1.00 6.96  ? 99  PRO A N   1 
ATOM   755  C  CA  . PRO A 1 121 ? 7.434  24.107 17.221  1.00 7.00  ? 99  PRO A CA  1 
ATOM   756  C  C   . PRO A 1 121 ? 8.812  23.484 17.422  1.00 6.95  ? 99  PRO A C   1 
ATOM   757  O  O   . PRO A 1 121 ? 9.096  22.966 18.504  1.00 7.06  ? 99  PRO A O   1 
ATOM   758  C  CB  . PRO A 1 121 ? 6.452  23.049 16.721  1.00 7.09  ? 99  PRO A CB  1 
ATOM   759  C  CG  . PRO A 1 121 ? 5.513  23.791 15.853  1.00 7.22  ? 99  PRO A CG  1 
ATOM   760  C  CD  . PRO A 1 121 ? 6.305  24.882 15.207  1.00 7.06  ? 99  PRO A CD  1 
ATOM   761  N  N   . LYS A 1 122 ? 9.643  23.530 16.381  1.00 6.80  ? 100 LYS A N   1 
ATOM   762  C  CA  . LYS A 1 122 ? 10.993 22.988 16.423  1.00 6.73  ? 100 LYS A CA  1 
ATOM   763  C  C   . LYS A 1 122 ? 11.995 24.121 16.624  1.00 6.57  ? 100 LYS A C   1 
ATOM   764  O  O   . LYS A 1 122 ? 11.728 25.256 16.230  1.00 6.50  ? 100 LYS A O   1 
ATOM   765  C  CB  . LYS A 1 122 ? 11.277 22.234 15.125  1.00 6.91  ? 100 LYS A CB  1 
ATOM   766  C  CG  . LYS A 1 122 ? 10.230 21.175 14.839  1.00 6.97  ? 100 LYS A CG  1 
ATOM   767  C  CD  . LYS A 1 122 ? 10.405 20.494 13.495  1.00 7.03  ? 100 LYS A CD  1 
ATOM   768  C  CE  . LYS A 1 122 ? 9.270  19.511 13.279  1.00 7.12  ? 100 LYS A CE  1 
ATOM   769  N  NZ  . LYS A 1 122 ? 9.345  18.729 12.017  1.00 7.12  ? 100 LYS A NZ  1 
ATOM   770  N  N   . PRO A 1 123 ? 13.146 23.828 17.251  1.00 6.33  ? 101 PRO A N   1 
ATOM   771  C  CA  . PRO A 1 123 ? 14.108 24.908 17.474  1.00 6.28  ? 101 PRO A CA  1 
ATOM   772  C  C   . PRO A 1 123 ? 14.720 25.463 16.193  1.00 6.20  ? 101 PRO A C   1 
ATOM   773  O  O   . PRO A 1 123 ? 14.983 24.718 15.246  1.00 6.26  ? 101 PRO A O   1 
ATOM   774  C  CB  . PRO A 1 123 ? 15.181 24.245 18.337  1.00 6.30  ? 101 PRO A CB  1 
ATOM   775  C  CG  . PRO A 1 123 ? 14.445 23.160 19.055  1.00 6.29  ? 101 PRO A CG  1 
ATOM   776  C  CD  . PRO A 1 123 ? 13.517 22.620 18.010  1.00 6.36  ? 101 PRO A CD  1 
ATOM   777  N  N   . THR A 1 124 ? 14.932 26.774 16.187  1.00 6.09  ? 102 THR A N   1 
ATOM   778  C  CA  . THR A 1 124 ? 15.471 27.483 15.042  1.00 6.06  ? 102 THR A CA  1 
ATOM   779  C  C   . THR A 1 124 ? 16.809 28.126 15.407  1.00 6.13  ? 102 THR A C   1 
ATOM   780  O  O   . THR A 1 124 ? 16.984 28.670 16.503  1.00 6.05  ? 102 THR A O   1 
ATOM   781  C  CB  . THR A 1 124 ? 14.483 28.564 14.563  1.00 6.07  ? 102 THR A CB  1 
ATOM   782  O  OG1 . THR A 1 124 ? 14.120 29.396 15.668  1.00 6.05  ? 102 THR A OG1 1 
ATOM   783  C  CG2 . THR A 1 124 ? 13.236 27.927 14.004  1.00 6.03  ? 102 THR A CG2 1 
ATOM   784  N  N   . ILE A 1 125 ? 17.764 28.025 14.486  1.00 6.20  ? 103 ILE A N   1 
ATOM   785  C  CA  . ILE A 1 125 ? 19.121 28.502 14.707  1.00 6.38  ? 103 ILE A CA  1 
ATOM   786  C  C   . ILE A 1 125 ? 19.505 29.403 13.543  1.00 6.34  ? 103 ILE A C   1 
ATOM   787  O  O   . ILE A 1 125 ? 19.505 28.956 12.404  1.00 6.35  ? 103 ILE A O   1 
ATOM   788  C  CB  . ILE A 1 125 ? 20.133 27.332 14.766  1.00 6.62  ? 103 ILE A CB  1 
ATOM   789  C  CG1 . ILE A 1 125 ? 19.747 26.312 15.846  1.00 6.81  ? 103 ILE A CG1 1 
ATOM   790  C  CG2 . ILE A 1 125 ? 21.543 27.851 15.013  1.00 6.68  ? 103 ILE A CG2 1 
ATOM   791  C  CD1 . ILE A 1 125 ? 20.193 24.905 15.527  1.00 7.07  ? 103 ILE A CD1 1 
ATOM   792  N  N   . ALA A 1 126 ? 19.819 30.663 13.833  1.00 6.32  ? 104 ALA A N   1 
ATOM   793  C  CA  . ALA A 1 126 ? 20.318 31.585 12.816  1.00 6.42  ? 104 ALA A CA  1 
ATOM   794  C  C   . ALA A 1 126 ? 21.834 31.480 12.806  1.00 6.50  ? 104 ALA A C   1 
ATOM   795  O  O   . ALA A 1 126 ? 22.466 31.540 13.854  1.00 6.56  ? 104 ALA A O   1 
ATOM   796  C  CB  . ALA A 1 126 ? 19.889 33.012 13.118  1.00 6.38  ? 104 ALA A CB  1 
ATOM   797  N  N   . ALA A 1 127 ? 22.406 31.306 11.618  1.00 6.70  ? 105 ALA A N   1 
ATOM   798  C  CA  . ALA A 1 127 ? 23.849 31.194 11.446  1.00 6.84  ? 105 ALA A CA  1 
ATOM   799  C  C   . ALA A 1 127 ? 24.299 32.328 10.533  1.00 6.98  ? 105 ALA A C   1 
ATOM   800  O  O   . ALA A 1 127 ? 24.046 32.295 9.325   1.00 6.96  ? 105 ALA A O   1 
ATOM   801  C  CB  . ALA A 1 127 ? 24.205 29.842 10.851  1.00 6.81  ? 105 ALA A CB  1 
ATOM   802  N  N   . VAL A 1 128 ? 24.949 33.327 11.128  1.00 7.20  ? 106 VAL A N   1 
ATOM   803  C  CA  . VAL A 1 128 ? 25.182 34.629 10.497  1.00 7.42  ? 106 VAL A CA  1 
ATOM   804  C  C   . VAL A 1 128 ? 26.640 34.861 10.082  1.00 7.81  ? 106 VAL A C   1 
ATOM   805  O  O   . VAL A 1 128 ? 27.554 34.744 10.894  1.00 7.70  ? 106 VAL A O   1 
ATOM   806  C  CB  . VAL A 1 128 ? 24.739 35.755 11.458  1.00 7.46  ? 106 VAL A CB  1 
ATOM   807  C  CG1 . VAL A 1 128 ? 25.026 37.129 10.872  1.00 7.39  ? 106 VAL A CG1 1 
ATOM   808  C  CG2 . VAL A 1 128 ? 23.259 35.605 11.788  1.00 7.44  ? 106 VAL A CG2 1 
ATOM   809  N  N   . ARG A 1 129 ? 26.826 35.191 8.804   1.00 8.42  ? 107 ARG A N   1 
ATOM   810  C  CA  . ARG A 1 129 ? 28.066 35.773 8.282   1.00 9.11  ? 107 ARG A CA  1 
ATOM   811  C  C   . ARG A 1 129 ? 27.751 37.178 7.808   1.00 8.63  ? 107 ARG A C   1 
ATOM   812  O  O   . ARG A 1 129 ? 26.642 37.441 7.344   1.00 8.46  ? 107 ARG A O   1 
ATOM   813  C  CB  . ARG A 1 129 ? 28.578 34.995 7.071   1.00 10.24 ? 107 ARG A CB  1 
ATOM   814  C  CG  . ARG A 1 129 ? 28.927 33.546 7.319   1.00 11.71 ? 107 ARG A CG  1 
ATOM   815  C  CD  . ARG A 1 129 ? 29.489 32.917 6.054   1.00 13.01 ? 107 ARG A CD  1 
ATOM   816  N  NE  . ARG A 1 129 ? 29.508 31.456 6.111   1.00 14.90 ? 107 ARG A NE  1 
ATOM   817  C  CZ  . ARG A 1 129 ? 30.475 30.722 6.652   1.00 16.02 ? 107 ARG A CZ  1 
ATOM   818  N  NH1 . ARG A 1 129 ? 31.535 31.293 7.214   1.00 17.30 ? 107 ARG A NH1 1 
ATOM   819  N  NH2 . ARG A 1 129 ? 30.373 29.401 6.642   1.00 17.27 ? 107 ARG A NH2 1 
ATOM   820  N  N   . GLY A 1 130 ? 28.727 38.076 7.895   1.00 8.24  ? 108 GLY A N   1 
ATOM   821  C  CA  . GLY A 1 130 ? 28.573 39.414 7.333   1.00 7.91  ? 108 GLY A CA  1 
ATOM   822  C  C   . GLY A 1 130 ? 27.337 40.147 7.851   1.00 7.74  ? 108 GLY A C   1 
ATOM   823  O  O   . GLY A 1 130 ? 27.015 40.037 9.034   1.00 7.68  ? 108 GLY A O   1 
ATOM   824  N  N   . PRO A 1 131 ? 26.642 40.895 6.970   1.00 7.52  ? 109 PRO A N   1 
ATOM   825  C  CA  . PRO A 1 131 ? 25.538 41.739 7.432   1.00 7.39  ? 109 PRO A CA  1 
ATOM   826  C  C   . PRO A 1 131 ? 24.304 40.953 7.856   1.00 7.22  ? 109 PRO A C   1 
ATOM   827  O  O   . PRO A 1 131 ? 23.908 40.002 7.180   1.00 7.16  ? 109 PRO A O   1 
ATOM   828  C  CB  . PRO A 1 131 ? 25.210 42.600 6.210   1.00 7.44  ? 109 PRO A CB  1 
ATOM   829  C  CG  . PRO A 1 131 ? 25.665 41.796 5.045   1.00 7.49  ? 109 PRO A CG  1 
ATOM   830  C  CD  . PRO A 1 131 ? 26.891 41.073 5.527   1.00 7.46  ? 109 PRO A CD  1 
ATOM   831  N  N   . CYS A 1 132 ? 23.711 41.379 8.969   1.00 7.11  ? 110 CYS A N   1 
ATOM   832  C  CA  . CYS A 1 132 ? 22.444 40.860 9.454   1.00 7.17  ? 110 CYS A CA  1 
ATOM   833  C  C   . CYS A 1 132 ? 21.701 42.082 9.956   1.00 6.99  ? 110 CYS A C   1 
ATOM   834  O  O   . CYS A 1 132 ? 21.836 42.460 11.117  1.00 6.97  ? 110 CYS A O   1 
ATOM   835  C  CB  . CYS A 1 132 ? 22.665 39.842 10.572  1.00 7.25  ? 110 CYS A CB  1 
ATOM   836  S  SG  . CYS A 1 132 ? 21.157 39.164 11.296  1.00 7.50  ? 110 CYS A SG  1 
ATOM   837  N  N   . LEU A 1 133 ? 20.938 42.710 9.064   1.00 7.04  ? 111 LEU A N   1 
ATOM   838  C  CA  . LEU A 1 133 ? 20.418 44.056 9.301   1.00 7.01  ? 111 LEU A CA  1 
ATOM   839  C  C   . LEU A 1 133 ? 18.921 44.165 9.125   1.00 6.89  ? 111 LEU A C   1 
ATOM   840  O  O   . LEU A 1 133 ? 18.326 43.436 8.336   1.00 6.82  ? 111 LEU A O   1 
ATOM   841  C  CB  . LEU A 1 133 ? 21.073 45.049 8.340   1.00 7.17  ? 111 LEU A CB  1 
ATOM   842  C  CG  . LEU A 1 133 ? 22.597 45.109 8.380   1.00 7.33  ? 111 LEU A CG  1 
ATOM   843  C  CD1 . LEU A 1 133 ? 23.106 46.029 7.283   1.00 7.45  ? 111 LEU A CD1 1 
ATOM   844  C  CD2 . LEU A 1 133 ? 23.078 45.554 9.744   1.00 7.37  ? 111 LEU A CD2 1 
ATOM   845  N  N   . ALA A 1 134 ? 18.328 45.102 9.861   1.00 6.83  ? 112 ALA A N   1 
ATOM   846  C  CA  . ALA A 1 134 ? 16.945 45.503 9.655   1.00 6.80  ? 112 ALA A CA  1 
ATOM   847  C  C   . ALA A 1 134 ? 16.004 44.301 9.809   1.00 6.71  ? 112 ALA A C   1 
ATOM   848  O  O   . ALA A 1 134 ? 16.083 43.603 10.819  1.00 6.62  ? 112 ALA A O   1 
ATOM   849  C  CB  . ALA A 1 134 ? 16.799 46.196 8.305   1.00 6.90  ? 112 ALA A CB  1 
ATOM   850  N  N   . GLY A 1 135 ? 15.126 44.052 8.838   1.00 6.68  ? 113 GLY A N   1 
ATOM   851  C  CA  . GLY A 1 135 ? 14.224 42.905 8.898   1.00 6.68  ? 113 GLY A CA  1 
ATOM   852  C  C   . GLY A 1 135 ? 14.922 41.570 9.093   1.00 6.71  ? 113 GLY A C   1 
ATOM   853  O  O   . GLY A 1 135 ? 14.359 40.655 9.677   1.00 6.77  ? 113 GLY A O   1 
ATOM   854  N  N   . ALA A 1 136 ? 16.154 41.456 8.595   1.00 6.74  ? 114 ALA A N   1 
ATOM   855  C  CA  . ALA A 1 136 ? 16.938 40.228 8.743   1.00 6.87  ? 114 ALA A CA  1 
ATOM   856  C  C   . ALA A 1 136 ? 17.516 40.101 10.149  1.00 7.10  ? 114 ALA A C   1 
ATOM   857  O  O   . ALA A 1 136 ? 17.651 38.993 10.674  1.00 7.03  ? 114 ALA A O   1 
ATOM   858  C  CB  . ALA A 1 136 ? 18.055 40.188 7.712   1.00 6.85  ? 114 ALA A CB  1 
ATOM   859  N  N   . CYS A 1 137 ? 17.859 41.233 10.757  1.00 7.41  ? 115 CYS A N   1 
ATOM   860  C  CA  . CYS A 1 137 ? 18.274 41.253 12.160  1.00 7.81  ? 115 CYS A CA  1 
ATOM   861  C  C   . CYS A 1 137 ? 17.104 40.767 13.026  1.00 7.82  ? 115 CYS A C   1 
ATOM   862  O  O   . CYS A 1 137 ? 17.290 39.992 13.956  1.00 7.61  ? 115 CYS A O   1 
ATOM   863  C  CB  . CYS A 1 137 ? 18.718 42.660 12.575  1.00 8.20  ? 115 CYS A CB  1 
ATOM   864  S  SG  . CYS A 1 137 ? 19.409 42.763 14.243  1.00 9.34  ? 115 CYS A SG  1 
ATOM   865  N  N   . GLU A 1 138 ? 15.894 41.197 12.679  1.00 7.83  ? 116 GLU A N   1 
ATOM   866  C  CA  . GLU A 1 138 ? 14.689 40.782 13.401  1.00 7.98  ? 116 GLU A CA  1 
ATOM   867  C  C   . GLU A 1 138 ? 14.413 39.287 13.216  1.00 7.46  ? 116 GLU A C   1 
ATOM   868  O  O   . GLU A 1 138 ? 14.046 38.598 14.163  1.00 7.23  ? 116 GLU A O   1 
ATOM   869  C  CB  . GLU A 1 138 ? 13.494 41.623 12.953  1.00 8.71  ? 116 GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 138 ? 13.650 43.099 13.288  1.00 9.52  ? 116 GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 138 ? 12.663 44.008 12.575  1.00 10.43 ? 116 GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 138 ? 11.822 43.531 11.799  1.00 11.77 ? 116 GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 138 ? 12.737 45.224 12.812  1.00 12.51 ? 116 GLU A OE2 1 
ATOM   874  N  N   . LEU A 1 139 ? 14.607 38.790 11.996  1.00 7.02  ? 117 LEU A N   1 
ATOM   875  C  CA  . LEU A 1 139 ? 14.470 37.363 11.717  1.00 6.87  ? 117 LEU A CA  1 
ATOM   876  C  C   . LEU A 1 139 ? 15.406 36.559 12.628  1.00 6.59  ? 117 LEU A C   1 
ATOM   877  O  O   . LEU A 1 139 ? 14.995 35.591 13.266  1.00 6.38  ? 117 LEU A O   1 
ATOM   878  C  CB  . LEU A 1 139 ? 14.755 37.083 10.234  1.00 7.02  ? 117 LEU A CB  1 
ATOM   879  C  CG  . LEU A 1 139 ? 14.294 35.725 9.690   1.00 7.24  ? 117 LEU A CG  1 
ATOM   880  C  CD1 . LEU A 1 139 ? 14.110 35.811 8.181   1.00 7.45  ? 117 LEU A CD1 1 
ATOM   881  C  CD2 . LEU A 1 139 ? 15.260 34.605 10.051  1.00 7.34  ? 117 LEU A CD2 1 
ATOM   882  N  N   . ALA A 1 140 ? 16.668 36.964 12.697  1.00 6.41  ? 118 ALA A N   1 
ATOM   883  C  CA  . ALA A 1 140 ? 17.616 36.293 13.579  1.00 6.30  ? 118 ALA A CA  1 
ATOM   884  C  C   . ALA A 1 140 ? 17.218 36.432 15.057  1.00 6.27  ? 118 ALA A C   1 
ATOM   885  O  O   . ALA A 1 140 ? 17.337 35.477 15.820  1.00 6.29  ? 118 ALA A O   1 
ATOM   886  C  CB  . ALA A 1 140 ? 19.024 36.813 13.347  1.00 6.28  ? 118 ALA A CB  1 
ATOM   887  N  N   . LEU A 1 141 ? 16.745 37.611 15.456  1.00 6.20  ? 119 LEU A N   1 
ATOM   888  C  CA  . LEU A 1 141 ? 16.303 37.825 16.841  1.00 6.24  ? 119 LEU A CA  1 
ATOM   889  C  C   . LEU A 1 141 ? 15.201 36.839 17.236  1.00 6.22  ? 119 LEU A C   1 
ATOM   890  O  O   . LEU A 1 141 ? 15.140 36.385 18.384  1.00 6.36  ? 119 LEU A O   1 
ATOM   891  C  CB  . LEU A 1 141 ? 15.791 39.255 17.048  1.00 6.34  ? 119 LEU A CB  1 
ATOM   892  C  CG  . LEU A 1 141 ? 16.811 40.395 17.123  1.00 6.46  ? 119 LEU A CG  1 
ATOM   893  C  CD1 . LEU A 1 141 ? 16.110 41.742 17.204  1.00 6.56  ? 119 LEU A CD1 1 
ATOM   894  C  CD2 . LEU A 1 141 ? 17.756 40.228 18.303  1.00 6.57  ? 119 LEU A CD2 1 
ATOM   895  N  N   . ALA A 1 142 ? 14.341 36.509 16.278  1.00 6.13  ? 120 ALA A N   1 
ATOM   896  C  CA  . ALA A 1 142 ? 13.221 35.599 16.514  1.00 6.24  ? 120 ALA A CA  1 
ATOM   897  C  C   . ALA A 1 142 ? 13.650 34.134 16.679  1.00 6.38  ? 120 ALA A C   1 
ATOM   898  O  O   . ALA A 1 142 ? 12.897 33.330 17.235  1.00 6.52  ? 120 ALA A O   1 
ATOM   899  C  CB  . ALA A 1 142 ? 12.207 35.711 15.384  1.00 6.21  ? 120 ALA A CB  1 
ATOM   900  N  N   . CYS A 1 143 ? 14.834 33.779 16.180  1.00 6.55  ? 121 CYS A N   1 
ATOM   901  C  CA  . CYS A 1 143 ? 15.316 32.401 16.279  1.00 6.64  ? 121 CYS A CA  1 
ATOM   902  C  C   . CYS A 1 143 ? 15.673 32.029 17.714  1.00 6.98  ? 121 CYS A C   1 
ATOM   903  O  O   . CYS A 1 143 ? 16.048 32.878 18.518  1.00 6.95  ? 121 CYS A O   1 
ATOM   904  C  CB  . CYS A 1 143 ? 16.530 32.164 15.376  1.00 6.51  ? 121 CYS A CB  1 
ATOM   905  S  SG  . CYS A 1 143 ? 16.129 32.214 13.616  1.00 6.34  ? 121 CYS A SG  1 
ATOM   906  N  N   . ASP A 1 144 ? 15.556 30.750 18.035  1.00 7.37  ? 122 ASP A N   1 
ATOM   907  C  CA  . ASP A 1 144 ? 15.871 30.306 19.389  1.00 7.93  ? 122 ASP A CA  1 
ATOM   908  C  C   . ASP A 1 144 ? 17.313 30.608 19.745  1.00 8.39  ? 122 ASP A C   1 
ATOM   909  O  O   . ASP A 1 144 ? 17.595 31.054 20.858  1.00 8.41  ? 122 ASP A O   1 
ATOM   910  C  CB  . ASP A 1 144 ? 15.546 28.832 19.552  1.00 8.12  ? 122 ASP A CB  1 
ATOM   911  C  CG  . ASP A 1 144 ? 14.077 28.569 19.406  1.00 8.35  ? 122 ASP A CG  1 
ATOM   912  O  OD1 . ASP A 1 144 ? 13.295 29.131 20.205  1.00 8.94  ? 122 ASP A OD1 1 
ATOM   913  O  OD2 . ASP A 1 144 ? 13.686 27.853 18.471  1.00 8.40  ? 122 ASP A OD2 1 
HETATM 914  N  N   . MSE A 1 145 ? 18.216 30.390 18.789  1.00 8.98  ? 123 MSE A N   1 
HETATM 915  C  CA  . MSE A 1 145 ? 19.626 30.710 18.966  1.00 9.74  ? 123 MSE A CA  1 
HETATM 916  C  C   . MSE A 1 145 ? 20.172 31.399 17.744  1.00 8.80  ? 123 MSE A C   1 
HETATM 917  O  O   . MSE A 1 145 ? 19.654 31.235 16.649  1.00 8.25  ? 123 MSE A O   1 
HETATM 918  C  CB  . MSE A 1 145 ? 20.446 29.447 19.196  1.00 12.02 ? 123 MSE A CB  1 
HETATM 919  C  CG  . MSE A 1 145 ? 20.156 28.821 20.554  1.00 14.30 ? 123 MSE A CG  1 
HETATM 920  SE SE  . MSE A 1 145 ? 21.211 27.163 20.714  1.00 21.40 ? 123 MSE A SE  1 
HETATM 921  C  CE  . MSE A 1 145 ? 23.015 27.960 20.720  1.00 19.50 ? 123 MSE A CE  1 
ATOM   922  N  N   . THR A 1 146 ? 21.227 32.180 17.944  1.00 8.10  ? 124 THR A N   1 
ATOM   923  C  CA  . THR A 1 146 ? 21.963 32.821 16.860  1.00 7.72  ? 124 THR A CA  1 
ATOM   924  C  C   . THR A 1 146 ? 23.443 32.584 17.081  1.00 7.65  ? 124 THR A C   1 
ATOM   925  O  O   . THR A 1 146 ? 23.964 32.863 18.158  1.00 7.46  ? 124 THR A O   1 
ATOM   926  C  CB  . THR A 1 146 ? 21.720 34.342 16.816  1.00 7.74  ? 124 THR A CB  1 
ATOM   927  O  OG1 . THR A 1 146 ? 20.322 34.596 16.634  1.00 7.55  ? 124 THR A OG1 1 
ATOM   928  C  CG2 . THR A 1 146 ? 22.509 34.991 15.666  1.00 7.77  ? 124 THR A CG2 1 
ATOM   929  N  N   . ILE A 1 147 ? 24.120 32.076 16.061  1.00 7.57  ? 125 ILE A N   1 
ATOM   930  C  CA  . ILE A 1 147 ? 25.575 31.988 16.105  1.00 7.83  ? 125 ILE A CA  1 
ATOM   931  C  C   . ILE A 1 147 ? 26.108 32.816 14.948  1.00 7.85  ? 125 ILE A C   1 
ATOM   932  O  O   . ILE A 1 147 ? 25.417 33.019 13.948  1.00 7.60  ? 125 ILE A O   1 
ATOM   933  C  CB  . ILE A 1 147 ? 26.087 30.532 16.060  1.00 8.09  ? 125 ILE A CB  1 
ATOM   934  C  CG1 . ILE A 1 147 ? 25.714 29.842 14.752  1.00 8.23  ? 125 ILE A CG1 1 
ATOM   935  C  CG2 . ILE A 1 147 ? 25.547 29.744 17.251  1.00 8.24  ? 125 ILE A CG2 1 
ATOM   936  C  CD1 . ILE A 1 147 ? 26.412 28.508 14.564  1.00 8.34  ? 125 ILE A CD1 1 
ATOM   937  N  N   . ALA A 1 148 ? 27.327 33.318 15.091  1.00 8.05  ? 126 ALA A N   1 
ATOM   938  C  CA  . ALA A 1 148 ? 27.854 34.251 14.115  1.00 8.31  ? 126 ALA A CA  1 
ATOM   939  C  C   . ALA A 1 148 ? 29.359 34.132 14.026  1.00 8.93  ? 126 ALA A C   1 
ATOM   940  O  O   . ALA A 1 148 ? 30.011 33.705 14.976  1.00 8.74  ? 126 ALA A O   1 
ATOM   941  C  CB  . ALA A 1 148 ? 27.472 35.672 14.501  1.00 8.32  ? 126 ALA A CB  1 
ATOM   942  N  N   . THR A 1 149 ? 29.905 34.513 12.882  1.00 9.61  ? 127 THR A N   1 
ATOM   943  C  CA  . THR A 1 149 ? 31.348 34.632 12.742  1.00 10.50 ? 127 THR A CA  1 
ATOM   944  C  C   . THR A 1 149 ? 31.818 35.985 13.272  1.00 11.36 ? 127 THR A C   1 
ATOM   945  O  O   . THR A 1 149 ? 31.020 36.903 13.447  1.00 11.05 ? 127 THR A O   1 
ATOM   946  C  CB  . THR A 1 149 ? 31.759 34.506 11.269  1.00 10.69 ? 127 THR A CB  1 
ATOM   947  O  OG1 . THR A 1 149 ? 31.068 35.495 10.507  1.00 10.98 ? 127 THR A OG1 1 
ATOM   948  C  CG2 . THR A 1 149 ? 31.420 33.138 10.741  1.00 11.08 ? 127 THR A CG2 1 
ATOM   949  N  N   . GLU A 1 150 ? 33.125 36.109 13.500  1.00 12.80 ? 128 GLU A N   1 
ATOM   950  C  CA  . GLU A 1 150 ? 33.717 37.360 13.986  1.00 14.30 ? 128 GLU A CA  1 
ATOM   951  C  C   . GLU A 1 150 ? 33.419 38.549 13.072  1.00 13.91 ? 128 GLU A C   1 
ATOM   952  O  O   . GLU A 1 150 ? 33.271 39.666 13.547  1.00 14.38 ? 128 GLU A O   1 
ATOM   953  C  CB  . GLU A 1 150 ? 35.236 37.212 14.129  1.00 16.11 ? 128 GLU A CB  1 
ATOM   954  C  CG  . GLU A 1 150 ? 35.684 36.261 15.229  1.00 18.13 ? 128 GLU A CG  1 
ATOM   955  C  CD  . GLU A 1 150 ? 35.671 36.869 16.622  1.00 20.09 ? 128 GLU A CD  1 
ATOM   956  O  OE1 . GLU A 1 150 ? 35.373 38.079 16.778  1.00 22.97 ? 128 GLU A OE1 1 
ATOM   957  O  OE2 . GLU A 1 150 ? 35.967 36.117 17.576  1.00 22.90 ? 128 GLU A OE2 1 
ATOM   958  N  N   . ASP A 1 151 ? 33.325 38.286 11.770  1.00 13.47 ? 129 ASP A N   1 
ATOM   959  C  CA  . ASP A 1 151 ? 33.092 39.316 10.752  1.00 13.26 ? 129 ASP A CA  1 
ATOM   960  C  C   . ASP A 1 151 ? 31.635 39.754 10.623  1.00 12.08 ? 129 ASP A C   1 
ATOM   961  O  O   . ASP A 1 151 ? 31.338 40.683 9.866   1.00 12.05 ? 129 ASP A O   1 
ATOM   962  C  CB  . ASP A 1 151 ? 33.557 38.796 9.384   1.00 14.24 ? 129 ASP A CB  1 
ATOM   963  C  CG  . ASP A 1 151 ? 32.836 37.520 8.973   1.00 15.12 ? 129 ASP A CG  1 
ATOM   964  O  OD1 . ASP A 1 151 ? 33.347 36.427 9.291   1.00 17.18 ? 129 ASP A OD1 1 
ATOM   965  O  OD2 . ASP A 1 151 ? 31.749 37.593 8.364   1.00 16.10 ? 129 ASP A OD2 1 
ATOM   966  N  N   . ALA A 1 152 ? 30.726 39.080 11.328  1.00 10.60 ? 130 ALA A N   1 
ATOM   967  C  CA  . ALA A 1 152 ? 29.304 39.411 11.237  1.00 9.79  ? 130 ALA A CA  1 
ATOM   968  C  C   . ALA A 1 152 ? 29.040 40.735 11.928  1.00 9.13  ? 130 ALA A C   1 
ATOM   969  O  O   . ALA A 1 152 ? 29.724 41.094 12.889  1.00 8.85  ? 130 ALA A O   1 
ATOM   970  C  CB  . ALA A 1 152 ? 28.449 38.316 11.857  1.00 9.74  ? 130 ALA A CB  1 
ATOM   971  N  N   . PHE A 1 153 ? 28.060 41.470 11.418  1.00 8.49  ? 131 PHE A N   1 
ATOM   972  C  CA  . PHE A 1 153 ? 27.653 42.717 12.044  1.00 8.29  ? 131 PHE A CA  1 
ATOM   973  C  C   . PHE A 1 153 ? 26.143 42.867 11.957  1.00 7.97  ? 131 PHE A C   1 
ATOM   974  O  O   . PHE A 1 153 ? 25.509 42.376 11.023  1.00 7.89  ? 131 PHE A O   1 
ATOM   975  C  CB  . PHE A 1 153 ? 28.389 43.929 11.454  1.00 8.41  ? 131 PHE A CB  1 
ATOM   976  C  CG  . PHE A 1 153 ? 28.269 44.071 9.961   1.00 8.59  ? 131 PHE A CG  1 
ATOM   977  C  CD1 . PHE A 1 153 ? 29.116 43.372 9.109   1.00 8.65  ? 131 PHE A CD1 1 
ATOM   978  C  CD2 . PHE A 1 153 ? 27.338 44.938 9.403   1.00 8.69  ? 131 PHE A CD2 1 
ATOM   979  C  CE1 . PHE A 1 153 ? 29.018 43.515 7.736   1.00 8.77  ? 131 PHE A CE1 1 
ATOM   980  C  CE2 . PHE A 1 153 ? 27.236 45.086 8.029   1.00 8.87  ? 131 PHE A CE2 1 
ATOM   981  C  CZ  . PHE A 1 153 ? 28.080 44.375 7.193   1.00 8.82  ? 131 PHE A CZ  1 
ATOM   982  N  N   . PHE A 1 154 ? 25.587 43.555 12.948  1.00 7.74  ? 132 PHE A N   1 
ATOM   983  C  CA  . PHE A 1 154 ? 24.151 43.563 13.191  1.00 7.64  ? 132 PHE A CA  1 
ATOM   984  C  C   . PHE A 1 154 ? 23.617 44.969 13.343  1.00 7.75  ? 132 PHE A C   1 
ATOM   985  O  O   . PHE A 1 154 ? 24.367 45.912 13.579  1.00 7.70  ? 132 PHE A O   1 
ATOM   986  C  CB  . PHE A 1 154 ? 23.851 42.806 14.482  1.00 7.53  ? 132 PHE A CB  1 
ATOM   987  C  CG  . PHE A 1 154 ? 24.191 41.351 14.420  1.00 7.36  ? 132 PHE A CG  1 
ATOM   988  C  CD1 . PHE A 1 154 ? 25.487 40.919 14.658  1.00 7.39  ? 132 PHE A CD1 1 
ATOM   989  C  CD2 . PHE A 1 154 ? 23.219 40.412 14.117  1.00 7.33  ? 132 PHE A CD2 1 
ATOM   990  C  CE1 . PHE A 1 154 ? 25.804 39.577 14.591  1.00 7.34  ? 132 PHE A CE1 1 
ATOM   991  C  CE2 . PHE A 1 154 ? 23.529 39.068 14.063  1.00 7.30  ? 132 PHE A CE2 1 
ATOM   992  C  CZ  . PHE A 1 154 ? 24.825 38.650 14.296  1.00 7.34  ? 132 PHE A CZ  1 
ATOM   993  N  N   . GLY A 1 155 ? 22.302 45.097 13.249  1.00 7.99  ? 133 GLY A N   1 
ATOM   994  C  CA  . GLY A 1 155 ? 21.650 46.324 13.652  1.00 8.38  ? 133 GLY A CA  1 
ATOM   995  C  C   . GLY A 1 155 ? 20.358 46.604 12.935  1.00 8.74  ? 133 GLY A C   1 
ATOM   996  O  O   . GLY A 1 155 ? 19.885 45.800 12.128  1.00 8.44  ? 133 GLY A O   1 
ATOM   997  N  N   . GLU A 1 156 ? 19.799 47.767 13.237  1.00 9.47  ? 134 GLU A N   1 
ATOM   998  C  CA  . GLU A 1 156 ? 18.495 48.156 12.725  1.00 10.33 ? 134 GLU A CA  1 
ATOM   999  C  C   . GLU A 1 156 ? 18.596 49.588 12.215  1.00 9.89  ? 134 GLU A C   1 
ATOM   1000 O  O   . GLU A 1 156 ? 18.290 50.522 12.941  1.00 9.52  ? 134 GLU A O   1 
ATOM   1001 C  CB  . GLU A 1 156 ? 17.436 48.013 13.830  1.00 11.92 ? 134 GLU A CB  1 
ATOM   1002 C  CG  . GLU A 1 156 ? 17.296 46.574 14.322  1.00 13.56 ? 134 GLU A CG  1 
ATOM   1003 C  CD  . GLU A 1 156 ? 15.920 46.227 14.869  1.00 15.56 ? 134 GLU A CD  1 
ATOM   1004 O  OE1 . GLU A 1 156 ? 14.940 46.214 14.101  1.00 18.50 ? 134 GLU A OE1 1 
ATOM   1005 O  OE2 . GLU A 1 156 ? 15.821 45.950 16.072  1.00 17.99 ? 134 GLU A OE2 1 
ATOM   1006 N  N   . PRO A 1 157 ? 19.031 49.763 10.952  1.00 9.45  ? 135 PRO A N   1 
ATOM   1007 C  CA  . PRO A 1 157 ? 19.231 51.104 10.391  1.00 9.35  ? 135 PRO A CA  1 
ATOM   1008 C  C   . PRO A 1 157 ? 17.949 51.825 9.955   1.00 9.31  ? 135 PRO A C   1 
ATOM   1009 O  O   . PRO A 1 157 ? 18.034 52.946 9.465   1.00 9.21  ? 135 PRO A O   1 
ATOM   1010 C  CB  . PRO A 1 157 ? 20.105 50.836 9.166   1.00 9.39  ? 135 PRO A CB  1 
ATOM   1011 C  CG  . PRO A 1 157 ? 19.730 49.463 8.738   1.00 9.34  ? 135 PRO A CG  1 
ATOM   1012 C  CD  . PRO A 1 157 ? 19.444 48.707 10.007  1.00 9.39  ? 135 PRO A CD  1 
ATOM   1013 N  N   . GLU A 1 158 ? 16.792 51.192 10.146  1.00 9.29  ? 136 GLU A N   1 
ATOM   1014 C  CA  . GLU A 1 158 ? 15.505 51.691 9.648   1.00 9.41  ? 136 GLU A CA  1 
ATOM   1015 C  C   . GLU A 1 158 ? 15.303 53.203 9.782   1.00 9.20  ? 136 GLU A C   1 
ATOM   1016 O  O   . GLU A 1 158 ? 14.975 53.873 8.804   1.00 8.94  ? 136 GLU A O   1 
ATOM   1017 C  CB  . GLU A 1 158 ? 14.343 50.954 10.338  1.00 9.87  ? 136 GLU A CB  1 
ATOM   1018 C  CG  . GLU A 1 158 ? 14.100 49.525 9.852   1.00 10.43 ? 136 GLU A CG  1 
ATOM   1019 C  CD  . GLU A 1 158 ? 14.927 48.465 10.567  1.00 11.07 ? 136 GLU A CD  1 
ATOM   1020 O  OE1 . GLU A 1 158 ? 16.119 48.700 10.841  1.00 11.58 ? 136 GLU A OE1 1 
ATOM   1021 O  OE2 . GLU A 1 158 ? 14.390 47.365 10.848  1.00 11.88 ? 136 GLU A OE2 1 
ATOM   1022 N  N   . LEU A 1 159 ? 15.501 53.751 10.977  1.00 8.96  ? 137 LEU A N   1 
ATOM   1023 C  CA  . LEU A 1 159 ? 15.167 55.160 11.199  1.00 9.00  ? 137 LEU A CA  1 
ATOM   1024 C  C   . LEU A 1 159 ? 16.016 56.101 10.347  1.00 9.20  ? 137 LEU A C   1 
ATOM   1025 O  O   . LEU A 1 159 ? 15.544 57.174 9.977   1.00 9.36  ? 137 LEU A O   1 
ATOM   1026 C  CB  . LEU A 1 159 ? 15.229 55.552 12.680  1.00 8.84  ? 137 LEU A CB  1 
ATOM   1027 C  CG  . LEU A 1 159 ? 13.880 55.490 13.408  1.00 8.79  ? 137 LEU A CG  1 
ATOM   1028 C  CD1 . LEU A 1 159 ? 13.375 54.060 13.503  1.00 8.69  ? 137 LEU A CD1 1 
ATOM   1029 C  CD2 . LEU A 1 159 ? 13.993 56.121 14.786  1.00 8.73  ? 137 LEU A CD2 1 
ATOM   1030 N  N   . LYS A 1 160 ? 17.237 55.695 10.009  1.00 9.45  ? 138 LYS A N   1 
ATOM   1031 C  CA  . LYS A 1 160 ? 18.091 56.506 9.135   1.00 9.82  ? 138 LYS A CA  1 
ATOM   1032 C  C   . LYS A 1 160 ? 17.541 56.562 7.708   1.00 10.04 ? 138 LYS A C   1 
ATOM   1033 O  O   . LYS A 1 160 ? 17.779 57.541 7.000   1.00 10.69 ? 138 LYS A O   1 
ATOM   1034 C  CB  . LYS A 1 160 ? 19.530 55.989 9.125   1.00 9.84  ? 138 LYS A CB  1 
ATOM   1035 C  CG  . LYS A 1 160 ? 20.183 55.988 10.501  1.00 10.00 ? 138 LYS A CG  1 
ATOM   1036 C  CD  . LYS A 1 160 ? 21.689 55.790 10.434  1.00 10.26 ? 138 LYS A CD  1 
ATOM   1037 C  CE  . LYS A 1 160 ? 22.060 54.465 9.787   1.00 10.42 ? 138 LYS A CE  1 
ATOM   1038 N  NZ  . LYS A 1 160 ? 23.509 54.156 9.928   1.00 10.71 ? 138 LYS A NZ  1 
ATOM   1039 N  N   . PHE A 1 161 ? 16.821 55.515 7.301   1.00 10.25 ? 139 PHE A N   1 
ATOM   1040 C  CA  . PHE A 1 161 ? 16.110 55.465 6.009   1.00 10.43 ? 139 PHE A CA  1 
ATOM   1041 C  C   . PHE A 1 161 ? 14.730 56.144 6.046   1.00 10.06 ? 139 PHE A C   1 
ATOM   1042 O  O   . PHE A 1 161 ? 14.050 56.212 5.021   1.00 10.29 ? 139 PHE A O   1 
ATOM   1043 C  CB  . PHE A 1 161 ? 15.871 54.010 5.579   1.00 10.87 ? 139 PHE A CB  1 
ATOM   1044 C  CG  . PHE A 1 161 ? 17.098 53.280 5.123   1.00 11.28 ? 139 PHE A CG  1 
ATOM   1045 C  CD1 . PHE A 1 161 ? 17.690 53.589 3.906   1.00 11.51 ? 139 PHE A CD1 1 
ATOM   1046 C  CD2 . PHE A 1 161 ? 17.622 52.235 5.872   1.00 11.69 ? 139 PHE A CD2 1 
ATOM   1047 C  CE1 . PHE A 1 161 ? 18.808 52.896 3.466   1.00 11.67 ? 139 PHE A CE1 1 
ATOM   1048 C  CE2 . PHE A 1 161 ? 18.731 51.533 5.432   1.00 11.87 ? 139 PHE A CE2 1 
ATOM   1049 C  CZ  . PHE A 1 161 ? 19.325 51.863 4.225   1.00 11.91 ? 139 PHE A CZ  1 
ATOM   1050 N  N   . GLY A 1 162 ? 14.293 56.595 7.218   1.00 9.40  ? 140 GLY A N   1 
ATOM   1051 C  CA  . GLY A 1 162 ? 12.943 57.127 7.380   1.00 8.91  ? 140 GLY A CA  1 
ATOM   1052 C  C   . GLY A 1 162 ? 11.884 56.046 7.534   1.00 8.49  ? 140 GLY A C   1 
ATOM   1053 O  O   . GLY A 1 162 ? 10.697 56.327 7.386   1.00 8.43  ? 140 GLY A O   1 
ATOM   1054 N  N   . ALA A 1 163 ? 12.318 54.816 7.819   1.00 7.95  ? 141 ALA A N   1 
ATOM   1055 C  CA  . ALA A 1 163 ? 11.412 53.684 8.028   1.00 7.61  ? 141 ALA A CA  1 
ATOM   1056 C  C   . ALA A 1 163 ? 11.255 53.440 9.524   1.00 7.37  ? 141 ALA A C   1 
ATOM   1057 O  O   . ALA A 1 163 ? 12.148 53.741 10.299  1.00 7.41  ? 141 ALA A O   1 
ATOM   1058 C  CB  . ALA A 1 163 ? 11.963 52.438 7.356   1.00 7.60  ? 141 ALA A CB  1 
ATOM   1059 N  N   . GLY A 1 164 ? 10.106 52.909 9.927   1.00 7.14  ? 142 GLY A N   1 
ATOM   1060 C  CA  . GLY A 1 164 ? 9.928  52.454 11.301  1.00 6.97  ? 142 GLY A CA  1 
ATOM   1061 C  C   . GLY A 1 164 ? 10.311 50.993 11.463  1.00 6.93  ? 142 GLY A C   1 
ATOM   1062 O  O   . GLY A 1 164 ? 10.664 50.311 10.501  1.00 6.97  ? 142 GLY A O   1 
ATOM   1063 N  N   . ILE A 1 165 ? 10.238 50.515 12.701  1.00 6.82  ? 143 ILE A N   1 
ATOM   1064 C  CA  . ILE A 1 165 ? 10.575 49.132 13.036  1.00 6.73  ? 143 ILE A CA  1 
ATOM   1065 C  C   . ILE A 1 165 ? 9.343  48.244 12.855  1.00 6.72  ? 143 ILE A C   1 
ATOM   1066 O  O   . ILE A 1 165 ? 8.296  48.509 13.438  1.00 6.76  ? 143 ILE A O   1 
ATOM   1067 C  CB  . ILE A 1 165 ? 11.067 49.034 14.495  1.00 6.67  ? 143 ILE A CB  1 
ATOM   1068 C  CG1 . ILE A 1 165 ? 12.301 49.928 14.718  1.00 6.71  ? 143 ILE A CG1 1 
ATOM   1069 C  CG2 . ILE A 1 165 ? 11.326 47.588 14.904  1.00 6.61  ? 143 ILE A CG2 1 
ATOM   1070 C  CD1 . ILE A 1 165 ? 13.519 49.576 13.891  1.00 6.81  ? 143 ILE A CD1 1 
ATOM   1071 N  N   . VAL A 1 166 ? 9.476  47.183 12.067  1.00 6.81  ? 144 VAL A N   1 
ATOM   1072 C  CA  . VAL A 1 166 ? 8.350  46.283 11.799  1.00 6.78  ? 144 VAL A CA  1 
ATOM   1073 C  C   . VAL A 1 166 ? 8.133  45.308 12.954  1.00 6.92  ? 144 VAL A C   1 
ATOM   1074 O  O   . VAL A 1 166 ? 7.009  45.175 13.444  1.00 6.63  ? 144 VAL A O   1 
ATOM   1075 C  CB  . VAL A 1 166 ? 8.542  45.480 10.494  1.00 6.78  ? 144 VAL A CB  1 
ATOM   1076 C  CG1 . VAL A 1 166 ? 7.358  44.550 10.254  1.00 6.78  ? 144 VAL A CG1 1 
ATOM   1077 C  CG2 . VAL A 1 166 ? 8.715  46.417 9.310   1.00 6.77  ? 144 VAL A CG2 1 
ATOM   1078 N  N   . VAL A 1 167 ? 9.203  44.618 13.360  1.00 7.14  ? 145 VAL A N   1 
ATOM   1079 C  CA  . VAL A 1 167 ? 9.138  43.615 14.424  1.00 7.47  ? 145 VAL A CA  1 
ATOM   1080 C  C   . VAL A 1 167 ? 10.028 44.069 15.575  1.00 7.87  ? 145 VAL A C   1 
ATOM   1081 O  O   . VAL A 1 167 ? 11.251 43.912 15.523  1.00 7.82  ? 145 VAL A O   1 
ATOM   1082 C  CB  . VAL A 1 167 ? 9.574  42.214 13.929  1.00 7.47  ? 145 VAL A CB  1 
ATOM   1083 C  CG1 . VAL A 1 167 ? 9.234  41.161 14.975  1.00 7.54  ? 145 VAL A CG1 1 
ATOM   1084 C  CG2 . VAL A 1 167 ? 8.899  41.883 12.606  1.00 7.49  ? 145 VAL A CG2 1 
HETATM 1085 N  N   . MSE A 1 168 ? 9.418  44.620 16.625  1.00 8.48  ? 146 MSE A N   1 
HETATM 1086 C  CA  . MSE A 1 168 ? 10.192 45.212 17.728  1.00 9.45  ? 146 MSE A CA  1 
HETATM 1087 C  C   . MSE A 1 168 ? 10.572 44.180 18.768  1.00 8.52  ? 146 MSE A C   1 
HETATM 1088 O  O   . MSE A 1 168 ? 10.245 44.308 19.949  1.00 7.90  ? 146 MSE A O   1 
HETATM 1089 C  CB  . MSE A 1 168 ? 9.466  46.421 18.327  1.00 11.63 ? 146 MSE A CB  1 
HETATM 1090 C  CG  . MSE A 1 168 ? 10.454 47.283 19.127  1.00 14.19 ? 146 MSE A CG  1 
HETATM 1091 SE SE  . MSE A 1 168 ? 9.592  48.965 19.654  1.00 20.85 ? 146 MSE A SE  1 
HETATM 1092 C  CE  . MSE A 1 168 ? 10.087 49.982 18.040  1.00 18.27 ? 146 MSE A CE  1 
ATOM   1093 N  N   . LEU A 1 169 ? 11.298 43.151 18.335  1.00 7.74  ? 147 LEU A N   1 
ATOM   1094 C  CA  . LEU A 1 169 ? 11.821 42.137 19.255  1.00 7.41  ? 147 LEU A CA  1 
ATOM   1095 C  C   . LEU A 1 169 ? 12.985 42.632 20.108  1.00 7.19  ? 147 LEU A C   1 
ATOM   1096 O  O   . LEU A 1 169 ? 13.231 42.093 21.180  1.00 7.06  ? 147 LEU A O   1 
ATOM   1097 C  CB  . LEU A 1 169 ? 12.295 40.899 18.485  1.00 7.36  ? 147 LEU A CB  1 
ATOM   1098 C  CG  . LEU A 1 169 ? 11.208 39.915 18.055  1.00 7.43  ? 147 LEU A CG  1 
ATOM   1099 C  CD1 . LEU A 1 169 ? 11.715 39.036 16.924  1.00 7.49  ? 147 LEU A CD1 1 
ATOM   1100 C  CD2 . LEU A 1 169 ? 10.744 39.077 19.239  1.00 7.47  ? 147 LEU A CD2 1 
ATOM   1101 N  N   . LEU A 1 170 ? 13.732 43.622 19.630  1.00 7.09  ? 148 LEU A N   1 
ATOM   1102 C  CA  . LEU A 1 170 ? 15.001 43.972 20.277  1.00 7.06  ? 148 LEU A CA  1 
ATOM   1103 C  C   . LEU A 1 170 ? 14.928 44.193 21.800  1.00 7.33  ? 148 LEU A C   1 
ATOM   1104 O  O   . LEU A 1 170 ? 15.734 43.625 22.527  1.00 7.24  ? 148 LEU A O   1 
ATOM   1105 C  CB  . LEU A 1 170 ? 15.669 45.161 19.573  1.00 7.01  ? 148 LEU A CB  1 
ATOM   1106 C  CG  . LEU A 1 170 ? 17.123 45.430 19.939  1.00 6.94  ? 148 LEU A CG  1 
ATOM   1107 C  CD1 . LEU A 1 170 ? 17.978 44.194 19.677  1.00 6.90  ? 148 LEU A CD1 1 
ATOM   1108 C  CD2 . LEU A 1 170 ? 17.618 46.619 19.134  1.00 7.03  ? 148 LEU A CD2 1 
ATOM   1109 N  N   . PRO A 1 171 ? 13.955 44.986 22.299  1.00 7.58  ? 149 PRO A N   1 
ATOM   1110 C  CA  . PRO A 1 171 ? 13.914 45.193 23.754  1.00 7.95  ? 149 PRO A CA  1 
ATOM   1111 C  C   . PRO A 1 171 ? 13.610 43.942 24.574  1.00 8.33  ? 149 PRO A C   1 
ATOM   1112 O  O   . PRO A 1 171 ? 13.917 43.917 25.774  1.00 9.50  ? 149 PRO A O   1 
ATOM   1113 C  CB  . PRO A 1 171 ? 12.818 46.256 23.949  1.00 7.83  ? 149 PRO A CB  1 
ATOM   1114 C  CG  . PRO A 1 171 ? 12.052 46.279 22.683  1.00 7.80  ? 149 PRO A CG  1 
ATOM   1115 C  CD  . PRO A 1 171 ? 12.966 45.816 21.592  1.00 7.68  ? 149 PRO A CD  1 
ATOM   1116 N  N   . TRP A 1 172 ? 13.044 42.918 23.938  1.00 8.11  ? 150 TRP A N   1 
ATOM   1117 C  CA  . TRP A 1 172 ? 12.790 41.630 24.595  1.00 8.04  ? 150 TRP A CA  1 
ATOM   1118 C  C   . TRP A 1 172 ? 14.041 40.752 24.677  1.00 8.49  ? 150 TRP A C   1 
ATOM   1119 O  O   . TRP A 1 172 ? 14.133 39.880 25.553  1.00 9.02  ? 150 TRP A O   1 
ATOM   1120 C  CB  . TRP A 1 172 ? 11.652 40.891 23.884  1.00 7.64  ? 150 TRP A CB  1 
ATOM   1121 C  CG  . TRP A 1 172 ? 10.397 41.682 23.955  1.00 7.27  ? 150 TRP A CG  1 
ATOM   1122 C  CD1 . TRP A 1 172 ? 9.940  42.590 23.043  1.00 7.08  ? 150 TRP A CD1 1 
ATOM   1123 C  CD2 . TRP A 1 172 ? 9.468  41.698 25.039  1.00 6.93  ? 150 TRP A CD2 1 
ATOM   1124 N  NE1 . TRP A 1 172 ? 8.770  43.159 23.486  1.00 7.01  ? 150 TRP A NE1 1 
ATOM   1125 C  CE2 . TRP A 1 172 ? 8.456  42.626 24.708  1.00 6.93  ? 150 TRP A CE2 1 
ATOM   1126 C  CE3 . TRP A 1 172 ? 9.385  41.012 26.256  1.00 6.93  ? 150 TRP A CE3 1 
ATOM   1127 C  CZ2 . TRP A 1 172 ? 7.376  42.880 25.548  1.00 6.87  ? 150 TRP A CZ2 1 
ATOM   1128 C  CZ3 . TRP A 1 172 ? 8.310  41.263 27.083  1.00 6.84  ? 150 TRP A CZ3 1 
ATOM   1129 C  CH2 . TRP A 1 172 ? 7.320  42.184 26.725  1.00 6.84  ? 150 TRP A CH2 1 
ATOM   1130 N  N   . ILE A 1 173 ? 15.005 40.998 23.796  1.00 8.67  ? 151 ILE A N   1 
ATOM   1131 C  CA  . ILE A 1 173 ? 16.216 40.173 23.708  1.00 9.01  ? 151 ILE A CA  1 
ATOM   1132 C  C   . ILE A 1 173 ? 17.408 40.802 24.437  1.00 9.42  ? 151 ILE A C   1 
ATOM   1133 O  O   . ILE A 1 173 ? 18.196 40.092 25.070  1.00 9.88  ? 151 ILE A O   1 
ATOM   1134 C  CB  . ILE A 1 173 ? 16.598 39.924 22.229  1.00 9.11  ? 151 ILE A CB  1 
ATOM   1135 C  CG1 . ILE A 1 173 ? 15.422 39.313 21.440  1.00 9.27  ? 151 ILE A CG1 1 
ATOM   1136 C  CG2 . ILE A 1 173 ? 17.840 39.052 22.130  1.00 9.20  ? 151 ILE A CG2 1 
ATOM   1137 C  CD1 . ILE A 1 173 ? 14.869 38.011 21.980  1.00 9.43  ? 151 ILE A CD1 1 
ATOM   1138 N  N   . VAL A 1 174 ? 17.552 42.121 24.334  1.00 9.73  ? 152 VAL A N   1 
ATOM   1139 C  CA  . VAL A 1 174 ? 18.716 42.823 24.888  1.00 10.01 ? 152 VAL A CA  1 
ATOM   1140 C  C   . VAL A 1 174 ? 18.391 43.862 25.958  1.00 10.57 ? 152 VAL A C   1 
ATOM   1141 O  O   . VAL A 1 174 ? 19.300 44.442 26.550  1.00 11.43 ? 152 VAL A O   1 
ATOM   1142 C  CB  . VAL A 1 174 ? 19.561 43.502 23.783  1.00 9.88  ? 152 VAL A CB  1 
ATOM   1143 C  CG1 . VAL A 1 174 ? 19.935 42.495 22.714  1.00 9.89  ? 152 VAL A CG1 1 
ATOM   1144 C  CG2 . VAL A 1 174 ? 18.833 44.693 23.169  1.00 9.75  ? 152 VAL A CG2 1 
ATOM   1145 N  N   . GLY A 1 175 ? 17.116 44.119 26.208  1.00 10.82 ? 153 GLY A N   1 
ATOM   1146 C  CA  . GLY A 1 175 ? 16.765 45.033 27.288  1.00 11.35 ? 153 GLY A CA  1 
ATOM   1147 C  C   . GLY A 1 175 ? 16.819 46.480 26.860  1.00 11.38 ? 153 GLY A C   1 
ATOM   1148 O  O   . GLY A 1 175 ? 17.284 46.806 25.759  1.00 12.04 ? 153 GLY A O   1 
ATOM   1149 N  N   . PRO A 1 176 ? 16.370 47.371 27.744  1.00 10.85 ? 154 PRO A N   1 
ATOM   1150 C  CA  . PRO A 1 176 ? 15.858 48.654 27.280  1.00 10.37 ? 154 PRO A CA  1 
ATOM   1151 C  C   . PRO A 1 176 ? 16.885 49.667 26.781  1.00 9.81  ? 154 PRO A C   1 
ATOM   1152 O  O   . PRO A 1 176 ? 16.693 50.227 25.712  1.00 9.50  ? 154 PRO A O   1 
ATOM   1153 C  CB  . PRO A 1 176 ? 15.103 49.194 28.500  1.00 10.45 ? 154 PRO A CB  1 
ATOM   1154 C  CG  . PRO A 1 176 ? 15.723 48.513 29.668  1.00 10.64 ? 154 PRO A CG  1 
ATOM   1155 C  CD  . PRO A 1 176 ? 16.165 47.166 29.189  1.00 10.73 ? 154 PRO A CD  1 
ATOM   1156 N  N   . LYS A 1 177 ? 17.944 49.916 27.549  1.00 9.37  ? 155 LYS A N   1 
ATOM   1157 C  CA  . LYS A 1 177 ? 18.923 50.951 27.185  1.00 9.10  ? 155 LYS A CA  1 
ATOM   1158 C  C   . LYS A 1 177 ? 19.597 50.637 25.855  1.00 8.63  ? 155 LYS A C   1 
ATOM   1159 O  O   . LYS A 1 177 ? 19.744 51.505 24.995  1.00 8.24  ? 155 LYS A O   1 
ATOM   1160 C  CB  . LYS A 1 177 ? 20.002 51.066 28.261  1.00 9.37  ? 155 LYS A CB  1 
ATOM   1161 C  CG  . LYS A 1 177 ? 19.506 51.581 29.601  1.00 9.78  ? 155 LYS A CG  1 
ATOM   1162 C  CD  . LYS A 1 177 ? 19.684 53.074 29.727  1.00 9.73  ? 155 LYS A CD  1 
ATOM   1163 C  CE  . LYS A 1 177 ? 19.485 53.550 31.154  1.00 9.64  ? 155 LYS A CE  1 
ATOM   1164 N  NZ  . LYS A 1 177 ? 19.385 55.033 31.137  1.00 9.54  ? 155 LYS A NZ  1 
ATOM   1165 N  N   . ILE A 1 178 ? 20.012 49.384 25.701  1.00 8.44  ? 156 ILE A N   1 
ATOM   1166 C  CA  . ILE A 1 178 ? 20.735 48.960 24.510  1.00 8.42  ? 156 ILE A CA  1 
ATOM   1167 C  C   . ILE A 1 178 ? 19.802 48.940 23.298  1.00 8.07  ? 156 ILE A C   1 
ATOM   1168 O  O   . ILE A 1 178 ? 20.192 49.355 22.207  1.00 7.71  ? 156 ILE A O   1 
ATOM   1169 C  CB  . ILE A 1 178 ? 21.404 47.580 24.727  1.00 8.92  ? 156 ILE A CB  1 
ATOM   1170 C  CG1 . ILE A 1 178 ? 22.370 47.620 25.921  1.00 9.36  ? 156 ILE A CG1 1 
ATOM   1171 C  CG2 . ILE A 1 178 ? 22.124 47.127 23.467  1.00 9.01  ? 156 ILE A CG2 1 
ATOM   1172 C  CD1 . ILE A 1 178 ? 23.430 48.685 25.841  1.00 9.58  ? 156 ILE A CD1 1 
ATOM   1173 N  N   . ALA A 1 179 ? 18.566 48.490 23.494  1.00 7.83  ? 157 ALA A N   1 
ATOM   1174 C  CA  . ALA A 1 179 ? 17.579 48.480 22.411  1.00 7.77  ? 157 ALA A CA  1 
ATOM   1175 C  C   . ALA A 1 179 ? 17.280 49.891 21.918  1.00 7.80  ? 157 ALA A C   1 
ATOM   1176 O  O   . ALA A 1 179 ? 17.161 50.134 20.716  1.00 7.66  ? 157 ALA A O   1 
ATOM   1177 C  CB  . ALA A 1 179 ? 16.293 47.814 22.864  1.00 7.82  ? 157 ALA A CB  1 
ATOM   1178 N  N   . LYS A 1 180 ? 17.147 50.825 22.852  1.00 7.90  ? 158 LYS A N   1 
ATOM   1179 C  CA  . LYS A 1 180 ? 16.866 52.209 22.483  1.00 8.11  ? 158 LYS A CA  1 
ATOM   1180 C  C   . LYS A 1 180 ? 18.004 52.829 21.678  1.00 8.00  ? 158 LYS A C   1 
ATOM   1181 O  O   . LYS A 1 180 ? 17.764 53.511 20.689  1.00 8.02  ? 158 LYS A O   1 
ATOM   1182 C  CB  . LYS A 1 180 ? 16.561 53.045 23.720  1.00 8.46  ? 158 LYS A CB  1 
ATOM   1183 C  CG  . LYS A 1 180 ? 15.190 52.734 24.295  1.00 8.85  ? 158 LYS A CG  1 
ATOM   1184 C  CD  . LYS A 1 180 ? 14.778 53.769 25.302  1.00 9.20  ? 158 LYS A CD  1 
ATOM   1185 C  CE  . LYS A 1 180 ? 13.385 53.514 25.827  1.00 9.31  ? 158 LYS A CE  1 
ATOM   1186 N  NZ  . LYS A 1 180 ? 13.114 54.380 26.998  1.00 9.59  ? 158 LYS A NZ  1 
ATOM   1187 N  N   . GLU A 1 181 ? 19.238 52.585 22.103  1.00 7.87  ? 159 GLU A N   1 
ATOM   1188 C  CA  . GLU A 1 181 ? 20.402 53.066 21.372  1.00 7.83  ? 159 GLU A CA  1 
ATOM   1189 C  C   . GLU A 1 181 ? 20.436 52.519 19.947  1.00 7.66  ? 159 GLU A C   1 
ATOM   1190 O  O   . GLU A 1 181 ? 20.590 53.271 18.991  1.00 7.59  ? 159 GLU A O   1 
ATOM   1191 C  CB  . GLU A 1 181 ? 21.688 52.688 22.113  1.00 8.15  ? 159 GLU A CB  1 
ATOM   1192 C  CG  . GLU A 1 181 ? 22.959 53.011 21.345  1.00 8.56  ? 159 GLU A CG  1 
ATOM   1193 C  CD  . GLU A 1 181 ? 24.211 52.535 22.041  1.00 8.85  ? 159 GLU A CD  1 
ATOM   1194 O  OE1 . GLU A 1 181 ? 24.111 51.849 23.083  1.00 8.92  ? 159 GLU A OE1 1 
ATOM   1195 O  OE2 . GLU A 1 181 ? 25.307 52.844 21.529  1.00 9.49  ? 159 GLU A OE2 1 
ATOM   1196 N  N   . ILE A 1 182 ? 20.294 51.207 19.802  1.00 7.37  ? 160 ILE A N   1 
ATOM   1197 C  CA  . ILE A 1 182 ? 20.407 50.596 18.478  1.00 7.24  ? 160 ILE A CA  1 
ATOM   1198 C  C   . ILE A 1 182 ? 19.313 51.107 17.539  1.00 7.32  ? 160 ILE A C   1 
ATOM   1199 O  O   . ILE A 1 182 ? 19.595 51.466 16.395  1.00 7.39  ? 160 ILE A O   1 
ATOM   1200 C  CB  . ILE A 1 182 ? 20.406 49.055 18.553  1.00 7.20  ? 160 ILE A CB  1 
ATOM   1201 C  CG1 . ILE A 1 182 ? 21.724 48.563 19.156  1.00 7.19  ? 160 ILE A CG1 1 
ATOM   1202 C  CG2 . ILE A 1 182 ? 20.207 48.443 17.171  1.00 7.16  ? 160 ILE A CG2 1 
ATOM   1203 C  CD1 . ILE A 1 182 ? 21.719 47.102 19.544  1.00 7.22  ? 160 ILE A CD1 1 
ATOM   1204 N  N   . ILE A 1 183 ? 18.078 51.170 18.026  1.00 7.38  ? 161 ILE A N   1 
ATOM   1205 C  CA  . ILE A 1 183 ? 16.953 51.550 17.172  1.00 7.55  ? 161 ILE A CA  1 
ATOM   1206 C  C   . ILE A 1 183 ? 16.875 53.060 16.939  1.00 7.83  ? 161 ILE A C   1 
ATOM   1207 O  O   . ILE A 1 183 ? 16.707 53.496 15.798  1.00 7.93  ? 161 ILE A O   1 
ATOM   1208 C  CB  . ILE A 1 183 ? 15.625 50.962 17.699  1.00 7.55  ? 161 ILE A CB  1 
ATOM   1209 C  CG1 . ILE A 1 183 ? 15.582 49.466 17.366  1.00 7.58  ? 161 ILE A CG1 1 
ATOM   1210 C  CG2 . ILE A 1 183 ? 14.420 51.675 17.092  1.00 7.52  ? 161 ILE A CG2 1 
ATOM   1211 C  CD1 . ILE A 1 183 ? 14.532 48.676 18.111  1.00 7.65  ? 161 ILE A CD1 1 
ATOM   1212 N  N   . LEU A 1 184 ? 17.013 53.863 17.989  1.00 8.14  ? 162 LEU A N   1 
ATOM   1213 C  CA  . LEU A 1 184 ? 16.879 55.320 17.819  1.00 8.50  ? 162 LEU A CA  1 
ATOM   1214 C  C   . LEU A 1 184 ? 18.032 55.944 17.026  1.00 8.84  ? 162 LEU A C   1 
ATOM   1215 O  O   . LEU A 1 184 ? 17.843 56.979 16.375  1.00 9.26  ? 162 LEU A O   1 
ATOM   1216 C  CB  . LEU A 1 184 ? 16.715 56.030 19.163  1.00 8.51  ? 162 LEU A CB  1 
ATOM   1217 C  CG  . LEU A 1 184 ? 15.435 55.718 19.936  1.00 8.56  ? 162 LEU A CG  1 
ATOM   1218 C  CD1 . LEU A 1 184 ? 15.509 56.338 21.328  1.00 8.62  ? 162 LEU A CD1 1 
ATOM   1219 C  CD2 . LEU A 1 184 ? 14.205 56.202 19.188  1.00 8.72  ? 162 LEU A CD2 1 
ATOM   1220 N  N   . LEU A 1 185 ? 19.208 55.325 17.064  1.00 9.20  ? 163 LEU A N   1 
ATOM   1221 C  CA  . LEU A 1 185 ? 20.350 55.810 16.284  1.00 9.61  ? 163 LEU A CA  1 
ATOM   1222 C  C   . LEU A 1 185 ? 20.522 55.082 14.956  1.00 9.92  ? 163 LEU A C   1 
ATOM   1223 O  O   . LEU A 1 185 ? 21.310 55.506 14.115  1.00 10.50 ? 163 LEU A O   1 
ATOM   1224 C  CB  . LEU A 1 185 ? 21.642 55.711 17.092  1.00 9.70  ? 163 LEU A CB  1 
ATOM   1225 C  CG  . LEU A 1 185 ? 21.628 56.402 18.456  1.00 9.88  ? 163 LEU A CG  1 
ATOM   1226 C  CD1 . LEU A 1 185 ? 22.977 56.260 19.145  1.00 10.00 ? 163 LEU A CD1 1 
ATOM   1227 C  CD2 . LEU A 1 185 ? 21.249 57.869 18.318  1.00 10.02 ? 163 LEU A CD2 1 
ATOM   1228 N  N   . GLY A 1 186 ? 19.786 53.996 14.758  1.00 10.06 ? 164 GLY A N   1 
ATOM   1229 C  CA  . GLY A 1 186 ? 19.933 53.206 13.543  1.00 10.21 ? 164 GLY A CA  1 
ATOM   1230 C  C   . GLY A 1 186 ? 21.297 52.555 13.440  1.00 10.58 ? 164 GLY A C   1 
ATOM   1231 O  O   . GLY A 1 186 ? 21.883 52.513 12.358  1.00 10.47 ? 164 GLY A O   1 
ATOM   1232 N  N   . GLU A 1 187 ? 21.803 52.035 14.559  1.00 10.90 ? 165 GLU A N   1 
ATOM   1233 C  CA  . GLU A 1 187 ? 23.104 51.362 14.571  1.00 11.57 ? 165 GLU A CA  1 
ATOM   1234 C  C   . GLU A 1 187 ? 23.064 50.174 13.626  1.00 11.42 ? 165 GLU A C   1 
ATOM   1235 O  O   . GLU A 1 187 ? 22.146 49.362 13.699  1.00 11.30 ? 165 GLU A O   1 
ATOM   1236 C  CB  . GLU A 1 187 ? 23.468 50.878 15.980  1.00 12.31 ? 165 GLU A CB  1 
ATOM   1237 C  CG  . GLU A 1 187 ? 23.726 51.987 16.986  1.00 13.39 ? 165 GLU A CG  1 
ATOM   1238 C  CD  . GLU A 1 187 ? 24.948 52.824 16.655  1.00 14.50 ? 165 GLU A CD  1 
ATOM   1239 O  OE1 . GLU A 1 187 ? 26.005 52.251 16.302  1.00 16.93 ? 165 GLU A OE1 1 
ATOM   1240 O  OE2 . GLU A 1 187 ? 24.862 54.062 16.754  1.00 15.89 ? 165 GLU A OE2 1 
ATOM   1241 N  N   . ASP A 1 188 ? 24.051 50.081 12.738  1.00 11.20 ? 166 ASP A N   1 
ATOM   1242 C  CA  . ASP A 1 188 ? 24.059 49.055 11.691  1.00 11.17 ? 166 ASP A CA  1 
ATOM   1243 C  C   . ASP A 1 188 ? 25.439 48.431 11.464  1.00 10.98 ? 166 ASP A C   1 
ATOM   1244 O  O   . ASP A 1 188 ? 25.682 47.824 10.420  1.00 10.56 ? 166 ASP A O   1 
ATOM   1245 C  CB  . ASP A 1 188 ? 23.523 49.645 10.378  1.00 11.41 ? 166 ASP A CB  1 
ATOM   1246 C  CG  . ASP A 1 188 ? 24.305 50.870 9.907   1.00 11.74 ? 166 ASP A CG  1 
ATOM   1247 O  OD1 . ASP A 1 188 ? 25.368 51.188 10.483  1.00 11.84 ? 166 ASP A OD1 1 
ATOM   1248 O  OD2 . ASP A 1 188 ? 23.844 51.535 8.950   1.00 12.34 ? 166 ASP A OD2 1 
ATOM   1249 N  N   . ARG A 1 189 ? 26.330 48.574 12.442  1.00 10.96 ? 167 ARG A N   1 
ATOM   1250 C  CA  . ARG A 1 189 ? 27.665 47.982 12.371  1.00 11.24 ? 167 ARG A CA  1 
ATOM   1251 C  C   . ARG A 1 189 ? 28.053 47.386 13.721  1.00 10.54 ? 167 ARG A C   1 
ATOM   1252 O  O   . ARG A 1 189 ? 29.224 47.406 14.108  1.00 10.62 ? 167 ARG A O   1 
ATOM   1253 C  CB  . ARG A 1 189 ? 28.697 49.031 11.933  1.00 12.11 ? 167 ARG A CB  1 
ATOM   1254 C  CG  . ARG A 1 189 ? 28.483 49.591 10.534  1.00 13.26 ? 167 ARG A CG  1 
ATOM   1255 C  CD  . ARG A 1 189 ? 28.768 48.565 9.445   1.00 14.42 ? 167 ARG A CD  1 
ATOM   1256 N  NE  . ARG A 1 189 ? 28.624 49.140 8.102   1.00 15.73 ? 167 ARG A NE  1 
ATOM   1257 C  CZ  . ARG A 1 189 ? 27.490 49.195 7.397   1.00 16.62 ? 167 ARG A CZ  1 
ATOM   1258 N  NH1 . ARG A 1 189 ? 26.344 48.699 7.872   1.00 16.77 ? 167 ARG A NH1 1 
ATOM   1259 N  NH2 . ARG A 1 189 ? 27.498 49.753 6.190   1.00 17.55 ? 167 ARG A NH2 1 
ATOM   1260 N  N   . VAL A 1 190 ? 27.066 46.851 14.439  1.00 9.65  ? 168 VAL A N   1 
ATOM   1261 C  CA  . VAL A 1 190 ? 27.314 46.263 15.748  1.00 9.17  ? 168 VAL A CA  1 
ATOM   1262 C  C   . VAL A 1 190 ? 28.079 44.958 15.527  1.00 8.92  ? 168 VAL A C   1 
ATOM   1263 O  O   . VAL A 1 190 ? 27.535 44.032 14.930  1.00 8.51  ? 168 VAL A O   1 
ATOM   1264 C  CB  . VAL A 1 190 ? 26.005 45.971 16.507  1.00 9.02  ? 168 VAL A CB  1 
ATOM   1265 C  CG1 . VAL A 1 190 ? 26.309 45.367 17.874  1.00 9.06  ? 168 VAL A CG1 1 
ATOM   1266 C  CG2 . VAL A 1 190 ? 25.167 47.239 16.658  1.00 9.10  ? 168 VAL A CG2 1 
ATOM   1267 N  N   . PRO A 1 191 ? 29.344 44.876 15.994  1.00 8.91  ? 169 PRO A N   1 
ATOM   1268 C  CA  . PRO A 1 191 ? 30.113 43.660 15.715  1.00 8.91  ? 169 PRO A CA  1 
ATOM   1269 C  C   . PRO A 1 191 ? 29.576 42.441 16.454  1.00 8.89  ? 169 PRO A C   1 
ATOM   1270 O  O   . PRO A 1 191 ? 28.972 42.575 17.520  1.00 8.48  ? 169 PRO A O   1 
ATOM   1271 C  CB  . PRO A 1 191 ? 31.531 44.001 16.207  1.00 9.08  ? 169 PRO A CB  1 
ATOM   1272 C  CG  . PRO A 1 191 ? 31.546 45.475 16.411  1.00 9.22  ? 169 PRO A CG  1 
ATOM   1273 C  CD  . PRO A 1 191 ? 30.142 45.866 16.738  1.00 9.05  ? 169 PRO A CD  1 
ATOM   1274 N  N   . ALA A 1 192 ? 29.809 41.263 15.889  1.00 9.08  ? 170 ALA A N   1 
ATOM   1275 C  CA  . ALA A 1 192 ? 29.371 40.015 16.509  1.00 9.26  ? 170 ALA A CA  1 
ATOM   1276 C  C   . ALA A 1 192 ? 29.787 39.911 17.976  1.00 9.56  ? 170 ALA A C   1 
ATOM   1277 O  O   . ALA A 1 192 ? 29.002 39.463 18.804  1.00 9.36  ? 170 ALA A O   1 
ATOM   1278 C  CB  . ALA A 1 192 ? 29.896 38.818 15.728  1.00 9.30  ? 170 ALA A CB  1 
ATOM   1279 N  N   . ARG A 1 193 ? 31.011 40.326 18.305  1.00 10.25 ? 171 ARG A N   1 
ATOM   1280 C  CA  . ARG A 1 193 ? 31.475 40.279 19.693  1.00 10.87 ? 171 ARG A CA  1 
ATOM   1281 C  C   . ARG A 1 193 ? 30.581 41.083 20.630  1.00 9.73  ? 171 ARG A C   1 
ATOM   1282 O  O   . ARG A 1 193 ? 30.243 40.626 21.721  1.00 9.22  ? 171 ARG A O   1 
ATOM   1283 C  CB  . ARG A 1 193 ? 32.911 40.789 19.802  1.00 12.64 ? 171 ARG A CB  1 
ATOM   1284 C  CG  . ARG A 1 193 ? 33.946 39.856 19.211  1.00 14.87 ? 171 ARG A CG  1 
ATOM   1285 C  CD  . ARG A 1 193 ? 34.054 38.557 19.988  1.00 17.12 ? 171 ARG A CD  1 
ATOM   1286 N  NE  . ARG A 1 193 ? 35.410 38.020 19.961  1.00 19.87 ? 171 ARG A NE  1 
ATOM   1287 C  CZ  . ARG A 1 193 ? 35.759 36.812 20.402  1.00 22.19 ? 171 ARG A CZ  1 
ATOM   1288 N  NH1 . ARG A 1 193 ? 34.853 35.973 20.897  1.00 22.97 ? 171 ARG A NH1 1 
ATOM   1289 N  NH2 . ARG A 1 193 ? 37.031 36.433 20.330  1.00 23.32 ? 171 ARG A NH2 1 
ATOM   1290 N  N   . ARG A 1 194 ? 30.203 42.282 20.199  1.00 8.76  ? 172 ARG A N   1 
ATOM   1291 C  CA  . ARG A 1 194 ? 29.317 43.133 20.989  1.00 8.24  ? 172 ARG A CA  1 
ATOM   1292 C  C   . ARG A 1 194 ? 27.907 42.543 21.043  1.00 7.92  ? 172 ARG A C   1 
ATOM   1293 O  O   . ARG A 1 194 ? 27.254 42.559 22.089  1.00 7.79  ? 172 ARG A O   1 
ATOM   1294 C  CB  . ARG A 1 194 ? 29.292 44.546 20.411  1.00 8.13  ? 172 ARG A CB  1 
ATOM   1295 C  CG  . ARG A 1 194 ? 28.356 45.508 21.115  1.00 8.04  ? 172 ARG A CG  1 
ATOM   1296 C  CD  . ARG A 1 194 ? 28.649 45.604 22.599  1.00 8.05  ? 172 ARG A CD  1 
ATOM   1297 N  NE  . ARG A 1 194 ? 27.757 46.548 23.250  1.00 8.09  ? 172 ARG A NE  1 
ATOM   1298 C  CZ  . ARG A 1 194 ? 27.536 46.609 24.563  1.00 8.10  ? 172 ARG A CZ  1 
ATOM   1299 N  NH1 . ARG A 1 194 ? 28.143 45.780 25.411  1.00 8.12  ? 172 ARG A NH1 1 
ATOM   1300 N  NH2 . ARG A 1 194 ? 26.681 47.508 25.026  1.00 8.21  ? 172 ARG A NH2 1 
ATOM   1301 N  N   . ALA A 1 195 ? 27.445 42.019 19.913  1.00 7.63  ? 173 ALA A N   1 
ATOM   1302 C  CA  . ALA A 1 195 ? 26.147 41.344 19.860  1.00 7.48  ? 173 ALA A CA  1 
ATOM   1303 C  C   . ALA A 1 195 ? 26.091 40.187 20.863  1.00 7.58  ? 173 ALA A C   1 
ATOM   1304 O  O   . ALA A 1 195 ? 25.056 39.953 21.487  1.00 7.40  ? 173 ALA A O   1 
ATOM   1305 C  CB  . ALA A 1 195 ? 25.856 40.851 18.451  1.00 7.48  ? 173 ALA A CB  1 
ATOM   1306 N  N   . ALA A 1 196 ? 27.214 39.489 21.037  1.00 7.60  ? 174 ALA A N   1 
ATOM   1307 C  CA  . ALA A 1 196 ? 27.303 38.412 22.020  1.00 7.81  ? 174 ALA A CA  1 
ATOM   1308 C  C   . ALA A 1 196 ? 27.249 38.937 23.458  1.00 8.10  ? 174 ALA A C   1 
ATOM   1309 O  O   . ALA A 1 196 ? 26.608 38.336 24.317  1.00 8.29  ? 174 ALA A O   1 
ATOM   1310 C  CB  . ALA A 1 196 ? 28.565 37.591 21.798  1.00 7.80  ? 174 ALA A CB  1 
ATOM   1311 N  N   . GLU A 1 197 ? 27.911 40.064 23.719  1.00 8.50  ? 175 GLU A N   1 
ATOM   1312 C  CA  . GLU A 1 197 ? 27.891 40.673 25.054  1.00 8.79  ? 175 GLU A CA  1 
ATOM   1313 C  C   . GLU A 1 197 ? 26.487 41.067 25.512  1.00 8.70  ? 175 GLU A C   1 
ATOM   1314 O  O   . GLU A 1 197 ? 26.174 40.990 26.705  1.00 8.93  ? 175 GLU A O   1 
ATOM   1315 C  CB  . GLU A 1 197 ? 28.772 41.922 25.093  1.00 9.36  ? 175 GLU A CB  1 
ATOM   1316 C  CG  . GLU A 1 197 ? 30.258 41.644 24.975  1.00 9.93  ? 175 GLU A CG  1 
ATOM   1317 C  CD  . GLU A 1 197 ? 31.086 42.907 24.801  1.00 10.62 ? 175 GLU A CD  1 
ATOM   1318 O  OE1 . GLU A 1 197 ? 30.547 44.038 24.930  1.00 11.05 ? 175 GLU A OE1 1 
ATOM   1319 O  OE2 . GLU A 1 197 ? 32.298 42.762 24.538  1.00 11.87 ? 175 GLU A OE2 1 
ATOM   1320 N  N   . ILE A 1 198 ? 25.651 41.497 24.571  1.00 8.49  ? 176 ILE A N   1 
ATOM   1321 C  CA  . ILE A 1 198 ? 24.330 42.034 24.914  1.00 8.40  ? 176 ILE A CA  1 
ATOM   1322 C  C   . ILE A 1 198 ? 23.218 40.988 24.826  1.00 8.58  ? 176 ILE A C   1 
ATOM   1323 O  O   . ILE A 1 198 ? 22.080 41.276 25.176  1.00 8.35  ? 176 ILE A O   1 
ATOM   1324 C  CB  . ILE A 1 198 ? 23.994 43.287 24.071  1.00 8.29  ? 176 ILE A CB  1 
ATOM   1325 C  CG1 . ILE A 1 198 ? 23.834 42.939 22.582  1.00 8.23  ? 176 ILE A CG1 1 
ATOM   1326 C  CG2 . ILE A 1 198 ? 25.077 44.343 24.270  1.00 8.39  ? 176 ILE A CG2 1 
ATOM   1327 C  CD1 . ILE A 1 198 ? 23.596 44.135 21.674  1.00 8.33  ? 176 ILE A CD1 1 
ATOM   1328 N  N   . GLY A 1 199 ? 23.554 39.777 24.386  1.00 8.91  ? 177 GLY A N   1 
ATOM   1329 C  CA  . GLY A 1 199 ? 22.603 38.662 24.382  1.00 9.39  ? 177 GLY A CA  1 
ATOM   1330 C  C   . GLY A 1 199 ? 21.884 38.419 23.064  1.00 9.99  ? 177 GLY A C   1 
ATOM   1331 O  O   . GLY A 1 199 ? 20.985 37.577 22.999  1.00 9.77  ? 177 GLY A O   1 
HETATM 1332 N  N   . MSE A 1 200 ? 22.282 39.142 22.016  1.00 10.76 ? 178 MSE A N   1 
HETATM 1333 C  CA  . MSE A 1 200 ? 21.697 38.982 20.673  1.00 11.86 ? 178 MSE A CA  1 
HETATM 1334 C  C   . MSE A 1 200 ? 22.269 37.769 19.980  1.00 10.58 ? 178 MSE A C   1 
HETATM 1335 O  O   . MSE A 1 200 ? 21.613 37.161 19.135  1.00 10.09 ? 178 MSE A O   1 
HETATM 1336 C  CB  . MSE A 1 200 ? 21.970 40.251 19.853  1.00 15.05 ? 178 MSE A CB  1 
HETATM 1337 C  CG  . MSE A 1 200 ? 21.566 40.116 18.385  1.00 18.00 ? 178 MSE A CG  1 
HETATM 1338 SE SE  . MSE A 1 200 ? 21.930 41.768 17.370  1.00 27.67 ? 178 MSE A SE  1 
HETATM 1339 C  CE  . MSE A 1 200 ? 21.576 43.084 18.780  1.00 23.52 ? 178 MSE A CE  1 
ATOM   1340 N  N   . VAL A 1 201 ? 23.514 37.434 20.309  1.00 9.31  ? 179 VAL A N   1 
ATOM   1341 C  CA  . VAL A 1 201 ? 24.213 36.302 19.712  1.00 8.85  ? 179 VAL A CA  1 
ATOM   1342 C  C   . VAL A 1 201 ? 24.659 35.360 20.829  1.00 8.60  ? 179 VAL A C   1 
ATOM   1343 O  O   . VAL A 1 201 ? 25.212 35.804 21.832  1.00 8.50  ? 179 VAL A O   1 
ATOM   1344 C  CB  . VAL A 1 201 ? 25.434 36.779 18.893  1.00 8.75  ? 179 VAL A CB  1 
ATOM   1345 C  CG1 . VAL A 1 201 ? 26.359 35.619 18.535  1.00 8.79  ? 179 VAL A CG1 1 
ATOM   1346 C  CG2 . VAL A 1 201 ? 24.972 37.503 17.634  1.00 8.78  ? 179 VAL A CG2 1 
ATOM   1347 N  N   . ASN A 1 202 ? 24.430 34.066 20.638  1.00 8.30  ? 180 ASN A N   1 
ATOM   1348 C  CA  . ASN A 1 202 ? 24.815 33.053 21.619  1.00 8.39  ? 180 ASN A CA  1 
ATOM   1349 C  C   . ASN A 1 202 ? 26.303 32.761 21.598  1.00 8.74  ? 180 ASN A C   1 
ATOM   1350 O  O   . ASN A 1 202 ? 26.936 32.682 22.651  1.00 8.65  ? 180 ASN A O   1 
ATOM   1351 C  CB  . ASN A 1 202 ? 24.069 31.742 21.375  1.00 8.16  ? 180 ASN A CB  1 
ATOM   1352 C  CG  . ASN A 1 202 ? 22.607 31.829 21.743  1.00 7.93  ? 180 ASN A CG  1 
ATOM   1353 O  OD1 . ASN A 1 202 ? 22.198 31.406 22.831  1.00 8.17  ? 180 ASN A OD1 1 
ATOM   1354 N  ND2 . ASN A 1 202 ? 21.820 32.403 20.870  1.00 7.58  ? 180 ASN A ND2 1 
ATOM   1355 N  N   . ARG A 1 203 ? 26.843 32.573 20.397  1.00 9.22  ? 181 ARG A N   1 
ATOM   1356 C  CA  . ARG A 1 203 ? 28.235 32.162 20.208  1.00 10.02 ? 181 ARG A CA  1 
ATOM   1357 C  C   . ARG A 1 203 ? 28.846 32.842 19.002  1.00 10.30 ? 181 ARG A C   1 
ATOM   1358 O  O   . ARG A 1 203 ? 28.215 32.923 17.946  1.00 9.82  ? 181 ARG A O   1 
ATOM   1359 C  CB  . ARG A 1 203 ? 28.313 30.658 19.963  1.00 10.59 ? 181 ARG A CB  1 
ATOM   1360 C  CG  . ARG A 1 203 ? 27.677 29.804 21.034  1.00 11.17 ? 181 ARG A CG  1 
ATOM   1361 C  CD  . ARG A 1 203 ? 27.836 28.329 20.724  1.00 11.88 ? 181 ARG A CD  1 
ATOM   1362 N  NE  . ARG A 1 203 ? 27.137 27.529 21.713  1.00 12.59 ? 181 ARG A NE  1 
ATOM   1363 C  CZ  . ARG A 1 203 ? 27.088 26.201 21.730  1.00 13.11 ? 181 ARG A CZ  1 
ATOM   1364 N  NH1 . ARG A 1 203 ? 27.705 25.481 20.794  1.00 13.46 ? 181 ARG A NH1 1 
ATOM   1365 N  NH2 . ARG A 1 203 ? 26.418 25.592 22.699  1.00 13.40 ? 181 ARG A NH2 1 
ATOM   1366 N  N   . VAL A 1 204 ? 30.081 33.311 19.159  1.00 10.94 ? 182 VAL A N   1 
ATOM   1367 C  CA  . VAL A 1 204 ? 30.884 33.759 18.033  1.00 11.58 ? 182 VAL A CA  1 
ATOM   1368 C  C   . VAL A 1 204 ? 31.875 32.652 17.707  1.00 12.96 ? 182 VAL A C   1 
ATOM   1369 O  O   . VAL A 1 204 ? 32.605 32.184 18.587  1.00 12.76 ? 182 VAL A O   1 
ATOM   1370 C  CB  . VAL A 1 204 ? 31.633 35.067 18.331  1.00 11.33 ? 182 VAL A CB  1 
ATOM   1371 C  CG1 . VAL A 1 204 ? 32.502 35.458 17.142  1.00 11.26 ? 182 VAL A CG1 1 
ATOM   1372 C  CG2 . VAL A 1 204 ? 30.645 36.179 18.651  1.00 11.35 ? 182 VAL A CG2 1 
ATOM   1373 N  N   . VAL A 1 205 ? 31.887 32.232 16.448  1.00 15.06 ? 183 VAL A N   1 
ATOM   1374 C  CA  . VAL A 1 205 ? 32.713 31.109 16.011  1.00 17.47 ? 183 VAL A CA  1 
ATOM   1375 C  C   . VAL A 1 205 ? 33.674 31.520 14.904  1.00 19.69 ? 183 VAL A C   1 
ATOM   1376 O  O   . VAL A 1 205 ? 33.501 32.555 14.271  1.00 19.94 ? 183 VAL A O   1 
ATOM   1377 C  CB  . VAL A 1 205 ? 31.852 29.931 15.516  1.00 17.97 ? 183 VAL A CB  1 
ATOM   1378 C  CG1 . VAL A 1 205 ? 30.969 29.414 16.639  1.00 18.59 ? 183 VAL A CG1 1 
ATOM   1379 C  CG2 . VAL A 1 205 ? 31.007 30.321 14.311  1.00 18.22 ? 183 VAL A CG2 1 
ATOM   1380 N  N   . ASP A 1 206 ? 34.677 30.680 14.669  1.00 22.95 ? 184 ASP A N   1 
ATOM   1381 C  CA  . ASP A 1 206 ? 35.614 30.870 13.562  1.00 25.86 ? 184 ASP A CA  1 
ATOM   1382 C  C   . ASP A 1 206 ? 34.874 30.838 12.223  1.00 26.39 ? 184 ASP A C   1 
ATOM   1383 O  O   . ASP A 1 206 ? 33.939 30.056 12.043  1.00 26.95 ? 184 ASP A O   1 
ATOM   1384 C  CB  . ASP A 1 206 ? 36.681 29.773 13.600  1.00 27.73 ? 184 ASP A CB  1 
ATOM   1385 C  CG  . ASP A 1 206 ? 37.826 30.020 12.629  1.00 29.98 ? 184 ASP A CG  1 
ATOM   1386 O  OD1 . ASP A 1 206 ? 37.717 30.904 11.753  1.00 31.55 ? 184 ASP A OD1 1 
ATOM   1387 O  OD2 . ASP A 1 206 ? 38.853 29.317 12.750  1.00 33.18 ? 184 ASP A OD2 1 
ATOM   1388 N  N   . GLY A 1 207 ? 35.305 31.689 11.294  1.00 27.41 ? 185 GLY A N   1 
ATOM   1389 C  CA  . GLY A 1 207 ? 34.677 31.813 9.976   1.00 27.77 ? 185 GLY A CA  1 
ATOM   1390 C  C   . GLY A 1 207 ? 34.566 30.506 9.217   1.00 28.17 ? 185 GLY A C   1 
ATOM   1391 O  O   . GLY A 1 207 ? 33.535 30.215 8.601   1.00 29.08 ? 185 GLY A O   1 
ATOM   1392 N  N   . ASP A 1 208 ? 35.624 29.704 9.274   1.00 28.02 ? 186 ASP A N   1 
ATOM   1393 C  CA  . ASP A 1 208 ? 35.640 28.413 8.584   1.00 28.03 ? 186 ASP A CA  1 
ATOM   1394 C  C   . ASP A 1 208 ? 34.772 27.345 9.263   1.00 25.72 ? 186 ASP A C   1 
ATOM   1395 O  O   . ASP A 1 208 ? 34.603 26.259 8.713   1.00 26.98 ? 186 ASP A O   1 
ATOM   1396 C  CB  . ASP A 1 208 ? 37.081 27.901 8.414   1.00 29.83 ? 186 ASP A CB  1 
ATOM   1397 C  CG  . ASP A 1 208 ? 37.824 27.760 9.737   1.00 31.30 ? 186 ASP A CG  1 
ATOM   1398 O  OD1 . ASP A 1 208 ? 37.395 26.953 10.590  1.00 33.40 ? 186 ASP A OD1 1 
ATOM   1399 O  OD2 . ASP A 1 208 ? 38.850 28.451 9.920   1.00 33.26 ? 186 ASP A OD2 1 
ATOM   1400 N  N   . GLY A 1 209 ? 34.223 27.646 10.442  1.00 22.39 ? 187 GLY A N   1 
ATOM   1401 C  CA  . GLY A 1 209 ? 33.481 26.657 11.213  1.00 20.00 ? 187 GLY A CA  1 
ATOM   1402 C  C   . GLY A 1 209 ? 32.012 26.951 11.470  1.00 17.82 ? 187 GLY A C   1 
ATOM   1403 O  O   . GLY A 1 209 ? 31.381 26.241 12.246  1.00 17.61 ? 187 GLY A O   1 
ATOM   1404 N  N   . LEU A 1 210 ? 31.455 27.975 10.826  1.00 16.11 ? 188 LEU A N   1 
ATOM   1405 C  CA  . LEU A 1 210 ? 30.067 28.382 11.107  1.00 14.79 ? 188 LEU A CA  1 
ATOM   1406 C  C   . LEU A 1 210 ? 29.038 27.314 10.743  1.00 14.14 ? 188 LEU A C   1 
ATOM   1407 O  O   . LEU A 1 210 ? 28.175 26.975 11.558  1.00 13.21 ? 188 LEU A O   1 
ATOM   1408 C  CB  . LEU A 1 210 ? 29.718 29.680 10.381  1.00 14.64 ? 188 LEU A CB  1 
ATOM   1409 C  CG  . LEU A 1 210 ? 28.304 30.217 10.648  1.00 14.70 ? 188 LEU A CG  1 
ATOM   1410 C  CD1 . LEU A 1 210 ? 28.152 30.690 12.082  1.00 14.77 ? 188 LEU A CD1 1 
ATOM   1411 C  CD2 . LEU A 1 210 ? 27.969 31.337 9.686   1.00 14.64 ? 188 LEU A CD2 1 
ATOM   1412 N  N   . ASP A 1 211 ? 29.101 26.806 9.517   1.00 13.68 ? 189 ASP A N   1 
ATOM   1413 C  CA  . ASP A 1 211 ? 28.135 25.798 9.084   1.00 13.69 ? 189 ASP A CA  1 
ATOM   1414 C  C   . ASP A 1 211 ? 28.250 24.536 9.937   1.00 12.77 ? 189 ASP A C   1 
ATOM   1415 O  O   . ASP A 1 211 ? 27.239 23.942 10.304  1.00 12.23 ? 189 ASP A O   1 
ATOM   1416 C  CB  . ASP A 1 211 ? 28.300 25.459 7.601   1.00 14.64 ? 189 ASP A CB  1 
ATOM   1417 C  CG  . ASP A 1 211 ? 27.778 26.556 6.688   1.00 15.57 ? 189 ASP A CG  1 
ATOM   1418 O  OD1 . ASP A 1 211 ? 26.651 27.043 6.903   1.00 16.62 ? 189 ASP A OD1 1 
ATOM   1419 O  OD2 . ASP A 1 211 ? 28.490 26.922 5.735   1.00 17.39 ? 189 ASP A OD2 1 
ATOM   1420 N  N   . ALA A 1 212 ? 29.478 24.139 10.263  1.00 12.18 ? 190 ALA A N   1 
ATOM   1421 C  CA  . ALA A 1 212 ? 29.700 22.946 11.083  1.00 12.02 ? 190 ALA A CA  1 
ATOM   1422 C  C   . ALA A 1 212 ? 29.146 23.117 12.496  1.00 11.83 ? 190 ALA A C   1 
ATOM   1423 O  O   . ALA A 1 212 ? 28.567 22.189 13.053  1.00 11.33 ? 190 ALA A O   1 
ATOM   1424 C  CB  . ALA A 1 212 ? 31.184 22.611 11.140  1.00 12.11 ? 190 ALA A CB  1 
ATOM   1425 N  N   . GLU A 1 213 ? 29.328 24.301 13.074  1.00 11.84 ? 191 GLU A N   1 
ATOM   1426 C  CA  . GLU A 1 213 ? 28.823 24.575 14.423  1.00 12.16 ? 191 GLU A CA  1 
ATOM   1427 C  C   . GLU A 1 213 ? 27.296 24.587 14.452  1.00 11.22 ? 191 GLU A C   1 
ATOM   1428 O  O   . GLU A 1 213 ? 26.691 24.042 15.374  1.00 10.62 ? 191 GLU A O   1 
ATOM   1429 C  CB  . GLU A 1 213 ? 29.378 25.901 14.958  1.00 13.29 ? 191 GLU A CB  1 
ATOM   1430 C  CG  . GLU A 1 213 ? 28.868 26.302 16.343  1.00 14.65 ? 191 GLU A CG  1 
ATOM   1431 C  CD  . GLU A 1 213 ? 29.537 25.565 17.490  1.00 15.96 ? 191 GLU A CD  1 
ATOM   1432 O  OE1 . GLU A 1 213 ? 30.067 24.450 17.285  1.00 17.44 ? 191 GLU A OE1 1 
ATOM   1433 O  OE2 . GLU A 1 213 ? 29.526 26.109 18.618  1.00 17.50 ? 191 GLU A OE2 1 
ATOM   1434 N  N   . ALA A 1 214 ? 26.671 25.195 13.447  1.00 10.47 ? 192 ALA A N   1 
ATOM   1435 C  CA  . ALA A 1 214 ? 25.207 25.215 13.391  1.00 10.22 ? 192 ALA A CA  1 
ATOM   1436 C  C   . ALA A 1 214 ? 24.667 23.794 13.271  1.00 10.29 ? 192 ALA A C   1 
ATOM   1437 O  O   . ALA A 1 214 ? 23.677 23.444 13.908  1.00 9.93  ? 192 ALA A O   1 
ATOM   1438 C  CB  . ALA A 1 214 ? 24.717 26.074 12.232  1.00 10.13 ? 192 ALA A CB  1 
ATOM   1439 N  N   . LEU A 1 215 ? 25.328 22.976 12.458  1.00 10.58 ? 193 LEU A N   1 
ATOM   1440 C  CA  . LEU A 1 215 ? 24.917 21.585 12.276  1.00 11.08 ? 193 LEU A CA  1 
ATOM   1441 C  C   . LEU A 1 215 ? 25.115 20.755 13.553  1.00 11.14 ? 193 LEU A C   1 
ATOM   1442 O  O   . LEU A 1 215 ? 24.270 19.923 13.883  1.00 10.67 ? 193 LEU A O   1 
ATOM   1443 C  CB  . LEU A 1 215 ? 25.673 20.961 11.095  1.00 11.69 ? 193 LEU A CB  1 
ATOM   1444 C  CG  . LEU A 1 215 ? 25.109 19.665 10.514  1.00 12.37 ? 193 LEU A CG  1 
ATOM   1445 C  CD1 . LEU A 1 215 ? 23.691 19.857 9.993   1.00 12.45 ? 193 LEU A CD1 1 
ATOM   1446 C  CD2 . LEU A 1 215 ? 26.012 19.156 9.399   1.00 12.75 ? 193 LEU A CD2 1 
ATOM   1447 N  N   . ARG A 1 216 ? 26.214 20.981 14.272  1.00 11.58 ? 194 ARG A N   1 
ATOM   1448 C  CA  . ARG A 1 216 ? 26.435 20.299 15.554  1.00 11.98 ? 194 ARG A CA  1 
ATOM   1449 C  C   . ARG A 1 216 ? 25.321 20.625 16.542  1.00 10.95 ? 194 ARG A C   1 
ATOM   1450 O  O   . ARG A 1 216 ? 24.795 19.745 17.212  1.00 10.58 ? 194 ARG A O   1 
ATOM   1451 C  CB  . ARG A 1 216 ? 27.783 20.678 16.171  1.00 13.75 ? 194 ARG A CB  1 
ATOM   1452 C  CG  . ARG A 1 216 ? 28.967 19.958 15.558  1.00 15.50 ? 194 ARG A CG  1 
ATOM   1453 C  CD  . ARG A 1 216 ? 30.271 20.473 16.142  1.00 17.24 ? 194 ARG A CD  1 
ATOM   1454 N  NE  . ARG A 1 216 ? 30.497 20.014 17.512  1.00 19.49 ? 194 ARG A NE  1 
ATOM   1455 C  CZ  . ARG A 1 216 ? 30.328 20.732 18.625  1.00 21.39 ? 194 ARG A CZ  1 
ATOM   1456 N  NH1 . ARG A 1 216 ? 29.898 21.997 18.594  1.00 22.98 ? 194 ARG A NH1 1 
ATOM   1457 N  NH2 . ARG A 1 216 ? 30.589 20.166 19.801  1.00 22.53 ? 194 ARG A NH2 1 
ATOM   1458 N  N   . ILE A 1 217 ? 24.964 21.900 16.622  1.00 9.91  ? 195 ILE A N   1 
ATOM   1459 C  CA  . ILE A 1 217 ? 23.912 22.326 17.541  1.00 9.38  ? 195 ILE A CA  1 
ATOM   1460 C  C   . ILE A 1 217 ? 22.583 21.687 17.141  1.00 9.04  ? 195 ILE A C   1 
ATOM   1461 O  O   . ILE A 1 217 ? 21.854 21.166 17.984  1.00 8.97  ? 195 ILE A O   1 
ATOM   1462 C  CB  . ILE A 1 217 ? 23.794 23.863 17.563  1.00 9.23  ? 195 ILE A CB  1 
ATOM   1463 C  CG1 . ILE A 1 217 ? 25.032 24.468 18.233  1.00 9.23  ? 195 ILE A CG1 1 
ATOM   1464 C  CG2 . ILE A 1 217 ? 22.537 24.308 18.299  1.00 9.12  ? 195 ILE A CG2 1 
ATOM   1465 C  CD1 . ILE A 1 217 ? 25.204 25.948 17.972  1.00 9.23  ? 195 ILE A CD1 1 
ATOM   1466 N  N   . ALA A 1 218 ? 22.274 21.723 15.850  1.00 8.93  ? 196 ALA A N   1 
ATOM   1467 C  CA  . ALA A 1 218 ? 21.013 21.178 15.356  1.00 8.90  ? 196 ALA A CA  1 
ATOM   1468 C  C   . ALA A 1 218 ? 20.949 19.659 15.540  1.00 9.01  ? 196 ALA A C   1 
ATOM   1469 O  O   . ALA A 1 218 ? 19.906 19.123 15.889  1.00 8.81  ? 196 ALA A O   1 
ATOM   1470 C  CB  . ALA A 1 218 ? 20.803 21.556 13.899  1.00 8.97  ? 196 ALA A CB  1 
ATOM   1471 N  N   . ARG A 1 219 ? 22.071 18.974 15.309  1.00 9.31  ? 197 ARG A N   1 
ATOM   1472 C  CA  . ARG A 1 219 ? 22.123 17.516 15.474  1.00 9.67  ? 197 ARG A CA  1 
ATOM   1473 C  C   . ARG A 1 219 ? 22.092 17.106 16.938  1.00 9.53  ? 197 ARG A C   1 
ATOM   1474 O  O   . ARG A 1 219 ? 21.605 16.024 17.274  1.00 9.45  ? 197 ARG A O   1 
ATOM   1475 C  CB  . ARG A 1 219 ? 23.359 16.937 14.788  1.00 10.29 ? 197 ARG A CB  1 
ATOM   1476 C  CG  . ARG A 1 219 ? 23.259 17.007 13.278  1.00 10.89 ? 197 ARG A CG  1 
ATOM   1477 C  CD  . ARG A 1 219 ? 24.525 16.513 12.605  1.00 11.69 ? 197 ARG A CD  1 
ATOM   1478 N  NE  . ARG A 1 219 ? 24.641 15.060 12.668  1.00 12.78 ? 197 ARG A NE  1 
ATOM   1479 C  CZ  . ARG A 1 219 ? 25.618 14.356 12.097  1.00 13.89 ? 197 ARG A CZ  1 
ATOM   1480 N  NH1 . ARG A 1 219 ? 26.578 14.965 11.405  1.00 14.54 ? 197 ARG A NH1 1 
ATOM   1481 N  NH2 . ARG A 1 219 ? 25.630 13.032 12.210  1.00 14.62 ? 197 ARG A NH2 1 
ATOM   1482 N  N   . HIS A 1 220 ? 22.620 17.964 17.803  1.00 9.46  ? 198 HIS A N   1 
ATOM   1483 C  CA  . HIS A 1 220 ? 22.510 17.772 19.243  1.00 9.66  ? 198 HIS A CA  1 
ATOM   1484 C  C   . HIS A 1 220 ? 21.028 17.768 19.639  1.00 9.35  ? 198 HIS A C   1 
ATOM   1485 O  O   . HIS A 1 220 ? 20.545 16.848 20.294  1.00 9.12  ? 198 HIS A O   1 
ATOM   1486 C  CB  . HIS A 1 220 ? 23.286 18.878 19.962  1.00 10.05 ? 198 HIS A CB  1 
ATOM   1487 C  CG  . HIS A 1 220 ? 23.343 18.722 21.445  1.00 10.66 ? 198 HIS A CG  1 
ATOM   1488 N  ND1 . HIS A 1 220 ? 22.240 18.879 22.253  1.00 11.18 ? 198 HIS A ND1 1 
ATOM   1489 C  CD2 . HIS A 1 220 ? 24.379 18.449 22.271  1.00 10.91 ? 198 HIS A CD2 1 
ATOM   1490 C  CE1 . HIS A 1 220 ? 22.591 18.692 23.511  1.00 11.16 ? 198 HIS A CE1 1 
ATOM   1491 N  NE2 . HIS A 1 220 ? 23.886 18.447 23.550  1.00 11.44 ? 198 HIS A NE2 1 
ATOM   1492 N  N   . ILE A 1 221 ? 20.308 18.801 19.214  1.00 9.18  ? 199 ILE A N   1 
ATOM   1493 C  CA  . ILE A 1 221 ? 18.869 18.884 19.443  1.00 9.16  ? 199 ILE A CA  1 
ATOM   1494 C  C   . ILE A 1 221 ? 18.149 17.670 18.845  1.00 9.07  ? 199 ILE A C   1 
ATOM   1495 O  O   . ILE A 1 221 ? 17.250 17.099 19.464  1.00 8.87  ? 199 ILE A O   1 
ATOM   1496 C  CB  . ILE A 1 221 ? 18.298 20.201 18.863  1.00 9.21  ? 199 ILE A CB  1 
ATOM   1497 C  CG1 . ILE A 1 221 ? 18.769 21.375 19.727  1.00 9.37  ? 199 ILE A CG1 1 
ATOM   1498 C  CG2 . ILE A 1 221 ? 16.778 20.161 18.793  1.00 9.30  ? 199 ILE A CG2 1 
ATOM   1499 C  CD1 . ILE A 1 221 ? 18.604 22.739 19.093  1.00 9.46  ? 199 ILE A CD1 1 
ATOM   1500 N  N   . GLY A 1 222 ? 18.569 17.266 17.650  1.00 9.06  ? 200 GLY A N   1 
ATOM   1501 C  CA  . GLY A 1 222 ? 17.965 16.138 16.952  1.00 9.19  ? 200 GLY A CA  1 
ATOM   1502 C  C   . GLY A 1 222 ? 18.105 14.788 17.636  1.00 9.21  ? 200 GLY A C   1 
ATOM   1503 O  O   . GLY A 1 222 ? 17.388 13.851 17.288  1.00 9.65  ? 200 GLY A O   1 
ATOM   1504 N  N   . ALA A 1 223 ? 19.034 14.682 18.584  1.00 9.28  ? 201 ALA A N   1 
ATOM   1505 C  CA  . ALA A 1 223 ? 19.241 13.445 19.351  1.00 9.29  ? 201 ALA A CA  1 
ATOM   1506 C  C   . ALA A 1 223 ? 18.199 13.266 20.451  1.00 9.30  ? 201 ALA A C   1 
ATOM   1507 O  O   . ALA A 1 223 ? 18.049 12.171 20.988  1.00 9.58  ? 201 ALA A O   1 
ATOM   1508 C  CB  . ALA A 1 223 ? 20.634 13.428 19.959  1.00 9.44  ? 201 ALA A CB  1 
ATOM   1509 N  N   . ILE A 1 224 ? 17.491 14.343 20.784  1.00 9.15  ? 202 ILE A N   1 
ATOM   1510 C  CA  . ILE A 1 224 ? 16.542 14.356 21.900  1.00 8.99  ? 202 ILE A CA  1 
ATOM   1511 C  C   . ILE A 1 224 ? 15.145 13.991 21.400  1.00 9.12  ? 202 ILE A C   1 
ATOM   1512 O  O   . ILE A 1 224 ? 14.770 14.329 20.276  1.00 9.17  ? 202 ILE A O   1 
ATOM   1513 C  CB  . ILE A 1 224 ? 16.513 15.745 22.581  1.00 8.86  ? 202 ILE A CB  1 
ATOM   1514 C  CG1 . ILE A 1 224 ? 17.925 16.152 23.031  1.00 8.96  ? 202 ILE A CG1 1 
ATOM   1515 C  CG2 . ILE A 1 224 ? 15.564 15.751 23.779  1.00 8.82  ? 202 ILE A CG2 1 
ATOM   1516 C  CD1 . ILE A 1 224 ? 18.051 17.604 23.436  1.00 9.14  ? 202 ILE A CD1 1 
ATOM   1517 N  N   . ASP A 1 225 ? 14.398 13.267 22.231  1.00 9.18  ? 203 ASP A N   1 
ATOM   1518 C  CA  . ASP A 1 225 ? 12.975 12.985 22.008  1.00 9.46  ? 203 ASP A CA  1 
ATOM   1519 C  C   . ASP A 1 225 ? 12.285 14.246 21.479  1.00 8.94  ? 203 ASP A C   1 
ATOM   1520 O  O   . ASP A 1 225 ? 12.285 15.254 22.172  1.00 8.78  ? 203 ASP A O   1 
ATOM   1521 C  CB  . ASP A 1 225 ? 12.367 12.547 23.350  1.00 10.22 ? 203 ASP A CB  1 
ATOM   1522 C  CG  . ASP A 1 225 ? 10.861 12.411 23.323  1.00 11.25 ? 203 ASP A CG  1 
ATOM   1523 O  OD1 . ASP A 1 225 ? 10.265 12.342 22.235  1.00 12.72 ? 203 ASP A OD1 1 
ATOM   1524 O  OD2 . ASP A 1 225 ? 10.273 12.342 24.420  1.00 12.28 ? 203 ASP A OD2 1 
ATOM   1525 N  N   . PRO A 1 226 ? 11.712 14.199 20.253  1.00 8.34  ? 204 PRO A N   1 
ATOM   1526 C  CA  . PRO A 1 226 ? 11.139 15.431 19.691  1.00 8.13  ? 204 PRO A CA  1 
ATOM   1527 C  C   . PRO A 1 226 ? 10.024 16.042 20.539  1.00 7.76  ? 204 PRO A C   1 
ATOM   1528 O  O   . PRO A 1 226 ? 9.888  17.270 20.583  1.00 7.63  ? 204 PRO A O   1 
ATOM   1529 C  CB  . PRO A 1 226 ? 10.587 14.988 18.331  1.00 8.31  ? 204 PRO A CB  1 
ATOM   1530 C  CG  . PRO A 1 226 ? 11.342 13.763 17.981  1.00 8.46  ? 204 PRO A CG  1 
ATOM   1531 C  CD  . PRO A 1 226 ? 11.683 13.090 19.276  1.00 8.42  ? 204 PRO A CD  1 
ATOM   1532 N  N   . GLY A 1 227 ? 9.236  15.203 21.199  1.00 7.51  ? 205 GLY A N   1 
ATOM   1533 C  CA  . GLY A 1 227 ? 8.162  15.705 22.057  1.00 7.30  ? 205 GLY A CA  1 
ATOM   1534 C  C   . GLY A 1 227 ? 8.701  16.497 23.235  1.00 7.05  ? 205 GLY A C   1 
ATOM   1535 O  O   . GLY A 1 227 ? 8.135  17.519 23.634  1.00 7.09  ? 205 GLY A O   1 
ATOM   1536 N  N   . LEU A 1 228 ? 9.809  16.027 23.790  1.00 6.77  ? 206 LEU A N   1 
ATOM   1537 C  CA  . LEU A 1 228 ? 10.450 16.689 24.924  1.00 6.57  ? 206 LEU A CA  1 
ATOM   1538 C  C   . LEU A 1 228 ? 10.965 18.069 24.514  1.00 6.41  ? 206 LEU A C   1 
ATOM   1539 O  O   . LEU A 1 228 ? 10.789 19.047 25.236  1.00 6.16  ? 206 LEU A O   1 
ATOM   1540 C  CB  . LEU A 1 228 ? 11.589 15.822 25.469  1.00 6.64  ? 206 LEU A CB  1 
ATOM   1541 C  CG  . LEU A 1 228 ? 12.449 16.391 26.595  1.00 6.63  ? 206 LEU A CG  1 
ATOM   1542 C  CD1 . LEU A 1 228 ? 11.590 16.792 27.784  1.00 6.66  ? 206 LEU A CD1 1 
ATOM   1543 C  CD2 . LEU A 1 228 ? 13.510 15.379 27.013  1.00 6.68  ? 206 LEU A CD2 1 
ATOM   1544 N  N   . VAL A 1 229 ? 11.599 18.137 23.349  1.00 6.37  ? 207 VAL A N   1 
ATOM   1545 C  CA  . VAL A 1 229 ? 12.086 19.408 22.824  1.00 6.49  ? 207 VAL A CA  1 
ATOM   1546 C  C   . VAL A 1 229 ? 10.912 20.350 22.556  1.00 6.63  ? 207 VAL A C   1 
ATOM   1547 O  O   . VAL A 1 229 ? 10.959 21.526 22.911  1.00 6.48  ? 207 VAL A O   1 
ATOM   1548 C  CB  . VAL A 1 229 ? 12.909 19.206 21.533  1.00 6.52  ? 207 VAL A CB  1 
ATOM   1549 C  CG1 . VAL A 1 229 ? 13.239 20.542 20.885  1.00 6.54  ? 207 VAL A CG1 1 
ATOM   1550 C  CG2 . VAL A 1 229 ? 14.187 18.437 21.840  1.00 6.55  ? 207 VAL A CG2 1 
ATOM   1551 N  N   . LYS A 1 230 ? 9.863  19.823 21.935  1.00 6.98  ? 208 LYS A N   1 
ATOM   1552 C  CA  . LYS A 1 230 ? 8.689  20.626 21.601  1.00 7.31  ? 208 LYS A CA  1 
ATOM   1553 C  C   . LYS A 1 230 ? 8.055  21.228 22.845  1.00 7.08  ? 208 LYS A C   1 
ATOM   1554 O  O   . LYS A 1 230 ? 7.787  22.425 22.894  1.00 6.71  ? 208 LYS A O   1 
ATOM   1555 C  CB  . LYS A 1 230 ? 7.658  19.771 20.869  1.00 7.91  ? 208 LYS A CB  1 
ATOM   1556 C  CG  . LYS A 1 230 ? 6.349  20.472 20.551  1.00 8.76  ? 208 LYS A CG  1 
ATOM   1557 C  CD  . LYS A 1 230 ? 5.390  19.495 19.894  1.00 9.44  ? 208 LYS A CD  1 
ATOM   1558 C  CE  . LYS A 1 230 ? 3.969  20.028 19.830  1.00 10.27 ? 208 LYS A CE  1 
ATOM   1559 N  NZ  . LYS A 1 230 ? 3.057  19.046 19.178  1.00 10.94 ? 208 LYS A NZ  1 
ATOM   1560 N  N   . GLU A 1 231 ? 7.807  20.396 23.850  1.00 7.14  ? 209 GLU A N   1 
ATOM   1561 C  CA  . GLU A 1 231 ? 7.150  20.877 25.059  1.00 7.29  ? 209 GLU A CA  1 
ATOM   1562 C  C   . GLU A 1 231 ? 8.043  21.831 25.838  1.00 6.88  ? 209 GLU A C   1 
ATOM   1563 O  O   . GLU A 1 231 ? 7.557  22.790 26.427  1.00 6.70  ? 209 GLU A O   1 
ATOM   1564 C  CB  . GLU A 1 231 ? 6.697  19.712 25.941  1.00 7.89  ? 209 GLU A CB  1 
ATOM   1565 C  CG  . GLU A 1 231 ? 5.659  18.820 25.272  1.00 8.53  ? 209 GLU A CG  1 
ATOM   1566 C  CD  . GLU A 1 231 ? 4.431  19.578 24.808  1.00 9.15  ? 209 GLU A CD  1 
ATOM   1567 O  OE1 . GLU A 1 231 ? 3.935  20.427 25.575  1.00 10.13 ? 209 GLU A OE1 1 
ATOM   1568 O  OE2 . GLU A 1 231 ? 3.951  19.335 23.677  1.00 10.03 ? 209 GLU A OE2 1 
ATOM   1569 N  N   . THR A 1 232 ? 9.352  21.592 25.817  1.00 6.55  ? 210 THR A N   1 
ATOM   1570 C  CA  . THR A 1 232 ? 10.277 22.477 26.515  1.00 6.40  ? 210 THR A CA  1 
ATOM   1571 C  C   . THR A 1 232 ? 10.362 23.841 25.826  1.00 6.37  ? 210 THR A C   1 
ATOM   1572 O  O   . THR A 1 232 ? 10.358 24.873 26.503  1.00 6.18  ? 210 THR A O   1 
ATOM   1573 C  CB  . THR A 1 232 ? 11.654 21.811 26.664  1.00 6.32  ? 210 THR A CB  1 
ATOM   1574 O  OG1 . THR A 1 232 ? 11.484 20.587 27.390  1.00 6.24  ? 210 THR A OG1 1 
ATOM   1575 C  CG2 . THR A 1 232 ? 12.607 22.706 27.415  1.00 6.31  ? 210 THR A CG2 1 
ATOM   1576 N  N   . LYS A 1 233 ? 10.398 23.862 24.495  1.00 6.54  ? 211 LYS A N   1 
ATOM   1577 C  CA  . LYS A 1 233 ? 10.363 25.143 23.790  1.00 6.69  ? 211 LYS A CA  1 
ATOM   1578 C  C   . LYS A 1 233 ? 9.062  25.886 24.093  1.00 7.06  ? 211 LYS A C   1 
ATOM   1579 O  O   . LYS A 1 233 ? 9.082  27.102 24.291  1.00 6.89  ? 211 LYS A O   1 
ATOM   1580 C  CB  . LYS A 1 233 ? 10.540 25.006 22.275  1.00 6.73  ? 211 LYS A CB  1 
ATOM   1581 C  CG  . LYS A 1 233 ? 10.424 26.364 21.588  1.00 6.74  ? 211 LYS A CG  1 
ATOM   1582 C  CD  . LYS A 1 233 ? 10.824 26.363 20.125  1.00 6.79  ? 211 LYS A CD  1 
ATOM   1583 C  CE  . LYS A 1 233 ? 10.489 27.724 19.526  1.00 6.91  ? 211 LYS A CE  1 
ATOM   1584 N  NZ  . LYS A 1 233 ? 11.008 27.892 18.148  1.00 6.92  ? 211 LYS A NZ  1 
ATOM   1585 N  N   . ARG A 1 234 ? 7.942  25.168 24.131  1.00 7.52  ? 212 ARG A N   1 
ATOM   1586 C  CA  . ARG A 1 234 ? 6.655  25.793 24.466  1.00 8.13  ? 212 ARG A CA  1 
ATOM   1587 C  C   . ARG A 1 234 ? 6.744  26.513 25.801  1.00 7.66  ? 212 ARG A C   1 
ATOM   1588 O  O   . ARG A 1 234 ? 6.284  27.647 25.937  1.00 7.51  ? 212 ARG A O   1 
ATOM   1589 C  CB  . ARG A 1 234 ? 5.525  24.756 24.529  1.00 9.24  ? 212 ARG A CB  1 
ATOM   1590 C  CG  . ARG A 1 234 ? 5.063  24.270 23.171  1.00 10.47 ? 212 ARG A CG  1 
ATOM   1591 C  CD  . ARG A 1 234 ? 3.910  23.285 23.278  1.00 11.81 ? 212 ARG A CD  1 
ATOM   1592 N  NE  . ARG A 1 234 ? 2.666  23.957 23.654  1.00 13.10 ? 212 ARG A NE  1 
ATOM   1593 C  CZ  . ARG A 1 234 ? 1.928  23.695 24.736  1.00 14.24 ? 212 ARG A CZ  1 
ATOM   1594 N  NH1 . ARG A 1 234 ? 2.256  22.737 25.600  1.00 14.85 ? 212 ARG A NH1 1 
ATOM   1595 N  NH2 . ARG A 1 234 ? 0.822  24.395 24.943  1.00 15.03 ? 212 ARG A NH2 1 
ATOM   1596 N  N   . ALA A 1 235 ? 7.330  25.843 26.786  1.00 7.27  ? 213 ALA A N   1 
ATOM   1597 C  CA  . ALA A 1 235 ? 7.482  26.413 28.118  1.00 7.05  ? 213 ALA A CA  1 
ATOM   1598 C  C   . ALA A 1 235 ? 8.411  27.630 28.113  1.00 6.96  ? 213 ALA A C   1 
ATOM   1599 O  O   . ALA A 1 235 ? 8.120  28.631 28.765  1.00 6.88  ? 213 ALA A O   1 
ATOM   1600 C  CB  . ALA A 1 235 ? 7.961  25.359 29.099  1.00 7.08  ? 213 ALA A CB  1 
ATOM   1601 N  N   . LEU A 1 236 ? 9.502  27.560 27.351  1.00 6.70  ? 214 LEU A N   1 
ATOM   1602 C  CA  . LEU A 1 236 ? 10.436 28.688 27.251  1.00 6.70  ? 214 LEU A CA  1 
ATOM   1603 C  C   . LEU A 1 236 ? 9.768  29.907 26.610  1.00 6.77  ? 214 LEU A C   1 
ATOM   1604 O  O   . LEU A 1 236 ? 9.850  31.030 27.131  1.00 6.83  ? 214 LEU A O   1 
ATOM   1605 C  CB  . LEU A 1 236 ? 11.681 28.282 26.458  1.00 6.63  ? 214 LEU A CB  1 
ATOM   1606 C  CG  . LEU A 1 236 ? 12.687 27.402 27.202  1.00 6.62  ? 214 LEU A CG  1 
ATOM   1607 C  CD1 . LEU A 1 236 ? 13.476 26.542 26.228  1.00 6.67  ? 214 LEU A CD1 1 
ATOM   1608 C  CD2 . LEU A 1 236 ? 13.605 28.269 28.056  1.00 6.66  ? 214 LEU A CD2 1 
ATOM   1609 N  N   . ASN A 1 237 ? 9.091  29.686 25.489  1.00 6.82  ? 215 ASN A N   1 
ATOM   1610 C  CA  . ASN A 1 237 ? 8.391  30.779 24.816  1.00 6.99  ? 215 ASN A CA  1 
ATOM   1611 C  C   . ASN A 1 237 ? 7.302  31.381 25.692  1.00 7.12  ? 215 ASN A C   1 
ATOM   1612 O  O   . ASN A 1 237 ? 7.055  32.578 25.627  1.00 7.11  ? 215 ASN A O   1 
ATOM   1613 C  CB  . ASN A 1 237 ? 7.775  30.317 23.500  1.00 7.20  ? 215 ASN A CB  1 
ATOM   1614 C  CG  . ASN A 1 237 ? 8.765  30.291 22.358  1.00 7.36  ? 215 ASN A CG  1 
ATOM   1615 O  OD1 . ASN A 1 237 ? 9.964  30.453 22.550  1.00 7.90  ? 215 ASN A OD1 1 
ATOM   1616 N  ND2 . ASN A 1 237 ? 8.249  30.100 21.147  1.00 7.50  ? 215 ASN A ND2 1 
ATOM   1617 N  N   . ARG A 1 238 ? 6.660  30.547 26.506  1.00 7.30  ? 216 ARG A N   1 
ATOM   1618 C  CA  . ARG A 1 238 ? 5.588  31.008 27.390  1.00 7.67  ? 216 ARG A CA  1 
ATOM   1619 C  C   . ARG A 1 238 ? 6.078  32.066 28.377  1.00 7.55  ? 216 ARG A C   1 
ATOM   1620 O  O   . ARG A 1 238 ? 5.313  32.947 28.767  1.00 7.42  ? 216 ARG A O   1 
ATOM   1621 C  CB  . ARG A 1 238 ? 4.982  29.834 28.163  1.00 8.17  ? 216 ARG A CB  1 
ATOM   1622 C  CG  . ARG A 1 238 ? 3.743  30.182 28.982  1.00 8.62  ? 216 ARG A CG  1 
ATOM   1623 C  CD  . ARG A 1 238 ? 2.521  30.441 28.111  1.00 9.06  ? 216 ARG A CD  1 
ATOM   1624 N  NE  . ARG A 1 238 ? 2.281  29.308 27.227  1.00 9.56  ? 216 ARG A NE  1 
ATOM   1625 C  CZ  . ARG A 1 238 ? 1.763  28.141 27.608  1.00 10.03 ? 216 ARG A CZ  1 
ATOM   1626 N  NH1 . ARG A 1 238 ? 1.366  27.938 28.859  1.00 10.36 ? 216 ARG A NH1 1 
ATOM   1627 N  NH2 . ARG A 1 238 ? 1.628  27.172 26.718  1.00 10.64 ? 216 ARG A NH2 1 
ATOM   1628 N  N   . ALA A 1 239 ? 7.336  31.963 28.803  1.00 7.39  ? 217 ALA A N   1 
ATOM   1629 C  CA  . ALA A 1 239 ? 7.902  32.944 29.732  1.00 7.50  ? 217 ALA A CA  1 
ATOM   1630 C  C   . ALA A 1 239 ? 7.765  34.359 29.181  1.00 7.66  ? 217 ALA A C   1 
ATOM   1631 O  O   . ALA A 1 239 ? 7.311  35.255 29.889  1.00 7.91  ? 217 ALA A O   1 
ATOM   1632 C  CB  . ALA A 1 239 ? 9.357  32.629 30.038  1.00 7.48  ? 217 ALA A CB  1 
ATOM   1633 N  N   . LEU A 1 240 ? 8.125  34.557 27.913  1.00 7.88  ? 218 LEU A N   1 
ATOM   1634 C  CA  . LEU A 1 240 ? 8.048  35.894 27.299  1.00 8.22  ? 218 LEU A CA  1 
ATOM   1635 C  C   . LEU A 1 240 ? 6.624  36.256 26.887  1.00 8.17  ? 218 LEU A C   1 
ATOM   1636 O  O   . LEU A 1 240 ? 6.214  37.412 27.000  1.00 8.07  ? 218 LEU A O   1 
ATOM   1637 C  CB  . LEU A 1 240 ? 9.004  36.023 26.104  1.00 8.68  ? 218 LEU A CB  1 
ATOM   1638 C  CG  . LEU A 1 240 ? 10.434 36.443 26.480  1.00 9.10  ? 218 LEU A CG  1 
ATOM   1639 C  CD1 . LEU A 1 240 ? 11.133 35.359 27.294  1.00 9.40  ? 218 LEU A CD1 1 
ATOM   1640 C  CD2 . LEU A 1 240 ? 11.237 36.801 25.241  1.00 9.49  ? 218 LEU A CD2 1 
ATOM   1641 N  N   . GLU A 1 241 ? 5.859  35.274 26.421  1.00 8.17  ? 219 GLU A N   1 
ATOM   1642 C  CA  . GLU A 1 241 ? 4.478  35.534 26.021  1.00 8.31  ? 219 GLU A CA  1 
ATOM   1643 C  C   . GLU A 1 241 ? 3.628  35.922 27.233  1.00 7.88  ? 219 GLU A C   1 
ATOM   1644 O  O   . GLU A 1 241 ? 2.712  36.739 27.123  1.00 7.66  ? 219 GLU A O   1 
ATOM   1645 C  CB  . GLU A 1 241 ? 3.905  34.327 25.279  1.00 9.08  ? 219 GLU A CB  1 
ATOM   1646 C  CG  . GLU A 1 241 ? 4.619  34.112 23.951  1.00 9.97  ? 219 GLU A CG  1 
ATOM   1647 C  CD  . GLU A 1 241 ? 4.270  32.815 23.258  1.00 11.22 ? 219 GLU A CD  1 
ATOM   1648 O  OE1 . GLU A 1 241 ? 3.379  32.081 23.741  1.00 13.28 ? 219 GLU A OE1 1 
ATOM   1649 O  OE2 . GLU A 1 241 ? 4.895  32.531 22.217  1.00 11.66 ? 219 GLU A OE2 1 
ATOM   1650 N  N   . THR A 1 242 ? 3.964  35.365 28.393  1.00 7.46  ? 220 THR A N   1 
ATOM   1651 C  CA  . THR A 1 242 ? 3.292  35.721 29.650  1.00 7.38  ? 220 THR A CA  1 
ATOM   1652 C  C   . THR A 1 242 ? 3.438  37.212 29.972  1.00 7.51  ? 220 THR A C   1 
ATOM   1653 O  O   . THR A 1 242 ? 2.525  37.836 30.522  1.00 7.48  ? 220 THR A O   1 
ATOM   1654 C  CB  . THR A 1 242 ? 3.843  34.866 30.805  1.00 7.39  ? 220 THR A CB  1 
ATOM   1655 O  OG1 . THR A 1 242 ? 3.466  33.501 30.584  1.00 7.47  ? 220 THR A OG1 1 
ATOM   1656 C  CG2 . THR A 1 242 ? 3.313  35.326 32.155  1.00 7.38  ? 220 THR A CG2 1 
ATOM   1657 N  N   . GLN A 1 243 ? 4.578  37.775 29.596  1.00 7.68  ? 221 GLN A N   1 
ATOM   1658 C  CA  . GLN A 1 243 ? 4.878  39.185 29.848  1.00 8.01  ? 221 GLN A CA  1 
ATOM   1659 C  C   . GLN A 1 243 ? 4.133  40.127 28.908  1.00 8.01  ? 221 GLN A C   1 
ATOM   1660 O  O   . GLN A 1 243 ? 4.169  41.348 29.100  1.00 8.16  ? 221 GLN A O   1 
ATOM   1661 C  CB  . GLN A 1 243 ? 6.373  39.431 29.714  1.00 8.44  ? 221 GLN A CB  1 
ATOM   1662 C  CG  . GLN A 1 243 ? 7.215  38.589 30.650  1.00 8.88  ? 221 GLN A CG  1 
ATOM   1663 C  CD  . GLN A 1 243 ? 8.696  38.751 30.396  1.00 9.36  ? 221 GLN A CD  1 
ATOM   1664 O  OE1 . GLN A 1 243 ? 9.182  39.860 30.210  1.00 10.00 ? 221 GLN A OE1 1 
ATOM   1665 N  NE2 . GLN A 1 243 ? 9.426  37.649 30.404  1.00 9.76  ? 221 GLN A NE2 1 
ATOM   1666 N  N   . GLY A 1 244 ? 3.481  39.565 27.894  1.00 7.86  ? 222 GLY A N   1 
ATOM   1667 C  CA  . GLY A 1 244 ? 2.682  40.324 26.940  1.00 7.82  ? 222 GLY A CA  1 
ATOM   1668 C  C   . GLY A 1 244 ? 3.428  40.634 25.655  1.00 7.97  ? 222 GLY A C   1 
ATOM   1669 O  O   . GLY A 1 244 ? 3.012  41.504 24.900  1.00 7.53  ? 222 GLY A O   1 
HETATM 1670 N  N   . MSE A 1 245 ? 4.513  39.910 25.380  1.00 8.40  ? 223 MSE A N   1 
HETATM 1671 C  CA  . MSE A 1 245 ? 5.360  40.236 24.228  1.00 9.17  ? 223 MSE A CA  1 
HETATM 1672 C  C   . MSE A 1 245 ? 4.572  40.306 22.943  1.00 8.45  ? 223 MSE A C   1 
HETATM 1673 O  O   . MSE A 1 245 ? 4.798  41.195 22.128  1.00 7.88  ? 223 MSE A O   1 
HETATM 1674 C  CB  . MSE A 1 245 ? 6.519  39.251 24.057  1.00 10.97 ? 223 MSE A CB  1 
HETATM 1675 C  CG  . MSE A 1 245 ? 7.384  39.653 22.862  1.00 12.82 ? 223 MSE A CG  1 
HETATM 1676 SE SE  . MSE A 1 245 ? 8.980  38.516 22.721  1.00 18.34 ? 223 MSE A SE  1 
HETATM 1677 C  CE  . MSE A 1 245 ? 8.089  37.021 21.811  1.00 16.30 ? 223 MSE A CE  1 
ATOM   1678 N  N   . LEU A 1 246 ? 3.651  39.376 22.728  1.00 7.92  ? 224 LEU A N   1 
ATOM   1679 C  CA  . LEU A 1 246 ? 2.926  39.371 21.457  1.00 7.70  ? 224 LEU A CA  1 
ATOM   1680 C  C   . LEU A 1 246 ? 2.056  40.617 21.298  1.00 7.52  ? 224 LEU A C   1 
ATOM   1681 O  O   . LEU A 1 246 ? 1.914  41.128 20.188  1.00 7.57  ? 224 LEU A O   1 
ATOM   1682 C  CB  . LEU A 1 246 ? 2.095  38.097 21.282  1.00 7.66  ? 224 LEU A CB  1 
ATOM   1683 C  CG  . LEU A 1 246 ? 2.887  36.786 21.294  1.00 7.83  ? 224 LEU A CG  1 
ATOM   1684 C  CD1 . LEU A 1 246 ? 1.945  35.622 21.032  1.00 8.02  ? 224 LEU A CD1 1 
ATOM   1685 C  CD2 . LEU A 1 246 ? 4.017  36.771 20.271  1.00 7.91  ? 224 LEU A CD2 1 
ATOM   1686 N  N   . GLN A 1 247 ? 1.482  41.111 22.395  1.00 7.36  ? 225 GLN A N   1 
ATOM   1687 C  CA  . GLN A 1 247 ? 0.712  42.357 22.337  1.00 7.35  ? 225 GLN A CA  1 
ATOM   1688 C  C   . GLN A 1 247 ? 1.630  43.554 22.088  1.00 6.99  ? 225 GLN A C   1 
ATOM   1689 O  O   . GLN A 1 247 ? 1.287  44.442 21.314  1.00 6.97  ? 225 GLN A O   1 
ATOM   1690 C  CB  . GLN A 1 247 ? -0.108 42.586 23.613  1.00 7.67  ? 225 GLN A CB  1 
ATOM   1691 C  CG  . GLN A 1 247 ? -1.331 41.691 23.721  1.00 8.02  ? 225 GLN A CG  1 
ATOM   1692 C  CD  . GLN A 1 247 ? -0.987 40.301 24.198  1.00 8.37  ? 225 GLN A CD  1 
ATOM   1693 O  OE1 . GLN A 1 247 ? -0.325 40.141 25.220  1.00 9.21  ? 225 GLN A OE1 1 
ATOM   1694 N  NE2 . GLN A 1 247 ? -1.427 39.282 23.460  1.00 8.73  ? 225 GLN A NE2 1 
ATOM   1695 N  N   . ALA A 1 248 ? 2.790  43.580 22.738  1.00 6.76  ? 226 ALA A N   1 
ATOM   1696 C  CA  . ALA A 1 248 ? 3.751  44.669 22.521  1.00 6.52  ? 226 ALA A CA  1 
ATOM   1697 C  C   . ALA A 1 248 ? 4.222  44.704 21.061  1.00 6.49  ? 226 ALA A C   1 
ATOM   1698 O  O   . ALA A 1 248 ? 4.353  45.776 20.463  1.00 6.47  ? 226 ALA A O   1 
ATOM   1699 C  CB  . ALA A 1 248 ? 4.936  44.539 23.460  1.00 6.58  ? 226 ALA A CB  1 
ATOM   1700 N  N   . LEU A 1 249 ? 4.461  43.526 20.493  1.00 6.38  ? 227 LEU A N   1 
ATOM   1701 C  CA  . LEU A 1 249 ? 4.876  43.414 19.096  1.00 6.42  ? 227 LEU A CA  1 
ATOM   1702 C  C   . LEU A 1 249 ? 3.780  43.884 18.136  1.00 6.62  ? 227 LEU A C   1 
ATOM   1703 O  O   . LEU A 1 249 ? 4.054  44.634 17.199  1.00 6.58  ? 227 LEU A O   1 
ATOM   1704 C  CB  . LEU A 1 249 ? 5.289  41.972 18.766  1.00 6.34  ? 227 LEU A CB  1 
ATOM   1705 C  CG  . LEU A 1 249 ? 6.570  41.474 19.444  1.00 6.34  ? 227 LEU A CG  1 
ATOM   1706 C  CD1 . LEU A 1 249 ? 6.784  39.993 19.174  1.00 6.34  ? 227 LEU A CD1 1 
ATOM   1707 C  CD2 . LEU A 1 249 ? 7.783  42.261 18.977  1.00 6.37  ? 227 LEU A CD2 1 
ATOM   1708 N  N   . GLU A 1 250 ? 2.544  43.459 18.374  1.00 6.84  ? 228 GLU A N   1 
ATOM   1709 C  CA  . GLU A 1 250 ? 1.421  43.916 17.548  1.00 7.25  ? 228 GLU A CA  1 
ATOM   1710 C  C   . GLU A 1 250 ? 1.258  45.432 17.654  1.00 7.40  ? 228 GLU A C   1 
ATOM   1711 O  O   . GLU A 1 250 ? 0.989  46.094 16.656  1.00 7.43  ? 228 GLU A O   1 
ATOM   1712 C  CB  . GLU A 1 250 ? 0.110  43.212 17.924  1.00 7.55  ? 228 GLU A CB  1 
ATOM   1713 C  CG  . GLU A 1 250 ? 0.043  41.743 17.532  1.00 7.88  ? 228 GLU A CG  1 
ATOM   1714 C  CD  . GLU A 1 250 ? -0.095 41.486 16.044  1.00 8.26  ? 228 GLU A CD  1 
ATOM   1715 O  OE1 . GLU A 1 250 ? -0.537 42.385 15.283  1.00 8.70  ? 228 GLU A OE1 1 
ATOM   1716 O  OE2 . GLU A 1 250 ? 0.234  40.356 15.632  1.00 9.02  ? 228 GLU A OE2 1 
ATOM   1717 N  N   . SER A 1 251 ? 1.455  45.981 18.853  1.00 7.69  ? 229 SER A N   1 
ATOM   1718 C  CA  . SER A 1 251 ? 1.355  47.437 19.054  1.00 7.91  ? 229 SER A CA  1 
ATOM   1719 C  C   . SER A 1 251 ? 2.412  48.209 18.272  1.00 7.47  ? 229 SER A C   1 
ATOM   1720 O  O   . SER A 1 251 ? 2.114  49.242 17.667  1.00 7.45  ? 229 SER A O   1 
ATOM   1721 C  CB  . SER A 1 251 ? 1.457  47.793 20.535  1.00 8.54  ? 229 SER A CB  1 
ATOM   1722 O  OG  . SER A 1 251 ? 0.312  47.330 21.225  1.00 9.81  ? 229 SER A OG  1 
ATOM   1723 N  N   . ALA A 1 252 ? 3.644  47.709 18.265  1.00 7.02  ? 230 ALA A N   1 
ATOM   1724 C  CA  . ALA A 1 252 ? 4.704  48.353 17.491  1.00 6.68  ? 230 ALA A CA  1 
ATOM   1725 C  C   . ALA A 1 252 ? 4.424  48.260 15.988  1.00 6.58  ? 230 ALA A C   1 
ATOM   1726 O  O   . ALA A 1 252 ? 4.718  49.185 15.235  1.00 6.43  ? 230 ALA A O   1 
ATOM   1727 C  CB  . ALA A 1 252 ? 6.055  47.745 17.837  1.00 6.66  ? 230 ALA A CB  1 
ATOM   1728 N  N   . LEU A 1 253 ? 3.851  47.142 15.561  1.00 6.51  ? 231 LEU A N   1 
ATOM   1729 C  CA  . LEU A 1 253 ? 3.490  46.935 14.163  1.00 6.63  ? 231 LEU A CA  1 
ATOM   1730 C  C   . LEU A 1 253 ? 2.395  47.913 13.730  1.00 6.73  ? 231 LEU A C   1 
ATOM   1731 O  O   . LEU A 1 253 ? 2.433  48.442 12.620  1.00 6.68  ? 231 LEU A O   1 
ATOM   1732 C  CB  . LEU A 1 253 ? 3.037  45.490 13.968  1.00 6.67  ? 231 LEU A CB  1 
ATOM   1733 C  CG  . LEU A 1 253 ? 2.662  45.057 12.553  1.00 6.79  ? 231 LEU A CG  1 
ATOM   1734 C  CD1 . LEU A 1 253 ? 3.845  45.183 11.609  1.00 6.91  ? 231 LEU A CD1 1 
ATOM   1735 C  CD2 . LEU A 1 253 ? 2.123  43.634 12.576  1.00 6.79  ? 231 LEU A CD2 1 
ATOM   1736 N  N   . GLU A 1 254 ? 1.438  48.151 14.622  1.00 6.91  ? 232 GLU A N   1 
ATOM   1737 C  CA  . GLU A 1 254 ? 0.358  49.120 14.393  1.00 7.19  ? 232 GLU A CA  1 
ATOM   1738 C  C   . GLU A 1 254 ? 0.907  50.533 14.252  1.00 6.72  ? 232 GLU A C   1 
ATOM   1739 O  O   . GLU A 1 254 ? 0.473  51.312 13.390  1.00 6.66  ? 232 GLU A O   1 
ATOM   1740 C  CB  . GLU A 1 254 ? -0.637 49.076 15.558  1.00 7.90  ? 232 GLU A CB  1 
ATOM   1741 C  CG  . GLU A 1 254 ? -1.461 47.799 15.616  1.00 8.77  ? 232 GLU A CG  1 
ATOM   1742 C  CD  . GLU A 1 254 ? -2.003 47.435 16.996  1.00 9.56  ? 232 GLU A CD  1 
ATOM   1743 O  OE1 . GLU A 1 254 ? -1.974 48.251 17.956  1.00 10.32 ? 232 GLU A OE1 1 
ATOM   1744 O  OE2 . GLU A 1 254 ? -2.466 46.277 17.116  1.00 10.40 ? 232 GLU A OE2 1 
ATOM   1745 N  N   . ILE A 1 255 ? 1.857  50.867 15.115  1.00 6.22  ? 233 ILE A N   1 
ATOM   1746 C  CA  . ILE A 1 255 ? 2.531  52.156 15.060  1.00 6.00  ? 233 ILE A CA  1 
ATOM   1747 C  C   . ILE A 1 255 ? 3.279  52.283 13.730  1.00 5.83  ? 233 ILE A C   1 
ATOM   1748 O  O   . ILE A 1 255 ? 3.227  53.330 13.079  1.00 5.89  ? 233 ILE A O   1 
ATOM   1749 C  CB  . ILE A 1 255 ? 3.458  52.344 16.285  1.00 5.92  ? 233 ILE A CB  1 
ATOM   1750 C  CG1 . ILE A 1 255 ? 2.604  52.577 17.535  1.00 6.01  ? 233 ILE A CG1 1 
ATOM   1751 C  CG2 . ILE A 1 255 ? 4.430  53.501 16.085  1.00 5.91  ? 233 ILE A CG2 1 
ATOM   1752 C  CD1 . ILE A 1 255 ? 3.372  52.507 18.844  1.00 5.97  ? 233 ILE A CD1 1 
ATOM   1753 N  N   . ASP A 1 256 ? 3.950  51.214 13.309  1.00 5.66  ? 234 ASP A N   1 
ATOM   1754 C  CA  . ASP A 1 256 ? 4.686  51.260 12.045  1.00 5.61  ? 234 ASP A CA  1 
ATOM   1755 C  C   . ASP A 1 256 ? 3.751  51.432 10.849  1.00 5.58  ? 234 ASP A C   1 
ATOM   1756 O  O   . ASP A 1 256 ? 4.123  52.069 9.867   1.00 5.59  ? 234 ASP A O   1 
ATOM   1757 C  CB  . ASP A 1 256 ? 5.566  50.022 11.850  1.00 5.61  ? 234 ASP A CB  1 
ATOM   1758 C  CG  . ASP A 1 256 ? 6.605  50.211 10.761  1.00 5.66  ? 234 ASP A CG  1 
ATOM   1759 O  OD1 . ASP A 1 256 ? 7.139  51.328 10.631  1.00 5.72  ? 234 ASP A OD1 1 
ATOM   1760 O  OD2 . ASP A 1 256 ? 6.895  49.238 10.033  1.00 5.66  ? 234 ASP A OD2 1 
ATOM   1761 N  N   . LEU A 1 257 ? 2.549  50.858 10.915  1.00 5.57  ? 235 LEU A N   1 
ATOM   1762 C  CA  . LEU A 1 257 ? 1.575  51.055 9.836   1.00 5.66  ? 235 LEU A CA  1 
ATOM   1763 C  C   . LEU A 1 257 ? 1.213  52.533 9.691   1.00 5.83  ? 235 LEU A C   1 
ATOM   1764 O  O   . LEU A 1 257 ? 1.100  53.044 8.570   1.00 5.87  ? 235 LEU A O   1 
ATOM   1765 C  CB  . LEU A 1 257 ? 0.318  50.212 10.050  1.00 5.66  ? 235 LEU A CB  1 
ATOM   1766 C  CG  . LEU A 1 257 ? -0.757 50.340 8.967   1.00 5.66  ? 235 LEU A CG  1 
ATOM   1767 C  CD1 . LEU A 1 257 ? -0.189 50.070 7.584   1.00 5.68  ? 235 LEU A CD1 1 
ATOM   1768 C  CD2 . LEU A 1 257 ? -1.898 49.389 9.262   1.00 5.65  ? 235 LEU A CD2 1 
ATOM   1769 N  N   . ALA A 1 258 ? 1.033  53.220 10.813  1.00 6.06  ? 236 ALA A N   1 
ATOM   1770 C  CA  . ALA A 1 258 ? 0.776  54.661 10.771  1.00 6.25  ? 236 ALA A CA  1 
ATOM   1771 C  C   . ALA A 1 258 ? 1.969  55.414 10.181  1.00 6.51  ? 236 ALA A C   1 
ATOM   1772 O  O   . ALA A 1 258 ? 1.797  56.315 9.350   1.00 6.65  ? 236 ALA A O   1 
ATOM   1773 C  CB  . ALA A 1 258 ? 0.434  55.189 12.152  1.00 6.30  ? 236 ALA A CB  1 
ATOM   1774 N  N   . ILE A 1 259 ? 3.173  55.040 10.605  1.00 6.71  ? 237 ILE A N   1 
ATOM   1775 C  CA  . ILE A 1 259 ? 4.395  55.684 10.120  1.00 6.91  ? 237 ILE A CA  1 
ATOM   1776 C  C   . ILE A 1 259 ? 4.528  55.533 8.606   1.00 7.12  ? 237 ILE A C   1 
ATOM   1777 O  O   . ILE A 1 259 ? 4.748  56.515 7.890   1.00 7.08  ? 237 ILE A O   1 
ATOM   1778 C  CB  . ILE A 1 259 ? 5.649  55.101 10.800  1.00 6.95  ? 237 ILE A CB  1 
ATOM   1779 C  CG1 . ILE A 1 259 ? 5.719  55.531 12.269  1.00 6.95  ? 237 ILE A CG1 1 
ATOM   1780 C  CG2 . ILE A 1 259 ? 6.912  55.541 10.067  1.00 6.95  ? 237 ILE A CG2 1 
ATOM   1781 C  CD1 . ILE A 1 259 ? 6.721  54.748 13.090  1.00 7.12  ? 237 ILE A CD1 1 
ATOM   1782 N  N   . GLU A 1 260 ? 4.407  54.301 8.123   1.00 7.31  ? 238 GLU A N   1 
ATOM   1783 C  CA  . GLU A 1 260 ? 4.625  54.019 6.706   1.00 7.57  ? 238 GLU A CA  1 
ATOM   1784 C  C   . GLU A 1 260 ? 3.425  54.428 5.853   1.00 7.80  ? 238 GLU A C   1 
ATOM   1785 O  O   . GLU A 1 260 ? 3.589  54.832 4.701   1.00 7.91  ? 238 GLU A O   1 
ATOM   1786 C  CB  . GLU A 1 260 ? 4.955  52.542 6.491   1.00 7.68  ? 238 GLU A CB  1 
ATOM   1787 C  CG  . GLU A 1 260 ? 6.198  52.055 7.227   1.00 7.80  ? 238 GLU A CG  1 
ATOM   1788 C  CD  . GLU A 1 260 ? 7.502  52.615 6.683   1.00 7.97  ? 238 GLU A CD  1 
ATOM   1789 O  OE1 . GLU A 1 260 ? 7.489  53.416 5.727   1.00 8.23  ? 238 GLU A OE1 1 
ATOM   1790 O  OE2 . GLU A 1 260 ? 8.568  52.248 7.213   1.00 8.04  ? 238 GLU A OE2 1 
ATOM   1791 N  N   . GLY A 1 261 ? 2.223  54.330 6.419   1.00 8.06  ? 239 GLY A N   1 
ATOM   1792 C  CA  . GLY A 1 261 ? 1.019  54.743 5.715   1.00 8.53  ? 239 GLY A CA  1 
ATOM   1793 C  C   . GLY A 1 261 ? 1.034  56.233 5.432   1.00 8.98  ? 239 GLY A C   1 
ATOM   1794 O  O   . GLY A 1 261 ? 0.595  56.667 4.360   1.00 9.65  ? 239 GLY A O   1 
ATOM   1795 N  N   . ALA A 1 262 ? 1.544  57.014 6.386   1.00 9.22  ? 240 ALA A N   1 
ATOM   1796 C  CA  . ALA A 1 262 ? 1.745  58.453 6.187   1.00 9.54  ? 240 ALA A CA  1 
ATOM   1797 C  C   . ALA A 1 262 ? 2.915  58.691 5.243   1.00 9.89  ? 240 ALA A C   1 
ATOM   1798 O  O   . ALA A 1 262 ? 2.822  59.512 4.318   1.00 10.46 ? 240 ALA A O   1 
ATOM   1799 C  CB  . ALA A 1 262 ? 1.996  59.152 7.515   1.00 9.58  ? 240 ALA A CB  1 
ATOM   1800 N  N   . GLY A 1 263 ? 4.007  57.968 5.487   1.00 10.00 ? 241 GLY A N   1 
ATOM   1801 C  CA  . GLY A 1 263 ? 5.259  58.124 4.749   1.00 10.11 ? 241 GLY A CA  1 
ATOM   1802 C  C   . GLY A 1 263 ? 6.087  59.234 5.366   1.00 10.08 ? 241 GLY A C   1 
ATOM   1803 O  O   . GLY A 1 263 ? 5.718  60.403 5.282   1.00 10.27 ? 241 GLY A O   1 
ATOM   1804 N  N   . SER A 1 264 ? 7.191  58.878 6.014   1.00 10.06 ? 242 SER A N   1 
ATOM   1805 C  CA  . SER A 1 264 ? 8.044  59.882 6.629   1.00 10.06 ? 242 SER A CA  1 
ATOM   1806 C  C   . SER A 1 264 ? 8.704  60.715 5.538   1.00 9.83  ? 242 SER A C   1 
ATOM   1807 O  O   . SER A 1 264 ? 9.110  60.166 4.518   1.00 9.68  ? 242 SER A O   1 
ATOM   1808 C  CB  . SER A 1 264 ? 9.122  59.236 7.498   1.00 10.35 ? 242 SER A CB  1 
ATOM   1809 O  OG  . SER A 1 264 ? 10.054 60.212 7.926   1.00 10.88 ? 242 SER A OG  1 
ATOM   1810 N  N   . PRO A 1 265 ? 8.818  62.037 5.750   1.00 9.90  ? 243 PRO A N   1 
ATOM   1811 C  CA  . PRO A 1 265 ? 9.518  62.846 4.751   1.00 9.98  ? 243 PRO A CA  1 
ATOM   1812 C  C   . PRO A 1 265 ? 10.965 62.395 4.544   1.00 9.85  ? 243 PRO A C   1 
ATOM   1813 O  O   . PRO A 1 265 ? 11.517 62.592 3.457   1.00 9.91  ? 243 PRO A O   1 
ATOM   1814 C  CB  . PRO A 1 265 ? 9.451  64.270 5.324   1.00 10.13 ? 243 PRO A CB  1 
ATOM   1815 C  CG  . PRO A 1 265 ? 9.092  64.115 6.759   1.00 10.26 ? 243 PRO A CG  1 
ATOM   1816 C  CD  . PRO A 1 265 ? 8.298  62.851 6.859   1.00 10.06 ? 243 PRO A CD  1 
ATOM   1817 N  N   . ASP A 1 266 ? 11.569 61.778 5.563   1.00 9.75  ? 244 ASP A N   1 
ATOM   1818 C  CA  . ASP A 1 266 ? 12.935 61.248 5.438   1.00 9.70  ? 244 ASP A CA  1 
ATOM   1819 C  C   . ASP A 1 266 ? 13.019 60.123 4.405   1.00 9.63  ? 244 ASP A C   1 
ATOM   1820 O  O   . ASP A 1 266 ? 13.988 60.045 3.642   1.00 9.69  ? 244 ASP A O   1 
ATOM   1821 C  CB  . ASP A 1 266 ? 13.450 60.706 6.780   1.00 9.89  ? 244 ASP A CB  1 
ATOM   1822 C  CG  . ASP A 1 266 ? 13.633 61.779 7.840   1.00 10.11 ? 244 ASP A CG  1 
ATOM   1823 O  OD1 . ASP A 1 266 ? 13.360 62.975 7.603   1.00 10.49 ? 244 ASP A OD1 1 
ATOM   1824 O  OD2 . ASP A 1 266 ? 14.060 61.406 8.947   1.00 10.18 ? 244 ASP A OD2 1 
ATOM   1825 N  N   . LYS A 1 267 ? 12.017 59.243 4.393   1.00 9.39  ? 245 LYS A N   1 
ATOM   1826 C  CA  . LYS A 1 267 ? 11.983 58.142 3.442   1.00 9.50  ? 245 LYS A CA  1 
ATOM   1827 C  C   . LYS A 1 267 ? 11.638 58.668 2.051   1.00 9.70  ? 245 LYS A C   1 
ATOM   1828 O  O   . LYS A 1 267 ? 12.232 58.251 1.058   1.00 9.70  ? 245 LYS A O   1 
ATOM   1829 C  CB  . LYS A 1 267 ? 10.978 57.064 3.867   1.00 9.53  ? 245 LYS A CB  1 
ATOM   1830 C  CG  . LYS A 1 267 ? 10.757 55.998 2.807   1.00 9.53  ? 245 LYS A CG  1 
ATOM   1831 C  CD  . LYS A 1 267 ? 9.853  54.875 3.280   1.00 9.61  ? 245 LYS A CD  1 
ATOM   1832 C  CE  . LYS A 1 267 ? 10.600 53.841 4.110   1.00 9.66  ? 245 LYS A CE  1 
ATOM   1833 N  NZ  . LYS A 1 267 ? 9.781  52.615 4.321   1.00 9.66  ? 245 LYS A NZ  1 
ATOM   1834 N  N   . ILE A 1 268 ? 10.677 59.582 1.984   1.00 10.14 ? 246 ILE A N   1 
ATOM   1835 C  CA  . ILE A 1 268 ? 10.271 60.150 0.703   1.00 10.52 ? 246 ILE A CA  1 
ATOM   1836 C  C   . ILE A 1 268 ? 11.478 60.811 0.034   1.00 10.78 ? 246 ILE A C   1 
ATOM   1837 O  O   . ILE A 1 268 ? 11.732 60.596 -1.150  1.00 11.23 ? 246 ILE A O   1 
ATOM   1838 C  CB  . ILE A 1 268 ? 9.105  61.149 0.863   1.00 10.78 ? 246 ILE A CB  1 
ATOM   1839 C  CG1 . ILE A 1 268 ? 7.829  60.400 1.263   1.00 11.00 ? 246 ILE A CG1 1 
ATOM   1840 C  CG2 . ILE A 1 268 ? 8.874  61.917 -0.433  1.00 10.94 ? 246 ILE A CG2 1 
ATOM   1841 C  CD1 . ILE A 1 268 ? 6.760  61.281 1.875   1.00 11.14 ? 246 ILE A CD1 1 
ATOM   1842 N  N   . ALA A 1 269 ? 12.233 61.590 0.803   1.00 11.10 ? 247 ALA A N   1 
ATOM   1843 C  CA  . ALA A 1 269 ? 13.428 62.256 0.288   1.00 11.35 ? 247 ALA A CA  1 
ATOM   1844 C  C   . ALA A 1 269 ? 14.501 61.248 -0.117  1.00 11.54 ? 247 ALA A C   1 
ATOM   1845 O  O   . ALA A 1 269 ? 15.160 61.421 -1.142  1.00 11.91 ? 247 ALA A O   1 
ATOM   1846 C  CB  . ALA A 1 269 ? 13.973 63.230 1.317   1.00 11.44 ? 247 ALA A CB  1 
ATOM   1847 N  N   . PHE A 1 270 ? 14.672 60.194 0.680   1.00 11.54 ? 248 PHE A N   1 
ATOM   1848 C  CA  . PHE A 1 270 ? 15.652 59.152 0.371   1.00 11.63 ? 248 PHE A CA  1 
ATOM   1849 C  C   . PHE A 1 270 ? 15.398 58.537 -1.002  1.00 12.02 ? 248 PHE A C   1 
ATOM   1850 O  O   . PHE A 1 270 ? 16.315 58.427 -1.817  1.00 11.98 ? 248 PHE A O   1 
ATOM   1851 C  CB  . PHE A 1 270 ? 15.644 58.053 1.441   1.00 11.61 ? 248 PHE A CB  1 
ATOM   1852 C  CG  . PHE A 1 270 ? 16.585 56.924 1.145   1.00 11.54 ? 248 PHE A CG  1 
ATOM   1853 C  CD1 . PHE A 1 270 ? 17.919 57.010 1.507   1.00 11.57 ? 248 PHE A CD1 1 
ATOM   1854 C  CD2 . PHE A 1 270 ? 16.143 55.785 0.486   1.00 11.54 ? 248 PHE A CD2 1 
ATOM   1855 C  CE1 . PHE A 1 270 ? 18.795 55.977 1.227   1.00 11.50 ? 248 PHE A CE1 1 
ATOM   1856 C  CE2 . PHE A 1 270 ? 17.015 54.749 0.201   1.00 11.66 ? 248 PHE A CE2 1 
ATOM   1857 C  CZ  . PHE A 1 270 ? 18.345 54.848 0.576   1.00 11.60 ? 248 PHE A CZ  1 
ATOM   1858 N  N   . PHE A 1 271 ? 14.151 58.155 -1.267  1.00 12.11 ? 249 PHE A N   1 
ATOM   1859 C  CA  . PHE A 1 271 ? 13.828 57.487 -2.525  1.00 12.78 ? 249 PHE A CA  1 
ATOM   1860 C  C   . PHE A 1 271 ? 13.777 58.468 -3.692  1.00 13.53 ? 249 PHE A C   1 
ATOM   1861 O  O   . PHE A 1 271 ? 13.978 58.071 -4.839  1.00 13.41 ? 249 PHE A O   1 
ATOM   1862 C  CB  . PHE A 1 271 ? 12.531 56.681 -2.411  1.00 12.67 ? 249 PHE A CB  1 
ATOM   1863 C  CG  . PHE A 1 271 ? 12.705 55.372 -1.688  1.00 12.75 ? 249 PHE A CG  1 
ATOM   1864 C  CD1 . PHE A 1 271 ? 13.521 54.378 -2.213  1.00 12.68 ? 249 PHE A CD1 1 
ATOM   1865 C  CD2 . PHE A 1 271 ? 12.068 55.135 -0.479  1.00 12.89 ? 249 PHE A CD2 1 
ATOM   1866 C  CE1 . PHE A 1 271 ? 13.694 53.173 -1.555  1.00 12.99 ? 249 PHE A CE1 1 
ATOM   1867 C  CE2 . PHE A 1 271 ? 12.236 53.931 0.185   1.00 12.93 ? 249 PHE A CE2 1 
ATOM   1868 C  CZ  . PHE A 1 271 ? 13.046 52.947 -0.353  1.00 12.99 ? 249 PHE A CZ  1 
ATOM   1869 N  N   . GLU A 1 272 ? 13.529 59.741 -3.399  1.00 14.99 ? 250 GLU A N   1 
ATOM   1870 C  CA  . GLU A 1 272 ? 13.620 60.784 -4.421  1.00 16.87 ? 250 GLU A CA  1 
ATOM   1871 C  C   . GLU A 1 272 ? 15.045 60.839 -4.962  1.00 16.60 ? 250 GLU A C   1 
ATOM   1872 O  O   . GLU A 1 272 ? 15.252 60.835 -6.176  1.00 17.00 ? 250 GLU A O   1 
ATOM   1873 C  CB  . GLU A 1 272 ? 13.214 62.141 -3.852  1.00 18.67 ? 250 GLU A CB  1 
ATOM   1874 C  CG  . GLU A 1 272 ? 12.925 63.204 -4.900  1.00 21.32 ? 250 GLU A CG  1 
ATOM   1875 C  CD  . GLU A 1 272 ? 12.104 64.358 -4.349  1.00 23.43 ? 250 GLU A CD  1 
ATOM   1876 O  OE1 . GLU A 1 272 ? 11.234 64.127 -3.471  1.00 25.95 ? 250 GLU A OE1 1 
ATOM   1877 O  OE2 . GLU A 1 272 ? 12.326 65.503 -4.797  1.00 26.55 ? 250 GLU A OE2 1 
ATOM   1878 N  N   . VAL A 1 273 ? 16.024 60.862 -4.060  1.00 16.33 ? 251 VAL A N   1 
ATOM   1879 C  CA  . VAL A 1 273 ? 17.434 60.818 -4.465  1.00 16.24 ? 251 VAL A CA  1 
ATOM   1880 C  C   . VAL A 1 273 ? 17.748 59.492 -5.167  1.00 16.21 ? 251 VAL A C   1 
ATOM   1881 O  O   . VAL A 1 273 ? 18.416 59.478 -6.202  1.00 16.16 ? 251 VAL A O   1 
ATOM   1882 C  CB  . VAL A 1 273 ? 18.400 61.018 -3.272  1.00 16.13 ? 251 VAL A CB  1 
ATOM   1883 C  CG1 . VAL A 1 273 ? 19.849 60.903 -3.733  1.00 16.25 ? 251 VAL A CG1 1 
ATOM   1884 C  CG2 . VAL A 1 273 ? 18.175 62.370 -2.607  1.00 16.14 ? 251 VAL A CG2 1 
ATOM   1885 N  N   . ALA A 1 274 ? 17.253 58.384 -4.617  1.00 16.22 ? 252 ALA A N   1 
ATOM   1886 C  CA  . ALA A 1 274 ? 17.546 57.052 -5.161  1.00 16.47 ? 252 ALA A CA  1 
ATOM   1887 C  C   . ALA A 1 274 ? 17.062 56.860 -6.603  1.00 17.26 ? 252 ALA A C   1 
ATOM   1888 O  O   . ALA A 1 274 ? 17.787 56.303 -7.432  1.00 17.31 ? 252 ALA A O   1 
ATOM   1889 C  CB  . ALA A 1 274 ? 16.971 55.968 -4.259  1.00 16.46 ? 252 ALA A CB  1 
ATOM   1890 N  N   . ARG A 1 275 ? 15.849 57.318 -6.906  1.00 18.03 ? 253 ARG A N   1 
ATOM   1891 C  CA  . ARG A 1 275 ? 15.306 57.192 -8.263  1.00 19.18 ? 253 ARG A CA  1 
ATOM   1892 C  C   . ARG A 1 275 ? 16.046 58.084 -9.260  1.00 20.31 ? 253 ARG A C   1 
ATOM   1893 O  O   . ARG A 1 275 ? 16.155 57.741 -10.439 1.00 21.15 ? 253 ARG A O   1 
ATOM   1894 C  CB  . ARG A 1 275 ? 13.814 57.531 -8.291  1.00 19.51 ? 253 ARG A CB  1 
ATOM   1895 C  CG  . ARG A 1 275 ? 12.921 56.513 -7.594  1.00 19.83 ? 253 ARG A CG  1 
ATOM   1896 C  CD  . ARG A 1 275 ? 11.449 56.773 -7.892  1.00 20.03 ? 253 ARG A CD  1 
ATOM   1897 N  NE  . ARG A 1 275 ? 11.088 58.174 -7.672  1.00 20.60 ? 253 ARG A NE  1 
ATOM   1898 C  CZ  . ARG A 1 275 ? 10.704 58.698 -6.507  1.00 21.16 ? 253 ARG A CZ  1 
ATOM   1899 N  NH1 . ARG A 1 275 ? 10.605 57.945 -5.412  1.00 20.97 ? 253 ARG A NH1 1 
ATOM   1900 N  NH2 . ARG A 1 275 ? 10.414 59.992 -6.436  1.00 21.81 ? 253 ARG A NH2 1 
ATOM   1901 N  N   . ARG A 1 276 ? 16.547 59.221 -8.782  1.00 21.25 ? 254 ARG A N   1 
ATOM   1902 C  CA  . ARG A 1 276 ? 17.232 60.202 -9.628  1.00 22.61 ? 254 ARG A CA  1 
ATOM   1903 C  C   . ARG A 1 276 ? 18.706 59.864 -9.843  1.00 22.60 ? 254 ARG A C   1 
ATOM   1904 O  O   . ARG A 1 276 ? 19.175 59.817 -10.986 1.00 22.88 ? 254 ARG A O   1 
ATOM   1905 C  CB  . ARG A 1 276 ? 17.116 61.589 -8.997  1.00 23.99 ? 254 ARG A CB  1 
ATOM   1906 C  CG  . ARG A 1 276 ? 17.660 62.732 -9.841  1.00 25.63 ? 254 ARG A CG  1 
ATOM   1907 C  CD  . ARG A 1 276 ? 17.473 64.052 -9.116  1.00 27.23 ? 254 ARG A CD  1 
ATOM   1908 N  NE  . ARG A 1 276 ? 18.197 64.065 -7.844  1.00 28.84 ? 254 ARG A NE  1 
ATOM   1909 C  CZ  . ARG A 1 276 ? 17.759 64.614 -6.709  1.00 30.22 ? 254 ARG A CZ  1 
ATOM   1910 N  NH1 . ARG A 1 276 ? 16.573 65.215 -6.641  1.00 31.39 ? 254 ARG A NH1 1 
ATOM   1911 N  NH2 . ARG A 1 276 ? 18.518 64.551 -5.622  1.00 30.77 ? 254 ARG A NH2 1 
ATOM   1912 N  N   . ASP A 1 277 ? 19.430 59.644 -8.747  1.00 22.24 ? 255 ASP A N   1 
ATOM   1913 C  CA  . ASP A 1 277 ? 20.887 59.458 -8.786  1.00 22.10 ? 255 ASP A CA  1 
ATOM   1914 C  C   . ASP A 1 277 ? 21.351 58.041 -8.430  1.00 20.86 ? 255 ASP A C   1 
ATOM   1915 O  O   . ASP A 1 277 ? 22.545 57.756 -8.504  1.00 21.34 ? 255 ASP A O   1 
ATOM   1916 C  CB  . ASP A 1 277 ? 21.571 60.446 -7.833  1.00 22.83 ? 255 ASP A CB  1 
ATOM   1917 C  CG  . ASP A 1 277 ? 21.269 61.895 -8.164  1.00 24.10 ? 255 ASP A CG  1 
ATOM   1918 O  OD1 . ASP A 1 277 ? 21.151 62.239 -9.360  1.00 25.23 ? 255 ASP A OD1 1 
ATOM   1919 O  OD2 . ASP A 1 277 ? 21.160 62.698 -7.217  1.00 25.00 ? 255 ASP A OD2 1 
ATOM   1920 N  N   . GLY A 1 278 ? 20.429 57.163 -8.038  1.00 19.29 ? 256 GLY A N   1 
ATOM   1921 C  CA  . GLY A 1 278 ? 20.772 55.786 -7.677  1.00 18.39 ? 256 GLY A CA  1 
ATOM   1922 C  C   . GLY A 1 278 ? 20.882 55.570 -6.174  1.00 17.53 ? 256 GLY A C   1 
ATOM   1923 O  O   . GLY A 1 278 ? 21.063 56.520 -5.409  1.00 17.19 ? 256 GLY A O   1 
ATOM   1924 N  N   . LEU A 1 279 ? 20.796 54.310 -5.754  1.00 17.24 ? 257 LEU A N   1 
ATOM   1925 C  CA  . LEU A 1 279 ? 20.795 53.968 -4.328  1.00 16.94 ? 257 LEU A CA  1 
ATOM   1926 C  C   . LEU A 1 279 ? 22.102 54.309 -3.595  1.00 16.82 ? 257 LEU A C   1 
ATOM   1927 O  O   . LEU A 1 279 ? 22.060 54.758 -2.454  1.00 16.10 ? 257 LEU A O   1 
ATOM   1928 C  CB  . LEU A 1 279 ? 20.429 52.494 -4.124  1.00 17.21 ? 257 LEU A CB  1 
ATOM   1929 C  CG  . LEU A 1 279 ? 18.938 52.185 -4.305  1.00 17.55 ? 257 LEU A CG  1 
ATOM   1930 C  CD1 . LEU A 1 279 ? 18.699 50.714 -4.613  1.00 17.91 ? 257 LEU A CD1 1 
ATOM   1931 C  CD2 . LEU A 1 279 ? 18.159 52.609 -3.067  1.00 17.64 ? 257 LEU A CD2 1 
ATOM   1932 N  N   . ARG A 1 280 ? 23.257 54.120 -4.235  1.00 16.45 ? 258 ARG A N   1 
ATOM   1933 C  CA  . ARG A 1 280 ? 24.519 54.546 -3.618  1.00 16.45 ? 258 ARG A CA  1 
ATOM   1934 C  C   . ARG A 1 280 ? 24.521 56.042 -3.300  1.00 16.02 ? 258 ARG A C   1 
ATOM   1935 O  O   . ARG A 1 280 ? 24.948 56.452 -2.220  1.00 15.97 ? 258 ARG A O   1 
ATOM   1936 C  CB  . ARG A 1 280 ? 25.722 54.198 -4.502  1.00 16.85 ? 258 ARG A CB  1 
ATOM   1937 C  CG  . ARG A 1 280 ? 26.101 52.730 -4.470  1.00 17.36 ? 258 ARG A CG  1 
ATOM   1938 C  CD  . ARG A 1 280 ? 27.423 52.496 -5.187  1.00 17.55 ? 258 ARG A CD  1 
ATOM   1939 N  NE  . ARG A 1 280 ? 27.378 52.921 -6.586  1.00 17.99 ? 258 ARG A NE  1 
ATOM   1940 C  CZ  . ARG A 1 280 ? 26.945 52.177 -7.606  1.00 17.73 ? 258 ARG A CZ  1 
ATOM   1941 N  NH1 . ARG A 1 280 ? 26.499 50.938 -7.419  1.00 17.86 ? 258 ARG A NH1 1 
ATOM   1942 N  NH2 . ARG A 1 280 ? 26.957 52.685 -8.836  1.00 18.10 ? 258 ARG A NH2 1 
ATOM   1943 N  N   . ALA A 1 281 ? 24.029 56.854 -4.230  1.00 15.62 ? 259 ALA A N   1 
ATOM   1944 C  CA  . ALA A 1 281 ? 23.941 58.294 -4.014  1.00 15.75 ? 259 ALA A CA  1 
ATOM   1945 C  C   . ALA A 1 281 ? 22.946 58.629 -2.895  1.00 15.45 ? 259 ALA A C   1 
ATOM   1946 O  O   . ALA A 1 281 ? 23.158 59.577 -2.140  1.00 15.67 ? 259 ALA A O   1 
ATOM   1947 C  CB  . ALA A 1 281 ? 23.558 59.005 -5.303  1.00 15.77 ? 259 ALA A CB  1 
ATOM   1948 N  N   . ALA A 1 282 ? 21.868 57.852 -2.797  1.00 15.26 ? 260 ALA A N   1 
ATOM   1949 C  CA  . ALA A 1 282 ? 20.875 58.039 -1.730  1.00 15.09 ? 260 ALA A CA  1 
ATOM   1950 C  C   . ALA A 1 282 ? 21.471 57.725 -0.361  1.00 15.12 ? 260 ALA A C   1 
ATOM   1951 O  O   . ALA A 1 282 ? 21.219 58.443 0.604   1.00 14.88 ? 260 ALA A O   1 
ATOM   1952 C  CB  . ALA A 1 282 ? 19.642 57.185 -1.984  1.00 15.07 ? 260 ALA A CB  1 
ATOM   1953 N  N   . ILE A 1 283 ? 22.271 56.663 -0.288  1.00 15.34 ? 261 ILE A N   1 
ATOM   1954 C  CA  . ILE A 1 283 ? 22.957 56.290 0.954   1.00 15.70 ? 261 ILE A CA  1 
ATOM   1955 C  C   . ILE A 1 283 ? 23.958 57.372 1.356   1.00 15.83 ? 261 ILE A C   1 
ATOM   1956 O  O   . ILE A 1 283 ? 24.075 57.705 2.533   1.00 15.98 ? 261 ILE A O   1 
ATOM   1957 C  CB  . ILE A 1 283 ? 23.664 54.917 0.828   1.00 15.98 ? 261 ILE A CB  1 
ATOM   1958 C  CG1 . ILE A 1 283 ? 22.640 53.788 0.650   1.00 16.26 ? 261 ILE A CG1 1 
ATOM   1959 C  CG2 . ILE A 1 283 ? 24.559 54.635 2.032   1.00 16.09 ? 261 ILE A CG2 1 
ATOM   1960 C  CD1 . ILE A 1 283 ? 21.880 53.409 1.903   1.00 16.57 ? 261 ILE A CD1 1 
ATOM   1961 N  N   . ALA A 1 284 ? 24.675 57.924 0.379   1.00 16.04 ? 262 ALA A N   1 
ATOM   1962 C  CA  . ALA A 1 284 ? 25.607 59.021 0.636   1.00 16.27 ? 262 ALA A CA  1 
ATOM   1963 C  C   . ALA A 1 284 ? 24.869 60.249 1.155   1.00 16.32 ? 262 ALA A C   1 
ATOM   1964 O  O   . ALA A 1 284 ? 25.313 60.897 2.110   1.00 16.21 ? 262 ALA A O   1 
ATOM   1965 C  CB  . ALA A 1 284 ? 26.377 59.366 -0.630  1.00 16.45 ? 262 ALA A CB  1 
ATOM   1966 N  N   . TRP A 1 285 ? 23.740 60.560 0.518   1.00 16.30 ? 263 TRP A N   1 
ATOM   1967 C  CA  . TRP A 1 285 ? 22.879 61.654 0.949   1.00 16.51 ? 263 TRP A CA  1 
ATOM   1968 C  C   . TRP A 1 285 ? 22.407 61.409 2.380   1.00 16.34 ? 263 TRP A C   1 
ATOM   1969 O  O   . TRP A 1 285 ? 22.429 62.313 3.207   1.00 16.78 ? 263 TRP A O   1 
ATOM   1970 C  CB  . TRP A 1 285 ? 21.681 61.795 0.005   1.00 16.68 ? 263 TRP A CB  1 
ATOM   1971 C  CG  . TRP A 1 285 ? 20.605 62.709 0.502   1.00 16.98 ? 263 TRP A CG  1 
ATOM   1972 C  CD1 . TRP A 1 285 ? 20.519 64.057 0.313   1.00 17.18 ? 263 TRP A CD1 1 
ATOM   1973 C  CD2 . TRP A 1 285 ? 19.454 62.336 1.266   1.00 17.05 ? 263 TRP A CD2 1 
ATOM   1974 N  NE1 . TRP A 1 285 ? 19.388 64.549 0.917   1.00 17.29 ? 263 TRP A NE1 1 
ATOM   1975 C  CE2 . TRP A 1 285 ? 18.717 63.513 1.512   1.00 17.20 ? 263 TRP A CE2 1 
ATOM   1976 C  CE3 . TRP A 1 285 ? 18.977 61.121 1.773   1.00 17.12 ? 263 TRP A CE3 1 
ATOM   1977 C  CZ2 . TRP A 1 285 ? 17.525 63.511 2.237   1.00 17.22 ? 263 TRP A CZ2 1 
ATOM   1978 C  CZ3 . TRP A 1 285 ? 17.791 61.120 2.499   1.00 17.16 ? 263 TRP A CZ3 1 
ATOM   1979 C  CH2 . TRP A 1 285 ? 17.081 62.307 2.723   1.00 17.09 ? 263 TRP A CH2 1 
ATOM   1980 N  N   . ARG A 1 286 ? 21.990 60.178 2.656   1.00 16.14 ? 264 ARG A N   1 
ATOM   1981 C  CA  . ARG A 1 286 ? 21.528 59.794 3.988   1.00 15.88 ? 264 ARG A CA  1 
ATOM   1982 C  C   . ARG A 1 286 ? 22.630 59.973 5.033   1.00 16.08 ? 264 ARG A C   1 
ATOM   1983 O  O   . ARG A 1 286 ? 22.425 60.625 6.057   1.00 15.81 ? 264 ARG A O   1 
ATOM   1984 C  CB  . ARG A 1 286 ? 21.055 58.340 3.978   1.00 15.95 ? 264 ARG A CB  1 
ATOM   1985 C  CG  . ARG A 1 286 ? 20.545 57.843 5.319   1.00 15.99 ? 264 ARG A CG  1 
ATOM   1986 C  CD  . ARG A 1 286 ? 20.516 56.327 5.368   1.00 16.02 ? 264 ARG A CD  1 
ATOM   1987 N  NE  . ARG A 1 286 ? 21.856 55.754 5.457   1.00 16.32 ? 264 ARG A NE  1 
ATOM   1988 C  CZ  . ARG A 1 286 ? 22.119 54.480 5.744   1.00 16.51 ? 264 ARG A CZ  1 
ATOM   1989 N  NH1 . ARG A 1 286 ? 21.135 53.618 5.979   1.00 16.88 ? 264 ARG A NH1 1 
ATOM   1990 N  NH2 . ARG A 1 286 ? 23.374 54.063 5.810   1.00 16.62 ? 264 ARG A NH2 1 
ATOM   1991 N  N   . ASP A 1 287 ? 23.796 59.397 4.759   1.00 16.16 ? 265 ASP A N   1 
ATOM   1992 C  CA  . ASP A 1 287 ? 24.918 59.425 5.705   1.00 16.60 ? 265 ASP A CA  1 
ATOM   1993 C  C   . ASP A 1 287 ? 25.397 60.846 6.007   1.00 16.80 ? 265 ASP A C   1 
ATOM   1994 O  O   . ASP A 1 287 ? 25.836 61.131 7.123   1.00 16.61 ? 265 ASP A O   1 
ATOM   1995 C  CB  . ASP A 1 287 ? 26.084 58.585 5.174   1.00 16.75 ? 265 ASP A CB  1 
ATOM   1996 C  CG  . ASP A 1 287 ? 25.761 57.101 5.108   1.00 17.20 ? 265 ASP A CG  1 
ATOM   1997 O  OD1 . ASP A 1 287 ? 24.714 56.666 5.642   1.00 17.44 ? 265 ASP A OD1 1 
ATOM   1998 O  OD2 . ASP A 1 287 ? 26.560 56.361 4.513   1.00 17.44 ? 265 ASP A OD2 1 
ATOM   1999 N  N   . ALA A 1 288 ? 25.300 61.735 5.018   1.00 17.01 ? 266 ALA A N   1 
ATOM   2000 C  CA  . ALA A 1 288 ? 25.709 63.134 5.179   1.00 17.43 ? 266 ALA A CA  1 
ATOM   2001 C  C   . ALA A 1 288 ? 24.834 63.918 6.161   1.00 17.71 ? 266 ALA A C   1 
ATOM   2002 O  O   . ALA A 1 288 ? 25.257 64.954 6.674   1.00 17.86 ? 266 ALA A O   1 
ATOM   2003 C  CB  . ALA A 1 288 ? 25.734 63.836 3.827   1.00 17.72 ? 266 ALA A CB  1 
ATOM   2004 N  N   . ARG A 1 289 ? 23.619 63.429 6.419   1.00 17.52 ? 267 ARG A N   1 
ATOM   2005 C  CA  . ARG A 1 289 ? 22.716 64.066 7.379   1.00 17.67 ? 267 ARG A CA  1 
ATOM   2006 C  C   . ARG A 1 289 ? 23.141 63.815 8.830   1.00 17.16 ? 267 ARG A C   1 
ATOM   2007 O  O   . ARG A 1 289 ? 22.735 64.551 9.731   1.00 17.21 ? 267 ARG A O   1 
ATOM   2008 C  CB  . ARG A 1 289 ? 21.281 63.558 7.188   1.00 17.99 ? 267 ARG A CB  1 
ATOM   2009 C  CG  . ARG A 1 289 ? 20.661 63.837 5.822   1.00 18.31 ? 267 ARG A CG  1 
ATOM   2010 C  CD  . ARG A 1 289 ? 19.444 62.948 5.594   1.00 18.83 ? 267 ARG A CD  1 
ATOM   2011 N  NE  . ARG A 1 289 ? 18.559 62.968 6.759   1.00 19.28 ? 267 ARG A NE  1 
ATOM   2012 C  CZ  . ARG A 1 289 ? 17.835 61.942 7.206   1.00 19.43 ? 267 ARG A CZ  1 
ATOM   2013 N  NH1 . ARG A 1 289 ? 17.847 60.757 6.597   1.00 19.56 ? 267 ARG A NH1 1 
ATOM   2014 N  NH2 . ARG A 1 289 ? 17.086 62.109 8.287   1.00 19.63 ? 267 ARG A NH2 1 
ATOM   2015 N  N   . PHE A 1 290 ? 23.946 62.780 9.055   1.00 17.15 ? 268 PHE A N   1 
ATOM   2016 C  CA  . PHE A 1 290 ? 24.341 62.387 10.408  1.00 17.38 ? 268 PHE A CA  1 
ATOM   2017 C  C   . PHE A 1 290 ? 25.793 62.733 10.696  1.00 18.31 ? 268 PHE A C   1 
ATOM   2018 O  O   . PHE A 1 290 ? 26.579 62.914 9.766   1.00 18.16 ? 268 PHE A O   1 
ATOM   2019 C  CB  . PHE A 1 290 ? 24.090 60.892 10.602  1.00 16.72 ? 268 PHE A CB  1 
ATOM   2020 C  CG  . PHE A 1 290 ? 22.653 60.516 10.423  1.00 16.03 ? 268 PHE A CG  1 
ATOM   2021 C  CD1 . PHE A 1 290 ? 21.748 60.682 11.464  1.00 15.60 ? 268 PHE A CD1 1 
ATOM   2022 C  CD2 . PHE A 1 290 ? 22.189 60.046 9.206   1.00 15.71 ? 268 PHE A CD2 1 
ATOM   2023 C  CE1 . PHE A 1 290 ? 20.414 60.364 11.298  1.00 15.44 ? 268 PHE A CE1 1 
ATOM   2024 C  CE2 . PHE A 1 290 ? 20.851 59.725 9.034   1.00 15.58 ? 268 PHE A CE2 1 
ATOM   2025 C  CZ  . PHE A 1 290 ? 19.961 59.891 10.081  1.00 15.48 ? 268 PHE A CZ  1 
ATOM   2026 N  N   . PRO A 1 291 ? 26.157 62.838 11.989  1.00 19.67 ? 269 PRO A N   1 
ATOM   2027 C  CA  . PRO A 1 291 ? 27.548 63.112 12.357  1.00 20.70 ? 269 PRO A CA  1 
ATOM   2028 C  C   . PRO A 1 291 ? 28.543 62.101 11.782  1.00 22.25 ? 269 PRO A C   1 
ATOM   2029 O  O   . PRO A 1 291 ? 28.183 60.950 11.525  1.00 22.36 ? 269 PRO A O   1 
ATOM   2030 C  CB  . PRO A 1 291 ? 27.532 63.019 13.887  1.00 20.33 ? 269 PRO A CB  1 
ATOM   2031 C  CG  . PRO A 1 291 ? 26.137 63.350 14.275  1.00 20.04 ? 269 PRO A CG  1 
ATOM   2032 C  CD  . PRO A 1 291 ? 25.272 62.809 13.171  1.00 19.74 ? 269 PRO A CD  1 
ATOM   2033 N  N   . ALA A 1 292 ? 29.781 62.545 11.576  1.00 24.38 ? 270 ALA A N   1 
ATOM   2034 C  CA  . ALA A 1 292 ? 30.874 61.655 11.180  1.00 26.01 ? 270 ALA A CA  1 
ATOM   2035 C  C   . ALA A 1 292 ? 31.369 60.861 12.386  1.00 26.83 ? 270 ALA A C   1 
ATOM   2036 O  O   . ALA A 1 292 ? 31.066 59.677 12.531  1.00 28.82 ? 270 ALA A O   1 
ATOM   2037 C  CB  . ALA A 1 292 ? 32.019 62.458 10.580  1.00 26.40 ? 270 ALA A CB  1 
ATOM   2038 N  N   . TYR B 1 25  ? 17.277 80.332 35.936  1.00 17.97 ? 3   TYR B N   1 
ATOM   2039 C  CA  . TYR B 1 25  ? 17.288 79.244 36.957  1.00 17.16 ? 3   TYR B CA  1 
ATOM   2040 C  C   . TYR B 1 25  ? 18.406 79.413 37.979  1.00 17.34 ? 3   TYR B C   1 
ATOM   2041 O  O   . TYR B 1 25  ? 19.495 79.889 37.655  1.00 17.90 ? 3   TYR B O   1 
ATOM   2042 C  CB  . TYR B 1 25  ? 17.441 77.881 36.281  1.00 16.47 ? 3   TYR B CB  1 
ATOM   2043 C  CG  . TYR B 1 25  ? 16.339 77.551 35.310  1.00 15.84 ? 3   TYR B CG  1 
ATOM   2044 C  CD1 . TYR B 1 25  ? 15.041 77.331 35.753  1.00 15.59 ? 3   TYR B CD1 1 
ATOM   2045 C  CD2 . TYR B 1 25  ? 16.594 77.440 33.949  1.00 15.57 ? 3   TYR B CD2 1 
ATOM   2046 C  CE1 . TYR B 1 25  ? 14.027 77.023 34.868  1.00 15.55 ? 3   TYR B CE1 1 
ATOM   2047 C  CE2 . TYR B 1 25  ? 15.584 77.130 33.056  1.00 15.54 ? 3   TYR B CE2 1 
ATOM   2048 C  CZ  . TYR B 1 25  ? 14.303 76.919 33.522  1.00 15.50 ? 3   TYR B CZ  1 
ATOM   2049 O  OH  . TYR B 1 25  ? 13.292 76.611 32.648  1.00 15.71 ? 3   TYR B OH  1 
ATOM   2050 N  N   . SER B 1 26  ? 18.131 78.994 39.212  1.00 17.08 ? 4   SER B N   1 
ATOM   2051 C  CA  . SER B 1 26  ? 19.084 79.121 40.314  1.00 17.11 ? 4   SER B CA  1 
ATOM   2052 C  C   . SER B 1 26  ? 19.923 77.863 40.539  1.00 16.30 ? 4   SER B C   1 
ATOM   2053 O  O   . SER B 1 26  ? 21.094 77.962 40.908  1.00 16.78 ? 4   SER B O   1 
ATOM   2054 C  CB  . SER B 1 26  ? 18.340 79.459 41.605  1.00 17.60 ? 4   SER B CB  1 
ATOM   2055 O  OG  . SER B 1 26  ? 19.215 79.419 42.717  1.00 19.41 ? 4   SER B OG  1 
ATOM   2056 N  N   . LYS B 1 27  ? 19.318 76.691 40.337  1.00 15.52 ? 5   LYS B N   1 
ATOM   2057 C  CA  . LYS B 1 27  ? 19.939 75.409 40.689  1.00 14.97 ? 5   LYS B CA  1 
ATOM   2058 C  C   . LYS B 1 27  ? 20.214 74.499 39.480  1.00 13.78 ? 5   LYS B C   1 
ATOM   2059 O  O   . LYS B 1 27  ? 20.693 73.372 39.650  1.00 12.89 ? 5   LYS B O   1 
ATOM   2060 C  CB  . LYS B 1 27  ? 19.055 74.666 41.697  1.00 15.91 ? 5   LYS B CB  1 
ATOM   2061 C  CG  . LYS B 1 27  ? 18.703 75.461 42.949  1.00 17.00 ? 5   LYS B CG  1 
ATOM   2062 C  CD  . LYS B 1 27  ? 19.897 75.631 43.864  1.00 17.66 ? 5   LYS B CD  1 
ATOM   2063 C  CE  . LYS B 1 27  ? 19.541 76.339 45.170  1.00 18.12 ? 5   LYS B CE  1 
ATOM   2064 N  NZ  . LYS B 1 27  ? 18.581 75.582 46.021  1.00 18.44 ? 5   LYS B NZ  1 
ATOM   2065 N  N   . ILE B 1 28  ? 19.888 74.972 38.279  1.00 12.88 ? 6   ILE B N   1 
ATOM   2066 C  CA  . ILE B 1 28  ? 20.311 74.320 37.036  1.00 12.50 ? 6   ILE B CA  1 
ATOM   2067 C  C   . ILE B 1 28  ? 20.785 75.351 36.014  1.00 12.25 ? 6   ILE B C   1 
ATOM   2068 O  O   . ILE B 1 28  ? 20.522 76.549 36.157  1.00 12.50 ? 6   ILE B O   1 
ATOM   2069 C  CB  . ILE B 1 28  ? 19.183 73.478 36.383  1.00 12.46 ? 6   ILE B CB  1 
ATOM   2070 C  CG1 . ILE B 1 28  ? 18.002 74.355 35.954  1.00 12.44 ? 6   ILE B CG1 1 
ATOM   2071 C  CG2 . ILE B 1 28  ? 18.709 72.391 37.330  1.00 12.47 ? 6   ILE B CG2 1 
ATOM   2072 C  CD1 . ILE B 1 28  ? 17.008 73.646 35.053  1.00 12.58 ? 6   ILE B CD1 1 
ATOM   2073 N  N   . LEU B 1 29  ? 21.498 74.875 34.997  1.00 11.88 ? 7   LEU B N   1 
ATOM   2074 C  CA  . LEU B 1 29  ? 21.706 75.630 33.765  1.00 11.74 ? 7   LEU B CA  1 
ATOM   2075 C  C   . LEU B 1 29  ? 20.830 74.994 32.692  1.00 11.67 ? 7   LEU B C   1 
ATOM   2076 O  O   . LEU B 1 29  ? 20.627 73.780 32.693  1.00 11.64 ? 7   LEU B O   1 
ATOM   2077 C  CB  . LEU B 1 29  ? 23.170 75.594 33.320  1.00 11.86 ? 7   LEU B CB  1 
ATOM   2078 C  CG  . LEU B 1 29  ? 24.237 75.894 34.372  1.00 11.96 ? 7   LEU B CG  1 
ATOM   2079 C  CD1 . LEU B 1 29  ? 25.629 75.657 33.801  1.00 11.98 ? 7   LEU B CD1 1 
ATOM   2080 C  CD2 . LEU B 1 29  ? 24.095 77.318 34.878  1.00 12.06 ? 7   LEU B CD2 1 
ATOM   2081 N  N   . TYR B 1 30  ? 20.298 75.822 31.799  1.00 11.67 ? 8   TYR B N   1 
ATOM   2082 C  CA  . TYR B 1 30  ? 19.539 75.359 30.642  1.00 11.75 ? 8   TYR B CA  1 
ATOM   2083 C  C   . TYR B 1 30  ? 20.145 75.987 29.391  1.00 12.12 ? 8   TYR B C   1 
ATOM   2084 O  O   . TYR B 1 30  ? 20.307 77.212 29.321  1.00 12.37 ? 8   TYR B O   1 
ATOM   2085 C  CB  . TYR B 1 30  ? 18.068 75.750 30.769  1.00 11.71 ? 8   TYR B CB  1 
ATOM   2086 C  CG  . TYR B 1 30  ? 17.203 75.271 29.623  1.00 11.82 ? 8   TYR B CG  1 
ATOM   2087 C  CD1 . TYR B 1 30  ? 16.742 73.961 29.576  1.00 11.94 ? 8   TYR B CD1 1 
ATOM   2088 C  CD2 . TYR B 1 30  ? 16.853 76.122 28.579  1.00 11.99 ? 8   TYR B CD2 1 
ATOM   2089 C  CE1 . TYR B 1 30  ? 15.957 73.514 28.529  1.00 12.15 ? 8   TYR B CE1 1 
ATOM   2090 C  CE2 . TYR B 1 30  ? 16.060 75.684 27.528  1.00 12.17 ? 8   TYR B CE2 1 
ATOM   2091 C  CZ  . TYR B 1 30  ? 15.617 74.375 27.505  1.00 12.25 ? 8   TYR B CZ  1 
ATOM   2092 O  OH  . TYR B 1 30  ? 14.831 73.926 26.464  1.00 12.59 ? 8   TYR B OH  1 
ATOM   2093 N  N   . GLU B 1 31  ? 20.498 75.147 28.421  1.00 12.41 ? 9   GLU B N   1 
ATOM   2094 C  CA  . GLU B 1 31  ? 21.058 75.597 27.143  1.00 12.86 ? 9   GLU B CA  1 
ATOM   2095 C  C   . GLU B 1 31  ? 20.305 74.956 25.994  1.00 13.20 ? 9   GLU B C   1 
ATOM   2096 O  O   . GLU B 1 31  ? 19.848 73.818 26.108  1.00 12.99 ? 9   GLU B O   1 
ATOM   2097 C  CB  . GLU B 1 31  ? 22.509 75.144 26.984  1.00 13.18 ? 9   GLU B CB  1 
ATOM   2098 C  CG  . GLU B 1 31  ? 23.475 75.502 28.096  1.00 13.58 ? 9   GLU B CG  1 
ATOM   2099 C  CD  . GLU B 1 31  ? 24.750 74.691 27.994  1.00 14.12 ? 9   GLU B CD  1 
ATOM   2100 O  OE1 . GLU B 1 31  ? 24.834 73.632 28.649  1.00 14.12 ? 9   GLU B OE1 1 
ATOM   2101 O  OE2 . GLU B 1 31  ? 25.655 75.083 27.220  1.00 14.62 ? 9   GLU B OE2 1 
ATOM   2102 N  N   . THR B 1 32  ? 20.207 75.673 24.878  1.00 13.62 ? 10  THR B N   1 
ATOM   2103 C  CA  . THR B 1 32  ? 19.815 75.066 23.615  1.00 14.17 ? 10  THR B CA  1 
ATOM   2104 C  C   . THR B 1 32  ? 20.964 75.251 22.630  1.00 14.55 ? 10  THR B C   1 
ATOM   2105 O  O   . THR B 1 32  ? 21.486 76.358 22.470  1.00 14.35 ? 10  THR B O   1 
ATOM   2106 C  CB  . THR B 1 32  ? 18.509 75.653 23.053  1.00 14.57 ? 10  THR B CB  1 
ATOM   2107 O  OG1 . THR B 1 32  ? 18.590 77.082 23.012  1.00 15.18 ? 10  THR B OG1 1 
ATOM   2108 C  CG2 . THR B 1 32  ? 17.339 75.243 23.925  1.00 14.66 ? 10  THR B CG2 1 
ATOM   2109 N  N   . LEU B 1 33  ? 21.384 74.155 22.010  1.00 14.77 ? 11  LEU B N   1 
ATOM   2110 C  CA  . LEU B 1 33  ? 22.460 74.193 21.029  1.00 15.37 ? 11  LEU B CA  1 
ATOM   2111 C  C   . LEU B 1 33  ? 22.293 73.067 20.021  1.00 15.28 ? 11  LEU B C   1 
ATOM   2112 O  O   . LEU B 1 33  ? 21.992 71.932 20.394  1.00 15.18 ? 11  LEU B O   1 
ATOM   2113 C  CB  . LEU B 1 33  ? 23.835 74.129 21.709  1.00 15.78 ? 11  LEU B CB  1 
ATOM   2114 C  CG  . LEU B 1 33  ? 24.327 72.839 22.376  1.00 16.26 ? 11  LEU B CG  1 
ATOM   2115 C  CD1 . LEU B 1 33  ? 25.805 72.963 22.730  1.00 16.54 ? 11  LEU B CD1 1 
ATOM   2116 C  CD2 . LEU B 1 33  ? 23.507 72.481 23.605  1.00 16.29 ? 11  LEU B CD2 1 
ATOM   2117 N  N   . HIS B 1 34  ? 22.457 73.394 18.742  1.00 15.52 ? 12  HIS B N   1 
ATOM   2118 C  CA  . HIS B 1 34  ? 22.383 72.406 17.662  1.00 15.67 ? 12  HIS B CA  1 
ATOM   2119 C  C   . HIS B 1 34  ? 21.076 71.601 17.665  1.00 15.07 ? 12  HIS B C   1 
ATOM   2120 O  O   . HIS B 1 34  ? 21.075 70.420 17.324  1.00 14.92 ? 12  HIS B O   1 
ATOM   2121 C  CB  . HIS B 1 34  ? 23.586 71.453 17.717  1.00 16.39 ? 12  HIS B CB  1 
ATOM   2122 C  CG  . HIS B 1 34  ? 24.913 72.148 17.749  1.00 17.33 ? 12  HIS B CG  1 
ATOM   2123 N  ND1 . HIS B 1 34  ? 25.440 72.798 16.654  1.00 18.09 ? 12  HIS B ND1 1 
ATOM   2124 C  CD2 . HIS B 1 34  ? 25.826 72.280 18.740  1.00 17.79 ? 12  HIS B CD2 1 
ATOM   2125 C  CE1 . HIS B 1 34  ? 26.614 73.313 16.973  1.00 18.02 ? 12  HIS B CE1 1 
ATOM   2126 N  NE2 . HIS B 1 34  ? 26.873 73.011 18.232  1.00 18.21 ? 12  HIS B NE2 1 
ATOM   2127 N  N   . GLY B 1 35  ? 19.971 72.250 18.029  1.00 14.44 ? 13  GLY B N   1 
ATOM   2128 C  CA  . GLY B 1 35  ? 18.662 71.593 18.095  1.00 14.11 ? 13  GLY B CA  1 
ATOM   2129 C  C   . GLY B 1 35  ? 18.515 70.627 19.263  1.00 13.66 ? 13  GLY B C   1 
ATOM   2130 O  O   . GLY B 1 35  ? 17.668 69.725 19.231  1.00 13.86 ? 13  GLY B O   1 
ATOM   2131 N  N   . VAL B 1 36  ? 19.334 70.821 20.292  1.00 13.28 ? 14  VAL B N   1 
ATOM   2132 C  CA  . VAL B 1 36  ? 19.358 69.956 21.476  1.00 13.00 ? 14  VAL B CA  1 
ATOM   2133 C  C   . VAL B 1 36  ? 19.222 70.821 22.727  1.00 12.53 ? 14  VAL B C   1 
ATOM   2134 O  O   . VAL B 1 36  ? 19.833 71.883 22.814  1.00 13.21 ? 14  VAL B O   1 
ATOM   2135 C  CB  . VAL B 1 36  ? 20.689 69.176 21.550  1.00 13.15 ? 14  VAL B CB  1 
ATOM   2136 C  CG1 . VAL B 1 36  ? 20.787 68.350 22.830  1.00 13.37 ? 14  VAL B CG1 1 
ATOM   2137 C  CG2 . VAL B 1 36  ? 20.856 68.299 20.317  1.00 13.36 ? 14  VAL B CG2 1 
ATOM   2138 N  N   . ALA B 1 37  ? 18.437 70.368 23.698  1.00 11.62 ? 15  ALA B N   1 
ATOM   2139 C  CA  . ALA B 1 37  ? 18.390 71.039 24.991  1.00 11.08 ? 15  ALA B CA  1 
ATOM   2140 C  C   . ALA B 1 37  ? 19.343 70.326 25.939  1.00 10.62 ? 15  ALA B C   1 
ATOM   2141 O  O   . ALA B 1 37  ? 19.442 69.099 25.925  1.00 10.46 ? 15  ALA B O   1 
ATOM   2142 C  CB  . ALA B 1 37  ? 16.982 71.050 25.550  1.00 11.06 ? 15  ALA B CB  1 
ATOM   2143 N  N   . ARG B 1 38  ? 20.065 71.099 26.740  1.00 10.11 ? 16  ARG B N   1 
ATOM   2144 C  CA  . ARG B 1 38  ? 20.975 70.531 27.722  1.00 9.98  ? 16  ARG B CA  1 
ATOM   2145 C  C   . ARG B 1 38  ? 20.678 71.126 29.092  1.00 9.75  ? 16  ARG B C   1 
ATOM   2146 O  O   . ARG B 1 38  ? 20.677 72.353 29.266  1.00 9.37  ? 16  ARG B O   1 
ATOM   2147 C  CB  . ARG B 1 38  ? 22.434 70.772 27.325  1.00 10.24 ? 16  ARG B CB  1 
ATOM   2148 C  CG  . ARG B 1 38  ? 23.427 70.045 28.216  1.00 10.45 ? 16  ARG B CG  1 
ATOM   2149 C  CD  . ARG B 1 38  ? 24.792 69.907 27.569  1.00 10.79 ? 16  ARG B CD  1 
ATOM   2150 N  NE  . ARG B 1 38  ? 25.454 71.198 27.411  1.00 11.37 ? 16  ARG B NE  1 
ATOM   2151 C  CZ  . ARG B 1 38  ? 26.590 71.387 26.743  1.00 11.80 ? 16  ARG B CZ  1 
ATOM   2152 N  NH1 . ARG B 1 38  ? 27.208 70.369 26.153  1.00 12.12 ? 16  ARG B NH1 1 
ATOM   2153 N  NH2 . ARG B 1 38  ? 27.108 72.606 26.656  1.00 12.27 ? 16  ARG B NH2 1 
ATOM   2154 N  N   . ILE B 1 39  ? 20.408 70.243 30.050  1.00 9.35  ? 17  ILE B N   1 
ATOM   2155 C  CA  . ILE B 1 39  ? 20.132 70.615 31.428  1.00 9.38  ? 17  ILE B CA  1 
ATOM   2156 C  C   . ILE B 1 39  ? 21.333 70.215 32.273  1.00 9.33  ? 17  ILE B C   1 
ATOM   2157 O  O   . ILE B 1 39  ? 21.757 69.059 32.247  1.00 9.09  ? 17  ILE B O   1 
ATOM   2158 C  CB  . ILE B 1 39  ? 18.881 69.886 31.962  1.00 9.39  ? 17  ILE B CB  1 
ATOM   2159 C  CG1 . ILE B 1 39  ? 17.640 70.306 31.170  1.00 9.46  ? 17  ILE B CG1 1 
ATOM   2160 C  CG2 . ILE B 1 39  ? 18.694 70.164 33.452  1.00 9.43  ? 17  ILE B CG2 1 
ATOM   2161 C  CD1 . ILE B 1 39  ? 16.429 69.428 31.419  1.00 9.52  ? 17  ILE B CD1 1 
ATOM   2162 N  N   . THR B 1 40  ? 21.889 71.174 33.011  1.00 9.37  ? 18  THR B N   1 
ATOM   2163 C  CA  . THR B 1 40  ? 23.023 70.911 33.884  1.00 9.45  ? 18  THR B CA  1 
ATOM   2164 C  C   . THR B 1 40  ? 22.576 71.073 35.331  1.00 9.63  ? 18  THR B C   1 
ATOM   2165 O  O   . THR B 1 40  ? 22.167 72.161 35.733  1.00 9.80  ? 18  THR B O   1 
ATOM   2166 C  CB  . THR B 1 40  ? 24.204 71.868 33.600  1.00 9.47  ? 18  THR B CB  1 
ATOM   2167 O  OG1 . THR B 1 40  ? 24.557 71.802 32.209  1.00 9.51  ? 18  THR B OG1 1 
ATOM   2168 C  CG2 . THR B 1 40  ? 25.414 71.494 34.453  1.00 9.66  ? 18  THR B CG2 1 
ATOM   2169 N  N   . LEU B 1 41  ? 22.626 69.985 36.098  1.00 9.74  ? 19  LEU B N   1 
ATOM   2170 C  CA  . LEU B 1 41  ? 22.321 70.028 37.526  1.00 9.92  ? 19  LEU B CA  1 
ATOM   2171 C  C   . LEU B 1 41  ? 23.440 70.836 38.177  1.00 10.45 ? 19  LEU B C   1 
ATOM   2172 O  O   . LEU B 1 41  ? 24.612 70.545 37.955  1.00 10.33 ? 19  LEU B O   1 
ATOM   2173 C  CB  . LEU B 1 41  ? 22.243 68.612 38.109  1.00 9.90  ? 19  LEU B CB  1 
ATOM   2174 C  CG  . LEU B 1 41  ? 21.339 67.630 37.354  1.00 9.81  ? 19  LEU B CG  1 
ATOM   2175 C  CD1 . LEU B 1 41  ? 21.389 66.259 38.006  1.00 9.80  ? 19  LEU B CD1 1 
ATOM   2176 C  CD2 . LEU B 1 41  ? 19.909 68.139 37.283  1.00 9.91  ? 19  LEU B CD2 1 
ATOM   2177 N  N   . ASN B 1 42  ? 23.086 71.866 38.941  1.00 11.20 ? 20  ASN B N   1 
ATOM   2178 C  CA  . ASN B 1 42  ? 24.082 72.856 39.345  1.00 11.99 ? 20  ASN B CA  1 
ATOM   2179 C  C   . ASN B 1 42  ? 24.027 73.341 40.797  1.00 12.96 ? 20  ASN B C   1 
ATOM   2180 O  O   . ASN B 1 42  ? 23.535 74.437 41.088  1.00 12.78 ? 20  ASN B O   1 
ATOM   2181 C  CB  . ASN B 1 42  ? 24.026 74.053 38.399  1.00 12.06 ? 20  ASN B CB  1 
ATOM   2182 C  CG  . ASN B 1 42  ? 25.199 74.984 38.591  1.00 12.12 ? 20  ASN B CG  1 
ATOM   2183 O  OD1 . ASN B 1 42  ? 26.287 74.545 38.954  1.00 12.23 ? 20  ASN B OD1 1 
ATOM   2184 N  ND2 . ASN B 1 42  ? 24.982 76.275 38.363  1.00 12.31 ? 20  ASN B ND2 1 
ATOM   2185 N  N   . ARG B 1 43  ? 24.554 72.510 41.691  1.00 14.50 ? 21  ARG B N   1 
ATOM   2186 C  CA  . ARG B 1 43  ? 24.863 72.899 43.067  1.00 16.13 ? 21  ARG B CA  1 
ATOM   2187 C  C   . ARG B 1 43  ? 26.157 72.213 43.474  1.00 17.09 ? 21  ARG B C   1 
ATOM   2188 O  O   . ARG B 1 43  ? 26.136 71.254 44.255  1.00 16.46 ? 21  ARG B O   1 
ATOM   2189 C  CB  . ARG B 1 43  ? 23.760 72.475 44.020  1.00 16.98 ? 21  ARG B CB  1 
ATOM   2190 C  CG  . ARG B 1 43  ? 22.426 73.127 43.772  1.00 17.93 ? 21  ARG B CG  1 
ATOM   2191 C  CD  . ARG B 1 43  ? 21.385 72.455 44.641  1.00 19.02 ? 21  ARG B CD  1 
ATOM   2192 N  NE  . ARG B 1 43  ? 21.377 72.997 45.994  1.00 19.73 ? 21  ARG B NE  1 
ATOM   2193 C  CZ  . ARG B 1 43  ? 20.967 72.334 47.070  1.00 20.46 ? 21  ARG B CZ  1 
ATOM   2194 N  NH1 . ARG B 1 43  ? 20.554 71.068 46.981  1.00 20.16 ? 21  ARG B NH1 1 
ATOM   2195 N  NH2 . ARG B 1 43  ? 20.990 72.939 48.250  1.00 20.88 ? 21  ARG B NH2 1 
ATOM   2196 N  N   . PRO B 1 44  ? 27.294 72.691 42.941  1.00 18.79 ? 22  PRO B N   1 
ATOM   2197 C  CA  . PRO B 1 44  ? 28.574 71.996 43.131  1.00 19.85 ? 22  PRO B CA  1 
ATOM   2198 C  C   . PRO B 1 44  ? 28.974 71.802 44.594  1.00 20.71 ? 22  PRO B C   1 
ATOM   2199 O  O   . PRO B 1 44  ? 29.579 70.780 44.938  1.00 21.41 ? 22  PRO B O   1 
ATOM   2200 C  CB  . PRO B 1 44  ? 29.579 72.903 42.411  1.00 20.04 ? 22  PRO B CB  1 
ATOM   2201 C  CG  . PRO B 1 44  ? 28.765 73.695 41.446  1.00 19.87 ? 22  PRO B CG  1 
ATOM   2202 C  CD  . PRO B 1 44  ? 27.443 73.902 42.117  1.00 19.48 ? 22  PRO B CD  1 
ATOM   2203 N  N   . GLU B 1 45  ? 28.619 72.764 45.443  1.00 21.16 ? 23  GLU B N   1 
ATOM   2204 C  CA  . GLU B 1 45  ? 28.913 72.684 46.875  1.00 21.53 ? 23  GLU B CA  1 
ATOM   2205 C  C   . GLU B 1 45  ? 28.175 71.544 47.593  1.00 20.44 ? 23  GLU B C   1 
ATOM   2206 O  O   . GLU B 1 45  ? 28.599 71.121 48.671  1.00 20.17 ? 23  GLU B O   1 
ATOM   2207 C  CB  . GLU B 1 45  ? 28.623 74.029 47.565  1.00 23.01 ? 23  GLU B CB  1 
ATOM   2208 C  CG  . GLU B 1 45  ? 27.149 74.355 47.807  1.00 24.34 ? 23  GLU B CG  1 
ATOM   2209 C  CD  . GLU B 1 45  ? 26.447 75.022 46.627  1.00 25.69 ? 23  GLU B CD  1 
ATOM   2210 O  OE1 . GLU B 1 45  ? 26.830 74.790 45.455  1.00 26.88 ? 23  GLU B OE1 1 
ATOM   2211 O  OE2 . GLU B 1 45  ? 25.492 75.789 46.883  1.00 27.56 ? 23  GLU B OE2 1 
ATOM   2212 N  N   . ARG B 1 46  ? 27.078 71.060 47.004  1.00 18.86 ? 24  ARG B N   1 
ATOM   2213 C  CA  . ARG B 1 46  ? 26.322 69.932 47.555  1.00 17.99 ? 24  ARG B CA  1 
ATOM   2214 C  C   . ARG B 1 46  ? 26.280 68.738 46.591  1.00 16.13 ? 24  ARG B C   1 
ATOM   2215 O  O   . ARG B 1 46  ? 25.344 67.938 46.633  1.00 15.44 ? 24  ARG B O   1 
ATOM   2216 C  CB  . ARG B 1 46  ? 24.894 70.368 47.897  1.00 19.12 ? 24  ARG B CB  1 
ATOM   2217 C  CG  . ARG B 1 46  ? 24.798 71.375 49.031  1.00 20.47 ? 24  ARG B CG  1 
ATOM   2218 C  CD  . ARG B 1 46  ? 23.443 71.296 49.722  1.00 21.79 ? 24  ARG B CD  1 
ATOM   2219 N  NE  . ARG B 1 46  ? 23.175 72.463 50.564  1.00 22.96 ? 24  ARG B NE  1 
ATOM   2220 C  CZ  . ARG B 1 46  ? 22.058 72.658 51.268  1.00 23.83 ? 24  ARG B CZ  1 
ATOM   2221 N  NH1 . ARG B 1 46  ? 21.072 71.763 51.249  1.00 24.09 ? 24  ARG B NH1 1 
ATOM   2222 N  NH2 . ARG B 1 46  ? 21.921 73.760 51.998  1.00 24.22 ? 24  ARG B NH2 1 
ATOM   2223 N  N   . THR B 1 47  ? 27.291 68.618 45.732  1.00 14.71 ? 25  THR B N   1 
ATOM   2224 C  CA  . THR B 1 47  ? 27.355 67.535 44.744  1.00 13.65 ? 25  THR B CA  1 
ATOM   2225 C  C   . THR B 1 47  ? 26.055 67.458 43.930  1.00 12.65 ? 25  THR B C   1 
ATOM   2226 O  O   . THR B 1 47  ? 25.540 66.367 43.661  1.00 11.94 ? 25  THR B O   1 
ATOM   2227 C  CB  . THR B 1 47  ? 27.649 66.171 45.417  1.00 13.89 ? 25  THR B CB  1 
ATOM   2228 O  OG1 . THR B 1 47  ? 28.670 66.330 46.409  1.00 14.46 ? 25  THR B OG1 1 
ATOM   2229 C  CG2 . THR B 1 47  ? 28.129 65.143 44.401  1.00 13.99 ? 25  THR B CG2 1 
ATOM   2230 N  N   . ASN B 1 48  ? 25.532 68.626 43.555  1.00 11.64 ? 26  ASN B N   1 
ATOM   2231 C  CA  . ASN B 1 48  ? 24.301 68.748 42.762  1.00 11.20 ? 26  ASN B CA  1 
ATOM   2232 C  C   . ASN B 1 48  ? 23.122 67.978 43.358  1.00 11.21 ? 26  ASN B C   1 
ATOM   2233 O  O   . ASN B 1 48  ? 22.302 67.413 42.627  1.00 10.58 ? 26  ASN B O   1 
ATOM   2234 C  CB  . ASN B 1 48  ? 24.548 68.308 41.313  1.00 10.83 ? 26  ASN B CB  1 
ATOM   2235 C  CG  . ASN B 1 48  ? 25.744 69.003 40.688  1.00 10.66 ? 26  ASN B CG  1 
ATOM   2236 O  OD1 . ASN B 1 48  ? 26.026 70.170 40.982  1.00 10.78 ? 26  ASN B OD1 1 
ATOM   2237 N  ND2 . ASN B 1 48  ? 26.452 68.294 39.820  1.00 10.24 ? 26  ASN B ND2 1 
ATOM   2238 N  N   . ALA B 1 49  ? 23.037 67.972 44.688  1.00 11.47 ? 27  ALA B N   1 
ATOM   2239 C  CA  . ALA B 1 49  ? 21.941 67.304 45.387  1.00 12.01 ? 27  ALA B CA  1 
ATOM   2240 C  C   . ALA B 1 49  ? 20.597 67.845 44.919  1.00 12.44 ? 27  ALA B C   1 
ATOM   2241 O  O   . ALA B 1 49  ? 20.427 69.053 44.744  1.00 12.11 ? 27  ALA B O   1 
ATOM   2242 C  CB  . ALA B 1 49  ? 22.088 67.477 46.891  1.00 12.13 ? 27  ALA B CB  1 
ATOM   2243 N  N   . LEU B 1 50  ? 19.645 66.939 44.718  1.00 13.20 ? 28  LEU B N   1 
ATOM   2244 C  CA  . LEU B 1 50  ? 18.340 67.289 44.176  1.00 14.02 ? 28  LEU B CA  1 
ATOM   2245 C  C   . LEU B 1 50  ? 17.397 67.725 45.301  1.00 14.70 ? 28  LEU B C   1 
ATOM   2246 O  O   . LEU B 1 50  ? 16.748 66.888 45.930  1.00 15.40 ? 28  LEU B O   1 
ATOM   2247 C  CB  . LEU B 1 50  ? 17.747 66.089 43.424  1.00 14.36 ? 28  LEU B CB  1 
ATOM   2248 C  CG  . LEU B 1 50  ? 18.534 65.558 42.216  1.00 14.67 ? 28  LEU B CG  1 
ATOM   2249 C  CD1 . LEU B 1 50  ? 18.222 64.088 41.967  1.00 14.99 ? 28  LEU B CD1 1 
ATOM   2250 C  CD2 . LEU B 1 50  ? 18.247 66.378 40.972  1.00 15.05 ? 28  LEU B CD2 1 
ATOM   2251 N  N   . ASP B 1 51  ? 17.332 69.027 45.564  1.00 14.95 ? 29  ASP B N   1 
ATOM   2252 C  CA  . ASP B 1 51  ? 16.382 69.550 46.551  1.00 15.33 ? 29  ASP B CA  1 
ATOM   2253 C  C   . ASP B 1 51  ? 15.066 69.928 45.869  1.00 15.60 ? 29  ASP B C   1 
ATOM   2254 O  O   . ASP B 1 51  ? 14.923 69.765 44.657  1.00 14.73 ? 29  ASP B O   1 
ATOM   2255 C  CB  . ASP B 1 51  ? 16.987 70.712 47.363  1.00 15.59 ? 29  ASP B CB  1 
ATOM   2256 C  CG  . ASP B 1 51  ? 17.229 71.973 46.540  1.00 16.10 ? 29  ASP B CG  1 
ATOM   2257 O  OD1 . ASP B 1 51  ? 17.072 71.958 45.307  1.00 16.14 ? 29  ASP B OD1 1 
ATOM   2258 O  OD2 . ASP B 1 51  ? 17.595 73.000 47.154  1.00 16.63 ? 29  ASP B OD2 1 
ATOM   2259 N  N   . GLN B 1 52  ? 14.102 70.410 46.648  1.00 16.18 ? 30  GLN B N   1 
ATOM   2260 C  CA  . GLN B 1 52  ? 12.782 70.759 46.115  1.00 17.07 ? 30  GLN B CA  1 
ATOM   2261 C  C   . GLN B 1 52  ? 12.855 71.795 45.004  1.00 16.68 ? 30  GLN B C   1 
ATOM   2262 O  O   . GLN B 1 52  ? 12.170 71.667 43.989  1.00 15.96 ? 30  GLN B O   1 
ATOM   2263 C  CB  . GLN B 1 52  ? 11.869 71.289 47.228  1.00 17.98 ? 30  GLN B CB  1 
ATOM   2264 C  CG  . GLN B 1 52  ? 11.542 70.267 48.302  1.00 19.12 ? 30  GLN B CG  1 
ATOM   2265 C  CD  . GLN B 1 52  ? 10.805 69.068 47.749  1.00 19.80 ? 30  GLN B CD  1 
ATOM   2266 O  OE1 . GLN B 1 52  ? 11.404 68.024 47.503  1.00 21.27 ? 30  GLN B OE1 1 
ATOM   2267 N  NE2 . GLN B 1 52  ? 9.503  69.217 47.526  1.00 20.92 ? 30  GLN B NE2 1 
ATOM   2268 N  N   . GLU B 1 53  ? 13.680 72.817 45.209  1.00 16.53 ? 31  GLU B N   1 
ATOM   2269 C  CA  . GLU B 1 53  ? 13.837 73.890 44.239  1.00 16.95 ? 31  GLU B CA  1 
ATOM   2270 C  C   . GLU B 1 53  ? 14.383 73.357 42.916  1.00 16.25 ? 31  GLU B C   1 
ATOM   2271 O  O   . GLU B 1 53  ? 13.835 73.655 41.857  1.00 15.52 ? 31  GLU B O   1 
ATOM   2272 C  CB  . GLU B 1 53  ? 14.755 74.985 44.797  1.00 18.14 ? 31  GLU B CB  1 
ATOM   2273 C  CG  . GLU B 1 53  ? 14.910 76.198 43.891  1.00 19.71 ? 31  GLU B CG  1 
ATOM   2274 C  CD  . GLU B 1 53  ? 15.773 77.289 44.500  1.00 20.91 ? 31  GLU B CD  1 
ATOM   2275 O  OE1 . GLU B 1 53  ? 16.197 77.149 45.666  1.00 22.31 ? 31  GLU B OE1 1 
ATOM   2276 O  OE2 . GLU B 1 53  ? 16.026 78.294 43.807  1.00 22.59 ? 31  GLU B OE2 1 
HETATM 2277 N  N   . MSE B 1 54  ? 15.446 72.558 42.982  1.00 15.53 ? 32  MSE B N   1 
HETATM 2278 C  CA  . MSE B 1 54  ? 16.052 71.992 41.771  1.00 15.63 ? 32  MSE B CA  1 
HETATM 2279 C  C   . MSE B 1 54  ? 15.067 71.124 41.035  1.00 14.19 ? 32  MSE B C   1 
HETATM 2280 O  O   . MSE B 1 54  ? 14.998 71.176 39.810  1.00 13.43 ? 32  MSE B O   1 
HETATM 2281 C  CB  . MSE B 1 54  ? 17.324 71.194 42.058  1.00 17.40 ? 32  MSE B CB  1 
HETATM 2282 C  CG  . MSE B 1 54  ? 18.162 71.045 40.786  1.00 19.30 ? 32  MSE B CG  1 
HETATM 2283 SE SE  . MSE B 1 54  ? 19.591 69.709 41.016  1.00 24.44 ? 32  MSE B SE  1 
HETATM 2284 C  CE  . MSE B 1 54  ? 20.903 70.871 41.895  1.00 22.67 ? 32  MSE B CE  1 
ATOM   2285 N  N   . LEU B 1 55  ? 14.298 70.320 41.763  1.00 13.14 ? 33  LEU B N   1 
ATOM   2286 C  CA  . LEU B 1 55  ? 13.304 69.444 41.133  1.00 12.62 ? 33  LEU B CA  1 
ATOM   2287 C  C   . LEU B 1 55  ? 12.250 70.252 40.374  1.00 11.97 ? 33  LEU B C   1 
ATOM   2288 O  O   . LEU B 1 55  ? 11.851 69.885 39.264  1.00 11.66 ? 33  LEU B O   1 
ATOM   2289 C  CB  . LEU B 1 55  ? 12.636 68.538 42.174  1.00 12.71 ? 33  LEU B CB  1 
ATOM   2290 C  CG  . LEU B 1 55  ? 13.526 67.447 42.777  1.00 12.94 ? 33  LEU B CG  1 
ATOM   2291 C  CD1 . LEU B 1 55  ? 12.842 66.797 43.973  1.00 13.27 ? 33  LEU B CD1 1 
ATOM   2292 C  CD2 . LEU B 1 55  ? 13.899 66.399 41.741  1.00 12.99 ? 33  LEU B CD2 1 
ATOM   2293 N  N   . GLY B 1 56  ? 11.797 71.347 40.978  1.00 11.62 ? 34  GLY B N   1 
ATOM   2294 C  CA  . GLY B 1 56  ? 10.873 72.253 40.311  1.00 11.42 ? 34  GLY B CA  1 
ATOM   2295 C  C   . GLY B 1 56  ? 11.463 72.846 39.041  1.00 11.09 ? 34  GLY B C   1 
ATOM   2296 O  O   . GLY B 1 56  ? 10.775 72.950 38.026  1.00 11.36 ? 34  GLY B O   1 
ATOM   2297 N  N   . GLU B 1 57  ? 12.737 73.237 39.094  1.00 10.91 ? 35  GLU B N   1 
ATOM   2298 C  CA  . GLU B 1 57  ? 13.409 73.822 37.930  1.00 10.86 ? 35  GLU B CA  1 
ATOM   2299 C  C   . GLU B 1 57  ? 13.621 72.791 36.823  1.00 10.35 ? 35  GLU B C   1 
ATOM   2300 O  O   . GLU B 1 57  ? 13.463 73.106 35.647  1.00 10.05 ? 35  GLU B O   1 
ATOM   2301 C  CB  . GLU B 1 57  ? 14.731 74.475 38.333  1.00 11.30 ? 35  GLU B CB  1 
ATOM   2302 C  CG  . GLU B 1 57  ? 14.519 75.730 39.167  1.00 11.81 ? 35  GLU B CG  1 
ATOM   2303 C  CD  . GLU B 1 57  ? 15.790 76.503 39.450  1.00 12.34 ? 35  GLU B CD  1 
ATOM   2304 O  OE1 . GLU B 1 57  ? 16.886 75.909 39.449  1.00 12.55 ? 35  GLU B OE1 1 
ATOM   2305 O  OE2 . GLU B 1 57  ? 15.684 77.730 39.686  1.00 12.93 ? 35  GLU B OE2 1 
ATOM   2306 N  N   . ILE B 1 58  ? 13.948 71.556 37.201  1.00 9.98  ? 36  ILE B N   1 
ATOM   2307 C  CA  . ILE B 1 58  ? 14.063 70.474 36.224  1.00 9.71  ? 36  ILE B CA  1 
ATOM   2308 C  C   . ILE B 1 58  ? 12.730 70.280 35.494  1.00 9.61  ? 36  ILE B C   1 
ATOM   2309 O  O   . ILE B 1 58  ? 12.702 70.128 34.279  1.00 9.62  ? 36  ILE B O   1 
ATOM   2310 C  CB  . ILE B 1 58  ? 14.527 69.147 36.871  1.00 9.57  ? 36  ILE B CB  1 
ATOM   2311 C  CG1 . ILE B 1 58  ? 15.987 69.262 37.344  1.00 9.55  ? 36  ILE B CG1 1 
ATOM   2312 C  CG2 . ILE B 1 58  ? 14.390 67.992 35.881  1.00 9.57  ? 36  ILE B CG2 1 
ATOM   2313 C  CD1 . ILE B 1 58  ? 16.420 68.185 38.318  1.00 9.55  ? 36  ILE B CD1 1 
ATOM   2314 N  N   . ASN B 1 59  ? 11.625 70.279 36.236  1.00 9.59  ? 37  ASN B N   1 
ATOM   2315 C  CA  . ASN B 1 59  ? 10.308 70.178 35.610  1.00 9.70  ? 37  ASN B CA  1 
ATOM   2316 C  C   . ASN B 1 59  ? 10.021 71.342 34.662  1.00 9.66  ? 37  ASN B C   1 
ATOM   2317 O  O   . ASN B 1 59  ? 9.469  71.138 33.586  1.00 9.71  ? 37  ASN B O   1 
ATOM   2318 C  CB  . ASN B 1 59  ? 9.210  70.072 36.671  1.00 9.77  ? 37  ASN B CB  1 
ATOM   2319 C  CG  . ASN B 1 59  ? 9.132  68.692 37.293  1.00 9.92  ? 37  ASN B CG  1 
ATOM   2320 O  OD1 . ASN B 1 59  ? 9.434  68.494 38.476  1.00 10.57 ? 37  ASN B OD1 1 
ATOM   2321 N  ND2 . ASN B 1 59  ? 8.742  67.724 36.492  1.00 9.71  ? 37  ASN B ND2 1 
ATOM   2322 N  N   . ALA B 1 60  ? 10.379 72.557 35.071  1.00 9.90  ? 38  ALA B N   1 
ATOM   2323 C  CA  . ALA B 1 60  ? 10.188 73.734 34.225  1.00 10.07 ? 38  ALA B CA  1 
ATOM   2324 C  C   . ALA B 1 60  ? 11.030 73.638 32.951  1.00 10.21 ? 38  ALA B C   1 
ATOM   2325 O  O   . ALA B 1 60  ? 10.560 73.977 31.861  1.00 10.38 ? 38  ALA B O   1 
ATOM   2326 C  CB  . ALA B 1 60  ? 10.531 75.002 34.995  1.00 10.20 ? 38  ALA B CB  1 
ATOM   2327 N  N   . ALA B 1 61  ? 12.266 73.165 33.093  1.00 10.34 ? 39  ALA B N   1 
ATOM   2328 C  CA  . ALA B 1 61  ? 13.167 73.005 31.948  1.00 10.42 ? 39  ALA B CA  1 
ATOM   2329 C  C   . ALA B 1 61  ? 12.651 71.932 30.993  1.00 10.66 ? 39  ALA B C   1 
ATOM   2330 O  O   . ALA B 1 61  ? 12.724 72.096 29.775  1.00 10.21 ? 39  ALA B O   1 
ATOM   2331 C  CB  . ALA B 1 61  ? 14.569 72.659 32.415  1.00 10.44 ? 39  ALA B CB  1 
HETATM 2332 N  N   . MSE B 1 62  ? 12.123 70.843 31.547  1.00 11.02 ? 40  MSE B N   1 
HETATM 2333 C  CA  . MSE B 1 62  ? 11.570 69.770 30.715  1.00 11.80 ? 40  MSE B CA  1 
HETATM 2334 C  C   . MSE B 1 62  ? 10.333 70.258 30.009  1.00 11.45 ? 40  MSE B C   1 
HETATM 2335 O  O   . MSE B 1 62  ? 10.129 69.930 28.846  1.00 11.05 ? 40  MSE B O   1 
HETATM 2336 C  CB  . MSE B 1 62  ? 11.281 68.509 31.524  1.00 13.14 ? 40  MSE B CB  1 
HETATM 2337 C  CG  . MSE B 1 62  ? 12.570 67.813 31.959  1.00 14.63 ? 40  MSE B CG  1 
HETATM 2338 SE SE  . MSE B 1 62  ? 13.561 67.073 30.420  1.00 18.83 ? 40  MSE B SE  1 
HETATM 2339 C  CE  . MSE B 1 62  ? 12.574 65.371 30.281  1.00 17.05 ? 40  MSE B CE  1 
ATOM   2340 N  N   . ASP B 1 63  ? 9.497  71.044 30.692  1.00 11.27 ? 41  ASP B N   1 
ATOM   2341 C  CA  . ASP B 1 63  ? 8.335  71.663 30.042  1.00 11.46 ? 41  ASP B CA  1 
ATOM   2342 C  C   . ASP B 1 63  ? 8.780  72.494 28.843  1.00 11.20 ? 41  ASP B C   1 
ATOM   2343 O  O   . ASP B 1 63  ? 8.190  72.410 27.769  1.00 11.21 ? 41  ASP B O   1 
ATOM   2344 C  CB  . ASP B 1 63  ? 7.561  72.578 31.001  1.00 11.79 ? 41  ASP B CB  1 
ATOM   2345 C  CG  . ASP B 1 63  ? 6.781  71.818 32.067  1.00 12.22 ? 41  ASP B CG  1 
ATOM   2346 O  OD1 . ASP B 1 63  ? 6.684  70.573 32.019  1.00 12.34 ? 41  ASP B OD1 1 
ATOM   2347 O  OD2 . ASP B 1 63  ? 6.258  72.492 32.977  1.00 12.89 ? 41  ASP B OD2 1 
ATOM   2348 N  N   . ALA B 1 64  ? 9.816  73.307 29.045  1.00 10.88 ? 42  ALA B N   1 
ATOM   2349 C  CA  . ALA B 1 64  ? 10.347 74.170 27.989  1.00 10.93 ? 42  ALA B CA  1 
ATOM   2350 C  C   . ALA B 1 64  ? 10.889 73.355 26.821  1.00 10.72 ? 42  ALA B C   1 
ATOM   2351 O  O   . ALA B 1 64  ? 10.574 73.634 25.661  1.00 10.95 ? 42  ALA B O   1 
ATOM   2352 C  CB  . ALA B 1 64  ? 11.440 75.072 28.545  1.00 10.94 ? 42  ALA B CB  1 
ATOM   2353 N  N   . ALA B 1 65  ? 11.703 72.348 27.130  1.00 10.50 ? 43  ALA B N   1 
ATOM   2354 C  CA  . ALA B 1 65  ? 12.309 71.504 26.101  1.00 10.43 ? 43  ALA B CA  1 
ATOM   2355 C  C   . ALA B 1 65  ? 11.252 70.774 25.279  1.00 10.47 ? 43  ALA B C   1 
ATOM   2356 O  O   . ALA B 1 65  ? 11.388 70.640 24.066  1.00 10.07 ? 43  ALA B O   1 
ATOM   2357 C  CB  . ALA B 1 65  ? 13.261 70.495 26.726  1.00 10.51 ? 43  ALA B CB  1 
ATOM   2358 N  N   . GLU B 1 66  ? 10.198 70.311 25.946  1.00 10.66 ? 44  GLU B N   1 
ATOM   2359 C  CA  . GLU B 1 66  ? 9.140  69.551 25.280  1.00 11.11 ? 44  GLU B CA  1 
ATOM   2360 C  C   . GLU B 1 66  ? 8.239  70.434 24.411  1.00 11.40 ? 44  GLU B C   1 
ATOM   2361 O  O   . GLU B 1 66  ? 7.718  69.969 23.399  1.00 11.76 ? 44  GLU B O   1 
ATOM   2362 C  CB  . GLU B 1 66  ? 8.324  68.756 26.309  1.00 11.25 ? 44  GLU B CB  1 
ATOM   2363 C  CG  . GLU B 1 66  ? 9.126  67.600 26.891  1.00 11.36 ? 44  GLU B CG  1 
ATOM   2364 C  CD  . GLU B 1 66  ? 8.500  66.922 28.094  1.00 11.48 ? 44  GLU B CD  1 
ATOM   2365 O  OE1 . GLU B 1 66  ? 7.382  67.281 28.520  1.00 11.38 ? 44  GLU B OE1 1 
ATOM   2366 O  OE2 . GLU B 1 66  ? 9.153  66.006 28.628  1.00 11.61 ? 44  GLU B OE2 1 
ATOM   2367 N  N   . ALA B 1 67  ? 8.076  71.700 24.796  1.00 11.64 ? 45  ALA B N   1 
ATOM   2368 C  CA  . ALA B 1 67  ? 7.252  72.651 24.035  1.00 11.95 ? 45  ALA B CA  1 
ATOM   2369 C  C   . ALA B 1 67  ? 8.007  73.289 22.864  1.00 12.28 ? 45  ALA B C   1 
ATOM   2370 O  O   . ALA B 1 67  ? 7.380  73.795 21.930  1.00 12.78 ? 45  ALA B O   1 
ATOM   2371 C  CB  . ALA B 1 67  ? 6.722  73.739 24.956  1.00 12.03 ? 45  ALA B CB  1 
ATOM   2372 N  N   . ASP B 1 68  ? 9.337  73.278 22.923  1.00 12.20 ? 46  ASP B N   1 
ATOM   2373 C  CA  . ASP B 1 68  ? 10.180 73.918 21.909  1.00 12.32 ? 46  ASP B CA  1 
ATOM   2374 C  C   . ASP B 1 68  ? 10.363 72.980 20.721  1.00 12.28 ? 46  ASP B C   1 
ATOM   2375 O  O   . ASP B 1 68  ? 11.089 71.991 20.813  1.00 12.14 ? 46  ASP B O   1 
ATOM   2376 C  CB  . ASP B 1 68  ? 11.539 74.282 22.520  1.00 12.46 ? 46  ASP B CB  1 
ATOM   2377 C  CG  . ASP B 1 68  ? 12.412 75.130 21.594  1.00 12.75 ? 46  ASP B CG  1 
ATOM   2378 O  OD1 . ASP B 1 68  ? 12.118 75.241 20.384  1.00 13.23 ? 46  ASP B OD1 1 
ATOM   2379 O  OD2 . ASP B 1 68  ? 13.411 75.684 22.091  1.00 12.68 ? 46  ASP B OD2 1 
ATOM   2380 N  N   . ALA B 1 69  ? 9.720  73.307 19.599  1.00 12.43 ? 47  ALA B N   1 
ATOM   2381 C  CA  . ALA B 1 69  ? 9.822  72.492 18.387  1.00 12.50 ? 47  ALA B CA  1 
ATOM   2382 C  C   . ALA B 1 69  ? 11.240 72.430 17.820  1.00 12.46 ? 47  ALA B C   1 
ATOM   2383 O  O   . ALA B 1 69  ? 11.560 71.512 17.070  1.00 12.54 ? 47  ALA B O   1 
ATOM   2384 C  CB  . ALA B 1 69  ? 8.858  72.997 17.324  1.00 12.71 ? 47  ALA B CB  1 
ATOM   2385 N  N   . GLY B 1 70  ? 12.074 73.413 18.158  1.00 12.26 ? 48  GLY B N   1 
ATOM   2386 C  CA  . GLY B 1 70  ? 13.483 73.407 17.780  1.00 12.27 ? 48  GLY B CA  1 
ATOM   2387 C  C   . GLY B 1 70  ? 14.356 72.472 18.605  1.00 12.18 ? 48  GLY B C   1 
ATOM   2388 O  O   . GLY B 1 70  ? 15.530 72.295 18.290  1.00 13.09 ? 48  GLY B O   1 
ATOM   2389 N  N   . VAL B 1 71  ? 13.804 71.889 19.670  1.00 11.53 ? 49  VAL B N   1 
ATOM   2390 C  CA  . VAL B 1 71  ? 14.530 70.909 20.485  1.00 11.11 ? 49  VAL B CA  1 
ATOM   2391 C  C   . VAL B 1 71  ? 14.116 69.504 20.053  1.00 10.80 ? 49  VAL B C   1 
ATOM   2392 O  O   . VAL B 1 71  ? 12.928 69.195 20.024  1.00 10.55 ? 49  VAL B O   1 
ATOM   2393 C  CB  . VAL B 1 71  ? 14.234 71.086 21.990  1.00 11.01 ? 49  VAL B CB  1 
ATOM   2394 C  CG1 . VAL B 1 71  ? 14.761 69.900 22.792  1.00 10.96 ? 49  VAL B CG1 1 
ATOM   2395 C  CG2 . VAL B 1 71  ? 14.830 72.389 22.512  1.00 11.17 ? 49  VAL B CG2 1 
ATOM   2396 N  N   . LYS B 1 72  ? 15.100 68.673 19.720  1.00 10.59 ? 50  LYS B N   1 
ATOM   2397 C  CA  . LYS B 1 72  ? 14.866 67.316 19.213  1.00 10.69 ? 50  LYS B CA  1 
ATOM   2398 C  C   . LYS B 1 72  ? 15.240 66.226 20.226  1.00 9.96  ? 50  LYS B C   1 
ATOM   2399 O  O   . LYS B 1 72  ? 14.818 65.078 20.087  1.00 9.57  ? 50  LYS B O   1 
ATOM   2400 C  CB  . LYS B 1 72  ? 15.689 67.093 17.946  1.00 11.66 ? 50  LYS B CB  1 
ATOM   2401 C  CG  . LYS B 1 72  ? 15.539 68.171 16.878  1.00 12.81 ? 50  LYS B CG  1 
ATOM   2402 C  CD  . LYS B 1 72  ? 14.378 67.901 15.944  1.00 13.76 ? 50  LYS B CD  1 
ATOM   2403 C  CE  . LYS B 1 72  ? 14.343 68.886 14.776  1.00 14.52 ? 50  LYS B CE  1 
ATOM   2404 N  NZ  . LYS B 1 72  ? 13.609 70.127 15.123  1.00 15.29 ? 50  LYS B NZ  1 
ATOM   2405 N  N   . ALA B 1 73  ? 16.058 66.584 21.214  1.00 9.28  ? 51  ALA B N   1 
ATOM   2406 C  CA  . ALA B 1 73  ? 16.531 65.652 22.232  1.00 8.90  ? 51  ALA B CA  1 
ATOM   2407 C  C   . ALA B 1 73  ? 17.022 66.436 23.441  1.00 8.65  ? 51  ALA B C   1 
ATOM   2408 O  O   . ALA B 1 73  ? 17.294 67.634 23.345  1.00 8.49  ? 51  ALA B O   1 
ATOM   2409 C  CB  . ALA B 1 73  ? 17.644 64.777 21.681  1.00 8.91  ? 51  ALA B CB  1 
ATOM   2410 N  N   . VAL B 1 74  ? 17.128 65.755 24.574  1.00 8.31  ? 52  VAL B N   1 
ATOM   2411 C  CA  . VAL B 1 74  ? 17.524 66.392 25.822  1.00 8.26  ? 52  VAL B CA  1 
ATOM   2412 C  C   . VAL B 1 74  ? 18.711 65.654 26.441  1.00 8.08  ? 52  VAL B C   1 
ATOM   2413 O  O   . VAL B 1 74  ? 18.692 64.433 26.575  1.00 7.97  ? 52  VAL B O   1 
ATOM   2414 C  CB  . VAL B 1 74  ? 16.359 66.414 26.834  1.00 8.44  ? 52  VAL B CB  1 
ATOM   2415 C  CG1 . VAL B 1 74  ? 16.770 67.152 28.099  1.00 8.60  ? 52  VAL B CG1 1 
ATOM   2416 C  CG2 . VAL B 1 74  ? 15.118 67.051 26.216  1.00 8.52  ? 52  VAL B CG2 1 
ATOM   2417 N  N   . ILE B 1 75  ? 19.741 66.410 26.804  1.00 7.83  ? 53  ILE B N   1 
ATOM   2418 C  CA  . ILE B 1 75  ? 20.877 65.891 27.552  1.00 7.62  ? 53  ILE B CA  1 
ATOM   2419 C  C   . ILE B 1 75  ? 20.774 66.410 28.979  1.00 7.61  ? 53  ILE B C   1 
ATOM   2420 O  O   . ILE B 1 75  ? 20.523 67.599 29.194  1.00 7.58  ? 53  ILE B O   1 
ATOM   2421 C  CB  . ILE B 1 75  ? 22.221 66.370 26.954  1.00 7.57  ? 53  ILE B CB  1 
ATOM   2422 C  CG1 . ILE B 1 75  ? 22.416 65.818 25.542  1.00 7.61  ? 53  ILE B CG1 1 
ATOM   2423 C  CG2 . ILE B 1 75  ? 23.393 65.983 27.853  1.00 7.52  ? 53  ILE B CG2 1 
ATOM   2424 C  CD1 . ILE B 1 75  ? 23.472 66.560 24.752  1.00 7.61  ? 53  ILE B CD1 1 
ATOM   2425 N  N   . VAL B 1 76  ? 20.963 65.519 29.949  1.00 7.58  ? 54  VAL B N   1 
ATOM   2426 C  CA  . VAL B 1 76  ? 21.093 65.924 31.343  1.00 7.65  ? 54  VAL B CA  1 
ATOM   2427 C  C   . VAL B 1 76  ? 22.475 65.506 31.857  1.00 7.75  ? 54  VAL B C   1 
ATOM   2428 O  O   . VAL B 1 76  ? 22.943 64.395 31.601  1.00 7.79  ? 54  VAL B O   1 
ATOM   2429 C  CB  . VAL B 1 76  ? 19.938 65.389 32.234  1.00 7.59  ? 54  VAL B CB  1 
ATOM   2430 C  CG1 . VAL B 1 76  ? 19.873 63.869 32.223  1.00 7.61  ? 54  VAL B CG1 1 
ATOM   2431 C  CG2 . VAL B 1 76  ? 20.062 65.912 33.661  1.00 7.61  ? 54  VAL B CG2 1 
ATOM   2432 N  N   . ARG B 1 77  ? 23.124 66.429 32.565  1.00 7.84  ? 55  ARG B N   1 
ATOM   2433 C  CA  . ARG B 1 77  ? 24.471 66.242 33.088  1.00 7.90  ? 55  ARG B CA  1 
ATOM   2434 C  C   . ARG B 1 77  ? 24.608 67.057 34.369  1.00 7.88  ? 55  ARG B C   1 
ATOM   2435 O  O   . ARG B 1 77  ? 23.706 67.814 34.721  1.00 7.61  ? 55  ARG B O   1 
ATOM   2436 C  CB  . ARG B 1 77  ? 25.503 66.729 32.068  1.00 8.08  ? 55  ARG B CB  1 
ATOM   2437 C  CG  . ARG B 1 77  ? 25.348 68.208 31.731  1.00 8.34  ? 55  ARG B CG  1 
ATOM   2438 C  CD  . ARG B 1 77  ? 26.524 68.769 30.950  1.00 8.65  ? 55  ARG B CD  1 
ATOM   2439 N  NE  . ARG B 1 77  ? 26.453 70.226 30.905  1.00 8.90  ? 55  ARG B NE  1 
ATOM   2440 C  CZ  . ARG B 1 77  ? 27.352 71.022 30.334  1.00 9.18  ? 55  ARG B CZ  1 
ATOM   2441 N  NH1 . ARG B 1 77  ? 28.421 70.514 29.731  1.00 9.34  ? 55  ARG B NH1 1 
ATOM   2442 N  NH2 . ARG B 1 77  ? 27.176 72.336 30.376  1.00 9.34  ? 55  ARG B NH2 1 
ATOM   2443 N  N   . GLY B 1 78  ? 25.741 66.922 35.048  1.00 8.02  ? 56  GLY B N   1 
ATOM   2444 C  CA  . GLY B 1 78  ? 26.002 67.703 36.256  1.00 8.39  ? 56  GLY B CA  1 
ATOM   2445 C  C   . GLY B 1 78  ? 27.187 68.651 36.149  1.00 8.70  ? 56  GLY B C   1 
ATOM   2446 O  O   . GLY B 1 78  ? 28.096 68.446 35.350  1.00 8.70  ? 56  GLY B O   1 
ATOM   2447 N  N   . ALA B 1 79  ? 27.159 69.690 36.975  1.00 9.13  ? 57  ALA B N   1 
ATOM   2448 C  CA  . ALA B 1 79  ? 28.273 70.634 37.093  1.00 9.59  ? 57  ALA B CA  1 
ATOM   2449 C  C   . ALA B 1 79  ? 29.250 70.211 38.189  1.00 10.05 ? 57  ALA B C   1 
ATOM   2450 O  O   . ALA B 1 79  ? 28.956 69.352 39.024  1.00 10.06 ? 57  ALA B O   1 
ATOM   2451 C  CB  . ALA B 1 79  ? 27.735 72.024 37.392  1.00 9.55  ? 57  ALA B CB  1 
ATOM   2452 N  N   . GLY B 1 80  ? 30.426 70.831 38.198  1.00 10.66 ? 58  GLY B N   1 
ATOM   2453 C  CA  . GLY B 1 80  ? 31.367 70.637 39.297  1.00 11.08 ? 58  GLY B CA  1 
ATOM   2454 C  C   . GLY B 1 80  ? 31.998 69.261 39.385  1.00 11.38 ? 58  GLY B C   1 
ATOM   2455 O  O   . GLY B 1 80  ? 32.365 68.820 40.474  1.00 12.02 ? 58  GLY B O   1 
ATOM   2456 N  N   . ASN B 1 81  ? 32.117 68.583 38.244  1.00 11.55 ? 59  ASN B N   1 
ATOM   2457 C  CA  . ASN B 1 81  ? 32.803 67.297 38.141  1.00 11.86 ? 59  ASN B CA  1 
ATOM   2458 C  C   . ASN B 1 81  ? 32.015 66.151 38.780  1.00 11.22 ? 59  ASN B C   1 
ATOM   2459 O  O   . ASN B 1 81  ? 32.591 65.177 39.260  1.00 11.63 ? 59  ASN B O   1 
ATOM   2460 C  CB  . ASN B 1 81  ? 34.220 67.388 38.739  1.00 12.62 ? 59  ASN B CB  1 
ATOM   2461 C  CG  . ASN B 1 81  ? 35.192 66.400 38.122  1.00 13.50 ? 59  ASN B CG  1 
ATOM   2462 O  OD1 . ASN B 1 81  ? 36.255 66.132 38.686  1.00 15.39 ? 59  ASN B OD1 1 
ATOM   2463 N  ND2 . ASN B 1 81  ? 34.845 65.856 36.971  1.00 13.68 ? 59  ASN B ND2 1 
ATOM   2464 N  N   . ALA B 1 82  ? 30.691 66.276 38.757  1.00 10.51 ? 60  ALA B N   1 
ATOM   2465 C  CA  . ALA B 1 82  ? 29.794 65.261 39.303  1.00 10.09 ? 60  ALA B CA  1 
ATOM   2466 C  C   . ALA B 1 82  ? 28.467 65.344 38.577  1.00 9.73  ? 60  ALA B C   1 
ATOM   2467 O  O   . ALA B 1 82  ? 28.122 66.395 38.052  1.00 9.59  ? 60  ALA B O   1 
ATOM   2468 C  CB  . ALA B 1 82  ? 29.582 65.485 40.789  1.00 10.11 ? 60  ALA B CB  1 
ATOM   2469 N  N   . PHE B 1 83  ? 27.724 64.239 38.553  1.00 9.31  ? 61  PHE B N   1 
ATOM   2470 C  CA  . PHE B 1 83  ? 26.353 64.246 38.053  1.00 9.11  ? 61  PHE B CA  1 
ATOM   2471 C  C   . PHE B 1 83  ? 25.440 64.694 39.204  1.00 9.09  ? 61  PHE B C   1 
ATOM   2472 O  O   . PHE B 1 83  ? 24.991 65.840 39.227  1.00 8.84  ? 61  PHE B O   1 
ATOM   2473 C  CB  . PHE B 1 83  ? 25.981 62.866 37.495  1.00 9.00  ? 61  PHE B CB  1 
ATOM   2474 C  CG  . PHE B 1 83  ? 24.630 62.809 36.843  1.00 9.00  ? 61  PHE B CG  1 
ATOM   2475 C  CD1 . PHE B 1 83  ? 24.444 63.294 35.558  1.00 9.01  ? 61  PHE B CD1 1 
ATOM   2476 C  CD2 . PHE B 1 83  ? 23.545 62.244 37.504  1.00 8.99  ? 61  PHE B CD2 1 
ATOM   2477 C  CE1 . PHE B 1 83  ? 23.201 63.230 34.947  1.00 9.08  ? 61  PHE B CE1 1 
ATOM   2478 C  CE2 . PHE B 1 83  ? 22.305 62.178 36.898  1.00 9.16  ? 61  PHE B CE2 1 
ATOM   2479 C  CZ  . PHE B 1 83  ? 22.129 62.675 35.620  1.00 9.06  ? 61  PHE B CZ  1 
ATOM   2480 N  N   . SER B 1 84  ? 25.197 63.806 40.165  1.00 9.05  ? 62  SER B N   1 
ATOM   2481 C  CA  . SER B 1 84  ? 24.490 64.163 41.397  1.00 9.25  ? 62  SER B CA  1 
ATOM   2482 C  C   . SER B 1 84  ? 24.561 63.032 42.423  1.00 9.52  ? 62  SER B C   1 
ATOM   2483 O  O   . SER B 1 84  ? 24.575 61.853 42.064  1.00 9.38  ? 62  SER B O   1 
ATOM   2484 C  CB  . SER B 1 84  ? 23.028 64.536 41.116  1.00 9.16  ? 62  SER B CB  1 
ATOM   2485 O  OG  . SER B 1 84  ? 22.293 64.708 42.323  1.00 9.09  ? 62  SER B OG  1 
ATOM   2486 N  N   . SER B 1 85  ? 24.609 63.406 43.701  1.00 10.01 ? 63  SER B N   1 
ATOM   2487 C  CA  . SER B 1 85  ? 24.579 62.428 44.791  1.00 10.58 ? 63  SER B CA  1 
ATOM   2488 C  C   . SER B 1 85  ? 23.154 61.984 45.150  1.00 10.77 ? 63  SER B C   1 
ATOM   2489 O  O   . SER B 1 85  ? 22.983 61.100 45.986  1.00 10.75 ? 63  SER B O   1 
ATOM   2490 C  CB  . SER B 1 85  ? 25.282 62.981 46.029  1.00 10.88 ? 63  SER B CB  1 
ATOM   2491 O  OG  . SER B 1 85  ? 24.667 64.173 46.471  1.00 11.36 ? 63  SER B OG  1 
ATOM   2492 N  N   . GLY B 1 86  ? 22.146 62.596 44.529  1.00 11.24 ? 64  GLY B N   1 
ATOM   2493 C  CA  . GLY B 1 86  ? 20.748 62.210 44.727  1.00 11.91 ? 64  GLY B CA  1 
ATOM   2494 C  C   . GLY B 1 86  ? 19.930 63.245 45.472  1.00 12.73 ? 64  GLY B C   1 
ATOM   2495 O  O   . GLY B 1 86  ? 20.324 64.408 45.573  1.00 12.67 ? 64  GLY B O   1 
ATOM   2496 N  N   . PHE B 1 87  ? 18.776 62.827 45.988  1.00 13.36 ? 65  PHE B N   1 
ATOM   2497 C  CA  . PHE B 1 87  ? 17.892 63.757 46.693  1.00 14.00 ? 65  PHE B CA  1 
ATOM   2498 C  C   . PHE B 1 87  ? 18.622 64.311 47.920  1.00 14.34 ? 65  PHE B C   1 
ATOM   2499 O  O   . PHE B 1 87  ? 19.412 63.615 48.558  1.00 14.46 ? 65  PHE B O   1 
ATOM   2500 C  CB  . PHE B 1 87  ? 16.553 63.105 47.058  1.00 14.03 ? 65  PHE B CB  1 
ATOM   2501 C  CG  . PHE B 1 87  ? 15.803 62.547 45.870  1.00 14.27 ? 65  PHE B CG  1 
ATOM   2502 C  CD1 . PHE B 1 87  ? 15.553 63.338 44.752  1.00 14.45 ? 65  PHE B CD1 1 
ATOM   2503 C  CD2 . PHE B 1 87  ? 15.348 61.233 45.866  1.00 14.37 ? 65  PHE B CD2 1 
ATOM   2504 C  CE1 . PHE B 1 87  ? 14.876 62.830 43.655  1.00 14.51 ? 65  PHE B CE1 1 
ATOM   2505 C  CE2 . PHE B 1 87  ? 14.665 60.720 44.773  1.00 14.57 ? 65  PHE B CE2 1 
ATOM   2506 C  CZ  . PHE B 1 87  ? 14.431 61.518 43.663  1.00 14.68 ? 65  PHE B CZ  1 
ATOM   2507 N  N   . ASP B 1 88  ? 18.371 65.583 48.214  1.00 15.14 ? 66  ASP B N   1 
ATOM   2508 C  CA  . ASP B 1 88  ? 19.167 66.353 49.171  1.00 15.61 ? 66  ASP B CA  1 
ATOM   2509 C  C   . ASP B 1 88  ? 18.873 65.964 50.621  1.00 16.23 ? 66  ASP B C   1 
ATOM   2510 O  O   . ASP B 1 88  ? 17.782 66.221 51.121  1.00 15.96 ? 66  ASP B O   1 
ATOM   2511 C  CB  . ASP B 1 88  ? 18.881 67.847 48.948  1.00 15.83 ? 66  ASP B CB  1 
ATOM   2512 C  CG  . ASP B 1 88  ? 19.826 68.760 49.703  1.00 16.07 ? 66  ASP B CG  1 
ATOM   2513 O  OD1 . ASP B 1 88  ? 20.445 68.329 50.693  1.00 16.56 ? 66  ASP B OD1 1 
ATOM   2514 O  OD2 . ASP B 1 88  ? 19.932 69.940 49.302  1.00 16.14 ? 66  ASP B OD2 1 
ATOM   2515 N  N   . LEU B 1 89  ? 19.856 65.362 51.293  1.00 16.92 ? 67  LEU B N   1 
ATOM   2516 C  CA  . LEU B 1 89  ? 19.679 64.907 52.677  1.00 17.51 ? 67  LEU B CA  1 
ATOM   2517 C  C   . LEU B 1 89  ? 19.831 66.032 53.696  1.00 17.67 ? 67  LEU B C   1 
ATOM   2518 O  O   . LEU B 1 89  ? 19.228 65.974 54.769  1.00 17.30 ? 67  LEU B O   1 
ATOM   2519 C  CB  . LEU B 1 89  ? 20.654 63.779 53.015  1.00 17.96 ? 67  LEU B CB  1 
ATOM   2520 C  CG  . LEU B 1 89  ? 20.529 62.489 52.200  1.00 18.34 ? 67  LEU B CG  1 
ATOM   2521 C  CD1 . LEU B 1 89  ? 21.435 61.423 52.794  1.00 18.56 ? 67  LEU B CD1 1 
ATOM   2522 C  CD2 . LEU B 1 89  ? 19.085 62.006 52.128  1.00 18.48 ? 67  LEU B CD2 1 
ATOM   2523 N  N   . LYS B 1 90  ? 20.632 67.046 53.372  1.00 18.05 ? 68  LYS B N   1 
ATOM   2524 C  CA  . LYS B 1 90  ? 20.757 68.218 54.241  1.00 18.58 ? 68  LYS B CA  1 
ATOM   2525 C  C   . LYS B 1 90  ? 19.420 68.959 54.329  1.00 17.82 ? 68  LYS B C   1 
ATOM   2526 O  O   . LYS B 1 90  ? 19.009 69.382 55.408  1.00 17.79 ? 68  LYS B O   1 
ATOM   2527 C  CB  . LYS B 1 90  ? 21.856 69.164 53.749  1.00 19.55 ? 68  LYS B CB  1 
ATOM   2528 C  CG  . LYS B 1 90  ? 22.097 70.338 54.683  1.00 20.64 ? 68  LYS B CG  1 
ATOM   2529 C  CD  . LYS B 1 90  ? 23.364 71.103 54.348  1.00 21.76 ? 68  LYS B CD  1 
ATOM   2530 C  CE  . LYS B 1 90  ? 23.407 72.430 55.091  1.00 22.27 ? 68  LYS B CE  1 
ATOM   2531 N  NZ  . LYS B 1 90  ? 24.711 73.127 54.924  1.00 22.87 ? 68  LYS B NZ  1 
ATOM   2532 N  N   . ALA B 1 91  ? 18.746 69.105 53.192  1.00 17.27 ? 69  ALA B N   1 
ATOM   2533 C  CA  . ALA B 1 91  ? 17.415 69.704 53.157  1.00 17.22 ? 69  ALA B CA  1 
ATOM   2534 C  C   . ALA B 1 91  ? 16.423 68.859 53.960  1.00 17.17 ? 69  ALA B C   1 
ATOM   2535 O  O   . ALA B 1 91  ? 15.579 69.391 54.682  1.00 16.75 ? 69  ALA B O   1 
ATOM   2536 C  CB  . ALA B 1 91  ? 16.940 69.858 51.720  1.00 17.19 ? 69  ALA B CB  1 
ATOM   2537 N  N   . GLN B 1 92  ? 16.534 67.538 53.836  1.00 17.08 ? 70  GLN B N   1 
ATOM   2538 C  CA  . GLN B 1 92  ? 15.667 66.630 54.582  1.00 17.12 ? 70  GLN B CA  1 
ATOM   2539 C  C   . GLN B 1 92  ? 15.918 66.739 56.091  1.00 18.39 ? 70  GLN B C   1 
ATOM   2540 O  O   . GLN B 1 92  ? 14.970 66.763 56.878  1.00 18.04 ? 70  GLN B O   1 
ATOM   2541 C  CB  . GLN B 1 92  ? 15.866 65.185 54.111  1.00 16.62 ? 70  GLN B CB  1 
ATOM   2542 C  CG  . GLN B 1 92  ? 14.804 64.230 54.626  1.00 16.09 ? 70  GLN B CG  1 
ATOM   2543 C  CD  . GLN B 1 92  ? 15.072 62.790 54.239  1.00 15.47 ? 70  GLN B CD  1 
ATOM   2544 O  OE1 . GLN B 1 92  ? 15.495 62.494 53.116  1.00 16.04 ? 70  GLN B OE1 1 
ATOM   2545 N  NE2 . GLN B 1 92  ? 14.821 61.885 55.166  1.00 14.57 ? 70  GLN B NE2 1 
HETATM 2546 N  N   . MSE B 1 93  ? 17.192 66.814 56.477  1.00 19.88 ? 71  MSE B N   1 
HETATM 2547 C  CA  . MSE B 1 93  ? 17.592 66.974 57.882  1.00 22.06 ? 71  MSE B CA  1 
HETATM 2548 C  C   . MSE B 1 93  ? 16.957 68.201 58.489  1.00 21.69 ? 71  MSE B C   1 
HETATM 2549 O  O   . MSE B 1 93  ? 16.492 68.170 59.628  1.00 21.07 ? 71  MSE B O   1 
HETATM 2550 C  CB  . MSE B 1 93  ? 19.115 67.107 57.965  1.00 24.73 ? 71  MSE B CB  1 
HETATM 2551 C  CG  . MSE B 1 93  ? 19.641 67.211 59.396  1.00 27.47 ? 71  MSE B CG  1 
HETATM 2552 SE SE  . MSE B 1 93  ? 21.583 67.559 59.368  1.00 33.89 ? 71  MSE B SE  1 
HETATM 2553 C  CE  . MSE B 1 93  ? 21.544 69.409 58.684  1.00 31.98 ? 71  MSE B CE  1 
ATOM   2554 N  N   . GLU B 1 94  ? 16.933 69.292 57.732  1.00 21.64 ? 72  GLU B N   1 
ATOM   2555 C  CA  . GLU B 1 94  ? 16.392 70.560 58.221  1.00 22.15 ? 72  GLU B CA  1 
ATOM   2556 C  C   . GLU B 1 94  ? 14.861 70.572 58.258  1.00 21.28 ? 72  GLU B C   1 
ATOM   2557 O  O   . GLU B 1 94  ? 14.265 71.068 59.216  1.00 21.39 ? 72  GLU B O   1 
ATOM   2558 C  CB  . GLU B 1 94  ? 16.908 71.714 57.358  1.00 23.43 ? 72  GLU B CB  1 
ATOM   2559 C  CG  . GLU B 1 94  ? 18.402 71.969 57.511  1.00 24.95 ? 72  GLU B CG  1 
ATOM   2560 C  CD  . GLU B 1 94  ? 18.971 72.912 56.460  1.00 26.16 ? 72  GLU B CD  1 
ATOM   2561 O  OE1 . GLU B 1 94  ? 18.226 73.345 55.552  1.00 27.60 ? 72  GLU B OE1 1 
ATOM   2562 O  OE2 . GLU B 1 94  ? 20.178 73.219 56.540  1.00 28.04 ? 72  GLU B OE2 1 
ATOM   2563 N  N   . ALA B 1 95  ? 14.232 70.027 57.219  1.00 20.45 ? 73  ALA B N   1 
ATOM   2564 C  CA  . ALA B 1 95  ? 12.771 70.067 57.084  1.00 20.13 ? 73  ALA B CA  1 
ATOM   2565 C  C   . ALA B 1 95  ? 12.051 69.129 58.058  1.00 19.96 ? 73  ALA B C   1 
ATOM   2566 O  O   . ALA B 1 95  ? 10.942 69.431 58.502  1.00 19.64 ? 73  ALA B O   1 
ATOM   2567 C  CB  . ALA B 1 95  ? 12.365 69.752 55.652  1.00 20.46 ? 73  ALA B CB  1 
ATOM   2568 N  N   . ARG B 1 96  ? 12.677 67.999 58.378  1.00 19.60 ? 74  ARG B N   1 
ATOM   2569 C  CA  . ARG B 1 96  ? 12.130 67.034 59.338  1.00 19.74 ? 74  ARG B CA  1 
ATOM   2570 C  C   . ARG B 1 96  ? 10.702 66.595 58.987  1.00 18.06 ? 74  ARG B C   1 
ATOM   2571 O  O   . ARG B 1 96  ? 9.808  66.670 59.836  1.00 18.12 ? 74  ARG B O   1 
ATOM   2572 C  CB  . ARG B 1 96  ? 12.132 67.611 60.766  1.00 21.54 ? 74  ARG B CB  1 
ATOM   2573 C  CG  . ARG B 1 96  ? 13.453 68.182 61.259  1.00 23.22 ? 74  ARG B CG  1 
ATOM   2574 C  CD  . ARG B 1 96  ? 14.376 67.111 61.808  1.00 24.79 ? 74  ARG B CD  1 
ATOM   2575 N  NE  . ARG B 1 96  ? 13.888 66.459 63.030  1.00 26.22 ? 74  ARG B NE  1 
ATOM   2576 C  CZ  . ARG B 1 96  ? 14.116 66.870 64.280  1.00 27.62 ? 74  ARG B CZ  1 
ATOM   2577 N  NH1 . ARG B 1 96  ? 14.818 67.974 64.533  1.00 28.01 ? 74  ARG B NH1 1 
ATOM   2578 N  NH2 . ARG B 1 96  ? 13.624 66.168 65.295  1.00 28.56 ? 74  ARG B NH2 1 
ATOM   2579 N  N   . PRO B 1 97  ? 10.472 66.140 57.739  1.00 16.23 ? 75  PRO B N   1 
ATOM   2580 C  CA  . PRO B 1 97  ? 9.128  65.643 57.442  1.00 15.40 ? 75  PRO B CA  1 
ATOM   2581 C  C   . PRO B 1 97  ? 8.783  64.462 58.337  1.00 14.34 ? 75  PRO B C   1 
ATOM   2582 O  O   . PRO B 1 97  ? 9.632  63.611 58.595  1.00 14.45 ? 75  PRO B O   1 
ATOM   2583 C  CB  . PRO B 1 97  ? 9.222  65.201 55.974  1.00 15.58 ? 75  PRO B CB  1 
ATOM   2584 C  CG  . PRO B 1 97  ? 10.675 64.998 55.723  1.00 15.72 ? 75  PRO B CG  1 
ATOM   2585 C  CD  . PRO B 1 97  ? 11.371 66.013 56.579  1.00 16.06 ? 75  PRO B CD  1 
ATOM   2586 N  N   . ALA B 1 98  ? 7.547  64.410 58.810  1.00 13.35 ? 76  ALA B N   1 
ATOM   2587 C  CA  . ALA B 1 98  ? 7.153  63.370 59.751  1.00 12.39 ? 76  ALA B CA  1 
ATOM   2588 C  C   . ALA B 1 98  ? 5.776  62.835 59.400  1.00 11.58 ? 76  ALA B C   1 
ATOM   2589 O  O   . ALA B 1 98  ? 4.800  63.581 59.395  1.00 11.56 ? 76  ALA B O   1 
ATOM   2590 C  CB  . ALA B 1 98  ? 7.162  63.918 61.166  1.00 12.69 ? 76  ALA B CB  1 
ATOM   2591 N  N   . GLY B 1 99  ? 5.711  61.546 59.084  1.00 10.58 ? 77  GLY B N   1 
ATOM   2592 C  CA  . GLY B 1 99  ? 4.438  60.879 58.859  1.00 9.96  ? 77  GLY B CA  1 
ATOM   2593 C  C   . GLY B 1 99  ? 4.082  60.741 57.397  1.00 9.46  ? 77  GLY B C   1 
ATOM   2594 O  O   . GLY B 1 99  ? 4.693  61.369 56.527  1.00 9.21  ? 77  GLY B O   1 
ATOM   2595 N  N   . VAL B 1 100 ? 3.069  59.918 57.145  1.00 9.02  ? 78  VAL B N   1 
ATOM   2596 C  CA  . VAL B 1 100 ? 2.642  59.579 55.791  1.00 8.67  ? 78  VAL B CA  1 
ATOM   2597 C  C   . VAL B 1 100 ? 2.207  60.804 54.983  1.00 8.65  ? 78  VAL B C   1 
ATOM   2598 O  O   . VAL B 1 100 ? 2.631  60.977 53.840  1.00 8.41  ? 78  VAL B O   1 
ATOM   2599 C  CB  . VAL B 1 100 ? 1.504  58.529 55.833  1.00 8.61  ? 78  VAL B CB  1 
ATOM   2600 C  CG1 . VAL B 1 100 ? 0.860  58.340 54.462  1.00 8.55  ? 78  VAL B CG1 1 
ATOM   2601 C  CG2 . VAL B 1 100 ? 2.031  57.205 56.365  1.00 8.59  ? 78  VAL B CG2 1 
ATOM   2602 N  N   . ASP B 1 101 ? 1.361  61.650 55.561  1.00 8.50  ? 79  ASP B N   1 
ATOM   2603 C  CA  . ASP B 1 101 ? 0.794  62.769 54.800  1.00 8.70  ? 79  ASP B CA  1 
ATOM   2604 C  C   . ASP B 1 101 ? 1.854  63.798 54.401  1.00 8.61  ? 79  ASP B C   1 
ATOM   2605 O  O   . ASP B 1 101 ? 1.756  64.413 53.340  1.00 8.66  ? 79  ASP B O   1 
ATOM   2606 C  CB  . ASP B 1 101 ? -0.369 63.414 55.566  1.00 8.92  ? 79  ASP B CB  1 
ATOM   2607 C  CG  . ASP B 1 101 ? -1.608 62.530 55.606  1.00 9.21  ? 79  ASP B CG  1 
ATOM   2608 O  OD1 . ASP B 1 101 ? -1.716 61.566 54.813  1.00 9.23  ? 79  ASP B OD1 1 
ATOM   2609 O  OD2 . ASP B 1 101 ? -2.494 62.794 56.440  1.00 9.62  ? 79  ASP B OD2 1 
ATOM   2610 N  N   . ALA B 1 102 ? 2.870  63.963 55.243  1.00 8.56  ? 80  ALA B N   1 
ATOM   2611 C  CA  . ALA B 1 102 ? 4.001  64.833 54.936  1.00 8.62  ? 80  ALA B CA  1 
ATOM   2612 C  C   . ALA B 1 102 ? 4.874  64.247 53.834  1.00 8.43  ? 80  ALA B C   1 
ATOM   2613 O  O   . ALA B 1 102 ? 5.336  64.969 52.949  1.00 8.59  ? 80  ALA B O   1 
ATOM   2614 C  CB  . ALA B 1 102 ? 4.832  65.070 56.186  1.00 8.65  ? 80  ALA B CB  1 
ATOM   2615 N  N   . TRP B 1 103 ? 5.108  62.939 53.887  1.00 8.35  ? 81  TRP B N   1 
ATOM   2616 C  CA  . TRP B 1 103 ? 5.990  62.290 52.924  1.00 8.31  ? 81  TRP B CA  1 
ATOM   2617 C  C   . TRP B 1 103 ? 5.357  62.070 51.550  1.00 8.32  ? 81  TRP B C   1 
ATOM   2618 O  O   . TRP B 1 103 ? 6.061  62.064 50.540  1.00 8.43  ? 81  TRP B O   1 
ATOM   2619 C  CB  . TRP B 1 103 ? 6.515  60.963 53.478  1.00 8.32  ? 81  TRP B CB  1 
ATOM   2620 C  CG  . TRP B 1 103 ? 7.758  61.132 54.271  1.00 8.39  ? 81  TRP B CG  1 
ATOM   2621 C  CD1 . TRP B 1 103 ? 7.865  61.287 55.624  1.00 8.58  ? 81  TRP B CD1 1 
ATOM   2622 C  CD2 . TRP B 1 103 ? 9.093  61.169 53.756  1.00 8.47  ? 81  TRP B CD2 1 
ATOM   2623 N  NE1 . TRP B 1 103 ? 9.186  61.425 55.980  1.00 8.68  ? 81  TRP B NE1 1 
ATOM   2624 C  CE2 . TRP B 1 103 ? 9.959  61.350 54.852  1.00 8.62  ? 81  TRP B CE2 1 
ATOM   2625 C  CE3 . TRP B 1 103 ? 9.639  61.057 52.475  1.00 8.57  ? 81  TRP B CE3 1 
ATOM   2626 C  CZ2 . TRP B 1 103 ? 11.341 61.423 54.705  1.00 8.68  ? 81  TRP B CZ2 1 
ATOM   2627 C  CZ3 . TRP B 1 103 ? 11.011 61.131 52.330  1.00 8.60  ? 81  TRP B CZ3 1 
ATOM   2628 C  CH2 . TRP B 1 103 ? 11.847 61.317 53.438  1.00 8.64  ? 81  TRP B CH2 1 
ATOM   2629 N  N   . ARG B 1 104 ? 4.044  61.881 51.498  1.00 8.29  ? 82  ARG B N   1 
ATOM   2630 C  CA  . ARG B 1 104 ? 3.391  61.574 50.219  1.00 8.46  ? 82  ARG B CA  1 
ATOM   2631 C  C   . ARG B 1 104 ? 3.738  62.572 49.097  1.00 8.51  ? 82  ARG B C   1 
ATOM   2632 O  O   . ARG B 1 104 ? 4.182  62.152 48.026  1.00 8.43  ? 82  ARG B O   1 
ATOM   2633 C  CB  . ARG B 1 104 ? 1.870  61.423 50.374  1.00 8.48  ? 82  ARG B CB  1 
ATOM   2634 C  CG  . ARG B 1 104 ? 1.169  61.047 49.072  1.00 8.61  ? 82  ARG B CG  1 
ATOM   2635 C  CD  . ARG B 1 104 ? -0.338 60.946 49.204  1.00 8.63  ? 82  ARG B CD  1 
ATOM   2636 N  NE  . ARG B 1 104 ? -0.785 59.768 49.946  1.00 8.75  ? 82  ARG B NE  1 
ATOM   2637 C  CZ  . ARG B 1 104 ? -1.179 59.759 51.219  1.00 8.75  ? 82  ARG B CZ  1 
ATOM   2638 N  NH1 . ARG B 1 104 ? -1.175 60.869 51.959  1.00 8.88  ? 82  ARG B NH1 1 
ATOM   2639 N  NH2 . ARG B 1 104 ? -1.580 58.614 51.760  1.00 8.70  ? 82  ARG B NH2 1 
ATOM   2640 N  N   . PRO B 1 105 ? 3.539  63.889 49.323  1.00 8.79  ? 83  PRO B N   1 
ATOM   2641 C  CA  . PRO B 1 105 ? 3.865  64.829 48.244  1.00 8.98  ? 83  PRO B CA  1 
ATOM   2642 C  C   . PRO B 1 105 ? 5.358  64.916 47.901  1.00 9.09  ? 83  PRO B C   1 
ATOM   2643 O  O   . PRO B 1 105 ? 5.706  65.213 46.756  1.00 9.41  ? 83  PRO B O   1 
ATOM   2644 C  CB  . PRO B 1 105 ? 3.353  66.176 48.779  1.00 9.01  ? 83  PRO B CB  1 
ATOM   2645 C  CG  . PRO B 1 105 ? 3.283  66.006 50.254  1.00 9.03  ? 83  PRO B CG  1 
ATOM   2646 C  CD  . PRO B 1 105 ? 2.905  64.576 50.464  1.00 8.90  ? 83  PRO B CD  1 
ATOM   2647 N  N   . LEU B 1 106 ? 6.225  64.673 48.879  1.00 9.22  ? 84  LEU B N   1 
ATOM   2648 C  CA  . LEU B 1 106 ? 7.671  64.694 48.645  1.00 9.43  ? 84  LEU B CA  1 
ATOM   2649 C  C   . LEU B 1 106 ? 8.071  63.552 47.708  1.00 9.27  ? 84  LEU B C   1 
ATOM   2650 O  O   . LEU B 1 106 ? 8.762  63.764 46.709  1.00 9.34  ? 84  LEU B O   1 
ATOM   2651 C  CB  . LEU B 1 106 ? 8.438  64.592 49.964  1.00 9.72  ? 84  LEU B CB  1 
ATOM   2652 C  CG  . LEU B 1 106 ? 8.206  65.733 50.957  1.00 9.97  ? 84  LEU B CG  1 
ATOM   2653 C  CD1 . LEU B 1 106 ? 8.870  65.409 52.288  1.00 10.06 ? 84  LEU B CD1 1 
ATOM   2654 C  CD2 . LEU B 1 106 ? 8.702  67.054 50.396  1.00 10.20 ? 84  LEU B CD2 1 
ATOM   2655 N  N   . LEU B 1 107 ? 7.610  62.347 48.021  1.00 9.07  ? 85  LEU B N   1 
ATOM   2656 C  CA  . LEU B 1 107 ? 7.894  61.178 47.187  1.00 8.99  ? 85  LEU B CA  1 
ATOM   2657 C  C   . LEU B 1 107 ? 7.254  61.295 45.803  1.00 9.12  ? 85  LEU B C   1 
ATOM   2658 O  O   . LEU B 1 107 ? 7.842  60.880 44.804  1.00 8.94  ? 85  LEU B O   1 
ATOM   2659 C  CB  . LEU B 1 107 ? 7.440  59.890 47.889  1.00 8.96  ? 85  LEU B CB  1 
ATOM   2660 C  CG  . LEU B 1 107 ? 8.121  59.617 49.235  1.00 9.01  ? 85  LEU B CG  1 
ATOM   2661 C  CD1 . LEU B 1 107 ? 7.574  58.349 49.864  1.00 9.10  ? 85  LEU B CD1 1 
ATOM   2662 C  CD2 . LEU B 1 107 ? 9.630  59.521 49.080  1.00 9.02  ? 85  LEU B CD2 1 
ATOM   2663 N  N   . ARG B 1 108 ? 6.058  61.870 45.743  1.00 9.43  ? 86  ARG B N   1 
ATOM   2664 C  CA  . ARG B 1 108 ? 5.336  62.030 44.479  1.00 9.92  ? 86  ARG B CA  1 
ATOM   2665 C  C   . ARG B 1 108 ? 6.123  62.911 43.509  1.00 10.01 ? 86  ARG B C   1 
ATOM   2666 O  O   . ARG B 1 108 ? 6.250  62.592 42.320  1.00 9.82  ? 86  ARG B O   1 
ATOM   2667 C  CB  . ARG B 1 108 ? 3.970  62.661 44.755  1.00 10.32 ? 86  ARG B CB  1 
ATOM   2668 C  CG  . ARG B 1 108 ? 3.011  62.679 43.580  1.00 10.83 ? 86  ARG B CG  1 
ATOM   2669 C  CD  . ARG B 1 108 ? 2.418  61.298 43.340  1.00 11.34 ? 86  ARG B CD  1 
ATOM   2670 N  NE  . ARG B 1 108 ? 2.951  60.686 42.139  1.00 11.70 ? 86  ARG B NE  1 
ATOM   2671 C  CZ  . ARG B 1 108 ? 2.764  59.416 41.781  1.00 11.99 ? 86  ARG B CZ  1 
ATOM   2672 N  NH1 . ARG B 1 108 ? 2.071  58.585 42.549  1.00 12.01 ? 86  ARG B NH1 1 
ATOM   2673 N  NH2 . ARG B 1 108 ? 3.294  58.974 40.649  1.00 12.48 ? 86  ARG B NH2 1 
ATOM   2674 N  N   . LYS B 1 109 ? 6.656  64.013 44.028  1.00 10.30 ? 87  LYS B N   1 
ATOM   2675 C  CA  . LYS B 1 109 ? 7.452  64.940 43.229  1.00 10.94 ? 87  LYS B CA  1 
ATOM   2676 C  C   . LYS B 1 109 ? 8.771  64.295 42.809  1.00 10.67 ? 87  LYS B C   1 
ATOM   2677 O  O   . LYS B 1 109 ? 9.172  64.421 41.655  1.00 10.75 ? 87  LYS B O   1 
ATOM   2678 C  CB  . LYS B 1 109 ? 7.703  66.239 44.000  1.00 11.73 ? 87  LYS B CB  1 
ATOM   2679 C  CG  . LYS B 1 109 ? 8.467  67.297 43.217  1.00 12.78 ? 87  LYS B CG  1 
ATOM   2680 C  CD  . LYS B 1 109 ? 8.515  68.618 43.970  1.00 13.88 ? 87  LYS B CD  1 
ATOM   2681 C  CE  . LYS B 1 109 ? 9.141  69.702 43.107  1.00 14.80 ? 87  LYS B CE  1 
ATOM   2682 N  NZ  . LYS B 1 109 ? 9.281  71.020 43.783  1.00 15.54 ? 87  LYS B NZ  1 
ATOM   2683 N  N   . ASP B 1 110 ? 9.440  63.614 43.745  1.00 10.61 ? 88  ASP B N   1 
ATOM   2684 C  CA  . ASP B 1 110 ? 10.671 62.860 43.453  1.00 10.53 ? 88  ASP B CA  1 
ATOM   2685 C  C   . ASP B 1 110 ? 10.440 61.891 42.291  1.00 9.60  ? 88  ASP B C   1 
ATOM   2686 O  O   . ASP B 1 110 ? 11.152 61.896 41.285  1.00 9.12  ? 88  ASP B O   1 
ATOM   2687 C  CB  . ASP B 1 110 ? 11.113 62.025 44.671  1.00 11.52 ? 88  ASP B CB  1 
ATOM   2688 C  CG  . ASP B 1 110 ? 11.730 62.851 45.803  1.00 12.48 ? 88  ASP B CG  1 
ATOM   2689 O  OD1 . ASP B 1 110 ? 12.197 63.991 45.598  1.00 13.25 ? 88  ASP B OD1 1 
ATOM   2690 O  OD2 . ASP B 1 110 ? 11.769 62.312 46.933  1.00 14.41 ? 88  ASP B OD2 1 
ATOM   2691 N  N   . PHE B 1 111 ? 9.428  61.047 42.456  1.00 8.80  ? 89  PHE B N   1 
ATOM   2692 C  CA  . PHE B 1 111 ? 9.104  60.010 41.489  1.00 8.41  ? 89  PHE B CA  1 
ATOM   2693 C  C   . PHE B 1 111 ? 8.711  60.593 40.132  1.00 8.42  ? 89  PHE B C   1 
ATOM   2694 O  O   . PHE B 1 111 ? 9.244  60.194 39.092  1.00 8.30  ? 89  PHE B O   1 
ATOM   2695 C  CB  . PHE B 1 111 ? 7.972  59.154 42.060  1.00 8.07  ? 89  PHE B CB  1 
ATOM   2696 C  CG  . PHE B 1 111 ? 7.514  58.051 41.158  1.00 7.87  ? 89  PHE B CG  1 
ATOM   2697 C  CD1 . PHE B 1 111 ? 6.587  58.292 40.160  1.00 7.81  ? 89  PHE B CD1 1 
ATOM   2698 C  CD2 . PHE B 1 111 ? 7.979  56.762 41.337  1.00 7.73  ? 89  PHE B CD2 1 
ATOM   2699 C  CE1 . PHE B 1 111 ? 6.146  57.273 39.340  1.00 7.74  ? 89  PHE B CE1 1 
ATOM   2700 C  CE2 . PHE B 1 111 ? 7.544  55.735 40.520  1.00 7.79  ? 89  PHE B CE2 1 
ATOM   2701 C  CZ  . PHE B 1 111 ? 6.628  55.989 39.521  1.00 7.75  ? 89  PHE B CZ  1 
ATOM   2702 N  N   . ASP B 1 112 ? 7.793  61.552 40.139  1.00 8.38  ? 90  ASP B N   1 
ATOM   2703 C  CA  . ASP B 1 112 ? 7.306  62.118 38.886  1.00 8.58  ? 90  ASP B CA  1 
ATOM   2704 C  C   . ASP B 1 112 ? 8.395  62.878 38.134  1.00 8.38  ? 90  ASP B C   1 
ATOM   2705 O  O   . ASP B 1 112 ? 8.411  62.863 36.914  1.00 8.42  ? 90  ASP B O   1 
ATOM   2706 C  CB  . ASP B 1 112 ? 6.078  63.001 39.122  1.00 8.94  ? 90  ASP B CB  1 
ATOM   2707 C  CG  . ASP B 1 112 ? 4.821  62.188 39.424  1.00 9.35  ? 90  ASP B CG  1 
ATOM   2708 O  OD1 . ASP B 1 112 ? 4.791  60.963 39.175  1.00 9.67  ? 90  ASP B OD1 1 
ATOM   2709 O  OD2 . ASP B 1 112 ? 3.846  62.780 39.917  1.00 10.34 ? 90  ASP B OD2 1 
ATOM   2710 N  N   . THR B 1 113 ? 9.310  63.522 38.853  1.00 8.19  ? 91  THR B N   1 
ATOM   2711 C  CA  . THR B 1 113 ? 10.398 64.257 38.198  1.00 8.12  ? 91  THR B CA  1 
ATOM   2712 C  C   . THR B 1 113 ? 11.364 63.290 37.514  1.00 8.04  ? 91  THR B C   1 
ATOM   2713 O  O   . THR B 1 113 ? 11.763 63.509 36.375  1.00 7.92  ? 91  THR B O   1 
ATOM   2714 C  CB  . THR B 1 113 ? 11.147 65.169 39.190  1.00 8.15  ? 91  THR B CB  1 
ATOM   2715 O  OG1 . THR B 1 113 ? 10.207 66.044 39.827  1.00 8.12  ? 91  THR B OG1 1 
ATOM   2716 C  CG2 . THR B 1 113 ? 12.196 66.006 38.467  1.00 8.21  ? 91  THR B CG2 1 
ATOM   2717 N  N   . VAL B 1 114 ? 11.729 62.216 38.209  1.00 7.99  ? 92  VAL B N   1 
ATOM   2718 C  CA  . VAL B 1 114 ? 12.556 61.172 37.617  1.00 8.17  ? 92  VAL B CA  1 
ATOM   2719 C  C   . VAL B 1 114 ? 11.878 60.610 36.365  1.00 8.40  ? 92  VAL B C   1 
ATOM   2720 O  O   . VAL B 1 114 ? 12.502 60.481 35.311  1.00 8.30  ? 92  VAL B O   1 
ATOM   2721 C  CB  . VAL B 1 114 ? 12.843 60.045 38.638  1.00 8.15  ? 92  VAL B CB  1 
ATOM   2722 C  CG1 . VAL B 1 114 ? 13.328 58.773 37.950  1.00 8.21  ? 92  VAL B CG1 1 
ATOM   2723 C  CG2 . VAL B 1 114 ? 13.856 60.517 39.671  1.00 8.18  ? 92  VAL B CG2 1 
HETATM 2724 N  N   . MSE B 1 115 ? 10.590 60.303 36.468  1.00 8.85  ? 93  MSE B N   1 
HETATM 2725 C  CA  . MSE B 1 115 ? 9.889  59.663 35.358  1.00 9.62  ? 93  MSE B CA  1 
HETATM 2726 C  C   . MSE B 1 115 ? 9.631  60.595 34.191  1.00 8.94  ? 93  MSE B C   1 
HETATM 2727 O  O   . MSE B 1 115 ? 9.273  60.126 33.122  1.00 8.51  ? 93  MSE B O   1 
HETATM 2728 C  CB  . MSE B 1 115 ? 8.600  59.007 35.853  1.00 11.14 ? 93  MSE B CB  1 
HETATM 2729 C  CG  . MSE B 1 115 ? 8.879  57.817 36.779  1.00 12.71 ? 93  MSE B CG  1 
HETATM 2730 SE SE  . MSE B 1 115 ? 9.958  56.380 35.963  1.00 17.31 ? 93  MSE B SE  1 
HETATM 2731 C  CE  . MSE B 1 115 ? 8.635  55.789 34.630  1.00 15.41 ? 93  MSE B CE  1 
ATOM   2732 N  N   . ARG B 1 116 ? 9.831  61.904 34.358  1.00 8.43  ? 94  ARG B N   1 
ATOM   2733 C  CA  . ARG B 1 116 ? 9.798  62.831 33.208  1.00 8.27  ? 94  ARG B CA  1 
ATOM   2734 C  C   . ARG B 1 116 ? 10.730 62.363 32.093  1.00 7.85  ? 94  ARG B C   1 
ATOM   2735 O  O   . ARG B 1 116 ? 10.441 62.545 30.913  1.00 7.64  ? 94  ARG B O   1 
ATOM   2736 C  CB  . ARG B 1 116 ? 10.247 64.249 33.591  1.00 8.44  ? 94  ARG B CB  1 
ATOM   2737 C  CG  . ARG B 1 116 ? 9.358  65.031 34.541  1.00 8.75  ? 94  ARG B CG  1 
ATOM   2738 C  CD  . ARG B 1 116 ? 7.988  65.381 33.979  1.00 8.85  ? 94  ARG B CD  1 
ATOM   2739 N  NE  . ARG B 1 116 ? 7.983  66.153 32.723  1.00 8.99  ? 94  ARG B NE  1 
ATOM   2740 C  CZ  . ARG B 1 116 ? 7.858  67.480 32.611  1.00 9.23  ? 94  ARG B CZ  1 
ATOM   2741 N  NH1 . ARG B 1 116 ? 7.771  68.278 33.674  1.00 9.36  ? 94  ARG B NH1 1 
ATOM   2742 N  NH2 . ARG B 1 116 ? 7.839  68.027 31.404  1.00 9.29  ? 94  ARG B NH2 1 
ATOM   2743 N  N   . PHE B 1 117 ? 11.860 61.776 32.474  1.00 7.71  ? 95  PHE B N   1 
ATOM   2744 C  CA  . PHE B 1 117 ? 12.890 61.399 31.501  1.00 7.70  ? 95  PHE B CA  1 
ATOM   2745 C  C   . PHE B 1 117 ? 12.533 60.135 30.731  1.00 7.84  ? 95  PHE B C   1 
ATOM   2746 O  O   . PHE B 1 117 ? 12.981 59.950 29.595  1.00 7.74  ? 95  PHE B O   1 
ATOM   2747 C  CB  . PHE B 1 117 ? 14.256 61.315 32.185  1.00 7.79  ? 95  PHE B CB  1 
ATOM   2748 C  CG  . PHE B 1 117 ? 14.728 62.648 32.680  1.00 7.79  ? 95  PHE B CG  1 
ATOM   2749 C  CD1 . PHE B 1 117 ? 15.517 63.449 31.879  1.00 7.80  ? 95  PHE B CD1 1 
ATOM   2750 C  CD2 . PHE B 1 117 ? 14.312 63.136 33.909  1.00 7.84  ? 95  PHE B CD2 1 
ATOM   2751 C  CE1 . PHE B 1 117 ? 15.916 64.700 32.306  1.00 7.85  ? 95  PHE B CE1 1 
ATOM   2752 C  CE2 . PHE B 1 117 ? 14.707 64.386 34.343  1.00 7.91  ? 95  PHE B CE2 1 
ATOM   2753 C  CZ  . PHE B 1 117 ? 15.513 65.169 33.534  1.00 7.89  ? 95  PHE B CZ  1 
ATOM   2754 N  N   . TRP B 1 118 ? 11.702 59.287 31.332  1.00 7.84  ? 96  TRP B N   1 
ATOM   2755 C  CA  . TRP B 1 118 ? 11.161 58.116 30.639  1.00 8.05  ? 96  TRP B CA  1 
ATOM   2756 C  C   . TRP B 1 118 ? 10.020 58.539 29.704  1.00 8.00  ? 96  TRP B C   1 
ATOM   2757 O  O   . TRP B 1 118 ? 10.030 58.217 28.513  1.00 7.85  ? 96  TRP B O   1 
ATOM   2758 C  CB  . TRP B 1 118 ? 10.687 57.060 31.659  1.00 8.30  ? 96  TRP B CB  1 
ATOM   2759 C  CG  . TRP B 1 118 ? 9.902  55.926 31.046  1.00 8.57  ? 96  TRP B CG  1 
ATOM   2760 C  CD1 . TRP B 1 118 ? 8.546  55.864 30.889  1.00 8.78  ? 96  TRP B CD1 1 
ATOM   2761 C  CD2 . TRP B 1 118 ? 10.423 54.707 30.505  1.00 8.90  ? 96  TRP B CD2 1 
ATOM   2762 N  NE1 . TRP B 1 118 ? 8.193  54.686 30.283  1.00 9.07  ? 96  TRP B NE1 1 
ATOM   2763 C  CE2 . TRP B 1 118 ? 9.325  53.957 30.033  1.00 8.93  ? 96  TRP B CE2 1 
ATOM   2764 C  CE3 . TRP B 1 118 ? 11.711 54.180 30.366  1.00 8.98  ? 96  TRP B CE3 1 
ATOM   2765 C  CZ2 . TRP B 1 118 ? 9.478  52.706 29.434  1.00 9.00  ? 96  TRP B CZ2 1 
ATOM   2766 C  CZ3 . TRP B 1 118 ? 11.861 52.932 29.780  1.00 9.19  ? 96  TRP B CZ3 1 
ATOM   2767 C  CH2 . TRP B 1 118 ? 10.747 52.213 29.317  1.00 9.10  ? 96  TRP B CH2 1 
ATOM   2768 N  N   . HIS B 1 119 ? 9.051  59.277 30.242  1.00 8.04  ? 97  HIS B N   1 
ATOM   2769 C  CA  . HIS B 1 119 ? 7.852  59.660 29.487  1.00 8.26  ? 97  HIS B CA  1 
ATOM   2770 C  C   . HIS B 1 119 ? 8.081  60.749 28.441  1.00 8.21  ? 97  HIS B C   1 
ATOM   2771 O  O   . HIS B 1 119 ? 7.226  60.952 27.568  1.00 8.42  ? 97  HIS B O   1 
ATOM   2772 C  CB  . HIS B 1 119 ? 6.738  60.118 30.428  1.00 8.40  ? 97  HIS B CB  1 
ATOM   2773 C  CG  . HIS B 1 119 ? 6.210  59.036 31.313  1.00 8.77  ? 97  HIS B CG  1 
ATOM   2774 N  ND1 . HIS B 1 119 ? 5.530  57.943 30.826  1.00 9.08  ? 97  HIS B ND1 1 
ATOM   2775 C  CD2 . HIS B 1 119 ? 6.242  58.892 32.659  1.00 9.05  ? 97  HIS B CD2 1 
ATOM   2776 C  CE1 . HIS B 1 119 ? 5.177  57.163 31.833  1.00 9.04  ? 97  HIS B CE1 1 
ATOM   2777 N  NE2 . HIS B 1 119 ? 5.596  57.717 32.956  1.00 9.06  ? 97  HIS B NE2 1 
ATOM   2778 N  N   . CYS B 1 120 ? 9.201  61.458 28.522  1.00 8.09  ? 98  CYS B N   1 
ATOM   2779 C  CA  . CYS B 1 120 ? 9.480  62.536 27.574  1.00 8.15  ? 98  CYS B CA  1 
ATOM   2780 C  C   . CYS B 1 120 ? 9.242  62.062 26.138  1.00 8.12  ? 98  CYS B C   1 
ATOM   2781 O  O   . CYS B 1 120 ? 9.774  61.034 25.730  1.00 7.94  ? 98  CYS B O   1 
ATOM   2782 C  CB  . CYS B 1 120 ? 10.920 63.023 27.731  1.00 8.11  ? 98  CYS B CB  1 
ATOM   2783 S  SG  . CYS B 1 120 ? 11.320 64.461 26.708  1.00 8.18  ? 98  CYS B SG  1 
ATOM   2784 N  N   . PRO B 1 121 ? 8.423  62.797 25.367  1.00 8.23  ? 99  PRO B N   1 
ATOM   2785 C  CA  . PRO B 1 121 ? 8.220  62.413 23.966  1.00 8.24  ? 99  PRO B CA  1 
ATOM   2786 C  C   . PRO B 1 121 ? 9.503  62.390 23.131  1.00 8.16  ? 99  PRO B C   1 
ATOM   2787 O  O   . PRO B 1 121 ? 9.577  61.667 22.139  1.00 8.36  ? 99  PRO B O   1 
ATOM   2788 C  CB  . PRO B 1 121 ? 7.266  63.490 23.448  1.00 8.34  ? 99  PRO B CB  1 
ATOM   2789 C  CG  . PRO B 1 121 ? 6.512  63.918 24.648  1.00 8.46  ? 99  PRO B CG  1 
ATOM   2790 C  CD  . PRO B 1 121 ? 7.488  63.859 25.783  1.00 8.34  ? 99  PRO B CD  1 
ATOM   2791 N  N   . LYS B 1 122 ? 10.493 63.187 23.533  1.00 7.97  ? 100 LYS B N   1 
ATOM   2792 C  CA  . LYS B 1 122 ? 11.764 63.285 22.835  1.00 7.90  ? 100 LYS B CA  1 
ATOM   2793 C  C   . LYS B 1 122 ? 12.799 62.429 23.567  1.00 7.69  ? 100 LYS B C   1 
ATOM   2794 O  O   . LYS B 1 122 ? 12.679 62.206 24.778  1.00 7.71  ? 100 LYS B O   1 
ATOM   2795 C  CB  . LYS B 1 122 ? 12.213 64.751 22.793  1.00 8.08  ? 100 LYS B CB  1 
ATOM   2796 C  CG  . LYS B 1 122 ? 11.166 65.661 22.159  1.00 8.17  ? 100 LYS B CG  1 
ATOM   2797 C  CD  . LYS B 1 122 ? 11.498 67.140 22.275  1.00 8.28  ? 100 LYS B CD  1 
ATOM   2798 C  CE  . LYS B 1 122 ? 10.376 67.964 21.660  1.00 8.38  ? 100 LYS B CE  1 
ATOM   2799 N  NZ  . LYS B 1 122 ? 10.636 69.428 21.645  1.00 8.41  ? 100 LYS B NZ  1 
ATOM   2800 N  N   . PRO B 1 123 ? 13.827 61.954 22.847  1.00 7.44  ? 101 PRO B N   1 
ATOM   2801 C  CA  . PRO B 1 123 ? 14.812 61.133 23.542  1.00 7.37  ? 101 PRO B CA  1 
ATOM   2802 C  C   . PRO B 1 123 ? 15.646 61.893 24.572  1.00 7.28  ? 101 PRO B C   1 
ATOM   2803 O  O   . PRO B 1 123 ? 15.982 63.066 24.377  1.00 7.24  ? 101 PRO B O   1 
ATOM   2804 C  CB  . PRO B 1 123 ? 15.692 60.603 22.405  1.00 7.38  ? 101 PRO B CB  1 
ATOM   2805 C  CG  . PRO B 1 123 ? 14.794 60.632 21.213  1.00 7.46  ? 101 PRO B CG  1 
ATOM   2806 C  CD  . PRO B 1 123 ? 14.031 61.908 21.391  1.00 7.44  ? 101 PRO B CD  1 
ATOM   2807 N  N   . THR B 1 124 ? 15.967 61.202 25.661  1.00 7.12  ? 102 THR B N   1 
ATOM   2808 C  CA  . THR B 1 124 ? 16.729 61.775 26.761  1.00 7.03  ? 102 THR B CA  1 
ATOM   2809 C  C   . THR B 1 124 ? 18.021 60.998 26.953  1.00 7.05  ? 102 THR B C   1 
ATOM   2810 O  O   . THR B 1 124 ? 18.051 59.772 26.838  1.00 6.74  ? 102 THR B O   1 
ATOM   2811 C  CB  . THR B 1 124 ? 15.929 61.750 28.069  1.00 7.09  ? 102 THR B CB  1 
ATOM   2812 O  OG1 . THR B 1 124 ? 15.455 60.419 28.315  1.00 7.06  ? 102 THR B OG1 1 
ATOM   2813 C  CG2 . THR B 1 124 ? 14.755 62.696 27.995  1.00 7.15  ? 102 THR B CG2 1 
ATOM   2814 N  N   . ILE B 1 125 ? 19.095 61.730 27.243  1.00 7.04  ? 103 ILE B N   1 
ATOM   2815 C  CA  . ILE B 1 125 ? 20.423 61.156 27.351  1.00 7.24  ? 103 ILE B CA  1 
ATOM   2816 C  C   . ILE B 1 125 ? 21.071 61.664 28.632  1.00 7.21  ? 103 ILE B C   1 
ATOM   2817 O  O   . ILE B 1 125 ? 21.278 62.870 28.786  1.00 7.33  ? 103 ILE B O   1 
ATOM   2818 C  CB  . ILE B 1 125 ? 21.312 61.573 26.160  1.00 7.34  ? 103 ILE B CB  1 
ATOM   2819 C  CG1 . ILE B 1 125 ? 20.660 61.191 24.823  1.00 7.51  ? 103 ILE B CG1 1 
ATOM   2820 C  CG2 . ILE B 1 125 ? 22.709 60.982 26.299  1.00 7.50  ? 103 ILE B CG2 1 
ATOM   2821 C  CD1 . ILE B 1 125 ? 21.058 62.101 23.685  1.00 7.67  ? 103 ILE B CD1 1 
ATOM   2822 N  N   . ALA B 1 126 ? 21.376 60.752 29.552  1.00 7.18  ? 104 ALA B N   1 
ATOM   2823 C  CA  . ALA B 1 126 ? 22.116 61.097 30.762  1.00 7.19  ? 104 ALA B CA  1 
ATOM   2824 C  C   . ALA B 1 126 ? 23.605 61.026 30.440  1.00 7.26  ? 104 ALA B C   1 
ATOM   2825 O  O   . ALA B 1 126 ? 24.079 60.024 29.895  1.00 7.41  ? 104 ALA B O   1 
ATOM   2826 C  CB  . ALA B 1 126 ? 21.767 60.151 31.903  1.00 7.22  ? 104 ALA B CB  1 
ATOM   2827 N  N   . ALA B 1 127 ? 24.323 62.105 30.745  1.00 7.30  ? 105 ALA B N   1 
ATOM   2828 C  CA  . ALA B 1 127 ? 25.765 62.190 30.525  1.00 7.39  ? 105 ALA B CA  1 
ATOM   2829 C  C   . ALA B 1 127 ? 26.420 62.355 31.889  1.00 7.49  ? 105 ALA B C   1 
ATOM   2830 O  O   . ALA B 1 127 ? 26.297 63.404 32.524  1.00 7.45  ? 105 ALA B O   1 
ATOM   2831 C  CB  . ALA B 1 127 ? 26.094 63.358 29.611  1.00 7.45  ? 105 ALA B CB  1 
ATOM   2832 N  N   . VAL B 1 128 ? 27.090 61.301 32.345  1.00 7.46  ? 106 VAL B N   1 
ATOM   2833 C  CA  . VAL B 1 128 ? 27.492 61.171 33.743  1.00 7.63  ? 106 VAL B CA  1 
ATOM   2834 C  C   . VAL B 1 128 ? 29.010 61.197 33.930  1.00 7.84  ? 106 VAL B C   1 
ATOM   2835 O  O   . VAL B 1 128 ? 29.742 60.454 33.281  1.00 7.71  ? 106 VAL B O   1 
ATOM   2836 C  CB  . VAL B 1 128 ? 26.937 59.846 34.330  1.00 7.64  ? 106 VAL B CB  1 
ATOM   2837 C  CG1 . VAL B 1 128 ? 27.395 59.635 35.761  1.00 7.66  ? 106 VAL B CG1 1 
ATOM   2838 C  CG2 . VAL B 1 128 ? 25.419 59.821 34.244  1.00 7.69  ? 106 VAL B CG2 1 
ATOM   2839 N  N   . ARG B 1 129 ? 29.473 62.061 34.831  1.00 8.26  ? 107 ARG B N   1 
ATOM   2840 C  CA  . ARG B 1 129 ? 30.825 61.966 35.377  1.00 8.64  ? 107 ARG B CA  1 
ATOM   2841 C  C   . ARG B 1 129 ? 30.730 61.928 36.896  1.00 8.53  ? 107 ARG B C   1 
ATOM   2842 O  O   . ARG B 1 129 ? 29.733 62.364 37.471  1.00 8.29  ? 107 ARG B O   1 
ATOM   2843 C  CB  . ARG B 1 129 ? 31.705 63.131 34.910  1.00 9.22  ? 107 ARG B CB  1 
ATOM   2844 C  CG  . ARG B 1 129 ? 31.222 64.500 35.339  1.00 9.76  ? 107 ARG B CG  1 
ATOM   2845 C  CD  . ARG B 1 129 ? 32.184 65.591 34.888  1.00 10.21 ? 107 ARG B CD  1 
ATOM   2846 N  NE  . ARG B 1 129 ? 32.153 65.823 33.448  1.00 10.68 ? 107 ARG B NE  1 
ATOM   2847 C  CZ  . ARG B 1 129 ? 33.071 65.415 32.571  1.00 10.92 ? 107 ARG B CZ  1 
ATOM   2848 N  NH1 . ARG B 1 129 ? 34.141 64.723 32.951  1.00 11.34 ? 107 ARG B NH1 1 
ATOM   2849 N  NH2 . ARG B 1 129 ? 32.919 65.717 31.291  1.00 11.55 ? 107 ARG B NH2 1 
ATOM   2850 N  N   . GLY B 1 130 ? 31.752 61.386 37.548  1.00 8.38  ? 108 GLY B N   1 
ATOM   2851 C  CA  . GLY B 1 130 ? 31.755 61.302 39.006  1.00 8.35  ? 108 GLY B CA  1 
ATOM   2852 C  C   . GLY B 1 130 ? 30.541 60.570 39.563  1.00 8.25  ? 108 GLY B C   1 
ATOM   2853 O  O   . GLY B 1 130 ? 30.047 59.634 38.936  1.00 8.24  ? 108 GLY B O   1 
ATOM   2854 N  N   . PRO B 1 131 ? 30.032 61.006 40.731  1.00 8.13  ? 109 PRO B N   1 
ATOM   2855 C  CA  . PRO B 1 131 ? 28.943 60.249 41.366  1.00 8.03  ? 109 PRO B CA  1 
ATOM   2856 C  C   . PRO B 1 131 ? 27.598 60.399 40.666  1.00 7.96  ? 109 PRO B C   1 
ATOM   2857 O  O   . PRO B 1 131 ? 27.236 61.486 40.216  1.00 7.84  ? 109 PRO B O   1 
ATOM   2858 C  CB  . PRO B 1 131 ? 28.864 60.847 42.774  1.00 8.15  ? 109 PRO B CB  1 
ATOM   2859 C  CG  . PRO B 1 131 ? 29.417 62.221 42.619  1.00 8.20  ? 109 PRO B CG  1 
ATOM   2860 C  CD  . PRO B 1 131 ? 30.487 62.119 41.579  1.00 8.20  ? 109 PRO B CD  1 
ATOM   2861 N  N   . CYS B 1 132 ? 26.873 59.289 40.602  1.00 7.90  ? 110 CYS B N   1 
ATOM   2862 C  CA  . CYS B 1 132 ? 25.510 59.261 40.103  1.00 7.88  ? 110 CYS B CA  1 
ATOM   2863 C  C   . CYS B 1 132 ? 24.786 58.295 41.027  1.00 7.74  ? 110 CYS B C   1 
ATOM   2864 O  O   . CYS B 1 132 ? 24.760 57.090 40.776  1.00 7.69  ? 110 CYS B O   1 
ATOM   2865 C  CB  . CYS B 1 132 ? 25.496 58.772 38.662  1.00 7.95  ? 110 CYS B CB  1 
ATOM   2866 S  SG  . CYS B 1 132 ? 23.855 58.611 37.932  1.00 8.24  ? 110 CYS B SG  1 
ATOM   2867 N  N   . LEU B 1 133 ? 24.233 58.829 42.112  1.00 7.70  ? 111 LEU B N   1 
ATOM   2868 C  CA  . LEU B 1 133 ? 23.788 57.995 43.231  1.00 7.73  ? 111 LEU B CA  1 
ATOM   2869 C  C   . LEU B 1 133 ? 22.333 58.212 43.611  1.00 7.61  ? 111 LEU B C   1 
ATOM   2870 O  O   . LEU B 1 133 ? 21.789 59.302 43.439  1.00 7.67  ? 111 LEU B O   1 
ATOM   2871 C  CB  . LEU B 1 133 ? 24.665 58.260 44.455  1.00 7.92  ? 111 LEU B CB  1 
ATOM   2872 C  CG  . LEU B 1 133 ? 26.169 58.029 44.264  1.00 8.11  ? 111 LEU B CG  1 
ATOM   2873 C  CD1 . LEU B 1 133 ? 26.928 58.432 45.518  1.00 8.34  ? 111 LEU B CD1 1 
ATOM   2874 C  CD2 . LEU B 1 133 ? 26.465 56.584 43.901  1.00 8.24  ? 111 LEU B CD2 1 
ATOM   2875 N  N   . ALA B 1 134 ? 21.711 57.148 44.113  1.00 7.54  ? 112 ALA B N   1 
ATOM   2876 C  CA  . ALA B 1 134 ? 20.402 57.233 44.744  1.00 7.46  ? 112 ALA B CA  1 
ATOM   2877 C  C   . ALA B 1 134 ? 19.363 57.799 43.767  1.00 7.35  ? 112 ALA B C   1 
ATOM   2878 O  O   . ALA B 1 134 ? 19.237 57.290 42.658  1.00 7.23  ? 112 ALA B O   1 
ATOM   2879 C  CB  . ALA B 1 134 ? 20.498 58.045 46.033  1.00 7.60  ? 112 ALA B CB  1 
ATOM   2880 N  N   . GLY B 1 135 ? 18.636 58.846 44.149  1.00 7.35  ? 113 GLY B N   1 
ATOM   2881 C  CA  . GLY B 1 135 ? 17.658 59.467 43.249  1.00 7.38  ? 113 GLY B CA  1 
ATOM   2882 C  C   . GLY B 1 135 ? 18.222 59.922 41.911  1.00 7.50  ? 113 GLY B C   1 
ATOM   2883 O  O   . GLY B 1 135 ? 17.507 59.954 40.918  1.00 7.52  ? 113 GLY B O   1 
ATOM   2884 N  N   . ALA B 1 136 ? 19.501 60.286 41.883  1.00 7.59  ? 114 ALA B N   1 
ATOM   2885 C  CA  . ALA B 1 136 ? 20.158 60.676 40.639  1.00 7.73  ? 114 ALA B CA  1 
ATOM   2886 C  C   . ALA B 1 136 ? 20.490 59.474 39.763  1.00 7.93  ? 114 ALA B C   1 
ATOM   2887 O  O   . ALA B 1 136 ? 20.475 59.576 38.543  1.00 7.76  ? 114 ALA B O   1 
ATOM   2888 C  CB  . ALA B 1 136 ? 21.419 61.464 40.939  1.00 7.74  ? 114 ALA B CB  1 
ATOM   2889 N  N   . CYS B 1 137 ? 20.811 58.345 40.390  1.00 8.31  ? 115 CYS B N   1 
ATOM   2890 C  CA  . CYS B 1 137 ? 20.985 57.093 39.658  1.00 8.72  ? 115 CYS B CA  1 
ATOM   2891 C  C   . CYS B 1 137 ? 19.659 56.717 38.998  1.00 8.60  ? 115 CYS B C   1 
ATOM   2892 O  O   . CYS B 1 137 ? 19.629 56.291 37.841  1.00 8.40  ? 115 CYS B O   1 
ATOM   2893 C  CB  . CYS B 1 137 ? 21.461 55.982 40.593  1.00 9.18  ? 115 CYS B CB  1 
ATOM   2894 S  SG  . CYS B 1 137 ? 21.921 54.447 39.761  1.00 10.64 ? 115 CYS B SG  1 
ATOM   2895 N  N   . GLU B 1 138 ? 18.562 56.917 39.726  1.00 8.58  ? 116 GLU B N   1 
ATOM   2896 C  CA  . GLU B 1 138 ? 17.227 56.618 39.204  1.00 8.65  ? 116 GLU B CA  1 
ATOM   2897 C  C   . GLU B 1 138 ? 16.874 57.550 38.041  1.00 8.27  ? 116 GLU B C   1 
ATOM   2898 O  O   . GLU B 1 138 ? 16.329 57.117 37.024  1.00 7.87  ? 116 GLU B O   1 
ATOM   2899 C  CB  . GLU B 1 138 ? 16.192 56.689 40.341  1.00 9.27  ? 116 GLU B CB  1 
ATOM   2900 C  CG  . GLU B 1 138 ? 16.436 55.592 41.376  1.00 9.87  ? 116 GLU B CG  1 
ATOM   2901 C  CD  . GLU B 1 138 ? 15.733 55.779 42.707  1.00 10.63 ? 116 GLU B CD  1 
ATOM   2902 O  OE1 . GLU B 1 138 ? 14.957 56.729 42.896  1.00 11.17 ? 116 GLU B OE1 1 
ATOM   2903 O  OE2 . GLU B 1 138 ? 15.975 54.928 43.584  1.00 12.14 ? 116 GLU B OE2 1 
ATOM   2904 N  N   . LEU B 1 139 ? 17.211 58.828 38.186  1.00 8.01  ? 117 LEU B N   1 
ATOM   2905 C  CA  . LEU B 1 139 ? 17.055 59.790 37.102  1.00 7.96  ? 117 LEU B CA  1 
ATOM   2906 C  C   . LEU B 1 139 ? 17.774 59.311 35.832  1.00 7.58  ? 117 LEU B C   1 
ATOM   2907 O  O   . LEU B 1 139 ? 17.189 59.301 34.747  1.00 7.22  ? 117 LEU B O   1 
ATOM   2908 C  CB  . LEU B 1 139 ? 17.557 61.174 37.539  1.00 8.22  ? 117 LEU B CB  1 
ATOM   2909 C  CG  . LEU B 1 139 ? 17.092 62.369 36.694  1.00 8.56  ? 117 LEU B CG  1 
ATOM   2910 C  CD1 . LEU B 1 139 ? 17.153 63.660 37.504  1.00 8.86  ? 117 LEU B CD1 1 
ATOM   2911 C  CD2 . LEU B 1 139 ? 17.897 62.513 35.413  1.00 8.67  ? 117 LEU B CD2 1 
ATOM   2912 N  N   . ALA B 1 140 ? 19.033 58.905 35.967  1.00 7.28  ? 118 ALA B N   1 
ATOM   2913 C  CA  . ALA B 1 140 ? 19.778 58.393 34.820  1.00 7.15  ? 118 ALA B CA  1 
ATOM   2914 C  C   . ALA B 1 140 ? 19.171 57.095 34.275  1.00 7.07  ? 118 ALA B C   1 
ATOM   2915 O  O   . ALA B 1 140 ? 19.092 56.912 33.065  1.00 7.02  ? 118 ALA B O   1 
ATOM   2916 C  CB  . ALA B 1 140 ? 21.245 58.202 35.164  1.00 7.15  ? 118 ALA B CB  1 
ATOM   2917 N  N   . LEU B 1 141 ? 18.719 56.210 35.162  1.00 7.05  ? 119 LEU B N   1 
ATOM   2918 C  CA  . LEU B 1 141 ? 18.058 54.977 34.721  1.00 7.05  ? 119 LEU B CA  1 
ATOM   2919 C  C   . LEU B 1 141 ? 16.839 55.267 33.844  1.00 7.06  ? 119 LEU B C   1 
ATOM   2920 O  O   . LEU B 1 141 ? 16.561 54.525 32.901  1.00 7.09  ? 119 LEU B O   1 
ATOM   2921 C  CB  . LEU B 1 141 ? 17.628 54.116 35.911  1.00 7.17  ? 119 LEU B CB  1 
ATOM   2922 C  CG  . LEU B 1 141 ? 18.704 53.378 36.709  1.00 7.32  ? 119 LEU B CG  1 
ATOM   2923 C  CD1 . LEU B 1 141 ? 18.081 52.706 37.926  1.00 7.42  ? 119 LEU B CD1 1 
ATOM   2924 C  CD2 . LEU B 1 141 ? 19.431 52.346 35.864  1.00 7.47  ? 119 LEU B CD2 1 
ATOM   2925 N  N   . ALA B 1 142 ? 16.120 56.341 34.158  1.00 7.07  ? 120 ALA B N   1 
ATOM   2926 C  CA  . ALA B 1 142 ? 14.905 56.701 33.421  1.00 7.12  ? 120 ALA B CA  1 
ATOM   2927 C  C   . ALA B 1 142 ? 15.192 57.251 32.023  1.00 7.30  ? 120 ALA B C   1 
ATOM   2928 O  O   . ALA B 1 142 ? 14.307 57.258 31.161  1.00 7.47  ? 120 ALA B O   1 
ATOM   2929 C  CB  . ALA B 1 142 ? 14.087 57.711 34.220  1.00 7.04  ? 120 ALA B CB  1 
ATOM   2930 N  N   . CYS B 1 143 ? 16.411 57.726 31.791  1.00 7.37  ? 121 CYS B N   1 
ATOM   2931 C  CA  . CYS B 1 143 ? 16.760 58.285 30.485  1.00 7.55  ? 121 CYS B CA  1 
ATOM   2932 C  C   . CYS B 1 143 ? 16.867 57.186 29.438  1.00 7.76  ? 121 CYS B C   1 
ATOM   2933 O  O   . CYS B 1 143 ? 17.177 56.037 29.749  1.00 7.85  ? 121 CYS B O   1 
ATOM   2934 C  CB  . CYS B 1 143 ? 18.069 59.071 30.548  1.00 7.52  ? 121 CYS B CB  1 
ATOM   2935 S  SG  . CYS B 1 143 ? 17.960 60.609 31.488  1.00 7.64  ? 121 CYS B SG  1 
ATOM   2936 N  N   . ASP B 1 144 ? 16.607 57.544 28.189  1.00 8.21  ? 122 ASP B N   1 
ATOM   2937 C  CA  . ASP B 1 144 ? 16.647 56.569 27.108  1.00 8.63  ? 122 ASP B CA  1 
ATOM   2938 C  C   . ASP B 1 144 ? 18.025 55.950 26.958  1.00 8.98  ? 122 ASP B C   1 
ATOM   2939 O  O   . ASP B 1 144 ? 18.142 54.748 26.729  1.00 8.68  ? 122 ASP B O   1 
ATOM   2940 C  CB  . ASP B 1 144 ? 16.181 57.199 25.805  1.00 8.84  ? 122 ASP B CB  1 
ATOM   2941 C  CG  . ASP B 1 144 ? 14.742 57.627 25.877  1.00 9.13  ? 122 ASP B CG  1 
ATOM   2942 O  OD1 . ASP B 1 144 ? 13.886 56.762 26.166  1.00 9.74  ? 122 ASP B OD1 1 
ATOM   2943 O  OD2 . ASP B 1 144 ? 14.452 58.820 25.695  1.00 9.26  ? 122 ASP B OD2 1 
HETATM 2944 N  N   . MSE B 1 145 ? 19.064 56.777 27.093  1.00 9.47  ? 123 MSE B N   1 
HETATM 2945 C  CA  . MSE B 1 145 ? 20.440 56.304 27.067  1.00 10.23 ? 123 MSE B CA  1 
HETATM 2946 C  C   . MSE B 1 145 ? 21.240 56.959 28.158  1.00 9.11  ? 123 MSE B C   1 
HETATM 2947 O  O   . MSE B 1 145 ? 20.902 58.038 28.616  1.00 8.46  ? 123 MSE B O   1 
HETATM 2948 C  CB  . MSE B 1 145 ? 21.096 56.663 25.746  1.00 12.49 ? 123 MSE B CB  1 
HETATM 2949 C  CG  . MSE B 1 145 ? 20.491 55.875 24.594  1.00 14.73 ? 123 MSE B CG  1 
HETATM 2950 SE SE  . MSE B 1 145 ? 21.359 56.488 22.941  1.00 21.84 ? 123 MSE B SE  1 
HETATM 2951 C  CE  . MSE B 1 145 ? 23.194 55.907 23.365  1.00 20.02 ? 123 MSE B CE  1 
ATOM   2952 N  N   . THR B 1 146 ? 22.316 56.301 28.568  1.00 8.44  ? 124 THR B N   1 
ATOM   2953 C  CA  . THR B 1 146 ? 23.261 56.861 29.526  1.00 8.19  ? 124 THR B CA  1 
ATOM   2954 C  C   . THR B 1 146 ? 24.680 56.692 29.009  1.00 8.25  ? 124 THR B C   1 
ATOM   2955 O  O   . THR B 1 146 ? 25.079 55.593 28.624  1.00 7.97  ? 124 THR B O   1 
ATOM   2956 C  CB  . THR B 1 146 ? 23.158 56.174 30.894  1.00 8.05  ? 124 THR B CB  1 
ATOM   2957 O  OG1 . THR B 1 146 ? 21.834 56.343 31.405  1.00 7.80  ? 124 THR B OG1 1 
ATOM   2958 C  CG2 . THR B 1 146 ? 24.157 56.772 31.884  1.00 7.98  ? 124 THR B CG2 1 
ATOM   2959 N  N   . ILE B 1 147 ? 25.426 57.795 28.996  1.00 8.37  ? 125 ILE B N   1 
ATOM   2960 C  CA  . ILE B 1 147 ? 26.848 57.792 28.667  1.00 8.86  ? 125 ILE B CA  1 
ATOM   2961 C  C   . ILE B 1 147 ? 27.596 58.165 29.939  1.00 8.61  ? 125 ILE B C   1 
ATOM   2962 O  O   . ILE B 1 147 ? 27.106 58.974 30.722  1.00 8.38  ? 125 ILE B O   1 
ATOM   2963 C  CB  . ILE B 1 147 ? 27.178 58.838 27.574  1.00 9.40  ? 125 ILE B CB  1 
ATOM   2964 C  CG1 . ILE B 1 147 ? 26.245 58.684 26.367  1.00 9.87  ? 125 ILE B CG1 1 
ATOM   2965 C  CG2 . ILE B 1 147 ? 28.634 58.729 27.144  1.00 9.85  ? 125 ILE B CG2 1 
ATOM   2966 C  CD1 . ILE B 1 147 ? 26.295 57.333 25.720  1.00 9.86  ? 125 ILE B CD1 1 
ATOM   2967 N  N   . ALA B 1 148 ? 28.770 57.583 30.147  1.00 8.57  ? 126 ALA B N   1 
ATOM   2968 C  CA  . ALA B 1 148 ? 29.535 57.843 31.369  1.00 8.68  ? 126 ALA B CA  1 
ATOM   2969 C  C   . ALA B 1 148 ? 31.016 57.983 31.080  1.00 9.06  ? 126 ALA B C   1 
ATOM   2970 O  O   . ALA B 1 148 ? 31.530 57.386 30.140  1.00 8.66  ? 126 ALA B O   1 
ATOM   2971 C  CB  . ALA B 1 148 ? 29.310 56.736 32.386  1.00 8.69  ? 126 ALA B CB  1 
ATOM   2972 N  N   . THR B 1 149 ? 31.693 58.771 31.905  1.00 9.55  ? 127 THR B N   1 
ATOM   2973 C  CA  . THR B 1 149 ? 33.146 58.849 31.867  1.00 10.16 ? 127 THR B CA  1 
ATOM   2974 C  C   . THR B 1 149 ? 33.738 57.663 32.625  1.00 10.81 ? 127 THR B C   1 
ATOM   2975 O  O   . THR B 1 149 ? 33.046 57.000 33.397  1.00 10.34 ? 127 THR B O   1 
ATOM   2976 C  CB  . THR B 1 149 ? 33.649 60.158 32.500  1.00 10.24 ? 127 THR B CB  1 
ATOM   2977 O  OG1 . THR B 1 149 ? 33.205 60.226 33.856  1.00 10.54 ? 127 THR B OG1 1 
ATOM   2978 C  CG2 . THR B 1 149 ? 33.118 61.364 31.731  1.00 10.39 ? 127 THR B CG2 1 
ATOM   2979 N  N   . GLU B 1 150 ? 35.028 57.409 32.411  1.00 12.05 ? 128 GLU B N   1 
ATOM   2980 C  CA  . GLU B 1 150 ? 35.725 56.311 33.082  1.00 13.45 ? 128 GLU B CA  1 
ATOM   2981 C  C   . GLU B 1 150 ? 35.678 56.442 34.607  1.00 13.34 ? 128 GLU B C   1 
ATOM   2982 O  O   . GLU B 1 150 ? 35.654 55.429 35.306  1.00 13.45 ? 128 GLU B O   1 
ATOM   2983 C  CB  . GLU B 1 150 ? 37.193 56.242 32.633  1.00 14.78 ? 128 GLU B CB  1 
ATOM   2984 C  CG  . GLU B 1 150 ? 37.407 55.974 31.148  1.00 16.28 ? 128 GLU B CG  1 
ATOM   2985 C  CD  . GLU B 1 150 ? 37.284 54.513 30.756  1.00 17.86 ? 128 GLU B CD  1 
ATOM   2986 O  OE1 . GLU B 1 150 ? 37.111 53.643 31.641  1.00 19.64 ? 128 GLU B OE1 1 
ATOM   2987 O  OE2 . GLU B 1 150 ? 37.369 54.231 29.538  1.00 20.39 ? 128 GLU B OE2 1 
ATOM   2988 N  N   . ASP B 1 151 ? 35.641 57.683 35.106  1.00 13.28 ? 129 ASP B N   1 
ATOM   2989 C  CA  . ASP B 1 151 ? 35.654 57.963 36.549  1.00 13.34 ? 129 ASP B CA  1 
ATOM   2990 C  C   . ASP B 1 151 ? 34.273 57.977 37.202  1.00 12.14 ? 129 ASP B C   1 
ATOM   2991 O  O   . ASP B 1 151 ? 34.163 58.147 38.415  1.00 12.17 ? 129 ASP B O   1 
ATOM   2992 C  CB  . ASP B 1 151 ? 36.429 59.273 36.853  1.00 14.57 ? 129 ASP B CB  1 
ATOM   2993 C  CG  . ASP B 1 151 ? 35.578 60.561 36.745  1.00 15.83 ? 129 ASP B CG  1 
ATOM   2994 O  OD1 . ASP B 1 151 ? 34.475 60.579 36.177  1.00 16.81 ? 129 ASP B OD1 1 
ATOM   2995 O  OD2 . ASP B 1 151 ? 36.056 61.608 37.241  1.00 18.57 ? 129 ASP B OD2 1 
ATOM   2996 N  N   . ALA B 1 152 ? 33.222 57.793 36.407  1.00 10.72 ? 130 ALA B N   1 
ATOM   2997 C  CA  . ALA B 1 152 ? 31.864 57.828 36.940  1.00 9.90  ? 130 ALA B CA  1 
ATOM   2998 C  C   . ALA B 1 152 ? 31.605 56.592 37.796  1.00 9.37  ? 130 ALA B C   1 
ATOM   2999 O  O   . ALA B 1 152 ? 32.154 55.522 37.542  1.00 9.00  ? 130 ALA B O   1 
ATOM   3000 C  CB  . ALA B 1 152 ? 30.843 57.912 35.816  1.00 9.77  ? 130 ALA B CB  1 
ATOM   3001 N  N   . PHE B 1 153 ? 30.775 56.754 38.816  1.00 8.97  ? 131 PHE B N   1 
ATOM   3002 C  CA  . PHE B 1 153 ? 30.374 55.626 39.640  1.00 8.99  ? 131 PHE B CA  1 
ATOM   3003 C  C   . PHE B 1 153 ? 28.912 55.757 40.031  1.00 8.55  ? 131 PHE B C   1 
ATOM   3004 O  O   . PHE B 1 153 ? 28.383 56.864 40.152  1.00 8.43  ? 131 PHE B O   1 
ATOM   3005 C  CB  . PHE B 1 153 ? 31.288 55.433 40.855  1.00 9.30  ? 131 PHE B CB  1 
ATOM   3006 C  CG  . PHE B 1 153 ? 31.414 56.635 41.750  1.00 9.57  ? 131 PHE B CG  1 
ATOM   3007 C  CD1 . PHE B 1 153 ? 32.322 57.646 41.456  1.00 9.79  ? 131 PHE B CD1 1 
ATOM   3008 C  CD2 . PHE B 1 153 ? 30.654 56.742 42.905  1.00 9.73  ? 131 PHE B CD2 1 
ATOM   3009 C  CE1 . PHE B 1 153 ? 32.448 58.749 42.287  1.00 9.85  ? 131 PHE B CE1 1 
ATOM   3010 C  CE2 . PHE B 1 153 ? 30.777 57.840 43.744  1.00 9.89  ? 131 PHE B CE2 1 
ATOM   3011 C  CZ  . PHE B 1 153 ? 31.676 58.848 43.431  1.00 9.94  ? 131 PHE B CZ  1 
ATOM   3012 N  N   . PHE B 1 154 ? 28.272 54.607 40.206  1.00 8.16  ? 132 PHE B N   1 
ATOM   3013 C  CA  . PHE B 1 154 ? 26.824 54.528 40.302  1.00 7.99  ? 132 PHE B CA  1 
ATOM   3014 C  C   . PHE B 1 154 ? 26.393 53.740 41.520  1.00 8.04  ? 132 PHE B C   1 
ATOM   3015 O  O   . PHE B 1 154 ? 27.187 53.035 42.135  1.00 7.86  ? 132 PHE B O   1 
ATOM   3016 C  CB  . PHE B 1 154 ? 26.267 53.823 39.070  1.00 7.90  ? 132 PHE B CB  1 
ATOM   3017 C  CG  . PHE B 1 154 ? 26.519 54.552 37.787  1.00 7.77  ? 132 PHE B CG  1 
ATOM   3018 C  CD1 . PHE B 1 154 ? 27.740 54.441 37.142  1.00 7.72  ? 132 PHE B CD1 1 
ATOM   3019 C  CD2 . PHE B 1 154 ? 25.529 55.341 37.220  1.00 7.81  ? 132 PHE B CD2 1 
ATOM   3020 C  CE1 . PHE B 1 154 ? 27.972 55.114 35.960  1.00 7.71  ? 132 PHE B CE1 1 
ATOM   3021 C  CE2 . PHE B 1 154 ? 25.752 56.012 36.035  1.00 7.78  ? 132 PHE B CE2 1 
ATOM   3022 C  CZ  . PHE B 1 154 ? 26.977 55.901 35.406  1.00 7.68  ? 132 PHE B CZ  1 
ATOM   3023 N  N   . GLY B 1 155 ? 25.112 53.845 41.842  1.00 8.15  ? 133 GLY B N   1 
ATOM   3024 C  CA  . GLY B 1 155 ? 24.519 52.980 42.838  1.00 8.42  ? 133 GLY B CA  1 
ATOM   3025 C  C   . GLY B 1 155 ? 23.373 53.585 43.604  1.00 8.77  ? 133 GLY B C   1 
ATOM   3026 O  O   . GLY B 1 155 ? 22.966 54.721 43.364  1.00 8.59  ? 133 GLY B O   1 
ATOM   3027 N  N   . GLU B 1 156 ? 22.872 52.795 44.546  1.00 9.43  ? 134 GLU B N   1 
ATOM   3028 C  CA  . GLU B 1 156 ? 21.661 53.088 45.293  1.00 10.02 ? 134 GLU B CA  1 
ATOM   3029 C  C   . GLU B 1 156 ? 21.953 52.863 46.777  1.00 9.64  ? 134 GLU B C   1 
ATOM   3030 O  O   . GLU B 1 156 ? 21.624 51.806 47.310  1.00 9.59  ? 134 GLU B O   1 
ATOM   3031 C  CB  . GLU B 1 156 ? 20.555 52.121 44.857  1.00 11.11 ? 134 GLU B CB  1 
ATOM   3032 C  CG  . GLU B 1 156 ? 20.063 52.309 43.439  1.00 12.07 ? 134 GLU B CG  1 
ATOM   3033 C  CD  . GLU B 1 156 ? 18.868 53.217 43.378  1.00 13.11 ? 134 GLU B CD  1 
ATOM   3034 O  OE1 . GLU B 1 156 ? 17.825 52.788 42.838  1.00 13.56 ? 134 GLU B OE1 1 
ATOM   3035 O  OE2 . GLU B 1 156 ? 18.969 54.343 43.905  1.00 14.65 ? 134 GLU B OE2 1 
ATOM   3036 N  N   . PRO B 1 157 ? 22.579 53.848 47.450  1.00 9.18  ? 135 PRO B N   1 
ATOM   3037 C  CA  . PRO B 1 157 ? 22.958 53.670 48.857  1.00 9.12  ? 135 PRO B CA  1 
ATOM   3038 C  C   . PRO B 1 157 ? 21.810 53.792 49.870  1.00 9.07  ? 135 PRO B C   1 
ATOM   3039 O  O   . PRO B 1 157 ? 22.052 53.653 51.066  1.00 9.03  ? 135 PRO B O   1 
ATOM   3040 C  CB  . PRO B 1 157 ? 23.965 54.803 49.092  1.00 9.05  ? 135 PRO B CB  1 
ATOM   3041 C  CG  . PRO B 1 157 ? 23.563 55.860 48.129  1.00 9.10  ? 135 PRO B CG  1 
ATOM   3042 C  CD  . PRO B 1 157 ? 23.078 55.125 46.906  1.00 9.11  ? 135 PRO B CD  1 
ATOM   3043 N  N   . GLU B 1 158 ? 20.588 54.028 49.392  1.00 9.10  ? 136 GLU B N   1 
ATOM   3044 C  CA  . GLU B 1 158 ? 19.437 54.352 50.247  1.00 9.18  ? 136 GLU B CA  1 
ATOM   3045 C  C   . GLU B 1 158 ? 19.335 53.503 51.516  1.00 9.10  ? 136 GLU B C   1 
ATOM   3046 O  O   . GLU B 1 158 ? 19.202 54.040 52.608  1.00 8.62  ? 136 GLU B O   1 
ATOM   3047 C  CB  . GLU B 1 158 ? 18.124 54.244 49.450  1.00 9.54  ? 136 GLU B CB  1 
ATOM   3048 C  CG  . GLU B 1 158 ? 17.854 55.377 48.465  1.00 9.97  ? 136 GLU B CG  1 
ATOM   3049 C  CD  . GLU B 1 158 ? 18.455 55.160 47.083  1.00 10.40 ? 136 GLU B CD  1 
ATOM   3050 O  OE1 . GLU B 1 158 ? 19.592 54.660 46.977  1.00 10.58 ? 136 GLU B OE1 1 
ATOM   3051 O  OE2 . GLU B 1 158 ? 17.788 55.506 46.085  1.00 11.29 ? 136 GLU B OE2 1 
ATOM   3052 N  N   . LEU B 1 159 ? 19.394 52.178 51.381  1.00 8.96  ? 137 LEU B N   1 
ATOM   3053 C  CA  . LEU B 1 159 ? 19.147 51.305 52.536  1.00 9.21  ? 137 LEU B CA  1 
ATOM   3054 C  C   . LEU B 1 159 ? 20.183 51.493 53.649  1.00 9.48  ? 137 LEU B C   1 
ATOM   3055 O  O   . LEU B 1 159 ? 19.863 51.314 54.821  1.00 9.78  ? 137 LEU B O   1 
ATOM   3056 C  CB  . LEU B 1 159 ? 19.021 49.824 52.127  1.00 9.06  ? 137 LEU B CB  1 
ATOM   3057 C  CG  . LEU B 1 159 ? 17.572 49.358 51.887  1.00 8.98  ? 137 LEU B CG  1 
ATOM   3058 C  CD1 . LEU B 1 159 ? 16.951 50.080 50.705  1.00 8.94  ? 137 LEU B CD1 1 
ATOM   3059 C  CD2 . LEU B 1 159 ? 17.479 47.846 51.697  1.00 8.96  ? 137 LEU B CD2 1 
ATOM   3060 N  N   . LYS B 1 160 ? 21.397 51.900 53.289  1.00 9.84  ? 138 LYS B N   1 
ATOM   3061 C  CA  . LYS B 1 160 ? 22.426 52.203 54.287  1.00 10.32 ? 138 LYS B CA  1 
ATOM   3062 C  C   . LYS B 1 160 ? 22.082 53.458 55.092  1.00 10.65 ? 138 LYS B C   1 
ATOM   3063 O  O   . LYS B 1 160 ? 22.480 53.557 56.254  1.00 10.96 ? 138 LYS B O   1 
ATOM   3064 C  CB  . LYS B 1 160 ? 23.803 52.335 53.631  1.00 10.32 ? 138 LYS B CB  1 
ATOM   3065 C  CG  . LYS B 1 160 ? 24.249 51.065 52.924  1.00 10.52 ? 138 LYS B CG  1 
ATOM   3066 C  CD  . LYS B 1 160 ? 25.716 51.076 52.524  1.00 10.59 ? 138 LYS B CD  1 
ATOM   3067 C  CE  . LYS B 1 160 ? 26.059 52.250 51.627  1.00 10.77 ? 138 LYS B CE  1 
ATOM   3068 N  NZ  . LYS B 1 160 ? 27.446 52.123 51.102  1.00 10.97 ? 138 LYS B NZ  1 
ATOM   3069 N  N   . PHE B 1 161 ? 21.357 54.399 54.473  1.00 11.09 ? 139 PHE B N   1 
ATOM   3070 C  CA  . PHE B 1 161 ? 20.844 55.607 55.147  1.00 11.48 ? 139 PHE B CA  1 
ATOM   3071 C  C   . PHE B 1 161 ? 19.549 55.342 55.925  1.00 10.88 ? 139 PHE B C   1 
ATOM   3072 O  O   . PHE B 1 161 ? 19.036 56.244 56.580  1.00 11.16 ? 139 PHE B O   1 
ATOM   3073 C  CB  . PHE B 1 161 ? 20.529 56.731 54.135  1.00 12.11 ? 139 PHE B CB  1 
ATOM   3074 C  CG  . PHE B 1 161 ? 21.729 57.368 53.492  1.00 12.85 ? 139 PHE B CG  1 
ATOM   3075 C  CD1 . PHE B 1 161 ? 22.566 58.212 54.220  1.00 13.21 ? 139 PHE B CD1 1 
ATOM   3076 C  CD2 . PHE B 1 161 ? 21.978 57.194 52.134  1.00 13.20 ? 139 PHE B CD2 1 
ATOM   3077 C  CE1 . PHE B 1 161 ? 23.658 58.824 53.617  1.00 13.53 ? 139 PHE B CE1 1 
ATOM   3078 C  CE2 . PHE B 1 161 ? 23.065 57.811 51.526  1.00 13.80 ? 139 PHE B CE2 1 
ATOM   3079 C  CZ  . PHE B 1 161 ? 23.904 58.629 52.269  1.00 13.63 ? 139 PHE B CZ  1 
ATOM   3080 N  N   . GLY B 1 162 ? 18.993 54.134 55.826  1.00 9.97  ? 140 GLY B N   1 
ATOM   3081 C  CA  . GLY B 1 162 ? 17.676 53.854 56.393  1.00 9.30  ? 140 GLY B CA  1 
ATOM   3082 C  C   . GLY B 1 162 ? 16.527 54.356 55.531  1.00 8.79  ? 140 GLY B C   1 
ATOM   3083 O  O   . GLY B 1 162 ? 15.392 54.436 55.998  1.00 8.74  ? 140 GLY B O   1 
ATOM   3084 N  N   . ALA B 1 163 ? 16.818 54.678 54.273  1.00 8.25  ? 141 ALA B N   1 
ATOM   3085 C  CA  . ALA B 1 163 ? 15.812 55.138 53.319  1.00 7.93  ? 141 ALA B CA  1 
ATOM   3086 C  C   . ALA B 1 163 ? 15.401 53.998 52.401  1.00 7.75  ? 141 ALA B C   1 
ATOM   3087 O  O   . ALA B 1 163 ? 16.189 53.097 52.124  1.00 7.79  ? 141 ALA B O   1 
ATOM   3088 C  CB  . ALA B 1 163 ? 16.355 56.297 52.492  1.00 7.96  ? 141 ALA B CB  1 
ATOM   3089 N  N   . GLY B 1 164 ? 14.162 54.051 51.927  1.00 7.44  ? 142 GLY B N   1 
ATOM   3090 C  CA  . GLY B 1 164 ? 13.696 53.120 50.909  1.00 7.25  ? 142 GLY B CA  1 
ATOM   3091 C  C   . GLY B 1 164 ? 13.952 53.667 49.516  1.00 7.11  ? 142 GLY B C   1 
ATOM   3092 O  O   . GLY B 1 164 ? 14.364 54.820 49.335  1.00 7.07  ? 142 GLY B O   1 
ATOM   3093 N  N   . ILE B 1 165 ? 13.698 52.824 48.523  1.00 6.89  ? 143 ILE B N   1 
ATOM   3094 C  CA  . ILE B 1 165 ? 13.874 53.181 47.118  1.00 6.79  ? 143 ILE B CA  1 
ATOM   3095 C  C   . ILE B 1 165 ? 12.623 53.887 46.607  1.00 6.78  ? 143 ILE B C   1 
ATOM   3096 O  O   . ILE B 1 165 ? 11.531 53.343 46.686  1.00 6.72  ? 143 ILE B O   1 
ATOM   3097 C  CB  . ILE B 1 165 ? 14.119 51.914 46.274  1.00 6.76  ? 143 ILE B CB  1 
ATOM   3098 C  CG1 . ILE B 1 165 ? 15.389 51.186 46.746  1.00 6.79  ? 143 ILE B CG1 1 
ATOM   3099 C  CG2 . ILE B 1 165 ? 14.172 52.244 44.789  1.00 6.74  ? 143 ILE B CG2 1 
ATOM   3100 C  CD1 . ILE B 1 165 ? 16.669 51.986 46.647  1.00 6.82  ? 143 ILE B CD1 1 
ATOM   3101 N  N   . VAL B 1 166 ? 12.788 55.096 46.081  1.00 6.83  ? 144 VAL B N   1 
ATOM   3102 C  CA  . VAL B 1 166 ? 11.658 55.878 45.576  1.00 6.92  ? 144 VAL B CA  1 
ATOM   3103 C  C   . VAL B 1 166 ? 11.199 55.389 44.197  1.00 7.10  ? 144 VAL B C   1 
ATOM   3104 O  O   . VAL B 1 166 ? 10.001 55.162 43.971  1.00 6.90  ? 144 VAL B O   1 
ATOM   3105 C  CB  . VAL B 1 166 ? 12.000 57.383 45.495  1.00 6.88  ? 144 VAL B CB  1 
ATOM   3106 C  CG1 . VAL B 1 166 ? 10.814 58.172 44.952  1.00 6.91  ? 144 VAL B CG1 1 
ATOM   3107 C  CG2 . VAL B 1 166 ? 12.410 57.915 46.862  1.00 6.92  ? 144 VAL B CG2 1 
ATOM   3108 N  N   . VAL B 1 167 ? 12.151 55.248 43.277  1.00 7.42  ? 145 VAL B N   1 
ATOM   3109 C  CA  . VAL B 1 167 ? 11.856 54.845 41.899  1.00 7.67  ? 145 VAL B CA  1 
ATOM   3110 C  C   . VAL B 1 167 ? 12.589 53.546 41.589  1.00 8.15  ? 145 VAL B C   1 
ATOM   3111 O  O   . VAL B 1 167 ? 13.793 53.555 41.300  1.00 8.05  ? 145 VAL B O   1 
ATOM   3112 C  CB  . VAL B 1 167 ? 12.257 55.932 40.875  1.00 7.61  ? 145 VAL B CB  1 
ATOM   3113 C  CG1 . VAL B 1 167 ? 11.705 55.595 39.497  1.00 7.64  ? 145 VAL B CG1 1 
ATOM   3114 C  CG2 . VAL B 1 167 ? 11.767 57.303 41.325  1.00 7.64  ? 145 VAL B CG2 1 
HETATM 3115 N  N   . MSE B 1 168 ? 11.868 52.427 41.632  1.00 8.83  ? 146 MSE B N   1 
HETATM 3116 C  CA  . MSE B 1 168 ? 12.499 51.101 41.508  1.00 9.95  ? 146 MSE B CA  1 
HETATM 3117 C  C   . MSE B 1 168 ? 12.616 50.694 40.061  1.00 8.98  ? 146 MSE B C   1 
HETATM 3118 O  O   . MSE B 1 168 ? 12.097 49.666 39.643  1.00 8.18  ? 146 MSE B O   1 
HETATM 3119 C  CB  . MSE B 1 168 ? 11.771 50.040 42.339  1.00 12.36 ? 146 MSE B CB  1 
HETATM 3120 C  CG  . MSE B 1 168 ? 12.702 48.846 42.587  1.00 15.22 ? 146 MSE B CG  1 
HETATM 3121 SE SE  . MSE B 1 168 ? 11.863 47.617 43.862  1.00 22.45 ? 146 MSE B SE  1 
HETATM 3122 C  CE  . MSE B 1 168 ? 12.733 48.409 45.444  1.00 19.27 ? 146 MSE B CE  1 
ATOM   3123 N  N   . LEU B 1 169 ? 13.334 51.500 39.286  1.00 8.35  ? 147 LEU B N   1 
ATOM   3124 C  CA  . LEU B 1 169 ? 13.611 51.173 37.886  1.00 8.04  ? 147 LEU B CA  1 
ATOM   3125 C  C   . LEU B 1 169 ? 14.670 50.088 37.718  1.00 7.88  ? 147 LEU B C   1 
ATOM   3126 O  O   . LEU B 1 169 ? 14.704 49.417 36.696  1.00 7.79  ? 147 LEU B O   1 
ATOM   3127 C  CB  . LEU B 1 169 ? 14.097 52.418 37.137  1.00 8.14  ? 147 LEU B CB  1 
ATOM   3128 C  CG  . LEU B 1 169 ? 13.003 53.363 36.665  1.00 8.18  ? 147 LEU B CG  1 
ATOM   3129 C  CD1 . LEU B 1 169 ? 13.601 54.736 36.402  1.00 8.36  ? 147 LEU B CD1 1 
ATOM   3130 C  CD2 . LEU B 1 169 ? 12.298 52.799 35.434  1.00 8.29  ? 147 LEU B CD2 1 
ATOM   3131 N  N   . LEU B 1 170 ? 15.552 49.935 38.701  1.00 7.65  ? 148 LEU B N   1 
ATOM   3132 C  CA  . LEU B 1 170 ? 16.739 49.099 38.513  1.00 7.55  ? 148 LEU B CA  1 
ATOM   3133 C  C   . LEU B 1 170 ? 16.458 47.683 37.982  1.00 7.59  ? 148 LEU B C   1 
ATOM   3134 O  O   . LEU B 1 170 ? 17.105 47.265 37.023  1.00 7.35  ? 148 LEU B O   1 
ATOM   3135 C  CB  . LEU B 1 170 ? 17.596 49.056 39.785  1.00 7.52  ? 148 LEU B CB  1 
ATOM   3136 C  CG  . LEU B 1 170 ? 18.988 48.451 39.614  1.00 7.55  ? 148 LEU B CG  1 
ATOM   3137 C  CD1 . LEU B 1 170 ? 19.788 49.183 38.549  1.00 7.57  ? 148 LEU B CD1 1 
ATOM   3138 C  CD2 . LEU B 1 170 ? 19.721 48.466 40.946  1.00 7.59  ? 148 LEU B CD2 1 
ATOM   3139 N  N   . PRO B 1 171 ? 15.482 46.950 38.569  1.00 7.72  ? 149 PRO B N   1 
ATOM   3140 C  CA  . PRO B 1 171 ? 15.209 45.602 38.045  1.00 7.97  ? 149 PRO B CA  1 
ATOM   3141 C  C   . PRO B 1 171 ? 14.612 45.562 36.631  1.00 8.32  ? 149 PRO B C   1 
ATOM   3142 O  O   . PRO B 1 171 ? 14.570 44.489 36.018  1.00 9.42  ? 149 PRO B O   1 
ATOM   3143 C  CB  . PRO B 1 171 ? 14.228 45.007 39.066  1.00 7.86  ? 149 PRO B CB  1 
ATOM   3144 C  CG  . PRO B 1 171 ? 13.632 46.173 39.767  1.00 7.88  ? 149 PRO B CG  1 
ATOM   3145 C  CD  . PRO B 1 171 ? 14.672 47.251 39.765  1.00 7.76  ? 149 PRO B CD  1 
ATOM   3146 N  N   . TRP B 1 172 ? 14.161 46.703 36.119  1.00 8.13  ? 150 TRP B N   1 
ATOM   3147 C  CA  . TRP B 1 172 ? 13.707 46.798 34.731  1.00 8.18  ? 150 TRP B CA  1 
ATOM   3148 C  C   . TRP B 1 172 ? 14.858 47.057 33.757  1.00 8.54  ? 150 TRP B C   1 
ATOM   3149 O  O   . TRP B 1 172 ? 14.729 46.778 32.565  1.00 9.09  ? 150 TRP B O   1 
ATOM   3150 C  CB  . TRP B 1 172 ? 12.625 47.873 34.600  1.00 7.87  ? 150 TRP B CB  1 
ATOM   3151 C  CG  . TRP B 1 172 ? 11.438 47.522 35.420  1.00 7.60  ? 150 TRP B CG  1 
ATOM   3152 C  CD1 . TRP B 1 172 ? 11.175 47.918 36.694  1.00 7.43  ? 150 TRP B CD1 1 
ATOM   3153 C  CD2 . TRP B 1 172 ? 10.377 46.638 35.044  1.00 7.36  ? 150 TRP B CD2 1 
ATOM   3154 N  NE1 . TRP B 1 172 ? 10.000 47.347 37.137  1.00 7.39  ? 150 TRP B NE1 1 
ATOM   3155 C  CE2 . TRP B 1 172 ? 9.493  46.557 36.139  1.00 7.36  ? 150 TRP B CE2 1 
ATOM   3156 C  CE3 . TRP B 1 172 ? 10.081 45.917 33.880  1.00 7.38  ? 150 TRP B CE3 1 
ATOM   3157 C  CZ2 . TRP B 1 172 ? 8.326  45.786 36.105  1.00 7.32  ? 150 TRP B CZ2 1 
ATOM   3158 C  CZ3 . TRP B 1 172 ? 8.924  45.156 33.850  1.00 7.28  ? 150 TRP B CZ3 1 
ATOM   3159 C  CH2 . TRP B 1 172 ? 8.065  45.096 34.955  1.00 7.28  ? 150 TRP B CH2 1 
ATOM   3160 N  N   . ILE B 1 173 ? 15.977 47.563 34.267  1.00 8.81  ? 151 ILE B N   1 
ATOM   3161 C  CA  . ILE B 1 173 ? 17.112 47.965 33.430  1.00 9.09  ? 151 ILE B CA  1 
ATOM   3162 C  C   . ILE B 1 173 ? 18.208 46.899 33.410  1.00 9.40  ? 151 ILE B C   1 
ATOM   3163 O  O   . ILE B 1 173 ? 18.802 46.647 32.359  1.00 9.89  ? 151 ILE B O   1 
ATOM   3164 C  CB  . ILE B 1 173 ? 17.701 49.320 33.905  1.00 9.05  ? 151 ILE B CB  1 
ATOM   3165 C  CG1 . ILE B 1 173 ? 16.621 50.420 33.932  1.00 9.11  ? 151 ILE B CG1 1 
ATOM   3166 C  CG2 . ILE B 1 173 ? 18.897 49.735 33.049  1.00 9.06  ? 151 ILE B CG2 1 
ATOM   3167 C  CD1 . ILE B 1 173 ? 15.880 50.648 32.630  1.00 9.25  ? 151 ILE B CD1 1 
ATOM   3168 N  N   . VAL B 1 174 ? 18.483 46.293 34.565  1.00 9.65  ? 152 VAL B N   1 
ATOM   3169 C  CA  . VAL B 1 174 ? 19.507 45.257 34.709  1.00 9.90  ? 152 VAL B CA  1 
ATOM   3170 C  C   . VAL B 1 174 ? 18.823 43.976 35.196  1.00 10.29 ? 152 VAL B C   1 
ATOM   3171 O  O   . VAL B 1 174 ? 17.646 43.996 35.551  1.00 10.65 ? 152 VAL B O   1 
ATOM   3172 C  CB  . VAL B 1 174 ? 20.633 45.694 35.681  1.00 9.68  ? 152 VAL B CB  1 
ATOM   3173 C  CG1 . VAL B 1 174 ? 21.160 47.075 35.305  1.00 9.70  ? 152 VAL B CG1 1 
ATOM   3174 C  CG2 . VAL B 1 174 ? 20.162 45.685 37.134  1.00 9.65  ? 152 VAL B CG2 1 
ATOM   3175 N  N   . GLY B 1 175 ? 19.534 42.860 35.234  1.00 10.82 ? 153 GLY B N   1 
ATOM   3176 C  CA  . GLY B 1 175 ? 18.881 41.612 35.662  1.00 10.92 ? 153 GLY B CA  1 
ATOM   3177 C  C   . GLY B 1 175 ? 18.423 41.651 37.123  1.00 11.02 ? 153 GLY B C   1 
ATOM   3178 O  O   . GLY B 1 175 ? 18.862 42.513 37.889  1.00 11.85 ? 153 GLY B O   1 
ATOM   3179 N  N   . PRO B 1 176 ? 17.537 40.717 37.530  1.00 10.49 ? 154 PRO B N   1 
ATOM   3180 C  CA  . PRO B 1 176 ? 17.041 40.674 38.914  1.00 9.91  ? 154 PRO B CA  1 
ATOM   3181 C  C   . PRO B 1 176 ? 18.126 40.450 39.974  1.00 9.35  ? 154 PRO B C   1 
ATOM   3182 O  O   . PRO B 1 176 ? 18.092 41.088 41.018  1.00 9.00  ? 154 PRO B O   1 
ATOM   3183 C  CB  . PRO B 1 176 ? 16.043 39.502 38.908  1.00 10.22 ? 154 PRO B CB  1 
ATOM   3184 C  CG  . PRO B 1 176 ? 16.377 38.712 37.701  1.00 10.29 ? 154 PRO B CG  1 
ATOM   3185 C  CD  . PRO B 1 176 ? 16.892 39.692 36.693  1.00 10.48 ? 154 PRO B CD  1 
ATOM   3186 N  N   . LYS B 1 177 ? 19.073 39.553 39.719  1.00 8.73  ? 155 LYS B N   1 
ATOM   3187 C  CA  . LYS B 1 177 ? 20.127 39.284 40.699  1.00 8.59  ? 155 LYS B CA  1 
ATOM   3188 C  C   . LYS B 1 177 ? 20.981 40.516 40.937  1.00 8.21  ? 155 LYS B C   1 
ATOM   3189 O  O   . LYS B 1 177 ? 21.338 40.827 42.074  1.00 7.81  ? 155 LYS B O   1 
ATOM   3190 C  CB  . LYS B 1 177 ? 21.018 38.146 40.224  1.00 8.84  ? 155 LYS B CB  1 
ATOM   3191 C  CG  . LYS B 1 177 ? 20.292 36.819 40.138  1.00 9.24  ? 155 LYS B CG  1 
ATOM   3192 C  CD  . LYS B 1 177 ? 21.128 35.699 40.715  1.00 9.20  ? 155 LYS B CD  1 
ATOM   3193 C  CE  . LYS B 1 177 ? 20.370 34.386 40.755  1.00 9.12  ? 155 LYS B CE  1 
ATOM   3194 N  NZ  . LYS B 1 177 ? 20.473 33.786 42.112  1.00 9.04  ? 155 LYS B NZ  1 
ATOM   3195 N  N   . ILE B 1 178 ? 21.307 41.208 39.852  1.00 8.07  ? 156 ILE B N   1 
ATOM   3196 C  CA  . ILE B 1 178 ? 22.157 42.390 39.927  1.00 8.08  ? 156 ILE B CA  1 
ATOM   3197 C  C   . ILE B 1 178 ? 21.423 43.538 40.620  1.00 7.69  ? 156 ILE B C   1 
ATOM   3198 O  O   . ILE B 1 178 ? 22.009 44.237 41.444  1.00 7.29  ? 156 ILE B O   1 
ATOM   3199 C  CB  . ILE B 1 178 ? 22.668 42.808 38.526  1.00 8.56  ? 156 ILE B CB  1 
ATOM   3200 C  CG1 . ILE B 1 178 ? 23.475 41.671 37.869  1.00 8.99  ? 156 ILE B CG1 1 
ATOM   3201 C  CG2 . ILE B 1 178 ? 23.512 44.062 38.613  1.00 8.67  ? 156 ILE B CG2 1 
ATOM   3202 C  CD1 . ILE B 1 178 ? 24.615 41.140 38.690  1.00 9.25  ? 156 ILE B CD1 1 
ATOM   3203 N  N   . ALA B 1 179 ? 20.143 43.725 40.298  1.00 7.49  ? 157 ALA B N   1 
ATOM   3204 C  CA  . ALA B 1 179 ? 19.338 44.748 40.963  1.00 7.51  ? 157 ALA B CA  1 
ATOM   3205 C  C   . ALA B 1 179 ? 19.232 44.500 42.464  1.00 7.53  ? 157 ALA B C   1 
ATOM   3206 O  O   . ALA B 1 179 ? 19.327 45.435 43.263  1.00 7.54  ? 157 ALA B O   1 
ATOM   3207 C  CB  . ALA B 1 179 ? 17.946 44.825 40.344  1.00 7.43  ? 157 ALA B CB  1 
ATOM   3208 N  N   . LYS B 1 180 ? 19.032 43.245 42.857  1.00 7.60  ? 158 LYS B N   1 
ATOM   3209 C  CA  . LYS B 1 180 ? 18.921 42.918 44.286  1.00 7.89  ? 158 LYS B CA  1 
ATOM   3210 C  C   . LYS B 1 180 ? 20.208 43.192 45.050  1.00 7.78  ? 158 LYS B C   1 
ATOM   3211 O  O   . LYS B 1 180 ? 20.177 43.730 46.158  1.00 7.85  ? 158 LYS B O   1 
ATOM   3212 C  CB  . LYS B 1 180 ? 18.482 41.473 44.476  1.00 8.12  ? 158 LYS B CB  1 
ATOM   3213 C  CG  . LYS B 1 180 ? 17.033 41.252 44.070  1.00 8.53  ? 158 LYS B CG  1 
ATOM   3214 C  CD  . LYS B 1 180 ? 16.594 39.848 44.387  1.00 8.83  ? 158 LYS B CD  1 
ATOM   3215 C  CE  . LYS B 1 180 ? 15.118 39.640 44.123  1.00 9.00  ? 158 LYS B CE  1 
ATOM   3216 N  NZ  . LYS B 1 180 ? 14.740 38.233 44.396  1.00 9.17  ? 158 LYS B NZ  1 
ATOM   3217 N  N   . GLU B 1 181 ? 21.339 42.841 44.450  1.00 7.68  ? 159 GLU B N   1 
ATOM   3218 C  CA  . GLU B 1 181 ? 22.635 43.110 45.058  1.00 7.68  ? 159 GLU B CA  1 
ATOM   3219 C  C   . GLU B 1 181 ? 22.846 44.608 45.269  1.00 7.42  ? 159 GLU B C   1 
ATOM   3220 O  O   . GLU B 1 181 ? 23.191 45.042 46.365  1.00 7.40  ? 159 GLU B O   1 
ATOM   3221 C  CB  . GLU B 1 181 ? 23.756 42.548 44.189  1.00 8.01  ? 159 GLU B CB  1 
ATOM   3222 C  CG  . GLU B 1 181 ? 25.154 42.919 44.669  1.00 8.30  ? 159 GLU B CG  1 
ATOM   3223 C  CD  . GLU B 1 181 ? 26.247 42.435 43.734  1.00 8.65  ? 159 GLU B CD  1 
ATOM   3224 O  OE1 . GLU B 1 181 ? 25.928 41.884 42.661  1.00 8.67  ? 159 GLU B OE1 1 
ATOM   3225 O  OE2 . GLU B 1 181 ? 27.440 42.633 44.061  1.00 9.44  ? 159 GLU B OE2 1 
ATOM   3226 N  N   . ILE B 1 182 ? 22.625 45.401 44.227  1.00 7.17  ? 160 ILE B N   1 
ATOM   3227 C  CA  . ILE B 1 182 ? 22.867 46.842 44.328  1.00 7.03  ? 160 ILE B CA  1 
ATOM   3228 C  C   . ILE B 1 182 ? 21.971 47.480 45.389  1.00 7.08  ? 160 ILE B C   1 
ATOM   3229 O  O   . ILE B 1 182 ? 22.445 48.253 46.222  1.00 7.08  ? 160 ILE B O   1 
ATOM   3230 C  CB  . ILE B 1 182 ? 22.722 47.545 42.955  1.00 6.94  ? 160 ILE B CB  1 
ATOM   3231 C  CG1 . ILE B 1 182 ? 23.884 47.135 42.043  1.00 6.94  ? 160 ILE B CG1 1 
ATOM   3232 C  CG2 . ILE B 1 182 ? 22.676 49.065 43.112  1.00 6.90  ? 160 ILE B CG2 1 
ATOM   3233 C  CD1 . ILE B 1 182 ? 23.722 47.554 40.598  1.00 6.94  ? 160 ILE B CD1 1 
ATOM   3234 N  N   . ILE B 1 183 ? 20.685 47.140 45.381  1.00 7.16  ? 161 ILE B N   1 
ATOM   3235 C  CA  . ILE B 1 183 ? 19.730 47.792 46.278  1.00 7.38  ? 161 ILE B CA  1 
ATOM   3236 C  C   . ILE B 1 183 ? 19.790 47.263 47.711  1.00 7.65  ? 161 ILE B C   1 
ATOM   3237 O  O   . ILE B 1 183 ? 19.817 48.059 48.661  1.00 7.68  ? 161 ILE B O   1 
ATOM   3238 C  CB  . ILE B 1 183 ? 18.308 47.728 45.697  1.00 7.43  ? 161 ILE B CB  1 
ATOM   3239 C  CG1 . ILE B 1 183 ? 18.189 48.776 44.588  1.00 7.49  ? 161 ILE B CG1 1 
ATOM   3240 C  CG2 . ILE B 1 183 ? 17.252 47.975 46.770  1.00 7.47  ? 161 ILE B CG2 1 
ATOM   3241 C  CD1 . ILE B 1 183 ? 17.000 48.573 43.684  1.00 7.54  ? 161 ILE B CD1 1 
ATOM   3242 N  N   . LEU B 1 184 ? 19.834 45.943 47.883  1.00 7.91  ? 162 LEU B N   1 
ATOM   3243 C  CA  . LEU B 1 184 ? 19.831 45.369 49.237  1.00 8.32  ? 162 LEU B CA  1 
ATOM   3244 C  C   . LEU B 1 184 ? 21.130 45.634 49.992  1.00 8.77  ? 162 LEU B C   1 
ATOM   3245 O  O   . LEU B 1 184 ? 21.129 45.714 51.219  1.00 9.18  ? 162 LEU B O   1 
ATOM   3246 C  CB  . LEU B 1 184 ? 19.527 43.869 49.214  1.00 8.34  ? 162 LEU B CB  1 
ATOM   3247 C  CG  . LEU B 1 184 ? 18.132 43.462 48.739  1.00 8.38  ? 162 LEU B CG  1 
ATOM   3248 C  CD1 . LEU B 1 184 ? 18.041 41.948 48.604  1.00 8.34  ? 162 LEU B CD1 1 
ATOM   3249 C  CD2 . LEU B 1 184 ? 17.041 43.985 49.661  1.00 8.39  ? 162 LEU B CD2 1 
ATOM   3250 N  N   . LEU B 1 185 ? 22.235 45.780 49.270  1.00 9.01  ? 163 LEU B N   1 
ATOM   3251 C  CA  . LEU B 1 185 ? 23.514 46.096 49.908  1.00 9.47  ? 163 LEU B CA  1 
ATOM   3252 C  C   . LEU B 1 185 ? 23.826 47.591 49.891  1.00 9.76  ? 163 LEU B C   1 
ATOM   3253 O  O   . LEU B 1 185 ? 24.757 48.036 50.565  1.00 10.31 ? 163 LEU B O   1 
ATOM   3254 C  CB  . LEU B 1 185 ? 24.649 45.325 49.238  1.00 9.51  ? 163 LEU B CB  1 
ATOM   3255 C  CG  . LEU B 1 185 ? 24.490 43.805 49.171  1.00 9.61  ? 163 LEU B CG  1 
ATOM   3256 C  CD1 . LEU B 1 185 ? 25.707 43.182 48.517  1.00 9.69  ? 163 LEU B CD1 1 
ATOM   3257 C  CD2 . LEU B 1 185 ? 24.264 43.207 50.554  1.00 9.83  ? 163 LEU B CD2 1 
ATOM   3258 N  N   . GLY B 1 186 ? 23.061 48.370 49.134  1.00 9.95  ? 164 GLY B N   1 
ATOM   3259 C  CA  . GLY B 1 186 ? 23.329 49.799 49.019  1.00 10.16 ? 164 GLY B CA  1 
ATOM   3260 C  C   . GLY B 1 186 ? 24.644 50.100 48.318  1.00 10.49 ? 164 GLY B C   1 
ATOM   3261 O  O   . GLY B 1 186 ? 25.377 51.006 48.723  1.00 10.48 ? 164 GLY B O   1 
ATOM   3262 N  N   . GLU B 1 187 ? 24.948 49.346 47.265  1.00 10.76 ? 165 GLU B N   1 
ATOM   3263 C  CA  . GLU B 1 187 ? 26.183 49.548 46.509  1.00 11.33 ? 165 GLU B CA  1 
ATOM   3264 C  C   . GLU B 1 187 ? 26.184 50.947 45.934  1.00 11.05 ? 165 GLU B C   1 
ATOM   3265 O  O   . GLU B 1 187 ? 25.217 51.348 45.294  1.00 10.72 ? 165 GLU B O   1 
ATOM   3266 C  CB  . GLU B 1 187 ? 26.301 48.538 45.369  1.00 12.36 ? 165 GLU B CB  1 
ATOM   3267 C  CG  . GLU B 1 187 ? 26.469 47.099 45.824  1.00 13.41 ? 165 GLU B CG  1 
ATOM   3268 C  CD  . GLU B 1 187 ? 27.785 46.857 46.527  1.00 14.98 ? 165 GLU B CD  1 
ATOM   3269 O  OE1 . GLU B 1 187 ? 28.831 47.329 46.038  1.00 17.91 ? 165 GLU B OE1 1 
ATOM   3270 O  OE2 . GLU B 1 187 ? 27.781 46.188 47.571  1.00 16.90 ? 165 GLU B OE2 1 
ATOM   3271 N  N   . ASP B 1 188 ? 27.267 51.683 46.170  1.00 10.74 ? 166 ASP B N   1 
ATOM   3272 C  CA  . ASP B 1 188 ? 27.359 53.086 45.766  1.00 10.75 ? 166 ASP B CA  1 
ATOM   3273 C  C   . ASP B 1 188 ? 28.709 53.456 45.146  1.00 10.75 ? 166 ASP B C   1 
ATOM   3274 O  O   . ASP B 1 188 ? 29.065 54.633 45.098  1.00 10.67 ? 166 ASP B O   1 
ATOM   3275 C  CB  . ASP B 1 188 ? 27.056 53.989 46.972  1.00 10.92 ? 166 ASP B CB  1 
ATOM   3276 C  CG  . ASP B 1 188 ? 27.975 53.726 48.162  1.00 11.05 ? 166 ASP B CG  1 
ATOM   3277 O  OD1 . ASP B 1 188 ? 28.933 52.943 48.033  1.00 11.23 ? 166 ASP B OD1 1 
ATOM   3278 O  OD2 . ASP B 1 188 ? 27.726 54.297 49.251  1.00 11.59 ? 166 ASP B OD2 1 
ATOM   3279 N  N   . ARG B 1 189 ? 29.447 52.455 44.669  1.00 10.85 ? 167 ARG B N   1 
ATOM   3280 C  CA  . ARG B 1 189 ? 30.734 52.671 44.001  1.00 11.05 ? 167 ARG B CA  1 
ATOM   3281 C  C   . ARG B 1 189 ? 30.862 51.781 42.770  1.00 10.55 ? 167 ARG B C   1 
ATOM   3282 O  O   . ARG B 1 189 ? 31.960 51.329 42.427  1.00 10.73 ? 167 ARG B O   1 
ATOM   3283 C  CB  . ARG B 1 189 ? 31.897 52.403 44.966  1.00 11.95 ? 167 ARG B CB  1 
ATOM   3284 C  CG  . ARG B 1 189 ? 31.957 53.345 46.158  1.00 13.04 ? 167 ARG B CG  1 
ATOM   3285 C  CD  . ARG B 1 189 ? 32.338 54.756 45.752  1.00 14.15 ? 167 ARG B CD  1 
ATOM   3286 N  NE  . ARG B 1 189 ? 32.486 55.640 46.910  1.00 15.66 ? 167 ARG B NE  1 
ATOM   3287 C  CZ  . ARG B 1 189 ? 31.511 56.363 47.464  1.00 16.46 ? 167 ARG B CZ  1 
ATOM   3288 N  NH1 . ARG B 1 189 ? 30.264 56.337 46.992  1.00 16.63 ? 167 ARG B NH1 1 
ATOM   3289 N  NH2 . ARG B 1 189 ? 31.790 57.126 48.515  1.00 17.67 ? 167 ARG B NH2 1 
ATOM   3290 N  N   . VAL B 1 190 ? 29.745 51.554 42.084  1.00 9.76  ? 168 VAL B N   1 
ATOM   3291 C  CA  . VAL B 1 190 ? 29.747 50.694 40.909  1.00 9.30  ? 168 VAL B CA  1 
ATOM   3292 C  C   . VAL B 1 190 ? 30.441 51.457 39.784  1.00 9.05  ? 168 VAL B C   1 
ATOM   3293 O  O   . VAL B 1 190 ? 29.948 52.496 39.353  1.00 8.69  ? 168 VAL B O   1 
ATOM   3294 C  CB  . VAL B 1 190 ? 28.321 50.309 40.474  1.00 9.18  ? 168 VAL B CB  1 
ATOM   3295 C  CG1 . VAL B 1 190 ? 28.366 49.431 39.231  1.00 9.14  ? 168 VAL B CG1 1 
ATOM   3296 C  CG2 . VAL B 1 190 ? 27.597 49.598 41.614  1.00 9.23  ? 168 VAL B CG2 1 
ATOM   3297 N  N   . PRO B 1 191 ? 31.597 50.962 39.317  1.00 9.04  ? 169 PRO B N   1 
ATOM   3298 C  CA  . PRO B 1 191 ? 32.308 51.735 38.292  1.00 9.14  ? 169 PRO B CA  1 
ATOM   3299 C  C   . PRO B 1 191 ? 31.595 51.757 36.944  1.00 9.14  ? 169 PRO B C   1 
ATOM   3300 O  O   . PRO B 1 191 ? 30.833 50.850 36.641  1.00 8.92  ? 169 PRO B O   1 
ATOM   3301 C  CB  . PRO B 1 191 ? 33.657 51.014 38.158  1.00 9.21  ? 169 PRO B CB  1 
ATOM   3302 C  CG  . PRO B 1 191 ? 33.709 50.003 39.239  1.00 9.39  ? 169 PRO B CG  1 
ATOM   3303 C  CD  . PRO B 1 191 ? 32.306 49.721 39.669  1.00 9.19  ? 169 PRO B CD  1 
ATOM   3304 N  N   . ALA B 1 192 ? 31.866 52.785 36.142  1.00 9.26  ? 170 ALA B N   1 
ATOM   3305 C  CA  . ALA B 1 192 ? 31.261 52.935 34.816  1.00 9.56  ? 170 ALA B CA  1 
ATOM   3306 C  C   . ALA B 1 192 ? 31.397 51.675 33.954  1.00 9.80  ? 170 ALA B C   1 
ATOM   3307 O  O   . ALA B 1 192 ? 30.447 51.265 33.296  1.00 9.56  ? 170 ALA B O   1 
ATOM   3308 C  CB  . ALA B 1 192 ? 31.878 54.126 34.099  1.00 9.55  ? 170 ALA B CB  1 
ATOM   3309 N  N   . ARG B 1 193 ? 32.582 51.072 33.965  1.00 10.31 ? 171 ARG B N   1 
ATOM   3310 C  CA  . ARG B 1 193 ? 32.848 49.847 33.211  1.00 10.92 ? 171 ARG B CA  1 
ATOM   3311 C  C   . ARG B 1 193 ? 31.869 48.731 33.594  1.00 9.89  ? 171 ARG B C   1 
ATOM   3312 O  O   . ARG B 1 193 ? 31.343 48.032 32.727  1.00 9.45  ? 171 ARG B O   1 
ATOM   3313 C  CB  . ARG B 1 193 ? 34.288 49.407 33.476  1.00 12.73 ? 171 ARG B CB  1 
ATOM   3314 C  CG  . ARG B 1 193 ? 34.750 48.150 32.756  1.00 14.65 ? 171 ARG B CG  1 
ATOM   3315 C  CD  . ARG B 1 193 ? 35.735 47.350 33.603  1.00 16.42 ? 171 ARG B CD  1 
ATOM   3316 N  NE  . ARG B 1 193 ? 35.061 46.290 34.362  1.00 18.26 ? 171 ARG B NE  1 
ATOM   3317 C  CZ  . ARG B 1 193 ? 34.573 46.395 35.602  1.00 19.36 ? 171 ARG B CZ  1 
ATOM   3318 N  NH1 . ARG B 1 193 ? 34.661 47.525 36.312  1.00 19.92 ? 171 ARG B NH1 1 
ATOM   3319 N  NH2 . ARG B 1 193 ? 33.987 45.340 36.147  1.00 20.78 ? 171 ARG B NH2 1 
ATOM   3320 N  N   . ARG B 1 194 ? 31.639 48.569 34.894  1.00 8.97  ? 172 ARG B N   1 
ATOM   3321 C  CA  . ARG B 1 194 ? 30.716 47.545 35.391  1.00 8.50  ? 172 ARG B CA  1 
ATOM   3322 C  C   . ARG B 1 194 ? 29.280 47.909 35.039  1.00 8.10  ? 172 ARG B C   1 
ATOM   3323 O  O   . ARG B 1 194 ? 28.488 47.051 34.657  1.00 8.02  ? 172 ARG B O   1 
ATOM   3324 C  CB  . ARG B 1 194 ? 30.857 47.375 36.903  1.00 8.44  ? 172 ARG B CB  1 
ATOM   3325 C  CG  . ARG B 1 194 ? 29.907 46.364 37.529  1.00 8.43  ? 172 ARG B CG  1 
ATOM   3326 C  CD  . ARG B 1 194 ? 30.014 44.989 36.899  1.00 8.44  ? 172 ARG B CD  1 
ATOM   3327 N  NE  . ARG B 1 194 ? 29.105 44.039 37.537  1.00 8.49  ? 172 ARG B NE  1 
ATOM   3328 C  CZ  . ARG B 1 194 ? 28.684 42.902 36.984  1.00 8.53  ? 172 ARG B CZ  1 
ATOM   3329 N  NH1 . ARG B 1 194 ? 29.087 42.543 35.772  1.00 8.62  ? 172 ARG B NH1 1 
ATOM   3330 N  NH2 . ARG B 1 194 ? 27.846 42.120 37.645  1.00 8.72  ? 172 ARG B NH2 1 
ATOM   3331 N  N   . ALA B 1 195 ? 28.949 49.190 35.168  1.00 7.80  ? 173 ALA B N   1 
ATOM   3332 C  CA  . ALA B 1 195 ? 27.619 49.669 34.820  1.00 7.72  ? 173 ALA B CA  1 
ATOM   3333 C  C   . ALA B 1 195 ? 27.305 49.380 33.347  1.00 7.88  ? 173 ALA B C   1 
ATOM   3334 O  O   . ALA B 1 195 ? 26.168 49.073 32.998  1.00 7.82  ? 173 ALA B O   1 
ATOM   3335 C  CB  . ALA B 1 195 ? 27.494 51.155 35.113  1.00 7.69  ? 173 ALA B CB  1 
ATOM   3336 N  N   . ALA B 1 196 ? 28.319 49.486 32.491  1.00 8.00  ? 174 ALA B N   1 
ATOM   3337 C  CA  . ALA B 1 196 ? 28.164 49.158 31.080  1.00 8.18  ? 174 ALA B CA  1 
ATOM   3338 C  C   . ALA B 1 196 ? 27.959 47.658 30.869  1.00 8.48  ? 174 ALA B C   1 
ATOM   3339 O  O   . ALA B 1 196 ? 27.163 47.253 30.026  1.00 8.48  ? 174 ALA B O   1 
ATOM   3340 C  CB  . ALA B 1 196 ? 29.360 49.655 30.279  1.00 8.24  ? 174 ALA B CB  1 
ATOM   3341 N  N   . GLU B 1 197 ? 28.678 46.832 31.627  1.00 8.82  ? 175 GLU B N   1 
ATOM   3342 C  CA  . GLU B 1 197 ? 28.510 45.378 31.538  1.00 9.30  ? 175 GLU B CA  1 
ATOM   3343 C  C   . GLU B 1 197 ? 27.086 44.921 31.844  1.00 9.06  ? 175 GLU B C   1 
ATOM   3344 O  O   . GLU B 1 197 ? 26.595 43.965 31.238  1.00 9.17  ? 175 GLU B O   1 
ATOM   3345 C  CB  . GLU B 1 197 ? 29.461 44.662 32.497  1.00 9.96  ? 175 GLU B CB  1 
ATOM   3346 C  CG  . GLU B 1 197 ? 30.920 44.727 32.088  1.00 10.83 ? 175 GLU B CG  1 
ATOM   3347 C  CD  . GLU B 1 197 ? 31.874 44.223 33.158  1.00 11.70 ? 175 GLU B CD  1 
ATOM   3348 O  OE1 . GLU B 1 197 ? 31.429 43.637 34.176  1.00 12.27 ? 175 GLU B OE1 1 
ATOM   3349 O  OE2 . GLU B 1 197 ? 33.097 44.403 32.974  1.00 13.05 ? 175 GLU B OE2 1 
ATOM   3350 N  N   . ILE B 1 198 ? 26.440 45.585 32.797  1.00 8.88  ? 176 ILE B N   1 
ATOM   3351 C  CA  . ILE B 1 198 ? 25.126 45.151 33.267  1.00 8.81  ? 176 ILE B CA  1 
ATOM   3352 C  C   . ILE B 1 198 ? 23.978 45.852 32.549  1.00 9.07  ? 176 ILE B C   1 
ATOM   3353 O  O   . ILE B 1 198 ? 22.823 45.523 32.790  1.00 9.23  ? 176 ILE B O   1 
ATOM   3354 C  CB  . ILE B 1 198 ? 24.989 45.290 34.803  1.00 8.67  ? 176 ILE B CB  1 
ATOM   3355 C  CG1 . ILE B 1 198 ? 25.001 46.765 35.233  1.00 8.57  ? 176 ILE B CG1 1 
ATOM   3356 C  CG2 . ILE B 1 198 ? 26.096 44.503 35.491  1.00 8.67  ? 176 ILE B CG2 1 
ATOM   3357 C  CD1 . ILE B 1 198 ? 24.980 46.988 36.734  1.00 8.70  ? 176 ILE B CD1 1 
ATOM   3358 N  N   . GLY B 1 199 ? 24.296 46.790 31.655  1.00 9.35  ? 177 GLY B N   1 
ATOM   3359 C  CA  . GLY B 1 199 ? 23.284 47.457 30.830  1.00 9.74  ? 177 GLY B CA  1 
ATOM   3360 C  C   . GLY B 1 199 ? 22.710 48.745 31.396  1.00 10.24 ? 177 GLY B C   1 
ATOM   3361 O  O   . GLY B 1 199 ? 21.733 49.269 30.861  1.00 9.62  ? 177 GLY B O   1 
HETATM 3362 N  N   . MSE B 1 200 ? 23.320 49.258 32.465  1.00 11.06 ? 178 MSE B N   1 
HETATM 3363 C  CA  . MSE B 1 200 ? 22.933 50.539 33.072  1.00 12.19 ? 178 MSE B CA  1 
HETATM 3364 C  C   . MSE B 1 200 ? 23.495 51.691 32.274  1.00 11.02 ? 178 MSE B C   1 
HETATM 3365 O  O   . MSE B 1 200 ? 22.910 52.773 32.247  1.00 10.77 ? 178 MSE B O   1 
HETATM 3366 C  CB  . MSE B 1 200 ? 23.438 50.580 34.521  1.00 15.15 ? 178 MSE B CB  1 
HETATM 3367 C  CG  . MSE B 1 200 ? 23.211 51.930 35.207  1.00 18.16 ? 178 MSE B CG  1 
HETATM 3368 SE SE  . MSE B 1 200 ? 23.892 51.927 37.060  1.00 27.24 ? 178 MSE B SE  1 
HETATM 3369 C  CE  . MSE B 1 200 ? 23.375 50.106 37.563  1.00 23.46 ? 178 MSE B CE  1 
ATOM   3370 N  N   . VAL B 1 201 ? 24.639 51.466 31.631  1.00 9.65  ? 179 VAL B N   1 
ATOM   3371 C  CA  . VAL B 1 201 ? 25.329 52.485 30.835  1.00 9.27  ? 179 VAL B CA  1 
ATOM   3372 C  C   . VAL B 1 201 ? 25.531 51.947 29.416  1.00 8.95  ? 179 VAL B C   1 
ATOM   3373 O  O   . VAL B 1 201 ? 25.893 50.789 29.241  1.00 8.68  ? 179 VAL B O   1 
ATOM   3374 C  CB  . VAL B 1 201 ? 26.689 52.834 31.485  1.00 9.26  ? 179 VAL B CB  1 
ATOM   3375 C  CG1 . VAL B 1 201 ? 27.588 53.614 30.531  1.00 9.24  ? 179 VAL B CG1 1 
ATOM   3376 C  CG2 . VAL B 1 201 ? 26.473 53.598 32.784  1.00 9.28  ? 179 VAL B CG2 1 
ATOM   3377 N  N   . ASN B 1 202 ? 25.288 52.794 28.417  1.00 8.59  ? 180 ASN B N   1 
ATOM   3378 C  CA  . ASN B 1 202 ? 25.434 52.424 27.010  1.00 8.66  ? 180 ASN B CA  1 
ATOM   3379 C  C   . ASN B 1 202 ? 26.883 52.499 26.547  1.00 8.88  ? 180 ASN B C   1 
ATOM   3380 O  O   . ASN B 1 202 ? 27.360 51.616 25.831  1.00 8.85  ? 180 ASN B O   1 
ATOM   3381 C  CB  . ASN B 1 202 ? 24.601 53.353 26.116  1.00 8.45  ? 180 ASN B CB  1 
ATOM   3382 C  CG  . ASN B 1 202 ? 23.116 53.094 26.220  1.00 8.37  ? 180 ASN B CG  1 
ATOM   3383 O  OD1 . ASN B 1 202 ? 22.523 52.426 25.364  1.00 8.51  ? 180 ASN B OD1 1 
ATOM   3384 N  ND2 . ASN B 1 202 ? 22.506 53.603 27.260  1.00 8.10  ? 180 ASN B ND2 1 
ATOM   3385 N  N   . ARG B 1 203 ? 27.558 53.585 26.915  1.00 9.32  ? 181 ARG B N   1 
ATOM   3386 C  CA  . ARG B 1 203 ? 28.925 53.839 26.453  1.00 9.73  ? 181 ARG B CA  1 
ATOM   3387 C  C   . ARG B 1 203 ? 29.748 54.481 27.551  1.00 9.84  ? 181 ARG B C   1 
ATOM   3388 O  O   . ARG B 1 203 ? 29.264 55.358 28.268  1.00 9.51  ? 181 ARG B O   1 
ATOM   3389 C  CB  . ARG B 1 203 ? 28.938 54.773 25.236  1.00 10.06 ? 181 ARG B CB  1 
ATOM   3390 C  CG  . ARG B 1 203 ? 28.003 54.375 24.104  1.00 10.50 ? 181 ARG B CG  1 
ATOM   3391 C  CD  . ARG B 1 203 ? 28.039 55.359 22.946  1.00 10.89 ? 181 ARG B CD  1 
ATOM   3392 N  NE  . ARG B 1 203 ? 27.160 54.922 21.870  1.00 11.39 ? 181 ARG B NE  1 
ATOM   3393 C  CZ  . ARG B 1 203 ? 26.990 55.551 20.711  1.00 11.94 ? 181 ARG B CZ  1 
ATOM   3394 N  NH1 . ARG B 1 203 ? 27.635 56.680 20.451  1.00 12.46 ? 181 ARG B NH1 1 
ATOM   3395 N  NH2 . ARG B 1 203 ? 26.159 55.047 19.806  1.00 12.40 ? 181 ARG B NH2 1 
ATOM   3396 N  N   . VAL B 1 204 ? 30.998 54.047 27.662  1.00 10.26 ? 182 VAL B N   1 
ATOM   3397 C  CA  . VAL B 1 204 ? 31.968 54.689 28.534  1.00 10.84 ? 182 VAL B CA  1 
ATOM   3398 C  C   . VAL B 1 204 ? 32.967 55.441 27.661  1.00 11.61 ? 182 VAL B C   1 
ATOM   3399 O  O   . VAL B 1 204 ? 33.468 54.892 26.670  1.00 11.67 ? 182 VAL B O   1 
ATOM   3400 C  CB  . VAL B 1 204 ? 32.706 53.672 29.426  1.00 10.71 ? 182 VAL B CB  1 
ATOM   3401 C  CG1 . VAL B 1 204 ? 33.714 54.385 30.324  1.00 10.89 ? 182 VAL B CG1 1 
ATOM   3402 C  CG2 . VAL B 1 204 ? 31.711 52.884 30.268  1.00 10.77 ? 182 VAL B CG2 1 
ATOM   3403 N  N   . VAL B 1 205 ? 33.243 56.688 28.039  1.00 12.81 ? 183 VAL B N   1 
ATOM   3404 C  CA  . VAL B 1 205 ? 34.132 57.574 27.280  1.00 14.20 ? 183 VAL B CA  1 
ATOM   3405 C  C   . VAL B 1 205 ? 35.180 58.232 28.185  1.00 15.51 ? 183 VAL B C   1 
ATOM   3406 O  O   . VAL B 1 205 ? 35.094 58.157 29.416  1.00 15.48 ? 183 VAL B O   1 
ATOM   3407 C  CB  . VAL B 1 205 ? 33.331 58.666 26.541  1.00 14.34 ? 183 VAL B CB  1 
ATOM   3408 C  CG1 . VAL B 1 205 ? 32.342 58.034 25.574  1.00 14.54 ? 183 VAL B CG1 1 
ATOM   3409 C  CG2 . VAL B 1 205 ? 32.606 59.590 27.515  1.00 14.26 ? 183 VAL B CG2 1 
ATOM   3410 N  N   . ASP B 1 206 ? 36.171 58.872 27.567  1.00 17.44 ? 184 ASP B N   1 
ATOM   3411 C  CA  . ASP B 1 206 ? 37.185 59.629 28.308  1.00 19.36 ? 184 ASP B CA  1 
ATOM   3412 C  C   . ASP B 1 206 ? 36.561 60.827 29.010  1.00 19.40 ? 184 ASP B C   1 
ATOM   3413 O  O   . ASP B 1 206 ? 35.553 61.368 28.552  1.00 19.55 ? 184 ASP B O   1 
ATOM   3414 C  CB  . ASP B 1 206 ? 38.296 60.123 27.371  1.00 21.07 ? 184 ASP B CB  1 
ATOM   3415 C  CG  . ASP B 1 206 ? 39.163 58.998 26.832  1.00 22.86 ? 184 ASP B CG  1 
ATOM   3416 O  OD1 . ASP B 1 206 ? 39.259 57.932 27.476  1.00 24.96 ? 184 ASP B OD1 1 
ATOM   3417 O  OD2 . ASP B 1 206 ? 39.771 59.194 25.758  1.00 25.49 ? 184 ASP B OD2 1 
ATOM   3418 N  N   . GLY B 1 207 ? 37.178 61.249 30.112  1.00 19.72 ? 185 GLY B N   1 
ATOM   3419 C  CA  . GLY B 1 207 ? 36.669 62.355 30.923  1.00 19.82 ? 185 GLY B CA  1 
ATOM   3420 C  C   . GLY B 1 207 ? 36.378 63.627 30.148  1.00 20.33 ? 185 GLY B C   1 
ATOM   3421 O  O   . GLY B 1 207 ? 35.369 64.292 30.389  1.00 20.80 ? 185 GLY B O   1 
ATOM   3422 N  N   . ASP B 1 208 ? 37.260 63.967 29.211  1.00 20.51 ? 186 ASP B N   1 
ATOM   3423 C  CA  . ASP B 1 208 ? 37.114 65.199 28.435  1.00 20.84 ? 186 ASP B CA  1 
ATOM   3424 C  C   . ASP B 1 208 ? 36.245 65.026 27.187  1.00 18.97 ? 186 ASP B C   1 
ATOM   3425 O  O   . ASP B 1 208 ? 36.022 65.990 26.452  1.00 18.91 ? 186 ASP B O   1 
ATOM   3426 C  CB  . ASP B 1 208 ? 38.492 65.754 28.038  1.00 22.78 ? 186 ASP B CB  1 
ATOM   3427 C  CG  . ASP B 1 208 ? 39.234 64.856 27.054  1.00 24.69 ? 186 ASP B CG  1 
ATOM   3428 O  OD1 . ASP B 1 208 ? 39.999 65.394 26.224  1.00 27.44 ? 186 ASP B OD1 1 
ATOM   3429 O  OD2 . ASP B 1 208 ? 39.059 63.615 27.105  1.00 26.64 ? 186 ASP B OD2 1 
ATOM   3430 N  N   . GLY B 1 209 ? 35.762 63.807 26.942  1.00 16.74 ? 187 GLY B N   1 
ATOM   3431 C  CA  . GLY B 1 209 ? 34.989 63.524 25.736  1.00 15.15 ? 187 GLY B CA  1 
ATOM   3432 C  C   . GLY B 1 209 ? 33.500 63.339 25.968  1.00 13.62 ? 187 GLY B C   1 
ATOM   3433 O  O   . GLY B 1 209 ? 32.770 63.030 25.030  1.00 13.25 ? 187 GLY B O   1 
ATOM   3434 N  N   . LEU B 1 210 ? 33.043 63.544 27.203  1.00 12.49 ? 188 LEU B N   1 
ATOM   3435 C  CA  . LEU B 1 210 ? 31.642 63.296 27.560  1.00 11.77 ? 188 LEU B CA  1 
ATOM   3436 C  C   . LEU B 1 210 ? 30.668 64.227 26.836  1.00 11.51 ? 188 LEU B C   1 
ATOM   3437 O  O   . LEU B 1 210 ? 29.687 63.772 26.243  1.00 10.96 ? 188 LEU B O   1 
ATOM   3438 C  CB  . LEU B 1 210 ? 31.446 63.431 29.068  1.00 11.53 ? 188 LEU B CB  1 
ATOM   3439 C  CG  . LEU B 1 210 ? 30.035 63.174 29.613  1.00 11.41 ? 188 LEU B CG  1 
ATOM   3440 C  CD1 . LEU B 1 210 ? 29.684 61.696 29.513  1.00 11.43 ? 188 LEU B CD1 1 
ATOM   3441 C  CD2 . LEU B 1 210 ? 29.911 63.662 31.044  1.00 11.50 ? 188 LEU B CD2 1 
ATOM   3442 N  N   . ASP B 1 211 ? 30.924 65.531 26.895  1.00 11.47 ? 189 ASP B N   1 
ATOM   3443 C  CA  . ASP B 1 211 ? 30.026 66.501 26.271  1.00 11.85 ? 189 ASP B CA  1 
ATOM   3444 C  C   . ASP B 1 211 ? 29.905 66.249 24.775  1.00 11.40 ? 189 ASP B C   1 
ATOM   3445 O  O   . ASP B 1 211 ? 28.816 66.337 24.207  1.00 11.24 ? 189 ASP B O   1 
ATOM   3446 C  CB  . ASP B 1 211 ? 30.518 67.941 26.478  1.00 12.46 ? 189 ASP B CB  1 
ATOM   3447 C  CG  . ASP B 1 211 ? 30.228 68.484 27.867  1.00 13.49 ? 189 ASP B CG  1 
ATOM   3448 O  OD1 . ASP B 1 211 ? 29.406 67.903 28.608  1.00 14.25 ? 189 ASP B OD1 1 
ATOM   3449 O  OD2 . ASP B 1 211 ? 30.810 69.539 28.204  1.00 14.46 ? 189 ASP B OD2 1 
ATOM   3450 N  N   . ALA B 1 212 ? 31.037 65.965 24.138  1.00 11.27 ? 190 ALA B N   1 
ATOM   3451 C  CA  . ALA B 1 212 ? 31.075 65.777 22.695  1.00 11.18 ? 190 ALA B CA  1 
ATOM   3452 C  C   . ALA B 1 212 ? 30.315 64.523 22.275  1.00 11.05 ? 190 ALA B C   1 
ATOM   3453 O  O   . ALA B 1 212 ? 29.622 64.535 21.260  1.00 10.96 ? 190 ALA B O   1 
ATOM   3454 C  CB  . ALA B 1 212 ? 32.509 65.717 22.199  1.00 11.33 ? 190 ALA B CB  1 
ATOM   3455 N  N   . GLU B 1 213 ? 30.452 63.450 23.050  1.00 11.10 ? 191 GLU B N   1 
ATOM   3456 C  CA  . GLU B 1 213 ? 29.758 62.195 22.747  1.00 11.47 ? 191 GLU B CA  1 
ATOM   3457 C  C   . GLU B 1 213 ? 28.253 62.357 22.915  1.00 10.90 ? 191 GLU B C   1 
ATOM   3458 O  O   . GLU B 1 213 ? 27.485 61.963 22.038  1.00 10.47 ? 191 GLU B O   1 
ATOM   3459 C  CB  . GLU B 1 213 ? 30.276 61.051 23.625  1.00 12.25 ? 191 GLU B CB  1 
ATOM   3460 C  CG  . GLU B 1 213 ? 29.685 59.675 23.301  1.00 13.28 ? 191 GLU B CG  1 
ATOM   3461 C  CD  . GLU B 1 213 ? 30.213 59.062 22.009  1.00 14.45 ? 191 GLU B CD  1 
ATOM   3462 O  OE1 . GLU B 1 213 ? 31.019 59.697 21.301  1.00 15.98 ? 191 GLU B OE1 1 
ATOM   3463 O  OE2 . GLU B 1 213 ? 29.828 57.919 21.692  1.00 15.65 ? 191 GLU B OE2 1 
ATOM   3464 N  N   . ALA B 1 214 ? 27.831 62.948 24.030  1.00 10.55 ? 192 ALA B N   1 
ATOM   3465 C  CA  . ALA B 1 214 ? 26.407 63.195 24.262  1.00 10.32 ? 192 ALA B CA  1 
ATOM   3466 C  C   . ALA B 1 214 ? 25.816 64.061 23.147  1.00 10.49 ? 192 ALA B C   1 
ATOM   3467 O  O   . ALA B 1 214 ? 24.714 63.793 22.658  1.00 9.88  ? 192 ALA B O   1 
ATOM   3468 C  CB  . ALA B 1 214 ? 26.185 63.849 25.620  1.00 10.31 ? 192 ALA B CB  1 
ATOM   3469 N  N   . LEU B 1 215 ? 26.551 65.095 22.742  1.00 10.70 ? 193 LEU B N   1 
ATOM   3470 C  CA  . LEU B 1 215 ? 26.089 65.979 21.670  1.00 11.54 ? 193 LEU B CA  1 
ATOM   3471 C  C   . LEU B 1 215 ? 26.021 65.293 20.310  1.00 11.70 ? 193 LEU B C   1 
ATOM   3472 O  O   . LEU B 1 215 ? 25.089 65.538 19.547  1.00 11.58 ? 193 LEU B O   1 
ATOM   3473 C  CB  . LEU B 1 215 ? 26.965 67.231 21.574  1.00 12.01 ? 193 LEU B CB  1 
ATOM   3474 C  CG  . LEU B 1 215 ? 26.467 68.364 22.460  1.00 12.68 ? 193 LEU B CG  1 
ATOM   3475 C  CD1 . LEU B 1 215 ? 27.563 69.397 22.678  1.00 13.18 ? 193 LEU B CD1 1 
ATOM   3476 C  CD2 . LEU B 1 215 ? 25.217 68.997 21.851  1.00 12.85 ? 193 LEU B CD2 1 
ATOM   3477 N  N   . ARG B 1 216 ? 26.995 64.440 20.006  1.00 12.33 ? 194 ARG B N   1 
ATOM   3478 C  CA  . ARG B 1 216 ? 26.984 63.686 18.749  1.00 12.92 ? 194 ARG B CA  1 
ATOM   3479 C  C   . ARG B 1 216 ? 25.740 62.804 18.670  1.00 11.81 ? 194 ARG B C   1 
ATOM   3480 O  O   . ARG B 1 216 ? 25.067 62.750 17.639  1.00 11.36 ? 194 ARG B O   1 
ATOM   3481 C  CB  . ARG B 1 216 ? 28.236 62.814 18.612  1.00 14.71 ? 194 ARG B CB  1 
ATOM   3482 C  CG  . ARG B 1 216 ? 29.437 63.536 18.032  1.00 16.58 ? 194 ARG B CG  1 
ATOM   3483 C  CD  . ARG B 1 216 ? 30.646 62.620 17.945  1.00 18.53 ? 194 ARG B CD  1 
ATOM   3484 N  NE  . ARG B 1 216 ? 30.495 61.581 16.926  1.00 20.71 ? 194 ARG B NE  1 
ATOM   3485 C  CZ  . ARG B 1 216 ? 30.191 60.298 17.148  1.00 22.42 ? 194 ARG B CZ  1 
ATOM   3486 N  NH1 . ARG B 1 216 ? 29.979 59.820 18.379  1.00 23.73 ? 194 ARG B NH1 1 
ATOM   3487 N  NH2 . ARG B 1 216 ? 30.103 59.469 16.111  1.00 23.70 ? 194 ARG B NH2 1 
ATOM   3488 N  N   . ILE B 1 217 ? 25.438 62.130 19.775  1.00 10.76 ? 195 ILE B N   1 
ATOM   3489 C  CA  . ILE B 1 217 ? 24.264 61.261 19.849  1.00 10.33 ? 195 ILE B CA  1 
ATOM   3490 C  C   . ILE B 1 217 ? 22.983 62.081 19.684  1.00 9.95  ? 195 ILE B C   1 
ATOM   3491 O  O   . ILE B 1 217 ? 22.086 61.706 18.925  1.00 9.66  ? 195 ILE B O   1 
ATOM   3492 C  CB  . ILE B 1 217 ? 24.234 60.482 21.185  1.00 10.22 ? 195 ILE B CB  1 
ATOM   3493 C  CG1 . ILE B 1 217 ? 25.412 59.499 21.258  1.00 10.19 ? 195 ILE B CG1 1 
ATOM   3494 C  CG2 . ILE B 1 217 ? 22.913 59.741 21.342  1.00 10.23 ? 195 ILE B CG2 1 
ATOM   3495 C  CD1 . ILE B 1 217 ? 25.622 58.864 22.615  1.00 10.22 ? 195 ILE B CD1 1 
ATOM   3496 N  N   . ALA B 1 218 ? 22.901 63.202 20.401  1.00 9.75  ? 196 ALA B N   1 
ATOM   3497 C  CA  . ALA B 1 218 ? 21.717 64.051 20.361  1.00 9.70  ? 196 ALA B CA  1 
ATOM   3498 C  C   . ALA B 1 218 ? 21.497 64.678 18.984  1.00 9.83  ? 196 ALA B C   1 
ATOM   3499 O  O   . ALA B 1 218 ? 20.366 64.770 18.511  1.00 9.53  ? 196 ALA B O   1 
ATOM   3500 C  CB  . ALA B 1 218 ? 21.804 65.127 21.432  1.00 9.68  ? 196 ALA B CB  1 
ATOM   3501 N  N   . ARG B 1 219 ? 22.582 65.104 18.343  1.00 10.09 ? 197 ARG B N   1 
ATOM   3502 C  CA  . ARG B 1 219 ? 22.492 65.696 17.005  1.00 10.36 ? 197 ARG B CA  1 
ATOM   3503 C  C   . ARG B 1 219 ? 22.176 64.643 15.938  1.00 10.20 ? 197 ARG B C   1 
ATOM   3504 O  O   . ARG B 1 219 ? 21.550 64.952 14.924  1.00 10.37 ? 197 ARG B O   1 
ATOM   3505 C  CB  . ARG B 1 219 ? 23.777 66.448 16.670  1.00 10.97 ? 197 ARG B CB  1 
ATOM   3506 C  CG  . ARG B 1 219 ? 23.930 67.725 17.480  1.00 11.61 ? 197 ARG B CG  1 
ATOM   3507 C  CD  . ARG B 1 219 ? 25.270 68.387 17.223  1.00 12.39 ? 197 ARG B CD  1 
ATOM   3508 N  NE  . ARG B 1 219 ? 25.328 68.980 15.895  1.00 13.47 ? 197 ARG B NE  1 
ATOM   3509 C  CZ  . ARG B 1 219 ? 26.371 69.651 15.412  1.00 14.32 ? 197 ARG B CZ  1 
ATOM   3510 N  NH1 . ARG B 1 219 ? 27.465 69.825 16.149  1.00 14.79 ? 197 ARG B NH1 1 
ATOM   3511 N  NH2 . ARG B 1 219 ? 26.314 70.155 14.185  1.00 14.96 ? 197 ARG B NH2 1 
ATOM   3512 N  N   . HIS B 1 220 ? 22.605 63.406 16.173  1.00 10.05 ? 198 HIS B N   1 
ATOM   3513 C  CA  . HIS B 1 220 ? 22.249 62.279 15.301  1.00 10.15 ? 198 HIS B CA  1 
ATOM   3514 C  C   . HIS B 1 220 ? 20.733 62.088 15.320  1.00 9.95  ? 198 HIS B C   1 
ATOM   3515 O  O   . HIS B 1 220 ? 20.081 62.027 14.278  1.00 9.82  ? 198 HIS B O   1 
ATOM   3516 C  CB  . HIS B 1 220 ? 22.959 61.013 15.789  1.00 10.25 ? 198 HIS B CB  1 
ATOM   3517 C  CG  . HIS B 1 220 ? 22.778 59.821 14.906  1.00 10.63 ? 198 HIS B CG  1 
ATOM   3518 N  ND1 . HIS B 1 220 ? 23.791 59.325 14.116  1.00 10.87 ? 198 HIS B ND1 1 
ATOM   3519 C  CD2 . HIS B 1 220 ? 21.717 59.005 14.713  1.00 10.83 ? 198 HIS B CD2 1 
ATOM   3520 C  CE1 . HIS B 1 220 ? 23.359 58.260 13.465  1.00 10.99 ? 198 HIS B CE1 1 
ATOM   3521 N  NE2 . HIS B 1 220 ? 22.102 58.047 13.806  1.00 11.00 ? 198 HIS B NE2 1 
ATOM   3522 N  N   . ILE B 1 221 ? 20.180 62.017 16.523  1.00 10.01 ? 199 ILE B N   1 
ATOM   3523 C  CA  . ILE B 1 221 ? 18.732 61.938 16.714  1.00 10.15 ? 199 ILE B CA  1 
ATOM   3524 C  C   . ILE B 1 221 ? 18.020 63.125 16.072  1.00 10.25 ? 199 ILE B C   1 
ATOM   3525 O  O   . ILE B 1 221 ? 16.986 62.961 15.418  1.00 10.12 ? 199 ILE B O   1 
ATOM   3526 C  CB  . ILE B 1 221 ? 18.391 61.826 18.224  1.00 10.30 ? 199 ILE B CB  1 
ATOM   3527 C  CG1 . ILE B 1 221 ? 18.804 60.440 18.729  1.00 10.49 ? 199 ILE B CG1 1 
ATOM   3528 C  CG2 . ILE B 1 221 ? 16.912 62.076 18.480  1.00 10.48 ? 199 ILE B CG2 1 
ATOM   3529 C  CD1 . ILE B 1 221 ? 18.830 60.288 20.232  1.00 10.50 ? 199 ILE B CD1 1 
ATOM   3530 N  N   . GLY B 1 222 ? 18.591 64.316 16.242  1.00 10.30 ? 200 GLY B N   1 
ATOM   3531 C  CA  . GLY B 1 222 ? 18.010 65.544 15.718  1.00 10.61 ? 200 GLY B CA  1 
ATOM   3532 C  C   . GLY B 1 222 ? 17.948 65.657 14.203  1.00 10.85 ? 200 GLY B C   1 
ATOM   3533 O  O   . GLY B 1 222 ? 17.242 66.525 13.684  1.00 11.32 ? 200 GLY B O   1 
ATOM   3534 N  N   . ALA B 1 223 ? 18.693 64.803 13.501  1.00 10.98 ? 201 ALA B N   1 
ATOM   3535 C  CA  . ALA B 1 223 ? 18.649 64.724 12.037  1.00 11.03 ? 201 ALA B CA  1 
ATOM   3536 C  C   . ALA B 1 223 ? 17.450 63.934 11.527  1.00 11.07 ? 201 ALA B C   1 
ATOM   3537 O  O   . ALA B 1 223 ? 17.150 63.969 10.335  1.00 11.59 ? 201 ALA B O   1 
ATOM   3538 C  CB  . ALA B 1 223 ? 19.924 64.098 11.502  1.00 11.09 ? 201 ALA B CB  1 
ATOM   3539 N  N   . ILE B 1 224 ? 16.787 63.200 12.417  1.00 10.88 ? 202 ILE B N   1 
ATOM   3540 C  CA  . ILE B 1 224 ? 15.670 62.336 12.031  1.00 10.75 ? 202 ILE B CA  1 
ATOM   3541 C  C   . ILE B 1 224 ? 14.347 63.082 12.182  1.00 10.77 ? 202 ILE B C   1 
ATOM   3542 O  O   . ILE B 1 224 ? 14.181 63.908 13.082  1.00 10.49 ? 202 ILE B O   1 
ATOM   3543 C  CB  . ILE B 1 224 ? 15.652 61.050 12.883  1.00 10.67 ? 202 ILE B CB  1 
ATOM   3544 C  CG1 . ILE B 1 224 ? 17.000 60.331 12.773  1.00 10.79 ? 202 ILE B CG1 1 
ATOM   3545 C  CG2 . ILE B 1 224 ? 14.520 60.116 12.453  1.00 10.57 ? 202 ILE B CG2 1 
ATOM   3546 C  CD1 . ILE B 1 224 ? 17.194 59.217 13.780  1.00 10.95 ? 202 ILE B CD1 1 
ATOM   3547 N  N   . ASP B 1 225 ? 13.419 62.799 11.272  1.00 11.03 ? 203 ASP B N   1 
ATOM   3548 C  CA  . ASP B 1 225 ? 12.047 63.294 11.345  1.00 11.45 ? 203 ASP B CA  1 
ATOM   3549 C  C   . ASP B 1 225 ? 11.548 63.191 12.796  1.00 10.83 ? 203 ASP B C   1 
ATOM   3550 O  O   . ASP B 1 225 ? 11.522 62.092 13.345  1.00 10.44 ? 203 ASP B O   1 
ATOM   3551 C  CB  . ASP B 1 225 ? 11.185 62.448 10.400  1.00 12.53 ? 203 ASP B CB  1 
ATOM   3552 C  CG  . ASP B 1 225 ? 9.702  62.737 10.505  1.00 13.74 ? 203 ASP B CG  1 
ATOM   3553 O  OD1 . ASP B 1 225 ? 9.306  63.848 10.901  1.00 15.56 ? 203 ASP B OD1 1 
ATOM   3554 O  OD2 . ASP B 1 225 ? 8.925  61.835 10.147  1.00 15.23 ? 203 ASP B OD2 1 
ATOM   3555 N  N   . PRO B 1 226 ? 11.177 64.327 13.427  1.00 10.26 ? 204 PRO B N   1 
ATOM   3556 C  CA  . PRO B 1 226 ? 10.777 64.255 14.844  1.00 9.90  ? 204 PRO B CA  1 
ATOM   3557 C  C   . PRO B 1 226 ? 9.604  63.311 15.122  1.00 9.46  ? 204 PRO B C   1 
ATOM   3558 O  O   . PRO B 1 226 ? 9.585  62.645 16.166  1.00 9.36  ? 204 PRO B O   1 
ATOM   3559 C  CB  . PRO B 1 226 ? 10.392 65.700 15.182  1.00 10.22 ? 204 PRO B CB  1 
ATOM   3560 C  CG  . PRO B 1 226 ? 11.138 66.531 14.203  1.00 10.36 ? 204 PRO B CG  1 
ATOM   3561 C  CD  . PRO B 1 226 ? 11.237 65.721 12.947  1.00 10.26 ? 204 PRO B CD  1 
ATOM   3562 N  N   . GLY B 1 227 ? 8.638  63.255 14.210  1.00 8.92  ? 205 GLY B N   1 
ATOM   3563 C  CA  . GLY B 1 227 ? 7.497  62.353 14.365  1.00 8.58  ? 205 GLY B CA  1 
ATOM   3564 C  C   . GLY B 1 227 ? 7.913  60.891 14.373  1.00 8.19  ? 205 GLY B C   1 
ATOM   3565 O  O   . GLY B 1 227 ? 7.387  60.089 15.145  1.00 8.03  ? 205 GLY B O   1 
ATOM   3566 N  N   . LEU B 1 228 ? 8.869  60.544 13.515  1.00 7.77  ? 206 LEU B N   1 
ATOM   3567 C  CA  . LEU B 1 228 ? 9.384  59.179 13.435  1.00 7.69  ? 206 LEU B CA  1 
ATOM   3568 C  C   . LEU B 1 228 ? 10.051 58.774 14.749  1.00 7.57  ? 206 LEU B C   1 
ATOM   3569 O  O   . LEU B 1 228 ? 9.827  57.682 15.265  1.00 7.42  ? 206 LEU B O   1 
ATOM   3570 C  CB  . LEU B 1 228 ? 10.378 59.059 12.267  1.00 7.69  ? 206 LEU B CB  1 
ATOM   3571 C  CG  . LEU B 1 228 ? 11.057 57.703 12.064  1.00 7.70  ? 206 LEU B CG  1 
ATOM   3572 C  CD1 . LEU B 1 228 ? 10.038 56.582 11.939  1.00 7.76  ? 206 LEU B CD1 1 
ATOM   3573 C  CD2 . LEU B 1 228 ? 11.960 57.741 10.841  1.00 7.77  ? 206 LEU B CD2 1 
ATOM   3574 N  N   . VAL B 1 229 ? 10.877 59.667 15.284  1.00 7.65  ? 207 VAL B N   1 
ATOM   3575 C  CA  . VAL B 1 229 ? 11.540 59.435 16.564  1.00 7.72  ? 207 VAL B CA  1 
ATOM   3576 C  C   . VAL B 1 229 ? 10.499 59.296 17.673  1.00 7.88  ? 207 VAL B C   1 
ATOM   3577 O  O   . VAL B 1 229 ? 10.570 58.384 18.496  1.00 7.63  ? 207 VAL B O   1 
ATOM   3578 C  CB  . VAL B 1 229 ? 12.508 60.588 16.905  1.00 7.81  ? 207 VAL B CB  1 
ATOM   3579 C  CG1 . VAL B 1 229 ? 13.036 60.465 18.331  1.00 7.87  ? 207 VAL B CG1 1 
ATOM   3580 C  CG2 . VAL B 1 229 ? 13.653 60.616 15.902  1.00 7.89  ? 207 VAL B CG2 1 
ATOM   3581 N  N   . LYS B 1 230 ? 9.531  60.205 17.678  1.00 8.09  ? 208 LYS B N   1 
ATOM   3582 C  CA  . LYS B 1 230 ? 8.491  60.220 18.703  1.00 8.49  ? 208 LYS B CA  1 
ATOM   3583 C  C   . LYS B 1 230 ? 7.734  58.896 18.723  1.00 8.22  ? 208 LYS B C   1 
ATOM   3584 O  O   . LYS B 1 230 ? 7.560  58.288 19.776  1.00 8.09  ? 208 LYS B O   1 
ATOM   3585 C  CB  . LYS B 1 230 ? 7.514  61.380 18.458  1.00 9.30  ? 208 LYS B CB  1 
ATOM   3586 C  CG  . LYS B 1 230 ? 6.310  61.415 19.391  1.00 10.26 ? 208 LYS B CG  1 
ATOM   3587 C  CD  . LYS B 1 230 ? 5.397  62.591 19.073  1.00 11.15 ? 208 LYS B CD  1 
ATOM   3588 C  CE  . LYS B 1 230 ? 4.010  62.400 19.663  1.00 12.20 ? 208 LYS B CE  1 
ATOM   3589 N  NZ  . LYS B 1 230 ? 3.106  63.536 19.337  1.00 13.00 ? 208 LYS B NZ  1 
ATOM   3590 N  N   . GLU B 1 231 ? 7.280  58.457 17.557  1.00 8.11  ? 209 GLU B N   1 
ATOM   3591 C  CA  . GLU B 1 231 ? 6.464  57.247 17.486  1.00 8.05  ? 209 GLU B CA  1 
ATOM   3592 C  C   . GLU B 1 231 ? 7.281  55.999 17.783  1.00 7.60  ? 209 GLU B C   1 
ATOM   3593 O  O   . GLU B 1 231 ? 6.769  55.042 18.369  1.00 7.41  ? 209 GLU B O   1 
ATOM   3594 C  CB  . GLU B 1 231 ? 5.774  57.130 16.127  1.00 8.61  ? 209 GLU B CB  1 
ATOM   3595 C  CG  . GLU B 1 231 ? 4.766  58.243 15.855  1.00 9.12  ? 209 GLU B CG  1 
ATOM   3596 C  CD  . GLU B 1 231 ? 3.654  58.327 16.892  1.00 9.66  ? 209 GLU B CD  1 
ATOM   3597 O  OE1 . GLU B 1 231 ? 3.136  57.268 17.311  1.00 10.45 ? 209 GLU B OE1 1 
ATOM   3598 O  OE2 . GLU B 1 231 ? 3.290  59.454 17.295  1.00 10.36 ? 209 GLU B OE2 1 
ATOM   3599 N  N   . THR B 1 232 ? 8.550  56.012 17.401  1.00 7.18  ? 210 THR B N   1 
ATOM   3600 C  CA  . THR B 1 232 ? 9.415  54.865 17.659  1.00 6.99  ? 210 THR B CA  1 
ATOM   3601 C  C   . THR B 1 232 ? 9.730  54.768 19.151  1.00 7.03  ? 210 THR B C   1 
ATOM   3602 O  O   . THR B 1 232 ? 9.718  53.668 19.721  1.00 6.85  ? 210 THR B O   1 
ATOM   3603 C  CB  . THR B 1 232 ? 10.688 54.936 16.797  1.00 6.91  ? 210 THR B CB  1 
ATOM   3604 O  OG1 . THR B 1 232 ? 10.312 54.952 15.413  1.00 6.81  ? 210 THR B OG1 1 
ATOM   3605 C  CG2 . THR B 1 232 ? 11.592 53.744 17.053  1.00 6.85  ? 210 THR B CG2 1 
ATOM   3606 N  N   . LYS B 1 233 ? 9.976  55.905 19.807  1.00 7.13  ? 211 LYS B N   1 
ATOM   3607 C  CA  . LYS B 1 233 ? 10.157 55.883 21.262  1.00 7.33  ? 211 LYS B CA  1 
ATOM   3608 C  C   . LYS B 1 233 ? 8.881  55.390 21.951  1.00 7.46  ? 211 LYS B C   1 
ATOM   3609 O  O   . LYS B 1 233 ? 8.959  54.644 22.921  1.00 7.24  ? 211 LYS B O   1 
ATOM   3610 C  CB  . LYS B 1 233 ? 10.565 57.244 21.843  1.00 7.41  ? 211 LYS B CB  1 
ATOM   3611 C  CG  . LYS B 1 233 ? 10.690 57.187 23.362  1.00 7.55  ? 211 LYS B CG  1 
ATOM   3612 C  CD  . LYS B 1 233 ? 11.280 58.426 24.005  1.00 7.61  ? 211 LYS B CD  1 
ATOM   3613 C  CE  . LYS B 1 233 ? 11.105 58.328 25.516  1.00 7.71  ? 211 LYS B CE  1 
ATOM   3614 N  NZ  . LYS B 1 233 ? 11.851 59.365 26.262  1.00 7.77  ? 211 LYS B NZ  1 
ATOM   3615 N  N   . ARG B 1 234 ? 7.715  55.798 21.454  1.00 7.77  ? 212 ARG B N   1 
ATOM   3616 C  CA  . ARG B 1 234 ? 6.453  55.317 22.024  1.00 8.26  ? 212 ARG B CA  1 
ATOM   3617 C  C   . ARG B 1 234 ? 6.403  53.796 21.984  1.00 7.92  ? 212 ARG B C   1 
ATOM   3618 O  O   . ARG B 1 234 ? 6.020  53.154 22.966  1.00 7.88  ? 212 ARG B O   1 
ATOM   3619 C  CB  . ARG B 1 234 ? 5.239  55.884 21.281  1.00 9.01  ? 212 ARG B CB  1 
ATOM   3620 C  CG  . ARG B 1 234 ? 4.942  57.342 21.579  1.00 9.81  ? 212 ARG B CG  1 
ATOM   3621 C  CD  . ARG B 1 234 ? 3.698  57.812 20.839  1.00 10.56 ? 212 ARG B CD  1 
ATOM   3622 N  NE  . ARG B 1 234 ? 2.487  57.219 21.402  1.00 11.47 ? 212 ARG B NE  1 
ATOM   3623 C  CZ  . ARG B 1 234 ? 1.555  56.536 20.733  1.00 11.93 ? 212 ARG B CZ  1 
ATOM   3624 N  NH1 . ARG B 1 234 ? 1.622  56.350 19.415  1.00 12.38 ? 212 ARG B NH1 1 
ATOM   3625 N  NH2 . ARG B 1 234 ? 0.512  56.048 21.400  1.00 12.26 ? 212 ARG B NH2 1 
ATOM   3626 N  N   . ALA B 1 235 ? 6.796  53.232 20.846  1.00 7.58  ? 213 ALA B N   1 
ATOM   3627 C  CA  . ALA B 1 235 ? 6.769  51.787 20.647  1.00 7.48  ? 213 ALA B CA  1 
ATOM   3628 C  C   . ALA B 1 235 ? 7.769  51.098 21.575  1.00 7.42  ? 213 ALA B C   1 
ATOM   3629 O  O   . ALA B 1 235 ? 7.462  50.054 22.151  1.00 7.41  ? 213 ALA B O   1 
ATOM   3630 C  CB  . ALA B 1 235 ? 7.040  51.439 19.190  1.00 7.43  ? 213 ALA B CB  1 
ATOM   3631 N  N   . LEU B 1 236 ? 8.957  51.685 21.725  1.00 7.40  ? 214 LEU B N   1 
ATOM   3632 C  CA  . LEU B 1 236 ? 9.983  51.131 22.612  1.00 7.43  ? 214 LEU B CA  1 
ATOM   3633 C  C   . LEU B 1 236 ? 9.524  51.130 24.068  1.00 7.46  ? 214 LEU B C   1 
ATOM   3634 O  O   . LEU B 1 236 ? 9.651  50.118 24.765  1.00 7.28  ? 214 LEU B O   1 
ATOM   3635 C  CB  . LEU B 1 236 ? 11.289 51.920 22.481  1.00 7.55  ? 214 LEU B CB  1 
ATOM   3636 C  CG  . LEU B 1 236 ? 12.105 51.588 21.234  1.00 7.67  ? 214 LEU B CG  1 
ATOM   3637 C  CD1 . LEU B 1 236 ? 12.984 52.766 20.848  1.00 7.79  ? 214 LEU B CD1 1 
ATOM   3638 C  CD2 . LEU B 1 236 ? 12.938 50.333 21.460  1.00 7.81  ? 214 LEU B CD2 1 
ATOM   3639 N  N   . ASN B 1 237 ? 8.983  52.255 24.527  1.00 7.59  ? 215 ASN B N   1 
ATOM   3640 C  CA  . ASN B 1 237 ? 8.491  52.339 25.899  1.00 7.69  ? 215 ASN B CA  1 
ATOM   3641 C  C   . ASN B 1 237 ? 7.337  51.373 26.139  1.00 7.76  ? 215 ASN B C   1 
ATOM   3642 O  O   . ASN B 1 237 ? 7.197  50.830 27.238  1.00 7.63  ? 215 ASN B O   1 
ATOM   3643 C  CB  . ASN B 1 237 ? 8.058  53.763 26.256  1.00 7.93  ? 215 ASN B CB  1 
ATOM   3644 C  CG  . ASN B 1 237 ? 9.225  54.659 26.613  1.00 8.08  ? 215 ASN B CG  1 
ATOM   3645 O  OD1 . ASN B 1 237 ? 10.394 54.299 26.416  1.00 8.52  ? 215 ASN B OD1 1 
ATOM   3646 N  ND2 . ASN B 1 237 ? 8.915  55.833 27.158  1.00 8.15  ? 215 ASN B ND2 1 
ATOM   3647 N  N   . ARG B 1 238 ? 6.519  51.165 25.110  1.00 7.87  ? 216 ARG B N   1 
ATOM   3648 C  CA  . ARG B 1 238 ? 5.376  50.261 25.211  1.00 8.08  ? 216 ARG B CA  1 
ATOM   3649 C  C   . ARG B 1 238 ? 5.792  48.844 25.580  1.00 7.97  ? 216 ARG B C   1 
ATOM   3650 O  O   . ARG B 1 238 ? 5.039  48.143 26.248  1.00 7.80  ? 216 ARG B O   1 
ATOM   3651 C  CB  . ARG B 1 238 ? 4.584  50.230 23.900  1.00 8.47  ? 216 ARG B CB  1 
ATOM   3652 C  CG  . ARG B 1 238 ? 3.263  49.475 23.979  1.00 8.95  ? 216 ARG B CG  1 
ATOM   3653 C  CD  . ARG B 1 238 ? 2.214  50.223 24.784  1.00 9.44  ? 216 ARG B CD  1 
ATOM   3654 N  NE  . ARG B 1 238 ? 2.013  51.562 24.238  1.00 10.07 ? 216 ARG B NE  1 
ATOM   3655 C  CZ  . ARG B 1 238 ? 1.312  51.844 23.139  1.00 10.37 ? 216 ARG B CZ  1 
ATOM   3656 N  NH1 . ARG B 1 238 ? 0.679  50.891 22.461  1.00 10.74 ? 216 ARG B NH1 1 
ATOM   3657 N  NH2 . ARG B 1 238 ? 1.234  53.105 22.726  1.00 10.84 ? 216 ARG B NH2 1 
ATOM   3658 N  N   . ALA B 1 239 ? 6.972  48.418 25.133  1.00 8.01  ? 217 ALA B N   1 
ATOM   3659 C  CA  . ALA B 1 239 ? 7.472  47.083 25.467  1.00 8.23  ? 217 ALA B CA  1 
ATOM   3660 C  C   . ALA B 1 239 ? 7.567  46.885 26.981  1.00 8.49  ? 217 ALA B C   1 
ATOM   3661 O  O   . ALA B 1 239 ? 7.112  45.876 27.504  1.00 8.79  ? 217 ALA B O   1 
ATOM   3662 C  CB  . ALA B 1 239 ? 8.819  46.833 24.796  1.00 8.29  ? 217 ALA B CB  1 
ATOM   3663 N  N   . LEU B 1 240 ? 8.126  47.860 27.693  1.00 8.60  ? 218 LEU B N   1 
ATOM   3664 C  CA  . LEU B 1 240 ? 8.241  47.747 29.152  1.00 8.73  ? 218 LEU B CA  1 
ATOM   3665 C  C   . LEU B 1 240 ? 6.912  48.033 29.845  1.00 8.58  ? 218 LEU B C   1 
ATOM   3666 O  O   . LEU B 1 240 ? 6.581  47.408 30.845  1.00 8.51  ? 218 LEU B O   1 
ATOM   3667 C  CB  . LEU B 1 240 ? 9.356  48.657 29.691  1.00 9.15  ? 218 LEU B CB  1 
ATOM   3668 C  CG  . LEU B 1 240 ? 10.736 47.993 29.655  1.00 9.54  ? 218 LEU B CG  1 
ATOM   3669 C  CD1 . LEU B 1 240 ? 11.168 47.674 28.231  1.00 9.81  ? 218 LEU B CD1 1 
ATOM   3670 C  CD2 . LEU B 1 240 ? 11.781 48.833 30.373  1.00 9.85  ? 218 LEU B CD2 1 
ATOM   3671 N  N   . GLU B 1 241 ? 6.139  48.971 29.316  1.00 8.37  ? 219 GLU B N   1 
ATOM   3672 C  CA  . GLU B 1 241 ? 4.847  49.293 29.921  1.00 8.54  ? 219 GLU B CA  1 
ATOM   3673 C  C   . GLU B 1 241 ? 3.869  48.117 29.799  1.00 8.01  ? 219 GLU B C   1 
ATOM   3674 O  O   . GLU B 1 241 ? 3.067  47.869 30.701  1.00 7.57  ? 219 GLU B O   1 
ATOM   3675 C  CB  . GLU B 1 241 ? 4.293  50.579 29.326  1.00 9.41  ? 219 GLU B CB  1 
ATOM   3676 C  CG  . GLU B 1 241 ? 5.134  51.782 29.742  1.00 10.34 ? 219 GLU B CG  1 
ATOM   3677 C  CD  . GLU B 1 241 ? 4.966  52.992 28.849  1.00 11.54 ? 219 GLU B CD  1 
ATOM   3678 O  OE1 . GLU B 1 241 ? 4.281  52.894 27.800  1.00 13.33 ? 219 GLU B OE1 1 
ATOM   3679 O  OE2 . GLU B 1 241 ? 5.548  54.046 29.193  1.00 12.07 ? 219 GLU B OE2 1 
ATOM   3680 N  N   . THR B 1 242 ? 3.985  47.359 28.713  1.00 7.59  ? 220 THR B N   1 
ATOM   3681 C  CA  . THR B 1 242 ? 3.167  46.161 28.515  1.00 7.58  ? 220 THR B CA  1 
ATOM   3682 C  C   . THR B 1 242 ? 3.398  45.133 29.622  1.00 7.63  ? 220 THR B C   1 
ATOM   3683 O  O   . THR B 1 242 ? 2.474  44.422 30.035  1.00 7.40  ? 220 THR B O   1 
ATOM   3684 C  CB  . THR B 1 242 ? 3.472  45.527 27.146  1.00 7.60  ? 220 THR B CB  1 
ATOM   3685 O  OG1 . THR B 1 242 ? 3.025  46.425 26.122  1.00 7.68  ? 220 THR B OG1 1 
ATOM   3686 C  CG2 . THR B 1 242 ? 2.787  44.180 26.983  1.00 7.64  ? 220 THR B CG2 1 
ATOM   3687 N  N   . GLN B 1 243 ? 4.634  45.074 30.104  1.00 7.90  ? 221 GLN B N   1 
ATOM   3688 C  CA  . GLN B 1 243 ? 5.010  44.136 31.163  1.00 8.38  ? 221 GLN B CA  1 
ATOM   3689 C  C   . GLN B 1 243 ? 4.478  44.546 32.536  1.00 8.34  ? 221 GLN B C   1 
ATOM   3690 O  O   . GLN B 1 243 ? 4.585  43.778 33.495  1.00 8.43  ? 221 GLN B O   1 
ATOM   3691 C  CB  . GLN B 1 243 ? 6.526  44.006 31.223  1.00 8.87  ? 221 GLN B CB  1 
ATOM   3692 C  CG  . GLN B 1 243 ? 7.152  43.511 29.934  1.00 9.40  ? 221 GLN B CG  1 
ATOM   3693 C  CD  . GLN B 1 243 ? 8.661  43.545 29.984  1.00 9.94  ? 221 GLN B CD  1 
ATOM   3694 O  OE1 . GLN B 1 243 ? 9.256  43.110 30.963  1.00 11.05 ? 221 GLN B OE1 1 
ATOM   3695 N  NE2 . GLN B 1 243 ? 9.289  44.052 28.933  1.00 10.18 ? 221 GLN B NE2 1 
ATOM   3696 N  N   . GLY B 1 244 ? 3.926  45.755 32.632  1.00 8.25  ? 222 GLY B N   1 
ATOM   3697 C  CA  . GLY B 1 244 ? 3.354  46.270 33.868  1.00 8.21  ? 222 GLY B CA  1 
ATOM   3698 C  C   . GLY B 1 244 ? 4.298  47.145 34.670  1.00 8.35  ? 222 GLY B C   1 
ATOM   3699 O  O   . GLY B 1 244 ? 4.048  47.406 35.843  1.00 8.00  ? 222 GLY B O   1 
HETATM 3700 N  N   . MSE B 1 245 ? 5.358  47.644 34.034  1.00 8.76  ? 223 MSE B N   1 
HETATM 3701 C  CA  . MSE B 1 245 ? 6.368  48.422 34.758  1.00 9.45  ? 223 MSE B CA  1 
HETATM 3702 C  C   . MSE B 1 245 ? 5.776  49.571 35.541  1.00 8.70  ? 223 MSE B C   1 
HETATM 3703 O  O   . MSE B 1 245 ? 6.187  49.816 36.669  1.00 8.13  ? 223 MSE B O   1 
HETATM 3704 C  CB  . MSE B 1 245 ? 7.461  48.929 33.818  1.00 11.09 ? 223 MSE B CB  1 
HETATM 3705 C  CG  . MSE B 1 245 ? 8.476  49.753 34.611  1.00 12.83 ? 223 MSE B CG  1 
HETATM 3706 SE SE  . MSE B 1 245 ? 10.000 50.289 33.493  1.00 18.47 ? 223 MSE B SE  1 
HETATM 3707 C  CE  . MSE B 1 245 ? 9.195  51.912 32.737  1.00 16.20 ? 223 MSE B CE  1 
ATOM   3708 N  N   . LEU B 1 246 ? 4.818  50.295 34.971  1.00 8.11  ? 224 LEU B N   1 
ATOM   3709 C  CA  . LEU B 1 246 ? 4.280  51.468 35.669  1.00 7.96  ? 224 LEU B CA  1 
ATOM   3710 C  C   . LEU B 1 246 ? 3.524  51.076 36.938  1.00 7.83  ? 224 LEU B C   1 
ATOM   3711 O  O   . LEU B 1 246 ? 3.571  51.789 37.937  1.00 7.82  ? 224 LEU B O   1 
ATOM   3712 C  CB  . LEU B 1 246 ? 3.415  52.323 34.740  1.00 8.00  ? 224 LEU B CB  1 
ATOM   3713 C  CG  . LEU B 1 246 ? 4.130  52.843 33.491  1.00 8.16  ? 224 LEU B CG  1 
ATOM   3714 C  CD1 . LEU B 1 246 ? 3.176  53.677 32.652  1.00 8.33  ? 224 LEU B CD1 1 
ATOM   3715 C  CD2 . LEU B 1 246 ? 5.361  53.663 33.846  1.00 8.21  ? 224 LEU B CD2 1 
ATOM   3716 N  N   . GLN B 1 247 ? 2.851  49.929 36.916  1.00 7.69  ? 225 GLN B N   1 
ATOM   3717 C  CA  . GLN B 1 247 ? 2.190  49.435 38.129  1.00 7.78  ? 225 GLN B CA  1 
ATOM   3718 C  C   . GLN B 1 247 ? 3.220  48.990 39.171  1.00 7.47  ? 225 GLN B C   1 
ATOM   3719 O  O   . GLN B 1 247 ? 3.051  49.251 40.364  1.00 7.66  ? 225 GLN B O   1 
ATOM   3720 C  CB  . GLN B 1 247 ? 1.223  48.290 37.818  1.00 8.13  ? 225 GLN B CB  1 
ATOM   3721 C  CG  . GLN B 1 247 ? -0.072 48.730 37.139  1.00 8.52  ? 225 GLN B CG  1 
ATOM   3722 C  CD  . GLN B 1 247 ? 0.095  49.002 35.653  1.00 8.92  ? 225 GLN B CD  1 
ATOM   3723 O  OE1 . GLN B 1 247 ? 0.600  48.162 34.917  1.00 9.69  ? 225 GLN B OE1 1 
ATOM   3724 N  NE2 . GLN B 1 247 ? -0.337 50.172 35.207  1.00 9.21  ? 225 GLN B NE2 1 
ATOM   3725 N  N   . ALA B 1 248 ? 4.277  48.319 38.727  1.00 7.17  ? 226 ALA B N   1 
ATOM   3726 C  CA  . ALA B 1 248 ? 5.328  47.868 39.642  1.00 6.93  ? 226 ALA B CA  1 
ATOM   3727 C  C   . ALA B 1 248 ? 6.024  49.064 40.294  1.00 6.90  ? 226 ALA B C   1 
ATOM   3728 O  O   . ALA B 1 248 ? 6.318  49.046 41.483  1.00 6.78  ? 226 ALA B O   1 
ATOM   3729 C  CB  . ALA B 1 248 ? 6.331  46.985 38.925  1.00 6.98  ? 226 ALA B CB  1 
ATOM   3730 N  N   . LEU B 1 249 ? 6.254  50.112 39.511  1.00 6.87  ? 227 LEU B N   1 
ATOM   3731 C  CA  . LEU B 1 249 ? 6.877  51.331 40.026  1.00 6.90  ? 227 LEU B CA  1 
ATOM   3732 C  C   . LEU B 1 249 ? 5.985  52.034 41.044  1.00 7.20  ? 227 LEU B C   1 
ATOM   3733 O  O   . LEU B 1 249 ? 6.461  52.472 42.082  1.00 7.11  ? 227 LEU B O   1 
ATOM   3734 C  CB  . LEU B 1 249 ? 7.215  52.283 38.878  1.00 6.85  ? 227 LEU B CB  1 
ATOM   3735 C  CG  . LEU B 1 249 ? 8.376  51.848 37.985  1.00 6.82  ? 227 LEU B CG  1 
ATOM   3736 C  CD1 . LEU B 1 249 ? 8.493  52.762 36.776  1.00 6.82  ? 227 LEU B CD1 1 
ATOM   3737 C  CD2 . LEU B 1 249 ? 9.680  51.823 38.769  1.00 6.84  ? 227 LEU B CD2 1 
ATOM   3738 N  N   . GLU B 1 250 ? 4.691  52.137 40.747  1.00 7.44  ? 228 GLU B N   1 
ATOM   3739 C  CA  . GLU B 1 250 ? 3.745  52.756 41.680  1.00 7.90  ? 228 GLU B CA  1 
ATOM   3740 C  C   . GLU B 1 250 ? 3.637  51.933 42.967  1.00 7.98  ? 228 GLU B C   1 
ATOM   3741 O  O   . GLU B 1 250 ? 3.513  52.491 44.057  1.00 7.94  ? 228 GLU B O   1 
ATOM   3742 C  CB  . GLU B 1 250 ? 2.362  52.930 41.039  1.00 8.24  ? 228 GLU B CB  1 
ATOM   3743 C  CG  . GLU B 1 250 ? 2.292  53.987 39.942  1.00 8.72  ? 228 GLU B CG  1 
ATOM   3744 C  CD  . GLU B 1 250 ? 2.353  55.419 40.439  1.00 9.17  ? 228 GLU B CD  1 
ATOM   3745 O  OE1 . GLU B 1 250 ? 2.126  55.676 41.643  1.00 9.58  ? 228 GLU B OE1 1 
ATOM   3746 O  OE2 . GLU B 1 250 ? 2.624  56.311 39.605  1.00 9.84  ? 228 GLU B OE2 1 
ATOM   3747 N  N   . SER B 1 251 ? 3.685  50.608 42.842  1.00 8.06  ? 229 SER B N   1 
ATOM   3748 C  CA  . SER B 1 251 ? 3.667  49.734 44.021  1.00 8.46  ? 229 SER B CA  1 
ATOM   3749 C  C   . SER B 1 251 ? 4.892  49.955 44.901  1.00 7.98  ? 229 SER B C   1 
ATOM   3750 O  O   . SER B 1 251 ? 4.768  50.069 46.116  1.00 7.96  ? 229 SER B O   1 
ATOM   3751 C  CB  . SER B 1 251 ? 3.578  48.271 43.619  1.00 9.11  ? 229 SER B CB  1 
ATOM   3752 O  OG  . SER B 1 251 ? 2.329  48.020 43.016  1.00 10.70 ? 229 SER B OG  1 
ATOM   3753 N  N   . ALA B 1 252 ? 6.071  50.044 44.290  1.00 7.48  ? 230 ALA B N   1 
ATOM   3754 C  CA  . ALA B 1 252 ? 7.292  50.285 45.062  1.00 7.17  ? 230 ALA B CA  1 
ATOM   3755 C  C   . ALA B 1 252 ? 7.253  51.661 45.734  1.00 7.06  ? 230 ALA B C   1 
ATOM   3756 O  O   . ALA B 1 252 ? 7.721  51.821 46.859  1.00 6.71  ? 230 ALA B O   1 
ATOM   3757 C  CB  . ALA B 1 252 ? 8.524  50.142 44.178  1.00 7.13  ? 230 ALA B CB  1 
ATOM   3758 N  N   . LEU B 1 253 ? 6.672  52.640 45.048  1.00 6.99  ? 231 LEU B N   1 
ATOM   3759 C  CA  . LEU B 1 253 ? 6.528  53.987 45.597  1.00 7.05  ? 231 LEU B CA  1 
ATOM   3760 C  C   . LEU B 1 253 ? 5.599  53.989 46.817  1.00 7.28  ? 231 LEU B C   1 
ATOM   3761 O  O   . LEU B 1 253 ? 5.865  54.680 47.806  1.00 7.14  ? 231 LEU B O   1 
ATOM   3762 C  CB  . LEU B 1 253 ? 6.012  54.943 44.517  1.00 7.02  ? 231 LEU B CB  1 
ATOM   3763 C  CG  . LEU B 1 253 ? 5.849  56.415 44.905  1.00 7.10  ? 231 LEU B CG  1 
ATOM   3764 C  CD1 . LEU B 1 253 ? 7.180  57.030 45.305  1.00 7.22  ? 231 LEU B CD1 1 
ATOM   3765 C  CD2 . LEU B 1 253 ? 5.208  57.185 43.764  1.00 7.13  ? 231 LEU B CD2 1 
ATOM   3766 N  N   . GLU B 1 254 ? 4.525  53.204 46.755  1.00 7.65  ? 232 GLU B N   1 
ATOM   3767 C  CA  . GLU B 1 254 ? 3.595  53.110 47.886  1.00 8.10  ? 232 GLU B CA  1 
ATOM   3768 C  C   . GLU B 1 254 ? 4.230  52.389 49.073  1.00 7.50  ? 232 GLU B C   1 
ATOM   3769 O  O   . GLU B 1 254 ? 3.990  52.744 50.236  1.00 7.13  ? 232 GLU B O   1 
ATOM   3770 C  CB  . GLU B 1 254 ? 2.304  52.407 47.478  1.00 9.10  ? 232 GLU B CB  1 
ATOM   3771 C  CG  . GLU B 1 254 ? 1.119  52.757 48.369  1.00 10.30 ? 232 GLU B CG  1 
ATOM   3772 C  CD  . GLU B 1 254 ? 0.539  54.144 48.120  1.00 11.43 ? 232 GLU B CD  1 
ATOM   3773 O  OE1 . GLU B 1 254 ? 0.482  54.587 46.950  1.00 13.34 ? 232 GLU B OE1 1 
ATOM   3774 O  OE2 . GLU B 1 254 ? 0.089  54.783 49.098  1.00 12.50 ? 232 GLU B OE2 1 
ATOM   3775 N  N   . ILE B 1 255 ? 5.034  51.374 48.780  1.00 6.98  ? 233 ILE B N   1 
ATOM   3776 C  CA  . ILE B 1 255 ? 5.802  50.680 49.809  1.00 6.76  ? 233 ILE B CA  1 
ATOM   3777 C  C   . ILE B 1 255 ? 6.769  51.661 50.471  1.00 6.58  ? 233 ILE B C   1 
ATOM   3778 O  O   . ILE B 1 255 ? 6.906  51.665 51.699  1.00 6.47  ? 233 ILE B O   1 
ATOM   3779 C  CB  . ILE B 1 255 ? 6.533  49.447 49.226  1.00 6.83  ? 233 ILE B CB  1 
ATOM   3780 C  CG1 . ILE B 1 255 ? 5.508  48.359 48.882  1.00 6.93  ? 233 ILE B CG1 1 
ATOM   3781 C  CG2 . ILE B 1 255 ? 7.587  48.920 50.195  1.00 6.84  ? 233 ILE B CG2 1 
ATOM   3782 C  CD1 . ILE B 1 255 ? 6.079  47.176 48.127  1.00 7.01  ? 233 ILE B CD1 1 
ATOM   3783 N  N   . ASP B 1 256 ? 7.410  52.515 49.669  1.00 6.39  ? 234 ASP B N   1 
ATOM   3784 C  CA  . ASP B 1 256 ? 8.329  53.514 50.216  1.00 6.39  ? 234 ASP B CA  1 
ATOM   3785 C  C   . ASP B 1 256 ? 7.605  54.553 51.075  1.00 6.35  ? 234 ASP B C   1 
ATOM   3786 O  O   . ASP B 1 256 ? 8.159  55.049 52.063  1.00 6.29  ? 234 ASP B O   1 
ATOM   3787 C  CB  . ASP B 1 256 ? 9.131  54.218 49.112  1.00 6.44  ? 234 ASP B CB  1 
ATOM   3788 C  CG  . ASP B 1 256 ? 10.332 54.969 49.663  1.00 6.54  ? 234 ASP B CG  1 
ATOM   3789 O  OD1 . ASP B 1 256 ? 10.952 54.465 50.616  1.00 6.56  ? 234 ASP B OD1 1 
ATOM   3790 O  OD2 . ASP B 1 256 ? 10.650 56.062 49.150  1.00 6.64  ? 234 ASP B OD2 1 
ATOM   3791 N  N   . LEU B 1 257 ? 6.371  54.891 50.709  1.00 6.30  ? 235 LEU B N   1 
ATOM   3792 C  CA  . LEU B 1 257 ? 5.590  55.819 51.527  1.00 6.34  ? 235 LEU B CA  1 
ATOM   3793 C  C   . LEU B 1 257 ? 5.358  55.249 52.927  1.00 6.47  ? 235 LEU B C   1 
ATOM   3794 O  O   . LEU B 1 257 ? 5.449  55.977 53.915  1.00 6.61  ? 235 LEU B O   1 
ATOM   3795 C  CB  . LEU B 1 257 ? 4.261  56.165 50.853  1.00 6.30  ? 235 LEU B CB  1 
ATOM   3796 C  CG  . LEU B 1 257 ? 3.339  57.109 51.626  1.00 6.27  ? 235 LEU B CG  1 
ATOM   3797 C  CD1 . LEU B 1 257 ? 4.041  58.412 51.980  1.00 6.32  ? 235 LEU B CD1 1 
ATOM   3798 C  CD2 . LEU B 1 257 ? 2.083  57.374 50.816  1.00 6.26  ? 235 LEU B CD2 1 
ATOM   3799 N  N   . ALA B 1 258 ? 5.065  53.955 53.020  1.00 6.63  ? 236 ALA B N   1 
ATOM   3800 C  CA  . ALA B 1 258 ? 4.960  53.297 54.331  1.00 6.76  ? 236 ALA B CA  1 
ATOM   3801 C  C   . ALA B 1 258 ? 6.294  53.309 55.090  1.00 6.90  ? 236 ALA B C   1 
ATOM   3802 O  O   . ALA B 1 258 ? 6.328  53.596 56.288  1.00 6.84  ? 236 ALA B O   1 
ATOM   3803 C  CB  . ALA B 1 258 ? 4.446  51.874 54.185  1.00 6.83  ? 236 ALA B CB  1 
ATOM   3804 N  N   . ILE B 1 259 ? 7.384  52.998 54.393  1.00 7.08  ? 237 ILE B N   1 
ATOM   3805 C  CA  . ILE B 1 259 ? 8.709  52.988 55.016  1.00 7.33  ? 237 ILE B CA  1 
ATOM   3806 C  C   . ILE B 1 259 ? 9.039  54.360 55.602  1.00 7.61  ? 237 ILE B C   1 
ATOM   3807 O  O   . ILE B 1 259 ? 9.426  54.469 56.768  1.00 7.55  ? 237 ILE B O   1 
ATOM   3808 C  CB  . ILE B 1 259 ? 9.807  52.571 54.011  1.00 7.40  ? 237 ILE B CB  1 
ATOM   3809 C  CG1 . ILE B 1 259 ? 9.665  51.088 53.650  1.00 7.45  ? 237 ILE B CG1 1 
ATOM   3810 C  CG2 . ILE B 1 259 ? 11.197 52.831 54.586  1.00 7.38  ? 237 ILE B CG2 1 
ATOM   3811 C  CD1 . ILE B 1 259 ? 10.462 50.671 52.430  1.00 7.52  ? 237 ILE B CD1 1 
ATOM   3812 N  N   . GLU B 1 260 ? 8.895  55.402 54.790  1.00 7.93  ? 238 GLU B N   1 
ATOM   3813 C  CA  . GLU B 1 260 ? 9.297  56.744 55.210  1.00 8.21  ? 238 GLU B CA  1 
ATOM   3814 C  C   . GLU B 1 260 ? 8.266  57.371 56.143  1.00 8.47  ? 238 GLU B C   1 
ATOM   3815 O  O   . GLU B 1 260 ? 8.623  58.146 57.037  1.00 8.58  ? 238 GLU B O   1 
ATOM   3816 C  CB  . GLU B 1 260 ? 9.537  57.649 54.003  1.00 8.22  ? 238 GLU B CB  1 
ATOM   3817 C  CG  . GLU B 1 260 ? 10.607 57.161 53.031  1.00 8.26  ? 238 GLU B CG  1 
ATOM   3818 C  CD  . GLU B 1 260 ? 12.014 57.200 53.596  1.00 8.44  ? 238 GLU B CD  1 
ATOM   3819 O  OE1 . GLU B 1 260 ? 12.214 57.666 54.745  1.00 8.72  ? 238 GLU B OE1 1 
ATOM   3820 O  OE2 . GLU B 1 260 ? 12.941 56.776 52.875  1.00 8.49  ? 238 GLU B OE2 1 
ATOM   3821 N  N   . GLY B 1 261 ? 6.995  57.023 55.957  1.00 8.78  ? 239 GLY B N   1 
ATOM   3822 C  CA  . GLY B 1 261 ? 5.930  57.518 56.828  1.00 9.10  ? 239 GLY B CA  1 
ATOM   3823 C  C   . GLY B 1 261 ? 6.101  57.038 58.256  1.00 9.44  ? 239 GLY B C   1 
ATOM   3824 O  O   . GLY B 1 261 ? 5.854  57.793 59.200  1.00 9.92  ? 239 GLY B O   1 
ATOM   3825 N  N   . ALA B 1 262 ? 6.525  55.785 58.413  1.00 9.53  ? 240 ALA B N   1 
ATOM   3826 C  CA  . ALA B 1 262 ? 6.870  55.229 59.724  1.00 9.73  ? 240 ALA B CA  1 
ATOM   3827 C  C   . ALA B 1 262 ? 8.186  55.822 60.211  1.00 10.02 ? 240 ALA B C   1 
ATOM   3828 O  O   . ALA B 1 262 ? 8.306  56.224 61.382  1.00 10.07 ? 240 ALA B O   1 
ATOM   3829 C  CB  . ALA B 1 262 ? 6.980  53.709 59.653  1.00 9.71  ? 240 ALA B CB  1 
ATOM   3830 N  N   . GLY B 1 263 ? 9.163  55.860 59.303  1.00 10.12 ? 241 GLY B N   1 
ATOM   3831 C  CA  . GLY B 1 263 ? 10.523 56.298 59.601  1.00 10.41 ? 241 GLY B CA  1 
ATOM   3832 C  C   . GLY B 1 263 ? 11.349 55.144 60.131  1.00 10.62 ? 241 GLY B C   1 
ATOM   3833 O  O   . GLY B 1 263 ? 11.097 54.648 61.232  1.00 10.87 ? 241 GLY B O   1 
ATOM   3834 N  N   . SER B 1 264 ? 12.335 54.696 59.356  1.00 10.72 ? 242 SER B N   1 
ATOM   3835 C  CA  . SER B 1 264 ? 13.207 53.621 59.805  1.00 11.04 ? 242 SER B CA  1 
ATOM   3836 C  C   . SER B 1 264 ? 14.062 54.113 60.970  1.00 11.01 ? 242 SER B C   1 
ATOM   3837 O  O   . SER B 1 264 ? 14.581 55.227 60.913  1.00 11.04 ? 242 SER B O   1 
ATOM   3838 C  CB  . SER B 1 264 ? 14.139 53.160 58.686  1.00 11.25 ? 242 SER B CB  1 
ATOM   3839 O  OG  . SER B 1 264 ? 15.030 52.165 59.159  1.00 11.89 ? 242 SER B OG  1 
ATOM   3840 N  N   . PRO B 1 265 ? 14.231 53.281 62.014  1.00 11.17 ? 243 PRO B N   1 
ATOM   3841 C  CA  . PRO B 1 265 ? 15.158 53.671 63.080  1.00 11.22 ? 243 PRO B CA  1 
ATOM   3842 C  C   . PRO B 1 265 ? 16.575 53.922 62.570  1.00 11.12 ? 243 PRO B C   1 
ATOM   3843 O  O   . PRO B 1 265 ? 17.293 54.721 63.155  1.00 11.23 ? 243 PRO B O   1 
ATOM   3844 C  CB  . PRO B 1 265 ? 15.129 52.477 64.041  1.00 11.36 ? 243 PRO B CB  1 
ATOM   3845 C  CG  . PRO B 1 265 ? 14.559 51.347 63.265  1.00 11.55 ? 243 PRO B CG  1 
ATOM   3846 C  CD  . PRO B 1 265 ? 13.626 51.964 62.273  1.00 11.38 ? 243 PRO B CD  1 
ATOM   3847 N  N   . ASP B 1 266 ? 16.963 53.265 61.478  1.00 10.98 ? 244 ASP B N   1 
ATOM   3848 C  CA  . ASP B 1 266 ? 18.275 53.506 60.869  1.00 11.10 ? 244 ASP B CA  1 
ATOM   3849 C  C   . ASP B 1 266 ? 18.423 54.946 60.382  1.00 11.05 ? 244 ASP B C   1 
ATOM   3850 O  O   . ASP B 1 266 ? 19.489 55.547 60.525  1.00 11.17 ? 244 ASP B O   1 
ATOM   3851 C  CB  . ASP B 1 266 ? 18.526 52.553 59.693  1.00 11.21 ? 244 ASP B CB  1 
ATOM   3852 C  CG  . ASP B 1 266 ? 18.660 51.098 60.116  1.00 11.35 ? 244 ASP B CG  1 
ATOM   3853 O  OD1 . ASP B 1 266 ? 18.569 50.780 61.321  1.00 11.57 ? 244 ASP B OD1 1 
ATOM   3854 O  OD2 . ASP B 1 266 ? 18.855 50.252 59.219  1.00 11.29 ? 244 ASP B OD2 1 
ATOM   3855 N  N   . LYS B 1 267 ? 17.361 55.493 59.795  1.00 11.11 ? 245 LYS B N   1 
ATOM   3856 C  CA  . LYS B 1 267 ? 17.386 56.864 59.298  1.00 11.24 ? 245 LYS B CA  1 
ATOM   3857 C  C   . LYS B 1 267 ? 17.311 57.849 60.460  1.00 11.60 ? 245 LYS B C   1 
ATOM   3858 O  O   . LYS B 1 267 ? 18.045 58.838 60.494  1.00 11.69 ? 245 LYS B O   1 
ATOM   3859 C  CB  . LYS B 1 267 ? 16.238 57.123 58.321  1.00 11.18 ? 245 LYS B CB  1 
ATOM   3860 C  CG  . LYS B 1 267 ? 16.152 58.573 57.878  1.00 11.16 ? 245 LYS B CG  1 
ATOM   3861 C  CD  . LYS B 1 267 ? 15.081 58.808 56.832  1.00 11.09 ? 245 LYS B CD  1 
ATOM   3862 C  CE  . LYS B 1 267 ? 15.585 58.510 55.431  1.00 11.14 ? 245 LYS B CE  1 
ATOM   3863 N  NZ  . LYS B 1 267 ? 14.646 59.023 54.395  1.00 11.09 ? 245 LYS B NZ  1 
ATOM   3864 N  N   . ILE B 1 268 ? 16.432 57.567 61.413  1.00 12.07 ? 246 ILE B N   1 
ATOM   3865 C  CA  . ILE B 1 268 ? 16.282 58.427 62.589  1.00 12.72 ? 246 ILE B CA  1 
ATOM   3866 C  C   . ILE B 1 268 ? 17.631 58.555 63.298  1.00 12.91 ? 246 ILE B C   1 
ATOM   3867 O  O   . ILE B 1 268 ? 18.045 59.660 63.652  1.00 13.01 ? 246 ILE B O   1 
ATOM   3868 C  CB  . ILE B 1 268 ? 15.199 57.901 63.554  1.00 13.00 ? 246 ILE B CB  1 
ATOM   3869 C  CG1 . ILE B 1 268 ? 13.817 58.027 62.909  1.00 13.15 ? 246 ILE B CG1 1 
ATOM   3870 C  CG2 . ILE B 1 268 ? 15.226 58.677 64.870  1.00 13.22 ? 246 ILE B CG2 1 
ATOM   3871 C  CD1 . ILE B 1 268 ? 12.751 57.168 63.552  1.00 13.36 ? 246 ILE B CD1 1 
ATOM   3872 N  N   . ALA B 1 269 ? 18.318 57.430 63.469  1.00 13.27 ? 247 ALA B N   1 
ATOM   3873 C  CA  . ALA B 1 269 ? 19.649 57.409 64.079  1.00 13.61 ? 247 ALA B CA  1 
ATOM   3874 C  C   . ALA B 1 269 ? 20.681 58.181 63.252  1.00 14.07 ? 247 ALA B C   1 
ATOM   3875 O  O   . ALA B 1 269 ? 21.517 58.908 63.804  1.00 14.27 ? 247 ALA B O   1 
ATOM   3876 C  CB  . ALA B 1 269 ? 20.104 55.974 64.283  1.00 13.71 ? 247 ALA B CB  1 
ATOM   3877 N  N   . PHE B 1 270 ? 20.632 58.016 61.932  1.00 13.91 ? 248 PHE B N   1 
ATOM   3878 C  CA  . PHE B 1 270 ? 21.545 58.723 61.037  1.00 14.27 ? 248 PHE B CA  1 
ATOM   3879 C  C   . PHE B 1 270 ? 21.423 60.238 61.207  1.00 14.86 ? 248 PHE B C   1 
ATOM   3880 O  O   . PHE B 1 270 ? 22.431 60.933 61.344  1.00 15.22 ? 248 PHE B O   1 
ATOM   3881 C  CB  . PHE B 1 270 ? 21.286 58.335 59.577  1.00 14.14 ? 248 PHE B CB  1 
ATOM   3882 C  CG  . PHE B 1 270 ? 22.111 59.110 58.589  1.00 13.93 ? 248 PHE B CG  1 
ATOM   3883 C  CD1 . PHE B 1 270 ? 23.402 58.715 58.289  1.00 13.98 ? 248 PHE B CD1 1 
ATOM   3884 C  CD2 . PHE B 1 270 ? 21.596 60.245 57.967  1.00 14.07 ? 248 PHE B CD2 1 
ATOM   3885 C  CE1 . PHE B 1 270 ? 24.166 59.428 57.383  1.00 13.95 ? 248 PHE B CE1 1 
ATOM   3886 C  CE2 . PHE B 1 270 ? 22.358 60.962 57.062  1.00 14.07 ? 248 PHE B CE2 1 
ATOM   3887 C  CZ  . PHE B 1 270 ? 23.645 60.549 56.768  1.00 13.98 ? 248 PHE B CZ  1 
ATOM   3888 N  N   . PHE B 1 271 ? 20.195 60.748 61.209  1.00 15.37 ? 249 PHE B N   1 
ATOM   3889 C  CA  . PHE B 1 271 ? 19.988 62.195 61.310  1.00 16.02 ? 249 PHE B CA  1 
ATOM   3890 C  C   . PHE B 1 271 ? 20.248 62.729 62.719  1.00 17.29 ? 249 PHE B C   1 
ATOM   3891 O  O   . PHE B 1 271 ? 20.570 63.911 62.879  1.00 17.68 ? 249 PHE B O   1 
ATOM   3892 C  CB  . PHE B 1 271 ? 18.599 62.599 60.805  1.00 15.81 ? 249 PHE B CB  1 
ATOM   3893 C  CG  . PHE B 1 271 ? 18.489 62.603 59.307  1.00 15.58 ? 249 PHE B CG  1 
ATOM   3894 C  CD1 . PHE B 1 271 ? 19.274 63.461 58.545  1.00 15.57 ? 249 PHE B CD1 1 
ATOM   3895 C  CD2 . PHE B 1 271 ? 17.620 61.744 58.654  1.00 15.47 ? 249 PHE B CD2 1 
ATOM   3896 C  CE1 . PHE B 1 271 ? 19.192 63.463 57.161  1.00 15.57 ? 249 PHE B CE1 1 
ATOM   3897 C  CE2 . PHE B 1 271 ? 17.536 61.742 57.271  1.00 15.42 ? 249 PHE B CE2 1 
ATOM   3898 C  CZ  . PHE B 1 271 ? 18.321 62.603 56.523  1.00 15.36 ? 249 PHE B CZ  1 
ATOM   3899 N  N   . GLU B 1 272 ? 20.131 61.868 63.728  1.00 18.57 ? 250 GLU B N   1 
ATOM   3900 C  CA  . GLU B 1 272 ? 20.501 62.248 65.100  1.00 20.05 ? 250 GLU B CA  1 
ATOM   3901 C  C   . GLU B 1 272 ? 21.985 62.583 65.170  1.00 20.44 ? 250 GLU B C   1 
ATOM   3902 O  O   . GLU B 1 272 ? 22.371 63.578 65.783  1.00 21.07 ? 250 GLU B O   1 
ATOM   3903 C  CB  . GLU B 1 272 ? 20.156 61.146 66.104  1.00 21.62 ? 250 GLU B CB  1 
ATOM   3904 C  CG  . GLU B 1 272 ? 18.713 61.186 66.579  1.00 23.32 ? 250 GLU B CG  1 
ATOM   3905 C  CD  . GLU B 1 272 ? 18.357 60.039 67.505  1.00 24.85 ? 250 GLU B CD  1 
ATOM   3906 O  OE1 . GLU B 1 272 ? 19.273 59.291 67.916  1.00 26.93 ? 250 GLU B OE1 1 
ATOM   3907 O  OE2 . GLU B 1 272 ? 17.155 59.882 67.823  1.00 26.53 ? 250 GLU B OE2 1 
ATOM   3908 N  N   . VAL B 1 273 ? 22.810 61.761 64.529  1.00 20.10 ? 251 VAL B N   1 
ATOM   3909 C  CA  . VAL B 1 273 ? 24.244 62.037 64.431  1.00 20.34 ? 251 VAL B CA  1 
ATOM   3910 C  C   . VAL B 1 273 ? 24.492 63.265 63.548  1.00 20.76 ? 251 VAL B C   1 
ATOM   3911 O  O   . VAL B 1 273 ? 25.321 64.114 63.881  1.00 21.27 ? 251 VAL B O   1 
ATOM   3912 C  CB  . VAL B 1 273 ? 25.032 60.828 63.874  1.00 19.99 ? 251 VAL B CB  1 
ATOM   3913 C  CG1 . VAL B 1 273 ? 26.510 61.171 63.737  1.00 19.98 ? 251 VAL B CG1 1 
ATOM   3914 C  CG2 . VAL B 1 273 ? 24.857 59.608 64.768  1.00 19.92 ? 251 VAL B CG2 1 
ATOM   3915 N  N   . ALA B 1 274 ? 23.768 63.360 62.433  1.00 21.06 ? 252 ALA B N   1 
ATOM   3916 C  CA  . ALA B 1 274 ? 23.960 64.452 61.475  1.00 21.59 ? 252 ALA B CA  1 
ATOM   3917 C  C   . ALA B 1 274 ? 23.673 65.833 62.072  1.00 22.50 ? 252 ALA B C   1 
ATOM   3918 O  O   . ALA B 1 274 ? 24.418 66.783 61.819  1.00 22.44 ? 252 ALA B O   1 
ATOM   3919 C  CB  . ALA B 1 274 ? 23.106 64.233 60.232  1.00 21.70 ? 252 ALA B CB  1 
ATOM   3920 N  N   . ARG B 1 275 ? 22.595 65.941 62.847  1.00 23.12 ? 253 ARG B N   1 
ATOM   3921 C  CA  . ARG B 1 275 ? 22.225 67.208 63.489  1.00 24.57 ? 253 ARG B CA  1 
ATOM   3922 C  C   . ARG B 1 275 ? 23.225 67.607 64.574  1.00 25.91 ? 253 ARG B C   1 
ATOM   3923 O  O   . ARG B 1 275 ? 23.446 68.797 64.813  1.00 26.14 ? 253 ARG B O   1 
ATOM   3924 C  CB  . ARG B 1 275 ? 20.819 67.129 64.092  1.00 24.72 ? 253 ARG B CB  1 
ATOM   3925 C  CG  . ARG B 1 275 ? 19.695 67.124 63.065  1.00 24.59 ? 253 ARG B CG  1 
ATOM   3926 C  CD  . ARG B 1 275 ? 18.343 67.380 63.710  1.00 24.78 ? 253 ARG B CD  1 
ATOM   3927 N  NE  . ARG B 1 275 ? 18.084 66.486 64.840  1.00 25.27 ? 253 ARG B NE  1 
ATOM   3928 C  CZ  . ARG B 1 275 ? 17.591 65.249 64.753  1.00 25.41 ? 253 ARG B CZ  1 
ATOM   3929 N  NH1 . ARG B 1 275 ? 17.278 64.713 63.576  1.00 24.78 ? 253 ARG B NH1 1 
ATOM   3930 N  NH2 . ARG B 1 275 ? 17.407 64.539 65.863  1.00 25.61 ? 253 ARG B NH2 1 
ATOM   3931 N  N   . ARG B 1 276 ? 23.823 66.607 65.215  1.00 27.39 ? 254 ARG B N   1 
ATOM   3932 C  CA  . ARG B 1 276 ? 24.756 66.812 66.318  1.00 29.19 ? 254 ARG B CA  1 
ATOM   3933 C  C   . ARG B 1 276 ? 26.178 67.088 65.820  1.00 29.35 ? 254 ARG B C   1 
ATOM   3934 O  O   . ARG B 1 276 ? 26.784 68.096 66.192  1.00 29.97 ? 254 ARG B O   1 
ATOM   3935 C  CB  . ARG B 1 276 ? 24.752 65.572 67.216  1.00 30.56 ? 254 ARG B CB  1 
ATOM   3936 C  CG  . ARG B 1 276 ? 25.505 65.707 68.532  1.00 32.07 ? 254 ARG B CG  1 
ATOM   3937 C  CD  . ARG B 1 276 ? 25.855 64.333 69.077  1.00 33.39 ? 254 ARG B CD  1 
ATOM   3938 N  NE  . ARG B 1 276 ? 24.667 63.485 69.181  1.00 35.19 ? 254 ARG B NE  1 
ATOM   3939 C  CZ  . ARG B 1 276 ? 24.670 62.152 69.188  1.00 36.53 ? 254 ARG B CZ  1 
ATOM   3940 N  NH1 . ARG B 1 276 ? 25.803 61.463 69.092  1.00 37.25 ? 254 ARG B NH1 1 
ATOM   3941 N  NH2 . ARG B 1 276 ? 23.518 61.497 69.287  1.00 37.62 ? 254 ARG B NH2 1 
ATOM   3942 N  N   . ASP B 1 277 ? 26.703 66.190 64.986  1.00 29.21 ? 255 ASP B N   1 
ATOM   3943 C  CA  . ASP B 1 277 ? 28.111 66.236 64.561  1.00 28.67 ? 255 ASP B CA  1 
ATOM   3944 C  C   . ASP B 1 277 ? 28.317 66.558 63.077  1.00 27.75 ? 255 ASP B C   1 
ATOM   3945 O  O   . ASP B 1 277 ? 29.457 66.654 62.623  1.00 27.50 ? 255 ASP B O   1 
ATOM   3946 C  CB  . ASP B 1 277 ? 28.797 64.901 64.873  1.00 29.30 ? 255 ASP B CB  1 
ATOM   3947 C  CG  . ASP B 1 277 ? 28.700 64.513 66.340  1.00 30.27 ? 255 ASP B CG  1 
ATOM   3948 O  OD1 . ASP B 1 277 ? 28.525 65.402 67.199  1.00 30.90 ? 255 ASP B OD1 1 
ATOM   3949 O  OD2 . ASP B 1 277 ? 28.809 63.306 66.635  1.00 31.51 ? 255 ASP B OD2 1 
ATOM   3950 N  N   . GLY B 1 278 ? 27.230 66.720 62.325  1.00 26.44 ? 256 GLY B N   1 
ATOM   3951 C  CA  . GLY B 1 278 ? 27.314 67.019 60.898  1.00 25.93 ? 256 GLY B CA  1 
ATOM   3952 C  C   . GLY B 1 278 ? 27.164 65.778 60.035  1.00 25.54 ? 256 GLY B C   1 
ATOM   3953 O  O   . GLY B 1 278 ? 27.405 64.659 60.494  1.00 24.54 ? 256 GLY B O   1 
ATOM   3954 N  N   . LEU B 1 279 ? 26.777 65.993 58.778  1.00 25.58 ? 257 LEU B N   1 
ATOM   3955 C  CA  . LEU B 1 279 ? 26.537 64.906 57.817  1.00 25.50 ? 257 LEU B CA  1 
ATOM   3956 C  C   . LEU B 1 279 ? 27.783 64.061 57.560  1.00 25.69 ? 257 LEU B C   1 
ATOM   3957 O  O   . LEU B 1 279 ? 27.709 62.839 57.478  1.00 25.05 ? 257 LEU B O   1 
ATOM   3958 C  CB  . LEU B 1 279 ? 26.017 65.475 56.490  1.00 25.28 ? 257 LEU B CB  1 
ATOM   3959 C  CG  . LEU B 1 279 ? 24.550 65.911 56.486  1.00 25.55 ? 257 LEU B CG  1 
ATOM   3960 C  CD1 . LEU B 1 279 ? 24.251 66.814 55.298  1.00 25.53 ? 257 LEU B CD1 1 
ATOM   3961 C  CD2 . LEU B 1 279 ? 23.628 64.699 56.483  1.00 25.45 ? 257 LEU B CD2 1 
ATOM   3962 N  N   . ARG B 1 280 ? 28.916 64.734 57.395  1.00 26.38 ? 258 ARG B N   1 
ATOM   3963 C  CA  . ARG B 1 280 ? 30.230 64.096 57.326  1.00 26.87 ? 258 ARG B CA  1 
ATOM   3964 C  C   . ARG B 1 280 ? 30.431 63.023 58.408  1.00 25.80 ? 258 ARG B C   1 
ATOM   3965 O  O   . ARG B 1 280 ? 30.793 61.886 58.097  1.00 25.67 ? 258 ARG B O   1 
ATOM   3966 C  CB  . ARG B 1 280 ? 31.350 65.166 57.357  1.00 28.37 ? 258 ARG B CB  1 
ATOM   3967 C  CG  . ARG B 1 280 ? 31.654 65.857 58.696  1.00 29.73 ? 258 ARG B CG  1 
ATOM   3968 C  CD  . ARG B 1 280 ? 30.486 66.598 59.356  1.00 30.24 ? 258 ARG B CD  1 
ATOM   3969 N  NE  . ARG B 1 280 ? 30.471 68.052 59.130  1.00 31.67 ? 258 ARG B NE  1 
ATOM   3970 C  CZ  . ARG B 1 280 ? 29.790 68.697 58.177  1.00 32.57 ? 258 ARG B CZ  1 
ATOM   3971 N  NH1 . ARG B 1 280 ? 29.043 68.054 57.288  1.00 32.81 ? 258 ARG B NH1 1 
ATOM   3972 N  NH2 . ARG B 1 280 ? 29.868 70.022 58.100  1.00 34.19 ? 258 ARG B NH2 1 
ATOM   3973 N  N   . ALA B 1 281 ? 30.161 63.373 59.663  1.00 24.49 ? 259 ALA B N   1 
ATOM   3974 C  CA  . ALA B 1 281 ? 30.311 62.442 60.780  1.00 23.53 ? 259 ALA B CA  1 
ATOM   3975 C  C   . ALA B 1 281 ? 29.236 61.354 60.735  1.00 22.54 ? 259 ALA B C   1 
ATOM   3976 O  O   . ALA B 1 281 ? 29.489 60.212 61.114  1.00 22.81 ? 259 ALA B O   1 
ATOM   3977 C  CB  . ALA B 1 281 ? 30.244 63.188 62.103  1.00 23.75 ? 259 ALA B CB  1 
ATOM   3978 N  N   . ALA B 1 282 ? 28.040 61.722 60.279  1.00 21.44 ? 260 ALA B N   1 
ATOM   3979 C  CA  . ALA B 1 282 ? 26.925 60.778 60.164  1.00 20.47 ? 260 ALA B CA  1 
ATOM   3980 C  C   . ALA B 1 282 ? 27.225 59.681 59.145  1.00 20.17 ? 260 ALA B C   1 
ATOM   3981 O  O   . ALA B 1 282 ? 26.891 58.519 59.364  1.00 19.38 ? 260 ALA B O   1 
ATOM   3982 C  CB  . ALA B 1 282 ? 25.640 61.513 59.797  1.00 20.39 ? 260 ALA B CB  1 
ATOM   3983 N  N   . ILE B 1 283 ? 27.861 60.060 58.038  1.00 20.24 ? 261 ILE B N   1 
ATOM   3984 C  CA  . ILE B 1 283 ? 28.284 59.096 57.017  1.00 20.58 ? 261 ILE B CA  1 
ATOM   3985 C  C   . ILE B 1 283 ? 29.381 58.174 57.560  1.00 20.42 ? 261 ILE B C   1 
ATOM   3986 O  O   . ILE B 1 283 ? 29.397 56.979 57.260  1.00 20.02 ? 261 ILE B O   1 
ATOM   3987 C  CB  . ILE B 1 283 ? 28.743 59.808 55.724  1.00 21.15 ? 261 ILE B CB  1 
ATOM   3988 C  CG1 . ILE B 1 283 ? 27.536 60.461 55.035  1.00 21.52 ? 261 ILE B CG1 1 
ATOM   3989 C  CG2 . ILE B 1 283 ? 29.429 58.826 54.776  1.00 21.32 ? 261 ILE B CG2 1 
ATOM   3990 C  CD1 . ILE B 1 283 ? 27.894 61.427 53.925  1.00 21.80 ? 261 ILE B CD1 1 
ATOM   3991 N  N   . ALA B 1 284 ? 30.293 58.723 58.363  1.00 19.98 ? 262 ALA B N   1 
ATOM   3992 C  CA  . ALA B 1 284 ? 31.312 57.909 59.028  1.00 19.68 ? 262 ALA B CA  1 
ATOM   3993 C  C   . ALA B 1 284 ? 30.683 56.924 60.019  1.00 19.36 ? 262 ALA B C   1 
ATOM   3994 O  O   . ALA B 1 284 ? 31.082 55.766 60.083  1.00 19.33 ? 262 ALA B O   1 
ATOM   3995 C  CB  . ALA B 1 284 ? 32.323 58.801 59.738  1.00 19.87 ? 262 ALA B CB  1 
ATOM   3996 N  N   . TRP B 1 285 ? 29.704 57.400 60.788  1.00 18.87 ? 263 TRP B N   1 
ATOM   3997 C  CA  . TRP B 1 285 ? 28.925 56.550 61.693  1.00 18.66 ? 263 TRP B CA  1 
ATOM   3998 C  C   . TRP B 1 285 ? 28.206 55.448 60.909  1.00 18.22 ? 263 TRP B C   1 
ATOM   3999 O  O   . TRP B 1 285 ? 28.200 54.281 61.308  1.00 18.45 ? 263 TRP B O   1 
ATOM   4000 C  CB  . TRP B 1 285 ? 27.913 57.405 62.467  1.00 18.73 ? 263 TRP B CB  1 
ATOM   4001 C  CG  . TRP B 1 285 ? 26.876 56.631 63.226  1.00 19.12 ? 263 TRP B CG  1 
ATOM   4002 C  CD1 . TRP B 1 285 ? 26.961 56.187 64.513  1.00 19.47 ? 263 TRP B CD1 1 
ATOM   4003 C  CD2 . TRP B 1 285 ? 25.587 56.225 62.747  1.00 19.12 ? 263 TRP B CD2 1 
ATOM   4004 N  NE1 . TRP B 1 285 ? 25.809 55.526 64.865  1.00 19.64 ? 263 TRP B NE1 1 
ATOM   4005 C  CE2 . TRP B 1 285 ? 24.950 55.533 63.798  1.00 19.13 ? 263 TRP B CE2 1 
ATOM   4006 C  CE3 . TRP B 1 285 ? 24.912 56.378 61.532  1.00 19.03 ? 263 TRP B CE3 1 
ATOM   4007 C  CZ2 . TRP B 1 285 ? 23.668 54.993 63.672  1.00 19.03 ? 263 TRP B CZ2 1 
ATOM   4008 C  CZ3 . TRP B 1 285 ? 23.638 55.836 61.403  1.00 18.83 ? 263 TRP B CZ3 1 
ATOM   4009 C  CH2 . TRP B 1 285 ? 23.030 55.153 62.469  1.00 19.14 ? 263 TRP B CH2 1 
ATOM   4010 N  N   . ARG B 1 286 ? 27.617 55.833 59.785  1.00 17.72 ? 264 ARG B N   1 
ATOM   4011 C  CA  . ARG B 1 286 ? 26.902 54.892 58.921  1.00 17.42 ? 264 ARG B CA  1 
ATOM   4012 C  C   . ARG B 1 286 ? 27.823 53.784 58.416  1.00 17.40 ? 264 ARG B C   1 
ATOM   4013 O  O   . ARG B 1 286 ? 27.507 52.600 58.537  1.00 16.99 ? 264 ARG B O   1 
ATOM   4014 C  CB  . ARG B 1 286 ? 26.300 55.638 57.735  1.00 17.44 ? 264 ARG B CB  1 
ATOM   4015 C  CG  . ARG B 1 286 ? 25.475 54.774 56.795  1.00 17.62 ? 264 ARG B CG  1 
ATOM   4016 C  CD  . ARG B 1 286 ? 25.314 55.449 55.447  1.00 17.65 ? 264 ARG B CD  1 
ATOM   4017 N  NE  . ARG B 1 286 ? 26.565 55.455 54.694  1.00 17.90 ? 264 ARG B NE  1 
ATOM   4018 C  CZ  . ARG B 1 286 ? 26.677 55.776 53.408  1.00 18.25 ? 264 ARG B CZ  1 
ATOM   4019 N  NH1 . ARG B 1 286 ? 25.608 56.122 52.698  1.00 18.58 ? 264 ARG B NH1 1 
ATOM   4020 N  NH2 . ARG B 1 286 ? 27.866 55.735 52.822  1.00 18.45 ? 264 ARG B NH2 1 
ATOM   4021 N  N   . ASP B 1 287 ? 28.961 54.173 57.851  1.00 17.37 ? 265 ASP B N   1 
ATOM   4022 C  CA  . ASP B 1 287 ? 29.901 53.211 57.275  1.00 17.40 ? 265 ASP B CA  1 
ATOM   4023 C  C   . ASP B 1 287 ? 30.440 52.221 58.313  1.00 17.04 ? 265 ASP B C   1 
ATOM   4024 O  O   . ASP B 1 287 ? 30.670 51.055 57.995  1.00 16.79 ? 265 ASP B O   1 
ATOM   4025 C  CB  . ASP B 1 287 ? 31.061 53.937 56.580  1.00 17.90 ? 265 ASP B CB  1 
ATOM   4026 C  CG  . ASP B 1 287 ? 30.609 54.762 55.385  1.00 18.54 ? 265 ASP B CG  1 
ATOM   4027 O  OD1 . ASP B 1 287 ? 29.467 54.570 54.904  1.00 19.07 ? 265 ASP B OD1 1 
ATOM   4028 O  OD2 . ASP B 1 287 ? 31.397 55.612 54.919  1.00 18.90 ? 265 ASP B OD2 1 
ATOM   4029 N  N   . ALA B 1 288 ? 30.618 52.678 59.551  1.00 16.76 ? 266 ALA B N   1 
ATOM   4030 C  CA  . ALA B 1 288 ? 31.111 51.819 60.634  1.00 16.83 ? 266 ALA B CA  1 
ATOM   4031 C  C   . ALA B 1 288 ? 30.135 50.700 61.025  1.00 16.64 ? 266 ALA B C   1 
ATOM   4032 O  O   . ALA B 1 288 ? 30.528 49.730 61.668  1.00 16.71 ? 266 ALA B O   1 
ATOM   4033 C  CB  . ALA B 1 288 ? 31.456 52.660 61.856  1.00 16.94 ? 266 ALA B CB  1 
ATOM   4034 N  N   . ARG B 1 289 ? 28.866 50.833 60.643  1.00 16.42 ? 267 ARG B N   1 
ATOM   4035 C  CA  . ARG B 1 289 ? 27.876 49.787 60.901  1.00 16.39 ? 267 ARG B CA  1 
ATOM   4036 C  C   . ARG B 1 289 ? 28.054 48.560 60.002  1.00 16.12 ? 267 ARG B C   1 
ATOM   4037 O  O   . ARG B 1 289 ? 27.553 47.484 60.321  1.00 16.03 ? 267 ARG B O   1 
ATOM   4038 C  CB  . ARG B 1 289 ? 26.457 50.327 60.712  1.00 16.49 ? 267 ARG B CB  1 
ATOM   4039 C  CG  . ARG B 1 289 ? 26.056 51.448 61.666  1.00 16.59 ? 267 ARG B CG  1 
ATOM   4040 C  CD  . ARG B 1 289 ? 24.788 52.137 61.180  1.00 16.90 ? 267 ARG B CD  1 
ATOM   4041 N  NE  . ARG B 1 289 ? 23.766 51.147 60.848  1.00 17.30 ? 267 ARG B NE  1 
ATOM   4042 C  CZ  . ARG B 1 289 ? 22.873 51.245 59.863  1.00 17.50 ? 267 ARG B CZ  1 
ATOM   4043 N  NH1 . ARG B 1 289 ? 22.823 52.313 59.070  1.00 17.81 ? 267 ARG B NH1 1 
ATOM   4044 N  NH2 . ARG B 1 289 ? 22.016 50.250 59.669  1.00 17.88 ? 267 ARG B NH2 1 
ATOM   4045 N  N   . PHE B 1 290 ? 28.749 48.732 58.877  1.00 16.04 ? 268 PHE B N   1 
ATOM   4046 C  CA  . PHE B 1 290 ? 28.878 47.684 57.867  1.00 16.02 ? 268 PHE B CA  1 
ATOM   4047 C  C   . PHE B 1 290 ? 30.309 47.164 57.780  1.00 17.19 ? 268 PHE B C   1 
ATOM   4048 O  O   . PHE B 1 290 ? 31.246 47.856 58.190  1.00 16.93 ? 268 PHE B O   1 
ATOM   4049 C  CB  . PHE B 1 290 ? 28.445 48.233 56.506  1.00 15.54 ? 268 PHE B CB  1 
ATOM   4050 C  CG  . PHE B 1 290 ? 27.033 48.725 56.489  1.00 14.81 ? 268 PHE B CG  1 
ATOM   4051 C  CD1 . PHE B 1 290 ? 25.982 47.838 56.309  1.00 14.58 ? 268 PHE B CD1 1 
ATOM   4052 C  CD2 . PHE B 1 290 ? 26.745 50.070 56.682  1.00 14.62 ? 268 PHE B CD2 1 
ATOM   4053 C  CE1 . PHE B 1 290 ? 24.673 48.286 56.312  1.00 14.43 ? 268 PHE B CE1 1 
ATOM   4054 C  CE2 . PHE B 1 290 ? 25.438 50.521 56.681  1.00 14.53 ? 268 PHE B CE2 1 
ATOM   4055 C  CZ  . PHE B 1 290 ? 24.399 49.626 56.501  1.00 14.40 ? 268 PHE B CZ  1 
ATOM   4056 N  N   . PRO B 1 291 ? 30.487 45.945 57.241  1.00 18.40 ? 269 PRO B N   1 
ATOM   4057 C  CA  . PRO B 1 291 ? 31.841 45.432 57.020  1.00 19.41 ? 269 PRO B CA  1 
ATOM   4058 C  C   . PRO B 1 291 ? 32.701 46.420 56.234  1.00 20.48 ? 269 PRO B C   1 
ATOM   4059 O  O   . PRO B 1 291 ? 32.203 47.086 55.324  1.00 20.62 ? 269 PRO B O   1 
ATOM   4060 C  CB  . PRO B 1 291 ? 31.602 44.159 56.204  1.00 19.28 ? 269 PRO B CB  1 
ATOM   4061 C  CG  . PRO B 1 291 ? 30.244 43.701 56.609  1.00 18.99 ? 269 PRO B CG  1 
ATOM   4062 C  CD  . PRO B 1 291 ? 29.456 44.948 56.891  1.00 18.74 ? 269 PRO B CD  1 
ATOM   4063 N  N   . ALA B 1 292 ? 33.977 46.525 56.595  1.00 21.66 ? 270 ALA B N   1 
ATOM   4064 C  CA  . ALA B 1 292 ? 34.897 47.435 55.914  1.00 22.97 ? 270 ALA B CA  1 
ATOM   4065 C  C   . ALA B 1 292 ? 35.104 47.026 54.455  1.00 23.85 ? 270 ALA B C   1 
ATOM   4066 O  O   . ALA B 1 292 ? 34.972 45.849 54.109  1.00 25.26 ? 270 ALA B O   1 
ATOM   4067 C  CB  . ALA B 1 292 ? 36.232 47.476 56.644  1.00 23.03 ? 270 ALA B CB  1 
ATOM   4068 N  N   . TYR C 1 25  ? 19.234 17.310 61.839  1.00 19.83 ? 3   TYR C N   1 
ATOM   4069 C  CA  . TYR C 1 25  ? 18.980 16.921 60.417  1.00 19.24 ? 3   TYR C CA  1 
ATOM   4070 C  C   . TYR C 1 25  ? 19.966 15.863 59.923  1.00 19.31 ? 3   TYR C C   1 
ATOM   4071 O  O   . TYR C 1 25  ? 21.102 15.805 60.386  1.00 19.99 ? 3   TYR C O   1 
ATOM   4072 C  CB  . TYR C 1 25  ? 19.065 18.146 59.507  1.00 19.01 ? 3   TYR C CB  1 
ATOM   4073 C  CG  . TYR C 1 25  ? 18.097 19.252 59.860  1.00 18.97 ? 3   TYR C CG  1 
ATOM   4074 C  CD1 . TYR C 1 25  ? 16.725 19.097 59.658  1.00 19.16 ? 3   TYR C CD1 1 
ATOM   4075 C  CD2 . TYR C 1 25  ? 18.549 20.460 60.379  1.00 18.95 ? 3   TYR C CD2 1 
ATOM   4076 C  CE1 . TYR C 1 25  ? 15.835 20.112 59.971  1.00 19.16 ? 3   TYR C CE1 1 
ATOM   4077 C  CE2 . TYR C 1 25  ? 17.666 21.480 60.693  1.00 19.23 ? 3   TYR C CE2 1 
ATOM   4078 C  CZ  . TYR C 1 25  ? 16.313 21.305 60.487  1.00 19.27 ? 3   TYR C CZ  1 
ATOM   4079 O  OH  . TYR C 1 25  ? 15.441 22.322 60.800  1.00 19.02 ? 3   TYR C OH  1 
ATOM   4080 N  N   . SER C 1 26  ? 19.519 15.047 58.973  1.00 19.13 ? 4   SER C N   1 
ATOM   4081 C  CA  . SER C 1 26  ? 20.298 13.923 58.447  1.00 19.02 ? 4   SER C CA  1 
ATOM   4082 C  C   . SER C 1 26  ? 21.022 14.227 57.130  1.00 18.07 ? 4   SER C C   1 
ATOM   4083 O  O   . SER C 1 26  ? 22.109 13.702 56.881  1.00 18.54 ? 4   SER C O   1 
ATOM   4084 C  CB  . SER C 1 26  ? 19.377 12.718 58.249  1.00 20.02 ? 4   SER C CB  1 
ATOM   4085 O  OG  . SER C 1 26  ? 20.076 11.621 57.692  1.00 21.71 ? 4   SER C OG  1 
ATOM   4086 N  N   . LYS C 1 27  ? 20.410 15.049 56.281  1.00 16.42 ? 5   LYS C N   1 
ATOM   4087 C  CA  . LYS C 1 27  ? 20.935 15.315 54.941  1.00 15.54 ? 5   LYS C CA  1 
ATOM   4088 C  C   . LYS C 1 27  ? 21.350 16.771 54.733  1.00 14.11 ? 5   LYS C C   1 
ATOM   4089 O  O   . LYS C 1 27  ? 21.863 17.119 53.670  1.00 13.15 ? 5   LYS C O   1 
ATOM   4090 C  CB  . LYS C 1 27  ? 19.894 14.926 53.889  1.00 16.04 ? 5   LYS C CB  1 
ATOM   4091 C  CG  . LYS C 1 27  ? 19.438 13.471 53.943  1.00 16.94 ? 5   LYS C CG  1 
ATOM   4092 C  CD  . LYS C 1 27  ? 20.399 12.552 53.215  1.00 17.59 ? 5   LYS C CD  1 
ATOM   4093 C  CE  . LYS C 1 27  ? 20.037 11.083 53.393  1.00 17.75 ? 5   LYS C CE  1 
ATOM   4094 N  NZ  . LYS C 1 27  ? 18.778 10.685 52.704  1.00 18.03 ? 5   LYS C NZ  1 
ATOM   4095 N  N   . ILE C 1 28  ? 21.101 17.624 55.722  1.00 13.04 ? 6   ILE C N   1 
ATOM   4096 C  CA  . ILE C 1 28  ? 21.598 18.996 55.692  1.00 12.81 ? 6   ILE C CA  1 
ATOM   4097 C  C   . ILE C 1 28  ? 22.237 19.345 57.026  1.00 12.68 ? 6   ILE C C   1 
ATOM   4098 O  O   . ILE C 1 28  ? 22.068 18.635 58.017  1.00 12.80 ? 6   ILE C O   1 
ATOM   4099 C  CB  . ILE C 1 28  ? 20.494 20.033 55.388  1.00 12.89 ? 6   ILE C CB  1 
ATOM   4100 C  CG1 . ILE C 1 28  ? 19.469 20.110 56.528  1.00 12.91 ? 6   ILE C CG1 1 
ATOM   4101 C  CG2 . ILE C 1 28  ? 19.814 19.709 54.063  1.00 13.00 ? 6   ILE C CG2 1 
ATOM   4102 C  CD1 . ILE C 1 28  ? 18.535 21.300 56.431  1.00 13.10 ? 6   ILE C CD1 1 
ATOM   4103 N  N   . LEU C 1 29  ? 22.988 20.435 57.033  1.00 12.40 ? 7   LEU C N   1 
ATOM   4104 C  CA  . LEU C 1 29  ? 23.382 21.082 58.268  1.00 12.51 ? 7   LEU C CA  1 
ATOM   4105 C  C   . LEU C 1 29  ? 22.629 22.395 58.335  1.00 12.13 ? 7   LEU C C   1 
ATOM   4106 O  O   . LEU C 1 29  ? 22.422 23.044 57.309  1.00 11.49 ? 7   LEU C O   1 
ATOM   4107 C  CB  . LEU C 1 29  ? 24.877 21.359 58.289  1.00 13.02 ? 7   LEU C CB  1 
ATOM   4108 C  CG  . LEU C 1 29  ? 25.782 20.151 58.071  1.00 13.70 ? 7   LEU C CG  1 
ATOM   4109 C  CD1 . LEU C 1 29  ? 27.217 20.594 57.840  1.00 14.13 ? 7   LEU C CD1 1 
ATOM   4110 C  CD2 . LEU C 1 29  ? 25.685 19.198 59.249  1.00 14.00 ? 7   LEU C CD2 1 
ATOM   4111 N  N   . TYR C 1 30  ? 22.203 22.764 59.538  1.00 11.84 ? 8   TYR C N   1 
ATOM   4112 C  CA  . TYR C 1 30  ? 21.596 24.066 59.784  1.00 11.85 ? 8   TYR C CA  1 
ATOM   4113 C  C   . TYR C 1 30  ? 22.357 24.739 60.919  1.00 12.10 ? 8   TYR C C   1 
ATOM   4114 O  O   . TYR C 1 30  ? 22.478 24.178 62.013  1.00 12.22 ? 8   TYR C O   1 
ATOM   4115 C  CB  . TYR C 1 30  ? 20.116 23.931 60.145  1.00 11.64 ? 8   TYR C CB  1 
ATOM   4116 C  CG  . TYR C 1 30  ? 19.451 25.256 60.455  1.00 11.56 ? 8   TYR C CG  1 
ATOM   4117 C  CD1 . TYR C 1 30  ? 19.078 26.124 59.435  1.00 11.38 ? 8   TYR C CD1 1 
ATOM   4118 C  CD2 . TYR C 1 30  ? 19.209 25.650 61.768  1.00 11.71 ? 8   TYR C CD2 1 
ATOM   4119 C  CE1 . TYR C 1 30  ? 18.479 27.341 59.714  1.00 11.45 ? 8   TYR C CE1 1 
ATOM   4120 C  CE2 . TYR C 1 30  ? 18.603 26.864 62.052  1.00 11.69 ? 8   TYR C CE2 1 
ATOM   4121 C  CZ  . TYR C 1 30  ? 18.244 27.707 61.019  1.00 11.60 ? 8   TYR C CZ  1 
ATOM   4122 O  OH  . TYR C 1 30  ? 17.644 28.917 61.286  1.00 11.80 ? 8   TYR C OH  1 
ATOM   4123 N  N   . GLU C 1 31  ? 22.877 25.929 60.639  1.00 12.48 ? 9   GLU C N   1 
ATOM   4124 C  CA  . GLU C 1 31  ? 23.646 26.720 61.599  1.00 13.01 ? 9   GLU C CA  1 
ATOM   4125 C  C   . GLU C 1 31  ? 23.037 28.106 61.680  1.00 12.82 ? 9   GLU C C   1 
ATOM   4126 O  O   . GLU C 1 31  ? 22.537 28.621 60.677  1.00 12.26 ? 9   GLU C O   1 
ATOM   4127 C  CB  . GLU C 1 31  ? 25.086 26.911 61.108  1.00 14.01 ? 9   GLU C CB  1 
ATOM   4128 C  CG  . GLU C 1 31  ? 25.929 25.659 60.937  1.00 14.95 ? 9   GLU C CG  1 
ATOM   4129 C  CD  . GLU C 1 31  ? 27.226 25.948 60.192  1.00 15.95 ? 9   GLU C CD  1 
ATOM   4130 O  OE1 . GLU C 1 31  ? 28.318 25.857 60.799  1.00 17.66 ? 9   GLU C OE1 1 
ATOM   4131 O  OE2 . GLU C 1 31  ? 27.166 26.288 58.993  1.00 15.95 ? 9   GLU C OE2 1 
ATOM   4132 N  N   . THR C 1 32  ? 23.101 28.722 62.855  1.00 12.37 ? 10  THR C N   1 
ATOM   4133 C  CA  . THR C 1 32  ? 22.975 30.172 62.945  1.00 12.42 ? 10  THR C CA  1 
ATOM   4134 C  C   . THR C 1 32  ? 24.294 30.733 63.470  1.00 12.00 ? 10  THR C C   1 
ATOM   4135 O  O   . THR C 1 32  ? 24.882 30.195 64.411  1.00 12.16 ? 10  THR C O   1 
ATOM   4136 C  CB  . THR C 1 32  ? 21.781 30.626 63.811  1.00 12.82 ? 10  THR C CB  1 
ATOM   4137 O  OG1 . THR C 1 32  ? 21.919 30.135 65.147  1.00 13.60 ? 10  THR C OG1 1 
ATOM   4138 C  CG2 . THR C 1 32  ? 20.481 30.106 63.220  1.00 13.00 ? 10  THR C CG2 1 
ATOM   4139 N  N   . LEU C 1 33  ? 24.772 31.787 62.819  1.00 11.39 ? 11  LEU C N   1 
ATOM   4140 C  CA  . LEU C 1 33  ? 25.989 32.474 63.227  1.00 11.06 ? 11  LEU C CA  1 
ATOM   4141 C  C   . LEU C 1 33  ? 25.930 33.927 62.796  1.00 10.62 ? 11  LEU C C   1 
ATOM   4142 O  O   . LEU C 1 33  ? 25.511 34.239 61.680  1.00 10.50 ? 11  LEU C O   1 
ATOM   4143 C  CB  . LEU C 1 33  ? 27.234 31.801 62.638  1.00 11.22 ? 11  LEU C CB  1 
ATOM   4144 C  CG  . LEU C 1 33  ? 27.526 31.876 61.132  1.00 11.42 ? 11  LEU C CG  1 
ATOM   4145 C  CD1 . LEU C 1 33  ? 28.913 31.317 60.859  1.00 11.58 ? 11  LEU C CD1 1 
ATOM   4146 C  CD2 . LEU C 1 33  ? 26.472 31.161 60.299  1.00 11.52 ? 11  LEU C CD2 1 
ATOM   4147 N  N   . HIS C 1 34  ? 26.331 34.823 63.688  1.00 10.31 ? 12  HIS C N   1 
ATOM   4148 C  CA  . HIS C 1 34  ? 26.412 36.242 63.372  1.00 10.24 ? 12  HIS C CA  1 
ATOM   4149 C  C   . HIS C 1 34  ? 25.126 36.822 62.780  1.00 10.13 ? 12  HIS C C   1 
ATOM   4150 O  O   . HIS C 1 34  ? 25.184 37.681 61.907  1.00 10.06 ? 12  HIS C O   1 
ATOM   4151 C  CB  . HIS C 1 34  ? 27.582 36.481 62.420  1.00 10.53 ? 12  HIS C CB  1 
ATOM   4152 C  CG  . HIS C 1 34  ? 28.848 35.829 62.871  1.00 10.83 ? 12  HIS C CG  1 
ATOM   4153 N  ND1 . HIS C 1 34  ? 29.541 34.916 62.107  1.00 11.16 ? 12  HIS C ND1 1 
ATOM   4154 C  CD2 . HIS C 1 34  ? 29.527 35.938 64.031  1.00 10.93 ? 12  HIS C CD2 1 
ATOM   4155 C  CE1 . HIS C 1 34  ? 30.606 34.510 62.776  1.00 10.99 ? 12  HIS C CE1 1 
ATOM   4156 N  NE2 . HIS C 1 34  ? 30.619 35.114 63.946  1.00 11.22 ? 12  HIS C NE2 1 
ATOM   4157 N  N   . GLY C 1 35  ? 23.980 36.355 63.269  1.00 10.03 ? 13  GLY C N   1 
ATOM   4158 C  CA  . GLY C 1 35  ? 22.677 36.826 62.797  1.00 10.20 ? 13  GLY C CA  1 
ATOM   4159 C  C   . GLY C 1 35  ? 22.293 36.320 61.416  1.00 10.40 ? 13  GLY C C   1 
ATOM   4160 O  O   . GLY C 1 35  ? 21.397 36.886 60.766  1.00 10.45 ? 13  GLY C O   1 
ATOM   4161 N  N   . VAL C 1 36  ? 22.955 35.255 60.976  1.00 10.34 ? 14  VAL C N   1 
ATOM   4162 C  CA  . VAL C 1 36  ? 22.745 34.668 59.655  1.00 10.51 ? 14  VAL C CA  1 
ATOM   4163 C  C   . VAL C 1 36  ? 22.435 33.185 59.843  1.00 10.21 ? 14  VAL C C   1 
ATOM   4164 O  O   . VAL C 1 36  ? 23.034 32.519 60.695  1.00 10.91 ? 14  VAL C O   1 
ATOM   4165 C  CB  . VAL C 1 36  ? 24.005 34.824 58.767  1.00 10.80 ? 14  VAL C CB  1 
ATOM   4166 C  CG1 . VAL C 1 36  ? 23.793 34.205 57.385  1.00 11.13 ? 14  VAL C CG1 1 
ATOM   4167 C  CG2 . VAL C 1 36  ? 24.398 36.291 58.654  1.00 10.93 ? 14  VAL C CG2 1 
ATOM   4168 N  N   . ALA C 1 37  ? 21.491 32.666 59.067  1.00 9.44  ? 15  ALA C N   1 
ATOM   4169 C  CA  . ALA C 1 37  ? 21.261 31.228 59.025  1.00 9.11  ? 15  ALA C CA  1 
ATOM   4170 C  C   . ALA C 1 37  ? 22.039 30.670 57.850  1.00 8.84  ? 15  ALA C C   1 
ATOM   4171 O  O   . ALA C 1 37  ? 22.144 31.320 56.814  1.00 8.69  ? 15  ALA C O   1 
ATOM   4172 C  CB  . ALA C 1 37  ? 19.785 30.922 58.876  1.00 9.06  ? 15  ALA C CB  1 
ATOM   4173 N  N   . ARG C 1 38  ? 22.608 29.482 58.021  1.00 8.52  ? 16  ARG C N   1 
ATOM   4174 C  CA  . ARG C 1 38  ? 23.337 28.833 56.941  1.00 8.56  ? 16  ARG C CA  1 
ATOM   4175 C  C   . ARG C 1 38  ? 22.891 27.387 56.796  1.00 8.40  ? 16  ARG C C   1 
ATOM   4176 O  O   . ARG C 1 38  ? 22.954 26.618 57.750  1.00 8.23  ? 16  ARG C O   1 
ATOM   4177 C  CB  . ARG C 1 38  ? 24.843 28.909 57.191  1.00 8.73  ? 16  ARG C CB  1 
ATOM   4178 C  CG  . ARG C 1 38  ? 25.683 28.374 56.049  1.00 8.98  ? 16  ARG C CG  1 
ATOM   4179 C  CD  . ARG C 1 38  ? 27.112 28.886 56.131  1.00 9.31  ? 16  ARG C CD  1 
ATOM   4180 N  NE  . ARG C 1 38  ? 27.831 28.325 57.274  1.00 9.62  ? 16  ARG C NE  1 
ATOM   4181 C  CZ  . ARG C 1 38  ? 29.057 28.688 57.654  1.00 9.90  ? 16  ARG C CZ  1 
ATOM   4182 N  NH1 . ARG C 1 38  ? 29.721 29.642 57.008  1.00 10.12 ? 16  ARG C NH1 1 
ATOM   4183 N  NH2 . ARG C 1 38  ? 29.625 28.094 58.699  1.00 10.23 ? 16  ARG C NH2 1 
ATOM   4184 N  N   . ILE C 1 39  ? 22.436 27.039 55.594  1.00 8.20  ? 17  ILE C N   1 
ATOM   4185 C  CA  . ILE C 1 39  ? 22.037 25.686 55.247  1.00 8.25  ? 17  ILE C CA  1 
ATOM   4186 C  C   . ILE C 1 39  ? 23.113 25.055 54.378  1.00 8.20  ? 17  ILE C C   1 
ATOM   4187 O  O   . ILE C 1 39  ? 23.484 25.605 53.339  1.00 8.03  ? 17  ILE C O   1 
ATOM   4188 C  CB  . ILE C 1 39  ? 20.704 25.687 54.476  1.00 8.38  ? 17  ILE C CB  1 
ATOM   4189 C  CG1 . ILE C 1 39  ? 19.588 26.221 55.375  1.00 8.50  ? 17  ILE C CG1 1 
ATOM   4190 C  CG2 . ILE C 1 39  ? 20.357 24.289 53.974  1.00 8.39  ? 17  ILE C CG2 1 
ATOM   4191 C  CD1 . ILE C 1 39  ? 18.316 26.574 54.629  1.00 8.66  ? 17  ILE C CD1 1 
ATOM   4192 N  N   . THR C 1 40  ? 23.607 23.897 54.800  1.00 8.30  ? 18  THR C N   1 
ATOM   4193 C  CA  . THR C 1 40  ? 24.595 23.155 54.028  1.00 8.47  ? 18  THR C CA  1 
ATOM   4194 C  C   . THR C 1 40  ? 23.979 21.863 53.497  1.00 8.61  ? 18  THR C C   1 
ATOM   4195 O  O   . THR C 1 40  ? 23.545 21.007 54.271  1.00 8.51  ? 18  THR C O   1 
ATOM   4196 C  CB  . THR C 1 40  ? 25.842 22.815 54.871  1.00 8.56  ? 18  THR C CB  1 
ATOM   4197 O  OG1 . THR C 1 40  ? 26.386 24.014 55.426  1.00 8.51  ? 18  THR C OG1 1 
ATOM   4198 C  CG2 . THR C 1 40  ? 26.902 22.123 54.019  1.00 8.73  ? 18  THR C CG2 1 
ATOM   4199 N  N   . LEU C 1 41  ? 23.938 21.734 52.172  1.00 8.90  ? 19  LEU C N   1 
ATOM   4200 C  CA  . LEU C 1 41  ? 23.465 20.516 51.524  1.00 9.42  ? 19  LEU C CA  1 
ATOM   4201 C  C   . LEU C 1 41  ? 24.542 19.464 51.748  1.00 10.12 ? 19  LEU C C   1 
ATOM   4202 O  O   . LEU C 1 41  ? 25.685 19.659 51.337  1.00 9.87  ? 19  LEU C O   1 
ATOM   4203 C  CB  . LEU C 1 41  ? 23.235 20.754 50.029  1.00 9.45  ? 19  LEU C CB  1 
ATOM   4204 C  CG  . LEU C 1 41  ? 22.389 21.981 49.660  1.00 9.55  ? 19  LEU C CG  1 
ATOM   4205 C  CD1 . LEU C 1 41  ? 22.325 22.137 48.152  1.00 9.74  ? 19  LEU C CD1 1 
ATOM   4206 C  CD2 . LEU C 1 41  ? 20.989 21.894 50.256  1.00 9.56  ? 19  LEU C CD2 1 
ATOM   4207 N  N   . ASN C 1 42  ? 24.185 18.365 52.413  1.00 11.08 ? 20  ASN C N   1 
ATOM   4208 C  CA  . ASN C 1 42  ? 25.196 17.499 53.018  1.00 12.07 ? 20  ASN C CA  1 
ATOM   4209 C  C   . ASN C 1 42  ? 25.075 16.007 52.710  1.00 12.90 ? 20  ASN C C   1 
ATOM   4210 O  O   . ASN C 1 42  ? 24.684 15.205 53.563  1.00 12.80 ? 20  ASN C O   1 
ATOM   4211 C  CB  . ASN C 1 42  ? 25.205 17.723 54.530  1.00 12.41 ? 20  ASN C CB  1 
ATOM   4212 C  CG  . ASN C 1 42  ? 26.460 17.193 55.186  1.00 12.78 ? 20  ASN C CG  1 
ATOM   4213 O  OD1 . ASN C 1 42  ? 27.463 16.948 54.517  1.00 13.34 ? 20  ASN C OD1 1 
ATOM   4214 N  ND2 . ASN C 1 42  ? 26.412 17.013 56.500  1.00 13.17 ? 20  ASN C ND2 1 
ATOM   4215 N  N   . ARG C 1 43  ? 25.446 15.646 51.487  1.00 13.93 ? 21  ARG C N   1 
ATOM   4216 C  CA  . ARG C 1 43  ? 25.635 14.250 51.116  1.00 15.41 ? 21  ARG C CA  1 
ATOM   4217 C  C   . ARG C 1 43  ? 26.782 14.172 50.111  1.00 16.20 ? 21  ARG C C   1 
ATOM   4218 O  O   . ARG C 1 43  ? 26.565 13.912 48.927  1.00 15.44 ? 21  ARG C O   1 
ATOM   4219 C  CB  . ARG C 1 43  ? 24.347 13.661 50.548  1.00 16.29 ? 21  ARG C CB  1 
ATOM   4220 C  CG  . ARG C 1 43  ? 24.314 12.142 50.585  1.00 17.47 ? 21  ARG C CG  1 
ATOM   4221 C  CD  . ARG C 1 43  ? 22.907 11.629 50.810  1.00 18.52 ? 21  ARG C CD  1 
ATOM   4222 N  NE  . ARG C 1 43  ? 22.007 12.179 49.807  1.00 19.18 ? 21  ARG C NE  1 
ATOM   4223 C  CZ  . ARG C 1 43  ? 21.268 11.472 48.957  1.00 19.32 ? 21  ARG C CZ  1 
ATOM   4224 N  NH1 . ARG C 1 43  ? 21.245 10.137 48.994  1.00 19.88 ? 21  ARG C NH1 1 
ATOM   4225 N  NH2 . ARG C 1 43  ? 20.514 12.120 48.078  1.00 18.56 ? 21  ARG C NH2 1 
ATOM   4226 N  N   . PRO C 1 44  ? 28.013 14.423 50.585  1.00 17.81 ? 22  PRO C N   1 
ATOM   4227 C  CA  . PRO C 1 44  ? 29.155 14.570 49.678  1.00 18.89 ? 22  PRO C CA  1 
ATOM   4228 C  C   . PRO C 1 44  ? 29.416 13.339 48.802  1.00 20.05 ? 22  PRO C C   1 
ATOM   4229 O  O   . PRO C 1 44  ? 29.835 13.489 47.649  1.00 20.55 ? 22  PRO C O   1 
ATOM   4230 C  CB  . PRO C 1 44  ? 30.334 14.867 50.621  1.00 18.84 ? 22  PRO C CB  1 
ATOM   4231 C  CG  . PRO C 1 44  ? 29.878 14.483 51.981  1.00 18.79 ? 22  PRO C CG  1 
ATOM   4232 C  CD  . PRO C 1 44  ? 28.390 14.625 51.995  1.00 18.15 ? 22  PRO C CD  1 
ATOM   4233 N  N   . GLU C 1 45  ? 29.132 12.145 49.321  1.00 20.75 ? 23  GLU C N   1 
ATOM   4234 C  CA  . GLU C 1 45  ? 29.300 10.916 48.536  1.00 21.52 ? 23  GLU C CA  1 
ATOM   4235 C  C   . GLU C 1 45  ? 28.368 10.838 47.317  1.00 20.42 ? 23  GLU C C   1 
ATOM   4236 O  O   . GLU C 1 45  ? 28.645 10.083 46.384  1.00 20.88 ? 23  GLU C O   1 
ATOM   4237 C  CB  . GLU C 1 45  ? 29.154 9.659  49.415  1.00 22.73 ? 23  GLU C CB  1 
ATOM   4238 C  CG  . GLU C 1 45  ? 27.729 9.240  49.766  1.00 24.08 ? 23  GLU C CG  1 
ATOM   4239 C  CD  . GLU C 1 45  ? 27.111 10.035 50.904  1.00 25.29 ? 23  GLU C CD  1 
ATOM   4240 O  OE1 . GLU C 1 45  ? 27.672 11.075 51.314  1.00 26.21 ? 23  GLU C OE1 1 
ATOM   4241 O  OE2 . GLU C 1 45  ? 26.045 9.603  51.394  1.00 27.72 ? 23  GLU C OE2 1 
ATOM   4242 N  N   . ARG C 1 46  ? 27.273 11.603 47.328  1.00 19.10 ? 24  ARG C N   1 
ATOM   4243 C  CA  . ARG C 1 46  ? 26.357 11.677 46.188  1.00 18.00 ? 24  ARG C CA  1 
ATOM   4244 C  C   . ARG C 1 46  ? 26.296 13.087 45.591  1.00 16.07 ? 24  ARG C C   1 
ATOM   4245 O  O   . ARG C 1 46  ? 25.285 13.469 45.004  1.00 15.08 ? 24  ARG C O   1 
ATOM   4246 C  CB  . ARG C 1 46  ? 24.943 11.245 46.599  1.00 19.28 ? 24  ARG C CB  1 
ATOM   4247 C  CG  . ARG C 1 46  ? 24.758 9.748  46.790  1.00 20.62 ? 24  ARG C CG  1 
ATOM   4248 C  CD  . ARG C 1 46  ? 23.318 9.338  46.497  1.00 21.66 ? 24  ARG C CD  1 
ATOM   4249 N  NE  . ARG C 1 46  ? 23.002 8.016  47.040  1.00 22.43 ? 24  ARG C NE  1 
ATOM   4250 C  CZ  . ARG C 1 46  ? 21.797 7.446  47.026  1.00 23.25 ? 24  ARG C CZ  1 
ATOM   4251 N  NH1 . ARG C 1 46  ? 20.748 8.063  46.484  1.00 23.60 ? 24  ARG C NH1 1 
ATOM   4252 N  NH2 . ARG C 1 46  ? 21.637 6.236  47.554  1.00 23.64 ? 24  ARG C NH2 1 
ATOM   4253 N  N   . THR C 1 47  ? 27.379 13.848 45.730  1.00 14.36 ? 25  THR C N   1 
ATOM   4254 C  CA  . THR C 1 47  ? 27.445 15.219 45.207  1.00 13.36 ? 25  THR C CA  1 
ATOM   4255 C  C   . THR C 1 47  ? 26.278 16.063 45.752  1.00 12.37 ? 25  THR C C   1 
ATOM   4256 O  O   . THR C 1 47  ? 25.716 16.903 45.047  1.00 11.92 ? 25  THR C O   1 
ATOM   4257 C  CB  . THR C 1 47  ? 27.479 15.236 43.657  1.00 13.55 ? 25  THR C CB  1 
ATOM   4258 O  OG1 . THR C 1 47  ? 28.363 14.212 43.176  1.00 14.17 ? 25  THR C OG1 1 
ATOM   4259 C  CG2 . THR C 1 47  ? 27.965 16.581 43.129  1.00 13.54 ? 25  THR C CG2 1 
ATOM   4260 N  N   . ASN C 1 48  ? 25.926 15.823 47.013  1.00 11.48 ? 26  ASN C N   1 
ATOM   4261 C  CA  . ASN C 1 48  ? 24.841 16.543 47.688  1.00 11.08 ? 26  ASN C CA  1 
ATOM   4262 C  C   . ASN C 1 48  ? 23.533 16.523 46.904  1.00 11.02 ? 26  ASN C C   1 
ATOM   4263 O  O   . ASN C 1 48  ? 22.791 17.506 46.896  1.00 10.54 ? 26  ASN C O   1 
ATOM   4264 C  CB  . ASN C 1 48  ? 25.260 17.989 47.971  1.00 11.04 ? 26  ASN C CB  1 
ATOM   4265 C  CG  . ASN C 1 48  ? 26.583 18.077 48.708  1.00 11.04 ? 26  ASN C CG  1 
ATOM   4266 O  OD1 . ASN C 1 48  ? 26.882 17.243 49.567  1.00 11.45 ? 26  ASN C OD1 1 
ATOM   4267 N  ND2 . ASN C 1 48  ? 27.377 19.085 48.381  1.00 10.93 ? 26  ASN C ND2 1 
ATOM   4268 N  N   . ALA C 1 49  ? 23.249 15.395 46.255  1.00 11.24 ? 27  ALA C N   1 
ATOM   4269 C  CA  . ALA C 1 49  ? 22.018 15.241 45.482  1.00 11.54 ? 27  ALA C CA  1 
ATOM   4270 C  C   . ALA C 1 49  ? 20.787 15.422 46.368  1.00 11.86 ? 27  ALA C C   1 
ATOM   4271 O  O   . ALA C 1 49  ? 20.723 14.901 47.486  1.00 11.76 ? 27  ALA C O   1 
ATOM   4272 C  CB  . ALA C 1 49  ? 21.985 13.881 44.805  1.00 11.72 ? 27  ALA C CB  1 
ATOM   4273 N  N   . LEU C 1 50  ? 19.809 16.163 45.855  1.00 12.28 ? 28  LEU C N   1 
ATOM   4274 C  CA  . LEU C 1 50  ? 18.607 16.509 46.603  1.00 12.94 ? 28  LEU C CA  1 
ATOM   4275 C  C   . LEU C 1 50  ? 17.580 15.380 46.525  1.00 13.21 ? 28  LEU C C   1 
ATOM   4276 O  O   . LEU C 1 50  ? 16.867 15.256 45.529  1.00 13.71 ? 28  LEU C O   1 
ATOM   4277 C  CB  . LEU C 1 50  ? 17.992 17.795 46.037  1.00 13.27 ? 28  LEU C CB  1 
ATOM   4278 C  CG  . LEU C 1 50  ? 18.802 19.097 46.130  1.00 13.66 ? 28  LEU C CG  1 
ATOM   4279 C  CD1 . LEU C 1 50  ? 18.577 19.950 44.892  1.00 13.92 ? 28  LEU C CD1 1 
ATOM   4280 C  CD2 . LEU C 1 50  ? 18.427 19.882 47.379  1.00 13.88 ? 28  LEU C CD2 1 
ATOM   4281 N  N   . ASP C 1 51  ? 17.496 14.564 47.567  1.00 13.56 ? 29  ASP C N   1 
ATOM   4282 C  CA  . ASP C 1 51  ? 16.467 13.528 47.620  1.00 13.91 ? 29  ASP C CA  1 
ATOM   4283 C  C   . ASP C 1 51  ? 15.258 14.042 48.405  1.00 14.10 ? 29  ASP C C   1 
ATOM   4284 O  O   . ASP C 1 51  ? 15.238 15.188 48.855  1.00 13.29 ? 29  ASP C O   1 
ATOM   4285 C  CB  . ASP C 1 51  ? 17.019 12.195 48.167  1.00 14.21 ? 29  ASP C CB  1 
ATOM   4286 C  CG  . ASP C 1 51  ? 17.473 12.274 49.621  1.00 14.43 ? 29  ASP C CG  1 
ATOM   4287 O  OD1 . ASP C 1 51  ? 17.374 13.350 50.241  1.00 14.53 ? 29  ASP C OD1 1 
ATOM   4288 O  OD2 . ASP C 1 51  ? 17.939 11.236 50.150  1.00 15.07 ? 29  ASP C OD2 1 
ATOM   4289 N  N   . GLN C 1 52  ? 14.242 13.197 48.536  1.00 14.75 ? 30  GLN C N   1 
ATOM   4290 C  CA  . GLN C 1 52  ? 13.006 13.574 49.216  1.00 15.56 ? 30  GLN C CA  1 
ATOM   4291 C  C   . GLN C 1 52  ? 13.248 14.009 50.648  1.00 15.07 ? 30  GLN C C   1 
ATOM   4292 O  O   . GLN C 1 52  ? 12.672 15.001 51.107  1.00 14.46 ? 30  GLN C O   1 
ATOM   4293 C  CB  . GLN C 1 52  ? 12.033 12.394 49.221  1.00 16.45 ? 30  GLN C CB  1 
ATOM   4294 C  CG  . GLN C 1 52  ? 11.546 12.001 47.844  1.00 17.44 ? 30  GLN C CG  1 
ATOM   4295 C  CD  . GLN C 1 52  ? 10.858 13.148 47.142  1.00 18.20 ? 30  GLN C CD  1 
ATOM   4296 O  OE1 . GLN C 1 52  ? 11.450 13.810 46.296  1.00 19.78 ? 30  GLN C OE1 1 
ATOM   4297 N  NE2 . GLN C 1 52  ? 9.613  13.409 47.513  1.00 19.15 ? 30  GLN C NE2 1 
ATOM   4298 N  N   . GLU C 1 53  ? 14.090 13.260 51.352  1.00 15.17 ? 31  GLU C N   1 
ATOM   4299 C  CA  . GLU C 1 53  ? 14.400 13.567 52.741  1.00 15.51 ? 31  GLU C CA  1 
ATOM   4300 C  C   . GLU C 1 53  ? 15.061 14.940 52.852  1.00 14.79 ? 31  GLU C C   1 
ATOM   4301 O  O   . GLU C 1 53  ? 14.654 15.758 53.675  1.00 14.13 ? 31  GLU C O   1 
ATOM   4302 C  CB  . GLU C 1 53  ? 15.292 12.483 53.364  1.00 16.61 ? 31  GLU C CB  1 
ATOM   4303 C  CG  . GLU C 1 53  ? 15.479 12.640 54.868  1.00 17.73 ? 31  GLU C CG  1 
ATOM   4304 C  CD  . GLU C 1 53  ? 16.332 11.552 55.499  1.00 18.88 ? 31  GLU C CD  1 
ATOM   4305 O  OE1 . GLU C 1 53  ? 16.911 10.717 54.769  1.00 20.61 ? 31  GLU C OE1 1 
ATOM   4306 O  OE2 . GLU C 1 53  ? 16.428 11.535 56.744  1.00 20.42 ? 31  GLU C OE2 1 
HETATM 4307 N  N   . MSE C 1 54  ? 16.052 15.201 52.000  1.00 14.39 ? 32  MSE C N   1 
HETATM 4308 C  CA  . MSE C 1 54  ? 16.772 16.480 52.025  1.00 14.64 ? 32  MSE C CA  1 
HETATM 4309 C  C   . MSE C 1 54  ? 15.841 17.634 51.748  1.00 13.21 ? 32  MSE C C   1 
HETATM 4310 O  O   . MSE C 1 54  ? 15.934 18.667 52.402  1.00 12.43 ? 32  MSE C O   1 
HETATM 4311 C  CB  . MSE C 1 54  ? 17.940 16.511 51.038  1.00 16.60 ? 32  MSE C CB  1 
HETATM 4312 C  CG  . MSE C 1 54  ? 18.918 17.623 51.423  1.00 18.77 ? 32  MSE C CG  1 
HETATM 4313 SE SE  . MSE C 1 54  ? 20.216 17.979 49.982  1.00 24.81 ? 32  MSE C SE  1 
HETATM 4314 C  CE  . MSE C 1 54  ? 21.430 16.456 50.269  1.00 22.70 ? 32  MSE C CE  1 
ATOM   4315 N  N   . LEU C 1 55  ? 14.936 17.479 50.782  1.00 12.10 ? 33  LEU C N   1 
ATOM   4316 C  CA  . LEU C 1 55  ? 13.990 18.554 50.468  1.00 11.49 ? 33  LEU C CA  1 
ATOM   4317 C  C   . LEU C 1 55  ? 13.102 18.880 51.662  1.00 10.95 ? 33  LEU C C   1 
ATOM   4318 O  O   . LEU C 1 55  ? 12.856 20.048 51.956  1.00 10.52 ? 33  LEU C O   1 
ATOM   4319 C  CB  . LEU C 1 55  ? 13.138 18.196 49.247  1.00 11.56 ? 33  LEU C CB  1 
ATOM   4320 C  CG  . LEU C 1 55  ? 13.906 18.091 47.929  1.00 11.71 ? 33  LEU C CG  1 
ATOM   4321 C  CD1 . LEU C 1 55  ? 13.026 17.517 46.828  1.00 11.90 ? 33  LEU C CD1 1 
ATOM   4322 C  CD2 . LEU C 1 55  ? 14.451 19.446 47.506  1.00 11.63 ? 33  LEU C CD2 1 
ATOM   4323 N  N   . GLY C 1 56  ? 12.633 17.845 52.357  1.00 10.49 ? 34  GLY C N   1 
ATOM   4324 C  CA  . GLY C 1 56  ? 11.858 18.033 53.577  1.00 10.59 ? 34  GLY C CA  1 
ATOM   4325 C  C   . GLY C 1 56  ? 12.625 18.780 54.655  1.00 10.34 ? 34  GLY C C   1 
ATOM   4326 O  O   . GLY C 1 56  ? 12.070 19.652 55.327  1.00 10.37 ? 34  GLY C O   1 
ATOM   4327 N  N   . GLU C 1 57  ? 13.904 18.449 54.812  1.00 10.27 ? 35  GLU C N   1 
ATOM   4328 C  CA  . GLU C 1 57  ? 14.745 19.111 55.808  1.00 10.33 ? 35  GLU C CA  1 
ATOM   4329 C  C   . GLU C 1 57  ? 15.043 20.563 55.432  1.00 9.66  ? 35  GLU C C   1 
ATOM   4330 O  O   . GLU C 1 57  ? 15.117 21.423 56.306  1.00 9.58  ? 35  GLU C O   1 
ATOM   4331 C  CB  . GLU C 1 57  ? 16.040 18.329 56.029  1.00 10.94 ? 35  GLU C CB  1 
ATOM   4332 C  CG  . GLU C 1 57  ? 15.781 16.958 56.639  1.00 11.69 ? 35  GLU C CG  1 
ATOM   4333 C  CD  . GLU C 1 57  ? 17.037 16.218 57.021  1.00 12.57 ? 35  GLU C CD  1 
ATOM   4334 O  OE1 . GLU C 1 57  ? 18.104 16.503 56.448  1.00 13.54 ? 35  GLU C OE1 1 
ATOM   4335 O  OE2 . GLU C 1 57  ? 16.954 15.344 57.915  1.00 13.58 ? 35  GLU C OE2 1 
ATOM   4336 N  N   . ILE C 1 58  ? 15.198 20.839 54.138  1.00 9.04  ? 36  ILE C N   1 
ATOM   4337 C  CA  . ILE C 1 58  ? 15.394 22.219 53.676  1.00 8.70  ? 36  ILE C CA  1 
ATOM   4338 C  C   . ILE C 1 58  ? 14.175 23.053 54.059  1.00 8.59  ? 36  ILE C C   1 
ATOM   4339 O  O   . ILE C 1 58  ? 14.306 24.159 54.571  1.00 8.45  ? 36  ILE C O   1 
ATOM   4340 C  CB  . ILE C 1 58  ? 15.648 22.292 52.154  1.00 8.50  ? 36  ILE C CB  1 
ATOM   4341 C  CG1 . ILE C 1 58  ? 17.020 21.686 51.827  1.00 8.45  ? 36  ILE C CG1 1 
ATOM   4342 C  CG2 . ILE C 1 58  ? 15.568 23.741 51.661  1.00 8.53  ? 36  ILE C CG2 1 
ATOM   4343 C  CD1 . ILE C 1 58  ? 17.245 21.389 50.357  1.00 8.51  ? 36  ILE C CD1 1 
ATOM   4344 N  N   . ASN C 1 59  ? 12.987 22.513 53.826  1.00 8.59  ? 37  ASN C N   1 
ATOM   4345 C  CA  . ASN C 1 59  ? 11.770 23.209 54.220  1.00 8.72  ? 37  ASN C CA  1 
ATOM   4346 C  C   . ASN C 1 59  ? 11.689 23.461 55.726  1.00 8.75  ? 37  ASN C C   1 
ATOM   4347 O  O   . ASN C 1 59  ? 11.268 24.533 56.147  1.00 8.83  ? 37  ASN C O   1 
ATOM   4348 C  CB  . ASN C 1 59  ? 10.537 22.457 53.729  1.00 8.85  ? 37  ASN C CB  1 
ATOM   4349 C  CG  . ASN C 1 59  ? 10.326 22.614 52.240  1.00 8.84  ? 37  ASN C CG  1 
ATOM   4350 O  OD1 . ASN C 1 59  ? 10.519 21.681 51.460  1.00 9.49  ? 37  ASN C OD1 1 
ATOM   4351 N  ND2 . ASN C 1 59  ? 9.955  23.804 51.834  1.00 8.67  ? 37  ASN C ND2 1 
ATOM   4352 N  N   . ALA C 1 60  ? 12.100 22.482 56.526  1.00 8.77  ? 38  ALA C N   1 
ATOM   4353 C  CA  . ALA C 1 60  ? 12.115 22.645 57.981  1.00 8.74  ? 38  ALA C CA  1 
ATOM   4354 C  C   . ALA C 1 60  ? 13.111 23.726 58.415  1.00 8.86  ? 38  ALA C C   1 
ATOM   4355 O  O   . ALA C 1 60  ? 12.814 24.546 59.293  1.00 8.82  ? 38  ALA C O   1 
ATOM   4356 C  CB  . ALA C 1 60  ? 12.435 21.322 58.658  1.00 8.93  ? 38  ALA C CB  1 
ATOM   4357 N  N   . ALA C 1 61  ? 14.280 23.732 57.781  1.00 8.86  ? 39  ALA C N   1 
ATOM   4358 C  CA  . ALA C 1 61  ? 15.313 24.729 58.061  1.00 9.13  ? 39  ALA C CA  1 
ATOM   4359 C  C   . ALA C 1 61  ? 14.874 26.142 57.660  1.00 9.41  ? 39  ALA C C   1 
ATOM   4360 O  O   . ALA C 1 61  ? 15.132 27.104 58.383  1.00 9.11  ? 39  ALA C O   1 
ATOM   4361 C  CB  . ALA C 1 61  ? 16.617 24.351 57.373  1.00 9.09  ? 39  ALA C CB  1 
HETATM 4362 N  N   . MSE C 1 62  ? 14.200 26.268 56.518  1.00 9.93  ? 40  MSE C N   1 
HETATM 4363 C  CA  . MSE C 1 62  ? 13.693 27.572 56.083  1.00 10.48 ? 40  MSE C CA  1 
HETATM 4364 C  C   . MSE C 1 62  ? 12.589 28.041 56.999  1.00 10.03 ? 40  MSE C C   1 
HETATM 4365 O  O   . MSE C 1 62  ? 12.507 29.227 57.308  1.00 9.60  ? 40  MSE C O   1 
HETATM 4366 C  CB  . MSE C 1 62  ? 13.223 27.536 54.629  1.00 11.95 ? 40  MSE C CB  1 
HETATM 4367 C  CG  . MSE C 1 62  ? 14.402 27.362 53.668  1.00 13.24 ? 40  MSE C CG  1 
HETATM 4368 SE SE  . MSE C 1 62  ? 15.573 28.949 53.643  1.00 17.52 ? 40  MSE C SE  1 
HETATM 4369 C  CE  . MSE C 1 62  ? 14.493 30.023 52.392  1.00 15.85 ? 40  MSE C CE  1 
ATOM   4370 N  N   . ASP C 1 63  ? 11.734 27.126 57.450  1.00 9.74  ? 41  ASP C N   1 
ATOM   4371 C  CA  . ASP C 1 63  ? 10.717 27.479 58.446  1.00 9.80  ? 41  ASP C CA  1 
ATOM   4372 C  C   . ASP C 1 63  ? 11.392 28.038 59.692  1.00 9.45  ? 41  ASP C C   1 
ATOM   4373 O  O   . ASP C 1 63  ? 10.969 29.056 60.220  1.00 9.35  ? 41  ASP C O   1 
ATOM   4374 C  CB  . ASP C 1 63  ? 9.859  26.276 58.846  1.00 10.11 ? 41  ASP C CB  1 
ATOM   4375 C  CG  . ASP C 1 63  ? 8.892  25.833 57.756  1.00 10.42 ? 41  ASP C CG  1 
ATOM   4376 O  OD1 . ASP C 1 63  ? 8.711  26.535 56.741  1.00 10.76 ? 41  ASP C OD1 1 
ATOM   4377 O  OD2 . ASP C 1 63  ? 8.297  24.751 57.937  1.00 11.02 ? 41  ASP C OD2 1 
ATOM   4378 N  N   . ALA C 1 64  ? 12.449 27.371 60.151  1.00 9.23  ? 42  ALA C N   1 
ATOM   4379 C  CA  . ALA C 1 64  ? 13.185 27.822 61.334  1.00 9.35  ? 42  ALA C CA  1 
ATOM   4380 C  C   . ALA C 1 64  ? 13.814 29.199 61.123  1.00 9.24  ? 42  ALA C C   1 
ATOM   4381 O  O   . ALA C 1 64  ? 13.685 30.096 61.971  1.00 9.46  ? 42  ALA C O   1 
ATOM   4382 C  CB  . ALA C 1 64  ? 14.256 26.809 61.703  1.00 9.38  ? 42  ALA C CB  1 
ATOM   4383 N  N   . ALA C 1 65  ? 14.492 29.366 59.993  1.00 9.09  ? 43  ALA C N   1 
ATOM   4384 C  CA  . ALA C 1 65  ? 15.172 30.624 59.686  1.00 8.98  ? 43  ALA C CA  1 
ATOM   4385 C  C   . ALA C 1 65  ? 14.182 31.780 59.614  1.00 9.07  ? 43  ALA C C   1 
ATOM   4386 O  O   . ALA C 1 65  ? 14.460 32.879 60.092  1.00 8.96  ? 43  ALA C O   1 
ATOM   4387 C  CB  . ALA C 1 65  ? 15.943 30.509 58.373  1.00 8.84  ? 43  ALA C CB  1 
ATOM   4388 N  N   . GLU C 1 66  ? 13.024 31.528 59.014  1.00 9.18  ? 44  GLU C N   1 
ATOM   4389 C  CA  . GLU C 1 66  ? 12.020 32.571 58.829  1.00 9.54  ? 44  GLU C CA  1 
ATOM   4390 C  C   . GLU C 1 66  ? 11.348 32.970 60.143  1.00 9.73  ? 44  GLU C C   1 
ATOM   4391 O  O   . GLU C 1 66  ? 10.974 34.128 60.317  1.00 10.02 ? 44  GLU C O   1 
ATOM   4392 C  CB  . GLU C 1 66  ? 11.001 32.148 57.760  1.00 9.60  ? 44  GLU C CB  1 
ATOM   4393 C  CG  . GLU C 1 66  ? 11.614 32.238 56.369  1.00 9.72  ? 44  GLU C CG  1 
ATOM   4394 C  CD  . GLU C 1 66  ? 10.838 31.542 55.267  1.00 9.79  ? 44  GLU C CD  1 
ATOM   4395 O  OE1 . GLU C 1 66  ? 9.681  31.121 55.472  1.00 9.92  ? 44  GLU C OE1 1 
ATOM   4396 O  OE2 . GLU C 1 66  ? 11.411 31.427 54.165  1.00 9.96  ? 44  GLU C OE2 1 
ATOM   4397 N  N   . ALA C 1 67  ? 11.242 32.021 61.069  1.00 9.97  ? 45  ALA C N   1 
ATOM   4398 C  CA  . ALA C 1 67  ? 10.626 32.264 62.376  1.00 10.26 ? 45  ALA C CA  1 
ATOM   4399 C  C   . ALA C 1 67  ? 11.574 32.914 63.389  1.00 10.48 ? 45  ALA C C   1 
ATOM   4400 O  O   . ALA C 1 67  ? 11.121 33.526 64.360  1.00 11.01 ? 45  ALA C O   1 
ATOM   4401 C  CB  . ALA C 1 67  ? 10.094 30.958 62.936  1.00 10.30 ? 45  ALA C CB  1 
ATOM   4402 N  N   . ASP C 1 68  ? 12.877 32.775 63.167  1.00 10.51 ? 46  ASP C N   1 
ATOM   4403 C  CA  . ASP C 1 68  ? 13.896 33.243 64.107  1.00 10.53 ? 46  ASP C CA  1 
ATOM   4404 C  C   . ASP C 1 68  ? 14.201 34.726 63.852  1.00 10.43 ? 46  ASP C C   1 
ATOM   4405 O  O   . ASP C 1 68  ? 14.826 35.070 62.856  1.00 10.32 ? 46  ASP C O   1 
ATOM   4406 C  CB  . ASP C 1 68  ? 15.155 32.380 63.947  1.00 10.65 ? 46  ASP C CB  1 
ATOM   4407 C  CG  . ASP C 1 68  ? 16.216 32.656 65.003  1.00 10.72 ? 46  ASP C CG  1 
ATOM   4408 O  OD1 . ASP C 1 68  ? 16.128 33.668 65.720  1.00 10.98 ? 46  ASP C OD1 1 
ATOM   4409 O  OD2 . ASP C 1 68  ? 17.157 31.842 65.110  1.00 10.90 ? 46  ASP C OD2 1 
ATOM   4410 N  N   . ALA C 1 69  ? 13.779 35.597 64.768  1.00 10.48 ? 47  ALA C N   1 
ATOM   4411 C  CA  . ALA C 1 69  ? 13.994 37.042 64.619  1.00 10.53 ? 47  ALA C CA  1 
ATOM   4412 C  C   . ALA C 1 69  ? 15.473 37.424 64.684  1.00 10.58 ? 47  ALA C C   1 
ATOM   4413 O  O   . ALA C 1 69  ? 15.857 38.502 64.232  1.00 10.79 ? 47  ALA C O   1 
ATOM   4414 C  CB  . ALA C 1 69  ? 13.203 37.809 65.671  1.00 10.73 ? 47  ALA C CB  1 
ATOM   4415 N  N   . GLY C 1 70  ? 16.293 36.538 65.246  1.00 10.66 ? 48  GLY C N   1 
ATOM   4416 C  CA  . GLY C 1 70  ? 17.734 36.719 65.265  1.00 10.66 ? 48  GLY C CA  1 
ATOM   4417 C  C   . GLY C 1 70  ? 18.405 36.412 63.939  1.00 10.56 ? 48  GLY C C   1 
ATOM   4418 O  O   . GLY C 1 70  ? 19.592 36.667 63.786  1.00 11.26 ? 48  GLY C O   1 
ATOM   4419 N  N   . VAL C 1 71  ? 17.660 35.861 62.981  1.00 10.07 ? 49  VAL C N   1 
ATOM   4420 C  CA  . VAL C 1 71  ? 18.193 35.578 61.644  1.00 9.76  ? 49  VAL C CA  1 
ATOM   4421 C  C   . VAL C 1 71  ? 17.773 36.693 60.682  1.00 9.58  ? 49  VAL C C   1 
ATOM   4422 O  O   . VAL C 1 71  ? 16.592 37.000 60.572  1.00 9.59  ? 49  VAL C O   1 
ATOM   4423 C  CB  . VAL C 1 71  ? 17.697 34.207 61.129  1.00 9.68  ? 49  VAL C CB  1 
ATOM   4424 C  CG1 . VAL C 1 71  ? 17.980 34.029 59.639  1.00 9.62  ? 49  VAL C CG1 1 
ATOM   4425 C  CG2 . VAL C 1 71  ? 18.331 33.078 61.929  1.00 9.84  ? 49  VAL C CG2 1 
ATOM   4426 N  N   . LYS C 1 72  ? 18.744 37.295 59.999  1.00 9.47  ? 50  LYS C N   1 
ATOM   4427 C  CA  . LYS C 1 72  ? 18.490 38.425 59.091  1.00 9.55  ? 50  LYS C CA  1 
ATOM   4428 C  C   . LYS C 1 72  ? 18.634 38.056 57.617  1.00 8.87  ? 50  LYS C C   1 
ATOM   4429 O  O   . LYS C 1 72  ? 18.229 38.822 56.745  1.00 8.49  ? 50  LYS C O   1 
ATOM   4430 C  CB  . LYS C 1 72  ? 19.459 39.573 59.378  1.00 10.49 ? 50  LYS C CB  1 
ATOM   4431 C  CG  . LYS C 1 72  ? 19.619 39.954 60.836  1.00 11.47 ? 50  LYS C CG  1 
ATOM   4432 C  CD  . LYS C 1 72  ? 18.369 40.583 61.404  1.00 12.29 ? 50  LYS C CD  1 
ATOM   4433 C  CE  . LYS C 1 72  ? 18.610 41.049 62.836  1.00 13.10 ? 50  LYS C CE  1 
ATOM   4434 N  NZ  . LYS C 1 72  ? 17.368 41.028 63.641  1.00 14.24 ? 50  LYS C NZ  1 
ATOM   4435 N  N   . ALA C 1 73  ? 19.241 36.905 57.344  1.00 8.24  ? 51  ALA C N   1 
ATOM   4436 C  CA  . ALA C 1 73  ? 19.536 36.476 55.981  1.00 7.91  ? 51  ALA C CA  1 
ATOM   4437 C  C   . ALA C 1 73  ? 19.887 34.999 56.003  1.00 7.68  ? 51  ALA C C   1 
ATOM   4438 O  O   . ALA C 1 73  ? 20.238 34.460 57.054  1.00 7.63  ? 51  ALA C O   1 
ATOM   4439 C  CB  . ALA C 1 73  ? 20.689 37.282 55.399  1.00 8.03  ? 51  ALA C CB  1 
ATOM   4440 N  N   . VAL C 1 74  ? 19.796 34.355 54.844  1.00 7.27  ? 52  VAL C N   1 
ATOM   4441 C  CA  . VAL C 1 74  ? 20.075 32.925 54.732  1.00 7.17  ? 52  VAL C CA  1 
ATOM   4442 C  C   . VAL C 1 74  ? 21.124 32.650 53.656  1.00 6.89  ? 52  VAL C C   1 
ATOM   4443 O  O   . VAL C 1 74  ? 21.008 33.119 52.524  1.00 7.01  ? 52  VAL C O   1 
ATOM   4444 C  CB  . VAL C 1 74  ? 18.804 32.119 54.387  1.00 7.19  ? 52  VAL C CB  1 
ATOM   4445 C  CG1 . VAL C 1 74  ? 19.106 30.624 54.362  1.00 7.24  ? 52  VAL C CG1 1 
ATOM   4446 C  CG2 . VAL C 1 74  ? 17.692 32.419 55.382  1.00 7.29  ? 52  VAL C CG2 1 
ATOM   4447 N  N   . ILE C 1 75  ? 22.138 31.874 54.023  1.00 6.69  ? 53  ILE C N   1 
ATOM   4448 C  CA  . ILE C 1 75  ? 23.113 31.350 53.077  1.00 6.52  ? 53  ILE C CA  1 
ATOM   4449 C  C   . ILE C 1 75  ? 22.836 29.867 52.832  1.00 6.49  ? 53  ILE C C   1 
ATOM   4450 O  O   . ILE C 1 75  ? 22.613 29.107 53.778  1.00 6.34  ? 53  ILE C O   1 
ATOM   4451 C  CB  . ILE C 1 75  ? 24.555 31.480 53.614  1.00 6.49  ? 53  ILE C CB  1 
ATOM   4452 C  CG1 . ILE C 1 75  ? 24.916 32.951 53.822  1.00 6.51  ? 53  ILE C CG1 1 
ATOM   4453 C  CG2 . ILE C 1 75  ? 25.544 30.813 52.659  1.00 6.49  ? 53  ILE C CG2 1 
ATOM   4454 C  CD1 . ILE C 1 75  ? 26.150 33.147 54.685  1.00 6.52  ? 53  ILE C CD1 1 
ATOM   4455 N  N   . VAL C 1 76  ? 22.849 29.463 51.565  1.00 6.46  ? 54  VAL C N   1 
ATOM   4456 C  CA  . VAL C 1 76  ? 22.802 28.046 51.210  1.00 6.53  ? 54  VAL C CA  1 
ATOM   4457 C  C   . VAL C 1 76  ? 24.067 27.691 50.424  1.00 6.70  ? 54  VAL C C   1 
ATOM   4458 O  O   . VAL C 1 76  ? 24.499 28.439 49.553  1.00 6.62  ? 54  VAL C O   1 
ATOM   4459 C  CB  . VAL C 1 76  ? 21.504 27.655 50.457  1.00 6.55  ? 54  VAL C CB  1 
ATOM   4460 C  CG1 . VAL C 1 76  ? 21.367 28.401 49.138  1.00 6.57  ? 54  VAL C CG1 1 
ATOM   4461 C  CG2 . VAL C 1 76  ? 21.436 26.147 50.242  1.00 6.55  ? 54  VAL C CG2 1 
ATOM   4462 N  N   . ARG C 1 77  ? 24.660 26.555 50.777  1.00 6.99  ? 55  ARG C N   1 
ATOM   4463 C  CA  . ARG C 1 77  ? 25.917 26.092 50.193  1.00 7.34  ? 55  ARG C CA  1 
ATOM   4464 C  C   . ARG C 1 77  ? 25.929 24.568 50.229  1.00 7.53  ? 55  ARG C C   1 
ATOM   4465 O  O   . ARG C 1 77  ? 25.082 23.952 50.875  1.00 7.55  ? 55  ARG C O   1 
ATOM   4466 C  CB  . ARG C 1 77  ? 27.104 26.628 51.000  1.00 7.54  ? 55  ARG C CB  1 
ATOM   4467 C  CG  . ARG C 1 77  ? 27.141 26.091 52.421  1.00 7.81  ? 55  ARG C CG  1 
ATOM   4468 C  CD  . ARG C 1 77  ? 28.334 26.550 53.237  1.00 8.13  ? 55  ARG C CD  1 
ATOM   4469 N  NE  . ARG C 1 77  ? 28.352 25.819 54.502  1.00 8.52  ? 55  ARG C NE  1 
ATOM   4470 C  CZ  . ARG C 1 77  ? 29.319 25.876 55.416  1.00 8.75  ? 55  ARG C CZ  1 
ATOM   4471 N  NH1 . ARG C 1 77  ? 30.382 26.652 55.248  1.00 8.89  ? 55  ARG C NH1 1 
ATOM   4472 N  NH2 . ARG C 1 77  ? 29.211 25.147 56.518  1.00 9.04  ? 55  ARG C NH2 1 
ATOM   4473 N  N   . GLY C 1 78  ? 26.898 23.966 49.551  1.00 7.91  ? 56  GLY C N   1 
ATOM   4474 C  CA  . GLY C 1 78  ? 27.083 22.519 49.599  1.00 8.28  ? 56  GLY C CA  1 
ATOM   4475 C  C   . GLY C 1 78  ? 28.259 22.124 50.473  1.00 8.83  ? 56  GLY C C   1 
ATOM   4476 O  O   . GLY C 1 78  ? 29.183 22.914 50.689  1.00 8.99  ? 56  GLY C O   1 
ATOM   4477 N  N   . ALA C 1 79  ? 28.215 20.892 50.964  1.00 9.44  ? 57  ALA C N   1 
ATOM   4478 C  CA  . ALA C 1 79  ? 29.331 20.296 51.702  1.00 10.07 ? 57  ALA C CA  1 
ATOM   4479 C  C   . ALA C 1 79  ? 30.408 19.849 50.731  1.00 10.83 ? 57  ALA C C   1 
ATOM   4480 O  O   . ALA C 1 79  ? 30.117 19.480 49.596  1.00 10.75 ? 57  ALA C O   1 
ATOM   4481 C  CB  . ALA C 1 79  ? 28.846 19.103 52.501  1.00 10.05 ? 57  ALA C CB  1 
ATOM   4482 N  N   . GLY C 1 80  ? 31.656 19.864 51.190  1.00 11.79 ? 58  GLY C N   1 
ATOM   4483 C  CA  . GLY C 1 80  ? 32.767 19.362 50.393  1.00 12.57 ? 58  GLY C CA  1 
ATOM   4484 C  C   . GLY C 1 80  ? 33.073 20.236 49.196  1.00 13.14 ? 58  GLY C C   1 
ATOM   4485 O  O   . GLY C 1 80  ? 33.068 21.454 49.297  1.00 14.02 ? 58  GLY C O   1 
ATOM   4486 N  N   . ASN C 1 81  ? 33.310 19.609 48.052  1.00 13.76 ? 59  ASN C N   1 
ATOM   4487 C  CA  . ASN C 1 81  ? 33.794 20.314 46.869  1.00 13.90 ? 59  ASN C CA  1 
ATOM   4488 C  C   . ASN C 1 81  ? 32.690 20.655 45.865  1.00 12.60 ? 59  ASN C C   1 
ATOM   4489 O  O   . ASN C 1 81  ? 32.974 20.914 44.698  1.00 12.49 ? 59  ASN C O   1 
ATOM   4490 C  CB  . ASN C 1 81  ? 34.903 19.493 46.182  1.00 15.58 ? 59  ASN C CB  1 
ATOM   4491 C  CG  . ASN C 1 81  ? 34.420 18.142 45.665  1.00 17.07 ? 59  ASN C CG  1 
ATOM   4492 O  OD1 . ASN C 1 81  ? 33.259 17.766 45.836  1.00 19.32 ? 59  ASN C OD1 1 
ATOM   4493 N  ND2 . ASN C 1 81  ? 35.321 17.402 45.024  1.00 18.55 ? 59  ASN C ND2 1 
ATOM   4494 N  N   . ALA C 1 82  ? 31.441 20.673 46.324  1.00 11.20 ? 60  ALA C N   1 
ATOM   4495 C  CA  . ALA C 1 82  ? 30.294 20.795 45.421  1.00 10.43 ? 60  ALA C CA  1 
ATOM   4496 C  C   . ALA C 1 82  ? 29.130 21.513 46.086  1.00 9.85  ? 60  ALA C C   1 
ATOM   4497 O  O   . ALA C 1 82  ? 28.971 21.443 47.296  1.00 9.87  ? 60  ALA C O   1 
ATOM   4498 C  CB  . ALA C 1 82  ? 29.844 19.418 44.974  1.00 10.47 ? 60  ALA C CB  1 
ATOM   4499 N  N   . PHE C 1 83  ? 28.318 22.194 45.279  1.00 9.15  ? 61  PHE C N   1 
ATOM   4500 C  CA  . PHE C 1 83  ? 27.029 22.717 45.734  1.00 8.65  ? 61  PHE C CA  1 
ATOM   4501 C  C   . PHE C 1 83  ? 26.041 21.549 45.692  1.00 8.54  ? 61  PHE C C   1 
ATOM   4502 O  O   . PHE C 1 83  ? 25.706 20.987 46.735  1.00 8.32  ? 61  PHE C O   1 
ATOM   4503 C  CB  . PHE C 1 83  ? 26.590 23.909 44.866  1.00 8.45  ? 61  PHE C CB  1 
ATOM   4504 C  CG  . PHE C 1 83  ? 25.321 24.579 45.325  1.00 8.30  ? 61  PHE C CG  1 
ATOM   4505 C  CD1 . PHE C 1 83  ? 25.338 25.509 46.357  1.00 8.31  ? 61  PHE C CD1 1 
ATOM   4506 C  CD2 . PHE C 1 83  ? 24.113 24.315 44.688  1.00 8.25  ? 61  PHE C CD2 1 
ATOM   4507 C  CE1 . PHE C 1 83  ? 24.173 26.143 46.762  1.00 8.33  ? 61  PHE C CE1 1 
ATOM   4508 C  CE2 . PHE C 1 83  ? 22.947 24.944 45.090  1.00 8.26  ? 61  PHE C CE2 1 
ATOM   4509 C  CZ  . PHE C 1 83  ? 22.975 25.860 46.125  1.00 8.28  ? 61  PHE C CZ  1 
ATOM   4510 N  N   . SER C 1 84  ? 25.611 21.157 44.495  1.00 8.31  ? 62  SER C N   1 
ATOM   4511 C  CA  . SER C 1 84  ? 24.780 19.964 44.315  1.00 8.42  ? 62  SER C CA  1 
ATOM   4512 C  C   . SER C 1 84  ? 24.596 19.662 42.831  1.00 8.63  ? 62  SER C C   1 
ATOM   4513 O  O   . SER C 1 84  ? 24.531 20.581 42.015  1.00 8.29  ? 62  SER C O   1 
ATOM   4514 C  CB  . SER C 1 84  ? 23.411 20.131 44.987  1.00 8.38  ? 62  SER C CB  1 
ATOM   4515 O  OG  . SER C 1 84  ? 22.533 19.076 44.632  1.00 8.37  ? 62  SER C OG  1 
ATOM   4516 N  N   . SER C 1 85  ? 24.498 18.372 42.502  1.00 9.07  ? 63  SER C N   1 
ATOM   4517 C  CA  . SER C 1 85  ? 24.227 17.911 41.142  1.00 9.51  ? 63  SER C CA  1 
ATOM   4518 C  C   . SER C 1 85  ? 22.733 17.931 40.785  1.00 9.67  ? 63  SER C C   1 
ATOM   4519 O  O   . SER C 1 85  ? 22.368 17.643 39.637  1.00 9.58  ? 63  SER C O   1 
ATOM   4520 C  CB  . SER C 1 85  ? 24.783 16.494 40.952  1.00 9.68  ? 63  SER C CB  1 
ATOM   4521 O  OG  . SER C 1 85  ? 24.259 15.610 41.921  1.00 10.10 ? 63  SER C OG  1 
ATOM   4522 N  N   . GLY C 1 86  ? 21.877 18.254 41.756  1.00 10.04 ? 64  GLY C N   1 
ATOM   4523 C  CA  . GLY C 1 86  ? 20.435 18.382 41.532  1.00 10.47 ? 64  GLY C CA  1 
ATOM   4524 C  C   . GLY C 1 86  ? 19.636 17.274 42.192  1.00 11.04 ? 64  GLY C C   1 
ATOM   4525 O  O   . GLY C 1 86  ? 20.126 16.596 43.096  1.00 11.22 ? 64  GLY C O   1 
ATOM   4526 N  N   . PHE C 1 87  ? 18.401 17.082 41.738  1.00 11.53 ? 65  PHE C N   1 
ATOM   4527 C  CA  . PHE C 1 87  ? 17.535 16.066 42.330  1.00 12.06 ? 65  PHE C CA  1 
ATOM   4528 C  C   . PHE C 1 87  ? 18.150 14.679 42.106  1.00 12.67 ? 65  PHE C C   1 
ATOM   4529 O  O   . PHE C 1 87  ? 18.773 14.421 41.081  1.00 12.42 ? 65  PHE C O   1 
ATOM   4530 C  CB  . PHE C 1 87  ? 16.097 16.167 41.790  1.00 12.21 ? 65  PHE C CB  1 
ATOM   4531 C  CG  . PHE C 1 87  ? 15.465 17.528 41.980  1.00 12.22 ? 65  PHE C CG  1 
ATOM   4532 C  CD1 . PHE C 1 87  ? 15.459 18.146 43.221  1.00 12.30 ? 65  PHE C CD1 1 
ATOM   4533 C  CD2 . PHE C 1 87  ? 14.867 18.188 40.915  1.00 12.26 ? 65  PHE C CD2 1 
ATOM   4534 C  CE1 . PHE C 1 87  ? 14.885 19.391 43.398  1.00 12.32 ? 65  PHE C CE1 1 
ATOM   4535 C  CE2 . PHE C 1 87  ? 14.295 19.436 41.084  1.00 12.27 ? 65  PHE C CE2 1 
ATOM   4536 C  CZ  . PHE C 1 87  ? 14.307 20.041 42.328  1.00 12.28 ? 65  PHE C CZ  1 
ATOM   4537 N  N   . ASP C 1 88  ? 17.988 13.807 43.098  1.00 13.29 ? 66  ASP C N   1 
ATOM   4538 C  CA  . ASP C 1 88  ? 18.689 12.527 43.176  1.00 13.65 ? 66  ASP C CA  1 
ATOM   4539 C  C   . ASP C 1 88  ? 18.150 11.507 42.168  1.00 13.84 ? 66  ASP C C   1 
ATOM   4540 O  O   . ASP C 1 88  ? 17.036 11.011 42.320  1.00 13.64 ? 66  ASP C O   1 
ATOM   4541 C  CB  . ASP C 1 88  ? 18.541 11.993 44.606  1.00 13.96 ? 66  ASP C CB  1 
ATOM   4542 C  CG  . ASP C 1 88  ? 19.400 10.771 44.890  1.00 14.45 ? 66  ASP C CG  1 
ATOM   4543 O  OD1 . ASP C 1 88  ? 19.746 10.011 43.964  1.00 14.58 ? 66  ASP C OD1 1 
ATOM   4544 O  OD2 . ASP C 1 88  ? 19.700 10.553 46.082  1.00 15.00 ? 66  ASP C OD2 1 
ATOM   4545 N  N   . LEU C 1 89  ? 18.950 11.200 41.149  1.00 14.36 ? 67  LEU C N   1 
ATOM   4546 C  CA  . LEU C 1 89  ? 18.529 10.277 40.088  1.00 14.73 ? 67  LEU C CA  1 
ATOM   4547 C  C   . LEU C 1 89  ? 18.580 8.812  40.509  1.00 14.85 ? 67  LEU C C   1 
ATOM   4548 O  O   . LEU C 1 89  ? 17.765 8.016  40.048  1.00 14.76 ? 67  LEU C O   1 
ATOM   4549 C  CB  . LEU C 1 89  ? 19.361 10.484 38.824  1.00 15.18 ? 67  LEU C CB  1 
ATOM   4550 C  CG  . LEU C 1 89  ? 19.187 11.850 38.154  1.00 15.36 ? 67  LEU C CG  1 
ATOM   4551 C  CD1 . LEU C 1 89  ? 20.048 11.915 36.904  1.00 15.61 ? 67  LEU C CD1 1 
ATOM   4552 C  CD2 . LEU C 1 89  ? 17.728 12.130 37.818  1.00 15.59 ? 67  LEU C CD2 1 
ATOM   4553 N  N   . LYS C 1 90  ? 19.535 8.458  41.366  1.00 14.91 ? 68  LYS C N   1 
ATOM   4554 C  CA  . LYS C 1 90  ? 19.614 7.105  41.918  1.00 15.37 ? 68  LYS C CA  1 
ATOM   4555 C  C   . LYS C 1 90  ? 18.356 6.775  42.725  1.00 14.64 ? 68  LYS C C   1 
ATOM   4556 O  O   . LYS C 1 90  ? 17.806 5.682  42.613  1.00 14.53 ? 68  LYS C O   1 
ATOM   4557 C  CB  . LYS C 1 90  ? 20.867 6.964  42.782  1.00 16.15 ? 68  LYS C CB  1 
ATOM   4558 C  CG  . LYS C 1 90  ? 21.108 5.576  43.355  1.00 17.19 ? 68  LYS C CG  1 
ATOM   4559 C  CD  . LYS C 1 90  ? 22.466 5.520  44.042  1.00 18.34 ? 68  LYS C CD  1 
ATOM   4560 C  CE  . LYS C 1 90  ? 22.615 4.306  44.945  1.00 19.34 ? 68  LYS C CE  1 
ATOM   4561 N  NZ  . LYS C 1 90  ? 22.986 3.090  44.177  1.00 20.30 ? 68  LYS C NZ  1 
ATOM   4562 N  N   . ALA C 1 91  ? 17.899 7.734  43.523  1.00 14.12 ? 69  ALA C N   1 
ATOM   4563 C  CA  . ALA C 1 91  ? 16.665 7.578  44.287  1.00 13.89 ? 69  ALA C CA  1 
ATOM   4564 C  C   . ALA C 1 91  ? 15.465 7.437  43.347  1.00 14.02 ? 69  ALA C C   1 
ATOM   4565 O  O   . ALA C 1 91  ? 14.554 6.646  43.599  1.00 13.43 ? 69  ALA C O   1 
ATOM   4566 C  CB  . ALA C 1 91  ? 16.469 8.757  45.228  1.00 14.02 ? 69  ALA C CB  1 
ATOM   4567 N  N   . GLN C 1 92  ? 15.474 8.204  42.260  1.00 14.12 ? 70  GLN C N   1 
ATOM   4568 C  CA  . GLN C 1 92  ? 14.403 8.132  41.271  1.00 14.66 ? 70  GLN C CA  1 
ATOM   4569 C  C   . GLN C 1 92  ? 14.402 6.780  40.554  1.00 15.99 ? 70  GLN C C   1 
ATOM   4570 O  O   . GLN C 1 92  ? 13.340 6.198  40.333  1.00 16.22 ? 70  GLN C O   1 
ATOM   4571 C  CB  . GLN C 1 92  ? 14.540 9.272  40.257  1.00 13.98 ? 70  GLN C CB  1 
ATOM   4572 C  CG  . GLN C 1 92  ? 13.332 9.444  39.357  1.00 13.65 ? 70  GLN C CG  1 
ATOM   4573 C  CD  . GLN C 1 92  ? 13.553 10.495 38.289  1.00 13.09 ? 70  GLN C CD  1 
ATOM   4574 O  OE1 . GLN C 1 92  ? 14.072 11.585 38.562  1.00 13.71 ? 70  GLN C OE1 1 
ATOM   4575 N  NE2 . GLN C 1 92  ? 13.157 10.179 37.069  1.00 12.32 ? 70  GLN C NE2 1 
HETATM 4576 N  N   . MSE C 1 93  ? 15.593 6.299  40.199  1.00 17.96 ? 71  MSE C N   1 
HETATM 4577 C  CA  . MSE C 1 93  ? 15.779 4.983  39.560  1.00 20.27 ? 71  MSE C CA  1 
HETATM 4578 C  C   . MSE C 1 93  ? 15.170 3.891  40.397  1.00 19.89 ? 71  MSE C C   1 
HETATM 4579 O  O   . MSE C 1 93  ? 14.498 2.997  39.878  1.00 19.30 ? 71  MSE C O   1 
HETATM 4580 C  CB  . MSE C 1 93  ? 17.282 4.722  39.392  1.00 23.15 ? 71  MSE C CB  1 
HETATM 4581 C  CG  . MSE C 1 93  ? 17.640 3.398  38.705  1.00 26.39 ? 71  MSE C CG  1 
HETATM 4582 SE SE  . MSE C 1 93  ? 19.593 3.060  38.734  1.00 33.76 ? 71  MSE C SE  1 
HETATM 4583 C  CE  . MSE C 1 93  ? 20.180 4.911  38.424  1.00 31.93 ? 71  MSE C CE  1 
ATOM   4584 N  N   . GLU C 1 94  ? 15.400 3.961  41.704  1.00 19.49 ? 72  GLU C N   1 
ATOM   4585 C  CA  . GLU C 1 94  ? 14.923 2.934  42.627  1.00 19.71 ? 72  GLU C CA  1 
ATOM   4586 C  C   . GLU C 1 94  ? 13.418 3.041  42.893  1.00 18.76 ? 72  GLU C C   1 
ATOM   4587 O  O   . GLU C 1 94  ? 12.730 2.024  42.963  1.00 18.69 ? 72  GLU C O   1 
ATOM   4588 C  CB  . GLU C 1 94  ? 15.722 2.993  43.939  1.00 20.77 ? 72  GLU C CB  1 
ATOM   4589 C  CG  . GLU C 1 94  ? 17.179 2.575  43.767  1.00 22.31 ? 72  GLU C CG  1 
ATOM   4590 C  CD  . GLU C 1 94  ? 18.058 2.874  44.972  1.00 23.49 ? 72  GLU C CD  1 
ATOM   4591 O  OE1 . GLU C 1 94  ? 17.594 3.523  45.935  1.00 24.85 ? 72  GLU C OE1 1 
ATOM   4592 O  OE2 . GLU C 1 94  ? 19.234 2.459  44.950  1.00 25.29 ? 72  GLU C OE2 1 
ATOM   4593 N  N   . ALA C 1 95  ? 12.908 4.265  43.017  1.00 17.75 ? 73  ALA C N   1 
ATOM   4594 C  CA  . ALA C 1 95  ? 11.490 4.484  43.333  1.00 17.66 ? 73  ALA C CA  1 
ATOM   4595 C  C   . ALA C 1 95  ? 10.552 4.199  42.155  1.00 17.53 ? 73  ALA C C   1 
ATOM   4596 O  O   . ALA C 1 95  ? 9.392  3.841  42.362  1.00 17.80 ? 73  ALA C O   1 
ATOM   4597 C  CB  . ALA C 1 95  ? 11.273 5.900  43.847  1.00 17.69 ? 73  ALA C CB  1 
ATOM   4598 N  N   . ARG C 1 96  ? 11.051 4.366  40.931  1.00 17.18 ? 74  ARG C N   1 
ATOM   4599 C  CA  . ARG C 1 96  ? 10.268 4.116  39.717  1.00 17.32 ? 74  ARG C CA  1 
ATOM   4600 C  C   . ARG C 1 96  ? 8.873  4.759  39.751  1.00 15.83 ? 74  ARG C C   1 
ATOM   4601 O  O   . ARG C 1 96  ? 7.869  4.073  39.546  1.00 15.71 ? 74  ARG C O   1 
ATOM   4602 C  CB  . ARG C 1 96  ? 10.110 2.608  39.477  1.00 18.91 ? 74  ARG C CB  1 
ATOM   4603 C  CG  . ARG C 1 96  ? 11.400 1.823  39.299  1.00 20.67 ? 74  ARG C CG  1 
ATOM   4604 C  CD  . ARG C 1 96  ? 11.087 0.330  39.285  1.00 22.22 ? 74  ARG C CD  1 
ATOM   4605 N  NE  . ARG C 1 96  ? 12.199 -0.495 38.805  1.00 23.83 ? 74  ARG C NE  1 
ATOM   4606 C  CZ  . ARG C 1 96  ? 12.397 -0.869 37.538  1.00 24.42 ? 74  ARG C CZ  1 
ATOM   4607 N  NH1 . ARG C 1 96  ? 11.572 -0.498 36.564  1.00 25.03 ? 74  ARG C NH1 1 
ATOM   4608 N  NH2 . ARG C 1 96  ? 13.447 -1.624 37.240  1.00 25.71 ? 74  ARG C NH2 1 
ATOM   4609 N  N   . PRO C 1 97  ? 8.798  6.075  40.020  1.00 14.25 ? 75  PRO C N   1 
ATOM   4610 C  CA  . PRO C 1 97  ? 7.479  6.706  39.939  1.00 13.62 ? 75  PRO C CA  1 
ATOM   4611 C  C   . PRO C 1 97  ? 6.907  6.555  38.537  1.00 12.79 ? 75  PRO C C   1 
ATOM   4612 O  O   . PRO C 1 97  ? 7.629  6.718  37.552  1.00 12.85 ? 75  PRO C O   1 
ATOM   4613 C  CB  . PRO C 1 97  ? 7.766  8.179  40.257  1.00 13.74 ? 75  PRO C CB  1 
ATOM   4614 C  CG  . PRO C 1 97  ? 9.208  8.367  39.950  1.00 13.84 ? 75  PRO C CG  1 
ATOM   4615 C  CD  . PRO C 1 97  ? 9.867  7.055  40.270  1.00 14.10 ? 75  PRO C CD  1 
ATOM   4616 N  N   . ALA C 1 98  ? 5.623  6.233  38.446  1.00 11.84 ? 76  ALA C N   1 
ATOM   4617 C  CA  . ALA C 1 98  ? 5.008  5.961  37.160  1.00 11.26 ? 76  ALA C CA  1 
ATOM   4618 C  C   . ALA C 1 98  ? 3.663  6.649  37.059  1.00 10.43 ? 76  ALA C C   1 
ATOM   4619 O  O   . ALA C 1 98  ? 2.753  6.359  37.831  1.00 10.67 ? 76  ALA C O   1 
ATOM   4620 C  CB  . ALA C 1 98  ? 4.844  4.465  36.966  1.00 11.42 ? 76  ALA C CB  1 
ATOM   4621 N  N   . GLY C 1 99  ? 3.551  7.565  36.106  1.00 9.52  ? 77  GLY C N   1 
ATOM   4622 C  CA  . GLY C 1 99  ? 2.278  8.182  35.782  1.00 9.00  ? 77  GLY C CA  1 
ATOM   4623 C  C   . GLY C 1 99  ? 2.099  9.553  36.397  1.00 8.36  ? 77  GLY C C   1 
ATOM   4624 O  O   . GLY C 1 99  ? 2.859  9.969  37.270  1.00 8.19  ? 77  GLY C O   1 
ATOM   4625 N  N   . VAL C 1 100 ? 1.063  10.244 35.942  1.00 7.89  ? 78  VAL C N   1 
ATOM   4626 C  CA  . VAL C 1 100 ? 0.800  11.621 36.364  1.00 7.63  ? 78  VAL C CA  1 
ATOM   4627 C  C   . VAL C 1 100 ? 0.577  11.749 37.872  1.00 7.70  ? 78  VAL C C   1 
ATOM   4628 O  O   . VAL C 1 100 ? 1.155  12.619 38.519  1.00 7.48  ? 78  VAL C O   1 
ATOM   4629 C  CB  . VAL C 1 100 ? -0.421 12.204 35.611  1.00 7.46  ? 78  VAL C CB  1 
ATOM   4630 C  CG1 . VAL C 1 100 ? -0.864 13.525 36.232  1.00 7.43  ? 78  VAL C CG1 1 
ATOM   4631 C  CG2 . VAL C 1 100 ? -0.098 12.390 34.133  1.00 7.44  ? 78  VAL C CG2 1 
ATOM   4632 N  N   . ASP C 1 101 ? -0.276 10.904 38.440  1.00 7.85  ? 79  ASP C N   1 
ATOM   4633 C  CA  . ASP C 1 101 ? -0.635 11.059 39.848  1.00 8.04  ? 79  ASP C CA  1 
ATOM   4634 C  C   . ASP C 1 101 ? 0.551  10.818 40.793  1.00 7.98  ? 79  ASP C C   1 
ATOM   4635 O  O   . ASP C 1 101 ? 0.649  11.458 41.844  1.00 8.23  ? 79  ASP C O   1 
ATOM   4636 C  CB  . ASP C 1 101 ? -1.848 10.186 40.202  1.00 8.33  ? 79  ASP C CB  1 
ATOM   4637 C  CG  . ASP C 1 101 ? -3.138 10.698 39.572  1.00 8.55  ? 79  ASP C CG  1 
ATOM   4638 O  OD1 . ASP C 1 101 ? -3.190 11.872 39.138  1.00 8.64  ? 79  ASP C OD1 1 
ATOM   4639 O  OD2 . ASP C 1 101 ? -4.111 9.919  39.498  1.00 9.15  ? 79  ASP C OD2 1 
ATOM   4640 N  N   . ALA C 1 102 ? 1.465  9.935  40.398  1.00 7.75  ? 80  ALA C N   1 
ATOM   4641 C  CA  . ALA C 1 102 ? 2.694  9.686  41.164  1.00 7.65  ? 80  ALA C CA  1 
ATOM   4642 C  C   . ALA C 1 102 ? 3.660  10.863 41.058  1.00 7.55  ? 80  ALA C C   1 
ATOM   4643 O  O   . ALA C 1 102 ? 4.294  11.256 42.044  1.00 7.54  ? 80  ALA C O   1 
ATOM   4644 C  CB  . ALA C 1 102 ? 3.366  8.414  40.675  1.00 7.69  ? 80  ALA C CB  1 
ATOM   4645 N  N   . TRP C 1 103 ? 3.767  11.426 39.860  1.00 7.28  ? 81  TRP C N   1 
ATOM   4646 C  CA  . TRP C 1 103 ? 4.715  12.509 39.610  1.00 7.19  ? 81  TRP C CA  1 
ATOM   4647 C  C   . TRP C 1 103 ? 4.270  13.858 40.170  1.00 7.08  ? 81  TRP C C   1 
ATOM   4648 O  O   . TRP C 1 103 ? 5.112  14.670 40.550  1.00 6.95  ? 81  TRP C O   1 
ATOM   4649 C  CB  . TRP C 1 103 ? 5.016  12.617 38.120  1.00 7.30  ? 81  TRP C CB  1 
ATOM   4650 C  CG  . TRP C 1 103 ? 6.177  11.772 37.709  1.00 7.39  ? 81  TRP C CG  1 
ATOM   4651 C  CD1 . TRP C 1 103 ? 6.139  10.518 37.160  1.00 7.42  ? 81  TRP C CD1 1 
ATOM   4652 C  CD2 . TRP C 1 103 ? 7.556  12.115 37.830  1.00 7.51  ? 81  TRP C CD2 1 
ATOM   4653 N  NE1 . TRP C 1 103 ? 7.417  10.067 36.923  1.00 7.53  ? 81  TRP C NE1 1 
ATOM   4654 C  CE2 . TRP C 1 103 ? 8.304  11.032 37.322  1.00 7.52  ? 81  TRP C CE2 1 
ATOM   4655 C  CE3 . TRP C 1 103 ? 8.236  13.243 38.306  1.00 7.59  ? 81  TRP C CE3 1 
ATOM   4656 C  CZ2 . TRP C 1 103 ? 9.694  11.041 37.289  1.00 7.65  ? 81  TRP C CZ2 1 
ATOM   4657 C  CZ3 . TRP C 1 103 ? 9.612  13.254 38.261  1.00 7.72  ? 81  TRP C CZ3 1 
ATOM   4658 C  CH2 . TRP C 1 103 ? 10.329 12.159 37.760  1.00 7.70  ? 81  TRP C CH2 1 
ATOM   4659 N  N   . ARG C 1 104 ? 2.961  14.097 40.235  1.00 6.96  ? 82  ARG C N   1 
ATOM   4660 C  CA  . ARG C 1 104 ? 2.453  15.398 40.693  1.00 7.02  ? 82  ARG C CA  1 
ATOM   4661 C  C   . ARG C 1 104 ? 3.032  15.860 42.043  1.00 7.05  ? 82  ARG C C   1 
ATOM   4662 O  O   . ARG C 1 104 ? 3.567  16.972 42.121  1.00 6.73  ? 82  ARG C O   1 
ATOM   4663 C  CB  . ARG C 1 104 ? 0.918  15.444 40.704  1.00 7.09  ? 82  ARG C CB  1 
ATOM   4664 C  CG  . ARG C 1 104 ? 0.366  16.807 41.122  1.00 7.21  ? 82  ARG C CG  1 
ATOM   4665 C  CD  . ARG C 1 104 ? -1.149 16.843 41.186  1.00 7.41  ? 82  ARG C CD  1 
ATOM   4666 N  NE  . ARG C 1 104 ? -1.763 16.849 39.859  1.00 7.56  ? 82  ARG C NE  1 
ATOM   4667 C  CZ  . ARG C 1 104 ? -2.351 15.810 39.272  1.00 7.76  ? 82  ARG C CZ  1 
ATOM   4668 N  NH1 . ARG C 1 104 ? -2.413 14.619 39.866  1.00 7.92  ? 82  ARG C NH1 1 
ATOM   4669 N  NH2 . ARG C 1 104 ? -2.891 15.965 38.066  1.00 7.79  ? 82  ARG C NH2 1 
ATOM   4670 N  N   . PRO C 1 105 ? 2.942  15.023 43.103  1.00 7.17  ? 83  PRO C N   1 
ATOM   4671 C  CA  . PRO C 1 105 ? 3.496  15.479 44.389  1.00 7.44  ? 83  PRO C CA  1 
ATOM   4672 C  C   . PRO C 1 105 ? 5.023  15.610 44.404  1.00 7.69  ? 83  PRO C C   1 
ATOM   4673 O  O   . PRO C 1 105 ? 5.557  16.444 45.140  1.00 8.04  ? 83  PRO C O   1 
ATOM   4674 C  CB  . PRO C 1 105 ? 3.037  14.398 45.380  1.00 7.38  ? 83  PRO C CB  1 
ATOM   4675 C  CG  . PRO C 1 105 ? 2.786  13.196 44.542  1.00 7.33  ? 83  PRO C CG  1 
ATOM   4676 C  CD  . PRO C 1 105 ? 2.271  13.718 43.237  1.00 7.25  ? 83  PRO C CD  1 
ATOM   4677 N  N   . LEU C 1 106 ? 5.714  14.809 43.597  1.00 7.84  ? 84  LEU C N   1 
ATOM   4678 C  CA  . LEU C 1 106 ? 7.174  14.890 43.508  1.00 8.08  ? 84  LEU C CA  1 
ATOM   4679 C  C   . LEU C 1 106 ? 7.585  16.237 42.933  1.00 7.98  ? 84  LEU C C   1 
ATOM   4680 O  O   . LEU C 1 106 ? 8.430  16.932 43.495  1.00 7.96  ? 84  LEU C O   1 
ATOM   4681 C  CB  . LEU C 1 106 ? 7.739  13.766 42.633  1.00 8.38  ? 84  LEU C CB  1 
ATOM   4682 C  CG  . LEU C 1 106 ? 7.521  12.340 43.145  1.00 8.63  ? 84  LEU C CG  1 
ATOM   4683 C  CD1 . LEU C 1 106 ? 7.982  11.347 42.096  1.00 8.73  ? 84  LEU C CD1 1 
ATOM   4684 C  CD2 . LEU C 1 106 ? 8.241  12.112 44.462  1.00 8.79  ? 84  LEU C CD2 1 
ATOM   4685 N  N   . LEU C 1 107 ? 6.967  16.611 41.819  1.00 7.85  ? 85  LEU C N   1 
ATOM   4686 C  CA  . LEU C 1 107 ? 7.278  17.884 41.175  1.00 7.79  ? 85  LEU C CA  1 
ATOM   4687 C  C   . LEU C 1 107 ? 6.834  19.068 42.025  1.00 8.07  ? 85  LEU C C   1 
ATOM   4688 O  O   . LEU C 1 107 ? 7.513  20.090 42.060  1.00 7.74  ? 85  LEU C O   1 
ATOM   4689 C  CB  . LEU C 1 107 ? 6.646  17.954 39.782  1.00 7.79  ? 85  LEU C CB  1 
ATOM   4690 C  CG  . LEU C 1 107 ? 7.128  16.876 38.808  1.00 7.76  ? 85  LEU C CG  1 
ATOM   4691 C  CD1 . LEU C 1 107 ? 6.396  16.963 37.482  1.00 7.80  ? 85  LEU C CD1 1 
ATOM   4692 C  CD2 . LEU C 1 107 ? 8.631  16.979 38.592  1.00 7.81  ? 85  LEU C CD2 1 
ATOM   4693 N  N   . ARG C 1 108 ? 5.707  18.935 42.720  1.00 8.38  ? 86  ARG C N   1 
ATOM   4694 C  CA  . ARG C 1 108 ? 5.214  20.033 43.559  1.00 8.98  ? 86  ARG C CA  1 
ATOM   4695 C  C   . ARG C 1 108 ? 6.188  20.330 44.701  1.00 9.06  ? 86  ARG C C   1 
ATOM   4696 O  O   . ARG C 1 108 ? 6.457  21.491 45.009  1.00 8.61  ? 86  ARG C O   1 
ATOM   4697 C  CB  . ARG C 1 108 ? 3.814  19.732 44.105  1.00 9.64  ? 86  ARG C CB  1 
ATOM   4698 C  CG  . ARG C 1 108 ? 3.259  20.772 45.075  1.00 10.22 ? 86  ARG C CG  1 
ATOM   4699 C  CD  . ARG C 1 108 ? 3.388  22.222 44.604  1.00 11.06 ? 86  ARG C CD  1 
ATOM   4700 N  NE  . ARG C 1 108 ? 2.628  22.490 43.410  1.00 11.62 ? 86  ARG C NE  1 
ATOM   4701 C  CZ  . ARG C 1 108 ? 2.622  23.642 42.730  1.00 11.72 ? 86  ARG C CZ  1 
ATOM   4702 N  NH1 . ARG C 1 108 ? 3.347  24.696 43.094  1.00 11.99 ? 86  ARG C NH1 1 
ATOM   4703 N  NH2 . ARG C 1 108 ? 1.871  23.729 41.656  1.00 11.81 ? 86  ARG C NH2 1 
ATOM   4704 N  N   . LYS C 1 109 ? 6.717  19.279 45.316  1.00 9.31  ? 87  LYS C N   1 
ATOM   4705 C  CA  . LYS C 1 109 ? 7.699  19.432 46.384  1.00 9.82  ? 87  LYS C CA  1 
ATOM   4706 C  C   . LYS C 1 109 ? 9.018  20.011 45.860  1.00 9.37  ? 87  LYS C C   1 
ATOM   4707 O  O   . LYS C 1 109 ? 9.599  20.891 46.496  1.00 9.17  ? 87  LYS C O   1 
ATOM   4708 C  CB  . LYS C 1 109 ? 7.935  18.088 47.060  1.00 10.57 ? 87  LYS C CB  1 
ATOM   4709 C  CG  . LYS C 1 109 ? 8.803  18.143 48.300  1.00 11.63 ? 87  LYS C CG  1 
ATOM   4710 C  CD  . LYS C 1 109 ? 8.923  16.750 48.888  1.00 12.64 ? 87  LYS C CD  1 
ATOM   4711 C  CE  . LYS C 1 109 ? 9.787  16.738 50.127  1.00 13.55 ? 87  LYS C CE  1 
ATOM   4712 N  NZ  . LYS C 1 109 ? 10.119 15.351 50.524  1.00 14.25 ? 87  LYS C NZ  1 
ATOM   4713 N  N   . ASP C 1 110 ? 9.482  19.516 44.713  1.00 9.13  ? 88  ASP C N   1 
ATOM   4714 C  CA  . ASP C 1 110 ? 10.673 20.058 44.040  1.00 9.16  ? 88  ASP C CA  1 
ATOM   4715 C  C   . ASP C 1 110 ? 10.525 21.556 43.828  1.00 8.44  ? 88  ASP C C   1 
ATOM   4716 O  O   . ASP C 1 110 ? 11.395 22.353 44.196  1.00 8.31  ? 88  ASP C O   1 
ATOM   4717 C  CB  . ASP C 1 110 ? 10.848 19.454 42.640  1.00 9.89  ? 88  ASP C CB  1 
ATOM   4718 C  CG  . ASP C 1 110 ? 11.339 18.025 42.642  1.00 10.80 ? 88  ASP C CG  1 
ATOM   4719 O  OD1 . ASP C 1 110 ? 11.892 17.539 43.647  1.00 11.90 ? 88  ASP C OD1 1 
ATOM   4720 O  OD2 . ASP C 1 110 ? 11.174 17.380 41.583  1.00 12.00 ? 88  ASP C OD2 1 
ATOM   4721 N  N   . PHE C 1 111 ? 9.417  21.918 43.192  1.00 7.72  ? 89  PHE C N   1 
ATOM   4722 C  CA  . PHE C 1 111 ? 9.144  23.299 42.802  1.00 7.34  ? 89  PHE C CA  1 
ATOM   4723 C  C   . PHE C 1 111 ? 9.006  24.203 44.022  1.00 7.27  ? 89  PHE C C   1 
ATOM   4724 O  O   . PHE C 1 111 ? 9.655  25.247 44.108  1.00 7.10  ? 89  PHE C O   1 
ATOM   4725 C  CB  . PHE C 1 111 ? 7.865  23.332 41.960  1.00 7.16  ? 89  PHE C CB  1 
ATOM   4726 C  CG  . PHE C 1 111 ? 7.469  24.701 41.482  1.00 7.04  ? 89  PHE C CG  1 
ATOM   4727 C  CD1 . PHE C 1 111 ? 6.719  25.545 42.290  1.00 7.04  ? 89  PHE C CD1 1 
ATOM   4728 C  CD2 . PHE C 1 111 ? 7.817  25.131 40.213  1.00 6.95  ? 89  PHE C CD2 1 
ATOM   4729 C  CE1 . PHE C 1 111 ? 6.338  26.798 41.848  1.00 6.98  ? 89  PHE C CE1 1 
ATOM   4730 C  CE2 . PHE C 1 111 ? 7.441  26.382 39.762  1.00 6.96  ? 89  PHE C CE2 1 
ATOM   4731 C  CZ  . PHE C 1 111 ? 6.699  27.219 40.583  1.00 7.00  ? 89  PHE C CZ  1 
ATOM   4732 N  N   . ASP C 1 112 ? 8.166  23.806 44.969  1.00 7.30  ? 90  ASP C N   1 
ATOM   4733 C  CA  . ASP C 1 112 ? 7.909  24.660 46.127  1.00 7.49  ? 90  ASP C CA  1 
ATOM   4734 C  C   . ASP C 1 112 ? 9.145  24.826 46.997  1.00 7.31  ? 90  ASP C C   1 
ATOM   4735 O  O   . ASP C 1 112 ? 9.332  25.883 47.596  1.00 7.24  ? 90  ASP C O   1 
ATOM   4736 C  CB  . ASP C 1 112 ? 6.746  24.126 46.964  1.00 7.89  ? 90  ASP C CB  1 
ATOM   4737 C  CG  . ASP C 1 112 ? 5.397  24.337 46.303  1.00 8.39  ? 90  ASP C CG  1 
ATOM   4738 O  OD1 . ASP C 1 112 ? 5.274  25.167 45.380  1.00 8.87  ? 90  ASP C OD1 1 
ATOM   4739 O  OD2 . ASP C 1 112 ? 4.434  23.676 46.735  1.00 9.33  ? 90  ASP C OD2 1 
ATOM   4740 N  N   . THR C 1 113 ? 9.995  23.803 47.054  1.00 7.08  ? 91  THR C N   1 
ATOM   4741 C  CA  . THR C 1 113 ? 11.218 23.896 47.858  1.00 7.10  ? 91  THR C CA  1 
ATOM   4742 C  C   . THR C 1 113 ? 12.187 24.894 47.233  1.00 7.11  ? 91  THR C C   1 
ATOM   4743 O  O   . THR C 1 113 ? 12.703 25.774 47.915  1.00 7.00  ? 91  THR C O   1 
ATOM   4744 C  CB  . THR C 1 113 ? 11.893 22.528 48.046  1.00 7.17  ? 91  THR C CB  1 
ATOM   4745 O  OG1 . THR C 1 113 ? 10.951 21.611 48.612  1.00 7.31  ? 91  THR C OG1 1 
ATOM   4746 C  CG2 . THR C 1 113 ? 13.108 22.653 48.980  1.00 7.17  ? 91  THR C CG2 1 
ATOM   4747 N  N   . VAL C 1 114 ? 12.421 24.765 45.931  1.00 7.06  ? 92  VAL C N   1 
ATOM   4748 C  CA  . VAL C 1 114 ? 13.236 25.743 45.208  1.00 7.26  ? 92  VAL C CA  1 
ATOM   4749 C  C   . VAL C 1 114 ? 12.691 27.161 45.410  1.00 7.53  ? 92  VAL C C   1 
ATOM   4750 O  O   . VAL C 1 114 ? 13.449 28.087 45.693  1.00 7.13  ? 92  VAL C O   1 
ATOM   4751 C  CB  . VAL C 1 114 ? 13.314 25.408 43.697  1.00 7.18  ? 92  VAL C CB  1 
ATOM   4752 C  CG1 . VAL C 1 114 ? 13.818 26.596 42.884  1.00 7.18  ? 92  VAL C CG1 1 
ATOM   4753 C  CG2 . VAL C 1 114 ? 14.205 24.190 43.470  1.00 7.18  ? 92  VAL C CG2 1 
HETATM 4754 N  N   . MSE C 1 115 ? 11.377 27.327 45.295  1.00 8.05  ? 93  MSE C N   1 
HETATM 4755 C  CA  . MSE C 1 115 ? 10.781 28.662 45.372  1.00 8.83  ? 93  MSE C CA  1 
HETATM 4756 C  C   . MSE C 1 115 ? 10.757 29.245 46.770  1.00 8.23  ? 93  MSE C C   1 
HETATM 4757 O  O   . MSE C 1 115 ? 10.492 30.432 46.921  1.00 8.04  ? 93  MSE C O   1 
HETATM 4758 C  CB  . MSE C 1 115 ? 9.394  28.680 44.722  1.00 10.35 ? 93  MSE C CB  1 
HETATM 4759 C  CG  . MSE C 1 115 ? 9.477  28.437 43.211  1.00 11.99 ? 93  MSE C CG  1 
HETATM 4760 SE SE  . MSE C 1 115 ? 10.532 29.795 42.240  1.00 16.56 ? 93  MSE C SE  1 
HETATM 4761 C  CE  . MSE C 1 115 ? 9.349  31.341 42.533  1.00 14.57 ? 93  MSE C CE  1 
ATOM   4762 N  N   . ARG C 1 116 ? 11.057 28.447 47.797  1.00 7.64  ? 94  ARG C N   1 
ATOM   4763 C  CA  . ARG C 1 116 ? 11.248 28.992 49.150  1.00 7.44  ? 94  ARG C CA  1 
ATOM   4764 C  C   . ARG C 1 116 ? 12.288 30.107 49.147  1.00 7.08  ? 94  ARG C C   1 
ATOM   4765 O  O   . ARG C 1 116 ? 12.182 31.063 49.905  1.00 6.96  ? 94  ARG C O   1 
ATOM   4766 C  CB  . ARG C 1 116 ? 11.724 27.928 50.143  1.00 7.48  ? 94  ARG C CB  1 
ATOM   4767 C  CG  . ARG C 1 116 ? 10.761 26.803 50.475  1.00 7.63  ? 94  ARG C CG  1 
ATOM   4768 C  CD  . ARG C 1 116 ? 9.481  27.265 51.151  1.00 7.64  ? 94  ARG C CD  1 
ATOM   4769 N  NE  . ARG C 1 116 ? 9.672  27.958 52.434  1.00 7.70  ? 94  ARG C NE  1 
ATOM   4770 C  CZ  . ARG C 1 116 ? 9.658  27.388 53.640  1.00 7.78  ? 94  ARG C CZ  1 
ATOM   4771 N  NH1 . ARG C 1 116 ? 9.505  26.081 53.787  1.00 7.85  ? 94  ARG C NH1 1 
ATOM   4772 N  NH2 . ARG C 1 116 ? 9.812  28.141 54.721  1.00 7.91  ? 94  ARG C NH2 1 
ATOM   4773 N  N   . PHE C 1 117 ? 13.307 29.967 48.307  1.00 6.84  ? 95  PHE C N   1 
ATOM   4774 C  CA  . PHE C 1 117 ? 14.428 30.900 48.318  1.00 6.79  ? 95  PHE C CA  1 
ATOM   4775 C  C   . PHE C 1 117 ? 14.080 32.221 47.642  1.00 6.91  ? 95  PHE C C   1 
ATOM   4776 O  O   . PHE C 1 117 ? 14.669 33.253 47.955  1.00 6.86  ? 95  PHE C O   1 
ATOM   4777 C  CB  . PHE C 1 117 ? 15.658 30.227 47.726  1.00 6.72  ? 95  PHE C CB  1 
ATOM   4778 C  CG  . PHE C 1 117 ? 16.147 29.095 48.573  1.00 6.64  ? 95  PHE C CG  1 
ATOM   4779 C  CD1 . PHE C 1 117 ? 17.086 29.317 49.566  1.00 6.64  ? 95  PHE C CD1 1 
ATOM   4780 C  CD2 . PHE C 1 117 ? 15.607 27.832 48.444  1.00 6.64  ? 95  PHE C CD2 1 
ATOM   4781 C  CE1 . PHE C 1 117 ? 17.505 28.288 50.382  1.00 6.60  ? 95  PHE C CE1 1 
ATOM   4782 C  CE2 . PHE C 1 117 ? 16.022 26.797 49.256  1.00 6.68  ? 95  PHE C CE2 1 
ATOM   4783 C  CZ  . PHE C 1 117 ? 16.976 27.021 50.220  1.00 6.59  ? 95  PHE C CZ  1 
ATOM   4784 N  N   . TRP C 1 118 ? 13.090 32.192 46.754  1.00 6.96  ? 96  TRP C N   1 
ATOM   4785 C  CA  . TRP C 1 118 ? 12.555 33.414 46.150  1.00 7.15  ? 96  TRP C CA  1 
ATOM   4786 C  C   . TRP C 1 118 ? 11.608 34.107 47.129  1.00 7.17  ? 96  TRP C C   1 
ATOM   4787 O  O   . TRP C 1 118 ? 11.752 35.296 47.411  1.00 7.03  ? 96  TRP C O   1 
ATOM   4788 C  CB  . TRP C 1 118 ? 11.813 33.093 44.840  1.00 7.35  ? 96  TRP C CB  1 
ATOM   4789 C  CG  . TRP C 1 118 ? 11.060 34.277 44.263  1.00 7.65  ? 96  TRP C CG  1 
ATOM   4790 C  CD1 . TRP C 1 118 ? 9.754  34.599 44.484  1.00 7.79  ? 96  TRP C CD1 1 
ATOM   4791 C  CD2 . TRP C 1 118 ? 11.577 35.283 43.385  1.00 7.94  ? 96  TRP C CD2 1 
ATOM   4792 N  NE1 . TRP C 1 118 ? 9.425  35.742 43.802  1.00 8.05  ? 96  TRP C NE1 1 
ATOM   4793 C  CE2 . TRP C 1 118 ? 10.526 36.188 43.123  1.00 8.02  ? 96  TRP C CE2 1 
ATOM   4794 C  CE3 . TRP C 1 118 ? 12.825 35.507 42.794  1.00 8.17  ? 96  TRP C CE3 1 
ATOM   4795 C  CZ2 . TRP C 1 118 ? 10.686 37.300 42.295  1.00 8.14  ? 96  TRP C CZ2 1 
ATOM   4796 C  CZ3 . TRP C 1 118 ? 12.985 36.616 41.970  1.00 8.32  ? 96  TRP C CZ3 1 
ATOM   4797 C  CH2 . TRP C 1 118 ? 11.919 37.500 41.730  1.00 8.26  ? 96  TRP C CH2 1 
ATOM   4798 N  N   . HIS C 1 119 ? 10.643 33.353 47.643  1.00 7.22  ? 97  HIS C N   1 
ATOM   4799 C  CA  . HIS C 1 119 ? 9.585  33.915 48.484  1.00 7.41  ? 97  HIS C CA  1 
ATOM   4800 C  C   . HIS C 1 119 ? 10.028 34.269 49.897  1.00 7.40  ? 97  HIS C C   1 
ATOM   4801 O  O   . HIS C 1 119 ? 9.309  34.984 50.603  1.00 7.72  ? 97  HIS C O   1 
ATOM   4802 C  CB  . HIS C 1 119 ? 8.402  32.959 48.579  1.00 7.61  ? 97  HIS C CB  1 
ATOM   4803 C  CG  . HIS C 1 119 ? 7.673  32.766 47.289  1.00 7.79  ? 97  HIS C CG  1 
ATOM   4804 N  ND1 . HIS C 1 119 ? 6.980  33.781 46.668  1.00 8.12  ? 97  HIS C ND1 1 
ATOM   4805 C  CD2 . HIS C 1 119 ? 7.509  31.666 46.514  1.00 8.00  ? 97  HIS C CD2 1 
ATOM   4806 C  CE1 . HIS C 1 119 ? 6.434  33.317 45.556  1.00 8.14  ? 97  HIS C CE1 1 
ATOM   4807 N  NE2 . HIS C 1 119 ? 6.739  32.037 45.442  1.00 8.11  ? 97  HIS C NE2 1 
ATOM   4808 N  N   . CYS C 1 120 ? 11.178 33.756 50.322  1.00 7.30  ? 98  CYS C N   1 
ATOM   4809 C  CA  . CYS C 1 120 ? 11.674 34.025 51.664  1.00 7.29  ? 98  CYS C CA  1 
ATOM   4810 C  C   . CYS C 1 120 ? 11.614 35.526 51.958  1.00 7.24  ? 98  CYS C C   1 
ATOM   4811 O  O   . CYS C 1 120 ? 12.132 36.332 51.178  1.00 7.06  ? 98  CYS C O   1 
ATOM   4812 C  CB  . CYS C 1 120 ? 13.112 33.529 51.810  1.00 7.29  ? 98  CYS C CB  1 
ATOM   4813 S  SG  . CYS C 1 120 ? 13.749 33.645 53.491  1.00 7.47  ? 98  CYS C SG  1 
ATOM   4814 N  N   . PRO C 1 121 ? 10.965 35.914 53.071  1.00 7.29  ? 99  PRO C N   1 
ATOM   4815 C  CA  . PRO C 1 121 ? 10.927 37.334 53.432  1.00 7.36  ? 99  PRO C CA  1 
ATOM   4816 C  C   . PRO C 1 121 ? 12.303 37.951 53.655  1.00 7.33  ? 99  PRO C C   1 
ATOM   4817 O  O   . PRO C 1 121 ? 12.455 39.172 53.528  1.00 7.59  ? 99  PRO C O   1 
ATOM   4818 C  CB  . PRO C 1 121 ? 10.136 37.341 54.739  1.00 7.45  ? 99  PRO C CB  1 
ATOM   4819 C  CG  . PRO C 1 121 ? 9.284  36.134 54.663  1.00 7.51  ? 99  PRO C CG  1 
ATOM   4820 C  CD  . PRO C 1 121 ? 10.108 35.107 53.957  1.00 7.41  ? 99  PRO C CD  1 
ATOM   4821 N  N   . LYS C 1 122 ? 13.274 37.108 54.005  1.00 7.09  ? 100 LYS C N   1 
ATOM   4822 C  CA  . LYS C 1 122 ? 14.645 37.526 54.256  1.00 6.92  ? 100 LYS C CA  1 
ATOM   4823 C  C   . LYS C 1 122 ? 15.517 37.222 53.039  1.00 6.63  ? 100 LYS C C   1 
ATOM   4824 O  O   . LYS C 1 122 ? 15.228 36.284 52.289  1.00 6.49  ? 100 LYS C O   1 
ATOM   4825 C  CB  . LYS C 1 122 ? 15.177 36.802 55.492  1.00 7.05  ? 100 LYS C CB  1 
ATOM   4826 C  CG  . LYS C 1 122 ? 14.310 37.046 56.716  1.00 7.18  ? 100 LYS C CG  1 
ATOM   4827 C  CD  . LYS C 1 122 ? 14.695 36.187 57.903  1.00 7.25  ? 100 LYS C CD  1 
ATOM   4828 C  CE  . LYS C 1 122 ? 13.696 36.384 59.039  1.00 7.31  ? 100 LYS C CE  1 
ATOM   4829 N  NZ  . LYS C 1 122 ? 14.096 35.715 60.306  1.00 7.32  ? 100 LYS C NZ  1 
ATOM   4830 N  N   . PRO C 1 123 ? 16.595 38.000 52.836  1.00 6.37  ? 101 PRO C N   1 
ATOM   4831 C  CA  . PRO C 1 123 ? 17.413 37.726 51.656  1.00 6.35  ? 101 PRO C CA  1 
ATOM   4832 C  C   . PRO C 1 123 ? 18.131 36.389 51.720  1.00 6.30  ? 101 PRO C C   1 
ATOM   4833 O  O   . PRO C 1 123 ? 18.556 35.959 52.797  1.00 6.37  ? 101 PRO C O   1 
ATOM   4834 C  CB  . PRO C 1 123 ? 18.419 38.879 51.649  1.00 6.31  ? 101 PRO C CB  1 
ATOM   4835 C  CG  . PRO C 1 123 ? 17.700 39.976 52.343  1.00 6.31  ? 101 PRO C CG  1 
ATOM   4836 C  CD  . PRO C 1 123 ? 16.978 39.279 53.456  1.00 6.36  ? 101 PRO C CD  1 
ATOM   4837 N  N   . THR C 1 124 ? 18.253 35.760 50.554  1.00 6.21  ? 102 THR C N   1 
ATOM   4838 C  CA  . THR C 1 124 ? 18.871 34.457 50.403  1.00 6.17  ? 102 THR C CA  1 
ATOM   4839 C  C   . THR C 1 124 ? 20.070 34.563 49.467  1.00 6.23  ? 102 THR C C   1 
ATOM   4840 O  O   . THR C 1 124 ? 20.034 35.269 48.449  1.00 6.11  ? 102 THR C O   1 
ATOM   4841 C  CB  . THR C 1 124 ? 17.876 33.427 49.839  1.00 6.18  ? 102 THR C CB  1 
ATOM   4842 O  OG1 . THR C 1 124 ? 17.293 33.935 48.631  1.00 6.15  ? 102 THR C OG1 1 
ATOM   4843 C  CG2 . THR C 1 124 ? 16.780 33.143 50.840  1.00 6.22  ? 102 THR C CG2 1 
ATOM   4844 N  N   . ILE C 1 125 ? 21.141 33.872 49.832  1.00 6.26  ? 103 ILE C N   1 
ATOM   4845 C  CA  . ILE C 1 125 ? 22.405 33.935 49.114  1.00 6.45  ? 103 ILE C CA  1 
ATOM   4846 C  C   . ILE C 1 125 ? 22.878 32.518 48.840  1.00 6.43  ? 103 ILE C C   1 
ATOM   4847 O  O   . ILE C 1 125 ? 23.109 31.762 49.781  1.00 6.46  ? 103 ILE C O   1 
ATOM   4848 C  CB  . ILE C 1 125 ? 23.491 34.649 49.952  1.00 6.63  ? 103 ILE C CB  1 
ATOM   4849 C  CG1 . ILE C 1 125 ? 23.079 36.086 50.295  1.00 6.84  ? 103 ILE C CG1 1 
ATOM   4850 C  CG2 . ILE C 1 125 ? 24.823 34.655 49.215  1.00 6.72  ? 103 ILE C CG2 1 
ATOM   4851 C  CD1 . ILE C 1 125 ? 23.651 36.581 51.602  1.00 7.00  ? 103 ILE C CD1 1 
ATOM   4852 N  N   . ALA C 1 126 ? 23.021 32.161 47.566  1.00 6.40  ? 104 ALA C N   1 
ATOM   4853 C  CA  . ALA C 1 126 ? 23.615 30.878 47.192  1.00 6.52  ? 104 ALA C CA  1 
ATOM   4854 C  C   . ALA C 1 126 ? 25.126 31.048 47.095  1.00 6.66  ? 104 ALA C C   1 
ATOM   4855 O  O   . ALA C 1 126 ? 25.605 31.954 46.419  1.00 6.67  ? 104 ALA C O   1 
ATOM   4856 C  CB  . ALA C 1 126 ? 23.049 30.388 45.869  1.00 6.57  ? 104 ALA C CB  1 
ATOM   4857 N  N   . ALA C 1 127 ? 25.865 30.182 47.786  1.00 6.75  ? 105 ALA C N   1 
ATOM   4858 C  CA  . ALA C 1 127 ? 27.323 30.194 47.776  1.00 6.92  ? 105 ALA C CA  1 
ATOM   4859 C  C   . ALA C 1 127 ? 27.793 28.888 47.146  1.00 7.05  ? 105 ALA C C   1 
ATOM   4860 O  O   . ALA C 1 127 ? 27.691 27.820 47.759  1.00 7.20  ? 105 ALA C O   1 
ATOM   4861 C  CB  . ALA C 1 127 ? 27.850 30.345 49.194  1.00 6.89  ? 105 ALA C CB  1 
ATOM   4862 N  N   . VAL C 1 128 ? 28.286 28.982 45.913  1.00 7.22  ? 106 VAL C N   1 
ATOM   4863 C  CA  . VAL C 1 128 ? 28.487 27.822 45.059  1.00 7.40  ? 106 VAL C CA  1 
ATOM   4864 C  C   . VAL C 1 128 ? 29.957 27.516 44.803  1.00 7.68  ? 106 VAL C C   1 
ATOM   4865 O  O   . VAL C 1 128 ? 30.723 28.393 44.420  1.00 7.61  ? 106 VAL C O   1 
ATOM   4866 C  CB  . VAL C 1 128 ? 27.802 28.049 43.693  1.00 7.33  ? 106 VAL C CB  1 
ATOM   4867 C  CG1 . VAL C 1 128 ? 28.082 26.897 42.739  1.00 7.38  ? 106 VAL C CG1 1 
ATOM   4868 C  CG2 . VAL C 1 128 ? 26.303 28.246 43.883  1.00 7.37  ? 106 VAL C CG2 1 
ATOM   4869 N  N   . ARG C 1 129 ? 30.331 26.254 44.996  1.00 8.28  ? 107 ARG C N   1 
ATOM   4870 C  CA  . ARG C 1 129 ? 31.577 25.731 44.462  1.00 8.77  ? 107 ARG C CA  1 
ATOM   4871 C  C   . ARG C 1 129 ? 31.283 24.462 43.672  1.00 8.41  ? 107 ARG C C   1 
ATOM   4872 O  O   . ARG C 1 129 ? 30.278 23.794 43.903  1.00 8.15  ? 107 ARG C O   1 
ATOM   4873 C  CB  . ARG C 1 129 ? 32.585 25.458 45.580  1.00 9.73  ? 107 ARG C CB  1 
ATOM   4874 C  CG  . ARG C 1 129 ? 32.238 24.290 46.469  1.00 10.57 ? 107 ARG C CG  1 
ATOM   4875 C  CD  . ARG C 1 129 ? 33.344 24.020 47.469  1.00 11.34 ? 107 ARG C CD  1 
ATOM   4876 N  NE  . ARG C 1 129 ? 33.338 24.984 48.568  1.00 12.07 ? 107 ARG C NE  1 
ATOM   4877 C  CZ  . ARG C 1 129 ? 34.232 25.955 48.761  1.00 12.61 ? 107 ARG C CZ  1 
ATOM   4878 N  NH1 . ARG C 1 129 ? 35.259 26.137 47.933  1.00 13.23 ? 107 ARG C NH1 1 
ATOM   4879 N  NH2 . ARG C 1 129 ? 34.103 26.752 49.812  1.00 13.21 ? 107 ARG C NH2 1 
ATOM   4880 N  N   . GLY C 1 130 ? 32.166 24.123 42.740  1.00 8.11  ? 108 GLY C N   1 
ATOM   4881 C  CA  . GLY C 1 130 ? 31.986 22.912 41.953  1.00 7.93  ? 108 GLY C CA  1 
ATOM   4882 C  C   . GLY C 1 130 ? 30.659 22.899 41.207  1.00 7.76  ? 108 GLY C C   1 
ATOM   4883 O  O   . GLY C 1 130 ? 30.188 23.961 40.775  1.00 7.76  ? 108 GLY C O   1 
ATOM   4884 N  N   . PRO C 1 131 ? 30.052 21.709 41.045  1.00 7.64  ? 109 PRO C N   1 
ATOM   4885 C  CA  . PRO C 1 131 ? 28.819 21.606 40.267  1.00 7.47  ? 109 PRO C CA  1 
ATOM   4886 C  C   . PRO C 1 131 ? 27.619 22.245 40.949  1.00 7.36  ? 109 PRO C C   1 
ATOM   4887 O  O   . PRO C 1 131 ? 27.430 22.111 42.161  1.00 7.17  ? 109 PRO C O   1 
ATOM   4888 C  CB  . PRO C 1 131 ? 28.606 20.093 40.132  1.00 7.59  ? 109 PRO C CB  1 
ATOM   4889 C  CG  . PRO C 1 131 ? 29.340 19.505 41.284  1.00 7.66  ? 109 PRO C CG  1 
ATOM   4890 C  CD  . PRO C 1 131 ? 30.543 20.380 41.446  1.00 7.57  ? 109 PRO C CD  1 
ATOM   4891 N  N   . CYS C 1 132 ? 26.831 22.951 40.148  1.00 7.20  ? 110 CYS C N   1 
ATOM   4892 C  CA  . CYS C 1 132 ? 25.548 23.483 40.567  1.00 7.20  ? 110 CYS C CA  1 
ATOM   4893 C  C   . CYS C 1 132 ? 24.624 23.228 39.386  1.00 7.04  ? 110 CYS C C   1 
ATOM   4894 O  O   . CYS C 1 132 ? 24.536 24.052 38.473  1.00 7.11  ? 110 CYS C O   1 
ATOM   4895 C  CB  . CYS C 1 132 ? 25.677 24.974 40.879  1.00 7.31  ? 110 CYS C CB  1 
ATOM   4896 S  SG  . CYS C 1 132 ? 24.130 25.803 41.307  1.00 7.54  ? 110 CYS C SG  1 
ATOM   4897 N  N   . LEU C 1 133 ? 23.962 22.071 39.395  1.00 7.02  ? 111 LEU C N   1 
ATOM   4898 C  CA  . LEU C 1 133 ? 23.289 21.551 38.202  1.00 7.00  ? 111 LEU C CA  1 
ATOM   4899 C  C   . LEU C 1 133 ? 21.821 21.221 38.403  1.00 6.90  ? 111 LEU C C   1 
ATOM   4900 O  O   . LEU C 1 133 ? 21.398 20.845 39.497  1.00 6.67  ? 111 LEU C O   1 
ATOM   4901 C  CB  . LEU C 1 133 ? 23.988 20.277 37.728  1.00 7.21  ? 111 LEU C CB  1 
ATOM   4902 C  CG  . LEU C 1 133 ? 25.481 20.396 37.421  1.00 7.41  ? 111 LEU C CG  1 
ATOM   4903 C  CD1 . LEU C 1 133 ? 26.050 19.035 37.042  1.00 7.56  ? 111 LEU C CD1 1 
ATOM   4904 C  CD2 . LEU C 1 133 ? 25.716 21.411 36.318  1.00 7.53  ? 111 LEU C CD2 1 
ATOM   4905 N  N   . ALA C 1 134 ? 21.061 21.342 37.314  1.00 6.75  ? 112 ALA C N   1 
ATOM   4906 C  CA  . ALA C 1 134 ? 19.676 20.891 37.264  1.00 6.71  ? 112 ALA C CA  1 
ATOM   4907 C  C   . ALA C 1 134 ? 18.837 21.528 38.386  1.00 6.67  ? 112 ALA C C   1 
ATOM   4908 O  O   . ALA C 1 134 ? 18.816 22.753 38.504  1.00 6.55  ? 112 ALA C O   1 
ATOM   4909 C  CB  . ALA C 1 134 ? 19.621 19.366 37.285  1.00 6.76  ? 112 ALA C CB  1 
ATOM   4910 N  N   . GLY C 1 135 ? 18.161 20.729 39.211  1.00 6.62  ? 113 GLY C N   1 
ATOM   4911 C  CA  . GLY C 1 135 ? 17.357 21.276 40.308  1.00 6.68  ? 113 GLY C CA  1 
ATOM   4912 C  C   . GLY C 1 135 ? 18.129 22.169 41.272  1.00 6.73  ? 113 GLY C C   1 
ATOM   4913 O  O   . GLY C 1 135 ? 17.569 23.096 41.849  1.00 6.72  ? 113 GLY C O   1 
ATOM   4914 N  N   . ALA C 1 136 ? 19.423 21.897 41.441  1.00 6.75  ? 114 ALA C N   1 
ATOM   4915 C  CA  . ALA C 1 136 ? 20.286 22.720 42.295  1.00 6.83  ? 114 ALA C CA  1 
ATOM   4916 C  C   . ALA C 1 136 ? 20.626 24.057 41.643  1.00 7.00  ? 114 ALA C C   1 
ATOM   4917 O  O   . ALA C 1 136 ? 20.755 25.073 42.325  1.00 6.80  ? 114 ALA C O   1 
ATOM   4918 C  CB  . ALA C 1 136 ? 21.569 21.972 42.623  1.00 6.81  ? 114 ALA C CB  1 
ATOM   4919 N  N   . CYS C 1 137 ? 20.796 24.049 40.323  1.00 7.28  ? 115 CYS C N   1 
ATOM   4920 C  CA  . CYS C 1 137 ? 20.974 25.287 39.566  1.00 7.72  ? 115 CYS C CA  1 
ATOM   4921 C  C   . CYS C 1 137 ? 19.732 26.151 39.731  1.00 7.58  ? 115 CYS C C   1 
ATOM   4922 O  O   . CYS C 1 137 ? 19.824 27.363 39.921  1.00 7.35  ? 115 CYS C O   1 
ATOM   4923 C  CB  . CYS C 1 137 ? 21.225 24.987 38.085  1.00 8.24  ? 115 CYS C CB  1 
ATOM   4924 S  SG  . CYS C 1 137 ? 21.670 26.425 37.083  1.00 9.69  ? 115 CYS C SG  1 
ATOM   4925 N  N   . GLU C 1 138 ? 18.568 25.506 39.700  1.00 7.45  ? 116 GLU C N   1 
ATOM   4926 C  CA  . GLU C 1 138 ? 17.300 26.214 39.860  1.00 7.56  ? 116 GLU C CA  1 
ATOM   4927 C  C   . GLU C 1 138 ? 17.164 26.768 41.280  1.00 7.17  ? 116 GLU C C   1 
ATOM   4928 O  O   . GLU C 1 138 ? 16.720 27.896 41.468  1.00 6.91  ? 116 GLU C O   1 
ATOM   4929 C  CB  . GLU C 1 138 ? 16.131 25.306 39.460  1.00 8.09  ? 116 GLU C CB  1 
ATOM   4930 C  CG  . GLU C 1 138 ? 16.137 25.009 37.961  1.00 8.70  ? 116 GLU C CG  1 
ATOM   4931 C  CD  . GLU C 1 138 ? 15.281 23.830 37.525  1.00 9.49  ? 116 GLU C CD  1 
ATOM   4932 O  OE1 . GLU C 1 138 ? 14.523 23.268 38.333  1.00 10.04 ? 116 GLU C OE1 1 
ATOM   4933 O  OE2 . GLU C 1 138 ? 15.379 23.455 36.333  1.00 10.72 ? 116 GLU C OE2 1 
ATOM   4934 N  N   . LEU C 1 139 ? 17.590 25.997 42.276  1.00 6.94  ? 117 LEU C N   1 
ATOM   4935 C  CA  . LEU C 1 139 ? 17.594 26.478 43.657  1.00 6.85  ? 117 LEU C CA  1 
ATOM   4936 C  C   . LEU C 1 139 ? 18.449 27.745 43.767  1.00 6.58  ? 117 LEU C C   1 
ATOM   4937 O  O   . LEU C 1 139 ? 18.028 28.749 44.356  1.00 6.34  ? 117 LEU C O   1 
ATOM   4938 C  CB  . LEU C 1 139 ? 18.106 25.384 44.605  1.00 7.08  ? 117 LEU C CB  1 
ATOM   4939 C  CG  . LEU C 1 139 ? 17.855 25.550 46.113  1.00 7.35  ? 117 LEU C CG  1 
ATOM   4940 C  CD1 . LEU C 1 139 ? 17.988 24.201 46.808  1.00 7.58  ? 117 LEU C CD1 1 
ATOM   4941 C  CD2 . LEU C 1 139 ? 18.786 26.570 46.740  1.00 7.50  ? 117 LEU C CD2 1 
ATOM   4942 N  N   . ALA C 1 140 ? 19.639 27.719 43.174  1.00 6.34  ? 118 ALA C N   1 
ATOM   4943 C  CA  . ALA C 1 140 ? 20.506 28.893 43.211  1.00 6.29  ? 118 ALA C CA  1 
ATOM   4944 C  C   . ALA C 1 140 ? 19.899 30.059 42.428  1.00 6.29  ? 118 ALA C C   1 
ATOM   4945 O  O   . ALA C 1 140 ? 19.991 31.208 42.854  1.00 6.29  ? 118 ALA C O   1 
ATOM   4946 C  CB  . ALA C 1 140 ? 21.899 28.557 42.702  1.00 6.27  ? 118 ALA C CB  1 
ATOM   4947 N  N   . LEU C 1 141 ? 19.250 29.769 41.301  1.00 6.30  ? 119 LEU C N   1 
ATOM   4948 C  CA  . LEU C 1 141 ? 18.598 30.826 40.524  1.00 6.46  ? 119 LEU C CA  1 
ATOM   4949 C  C   . LEU C 1 141 ? 17.544 31.562 41.346  1.00 6.50  ? 119 LEU C C   1 
ATOM   4950 O  O   . LEU C 1 141 ? 17.353 32.765 41.168  1.00 6.70  ? 119 LEU C O   1 
ATOM   4951 C  CB  . LEU C 1 141 ? 17.945 30.267 39.257  1.00 6.51  ? 119 LEU C CB  1 
ATOM   4952 C  CG  . LEU C 1 141 ? 18.867 29.834 38.116  1.00 6.65  ? 119 LEU C CG  1 
ATOM   4953 C  CD1 . LEU C 1 141 ? 18.071 29.122 37.030  1.00 6.76  ? 119 LEU C CD1 1 
ATOM   4954 C  CD2 . LEU C 1 141 ? 19.620 31.010 37.521  1.00 6.75  ? 119 LEU C CD2 1 
ATOM   4955 N  N   . ALA C 1 142 ? 16.860 30.830 42.225  1.00 6.43  ? 120 ALA C N   1 
ATOM   4956 C  CA  . ALA C 1 142 ? 15.787 31.391 43.056  1.00 6.54  ? 120 ALA C CA  1 
ATOM   4957 C  C   . ALA C 1 142 ? 16.299 32.289 44.180  1.00 6.69  ? 120 ALA C C   1 
ATOM   4958 O  O   . ALA C 1 142 ? 15.545 33.108 44.706  1.00 6.86  ? 120 ALA C O   1 
ATOM   4959 C  CB  . ALA C 1 142 ? 14.930 30.279 43.635  1.00 6.51  ? 120 ALA C CB  1 
ATOM   4960 N  N   . CYS C 1 143 ? 17.565 32.140 44.559  1.00 6.76  ? 121 CYS C N   1 
ATOM   4961 C  CA  . CYS C 1 143 ? 18.133 32.984 45.610  1.00 6.91  ? 121 CYS C CA  1 
ATOM   4962 C  C   . CYS C 1 143 ? 18.310 34.426 45.145  1.00 7.22  ? 121 CYS C C   1 
ATOM   4963 O  O   . CYS C 1 143 ? 18.492 34.700 43.958  1.00 7.24  ? 121 CYS C O   1 
ATOM   4964 C  CB  . CYS C 1 143 ? 19.483 32.435 46.083  1.00 6.76  ? 121 CYS C CB  1 
ATOM   4965 S  SG  . CYS C 1 143 ? 19.389 30.841 46.925  1.00 6.81  ? 121 CYS C SG  1 
ATOM   4966 N  N   . ASP C 1 144 ? 18.281 35.353 46.091  1.00 7.72  ? 122 ASP C N   1 
ATOM   4967 C  CA  . ASP C 1 144 ? 18.386 36.766 45.745  1.00 8.24  ? 122 ASP C CA  1 
ATOM   4968 C  C   . ASP C 1 144 ? 19.721 37.078 45.096  1.00 8.70  ? 122 ASP C C   1 
ATOM   4969 O  O   . ASP C 1 144 ? 19.786 37.874 44.153  1.00 8.48  ? 122 ASP C O   1 
ATOM   4970 C  CB  . ASP C 1 144 ? 18.154 37.642 46.967  1.00 8.45  ? 122 ASP C CB  1 
ATOM   4971 C  CG  . ASP C 1 144 ? 16.760 37.482 47.522  1.00 8.73  ? 122 ASP C CG  1 
ATOM   4972 O  OD1 . ASP C 1 144 ? 15.786 37.754 46.780  1.00 9.40  ? 122 ASP C OD1 1 
ATOM   4973 O  OD2 . ASP C 1 144 ? 16.623 37.062 48.683  1.00 8.89  ? 122 ASP C OD2 1 
HETATM 4974 N  N   . MSE C 1 145 ? 20.772 36.434 45.601  1.00 9.17  ? 123 MSE C N   1 
HETATM 4975 C  CA  . MSE C 1 145 ? 22.113 36.566 45.054  1.00 9.99  ? 123 MSE C CA  1 
HETATM 4976 C  C   . MSE C 1 145 ? 22.784 35.222 44.976  1.00 8.94  ? 123 MSE C C   1 
HETATM 4977 O  O   . MSE C 1 145 ? 22.483 34.322 45.746  1.00 8.29  ? 123 MSE C O   1 
HETATM 4978 C  CB  . MSE C 1 145 ? 22.966 37.462 45.950  1.00 12.22 ? 123 MSE C CB  1 
HETATM 4979 C  CG  . MSE C 1 145 ? 22.458 38.897 45.983  1.00 14.54 ? 123 MSE C CG  1 
HETATM 4980 SE SE  . MSE C 1 145 ? 23.654 39.972 47.128  1.00 21.11 ? 123 MSE C SE  1 
HETATM 4981 C  CE  . MSE C 1 145 ? 25.342 39.717 46.139  1.00 19.48 ? 123 MSE C CE  1 
ATOM   4982 N  N   . THR C 1 146 ? 23.711 35.088 44.037  1.00 8.17  ? 124 THR C N   1 
ATOM   4983 C  CA  . THR C 1 146 ? 24.571 33.919 43.941  1.00 7.96  ? 124 THR C CA  1 
ATOM   4984 C  C   . THR C 1 146 ? 26.021 34.364 43.858  1.00 7.83  ? 124 THR C C   1 
ATOM   4985 O  O   . THR C 1 146 ? 26.368 35.226 43.050  1.00 7.62  ? 124 THR C O   1 
ATOM   4986 C  CB  . THR C 1 146 ? 24.232 33.091 42.694  1.00 7.89  ? 124 THR C CB  1 
ATOM   4987 O  OG1 . THR C 1 146 ? 22.876 32.638 42.785  1.00 7.72  ? 124 THR C OG1 1 
ATOM   4988 C  CG2 . THR C 1 146 ? 25.159 31.889 42.564  1.00 7.90  ? 124 THR C CG2 1 
ATOM   4989 N  N   . ILE C 1 147 ? 26.867 33.785 44.703  1.00 7.88  ? 125 ILE C N   1 
ATOM   4990 C  CA  . ILE C 1 147 ? 28.310 33.963 44.558  1.00 8.10  ? 125 ILE C CA  1 
ATOM   4991 C  C   . ILE C 1 147 ? 28.930 32.596 44.296  1.00 8.02  ? 125 ILE C C   1 
ATOM   4992 O  O   . ILE C 1 147 ? 28.411 31.575 44.743  1.00 7.84  ? 125 ILE C O   1 
ATOM   4993 C  CB  . ILE C 1 147 ? 28.948 34.675 45.767  1.00 8.49  ? 125 ILE C CB  1 
ATOM   4994 C  CG1 . ILE C 1 147 ? 28.878 33.819 47.025  1.00 8.73  ? 125 ILE C CG1 1 
ATOM   4995 C  CG2 . ILE C 1 147 ? 28.285 36.037 45.990  1.00 8.57  ? 125 ILE C CG2 1 
ATOM   4996 C  CD1 . ILE C 1 147 ? 29.721 34.361 48.166  1.00 9.02  ? 125 ILE C CD1 1 
ATOM   4997 N  N   . ALA C 1 148 ? 30.023 32.578 43.549  1.00 8.01  ? 126 ALA C N   1 
ATOM   4998 C  CA  . ALA C 1 148 ? 30.603 31.327 43.100  1.00 8.12  ? 126 ALA C CA  1 
ATOM   4999 C  C   . ALA C 1 148 ? 32.120 31.388 43.138  1.00 8.54  ? 126 ALA C C   1 
ATOM   5000 O  O   . ALA C 1 148 ? 32.717 32.450 42.988  1.00 8.50  ? 126 ALA C O   1 
ATOM   5001 C  CB  . ALA C 1 148 ? 30.133 31.012 41.690  1.00 8.11  ? 126 ALA C CB  1 
ATOM   5002 N  N   . THR C 1 149 ? 32.734 30.238 43.354  1.00 9.04  ? 127 THR C N   1 
ATOM   5003 C  CA  . THR C 1 149 ? 34.176 30.127 43.213  1.00 9.59  ? 127 THR C CA  1 
ATOM   5004 C  C   . THR C 1 149 ? 34.554 30.034 41.737  1.00 10.23 ? 127 THR C C   1 
ATOM   5005 O  O   . THR C 1 149 ? 33.725 29.724 40.879  1.00 10.00 ? 127 THR C O   1 
ATOM   5006 C  CB  . THR C 1 149 ? 34.701 28.873 43.918  1.00 9.64  ? 127 THR C CB  1 
ATOM   5007 O  OG1 . THR C 1 149 ? 34.076 27.727 43.342  1.00 9.71  ? 127 THR C OG1 1 
ATOM   5008 C  CG2 . THR C 1 149 ? 34.396 28.924 45.409  1.00 9.70  ? 127 THR C CG2 1 
ATOM   5009 N  N   . GLU C 1 150 ? 35.830 30.263 41.454  1.00 11.36 ? 128 GLU C N   1 
ATOM   5010 C  CA  . GLU C 1 150 ? 36.354 30.173 40.095  1.00 12.44 ? 128 GLU C CA  1 
ATOM   5011 C  C   . GLU C 1 150 ? 36.105 28.799 39.464  1.00 12.21 ? 128 GLU C C   1 
ATOM   5012 O  O   . GLU C 1 150 ? 35.907 28.701 38.261  1.00 12.58 ? 128 GLU C O   1 
ATOM   5013 C  CB  . GLU C 1 150 ? 37.862 30.453 40.093  1.00 13.64 ? 128 GLU C CB  1 
ATOM   5014 C  CG  . GLU C 1 150 ? 38.249 31.866 40.503  1.00 15.09 ? 128 GLU C CG  1 
ATOM   5015 C  CD  . GLU C 1 150 ? 38.030 32.899 39.410  1.00 16.63 ? 128 GLU C CD  1 
ATOM   5016 O  OE1 . GLU C 1 150 ? 37.611 32.537 38.288  1.00 18.71 ? 128 GLU C OE1 1 
ATOM   5017 O  OE2 . GLU C 1 150 ? 38.286 34.094 39.675  1.00 19.04 ? 128 GLU C OE2 1 
ATOM   5018 N  N   . ASP C 1 151 ? 36.099 27.757 40.293  1.00 11.87 ? 129 ASP C N   1 
ATOM   5019 C  CA  . ASP C 1 151 ? 35.948 26.370 39.843  1.00 12.02 ? 129 ASP C CA  1 
ATOM   5020 C  C   . ASP C 1 151 ? 34.498 25.920 39.668  1.00 11.09 ? 129 ASP C C   1 
ATOM   5021 O  O   . ASP C 1 151 ? 34.252 24.799 39.221  1.00 11.09 ? 129 ASP C O   1 
ATOM   5022 C  CB  . ASP C 1 151 ? 36.623 25.436 40.851  1.00 12.90 ? 129 ASP C CB  1 
ATOM   5023 C  CG  . ASP C 1 151 ? 36.029 25.563 42.248  1.00 13.76 ? 129 ASP C CG  1 
ATOM   5024 O  OD1 . ASP C 1 151 ? 36.581 26.328 43.069  1.00 15.59 ? 129 ASP C OD1 1 
ATOM   5025 O  OD2 . ASP C 1 151 ? 34.990 24.940 42.521  1.00 14.45 ? 129 ASP C OD2 1 
ATOM   5026 N  N   . ALA C 1 152 ? 33.548 26.768 40.053  1.00 10.07 ? 130 ALA C N   1 
ATOM   5027 C  CA  . ALA C 1 152 ? 32.130 26.409 39.979  1.00 9.38  ? 130 ALA C CA  1 
ATOM   5028 C  C   . ALA C 1 152 ? 31.672 26.292 38.532  1.00 8.94  ? 130 ALA C C   1 
ATOM   5029 O  O   . ALA C 1 152 ? 32.179 26.986 37.656  1.00 8.80  ? 130 ALA C O   1 
ATOM   5030 C  CB  . ALA C 1 152 ? 31.277 27.439 40.703  1.00 9.37  ? 130 ALA C CB  1 
ATOM   5031 N  N   . PHE C 1 153 ? 30.721 25.400 38.289  1.00 8.45  ? 131 PHE C N   1 
ATOM   5032 C  CA  . PHE C 1 153 ? 30.103 25.301 36.974  1.00 8.29  ? 131 PHE C CA  1 
ATOM   5033 C  C   . PHE C 1 153 ? 28.622 25.009 37.109  1.00 7.87  ? 131 PHE C C   1 
ATOM   5034 O  O   . PHE C 1 153 ? 28.178 24.395 38.087  1.00 7.76  ? 131 PHE C O   1 
ATOM   5035 C  CB  . PHE C 1 153 ? 30.800 24.281 36.067  1.00 8.38  ? 131 PHE C CB  1 
ATOM   5036 C  CG  . PHE C 1 153 ? 30.912 22.905 36.650  1.00 8.51  ? 131 PHE C CG  1 
ATOM   5037 C  CD1 . PHE C 1 153 ? 31.937 22.593 37.535  1.00 8.64  ? 131 PHE C CD1 1 
ATOM   5038 C  CD2 . PHE C 1 153 ? 30.025 21.904 36.284  1.00 8.60  ? 131 PHE C CD2 1 
ATOM   5039 C  CE1 . PHE C 1 153 ? 32.055 21.321 38.062  1.00 8.75  ? 131 PHE C CE1 1 
ATOM   5040 C  CE2 . PHE C 1 153 ? 30.140 20.626 36.807  1.00 8.67  ? 131 PHE C CE2 1 
ATOM   5041 C  CZ  . PHE C 1 153 ? 31.156 20.334 37.701  1.00 8.74  ? 131 PHE C CZ  1 
ATOM   5042 N  N   . PHE C 1 154 ? 27.876 25.456 36.105  1.00 7.53  ? 132 PHE C N   1 
ATOM   5043 C  CA  . PHE C 1 154 ? 26.429 25.566 36.188  1.00 7.39  ? 132 PHE C CA  1 
ATOM   5044 C  C   . PHE C 1 154 ? 25.750 24.951 34.983  1.00 7.42  ? 132 PHE C C   1 
ATOM   5045 O  O   . PHE C 1 154 ? 26.366 24.731 33.940  1.00 7.37  ? 132 PHE C O   1 
ATOM   5046 C  CB  . PHE C 1 154 ? 26.028 27.044 36.251  1.00 7.31  ? 132 PHE C CB  1 
ATOM   5047 C  CG  . PHE C 1 154 ? 26.501 27.754 37.486  1.00 7.20  ? 132 PHE C CG  1 
ATOM   5048 C  CD1 . PHE C 1 154 ? 27.769 28.306 37.542  1.00 7.26  ? 132 PHE C CD1 1 
ATOM   5049 C  CD2 . PHE C 1 154 ? 25.670 27.880 38.588  1.00 7.22  ? 132 PHE C CD2 1 
ATOM   5050 C  CE1 . PHE C 1 154 ? 28.202 28.961 38.681  1.00 7.24  ? 132 PHE C CE1 1 
ATOM   5051 C  CE2 . PHE C 1 154 ? 26.091 28.546 39.720  1.00 7.23  ? 132 PHE C CE2 1 
ATOM   5052 C  CZ  . PHE C 1 154 ? 27.364 29.079 39.769  1.00 7.24  ? 132 PHE C CZ  1 
ATOM   5053 N  N   . GLY C 1 155 ? 24.457 24.706 35.121  1.00 7.50  ? 133 GLY C N   1 
ATOM   5054 C  CA  . GLY C 1 155 ? 23.640 24.386 33.966  1.00 7.66  ? 133 GLY C CA  1 
ATOM   5055 C  C   . GLY C 1 155 ? 22.484 23.464 34.243  1.00 7.85  ? 133 GLY C C   1 
ATOM   5056 O  O   . GLY C 1 155 ? 22.206 23.115 35.391  1.00 7.74  ? 133 GLY C O   1 
ATOM   5057 N  N   . GLU C 1 156 ? 21.827 23.069 33.157  1.00 8.27  ? 134 GLU C N   1 
ATOM   5058 C  CA  . GLU C 1 156 ? 20.544 22.378 33.193  1.00 8.77  ? 134 GLU C CA  1 
ATOM   5059 C  C   . GLU C 1 156 ? 20.607 21.191 32.245  1.00 8.45  ? 134 GLU C C   1 
ATOM   5060 O  O   . GLU C 1 156 ? 20.123 21.273 31.124  1.00 8.36  ? 134 GLU C O   1 
ATOM   5061 C  CB  . GLU C 1 156 ? 19.437 23.323 32.720  1.00 9.68  ? 134 GLU C CB  1 
ATOM   5062 C  CG  . GLU C 1 156 ? 19.137 24.485 33.644  1.00 10.54 ? 134 GLU C CG  1 
ATOM   5063 C  CD  . GLU C 1 156 ? 18.039 24.167 34.618  1.00 11.77 ? 134 GLU C CD  1 
ATOM   5064 O  OE1 . GLU C 1 156 ? 18.164 23.133 35.305  1.00 13.27 ? 134 GLU C OE1 1 
ATOM   5065 O  OE2 . GLU C 1 156 ? 17.050 24.938 34.673  1.00 12.57 ? 134 GLU C OE2 1 
ATOM   5066 N  N   . PRO C 1 157 ? 21.187 20.070 32.696  1.00 8.01  ? 135 PRO C N   1 
ATOM   5067 C  CA  . PRO C 1 157 ? 21.382 18.918 31.812  1.00 8.02  ? 135 PRO C CA  1 
ATOM   5068 C  C   . PRO C 1 157 ? 20.126 18.076 31.557  1.00 8.10  ? 135 PRO C C   1 
ATOM   5069 O  O   . PRO C 1 157 ? 20.191 17.113 30.791  1.00 8.07  ? 135 PRO C O   1 
ATOM   5070 C  CB  . PRO C 1 157 ? 22.413 18.079 32.572  1.00 7.98  ? 135 PRO C CB  1 
ATOM   5071 C  CG  . PRO C 1 157 ? 22.168 18.408 34.000  1.00 7.96  ? 135 PRO C CG  1 
ATOM   5072 C  CD  . PRO C 1 157 ? 21.832 19.867 34.006  1.00 8.04  ? 135 PRO C CD  1 
ATOM   5073 N  N   . GLU C 1 158 ? 19.011 18.443 32.183  1.00 8.26  ? 136 GLU C N   1 
ATOM   5074 C  CA  . GLU C 1 158 ? 17.774 17.647 32.164  1.00 8.48  ? 136 GLU C CA  1 
ATOM   5075 C  C   . GLU C 1 158 ? 17.432 17.009 30.820  1.00 8.32  ? 136 GLU C C   1 
ATOM   5076 O  O   . GLU C 1 158 ? 17.181 15.800 30.752  1.00 8.11  ? 136 GLU C O   1 
ATOM   5077 C  CB  . GLU C 1 158 ? 16.583 18.503 32.627  1.00 8.85  ? 136 GLU C CB  1 
ATOM   5078 C  CG  . GLU C 1 158 ? 16.547 18.813 34.124  1.00 9.14  ? 136 GLU C CG  1 
ATOM   5079 C  CD  . GLU C 1 158 ? 17.313 20.066 34.529  1.00 9.55  ? 136 GLU C CD  1 
ATOM   5080 O  OE1 . GLU C 1 158 ? 18.446 20.271 34.063  1.00 9.81  ? 136 GLU C OE1 1 
ATOM   5081 O  OE2 . GLU C 1 158 ? 16.786 20.851 35.346  1.00 10.15 ? 136 GLU C OE2 1 
ATOM   5082 N  N   . LEU C 1 159 ? 17.405 17.802 29.751  1.00 8.13  ? 137 LEU C N   1 
ATOM   5083 C  CA  . LEU C 1 159 ? 16.896 17.277 28.482  1.00 8.26  ? 137 LEU C CA  1 
ATOM   5084 C  C   . LEU C 1 159 ? 17.771 16.143 27.945  1.00 8.77  ? 137 LEU C C   1 
ATOM   5085 O  O   . LEU C 1 159 ? 17.267 15.257 27.256  1.00 9.28  ? 137 LEU C O   1 
ATOM   5086 C  CB  . LEU C 1 159 ? 16.680 18.376 27.435  1.00 8.05  ? 137 LEU C CB  1 
ATOM   5087 C  CG  . LEU C 1 159 ? 15.250 18.922 27.365  1.00 7.91  ? 137 LEU C CG  1 
ATOM   5088 C  CD1 . LEU C 1 159 ? 14.844 19.596 28.667  1.00 7.76  ? 137 LEU C CD1 1 
ATOM   5089 C  CD2 . LEU C 1 159 ? 15.115 19.882 26.196  1.00 7.83  ? 137 LEU C CD2 1 
ATOM   5090 N  N   . LYS C 1 160 ? 19.055 16.149 28.298  1.00 8.92  ? 138 LYS C N   1 
ATOM   5091 C  CA  . LYS C 1 160 ? 19.979 15.103 27.847  1.00 9.38  ? 138 LYS C CA  1 
ATOM   5092 C  C   . LYS C 1 160 ? 19.697 13.720 28.426  1.00 9.84  ? 138 LYS C C   1 
ATOM   5093 O  O   . LYS C 1 160 ? 20.113 12.724 27.843  1.00 10.28 ? 138 LYS C O   1 
ATOM   5094 C  CB  . LYS C 1 160 ? 21.428 15.488 28.145  1.00 9.35  ? 138 LYS C CB  1 
ATOM   5095 C  CG  . LYS C 1 160 ? 21.906 16.698 27.363  1.00 9.48  ? 138 LYS C CG  1 
ATOM   5096 C  CD  . LYS C 1 160 ? 23.414 16.859 27.392  1.00 9.69  ? 138 LYS C CD  1 
ATOM   5097 C  CE  . LYS C 1 160 ? 23.930 17.038 28.808  1.00 9.90  ? 138 LYS C CE  1 
ATOM   5098 N  NZ  . LYS C 1 160 ? 25.360 17.452 28.805  1.00 10.11 ? 138 LYS C NZ  1 
ATOM   5099 N  N   . PHE C 1 161 ? 19.006 13.634 29.553  1.00 10.28 ? 139 PHE C N   1 
ATOM   5100 C  CA  . PHE C 1 161 ? 18.589 12.303 30.025  1.00 10.61 ? 139 PHE C CA  1 
ATOM   5101 C  C   . PHE C 1 161 ? 17.076 12.161 30.100  1.00 9.77  ? 139 PHE C C   1 
ATOM   5102 O  O   . PHE C 1 161 ? 16.548 11.336 30.846  1.00 9.83  ? 139 PHE C O   1 
ATOM   5103 C  CB  . PHE C 1 161 ? 19.284 11.922 31.325  1.00 11.40 ? 139 PHE C CB  1 
ATOM   5104 C  CG  . PHE C 1 161 ? 19.148 12.938 32.410  1.00 11.95 ? 139 PHE C CG  1 
ATOM   5105 C  CD1 . PHE C 1 161 ? 20.123 13.906 32.591  1.00 12.16 ? 139 PHE C CD1 1 
ATOM   5106 C  CD2 . PHE C 1 161 ? 18.067 12.911 33.263  1.00 12.48 ? 139 PHE C CD2 1 
ATOM   5107 C  CE1 . PHE C 1 161 ? 20.011 14.845 33.593  1.00 12.48 ? 139 PHE C CE1 1 
ATOM   5108 C  CE2 . PHE C 1 161 ? 17.946 13.842 34.277  1.00 12.69 ? 139 PHE C CE2 1 
ATOM   5109 C  CZ  . PHE C 1 161 ? 18.917 14.815 34.442  1.00 12.62 ? 139 PHE C CZ  1 
ATOM   5110 N  N   . GLY C 1 162 ? 16.388 12.947 29.276  1.00 8.88  ? 140 GLY C N   1 
ATOM   5111 C  CA  . GLY C 1 162 ? 14.965 12.774 29.062  1.00 8.20  ? 140 GLY C CA  1 
ATOM   5112 C  C   . GLY C 1 162 ? 14.060 13.371 30.122  1.00 7.64  ? 140 GLY C C   1 
ATOM   5113 O  O   . GLY C 1 162 ? 12.900 12.999 30.196  1.00 7.51  ? 140 GLY C O   1 
ATOM   5114 N  N   . ALA C 1 163 ? 14.588 14.285 30.932  1.00 7.03  ? 141 ALA C N   1 
ATOM   5115 C  CA  . ALA C 1 163 ? 13.808 14.954 31.961  1.00 6.79  ? 141 ALA C CA  1 
ATOM   5116 C  C   . ALA C 1 163 ? 13.422 16.333 31.462  1.00 6.54  ? 141 ALA C C   1 
ATOM   5117 O  O   . ALA C 1 163 ? 14.168 16.955 30.716  1.00 6.55  ? 141 ALA C O   1 
ATOM   5118 C  CB  . ALA C 1 163 ? 14.617 15.072 33.237  1.00 6.79  ? 141 ALA C CB  1 
ATOM   5119 N  N   . GLY C 1 164 ? 12.263 16.815 31.889  1.00 6.36  ? 142 GLY C N   1 
ATOM   5120 C  CA  . GLY C 1 164 ? 11.899 18.201 31.650  1.00 6.25  ? 142 GLY C CA  1 
ATOM   5121 C  C   . GLY C 1 164 ? 12.393 19.117 32.752  1.00 6.20  ? 142 GLY C C   1 
ATOM   5122 O  O   . GLY C 1 164 ? 12.948 18.681 33.764  1.00 6.23  ? 142 GLY C O   1 
ATOM   5123 N  N   . ILE C 1 165 ? 12.192 20.409 32.537  1.00 6.06  ? 143 ILE C N   1 
ATOM   5124 C  CA  . ILE C 1 165 ? 12.571 21.436 33.499  1.00 6.11  ? 143 ILE C CA  1 
ATOM   5125 C  C   . ILE C 1 165 ? 11.454 21.618 34.528  1.00 6.14  ? 143 ILE C C   1 
ATOM   5126 O  O   . ILE C 1 165 ? 10.311 21.905 34.170  1.00 6.12  ? 143 ILE C O   1 
ATOM   5127 C  CB  . ILE C 1 165 ? 12.842 22.766 32.774  1.00 6.06  ? 143 ILE C CB  1 
ATOM   5128 C  CG1 . ILE C 1 165 ? 13.981 22.599 31.754  1.00 6.09  ? 143 ILE C CG1 1 
ATOM   5129 C  CG2 . ILE C 1 165 ? 13.149 23.887 33.762  1.00 6.05  ? 143 ILE C CG2 1 
ATOM   5130 C  CD1 . ILE C 1 165 ? 15.323 22.228 32.350  1.00 6.17  ? 143 ILE C CD1 1 
ATOM   5131 N  N   . VAL C 1 166 ? 11.792 21.458 35.805  1.00 6.14  ? 144 VAL C N   1 
ATOM   5132 C  CA  . VAL C 1 166 ? 10.814 21.601 36.885  1.00 6.19  ? 144 VAL C CA  1 
ATOM   5133 C  C   . VAL C 1 166 ? 10.521 23.069 37.184  1.00 6.38  ? 144 VAL C C   1 
ATOM   5134 O  O   . VAL C 1 166 ? 9.360  23.467 37.243  1.00 6.06  ? 144 VAL C O   1 
ATOM   5135 C  CB  . VAL C 1 166 ? 11.278 20.909 38.183  1.00 6.14  ? 144 VAL C CB  1 
ATOM   5136 C  CG1 . VAL C 1 166 ? 10.237 21.071 39.290  1.00 6.15  ? 144 VAL C CG1 1 
ATOM   5137 C  CG2 . VAL C 1 166 ? 11.559 19.433 37.938  1.00 6.14  ? 144 VAL C CG2 1 
ATOM   5138 N  N   . VAL C 1 167 ? 11.573 23.857 37.408  1.00 6.76  ? 145 VAL C N   1 
ATOM   5139 C  CA  . VAL C 1 167 ? 11.433 25.271 37.772  1.00 7.26  ? 145 VAL C CA  1 
ATOM   5140 C  C   . VAL C 1 167 ? 12.089 26.126 36.693  1.00 8.04  ? 145 VAL C C   1 
ATOM   5141 O  O   . VAL C 1 167 ? 13.316 26.244 36.644  1.00 7.93  ? 145 VAL C O   1 
ATOM   5142 C  CB  . VAL C 1 167 ? 12.054 25.584 39.152  1.00 7.19  ? 145 VAL C CB  1 
ATOM   5143 C  CG1 . VAL C 1 167 ? 11.614 26.964 39.626  1.00 7.14  ? 145 VAL C CG1 1 
ATOM   5144 C  CG2 . VAL C 1 167 ? 11.659 24.519 40.171  1.00 7.15  ? 145 VAL C CG2 1 
HETATM 5145 N  N   . MSE C 1 168 ? 11.265 26.730 35.842  1.00 9.02  ? 146 MSE C N   1 
HETATM 5146 C  CA  . MSE C 1 168 ? 11.746 27.422 34.640  1.00 10.43 ? 146 MSE C CA  1 
HETATM 5147 C  C   . MSE C 1 168 ? 12.122 28.849 34.954  1.00 9.31  ? 146 MSE C C   1 
HETATM 5148 O  O   . MSE C 1 168 ? 11.625 29.782 34.334  1.00 8.62  ? 146 MSE C O   1 
HETATM 5149 C  CB  . MSE C 1 168 ? 10.624 27.330 33.598  1.00 13.67 ? 146 MSE C CB  1 
HETATM 5150 C  CG  . MSE C 1 168 ? 10.904 28.003 32.262  1.00 17.51 ? 146 MSE C CG  1 
HETATM 5151 SE SE  . MSE C 1 168 ? 12.440 27.165 31.379  1.00 27.50 ? 146 MSE C SE  1 
HETATM 5152 C  CE  . MSE C 1 168 ? 11.561 25.529 30.688  1.00 23.75 ? 146 MSE C CE  1 
ATOM   5153 N  N   . LEU C 1 169 ? 13.015 29.025 35.921  1.00 8.26  ? 147 LEU C N   1 
ATOM   5154 C  CA  . LEU C 1 169 ? 13.479 30.363 36.315  1.00 7.92  ? 147 LEU C CA  1 
ATOM   5155 C  C   . LEU C 1 169 ? 14.463 30.972 35.321  1.00 7.55  ? 147 LEU C C   1 
ATOM   5156 O  O   . LEU C 1 169 ? 14.584 32.193 35.235  1.00 7.38  ? 147 LEU C O   1 
ATOM   5157 C  CB  . LEU C 1 169 ? 14.147 30.320 37.697  1.00 7.86  ? 147 LEU C CB  1 
ATOM   5158 C  CG  . LEU C 1 169 ? 13.194 30.408 38.889  1.00 8.03  ? 147 LEU C CG  1 
ATOM   5159 C  CD1 . LEU C 1 169 ? 13.885 29.931 40.156  1.00 8.07  ? 147 LEU C CD1 1 
ATOM   5160 C  CD2 . LEU C 1 169 ? 12.667 31.822 39.072  1.00 8.07  ? 147 LEU C CD2 1 
ATOM   5161 N  N   . LEU C 1 170 ? 15.168 30.134 34.571  1.00 7.29  ? 148 LEU C N   1 
ATOM   5162 C  CA  . LEU C 1 170 ? 16.299 30.621 33.788  1.00 7.17  ? 148 LEU C CA  1 
ATOM   5163 C  C   . LEU C 1 170 ? 15.974 31.813 32.862  1.00 7.19  ? 148 LEU C C   1 
ATOM   5164 O  O   . LEU C 1 170 ? 16.708 32.804 32.875  1.00 7.17  ? 148 LEU C O   1 
ATOM   5165 C  CB  . LEU C 1 170 ? 16.962 29.475 33.018  1.00 7.13  ? 148 LEU C CB  1 
ATOM   5166 C  CG  . LEU C 1 170 ? 18.325 29.782 32.401  1.00 7.10  ? 148 LEU C CG  1 
ATOM   5167 C  CD1 . LEU C 1 170 ? 19.319 30.232 33.460  1.00 7.09  ? 148 LEU C CD1 1 
ATOM   5168 C  CD2 . LEU C 1 170 ? 18.844 28.566 31.658  1.00 7.14  ? 148 LEU C CD2 1 
ATOM   5169 N  N   . PRO C 1 171 ? 14.877 31.746 32.079  1.00 7.28  ? 149 PRO C N   1 
ATOM   5170 C  CA  . PRO C 1 171 ? 14.606 32.890 31.190  1.00 7.55  ? 149 PRO C CA  1 
ATOM   5171 C  C   . PRO C 1 171 ? 14.227 34.188 31.918  1.00 7.90  ? 149 PRO C C   1 
ATOM   5172 O  O   . PRO C 1 171 ? 14.171 35.255 31.283  1.00 8.76  ? 149 PRO C O   1 
ATOM   5173 C  CB  . PRO C 1 171 ? 13.450 32.389 30.305  1.00 7.42  ? 149 PRO C CB  1 
ATOM   5174 C  CG  . PRO C 1 171 ? 12.815 31.288 31.077  1.00 7.39  ? 149 PRO C CG  1 
ATOM   5175 C  CD  . PRO C 1 171 ? 13.915 30.649 31.876  1.00 7.31  ? 149 PRO C CD  1 
ATOM   5176 N  N   . TRP C 1 172 ? 13.973 34.110 33.222  1.00 7.86  ? 150 TRP C N   1 
ATOM   5177 C  CA  . TRP C 1 172 ? 13.715 35.309 34.036  1.00 7.97  ? 150 TRP C CA  1 
ATOM   5178 C  C   . TRP C 1 172 ? 14.996 35.922 34.604  1.00 8.37  ? 150 TRP C C   1 
ATOM   5179 O  O   . TRP C 1 172 ? 15.018 37.109 34.962  1.00 8.78  ? 150 TRP C O   1 
ATOM   5180 C  CB  . TRP C 1 172 ? 12.735 34.983 35.162  1.00 7.64  ? 150 TRP C CB  1 
ATOM   5181 C  CG  . TRP C 1 172 ? 11.411 34.558 34.633  1.00 7.42  ? 150 TRP C CG  1 
ATOM   5182 C  CD1 . TRP C 1 172 ? 10.997 33.290 34.382  1.00 7.31  ? 150 TRP C CD1 1 
ATOM   5183 C  CD2 . TRP C 1 172 ? 10.342 35.417 34.239  1.00 7.19  ? 150 TRP C CD2 1 
ATOM   5184 N  NE1 . TRP C 1 172 ? 9.726  33.299 33.862  1.00 7.27  ? 150 TRP C NE1 1 
ATOM   5185 C  CE2 . TRP C 1 172 ? 9.300  34.597 33.765  1.00 7.20  ? 150 TRP C CE2 1 
ATOM   5186 C  CE3 . TRP C 1 172 ? 10.158 36.802 34.255  1.00 7.20  ? 150 TRP C CE3 1 
ATOM   5187 C  CZ2 . TRP C 1 172 ? 8.090  35.116 33.312  1.00 7.07  ? 150 TRP C CZ2 1 
ATOM   5188 C  CZ3 . TRP C 1 172 ? 8.955  37.316 33.802  1.00 7.12  ? 150 TRP C CZ3 1 
ATOM   5189 C  CH2 . TRP C 1 172 ? 7.941  36.476 33.338  1.00 7.04  ? 150 TRP C CH2 1 
ATOM   5190 N  N   . ILE C 1 173 ? 16.059 35.126 34.665  1.00 8.44  ? 151 ILE C N   1 
ATOM   5191 C  CA  . ILE C 1 173 ? 17.334 35.561 35.241  1.00 8.61  ? 151 ILE C CA  1 
ATOM   5192 C  C   . ILE C 1 173 ? 18.336 36.005 34.173  1.00 8.79  ? 151 ILE C C   1 
ATOM   5193 O  O   . ILE C 1 173 ? 19.077 36.973 34.376  1.00 8.76  ? 151 ILE C O   1 
ATOM   5194 C  CB  . ILE C 1 173 ? 17.954 34.435 36.097  1.00 8.66  ? 151 ILE C CB  1 
ATOM   5195 C  CG1 . ILE C 1 173 ? 16.953 33.935 37.150  1.00 8.72  ? 151 ILE C CG1 1 
ATOM   5196 C  CG2 . ILE C 1 173 ? 19.256 34.896 36.749  1.00 8.70  ? 151 ILE C CG2 1 
ATOM   5197 C  CD1 . ILE C 1 173 ? 16.470 34.980 38.129  1.00 8.83  ? 151 ILE C CD1 1 
ATOM   5198 N  N   . VAL C 1 174 ? 18.372 35.291 33.050  1.00 8.97  ? 152 VAL C N   1 
ATOM   5199 C  CA  . VAL C 1 174 ? 19.294 35.585 31.958  1.00 9.32  ? 152 VAL C CA  1 
ATOM   5200 C  C   . VAL C 1 174 ? 18.478 35.881 30.694  1.00 9.80  ? 152 VAL C C   1 
ATOM   5201 O  O   . VAL C 1 174 ? 17.267 35.709 30.691  1.00 10.38 ? 152 VAL C O   1 
ATOM   5202 C  CB  . VAL C 1 174 ? 20.289 34.420 31.722  1.00 9.12  ? 152 VAL C CB  1 
ATOM   5203 C  CG1 . VAL C 1 174 ? 20.976 34.025 33.026  1.00 9.15  ? 152 VAL C CG1 1 
ATOM   5204 C  CG2 . VAL C 1 174 ? 19.602 33.210 31.101  1.00 9.14  ? 152 VAL C CG2 1 
ATOM   5205 N  N   . GLY C 1 175 ? 19.123 36.313 29.616  1.00 10.51 ? 153 GLY C N   1 
ATOM   5206 C  CA  . GLY C 1 175 ? 18.371 36.633 28.385  1.00 10.74 ? 153 GLY C CA  1 
ATOM   5207 C  C   . GLY C 1 175 ? 17.644 35.415 27.811  1.00 10.73 ? 153 GLY C C   1 
ATOM   5208 O  O   . GLY C 1 175 ? 18.005 34.277 28.132  1.00 11.70 ? 153 GLY C O   1 
ATOM   5209 N  N   . PRO C 1 176 ? 16.604 35.626 26.972  1.00 10.16 ? 154 PRO C N   1 
ATOM   5210 C  CA  . PRO C 1 176 ? 15.892 34.491 26.354  1.00 9.66  ? 154 PRO C CA  1 
ATOM   5211 C  C   . PRO C 1 176 ? 16.764 33.585 25.476  1.00 9.23  ? 154 PRO C C   1 
ATOM   5212 O  O   . PRO C 1 176 ? 16.613 32.367 25.523  1.00 8.93  ? 154 PRO C O   1 
ATOM   5213 C  CB  . PRO C 1 176 ? 14.794 35.157 25.510  1.00 9.90  ? 154 PRO C CB  1 
ATOM   5214 C  CG  . PRO C 1 176 ? 15.213 36.574 25.371  1.00 10.04 ? 154 PRO C CG  1 
ATOM   5215 C  CD  . PRO C 1 176 ? 15.991 36.914 26.603  1.00 10.15 ? 154 PRO C CD  1 
ATOM   5216 N  N   . LYS C 1 177 ? 17.661 34.168 24.684  1.00 8.79  ? 155 LYS C N   1 
ATOM   5217 C  CA  . LYS C 1 177 ? 18.524 33.365 23.814  1.00 8.51  ? 155 LYS C CA  1 
ATOM   5218 C  C   . LYS C 1 177 ? 19.453 32.471 24.619  1.00 8.10  ? 155 LYS C C   1 
ATOM   5219 O  O   . LYS C 1 177 ? 19.678 31.319 24.265  1.00 7.49  ? 155 LYS C O   1 
ATOM   5220 C  CB  . LYS C 1 177 ? 19.351 34.254 22.899  1.00 8.77  ? 155 LYS C CB  1 
ATOM   5221 C  CG  . LYS C 1 177 ? 18.503 34.978 21.875  1.00 9.14  ? 155 LYS C CG  1 
ATOM   5222 C  CD  . LYS C 1 177 ? 19.146 34.966 20.512  1.00 9.16  ? 155 LYS C CD  1 
ATOM   5223 C  CE  . LYS C 1 177 ? 18.276 35.658 19.487  1.00 8.95  ? 155 LYS C CE  1 
ATOM   5224 N  NZ  . LYS C 1 177 ? 18.107 34.776 18.301  1.00 8.78  ? 155 LYS C NZ  1 
ATOM   5225 N  N   . ILE C 1 178 ? 19.985 33.019 25.704  1.00 7.83  ? 156 ILE C N   1 
ATOM   5226 C  CA  . ILE C 1 178 ? 20.906 32.285 26.558  1.00 7.84  ? 156 ILE C CA  1 
ATOM   5227 C  C   . ILE C 1 178 ? 20.179 31.168 27.308  1.00 7.45  ? 156 ILE C C   1 
ATOM   5228 O  O   . ILE C 1 178 ? 20.694 30.049 27.429  1.00 7.09  ? 156 ILE C O   1 
ATOM   5229 C  CB  . ILE C 1 178 ? 21.624 33.243 27.535  1.00 8.29  ? 156 ILE C CB  1 
ATOM   5230 C  CG1 . ILE C 1 178 ? 22.366 34.352 26.767  1.00 8.68  ? 156 ILE C CG1 1 
ATOM   5231 C  CG2 . ILE C 1 178 ? 22.569 32.474 28.442  1.00 8.50  ? 156 ILE C CG2 1 
ATOM   5232 C  CD1 . ILE C 1 178 ? 23.319 33.873 25.710  1.00 8.92  ? 156 ILE C CD1 1 
ATOM   5233 N  N   . ALA C 1 179 ? 18.978 31.461 27.798  1.00 7.16  ? 157 ALA C N   1 
ATOM   5234 C  CA  . ALA C 1 179 ? 18.186 30.444 28.488  1.00 7.03  ? 157 ALA C CA  1 
ATOM   5235 C  C   . ALA C 1 179 ? 17.826 29.289 27.551  1.00 7.04  ? 157 ALA C C   1 
ATOM   5236 O  O   . ALA C 1 179 ? 17.894 28.113 27.934  1.00 6.93  ? 157 ALA C O   1 
ATOM   5237 C  CB  . ALA C 1 179 ? 16.933 31.061 29.092  1.00 6.98  ? 157 ALA C CB  1 
ATOM   5238 N  N   . LYS C 1 180 ? 17.454 29.612 26.315  1.00 7.04  ? 158 LYS C N   1 
ATOM   5239 C  CA  . LYS C 1 180 ? 17.105 28.577 25.344  1.00 7.18  ? 158 LYS C CA  1 
ATOM   5240 C  C   . LYS C 1 180 ? 18.293 27.682 25.018  1.00 6.97  ? 158 LYS C C   1 
ATOM   5241 O  O   . LYS C 1 180 ? 18.155 26.464 24.946  1.00 6.74  ? 158 LYS C O   1 
ATOM   5242 C  CB  . LYS C 1 180 ? 16.531 29.194 24.077  1.00 7.56  ? 158 LYS C CB  1 
ATOM   5243 C  CG  . LYS C 1 180 ? 15.139 29.751 24.294  1.00 8.04  ? 158 LYS C CG  1 
ATOM   5244 C  CD  . LYS C 1 180 ? 14.517 30.135 22.977  1.00 8.41  ? 158 LYS C CD  1 
ATOM   5245 C  CE  . LYS C 1 180 ? 13.079 30.566 23.151  1.00 8.77  ? 158 LYS C CE  1 
ATOM   5246 N  NZ  . LYS C 1 180 ? 12.548 31.119 21.880  1.00 9.05  ? 158 LYS C NZ  1 
ATOM   5247 N  N   . GLU C 1 181 ? 19.460 28.289 24.840  1.00 6.82  ? 159 GLU C N   1 
ATOM   5248 C  CA  . GLU C 1 181 ? 20.679 27.532 24.591  1.00 6.89  ? 159 GLU C CA  1 
ATOM   5249 C  C   . GLU C 1 181 ? 20.981 26.571 25.738  1.00 6.71  ? 159 GLU C C   1 
ATOM   5250 O  O   . GLU C 1 181 ? 21.238 25.392 25.517  1.00 6.55  ? 159 GLU C O   1 
ATOM   5251 C  CB  . GLU C 1 181 ? 21.862 28.477 24.405  1.00 7.19  ? 159 GLU C CB  1 
ATOM   5252 C  CG  . GLU C 1 181 ? 23.184 27.747 24.249  1.00 7.54  ? 159 GLU C CG  1 
ATOM   5253 C  CD  . GLU C 1 181 ? 24.375 28.671 24.130  1.00 7.82  ? 159 GLU C CD  1 
ATOM   5254 O  OE1 . GLU C 1 181 ? 24.216 29.907 24.203  1.00 8.05  ? 159 GLU C OE1 1 
ATOM   5255 O  OE2 . GLU C 1 181 ? 25.499 28.148 23.975  1.00 8.42  ? 159 GLU C OE2 1 
ATOM   5256 N  N   . ILE C 1 182 ? 20.980 27.081 26.966  1.00 6.52  ? 160 ILE C N   1 
ATOM   5257 C  CA  . ILE C 1 182 ? 21.347 26.249 28.111  1.00 6.56  ? 160 ILE C CA  1 
ATOM   5258 C  C   . ILE C 1 182 ? 20.374 25.087 28.287  1.00 6.63  ? 160 ILE C C   1 
ATOM   5259 O  O   . ILE C 1 182 ? 20.789 23.942 28.495  1.00 6.75  ? 160 ILE C O   1 
ATOM   5260 C  CB  . ILE C 1 182 ? 21.468 27.078 29.406  1.00 6.56  ? 160 ILE C CB  1 
ATOM   5261 C  CG1 . ILE C 1 182 ? 22.706 27.981 29.305  1.00 6.59  ? 160 ILE C CG1 1 
ATOM   5262 C  CG2 . ILE C 1 182 ? 21.541 26.168 30.629  1.00 6.57  ? 160 ILE C CG2 1 
ATOM   5263 C  CD1 . ILE C 1 182 ? 22.802 29.053 30.364  1.00 6.65  ? 160 ILE C CD1 1 
ATOM   5264 N  N   . ILE C 1 183 ? 19.082 25.374 28.198  1.00 6.70  ? 161 ILE C N   1 
ATOM   5265 C  CA  . ILE C 1 183 ? 18.065 24.353 28.435  1.00 6.76  ? 161 ILE C CA  1 
ATOM   5266 C  C   . ILE C 1 183 ? 17.906 23.386 27.257  1.00 7.05  ? 161 ILE C C   1 
ATOM   5267 O  O   . ILE C 1 183 ? 17.859 22.173 27.464  1.00 6.96  ? 161 ILE C O   1 
ATOM   5268 C  CB  . ILE C 1 183 ? 16.732 25.005 28.869  1.00 6.79  ? 161 ILE C CB  1 
ATOM   5269 C  CG1 . ILE C 1 183 ? 16.860 25.422 30.335  1.00 6.78  ? 161 ILE C CG1 1 
ATOM   5270 C  CG2 . ILE C 1 183 ? 15.552 24.052 28.696  1.00 6.75  ? 161 ILE C CG2 1 
ATOM   5271 C  CD1 . ILE C 1 183 ? 15.801 26.380 30.817  1.00 6.82  ? 161 ILE C CD1 1 
ATOM   5272 N  N   . LEU C 1 184 ? 17.841 23.899 26.032  1.00 7.36  ? 162 LEU C N   1 
ATOM   5273 C  CA  . LEU C 1 184 ? 17.591 23.020 24.885  1.00 7.84  ? 162 LEU C CA  1 
ATOM   5274 C  C   . LEU C 1 184 ? 18.787 22.122 24.580  1.00 8.22  ? 162 LEU C C   1 
ATOM   5275 O  O   . LEU C 1 184 ? 18.614 20.995 24.103  1.00 8.37  ? 162 LEU C O   1 
ATOM   5276 C  CB  . LEU C 1 184 ? 17.173 23.812 23.645  1.00 7.97  ? 162 LEU C CB  1 
ATOM   5277 C  CG  . LEU C 1 184 ? 15.796 24.485 23.717  1.00 8.06  ? 162 LEU C CG  1 
ATOM   5278 C  CD1 . LEU C 1 184 ? 15.560 25.320 22.468  1.00 8.19  ? 162 LEU C CD1 1 
ATOM   5279 C  CD2 . LEU C 1 184 ? 14.675 23.471 23.893  1.00 8.20  ? 162 LEU C CD2 1 
ATOM   5280 N  N   . LEU C 1 185 ? 19.994 22.599 24.876  1.00 8.58  ? 163 LEU C N   1 
ATOM   5281 C  CA  . LEU C 1 185 ? 21.203 21.793 24.670  1.00 9.00  ? 163 LEU C CA  1 
ATOM   5282 C  C   . LEU C 1 185 ? 21.646 21.055 25.927  1.00 9.44  ? 163 LEU C C   1 
ATOM   5283 O  O   . LEU C 1 185 ? 22.558 20.224 25.875  1.00 10.06 ? 163 LEU C O   1 
ATOM   5284 C  CB  . LEU C 1 185 ? 22.350 22.660 24.153  1.00 9.00  ? 163 LEU C CB  1 
ATOM   5285 C  CG  . LEU C 1 185 ? 22.031 23.493 22.909  1.00 9.11  ? 163 LEU C CG  1 
ATOM   5286 C  CD1 . LEU C 1 185 ? 23.274 24.230 22.447  1.00 9.15  ? 163 LEU C CD1 1 
ATOM   5287 C  CD2 . LEU C 1 185 ? 21.466 22.623 21.795  1.00 9.17  ? 163 LEU C CD2 1 
ATOM   5288 N  N   . GLY C 1 186 ? 21.018 21.347 27.058  1.00 9.45  ? 164 GLY C N   1 
ATOM   5289 C  CA  . GLY C 1 186 ? 21.425 20.733 28.316  1.00 9.60  ? 164 GLY C CA  1 
ATOM   5290 C  C   . GLY C 1 186 ? 22.847 21.080 28.723  1.00 9.89  ? 164 GLY C C   1 
ATOM   5291 O  O   . GLY C 1 186 ? 23.581 20.223 29.215  1.00 9.91  ? 164 GLY C O   1 
ATOM   5292 N  N   . GLU C 1 187 ? 23.238 22.337 28.525  1.00 10.21 ? 165 GLU C N   1 
ATOM   5293 C  CA  . GLU C 1 187 ? 24.569 22.794 28.918  1.00 10.76 ? 165 GLU C CA  1 
ATOM   5294 C  C   . GLU C 1 187 ? 24.740 22.573 30.411  1.00 10.52 ? 165 GLU C C   1 
ATOM   5295 O  O   . GLU C 1 187 ? 23.900 22.997 31.204  1.00 10.10 ? 165 GLU C O   1 
ATOM   5296 C  CB  . GLU C 1 187 ? 24.772 24.277 28.587  1.00 11.63 ? 165 GLU C CB  1 
ATOM   5297 C  CG  . GLU C 1 187 ? 24.783 24.610 27.102  1.00 12.67 ? 165 GLU C CG  1 
ATOM   5298 C  CD  . GLU C 1 187 ? 25.940 23.967 26.356  1.00 14.00 ? 165 GLU C CD  1 
ATOM   5299 O  OE1 . GLU C 1 187 ? 27.091 24.032 26.839  1.00 16.19 ? 165 GLU C OE1 1 
ATOM   5300 O  OE2 . GLU C 1 187 ? 25.701 23.398 25.274  1.00 15.62 ? 165 GLU C OE2 1 
ATOM   5301 N  N   . ASP C 1 188 ? 25.823 21.896 30.789  1.00 10.26 ? 166 ASP C N   1 
ATOM   5302 C  CA  . ASP C 1 188 ? 26.061 21.540 32.186  1.00 10.17 ? 166 ASP C CA  1 
ATOM   5303 C  C   . ASP C 1 188 ? 27.508 21.776 32.628  1.00 10.10 ? 166 ASP C C   1 
ATOM   5304 O  O   . ASP C 1 188 ? 27.944 21.213 33.633  1.00 9.76  ? 166 ASP C O   1 
ATOM   5305 C  CB  . ASP C 1 188 ? 25.657 20.078 32.418  1.00 10.30 ? 166 ASP C CB  1 
ATOM   5306 C  CG  . ASP C 1 188 ? 26.392 19.107 31.510  1.00 10.43 ? 166 ASP C CG  1 
ATOM   5307 O  OD1 . ASP C 1 188 ? 27.313 19.538 30.782  1.00 10.65 ? 166 ASP C OD1 1 
ATOM   5308 O  OD2 . ASP C 1 188 ? 26.045 17.900 31.524  1.00 10.95 ? 166 ASP C OD2 1 
ATOM   5309 N  N   . ARG C 1 189 ? 28.237 22.603 31.882  1.00 10.08 ? 167 ARG C N   1 
ATOM   5310 C  CA  . ARG C 1 189 ? 29.612 22.976 32.241  1.00 10.36 ? 167 ARG C CA  1 
ATOM   5311 C  C   . ARG C 1 189 ? 29.841 24.477 32.047  1.00 9.76  ? 167 ARG C C   1 
ATOM   5312 O  O   . ARG C 1 189 ? 30.931 24.914 31.655  1.00 9.84  ? 167 ARG C O   1 
ATOM   5313 C  CB  . ARG C 1 189 ? 30.616 22.170 31.412  1.00 11.26 ? 167 ARG C CB  1 
ATOM   5314 C  CG  . ARG C 1 189 ? 30.566 20.667 31.645  1.00 12.18 ? 167 ARG C CG  1 
ATOM   5315 C  CD  . ARG C 1 189 ? 31.084 20.304 33.028  1.00 13.37 ? 167 ARG C CD  1 
ATOM   5316 N  NE  . ARG C 1 189 ? 31.127 18.859 33.267  1.00 14.73 ? 167 ARG C NE  1 
ATOM   5317 C  CZ  . ARG C 1 189 ? 30.134 18.118 33.764  1.00 15.53 ? 167 ARG C CZ  1 
ATOM   5318 N  NH1 . ARG C 1 189 ? 28.952 18.649 34.091  1.00 15.66 ? 167 ARG C NH1 1 
ATOM   5319 N  NH2 . ARG C 1 189 ? 30.332 16.814 33.940  1.00 16.45 ? 167 ARG C NH2 1 
ATOM   5320 N  N   . VAL C 1 190 ? 28.816 25.268 32.342  1.00 8.99  ? 168 VAL C N   1 
ATOM   5321 C  CA  . VAL C 1 190 ? 28.912 26.710 32.183  1.00 8.65  ? 168 VAL C CA  1 
ATOM   5322 C  C   . VAL C 1 190 ? 29.812 27.247 33.294  1.00 8.41  ? 168 VAL C C   1 
ATOM   5323 O  O   . VAL C 1 190 ? 29.451 27.162 34.463  1.00 7.98  ? 168 VAL C O   1 
ATOM   5324 C  CB  . VAL C 1 190 ? 27.530 27.384 32.257  1.00 8.60  ? 168 VAL C CB  1 
ATOM   5325 C  CG1 . VAL C 1 190 ? 27.668 28.889 32.055  1.00 8.61  ? 168 VAL C CG1 1 
ATOM   5326 C  CG2 . VAL C 1 190 ? 26.587 26.768 31.226  1.00 8.66  ? 168 VAL C CG2 1 
ATOM   5327 N  N   . PRO C 1 191 ? 30.992 27.794 32.939  1.00 8.50  ? 169 PRO C N   1 
ATOM   5328 C  CA  . PRO C 1 191 ? 31.902 28.231 33.997  1.00 8.60  ? 169 PRO C CA  1 
ATOM   5329 C  C   . PRO C 1 191 ? 31.393 29.436 34.776  1.00 8.73  ? 169 PRO C C   1 
ATOM   5330 O  O   . PRO C 1 191 ? 30.592 30.223 34.262  1.00 8.49  ? 169 PRO C O   1 
ATOM   5331 C  CB  . PRO C 1 191 ? 33.191 28.604 33.243  1.00 8.76  ? 169 PRO C CB  1 
ATOM   5332 C  CG  . PRO C 1 191 ? 33.034 28.057 31.872  1.00 8.88  ? 169 PRO C CG  1 
ATOM   5333 C  CD  . PRO C 1 191 ? 31.567 28.015 31.601  1.00 8.66  ? 169 PRO C CD  1 
ATOM   5334 N  N   . ALA C 1 192 ? 31.884 29.587 36.004  1.00 8.94  ? 170 ALA C N   1 
ATOM   5335 C  CA  . ALA C 1 192 ? 31.469 30.680 36.877  1.00 9.19  ? 170 ALA C CA  1 
ATOM   5336 C  C   . ALA C 1 192 ? 31.612 32.044 36.211  1.00 9.39  ? 170 ALA C C   1 
ATOM   5337 O  O   . ALA C 1 192 ? 30.724 32.877 36.320  1.00 9.15  ? 170 ALA C O   1 
ATOM   5338 C  CB  . ALA C 1 192 ? 32.255 30.649 38.177  1.00 9.30  ? 170 ALA C CB  1 
ATOM   5339 N  N   . ARG C 1 193 ? 32.721 32.265 35.511  1.00 10.01 ? 171 ARG C N   1 
ATOM   5340 C  CA  . ARG C 1 193 ? 32.939 33.542 34.837  1.00 10.67 ? 171 ARG C CA  1 
ATOM   5341 C  C   . ARG C 1 193 ? 31.867 33.811 33.783  1.00 9.45  ? 171 ARG C C   1 
ATOM   5342 O  O   . ARG C 1 193 ? 31.405 34.946 33.643  1.00 9.26  ? 171 ARG C O   1 
ATOM   5343 C  CB  . ARG C 1 193 ? 34.339 33.607 34.220  1.00 12.42 ? 171 ARG C CB  1 
ATOM   5344 C  CG  . ARG C 1 193 ? 35.467 33.688 35.242  1.00 14.60 ? 171 ARG C CG  1 
ATOM   5345 C  CD  . ARG C 1 193 ? 35.497 35.017 35.980  1.00 16.80 ? 171 ARG C CD  1 
ATOM   5346 N  NE  . ARG C 1 193 ? 36.633 35.140 36.899  1.00 19.39 ? 171 ARG C NE  1 
ATOM   5347 C  CZ  . ARG C 1 193 ? 36.878 36.206 37.664  1.00 21.17 ? 171 ARG C CZ  1 
ATOM   5348 N  NH1 . ARG C 1 193 ? 36.081 37.268 37.629  1.00 22.20 ? 171 ARG C NH1 1 
ATOM   5349 N  NH2 . ARG C 1 193 ? 37.938 36.220 38.467  1.00 22.77 ? 171 ARG C NH2 1 
ATOM   5350 N  N   . ARG C 1 194 ? 31.460 32.775 33.055  1.00 8.43  ? 172 ARG C N   1 
ATOM   5351 C  CA  . ARG C 1 194 ? 30.407 32.930 32.050  1.00 7.86  ? 172 ARG C CA  1 
ATOM   5352 C  C   . ARG C 1 194 ? 29.054 33.150 32.725  1.00 7.56  ? 172 ARG C C   1 
ATOM   5353 O  O   . ARG C 1 194 ? 28.262 33.980 32.283  1.00 7.41  ? 172 ARG C O   1 
ATOM   5354 C  CB  . ARG C 1 194 ? 30.348 31.725 31.118  1.00 7.78  ? 172 ARG C CB  1 
ATOM   5355 C  CG  . ARG C 1 194 ? 29.224 31.766 30.089  1.00 7.73  ? 172 ARG C CG  1 
ATOM   5356 C  CD  . ARG C 1 194 ? 29.306 32.981 29.180  1.00 7.66  ? 172 ARG C CD  1 
ATOM   5357 N  NE  . ARG C 1 194 ? 28.238 32.971 28.179  1.00 7.64  ? 172 ARG C NE  1 
ATOM   5358 C  CZ  . ARG C 1 194 ? 27.801 34.046 27.519  1.00 7.70  ? 172 ARG C CZ  1 
ATOM   5359 N  NH1 . ARG C 1 194 ? 28.335 35.245 27.738  1.00 7.77  ? 172 ARG C NH1 1 
ATOM   5360 N  NH2 . ARG C 1 194 ? 26.811 33.919 26.644  1.00 7.78  ? 172 ARG C NH2 1 
ATOM   5361 N  N   . ALA C 1 195 ? 28.800 32.401 33.791  1.00 7.28  ? 173 ALA C N   1 
ATOM   5362 C  CA  . ALA C 1 195 ? 27.596 32.594 34.598  1.00 7.20  ? 173 ALA C CA  1 
ATOM   5363 C  C   . ALA C 1 195 ? 27.513 34.032 35.105  1.00 7.28  ? 173 ALA C C   1 
ATOM   5364 O  O   . ALA C 1 195 ? 26.431 34.608 35.156  1.00 7.14  ? 173 ALA C O   1 
ATOM   5365 C  CB  . ALA C 1 195 ? 27.556 31.605 35.753  1.00 7.23  ? 173 ALA C CB  1 
ATOM   5366 N  N   . ALA C 1 196 ? 28.652 34.623 35.461  1.00 7.38  ? 174 ALA C N   1 
ATOM   5367 C  CA  . ALA C 1 196 ? 28.659 36.028 35.879  1.00 7.56  ? 174 ALA C CA  1 
ATOM   5368 C  C   . ALA C 1 196 ? 28.334 36.979 34.721  1.00 7.90  ? 174 ALA C C   1 
ATOM   5369 O  O   . ALA C 1 196 ? 27.598 37.954 34.907  1.00 8.20  ? 174 ALA C O   1 
ATOM   5370 C  CB  . ALA C 1 196 ? 29.984 36.398 36.532  1.00 7.63  ? 174 ALA C CB  1 
ATOM   5371 N  N   . GLU C 1 197 ? 28.868 36.699 33.533  1.00 8.19  ? 175 GLU C N   1 
ATOM   5372 C  CA  . GLU C 1 197 ? 28.596 37.526 32.347  1.00 8.54  ? 175 GLU C CA  1 
ATOM   5373 C  C   . GLU C 1 197 ? 27.120 37.597 32.013  1.00 8.39  ? 175 GLU C C   1 
ATOM   5374 O  O   . GLU C 1 197 ? 26.641 38.628 31.544  1.00 8.33  ? 175 GLU C O   1 
ATOM   5375 C  CB  . GLU C 1 197 ? 29.333 36.996 31.117  1.00 9.15  ? 175 GLU C CB  1 
ATOM   5376 C  CG  . GLU C 1 197 ? 30.830 37.210 31.160  1.00 9.80  ? 175 GLU C CG  1 
ATOM   5377 C  CD  . GLU C 1 197 ? 31.569 36.469 30.062  1.00 10.41 ? 175 GLU C CD  1 
ATOM   5378 O  OE1 . GLU C 1 197 ? 30.933 35.963 29.105  1.00 10.78 ? 175 GLU C OE1 1 
ATOM   5379 O  OE2 . GLU C 1 197 ? 32.816 36.413 30.150  1.00 11.83 ? 175 GLU C OE2 1 
ATOM   5380 N  N   . ILE C 1 198 ? 26.402 36.500 32.233  1.00 8.27  ? 176 ILE C N   1 
ATOM   5381 C  CA  . ILE C 1 198 ? 25.002 36.427 31.814  1.00 8.33  ? 176 ILE C CA  1 
ATOM   5382 C  C   . ILE C 1 198 ? 24.012 36.796 32.922  1.00 8.70  ? 176 ILE C C   1 
ATOM   5383 O  O   . ILE C 1 198 ? 22.808 36.844 32.674  1.00 8.90  ? 176 ILE C O   1 
ATOM   5384 C  CB  . ILE C 1 198 ? 24.660 35.054 31.180  1.00 8.15  ? 176 ILE C CB  1 
ATOM   5385 C  CG1 . ILE C 1 198 ? 24.719 33.916 32.210  1.00 8.04  ? 176 ILE C CG1 1 
ATOM   5386 C  CG2 . ILE C 1 198 ? 25.590 34.790 29.995  1.00 8.15  ? 176 ILE C CG2 1 
ATOM   5387 C  CD1 . ILE C 1 198 ? 24.424 32.545 31.640  1.00 8.13  ? 176 ILE C CD1 1 
ATOM   5388 N  N   . GLY C 1 199 ? 24.517 37.062 34.128  1.00 9.04  ? 177 GLY C N   1 
ATOM   5389 C  CA  . GLY C 1 199 ? 23.689 37.521 35.246  1.00 9.43  ? 177 GLY C CA  1 
ATOM   5390 C  C   . GLY C 1 199 ? 23.162 36.429 36.166  1.00 9.97  ? 177 GLY C C   1 
ATOM   5391 O  O   . GLY C 1 199 ? 22.321 36.697 37.023  1.00 9.88  ? 177 GLY C O   1 
HETATM 5392 N  N   . MSE C 1 200 ? 23.652 35.204 35.990  1.00 10.79 ? 178 MSE C N   1 
HETATM 5393 C  CA  . MSE C 1 200 ? 23.301 34.078 36.862  1.00 11.90 ? 178 MSE C CA  1 
HETATM 5394 C  C   . MSE C 1 200 ? 24.065 34.129 38.159  1.00 10.54 ? 178 MSE C C   1 
HETATM 5395 O  O   . MSE C 1 200 ? 23.591 33.631 39.177  1.00 10.13 ? 178 MSE C O   1 
HETATM 5396 C  CB  . MSE C 1 200 ? 23.621 32.775 36.127  1.00 15.06 ? 178 MSE C CB  1 
HETATM 5397 C  CG  . MSE C 1 200 ? 23.322 31.542 36.971  1.00 18.63 ? 178 MSE C CG  1 
HETATM 5398 SE SE  . MSE C 1 200 ? 23.736 29.889 35.986  1.00 28.85 ? 178 MSE C SE  1 
HETATM 5399 C  CE  . MSE C 1 200 ? 23.266 30.467 34.173  1.00 24.37 ? 178 MSE C CE  1 
ATOM   5400 N  N   . VAL C 1 201 ? 25.258 34.716 38.122  1.00 9.33  ? 179 VAL C N   1 
ATOM   5401 C  CA  . VAL C 1 201 ? 26.128 34.831 39.291  1.00 8.90  ? 179 VAL C CA  1 
ATOM   5402 C  C   . VAL C 1 201 ? 26.479 36.303 39.494  1.00 8.66  ? 179 VAL C C   1 
ATOM   5403 O  O   . VAL C 1 201 ? 26.812 36.991 38.536  1.00 8.57  ? 179 VAL C O   1 
ATOM   5404 C  CB  . VAL C 1 201 ? 27.419 34.006 39.089  1.00 8.74  ? 179 VAL C CB  1 
ATOM   5405 C  CG1 . VAL C 1 201 ? 28.484 34.364 40.121  1.00 8.67  ? 179 VAL C CG1 1 
ATOM   5406 C  CG2 . VAL C 1 201 ? 27.103 32.519 39.135  1.00 8.67  ? 179 VAL C CG2 1 
ATOM   5407 N  N   . ASN C 1 202 ? 26.420 36.763 40.743  1.00 8.41  ? 180 ASN C N   1 
ATOM   5408 C  CA  . ASN C 1 202 ? 26.744 38.150 41.094  1.00 8.48  ? 180 ASN C CA  1 
ATOM   5409 C  C   . ASN C 1 202 ? 28.243 38.394 41.175  1.00 8.56  ? 180 ASN C C   1 
ATOM   5410 O  O   . ASN C 1 202 ? 28.736 39.404 40.669  1.00 8.32  ? 180 ASN C O   1 
ATOM   5411 C  CB  . ASN C 1 202 ? 26.120 38.528 42.443  1.00 8.37  ? 180 ASN C CB  1 
ATOM   5412 C  CG  . ASN C 1 202 ? 24.616 38.677 42.370  1.00 8.28  ? 180 ASN C CG  1 
ATOM   5413 O  OD1 . ASN C 1 202 ? 24.090 39.787 42.266  1.00 8.56  ? 180 ASN C OD1 1 
ATOM   5414 N  ND2 . ASN C 1 202 ? 23.921 37.572 42.401  1.00 8.08  ? 180 ASN C ND2 1 
ATOM   5415 N  N   . ARG C 1 203 ? 28.947 37.490 41.855  1.00 8.96  ? 181 ARG C N   1 
ATOM   5416 C  CA  . ARG C 1 203 ? 30.381 37.633 42.122  1.00 9.43  ? 181 ARG C CA  1 
ATOM   5417 C  C   . ARG C 1 203 ? 31.085 36.295 42.018  1.00 9.46  ? 181 ARG C C   1 
ATOM   5418 O  O   . ARG C 1 203 ? 30.574 35.274 42.492  1.00 9.04  ? 181 ARG C O   1 
ATOM   5419 C  CB  . ARG C 1 203 ? 30.615 38.174 43.533  1.00 9.90  ? 181 ARG C CB  1 
ATOM   5420 C  CG  . ARG C 1 203 ? 29.891 39.465 43.839  1.00 10.45 ? 181 ARG C CG  1 
ATOM   5421 C  CD  . ARG C 1 203 ? 30.207 39.976 45.233  1.00 11.05 ? 181 ARG C CD  1 
ATOM   5422 N  NE  . ARG C 1 203 ? 29.408 41.161 45.518  1.00 11.66 ? 181 ARG C NE  1 
ATOM   5423 C  CZ  . ARG C 1 203 ? 29.462 41.877 46.635  1.00 12.17 ? 181 ARG C CZ  1 
ATOM   5424 N  NH1 . ARG C 1 203 ? 30.290 41.542 47.618  1.00 12.71 ? 181 ARG C NH1 1 
ATOM   5425 N  NH2 . ARG C 1 203 ? 28.676 42.935 46.769  1.00 12.43 ? 181 ARG C NH2 1 
ATOM   5426 N  N   . VAL C 1 204 ? 32.264 36.313 41.404  1.00 9.74  ? 182 VAL C N   1 
ATOM   5427 C  CA  . VAL C 1 204 ? 33.150 35.164 41.396  1.00 10.21 ? 182 VAL C CA  1 
ATOM   5428 C  C   . VAL C 1 204 ? 34.301 35.477 42.344  1.00 10.82 ? 182 VAL C C   1 
ATOM   5429 O  O   . VAL C 1 204 ? 34.921 36.544 42.237  1.00 10.97 ? 182 VAL C O   1 
ATOM   5430 C  CB  . VAL C 1 204 ? 33.679 34.865 39.984  1.00 10.18 ? 182 VAL C CB  1 
ATOM   5431 C  CG1 . VAL C 1 204 ? 34.677 33.714 40.019  1.00 10.10 ? 182 VAL C CG1 1 
ATOM   5432 C  CG2 . VAL C 1 204 ? 32.521 34.536 39.052  1.00 10.17 ? 182 VAL C CG2 1 
ATOM   5433 N  N   . VAL C 1 205 ? 34.565 34.549 43.262  1.00 11.68 ? 183 VAL C N   1 
ATOM   5434 C  CA  . VAL C 1 205 ? 35.617 34.703 44.276  1.00 12.82 ? 183 VAL C CA  1 
ATOM   5435 C  C   . VAL C 1 205 ? 36.595 33.528 44.252  1.00 13.96 ? 183 VAL C C   1 
ATOM   5436 O  O   . VAL C 1 205 ? 36.346 32.511 43.608  1.00 13.79 ? 183 VAL C O   1 
ATOM   5437 C  CB  . VAL C 1 205 ? 35.018 34.843 45.693  1.00 13.05 ? 183 VAL C CB  1 
ATOM   5438 C  CG1 . VAL C 1 205 ? 34.108 36.057 45.761  1.00 13.24 ? 183 VAL C CG1 1 
ATOM   5439 C  CG2 . VAL C 1 205 ? 34.261 33.587 46.106  1.00 13.11 ? 183 VAL C CG2 1 
ATOM   5440 N  N   . ASP C 1 206 ? 37.706 33.671 44.972  1.00 15.95 ? 184 ASP C N   1 
ATOM   5441 C  CA  . ASP C 1 206 ? 38.662 32.576 45.134  1.00 17.55 ? 184 ASP C CA  1 
ATOM   5442 C  C   . ASP C 1 206 ? 38.051 31.414 45.906  1.00 17.45 ? 184 ASP C C   1 
ATOM   5443 O  O   . ASP C 1 206 ? 37.184 31.612 46.760  1.00 17.52 ? 184 ASP C O   1 
ATOM   5444 C  CB  . ASP C 1 206 ? 39.928 33.058 45.861  1.00 19.15 ? 184 ASP C CB  1 
ATOM   5445 C  CG  . ASP C 1 206 ? 40.861 33.838 44.957  1.00 21.08 ? 184 ASP C CG  1 
ATOM   5446 O  OD1 . ASP C 1 206 ? 40.587 33.933 43.740  1.00 23.13 ? 184 ASP C OD1 1 
ATOM   5447 O  OD2 . ASP C 1 206 ? 41.884 34.354 45.463  1.00 23.34 ? 184 ASP C OD2 1 
ATOM   5448 N  N   . GLY C 1 207 ? 38.530 30.207 45.614  1.00 17.65 ? 185 GLY C N   1 
ATOM   5449 C  CA  . GLY C 1 207 ? 38.023 28.988 46.239  1.00 17.76 ? 185 GLY C CA  1 
ATOM   5450 C  C   . GLY C 1 207 ? 38.083 28.990 47.756  1.00 17.95 ? 185 GLY C C   1 
ATOM   5451 O  O   . GLY C 1 207 ? 37.210 28.414 48.415  1.00 19.06 ? 185 GLY C O   1 
ATOM   5452 N  N   . ASP C 1 208 ? 39.101 29.648 48.309  1.00 17.61 ? 186 ASP C N   1 
ATOM   5453 C  CA  . ASP C 1 208 ? 39.269 29.743 49.761  1.00 17.39 ? 186 ASP C CA  1 
ATOM   5454 C  C   . ASP C 1 208 ? 38.555 30.937 50.382  1.00 15.71 ? 186 ASP C C   1 
ATOM   5455 O  O   . ASP C 1 208 ? 38.644 31.138 51.590  1.00 15.79 ? 186 ASP C O   1 
ATOM   5456 C  CB  . ASP C 1 208 ? 40.757 29.832 50.122  1.00 18.86 ? 186 ASP C CB  1 
ATOM   5457 C  CG  . ASP C 1 208 ? 41.531 28.596 49.732  1.00 20.70 ? 186 ASP C CG  1 
ATOM   5458 O  OD1 . ASP C 1 208 ? 40.942 27.495 49.690  1.00 22.41 ? 186 ASP C OD1 1 
ATOM   5459 O  OD2 . ASP C 1 208 ? 42.744 28.730 49.476  1.00 23.28 ? 186 ASP C OD2 1 
ATOM   5460 N  N   . GLY C 1 209 ? 37.845 31.721 49.570  1.00 13.93 ? 187 GLY C N   1 
ATOM   5461 C  CA  . GLY C 1 209 ? 37.196 32.937 50.047  1.00 12.66 ? 187 GLY C CA  1 
ATOM   5462 C  C   . GLY C 1 209 ? 35.680 32.913 49.983  1.00 11.57 ? 187 GLY C C   1 
ATOM   5463 O  O   . GLY C 1 209 ? 35.050 33.927 50.251  1.00 11.23 ? 187 GLY C O   1 
ATOM   5464 N  N   . LEU C 1 210 ? 35.093 31.762 49.655  1.00 10.74 ? 188 LEU C N   1 
ATOM   5465 C  CA  . LEU C 1 210 ? 33.642 31.678 49.432  1.00 10.22 ? 188 LEU C CA  1 
ATOM   5466 C  C   . LEU C 1 210 ? 32.833 31.944 50.699  1.00 10.10 ? 188 LEU C C   1 
ATOM   5467 O  O   . LEU C 1 210 ? 31.918 32.772 50.710  1.00 9.49  ? 188 LEU C O   1 
ATOM   5468 C  CB  . LEU C 1 210 ? 33.262 30.306 48.863  1.00 10.19 ? 188 LEU C CB  1 
ATOM   5469 C  CG  . LEU C 1 210 ? 31.780 30.098 48.527  1.00 10.04 ? 188 LEU C CG  1 
ATOM   5470 C  CD1 . LEU C 1 210 ? 31.327 31.067 47.439  1.00 10.02 ? 188 LEU C CD1 1 
ATOM   5471 C  CD2 . LEU C 1 210 ? 31.512 28.662 48.115  1.00 10.08 ? 188 LEU C CD2 1 
ATOM   5472 N  N   . ASP C 1 211 ? 33.162 31.230 51.768  1.00 10.20 ? 189 ASP C N   1 
ATOM   5473 C  CA  . ASP C 1 211 ? 32.393 31.342 53.002  1.00 10.39 ? 189 ASP C CA  1 
ATOM   5474 C  C   . ASP C 1 211 ? 32.510 32.734 53.615  1.00 9.85  ? 189 ASP C C   1 
ATOM   5475 O  O   . ASP C 1 211 ? 31.524 33.276 54.119  1.00 9.60  ? 189 ASP C O   1 
ATOM   5476 C  CB  . ASP C 1 211 ? 32.831 30.279 54.010  1.00 10.97 ? 189 ASP C CB  1 
ATOM   5477 C  CG  . ASP C 1 211 ? 32.338 28.888 53.649  1.00 11.69 ? 189 ASP C CG  1 
ATOM   5478 O  OD1 . ASP C 1 211 ? 31.142 28.735 53.314  1.00 12.57 ? 189 ASP C OD1 1 
ATOM   5479 O  OD2 . ASP C 1 211 ? 33.139 27.934 53.731  1.00 12.76 ? 189 ASP C OD2 1 
ATOM   5480 N  N   . ALA C 1 212 ? 33.709 33.312 53.557  1.00 9.44  ? 190 ALA C N   1 
ATOM   5481 C  CA  . ALA C 1 212 ? 33.938 34.665 54.064  1.00 9.44  ? 190 ALA C CA  1 
ATOM   5482 C  C   . ALA C 1 212 ? 33.128 35.708 53.293  1.00 9.48  ? 190 ALA C C   1 
ATOM   5483 O  O   . ALA C 1 212 ? 32.547 36.613 53.895  1.00 9.28  ? 190 ALA C O   1 
ATOM   5484 C  CB  . ALA C 1 212 ? 35.417 35.010 54.010  1.00 9.43  ? 190 ALA C CB  1 
ATOM   5485 N  N   . GLU C 1 213 ? 33.096 35.582 51.968  1.00 9.75  ? 191 GLU C N   1 
ATOM   5486 C  CA  . GLU C 1 213 ? 32.353 36.529 51.126  1.00 10.08 ? 191 GLU C CA  1 
ATOM   5487 C  C   . GLU C 1 213 ? 30.850 36.420 51.373  1.00 9.59  ? 191 GLU C C   1 
ATOM   5488 O  O   . GLU C 1 213 ? 30.165 37.435 51.511  1.00 9.27  ? 191 GLU C O   1 
ATOM   5489 C  CB  . GLU C 1 213 ? 32.649 36.293 49.644  1.00 10.88 ? 191 GLU C CB  1 
ATOM   5490 C  CG  . GLU C 1 213 ? 32.015 37.312 48.698  1.00 11.99 ? 191 GLU C CG  1 
ATOM   5491 C  CD  . GLU C 1 213 ? 32.734 38.650 48.659  1.00 13.24 ? 191 GLU C CD  1 
ATOM   5492 O  OE1 . GLU C 1 213 ? 33.769 38.816 49.349  1.00 14.82 ? 191 GLU C OE1 1 
ATOM   5493 O  OE2 . GLU C 1 213 ? 32.260 39.552 47.923  1.00 14.70 ? 191 GLU C OE2 1 
ATOM   5494 N  N   . ALA C 1 214 ? 30.338 35.192 51.431  1.00 9.29  ? 192 ALA C N   1 
ATOM   5495 C  CA  . ALA C 1 214 ? 28.915 34.984 51.696  1.00 9.10  ? 192 ALA C CA  1 
ATOM   5496 C  C   . ALA C 1 214 ? 28.521 35.569 53.052  1.00 9.16  ? 192 ALA C C   1 
ATOM   5497 O  O   . ALA C 1 214 ? 27.483 36.214 53.177  1.00 8.55  ? 192 ALA C O   1 
ATOM   5498 C  CB  . ALA C 1 214 ? 28.561 33.506 51.635  1.00 9.09  ? 192 ALA C CB  1 
ATOM   5499 N  N   . LEU C 1 215 ? 29.358 35.355 54.064  1.00 9.33  ? 193 LEU C N   1 
ATOM   5500 C  CA  . LEU C 1 215 ? 29.058 35.876 55.398  1.00 9.81  ? 193 LEU C CA  1 
ATOM   5501 C  C   . LEU C 1 215 ? 29.147 37.394 55.455  1.00 9.98  ? 193 LEU C C   1 
ATOM   5502 O  O   . LEU C 1 215 ? 28.363 38.033 56.150  1.00 10.05 ? 193 LEU C O   1 
ATOM   5503 C  CB  . LEU C 1 215 ? 29.975 35.256 56.465  1.00 10.14 ? 193 LEU C CB  1 
ATOM   5504 C  CG  . LEU C 1 215 ? 29.424 34.036 57.194  1.00 10.67 ? 193 LEU C CG  1 
ATOM   5505 C  CD1 . LEU C 1 215 ? 30.555 33.320 57.923  1.00 10.90 ? 193 LEU C CD1 1 
ATOM   5506 C  CD2 . LEU C 1 215 ? 28.318 34.437 58.165  1.00 10.76 ? 193 LEU C CD2 1 
ATOM   5507 N  N   . ARG C 1 216 ? 30.104 37.970 54.731  1.00 10.28 ? 194 ARG C N   1 
ATOM   5508 C  CA  . ARG C 1 216 ? 30.259 39.422 54.683  1.00 10.83 ? 194 ARG C CA  1 
ATOM   5509 C  C   . ARG C 1 216 ? 28.996 40.060 54.106  1.00 9.91  ? 194 ARG C C   1 
ATOM   5510 O  O   . ARG C 1 216 ? 28.481 41.042 54.636  1.00 9.72  ? 194 ARG C O   1 
ATOM   5511 C  CB  . ARG C 1 216 ? 31.491 39.794 53.849  1.00 12.31 ? 194 ARG C CB  1 
ATOM   5512 C  CG  . ARG C 1 216 ? 32.118 41.142 54.160  1.00 14.15 ? 194 ARG C CG  1 
ATOM   5513 C  CD  . ARG C 1 216 ? 33.620 41.161 53.852  1.00 15.50 ? 194 ARG C CD  1 
ATOM   5514 N  NE  . ARG C 1 216 ? 34.013 40.335 52.700  1.00 17.08 ? 194 ARG C NE  1 
ATOM   5515 C  CZ  . ARG C 1 216 ? 34.873 39.308 52.722  1.00 18.01 ? 194 ARG C CZ  1 
ATOM   5516 N  NH1 . ARG C 1 216 ? 35.497 38.932 53.842  1.00 18.63 ? 194 ARG C NH1 1 
ATOM   5517 N  NH2 . ARG C 1 216 ? 35.132 38.650 51.595  1.00 18.44 ? 194 ARG C NH2 1 
ATOM   5518 N  N   . ILE C 1 217 ? 28.491 39.478 53.025  1.00 9.22  ? 195 ILE C N   1 
ATOM   5519 C  CA  . ILE C 1 217 ? 27.272 39.972 52.391  1.00 8.75  ? 195 ILE C CA  1 
ATOM   5520 C  C   . ILE C 1 217 ? 26.093 39.823 53.351  1.00 8.37  ? 195 ILE C C   1 
ATOM   5521 O  O   . ILE C 1 217 ? 25.308 40.748 53.526  1.00 8.21  ? 195 ILE C O   1 
ATOM   5522 C  CB  . ILE C 1 217 ? 26.991 39.215 51.073  1.00 8.84  ? 195 ILE C CB  1 
ATOM   5523 C  CG1 . ILE C 1 217 ? 28.063 39.543 50.029  1.00 8.97  ? 195 ILE C CG1 1 
ATOM   5524 C  CG2 . ILE C 1 217 ? 25.606 39.555 50.526  1.00 8.92  ? 195 ILE C CG2 1 
ATOM   5525 C  CD1 . ILE C 1 217 ? 28.082 38.596 48.846  1.00 9.07  ? 195 ILE C CD1 1 
ATOM   5526 N  N   . ALA C 1 218 ? 25.970 38.652 53.966  1.00 8.03  ? 196 ALA C N   1 
ATOM   5527 C  CA  . ALA C 1 218 ? 24.848 38.378 54.861  1.00 7.96  ? 196 ALA C CA  1 
ATOM   5528 C  C   . ALA C 1 218 ? 24.872 39.279 56.107  1.00 7.99  ? 196 ALA C C   1 
ATOM   5529 O  O   . ALA C 1 218 ? 23.835 39.777 56.544  1.00 7.98  ? 196 ALA C O   1 
ATOM   5530 C  CB  . ALA C 1 218 ? 24.824 36.910 55.249  1.00 7.98  ? 196 ALA C CB  1 
ATOM   5531 N  N   . ARG C 1 219 ? 26.056 39.502 56.670  1.00 8.11  ? 197 ARG C N   1 
ATOM   5532 C  CA  . ARG C 1 219 ? 26.190 40.379 57.837  1.00 8.30  ? 197 ARG C CA  1 
ATOM   5533 C  C   . ARG C 1 219 ? 25.968 41.851 57.487  1.00 8.27  ? 197 ARG C C   1 
ATOM   5534 O  O   . ARG C 1 219 ? 25.489 42.627 58.313  1.00 8.33  ? 197 ARG C O   1 
ATOM   5535 C  CB  . ARG C 1 219 ? 27.553 40.193 58.494  1.00 8.47  ? 197 ARG C CB  1 
ATOM   5536 C  CG  . ARG C 1 219 ? 27.708 38.871 59.218  1.00 8.76  ? 197 ARG C CG  1 
ATOM   5537 C  CD  . ARG C 1 219 ? 29.073 38.784 59.868  1.00 9.10  ? 197 ARG C CD  1 
ATOM   5538 N  NE  . ARG C 1 219 ? 29.215 39.779 60.930  1.00 9.51  ? 197 ARG C NE  1 
ATOM   5539 C  CZ  . ARG C 1 219 ? 30.349 40.396 61.257  1.00 10.04 ? 197 ARG C CZ  1 
ATOM   5540 N  NH1 . ARG C 1 219 ? 31.473 40.155 60.597  1.00 10.24 ? 197 ARG C NH1 1 
ATOM   5541 N  NH2 . ARG C 1 219 ? 30.354 41.282 62.249  1.00 10.35 ? 197 ARG C NH2 1 
ATOM   5542 N  N   . HIS C 1 220 ? 26.331 42.237 56.270  1.00 8.40  ? 198 HIS C N   1 
ATOM   5543 C  CA  . HIS C 1 220 ? 26.016 43.569 55.757  1.00 8.65  ? 198 HIS C CA  1 
ATOM   5544 C  C   . HIS C 1 220 ? 24.500 43.781 55.762  1.00 8.69  ? 198 HIS C C   1 
ATOM   5545 O  O   . HIS C 1 220 ? 23.993 44.777 56.279  1.00 8.50  ? 198 HIS C O   1 
ATOM   5546 C  CB  . HIS C 1 220 ? 26.579 43.715 54.340  1.00 8.94  ? 198 HIS C CB  1 
ATOM   5547 C  CG  . HIS C 1 220 ? 26.428 45.080 53.755  1.00 9.38  ? 198 HIS C CG  1 
ATOM   5548 N  ND1 . HIS C 1 220 ? 27.493 45.938 53.593  1.00 9.66  ? 198 HIS C ND1 1 
ATOM   5549 C  CD2 . HIS C 1 220 ? 25.346 45.724 53.259  1.00 9.59  ? 198 HIS C CD2 1 
ATOM   5550 C  CE1 . HIS C 1 220 ? 27.071 47.061 53.042  1.00 9.85  ? 198 HIS C CE1 1 
ATOM   5551 N  NE2 . HIS C 1 220 ? 25.773 46.955 52.824  1.00 10.02 ? 198 HIS C NE2 1 
ATOM   5552 N  N   . ILE C 1 221 ? 23.782 42.823 55.191  1.00 8.91  ? 199 ILE C N   1 
ATOM   5553 C  CA  . ILE C 1 221 ? 22.322 42.839 55.212  1.00 9.10  ? 199 ILE C CA  1 
ATOM   5554 C  C   . ILE C 1 221 ? 21.816 42.877 56.652  1.00 9.17  ? 199 ILE C C   1 
ATOM   5555 O  O   . ILE C 1 221 ? 20.885 43.619 56.973  1.00 9.06  ? 199 ILE C O   1 
ATOM   5556 C  CB  . ILE C 1 221 ? 21.749 41.624 54.449  1.00 9.23  ? 199 ILE C CB  1 
ATOM   5557 C  CG1 . ILE C 1 221 ? 21.950 41.830 52.944  1.00 9.39  ? 199 ILE C CG1 1 
ATOM   5558 C  CG2 . ILE C 1 221 ? 20.272 41.424 54.759  1.00 9.25  ? 199 ILE C CG2 1 
ATOM   5559 C  CD1 . ILE C 1 221 ? 21.798 40.580 52.112  1.00 9.61  ? 199 ILE C CD1 1 
ATOM   5560 N  N   . GLY C 1 222 ? 22.448 42.094 57.519  1.00 9.28  ? 200 GLY C N   1 
ATOM   5561 C  CA  . GLY C 1 222 ? 22.050 42.011 58.921  1.00 9.51  ? 200 GLY C CA  1 
ATOM   5562 C  C   . GLY C 1 222 ? 22.213 43.284 59.734  1.00 9.65  ? 200 GLY C C   1 
ATOM   5563 O  O   . GLY C 1 222 ? 21.633 43.397 60.820  1.00 10.13 ? 200 GLY C O   1 
ATOM   5564 N  N   . ALA C 1 223 ? 22.986 44.243 59.228  1.00 9.67  ? 201 ALA C N   1 
ATOM   5565 C  CA  . ALA C 1 223 ? 23.162 45.531 59.906  1.00 9.87  ? 201 ALA C CA  1 
ATOM   5566 C  C   . ALA C 1 223 ? 21.984 46.475 59.674  1.00 10.00 ? 201 ALA C C   1 
ATOM   5567 O  O   . ALA C 1 223 ? 21.848 47.488 60.363  1.00 10.30 ? 201 ALA C O   1 
ATOM   5568 C  CB  . ALA C 1 223 ? 24.455 46.196 59.459  1.00 9.87  ? 201 ALA C CB  1 
ATOM   5569 N  N   . ILE C 1 224 ? 21.147 46.151 58.690  1.00 9.81  ? 202 ILE C N   1 
ATOM   5570 C  CA  . ILE C 1 224 ? 20.046 47.018 58.279  1.00 9.87  ? 202 ILE C CA  1 
ATOM   5571 C  C   . ILE C 1 224 ? 18.774 46.653 59.037  1.00 9.90  ? 202 ILE C C   1 
ATOM   5572 O  O   . ILE C 1 224 ? 18.546 45.488 59.345  1.00 9.86  ? 202 ILE C O   1 
ATOM   5573 C  CB  . ILE C 1 224 ? 19.800 46.894 56.758  1.00 9.75  ? 202 ILE C CB  1 
ATOM   5574 C  CG1 . ILE C 1 224 ? 21.093 47.194 55.992  1.00 9.93  ? 202 ILE C CG1 1 
ATOM   5575 C  CG2 . ILE C 1 224 ? 18.678 47.826 56.303  1.00 9.75  ? 202 ILE C CG2 1 
ATOM   5576 C  CD1 . ILE C 1 224 ? 21.049 46.831 54.523  1.00 9.90  ? 202 ILE C CD1 1 
ATOM   5577 N  N   . ASP C 1 225 ? 17.970 47.664 59.357  1.00 10.15 ? 203 ASP C N   1 
ATOM   5578 C  CA  . ASP C 1 225 ? 16.639 47.481 59.936  1.00 10.50 ? 203 ASP C CA  1 
ATOM   5579 C  C   . ASP C 1 225 ? 15.931 46.340 59.189  1.00 10.00 ? 203 ASP C C   1 
ATOM   5580 O  O   . ASP C 1 225 ? 15.735 46.446 57.983  1.00 9.59  ? 203 ASP C O   1 
ATOM   5581 C  CB  . ASP C 1 225 ? 15.862 48.802 59.806  1.00 11.58 ? 203 ASP C CB  1 
ATOM   5582 C  CG  . ASP C 1 225 ? 14.378 48.668 60.106  1.00 12.68 ? 203 ASP C CG  1 
ATOM   5583 O  OD1 . ASP C 1 225 ? 13.960 47.718 60.790  1.00 14.52 ? 203 ASP C OD1 1 
ATOM   5584 O  OD2 . ASP C 1 225 ? 13.621 49.552 59.655  1.00 14.06 ? 203 ASP C OD2 1 
ATOM   5585 N  N   . PRO C 1 226 ? 15.579 45.241 59.890  1.00 9.47  ? 204 PRO C N   1 
ATOM   5586 C  CA  . PRO C 1 226 ? 14.960 44.091 59.210  1.00 9.17  ? 204 PRO C CA  1 
ATOM   5587 C  C   . PRO C 1 226 ? 13.679 44.419 58.441  1.00 8.71  ? 204 PRO C C   1 
ATOM   5588 O  O   . PRO C 1 226 ? 13.427 43.821 57.399  1.00 8.66  ? 204 PRO C O   1 
ATOM   5589 C  CB  . PRO C 1 226 ? 14.657 43.121 60.355  1.00 9.38  ? 204 PRO C CB  1 
ATOM   5590 C  CG  . PRO C 1 226 ? 15.627 43.485 61.426  1.00 9.57  ? 204 PRO C CG  1 
ATOM   5591 C  CD  . PRO C 1 226 ? 15.808 44.966 61.322  1.00 9.55  ? 204 PRO C CD  1 
ATOM   5592 N  N   . GLY C 1 227 ? 12.874 45.347 58.947  1.00 8.34  ? 205 GLY C N   1 
ATOM   5593 C  CA  . GLY C 1 227 ? 11.648 45.740 58.257  1.00 8.11  ? 205 GLY C CA  1 
ATOM   5594 C  C   . GLY C 1 227 ? 11.936 46.432 56.936  1.00 7.82  ? 205 GLY C C   1 
ATOM   5595 O  O   . GLY C 1 227 ? 11.225 46.238 55.954  1.00 7.75  ? 205 GLY C O   1 
ATOM   5596 N  N   . LEU C 1 228 ? 12.986 47.249 56.915  1.00 7.43  ? 206 LEU C N   1 
ATOM   5597 C  CA  . LEU C 1 228 ? 13.400 47.938 55.696  1.00 7.24  ? 206 LEU C CA  1 
ATOM   5598 C  C   . LEU C 1 228 ? 13.848 46.952 54.622  1.00 7.07  ? 206 LEU C C   1 
ATOM   5599 O  O   . LEU C 1 228 ? 13.471 47.076 53.457  1.00 6.88  ? 206 LEU C O   1 
ATOM   5600 C  CB  . LEU C 1 228 ? 14.516 48.931 56.018  1.00 7.28  ? 206 LEU C CB  1 
ATOM   5601 C  CG  . LEU C 1 228 ? 15.127 49.707 54.859  1.00 7.32  ? 206 LEU C CG  1 
ATOM   5602 C  CD1 . LEU C 1 228 ? 14.068 50.461 54.082  1.00 7.40  ? 206 LEU C CD1 1 
ATOM   5603 C  CD2 . LEU C 1 228 ? 16.189 50.656 55.401  1.00 7.33  ? 206 LEU C CD2 1 
ATOM   5604 N  N   . VAL C 1 229 ? 14.650 45.971 55.026  1.00 6.99  ? 207 VAL C N   1 
ATOM   5605 C  CA  . VAL C 1 229 ? 15.092 44.903 54.123  1.00 7.11  ? 207 VAL C CA  1 
ATOM   5606 C  C   . VAL C 1 229 ? 13.884 44.120 53.604  1.00 7.24  ? 207 VAL C C   1 
ATOM   5607 O  O   . VAL C 1 229 ? 13.774 43.855 52.404  1.00 7.11  ? 207 VAL C O   1 
ATOM   5608 C  CB  . VAL C 1 229 ? 16.073 43.940 54.829  1.00 7.10  ? 207 VAL C CB  1 
ATOM   5609 C  CG1 . VAL C 1 229 ? 16.367 42.711 53.976  1.00 7.13  ? 207 VAL C CG1 1 
ATOM   5610 C  CG2 . VAL C 1 229 ? 17.359 44.664 55.176  1.00 7.15  ? 207 VAL C CG2 1 
ATOM   5611 N  N   . LYS C 1 230 ? 12.981 43.767 54.515  1.00 7.48  ? 208 LYS C N   1 
ATOM   5612 C  CA  . LYS C 1 230 ? 11.793 42.986 54.172  1.00 7.95  ? 208 LYS C CA  1 
ATOM   5613 C  C   . LYS C 1 230 ? 10.956 43.691 53.115  1.00 7.83  ? 208 LYS C C   1 
ATOM   5614 O  O   . LYS C 1 230 ? 10.590 43.093 52.104  1.00 7.78  ? 208 LYS C O   1 
ATOM   5615 C  CB  . LYS C 1 230 ? 10.946 42.724 55.419  1.00 8.50  ? 208 LYS C CB  1 
ATOM   5616 C  CG  . LYS C 1 230 ? 9.666  41.944 55.163  1.00 9.25  ? 208 LYS C CG  1 
ATOM   5617 C  CD  . LYS C 1 230 ? 8.953  41.634 56.465  1.00 9.84  ? 208 LYS C CD  1 
ATOM   5618 C  CE  . LYS C 1 230 ? 7.457  41.490 56.275  1.00 10.67 ? 208 LYS C CE  1 
ATOM   5619 N  NZ  . LYS C 1 230 ? 6.832  41.240 57.597  1.00 11.18 ? 208 LYS C NZ  1 
ATOM   5620 N  N   . GLU C 1 231 ? 10.651 44.961 53.349  1.00 7.92  ? 209 GLU C N   1 
ATOM   5621 C  CA  . GLU C 1 231 ? 9.766  45.691 52.447  1.00 8.06  ? 209 GLU C CA  1 
ATOM   5622 C  C   . GLU C 1 231 ? 10.447 45.963 51.117  1.00 7.62  ? 209 GLU C C   1 
ATOM   5623 O  O   . GLU C 1 231 ? 9.794  45.997 50.077  1.00 7.48  ? 209 GLU C O   1 
ATOM   5624 C  CB  . GLU C 1 231 ? 9.295  46.995 53.092  1.00 8.68  ? 209 GLU C CB  1 
ATOM   5625 C  CG  . GLU C 1 231 ? 8.465  46.770 54.347  1.00 9.40  ? 209 GLU C CG  1 
ATOM   5626 C  CD  . GLU C 1 231 ? 7.221  45.934 54.100  1.00 10.08 ? 209 GLU C CD  1 
ATOM   5627 O  OE1 . GLU C 1 231 ? 6.552  46.166 53.068  1.00 11.17 ? 209 GLU C OE1 1 
ATOM   5628 O  OE2 . GLU C 1 231 ? 6.905  45.051 54.938  1.00 11.02 ? 209 GLU C OE2 1 
ATOM   5629 N  N   . THR C 1 232 ? 11.763 46.158 51.149  1.00 7.25  ? 210 THR C N   1 
ATOM   5630 C  CA  . THR C 1 232 ? 12.509 46.407 49.925  1.00 7.14  ? 210 THR C CA  1 
ATOM   5631 C  C   . THR C 1 232 ? 12.589 45.145 49.067  1.00 7.13  ? 210 THR C C   1 
ATOM   5632 O  O   . THR C 1 232 ? 12.396 45.219 47.855  1.00 6.93  ? 210 THR C O   1 
ATOM   5633 C  CB  . THR C 1 232 ? 13.908 46.971 50.217  1.00 7.10  ? 210 THR C CB  1 
ATOM   5634 O  OG1 . THR C 1 232 ? 13.762 48.185 50.952  1.00 6.97  ? 210 THR C OG1 1 
ATOM   5635 C  CG2 . THR C 1 232 ? 14.655 47.269 48.917  1.00 7.07  ? 210 THR C CG2 1 
ATOM   5636 N  N   . LYS C 1 233 ? 12.848 43.990 49.682  1.00 7.20  ? 211 LYS C N   1 
ATOM   5637 C  CA  . LYS C 1 233 ? 12.790 42.737 48.922  1.00 7.42  ? 211 LYS C CA  1 
ATOM   5638 C  C   . LYS C 1 233 ? 11.385 42.512 48.350  1.00 7.78  ? 211 LYS C C   1 
ATOM   5639 O  O   . LYS C 1 233 ? 11.247 42.079 47.206  1.00 7.63  ? 211 LYS C O   1 
ATOM   5640 C  CB  . LYS C 1 233 ? 13.229 41.512 49.737  1.00 7.38  ? 211 LYS C CB  1 
ATOM   5641 C  CG  . LYS C 1 233 ? 13.115 40.235 48.912  1.00 7.36  ? 211 LYS C CG  1 
ATOM   5642 C  CD  . LYS C 1 233 ? 13.656 38.988 49.578  1.00 7.33  ? 211 LYS C CD  1 
ATOM   5643 C  CE  . LYS C 1 233 ? 13.255 37.776 48.748  1.00 7.35  ? 211 LYS C CE  1 
ATOM   5644 N  NZ  . LYS C 1 233 ? 13.952 36.537 49.184  1.00 7.34  ? 211 LYS C NZ  1 
ATOM   5645 N  N   . ARG C 1 234 ? 10.347 42.815 49.132  1.00 8.33  ? 212 ARG C N   1 
ATOM   5646 C  CA  . ARG C 1 234 ? 8.969  42.704 48.633  1.00 8.93  ? 212 ARG C CA  1 
ATOM   5647 C  C   . ARG C 1 234 ? 8.785  43.499 47.343  1.00 8.44  ? 212 ARG C C   1 
ATOM   5648 O  O   . ARG C 1 234 ? 8.225  42.998 46.364  1.00 8.39  ? 212 ARG C O   1 
ATOM   5649 C  CB  . ARG C 1 234 ? 7.952  43.167 49.685  1.00 10.14 ? 212 ARG C CB  1 
ATOM   5650 C  CG  . ARG C 1 234 ? 7.715  42.163 50.799  1.00 11.40 ? 212 ARG C CG  1 
ATOM   5651 C  CD  . ARG C 1 234 ? 6.626  42.635 51.748  1.00 12.68 ? 212 ARG C CD  1 
ATOM   5652 N  NE  . ARG C 1 234 ? 5.312  42.598 51.113  1.00 13.98 ? 212 ARG C NE  1 
ATOM   5653 C  CZ  . ARG C 1 234 ? 4.491  43.638 50.948  1.00 15.23 ? 212 ARG C CZ  1 
ATOM   5654 N  NH1 . ARG C 1 234 ? 4.796  44.853 51.398  1.00 15.97 ? 212 ARG C NH1 1 
ATOM   5655 N  NH2 . ARG C 1 234 ? 3.325  43.451 50.342  1.00 16.18 ? 212 ARG C NH2 1 
ATOM   5656 N  N   . ALA C 1 235 ? 9.269  44.736 47.346  1.00 7.88  ? 213 ALA C N   1 
ATOM   5657 C  CA  . ALA C 1 235 ? 9.180  45.597 46.172  1.00 7.61  ? 213 ALA C CA  1 
ATOM   5658 C  C   . ALA C 1 235 ? 10.007 45.044 45.006  1.00 7.44  ? 213 ALA C C   1 
ATOM   5659 O  O   . ALA C 1 235 ? 9.557  45.068 43.868  1.00 7.39  ? 213 ALA C O   1 
ATOM   5660 C  CB  . ALA C 1 235 ? 9.603  47.008 46.526  1.00 7.60  ? 213 ALA C CB  1 
ATOM   5661 N  N   . LEU C 1 236 ? 11.209 44.542 45.289  1.00 7.19  ? 214 LEU C N   1 
ATOM   5662 C  CA  . LEU C 1 236 ? 12.065 43.974 44.238  1.00 7.19  ? 214 LEU C CA  1 
ATOM   5663 C  C   . LEU C 1 236 ? 11.409 42.768 43.572  1.00 7.19  ? 214 LEU C C   1 
ATOM   5664 O  O   . LEU C 1 236 ? 11.354 42.681 42.337  1.00 7.15  ? 214 LEU C O   1 
ATOM   5665 C  CB  . LEU C 1 236 ? 13.439 43.583 44.802  1.00 7.21  ? 214 LEU C CB  1 
ATOM   5666 C  CG  . LEU C 1 236 ? 14.413 44.745 45.015  1.00 7.32  ? 214 LEU C CG  1 
ATOM   5667 C  CD1 . LEU C 1 236 ? 15.409 44.420 46.120  1.00 7.38  ? 214 LEU C CD1 1 
ATOM   5668 C  CD2 . LEU C 1 236 ? 15.129 45.087 43.719  1.00 7.49  ? 214 LEU C CD2 1 
ATOM   5669 N  N   . ASN C 1 237 ? 10.902 41.849 44.390  1.00 7.10  ? 215 ASN C N   1 
ATOM   5670 C  CA  . ASN C 1 237 ? 10.233 40.657 43.874  1.00 7.30  ? 215 ASN C CA  1 
ATOM   5671 C  C   . ASN C 1 237 ? 8.978  41.026 43.093  1.00 7.41  ? 215 ASN C C   1 
ATOM   5672 O  O   . ASN C 1 237 ? 8.647  40.374 42.099  1.00 7.32  ? 215 ASN C O   1 
ATOM   5673 C  CB  . ASN C 1 237 ? 9.873  39.693 45.007  1.00 7.46  ? 215 ASN C CB  1 
ATOM   5674 C  CG  . ASN C 1 237 ? 11.028 38.801 45.416  1.00 7.60  ? 215 ASN C CG  1 
ATOM   5675 O  OD1 . ASN C 1 237 ? 12.178 39.007 45.011  1.00 7.92  ? 215 ASN C OD1 1 
ATOM   5676 N  ND2 . ASN C 1 237 ? 10.719 37.785 46.213  1.00 7.76  ? 215 ASN C ND2 1 
ATOM   5677 N  N   . ARG C 1 238 ? 8.293  42.080 43.533  1.00 7.53  ? 216 ARG C N   1 
ATOM   5678 C  CA  . ARG C 1 238 ? 7.078  42.548 42.858  1.00 7.91  ? 216 ARG C CA  1 
ATOM   5679 C  C   . ARG C 1 238 ? 7.324  42.891 41.394  1.00 7.82  ? 216 ARG C C   1 
ATOM   5680 O  O   . ARG C 1 238 ? 6.433  42.717 40.559  1.00 7.56  ? 216 ARG C O   1 
ATOM   5681 C  CB  . ARG C 1 238 ? 6.487  43.773 43.566  1.00 8.42  ? 216 ARG C CB  1 
ATOM   5682 C  CG  . ARG C 1 238 ? 5.128  44.236 43.037  1.00 8.91  ? 216 ARG C CG  1 
ATOM   5683 C  CD  . ARG C 1 238 ? 4.010  43.255 43.360  1.00 9.39  ? 216 ARG C CD  1 
ATOM   5684 N  NE  . ARG C 1 238 ? 3.953  43.011 44.795  1.00 10.08 ? 216 ARG C NE  1 
ATOM   5685 C  CZ  . ARG C 1 238 ? 3.445  43.847 45.698  1.00 10.47 ? 216 ARG C CZ  1 
ATOM   5686 N  NH1 . ARG C 1 238 ? 2.878  44.994 45.333  1.00 10.86 ? 216 ARG C NH1 1 
ATOM   5687 N  NH2 . ARG C 1 238 ? 3.484  43.518 46.983  1.00 11.09 ? 216 ARG C NH2 1 
ATOM   5688 N  N   . ALA C 1 239 ? 8.519  43.387 41.080  1.00 7.65  ? 217 ALA C N   1 
ATOM   5689 C  CA  . ALA C 1 239 ? 8.842  43.744 39.695  1.00 7.88  ? 217 ALA C CA  1 
ATOM   5690 C  C   . ALA C 1 239 ? 8.681  42.542 38.770  1.00 8.04  ? 217 ALA C C   1 
ATOM   5691 O  O   . ALA C 1 239 ? 8.062  42.656 37.716  1.00 8.24  ? 217 ALA C O   1 
ATOM   5692 C  CB  . ALA C 1 239 ? 10.248 44.315 39.597  1.00 7.90  ? 217 ALA C CB  1 
ATOM   5693 N  N   . LEU C 1 240 ? 9.200  41.383 39.176  1.00 8.10  ? 218 LEU C N   1 
ATOM   5694 C  CA  . LEU C 1 240 ? 9.084  40.170 38.356  1.00 8.34  ? 218 LEU C CA  1 
ATOM   5695 C  C   . LEU C 1 240 ? 7.701  39.534 38.452  1.00 8.25  ? 218 LEU C C   1 
ATOM   5696 O  O   . LEU C 1 240 ? 7.176  39.031 37.463  1.00 8.24  ? 218 LEU C O   1 
ATOM   5697 C  CB  . LEU C 1 240 ? 10.183 39.153 38.710  1.00 8.75  ? 218 LEU C CB  1 
ATOM   5698 C  CG  . LEU C 1 240 ? 11.497 39.376 37.946  1.00 9.08  ? 218 LEU C CG  1 
ATOM   5699 C  CD1 . LEU C 1 240 ? 12.084 40.759 38.223  1.00 9.35  ? 218 LEU C CD1 1 
ATOM   5700 C  CD2 . LEU C 1 240 ? 12.509 38.287 38.269  1.00 9.48  ? 218 LEU C CD2 1 
ATOM   5701 N  N   . GLU C 1 241 ? 7.094  39.565 39.631  1.00 8.24  ? 219 GLU C N   1 
ATOM   5702 C  CA  . GLU C 1 241 ? 5.760  38.988 39.792  1.00 8.39  ? 219 GLU C CA  1 
ATOM   5703 C  C   . GLU C 1 241 ? 4.717  39.765 38.976  1.00 7.91  ? 219 GLU C C   1 
ATOM   5704 O  O   . GLU C 1 241 ? 3.776  39.189 38.438  1.00 7.54  ? 219 GLU C O   1 
ATOM   5705 C  CB  . GLU C 1 241 ? 5.405  38.885 41.274  1.00 9.23  ? 219 GLU C CB  1 
ATOM   5706 C  CG  . GLU C 1 241 ? 6.371  37.940 41.982  1.00 10.11 ? 219 GLU C CG  1 
ATOM   5707 C  CD  . GLU C 1 241 ? 6.100  37.755 43.454  1.00 11.21 ? 219 GLU C CD  1 
ATOM   5708 O  OE1 . GLU C 1 241 ? 5.038  38.204 43.944  1.00 12.78 ? 219 GLU C OE1 1 
ATOM   5709 O  OE2 . GLU C 1 241 ? 6.958  37.140 44.123  1.00 11.95 ? 219 GLU C OE2 1 
ATOM   5710 N  N   . THR C 1 242 ? 4.938  41.065 38.827  1.00 7.43  ? 220 THR C N   1 
ATOM   5711 C  CA  . THR C 1 242 ? 4.062  41.910 38.012  1.00 7.43  ? 220 THR C CA  1 
ATOM   5712 C  C   . THR C 1 242 ? 4.043  41.457 36.555  1.00 7.41  ? 220 THR C C   1 
ATOM   5713 O  O   . THR C 1 242 ? 3.010  41.537 35.873  1.00 7.20  ? 220 THR C O   1 
ATOM   5714 C  CB  . THR C 1 242 ? 4.521  43.374 38.116  1.00 7.52  ? 220 THR C CB  1 
ATOM   5715 O  OG1 . THR C 1 242 ? 4.299  43.818 39.461  1.00 7.82  ? 220 THR C OG1 1 
ATOM   5716 C  CG2 . THR C 1 242 ? 3.775  44.275 37.138  1.00 7.56  ? 220 THR C CG2 1 
ATOM   5717 N  N   . GLN C 1 243 ? 5.187  40.960 36.096  1.00 7.49  ? 221 GLN C N   1 
ATOM   5718 C  CA  . GLN C 1 243 ? 5.342  40.475 34.728  1.00 7.78  ? 221 GLN C CA  1 
ATOM   5719 C  C   . GLN C 1 243 ? 4.662  39.129 34.485  1.00 7.84  ? 221 GLN C C   1 
ATOM   5720 O  O   . GLN C 1 243 ? 4.601  38.675 33.340  1.00 8.03  ? 221 GLN C O   1 
ATOM   5721 C  CB  . GLN C 1 243 ? 6.823  40.352 34.391  1.00 8.05  ? 221 GLN C CB  1 
ATOM   5722 C  CG  . GLN C 1 243 ? 7.569  41.665 34.477  1.00 8.42  ? 221 GLN C CG  1 
ATOM   5723 C  CD  . GLN C 1 243 ? 9.057  41.498 34.295  1.00 8.81  ? 221 GLN C CD  1 
ATOM   5724 O  OE1 . GLN C 1 243 ? 9.501  40.765 33.411  1.00 9.45  ? 221 GLN C OE1 1 
ATOM   5725 N  NE2 . GLN C 1 243 ? 9.843  42.183 35.117  1.00 9.21  ? 221 GLN C NE2 1 
ATOM   5726 N  N   . GLY C 1 244 ? 4.176  38.496 35.554  1.00 7.69  ? 222 GLY C N   1 
ATOM   5727 C  CA  . GLY C 1 244 ? 3.484  37.208 35.472  1.00 7.74  ? 222 GLY C CA  1 
ATOM   5728 C  C   . GLY C 1 244 ? 4.382  36.008 35.723  1.00 7.88  ? 222 GLY C C   1 
ATOM   5729 O  O   . GLY C 1 244 ? 4.004  34.884 35.421  1.00 7.62  ? 222 GLY C O   1 
HETATM 5730 N  N   . MSE C 1 245 ? 5.562  36.229 36.302  1.00 8.29  ? 223 MSE C N   1 
HETATM 5731 C  CA  . MSE C 1 245 ? 6.526  35.130 36.486  1.00 8.91  ? 223 MSE C CA  1 
HETATM 5732 C  C   . MSE C 1 245 ? 5.924  33.923 37.165  1.00 8.24  ? 223 MSE C C   1 
HETATM 5733 O  O   . MSE C 1 245 ? 6.177  32.793 36.752  1.00 7.67  ? 223 MSE C O   1 
HETATM 5734 C  CB  . MSE C 1 245 ? 7.764  35.581 37.257  1.00 10.51 ? 223 MSE C CB  1 
HETATM 5735 C  CG  . MSE C 1 245 ? 8.736  34.408 37.381  1.00 12.13 ? 223 MSE C CG  1 
HETATM 5736 SE SE  . MSE C 1 245 ? 10.434 34.968 38.190  1.00 17.11 ? 223 MSE C SE  1 
HETATM 5737 C  CE  . MSE C 1 245 ? 9.834  34.932 40.059  1.00 15.01 ? 223 MSE C CE  1 
ATOM   5738 N  N   . LEU C 1 246 ? 5.133  34.123 38.214  1.00 7.82  ? 224 LEU C N   1 
ATOM   5739 C  CA  . LEU C 1 246 ? 4.601  32.971 38.938  1.00 7.66  ? 224 LEU C CA  1 
ATOM   5740 C  C   . LEU C 1 246 ? 3.652  32.135 38.080  1.00 7.44  ? 224 LEU C C   1 
ATOM   5741 O  O   . LEU C 1 246 ? 3.633  30.910 38.199  1.00 7.37  ? 224 LEU C O   1 
ATOM   5742 C  CB  . LEU C 1 246 ? 3.921  33.385 40.241  1.00 7.80  ? 224 LEU C CB  1 
ATOM   5743 C  CG  . LEU C 1 246 ? 4.789  34.113 41.260  1.00 8.04  ? 224 LEU C CG  1 
ATOM   5744 C  CD1 . LEU C 1 246 ? 3.995  34.301 42.544  1.00 8.29  ? 224 LEU C CD1 1 
ATOM   5745 C  CD2 . LEU C 1 246 ? 6.091  33.378 41.532  1.00 8.12  ? 224 LEU C CD2 1 
ATOM   5746 N  N   . GLN C 1 247 ? 2.871  32.781 37.217  1.00 7.19  ? 225 GLN C N   1 
ATOM   5747 C  CA  . GLN C 1 247 ? 2.018  32.046 36.280  1.00 7.23  ? 225 GLN C CA  1 
ATOM   5748 C  C   . GLN C 1 247 ? 2.850  31.279 35.243  1.00 6.86  ? 225 GLN C C   1 
ATOM   5749 O  O   . GLN C 1 247 ? 2.528  30.137 34.908  1.00 6.90  ? 225 GLN C O   1 
ATOM   5750 C  CB  . GLN C 1 247 ? 1.022  32.975 35.579  1.00 7.48  ? 225 GLN C CB  1 
ATOM   5751 C  CG  . GLN C 1 247 ? -0.123 33.428 36.469  1.00 7.88  ? 225 GLN C CG  1 
ATOM   5752 C  CD  . GLN C 1 247 ? 0.266  34.561 37.393  1.00 8.13  ? 225 GLN C CD  1 
ATOM   5753 O  OE1 . GLN C 1 247 ? 0.799  35.577 36.950  1.00 8.74  ? 225 GLN C OE1 1 
ATOM   5754 N  NE2 . GLN C 1 247 ? -0.002 34.399 38.682  1.00 8.44  ? 225 GLN C NE2 1 
ATOM   5755 N  N   . ALA C 1 248 ? 3.916  31.897 34.743  1.00 6.54  ? 226 ALA C N   1 
ATOM   5756 C  CA  . ALA C 1 248 ? 4.779  31.252 33.752  1.00 6.37  ? 226 ALA C CA  1 
ATOM   5757 C  C   . ALA C 1 248 ? 5.459  30.031 34.363  1.00 6.29  ? 226 ALA C C   1 
ATOM   5758 O  O   . ALA C 1 248 ? 5.588  28.985 33.710  1.00 6.26  ? 226 ALA C O   1 
ATOM   5759 C  CB  . ALA C 1 248 ? 5.813  32.227 33.211  1.00 6.35  ? 226 ALA C CB  1 
ATOM   5760 N  N   . LEU C 1 249 ? 5.882  30.167 35.617  1.00 6.19  ? 227 LEU C N   1 
ATOM   5761 C  CA  . LEU C 1 249 ? 6.531  29.062 36.325  1.00 6.20  ? 227 LEU C CA  1 
ATOM   5762 C  C   . LEU C 1 249 ? 5.551  27.915 36.551  1.00 6.43  ? 227 LEU C C   1 
ATOM   5763 O  O   . LEU C 1 249 ? 5.889  26.751 36.338  1.00 6.20  ? 227 LEU C O   1 
ATOM   5764 C  CB  . LEU C 1 249 ? 7.112  29.542 37.662  1.00 6.17  ? 227 LEU C CB  1 
ATOM   5765 C  CG  . LEU C 1 249 ? 8.320  30.473 37.565  1.00 6.20  ? 227 LEU C CG  1 
ATOM   5766 C  CD1 . LEU C 1 249 ? 8.678  31.039 38.932  1.00 6.18  ? 227 LEU C CD1 1 
ATOM   5767 C  CD2 . LEU C 1 249 ? 9.523  29.760 36.968  1.00 6.27  ? 227 LEU C CD2 1 
ATOM   5768 N  N   . GLU C 1 250 ? 4.337  28.237 36.983  1.00 6.75  ? 228 GLU C N   1 
ATOM   5769 C  CA  . GLU C 1 250 ? 3.315  27.204 37.184  1.00 7.22  ? 228 GLU C CA  1 
ATOM   5770 C  C   . GLU C 1 250 ? 2.976  26.503 35.863  1.00 7.35  ? 228 GLU C C   1 
ATOM   5771 O  O   . GLU C 1 250 ? 2.740  25.294 35.839  1.00 7.36  ? 228 GLU C O   1 
ATOM   5772 C  CB  . GLU C 1 250 ? 2.050  27.795 37.825  1.00 7.57  ? 228 GLU C CB  1 
ATOM   5773 C  CG  . GLU C 1 250 ? 2.220  28.210 39.288  1.00 8.07  ? 228 GLU C CG  1 
ATOM   5774 C  CD  . GLU C 1 250 ? 2.300  27.054 40.273  1.00 8.45  ? 228 GLU C CD  1 
ATOM   5775 O  OE1 . GLU C 1 250 ? 1.919  25.913 39.922  1.00 9.08  ? 228 GLU C OE1 1 
ATOM   5776 O  OE2 . GLU C 1 250 ? 2.742  27.297 41.429  1.00 9.24  ? 228 GLU C OE2 1 
ATOM   5777 N  N   . SER C 1 251 ? 2.945  27.264 34.771  1.00 7.65  ? 229 SER C N   1 
ATOM   5778 C  CA  . SER C 1 251 ? 2.677  26.708 33.442  1.00 7.96  ? 229 SER C CA  1 
ATOM   5779 C  C   . SER C 1 251 ? 3.768  25.734 33.024  1.00 7.40  ? 229 SER C C   1 
ATOM   5780 O  O   . SER C 1 251 ? 3.475  24.655 32.521  1.00 7.49  ? 229 SER C O   1 
ATOM   5781 C  CB  . SER C 1 251 ? 2.560  27.813 32.387  1.00 8.66  ? 229 SER C CB  1 
ATOM   5782 O  OG  . SER C 1 251 ? 1.432  28.631 32.633  1.00 10.17 ? 229 SER C OG  1 
ATOM   5783 N  N   . ALA C 1 252 ? 5.025  26.106 33.239  1.00 6.84  ? 230 ALA C N   1 
ATOM   5784 C  CA  . ALA C 1 252 ? 6.136  25.211 32.923  1.00 6.54  ? 230 ALA C CA  1 
ATOM   5785 C  C   . ALA C 1 252 ? 6.108  23.950 33.792  1.00 6.38  ? 230 ALA C C   1 
ATOM   5786 O  O   . ALA C 1 252 ? 6.431  22.858 33.314  1.00 6.15  ? 230 ALA C O   1 
ATOM   5787 C  CB  . ALA C 1 252 ? 7.468  25.935 33.057  1.00 6.49  ? 230 ALA C CB  1 
ATOM   5788 N  N   . LEU C 1 253 ? 5.708  24.105 35.051  1.00 6.25  ? 231 LEU C N   1 
ATOM   5789 C  CA  . LEU C 1 253 ? 5.588  22.971 35.965  1.00 6.31  ? 231 LEU C CA  1 
ATOM   5790 C  C   . LEU C 1 253 ? 4.515  21.996 35.484  1.00 6.47  ? 231 LEU C C   1 
ATOM   5791 O  O   . LEU C 1 253 ? 4.699  20.781 35.556  1.00 6.39  ? 231 LEU C O   1 
ATOM   5792 C  CB  . LEU C 1 253 ? 5.273  23.468 37.377  1.00 6.24  ? 231 LEU C CB  1 
ATOM   5793 C  CG  . LEU C 1 253 ? 5.150  22.405 38.468  1.00 6.31  ? 231 LEU C CG  1 
ATOM   5794 C  CD1 . LEU C 1 253 ? 6.450  21.640 38.628  1.00 6.30  ? 231 LEU C CD1 1 
ATOM   5795 C  CD2 . LEU C 1 253 ? 4.719  23.032 39.788  1.00 6.35  ? 231 LEU C CD2 1 
ATOM   5796 N  N   . GLU C 1 254 ? 3.411  22.529 34.971  1.00 6.76  ? 232 GLU C N   1 
ATOM   5797 C  CA  . GLU C 1 254 ? 2.321  21.687 34.477  1.00 7.25  ? 232 GLU C CA  1 
ATOM   5798 C  C   . GLU C 1 254 ? 2.729  20.960 33.192  1.00 6.65  ? 232 GLU C C   1 
ATOM   5799 O  O   . GLU C 1 254 ? 2.374  19.795 32.994  1.00 6.46  ? 232 GLU C O   1 
ATOM   5800 C  CB  . GLU C 1 254 ? 1.053  22.522 34.255  1.00 8.36  ? 232 GLU C CB  1 
ATOM   5801 C  CG  . GLU C 1 254 ? -0.262 21.751 34.391  1.00 9.66  ? 232 GLU C CG  1 
ATOM   5802 C  CD  . GLU C 1 254 ? -0.534 21.183 35.785  1.00 10.44 ? 232 GLU C CD  1 
ATOM   5803 O  OE1 . GLU C 1 254 ? -1.087 20.062 35.875  1.00 11.17 ? 232 GLU C OE1 1 
ATOM   5804 O  OE2 . GLU C 1 254 ? -0.208 21.848 36.804  1.00 12.61 ? 232 GLU C OE2 1 
ATOM   5805 N  N   . ILE C 1 255 ? 3.473  21.648 32.332  1.00 6.12  ? 233 ILE C N   1 
ATOM   5806 C  CA  . ILE C 1 255 ? 4.046  21.033 31.135  1.00 5.89  ? 233 ILE C CA  1 
ATOM   5807 C  C   . ILE C 1 255 ? 4.971  19.877 31.543  1.00 5.66  ? 233 ILE C C   1 
ATOM   5808 O  O   . ILE C 1 255 ? 4.910  18.792 30.955  1.00 5.53  ? 233 ILE C O   1 
ATOM   5809 C  CB  . ILE C 1 255 ? 4.777  22.081 30.256  1.00 5.93  ? 233 ILE C CB  1 
ATOM   5810 C  CG1 . ILE C 1 255 ? 3.738  22.980 29.572  1.00 5.98  ? 233 ILE C CG1 1 
ATOM   5811 C  CG2 . ILE C 1 255 ? 5.678  21.404 29.229  1.00 6.01  ? 233 ILE C CG2 1 
ATOM   5812 C  CD1 . ILE C 1 255 ? 4.309  24.172 28.835  1.00 5.99  ? 233 ILE C CD1 1 
ATOM   5813 N  N   . ASP C 1 256 ? 5.791  20.091 32.567  1.00 5.45  ? 234 ASP C N   1 
ATOM   5814 C  CA  . ASP C 1 256 ? 6.702  19.046 33.032  1.00 5.41  ? 234 ASP C CA  1 
ATOM   5815 C  C   . ASP C 1 256 ? 5.943  17.849 33.606  1.00 5.37  ? 234 ASP C C   1 
ATOM   5816 O  O   . ASP C 1 256 ? 6.385  16.704 33.467  1.00 5.46  ? 234 ASP C O   1 
ATOM   5817 C  CB  . ASP C 1 256 ? 7.692  19.578 34.069  1.00 5.41  ? 234 ASP C CB  1 
ATOM   5818 C  CG  . ASP C 1 256 ? 8.870  18.643 34.279  1.00 5.46  ? 234 ASP C CG  1 
ATOM   5819 O  OD1 . ASP C 1 256 ? 9.297  18.006 33.300  1.00 5.54  ? 234 ASP C OD1 1 
ATOM   5820 O  OD2 . ASP C 1 256 ? 9.364  18.542 35.423  1.00 5.50  ? 234 ASP C OD2 1 
ATOM   5821 N  N   . LEU C 1 257 ? 4.812  18.100 34.258  1.00 5.34  ? 235 LEU C N   1 
ATOM   5822 C  CA  . LEU C 1 257 ? 3.993  16.997 34.764  1.00 5.35  ? 235 LEU C CA  1 
ATOM   5823 C  C   . LEU C 1 257 ? 3.537  16.085 33.625  1.00 5.43  ? 235 LEU C C   1 
ATOM   5824 O  O   . LEU C 1 257 ? 3.548  14.857 33.762  1.00 5.45  ? 235 LEU C O   1 
ATOM   5825 C  CB  . LEU C 1 257 ? 2.796  17.510 35.567  1.00 5.34  ? 235 LEU C CB  1 
ATOM   5826 C  CG  . LEU C 1 257 ? 1.867  16.447 36.159  1.00 5.26  ? 235 LEU C CG  1 
ATOM   5827 C  CD1 . LEU C 1 257 ? 2.637  15.439 37.008  1.00 5.25  ? 235 LEU C CD1 1 
ATOM   5828 C  CD2 . LEU C 1 257 ? 0.764  17.109 36.971  1.00 5.25  ? 235 LEU C CD2 1 
ATOM   5829 N  N   . ALA C 1 258 ? 3.137  16.678 32.504  1.00 5.53  ? 236 ALA C N   1 
ATOM   5830 C  CA  . ALA C 1 258 ? 2.789  15.888 31.323  1.00 5.73  ? 236 ALA C CA  1 
ATOM   5831 C  C   . ALA C 1 258 ? 4.002  15.129 30.782  1.00 5.89  ? 236 ALA C C   1 
ATOM   5832 O  O   . ALA C 1 258 ? 3.903  13.944 30.458  1.00 6.12  ? 236 ALA C O   1 
ATOM   5833 C  CB  . ALA C 1 258 ? 2.180  16.758 30.246  1.00 5.75  ? 236 ALA C CB  1 
ATOM   5834 N  N   . ILE C 1 259 ? 5.145  15.804 30.698  1.00 5.99  ? 237 ILE C N   1 
ATOM   5835 C  CA  . ILE C 1 259 ? 6.372  15.162 30.227  1.00 6.10  ? 237 ILE C CA  1 
ATOM   5836 C  C   . ILE C 1 259 ? 6.718  13.938 31.077  1.00 6.17  ? 237 ILE C C   1 
ATOM   5837 O  O   . ILE C 1 259 ? 6.915  12.844 30.543  1.00 6.08  ? 237 ILE C O   1 
ATOM   5838 C  CB  . ILE C 1 259 ? 7.563  16.147 30.232  1.00 6.14  ? 237 ILE C CB  1 
ATOM   5839 C  CG1 . ILE C 1 259 ? 7.374  17.199 29.138  1.00 6.14  ? 237 ILE C CG1 1 
ATOM   5840 C  CG2 . ILE C 1 259 ? 8.882  15.393 30.054  1.00 6.20  ? 237 ILE C CG2 1 
ATOM   5841 C  CD1 . ILE C 1 259 ? 8.320  18.373 29.258  1.00 6.18  ? 237 ILE C CD1 1 
ATOM   5842 N  N   . GLU C 1 260 ? 6.793  14.126 32.391  1.00 6.26  ? 238 GLU C N   1 
ATOM   5843 C  CA  . GLU C 1 260 ? 7.234  13.061 33.289  1.00 6.52  ? 238 GLU C CA  1 
ATOM   5844 C  C   . GLU C 1 260 ? 6.133  12.028 33.517  1.00 6.80  ? 238 GLU C C   1 
ATOM   5845 O  O   . GLU C 1 260 ? 6.412  10.841 33.644  1.00 6.77  ? 238 GLU C O   1 
ATOM   5846 C  CB  . GLU C 1 260 ? 7.705  13.628 34.629  1.00 6.51  ? 238 GLU C CB  1 
ATOM   5847 C  CG  . GLU C 1 260 ? 8.873  14.606 34.543  1.00 6.56  ? 238 GLU C CG  1 
ATOM   5848 C  CD  . GLU C 1 260 ? 10.199 13.988 34.120  1.00 6.65  ? 238 GLU C CD  1 
ATOM   5849 O  OE1 . GLU C 1 260 ? 10.299 12.751 33.920  1.00 6.66  ? 238 GLU C OE1 1 
ATOM   5850 O  OE2 . GLU C 1 260 ? 11.178 14.758 33.992  1.00 6.68  ? 238 GLU C OE2 1 
ATOM   5851 N  N   . GLY C 1 261 ? 4.882  12.478 33.551  1.00 7.23  ? 239 GLY C N   1 
ATOM   5852 C  CA  . GLY C 1 261 ? 3.750  11.561 33.682  1.00 7.68  ? 239 GLY C CA  1 
ATOM   5853 C  C   . GLY C 1 261 ? 3.687  10.572 32.537  1.00 8.12  ? 239 GLY C C   1 
ATOM   5854 O  O   . GLY C 1 261 ? 3.397  9.386  32.744  1.00 8.59  ? 239 GLY C O   1 
ATOM   5855 N  N   . ALA C 1 262 ? 3.963  11.053 31.328  1.00 8.41  ? 240 ALA C N   1 
ATOM   5856 C  CA  . ALA C 1 262 ? 4.073  10.189 30.151  1.00 8.92  ? 240 ALA C CA  1 
ATOM   5857 C  C   . ALA C 1 262 ? 5.326  9.329  30.247  1.00 9.42  ? 240 ALA C C   1 
ATOM   5858 O  O   . ALA C 1 262 ? 5.269  8.117  30.006  1.00 10.16 ? 240 ALA C O   1 
ATOM   5859 C  CB  . ALA C 1 262 ? 4.104  11.016 28.872  1.00 8.89  ? 240 ALA C CB  1 
ATOM   5860 N  N   . GLY C 1 263 ? 6.441  9.963  30.613  1.00 9.75  ? 241 GLY C N   1 
ATOM   5861 C  CA  . GLY C 1 263 ? 7.758  9.318  30.674  1.00 10.08 ? 241 GLY C CA  1 
ATOM   5862 C  C   . GLY C 1 263 ? 8.426  9.348  29.315  1.00 10.20 ? 241 GLY C C   1 
ATOM   5863 O  O   . GLY C 1 263 ? 8.019  8.618  28.403  1.00 10.82 ? 241 GLY C O   1 
ATOM   5864 N  N   . SER C 1 264 ? 9.429  10.210 29.152  1.00 10.08 ? 242 SER C N   1 
ATOM   5865 C  CA  . SER C 1 264 ? 10.133 10.297 27.886  1.00 10.10 ? 242 SER C CA  1 
ATOM   5866 C  C   . SER C 1 264 ? 10.853 8.980  27.631  1.00 9.97  ? 242 SER C C   1 
ATOM   5867 O  O   . SER C 1 264 ? 11.438 8.421  28.554  1.00 9.95  ? 242 SER C O   1 
ATOM   5868 C  CB  . SER C 1 264 ? 11.161 11.432 27.892  1.00 10.39 ? 242 SER C CB  1 
ATOM   5869 O  OG  . SER C 1 264 ? 11.913 11.422 26.688  1.00 10.76 ? 242 SER C OG  1 
ATOM   5870 N  N   . PRO C 1 265 ? 10.819 8.488  26.381  1.00 9.97  ? 243 PRO C N   1 
ATOM   5871 C  CA  . PRO C 1 265 ? 11.613 7.297  26.074  1.00 9.81  ? 243 PRO C CA  1 
ATOM   5872 C  C   . PRO C 1 265 ? 13.115 7.501  26.308  1.00 9.45  ? 243 PRO C C   1 
ATOM   5873 O  O   . PRO C 1 265 ? 13.828 6.528  26.563  1.00 9.49  ? 243 PRO C O   1 
ATOM   5874 C  CB  . PRO C 1 265 ? 11.311 7.035  24.595  1.00 10.00 ? 243 PRO C CB  1 
ATOM   5875 C  CG  . PRO C 1 265 ? 10.772 8.317  24.065  1.00 10.20 ? 243 PRO C CG  1 
ATOM   5876 C  CD  . PRO C 1 265 ? 10.047 8.947  25.212  1.00 9.98  ? 243 PRO C CD  1 
ATOM   5877 N  N   . ASP C 1 266 ? 13.589 8.746  26.248  1.00 9.12  ? 244 ASP C N   1 
ATOM   5878 C  CA  . ASP C 1 266 ? 15.000 9.037  26.530  1.00 8.88  ? 244 ASP C CA  1 
ATOM   5879 C  C   . ASP C 1 266 ? 15.348 8.723  27.984  1.00 8.66  ? 244 ASP C C   1 
ATOM   5880 O  O   . ASP C 1 266 ? 16.421 8.191  28.270  1.00 8.54  ? 244 ASP C O   1 
ATOM   5881 C  CB  . ASP C 1 266 ? 15.338 10.508 26.248  1.00 9.08  ? 244 ASP C CB  1 
ATOM   5882 C  CG  . ASP C 1 266 ? 15.243 10.888 24.772  1.00 9.29  ? 244 ASP C CG  1 
ATOM   5883 O  OD1 . ASP C 1 266 ? 14.934 10.038 23.908  1.00 9.77  ? 244 ASP C OD1 1 
ATOM   5884 O  OD2 . ASP C 1 266 ? 15.487 12.079 24.471  1.00 9.50  ? 244 ASP C OD2 1 
ATOM   5885 N  N   . LYS C 1 267 ? 14.452 9.074  28.905  1.00 8.26  ? 245 LYS C N   1 
ATOM   5886 C  CA  . LYS C 1 267 ? 14.669 8.796  30.319  1.00 8.34  ? 245 LYS C CA  1 
ATOM   5887 C  C   . LYS C 1 267 ? 14.546 7.306  30.600  1.00 8.29  ? 245 LYS C C   1 
ATOM   5888 O  O   . LYS C 1 267 ? 15.339 6.746  31.351  1.00 8.27  ? 245 LYS C O   1 
ATOM   5889 C  CB  . LYS C 1 267 ? 13.679 9.563  31.195  1.00 8.36  ? 245 LYS C CB  1 
ATOM   5890 C  CG  . LYS C 1 267 ? 13.796 9.222  32.671  1.00 8.50  ? 245 LYS C CG  1 
ATOM   5891 C  CD  . LYS C 1 267 ? 12.936 10.117 33.548  1.00 8.47  ? 245 LYS C CD  1 
ATOM   5892 C  CE  . LYS C 1 267 ? 13.595 11.459 33.817  1.00 8.48  ? 245 LYS C CE  1 
ATOM   5893 N  NZ  . LYS C 1 267 ? 12.915 12.201 34.914  1.00 8.44  ? 245 LYS C NZ  1 
ATOM   5894 N  N   . ILE C 1 268 ? 13.547 6.673  29.999  1.00 8.46  ? 246 ILE C N   1 
ATOM   5895 C  CA  . ILE C 1 268 ? 13.347 5.240  30.191  1.00 8.75  ? 246 ILE C CA  1 
ATOM   5896 C  C   . ILE C 1 268 ? 14.614 4.501  29.739  1.00 8.78  ? 246 ILE C C   1 
ATOM   5897 O  O   . ILE C 1 268 ? 15.105 3.609  30.440  1.00 8.83  ? 246 ILE C O   1 
ATOM   5898 C  CB  . ILE C 1 268 ? 12.092 4.725  29.452  1.00 9.03  ? 246 ILE C CB  1 
ATOM   5899 C  CG1 . ILE C 1 268 ? 10.831 5.303  30.103  1.00 9.25  ? 246 ILE C CG1 1 
ATOM   5900 C  CG2 . ILE C 1 268 ? 12.031 3.198  29.489  1.00 9.08  ? 246 ILE C CG2 1 
ATOM   5901 C  CD1 . ILE C 1 268 ? 9.587  5.222  29.249  1.00 9.40  ? 246 ILE C CD1 1 
ATOM   5902 N  N   . ALA C 1 269 ? 15.153 4.901  28.593  1.00 8.92  ? 247 ALA C N   1 
ATOM   5903 C  CA  . ALA C 1 269 ? 16.386 4.304  28.059  1.00 9.03  ? 247 ALA C CA  1 
ATOM   5904 C  C   . ALA C 1 269 ? 17.575 4.543  28.989  1.00 9.33  ? 247 ALA C C   1 
ATOM   5905 O  O   . ALA C 1 269 ? 18.374 3.634  29.244  1.00 9.42  ? 247 ALA C O   1 
ATOM   5906 C  CB  . ALA C 1 269 ? 16.682 4.852  26.671  1.00 9.09  ? 247 ALA C CB  1 
ATOM   5907 N  N   . PHE C 1 270 ? 17.683 5.763  29.505  1.00 9.31  ? 248 PHE C N   1 
ATOM   5908 C  CA  . PHE C 1 270 ? 18.765 6.122  30.417  1.00 9.65  ? 248 PHE C CA  1 
ATOM   5909 C  C   . PHE C 1 270 ? 18.754 5.251  31.668  1.00 9.88  ? 248 PHE C C   1 
ATOM   5910 O  O   . PHE C 1 270 ? 19.788 4.715  32.064  1.00 9.82  ? 248 PHE C O   1 
ATOM   5911 C  CB  . PHE C 1 270 ? 18.681 7.601  30.800  1.00 9.71  ? 248 PHE C CB  1 
ATOM   5912 C  CG  . PHE C 1 270 ? 19.716 8.025  31.802  1.00 9.79  ? 248 PHE C CG  1 
ATOM   5913 C  CD1 . PHE C 1 270 ? 20.997 8.365  31.392  1.00 9.84  ? 248 PHE C CD1 1 
ATOM   5914 C  CD2 . PHE C 1 270 ? 19.417 8.070  33.156  1.00 10.00 ? 248 PHE C CD2 1 
ATOM   5915 C  CE1 . PHE C 1 270 ? 21.954 8.758  32.312  1.00 9.95  ? 248 PHE C CE1 1 
ATOM   5916 C  CE2 . PHE C 1 270 ? 20.374 8.452  34.083  1.00 10.17 ? 248 PHE C CE2 1 
ATOM   5917 C  CZ  . PHE C 1 270 ? 21.642 8.801  33.657  1.00 10.12 ? 248 PHE C CZ  1 
ATOM   5918 N  N   . PHE C 1 271 ? 17.586 5.100  32.285  1.00 10.32 ? 249 PHE C N   1 
ATOM   5919 C  CA  . PHE C 1 271 ? 17.489 4.316  33.513  1.00 10.94 ? 249 PHE C CA  1 
ATOM   5920 C  C   . PHE C 1 271 ? 17.641 2.819  33.262  1.00 11.52 ? 249 PHE C C   1 
ATOM   5921 O  O   . PHE C 1 271 ? 18.112 2.105  34.150  1.00 11.63 ? 249 PHE C O   1 
ATOM   5922 C  CB  . PHE C 1 271 ? 16.206 4.643  34.288  1.00 11.24 ? 249 PHE C CB  1 
ATOM   5923 C  CG  . PHE C 1 271 ? 16.283 5.944  35.037  1.00 11.53 ? 249 PHE C CG  1 
ATOM   5924 C  CD1 . PHE C 1 271 ? 17.236 6.125  36.032  1.00 11.95 ? 249 PHE C CD1 1 
ATOM   5925 C  CD2 . PHE C 1 271 ? 15.418 6.986  34.752  1.00 12.01 ? 249 PHE C CD2 1 
ATOM   5926 C  CE1 . PHE C 1 271 ? 17.332 7.322  36.722  1.00 12.23 ? 249 PHE C CE1 1 
ATOM   5927 C  CE2 . PHE C 1 271 ? 15.504 8.184  35.445  1.00 12.23 ? 249 PHE C CE2 1 
ATOM   5928 C  CZ  . PHE C 1 271 ? 16.461 8.353  36.427  1.00 12.14 ? 249 PHE C CZ  1 
ATOM   5929 N  N   . GLU C 1 272 ? 17.291 2.347  32.063  1.00 12.20 ? 250 GLU C N   1 
ATOM   5930 C  CA  . GLU C 1 272 ? 17.548 0.942  31.708  1.00 13.13 ? 250 GLU C CA  1 
ATOM   5931 C  C   . GLU C 1 272 ? 19.047 0.657  31.774  1.00 12.41 ? 250 GLU C C   1 
ATOM   5932 O  O   . GLU C 1 272 ? 19.473 -0.332 32.374  1.00 12.14 ? 250 GLU C O   1 
ATOM   5933 C  CB  . GLU C 1 272 ? 17.011 0.587  30.317  1.00 14.87 ? 250 GLU C CB  1 
ATOM   5934 C  CG  . GLU C 1 272 ? 17.150 -0.897 29.982  1.00 17.24 ? 250 GLU C CG  1 
ATOM   5935 C  CD  . GLU C 1 272 ? 16.692 -1.253 28.578  1.00 19.33 ? 250 GLU C CD  1 
ATOM   5936 O  OE1 . GLU C 1 272 ? 16.111 -0.387 27.887  1.00 22.31 ? 250 GLU C OE1 1 
ATOM   5937 O  OE2 . GLU C 1 272 ? 16.917 -2.413 28.162  1.00 22.03 ? 250 GLU C OE2 1 
ATOM   5938 N  N   . VAL C 1 273 ? 19.848 1.524  31.165  1.00 11.73 ? 251 VAL C N   1 
ATOM   5939 C  CA  . VAL C 1 273 ? 21.300 1.381  31.252  1.00 11.43 ? 251 VAL C CA  1 
ATOM   5940 C  C   . VAL C 1 273 ? 21.777 1.549  32.698  1.00 11.47 ? 251 VAL C C   1 
ATOM   5941 O  O   . VAL C 1 273 ? 22.609 0.775  33.183  1.00 11.38 ? 251 VAL C O   1 
ATOM   5942 C  CB  . VAL C 1 273 ? 22.039 2.371  30.327  1.00 11.35 ? 251 VAL C CB  1 
ATOM   5943 C  CG1 . VAL C 1 273 ? 23.546 2.203  30.464  1.00 11.32 ? 251 VAL C CG1 1 
ATOM   5944 C  CG2 . VAL C 1 273 ? 21.611 2.167  28.882  1.00 11.35 ? 251 VAL C CG2 1 
ATOM   5945 N  N   . ALA C 1 274 ? 21.243 2.547  33.401  1.00 11.22 ? 252 ALA C N   1 
ATOM   5946 C  CA  . ALA C 1 274 ? 21.681 2.823  34.769  1.00 11.50 ? 252 ALA C CA  1 
ATOM   5947 C  C   . ALA C 1 274 ? 21.454 1.627  35.704  1.00 11.68 ? 252 ALA C C   1 
ATOM   5948 O  O   . ALA C 1 274 ? 22.323 1.294  36.515  1.00 11.65 ? 252 ALA C O   1 
ATOM   5949 C  CB  . ALA C 1 274 ? 20.990 4.067  35.310  1.00 11.54 ? 252 ALA C CB  1 
ATOM   5950 N  N   . ARG C 1 275 ? 20.305 0.970  35.575  1.00 12.18 ? 253 ARG C N   1 
ATOM   5951 C  CA  . ARG C 1 275 ? 20.003 -0.196 36.409  1.00 12.84 ? 253 ARG C CA  1 
ATOM   5952 C  C   . ARG C 1 275 ? 20.893 -1.373 36.068  1.00 12.95 ? 253 ARG C C   1 
ATOM   5953 O  O   . ARG C 1 275 ? 21.305 -2.125 36.955  1.00 13.31 ? 253 ARG C O   1 
ATOM   5954 C  CB  . ARG C 1 275 ? 18.542 -0.610 36.273  1.00 13.55 ? 253 ARG C CB  1 
ATOM   5955 C  CG  . ARG C 1 275 ? 17.618 0.336  37.000  1.00 14.39 ? 253 ARG C CG  1 
ATOM   5956 C  CD  . ARG C 1 275 ? 16.204 -0.184 37.110  1.00 15.18 ? 253 ARG C CD  1 
ATOM   5957 N  NE  . ARG C 1 275 ? 15.343 0.950  37.416  1.00 16.20 ? 253 ARG C NE  1 
ATOM   5958 C  CZ  . ARG C 1 275 ? 14.706 1.689  36.511  1.00 16.62 ? 253 ARG C CZ  1 
ATOM   5959 N  NH1 . ARG C 1 275 ? 14.765 1.392  35.210  1.00 16.54 ? 253 ARG C NH1 1 
ATOM   5960 N  NH2 . ARG C 1 275 ? 13.980 2.723  36.919  1.00 17.22 ? 253 ARG C NH2 1 
ATOM   5961 N  N   . ARG C 1 276 ? 21.198 -1.519 34.785  1.00 12.64 ? 254 ARG C N   1 
ATOM   5962 C  CA  . ARG C 1 276 ? 21.951 -2.670 34.307  1.00 12.56 ? 254 ARG C CA  1 
ATOM   5963 C  C   . ARG C 1 276 ? 23.448 -2.507 34.531  1.00 12.42 ? 254 ARG C C   1 
ATOM   5964 O  O   . ARG C 1 276 ? 24.115 -3.450 34.967  1.00 12.42 ? 254 ARG C O   1 
ATOM   5965 C  CB  . ARG C 1 276 ? 21.683 -2.879 32.823  1.00 12.68 ? 254 ARG C CB  1 
ATOM   5966 C  CG  . ARG C 1 276 ? 22.218 -4.192 32.269  1.00 12.84 ? 254 ARG C CG  1 
ATOM   5967 C  CD  . ARG C 1 276 ? 22.087 -4.220 30.764  1.00 12.97 ? 254 ARG C CD  1 
ATOM   5968 N  NE  . ARG C 1 276 ? 22.955 -3.221 30.145  1.00 13.37 ? 254 ARG C NE  1 
ATOM   5969 C  CZ  . ARG C 1 276 ? 22.655 -2.503 29.061  1.00 13.60 ? 254 ARG C CZ  1 
ATOM   5970 N  NH1 . ARG C 1 276 ? 21.497 -2.658 28.421  1.00 13.90 ? 254 ARG C NH1 1 
ATOM   5971 N  NH2 . ARG C 1 276 ? 23.528 -1.613 28.612  1.00 13.98 ? 254 ARG C NH2 1 
ATOM   5972 N  N   . ASP C 1 277 ? 23.970 -1.324 34.215  1.00 11.99 ? 255 ASP C N   1 
ATOM   5973 C  CA  . ASP C 1 277 ? 25.418 -1.087 34.188  1.00 12.17 ? 255 ASP C CA  1 
ATOM   5974 C  C   . ASP C 1 277 ? 25.910 -0.045 35.187  1.00 12.26 ? 255 ASP C C   1 
ATOM   5975 O  O   . ASP C 1 277 ? 27.115 0.130  35.334  1.00 12.08 ? 255 ASP C O   1 
ATOM   5976 C  CB  . ASP C 1 277 ? 25.867 -0.643 32.791  1.00 12.32 ? 255 ASP C CB  1 
ATOM   5977 C  CG  . ASP C 1 277 ? 25.556 -1.659 31.707  1.00 12.59 ? 255 ASP C CG  1 
ATOM   5978 O  OD1 . ASP C 1 277 ? 25.368 -2.864 31.991  1.00 12.57 ? 255 ASP C OD1 1 
ATOM   5979 O  OD2 . ASP C 1 277 ? 25.508 -1.240 30.540  1.00 13.01 ? 255 ASP C OD2 1 
ATOM   5980 N  N   . GLY C 1 278 ? 24.996 0.653  35.859  1.00 12.35 ? 256 GLY C N   1 
ATOM   5981 C  CA  . GLY C 1 278 ? 25.377 1.701  36.801  1.00 12.84 ? 256 GLY C CA  1 
ATOM   5982 C  C   . GLY C 1 278 ? 25.321 3.086  36.184  1.00 13.49 ? 256 GLY C C   1 
ATOM   5983 O  O   . GLY C 1 278 ? 25.284 3.234  34.961  1.00 13.00 ? 256 GLY C O   1 
ATOM   5984 N  N   . LEU C 1 279 ? 25.331 4.106  37.038  1.00 14.87 ? 257 LEU C N   1 
ATOM   5985 C  CA  . LEU C 1 279 ? 25.171 5.488  36.576  1.00 15.53 ? 257 LEU C CA  1 
ATOM   5986 C  C   . LEU C 1 279 ? 26.335 5.981  35.714  1.00 15.34 ? 257 LEU C C   1 
ATOM   5987 O  O   . LEU C 1 279 ? 26.112 6.697  34.738  1.00 15.20 ? 257 LEU C O   1 
ATOM   5988 C  CB  . LEU C 1 279 ? 24.927 6.434  37.758  1.00 16.56 ? 257 LEU C CB  1 
ATOM   5989 C  CG  . LEU C 1 279 ? 23.489 6.388  38.280  1.00 17.42 ? 257 LEU C CG  1 
ATOM   5990 C  CD1 . LEU C 1 279 ? 23.393 6.912  39.706  1.00 18.12 ? 257 LEU C CD1 1 
ATOM   5991 C  CD2 . LEU C 1 279 ? 22.547 7.154  37.355  1.00 18.07 ? 257 LEU C CD2 1 
ATOM   5992 N  N   . ARG C 1 280 ? 27.566 5.597  36.052  1.00 15.49 ? 258 ARG C N   1 
ATOM   5993 C  CA  . ARG C 1 280 ? 28.732 5.988  35.254  1.00 15.83 ? 258 ARG C CA  1 
ATOM   5994 C  C   . ARG C 1 280 ? 28.589 5.518  33.802  1.00 14.54 ? 258 ARG C C   1 
ATOM   5995 O  O   . ARG C 1 280 ? 28.822 6.287  32.864  1.00 14.42 ? 258 ARG C O   1 
ATOM   5996 C  CB  . ARG C 1 280 ? 30.026 5.444  35.879  1.00 17.40 ? 258 ARG C CB  1 
ATOM   5997 C  CG  . ARG C 1 280 ? 31.292 5.692  35.070  1.00 18.79 ? 258 ARG C CG  1 
ATOM   5998 C  CD  . ARG C 1 280 ? 31.785 7.127  35.166  1.00 20.39 ? 258 ARG C CD  1 
ATOM   5999 N  NE  . ARG C 1 280 ? 32.776 7.407  34.125  1.00 21.87 ? 258 ARG C NE  1 
ATOM   6000 C  CZ  . ARG C 1 280 ? 34.067 7.068  34.171  1.00 23.04 ? 258 ARG C CZ  1 
ATOM   6001 N  NH1 . ARG C 1 280 ? 34.582 6.438  35.225  1.00 23.25 ? 258 ARG C NH1 1 
ATOM   6002 N  NH2 . ARG C 1 280 ? 34.859 7.374  33.149  1.00 23.85 ? 258 ARG C NH2 1 
ATOM   6003 N  N   . ALA C 1 281 ? 28.197 4.258  33.627  1.00 13.21 ? 259 ALA C N   1 
ATOM   6004 C  CA  . ALA C 1 281 ? 27.949 3.703  32.301  1.00 12.41 ? 259 ALA C CA  1 
ATOM   6005 C  C   . ALA C 1 281 ? 26.781 4.410  31.607  1.00 11.74 ? 259 ALA C C   1 
ATOM   6006 O  O   . ALA C 1 281 ? 26.819 4.643  30.400  1.00 11.73 ? 259 ALA C O   1 
ATOM   6007 C  CB  . ALA C 1 281 ? 27.684 2.208  32.391  1.00 12.29 ? 259 ALA C CB  1 
ATOM   6008 N  N   . ALA C 1 282 ? 25.745 4.752  32.370  1.00 11.27 ? 260 ALA C N   1 
ATOM   6009 C  CA  . ALA C 1 282 ? 24.576 5.424  31.802  1.00 10.95 ? 260 ALA C CA  1 
ATOM   6010 C  C   . ALA C 1 282 ? 24.926 6.827  31.303  1.00 10.81 ? 260 ALA C C   1 
ATOM   6011 O  O   . ALA C 1 282 ? 24.400 7.272  30.282  1.00 10.44 ? 260 ALA C O   1 
ATOM   6012 C  CB  . ALA C 1 282 ? 23.444 5.481  32.819  1.00 11.07 ? 260 ALA C CB  1 
ATOM   6013 N  N   . ILE C 1 283 ? 25.809 7.515  32.022  1.00 10.81 ? 261 ILE C N   1 
ATOM   6014 C  CA  . ILE C 1 283 ? 26.287 8.833  31.586  1.00 11.16 ? 261 ILE C CA  1 
ATOM   6015 C  C   . ILE C 1 283 ? 27.100 8.695  30.301  1.00 10.98 ? 261 ILE C C   1 
ATOM   6016 O  O   . ILE C 1 283 ? 26.982 9.525  29.402  1.00 10.73 ? 261 ILE C O   1 
ATOM   6017 C  CB  . ILE C 1 283 ? 27.117 9.539  32.683  1.00 11.43 ? 261 ILE C CB  1 
ATOM   6018 C  CG1 . ILE C 1 283 ? 26.233 9.879  33.886  1.00 11.81 ? 261 ILE C CG1 1 
ATOM   6019 C  CG2 . ILE C 1 283 ? 27.788 10.800 32.146  1.00 11.59 ? 261 ILE C CG2 1 
ATOM   6020 C  CD1 . ILE C 1 283 ? 25.108 10.850 33.598  1.00 12.05 ? 261 ILE C CD1 1 
ATOM   6021 N  N   . ALA C 1 284 ? 27.917 7.646  30.206  1.00 10.79 ? 262 ALA C N   1 
ATOM   6022 C  CA  . ALA C 1 284 ? 28.660 7.383  28.977  1.00 10.92 ? 262 ALA C CA  1 
ATOM   6023 C  C   . ALA C 1 284 ? 27.706 7.144  27.808  1.00 10.91 ? 262 ALA C C   1 
ATOM   6024 O  O   . ALA C 1 284 ? 27.897 7.701  26.726  1.00 11.02 ? 262 ALA C O   1 
ATOM   6025 C  CB  . ALA C 1 284 ? 29.597 6.191  29.157  1.00 10.89 ? 262 ALA C CB  1 
ATOM   6026 N  N   . TRP C 1 285 ? 26.686 6.316  28.033  1.00 10.78 ? 263 TRP C N   1 
ATOM   6027 C  CA  . TRP C 1 285 ? 25.647 6.062  27.037  1.00 10.95 ? 263 TRP C CA  1 
ATOM   6028 C  C   . TRP C 1 285 ? 24.991 7.379  26.631  1.00 10.82 ? 263 TRP C C   1 
ATOM   6029 O  O   . TRP C 1 285 ? 24.795 7.645  25.449  1.00 10.38 ? 263 TRP C O   1 
ATOM   6030 C  CB  . TRP C 1 285 ? 24.587 5.092  27.585  1.00 11.31 ? 263 TRP C CB  1 
ATOM   6031 C  CG  . TRP C 1 285 ? 23.349 4.973  26.727  1.00 11.75 ? 263 TRP C CG  1 
ATOM   6032 C  CD1 . TRP C 1 285 ? 23.145 4.104  25.697  1.00 12.01 ? 263 TRP C CD1 1 
ATOM   6033 C  CD2 . TRP C 1 285 ? 22.155 5.755  26.834  1.00 11.89 ? 263 TRP C CD2 1 
ATOM   6034 N  NE1 . TRP C 1 285 ? 21.897 4.293  25.154  1.00 12.38 ? 263 TRP C NE1 1 
ATOM   6035 C  CE2 . TRP C 1 285 ? 21.269 5.305  25.833  1.00 12.05 ? 263 TRP C CE2 1 
ATOM   6036 C  CE3 . TRP C 1 285 ? 21.750 6.795  27.676  1.00 11.94 ? 263 TRP C CE3 1 
ATOM   6037 C  CZ2 . TRP C 1 285 ? 19.999 5.859  25.656  1.00 12.17 ? 263 TRP C CZ2 1 
ATOM   6038 C  CZ3 . TRP C 1 285 ? 20.489 7.341  27.501  1.00 12.03 ? 263 TRP C CZ3 1 
ATOM   6039 C  CH2 . TRP C 1 285 ? 19.630 6.872  26.497  1.00 12.05 ? 263 TRP C CH2 1 
ATOM   6040 N  N   . ARG C 1 286 ? 24.672 8.201  27.623  1.00 10.96 ? 264 ARG C N   1 
ATOM   6041 C  CA  . ARG C 1 286 ? 24.017 9.485  27.377  1.00 11.42 ? 264 ARG C CA  1 
ATOM   6042 C  C   . ARG C 1 286 ? 24.881 10.388 26.500  1.00 11.72 ? 264 ARG C C   1 
ATOM   6043 O  O   . ARG C 1 286 ? 24.428 10.886 25.469  1.00 11.85 ? 264 ARG C O   1 
ATOM   6044 C  CB  . ARG C 1 286 ? 23.716 10.176 28.713  1.00 11.72 ? 264 ARG C CB  1 
ATOM   6045 C  CG  . ARG C 1 286 ? 22.958 11.492 28.605  1.00 12.06 ? 264 ARG C CG  1 
ATOM   6046 C  CD  . ARG C 1 286 ? 23.120 12.320 29.868  1.00 12.32 ? 264 ARG C CD  1 
ATOM   6047 N  NE  . ARG C 1 286 ? 24.467 12.876 29.988  1.00 12.79 ? 264 ARG C NE  1 
ATOM   6048 C  CZ  . ARG C 1 286 ? 24.854 13.734 30.930  1.00 13.28 ? 264 ARG C CZ  1 
ATOM   6049 N  NH1 . ARG C 1 286 ? 24.002 14.145 31.864  1.00 13.79 ? 264 ARG C NH1 1 
ATOM   6050 N  NH2 . ARG C 1 286 ? 26.101 14.188 30.939  1.00 13.63 ? 264 ARG C NH2 1 
ATOM   6051 N  N   . ASP C 1 287 ? 26.130 10.583 26.909  1.00 12.01 ? 265 ASP C N   1 
ATOM   6052 C  CA  . ASP C 1 287 ? 27.040 11.496 26.213  1.00 12.59 ? 265 ASP C CA  1 
ATOM   6053 C  C   . ASP C 1 287 ? 27.326 11.057 24.772  1.00 12.58 ? 265 ASP C C   1 
ATOM   6054 O  O   . ASP C 1 287 ? 27.516 11.899 23.891  1.00 12.60 ? 265 ASP C O   1 
ATOM   6055 C  CB  . ASP C 1 287 ? 28.352 11.647 26.987  1.00 13.04 ? 265 ASP C CB  1 
ATOM   6056 C  CG  . ASP C 1 287 ? 28.167 12.299 28.353  1.00 13.57 ? 265 ASP C CG  1 
ATOM   6057 O  OD1 . ASP C 1 287 ? 27.080 12.863 28.634  1.00 13.99 ? 265 ASP C OD1 1 
ATOM   6058 O  OD2 . ASP C 1 287 ? 29.119 12.236 29.156  1.00 14.20 ? 265 ASP C OD2 1 
ATOM   6059 N  N   . ALA C 1 288 ? 27.335 9.746  24.529  1.00 12.65 ? 266 ALA C N   1 
ATOM   6060 C  CA  . ALA C 1 288 ? 27.605 9.210  23.189  1.00 12.99 ? 266 ALA C CA  1 
ATOM   6061 C  C   . ALA C 1 288 ? 26.503 9.540  22.178  1.00 13.44 ? 266 ALA C C   1 
ATOM   6062 O  O   . ALA C 1 288 ? 26.713 9.443  20.967  1.00 13.52 ? 266 ALA C O   1 
ATOM   6063 C  CB  . ALA C 1 288 ? 27.827 7.703  23.253  1.00 13.00 ? 266 ALA C CB  1 
ATOM   6064 N  N   . ARG C 1 289 ? 25.329 9.928  22.668  1.00 13.68 ? 267 ARG C N   1 
ATOM   6065 C  CA  . ARG C 1 289 ? 24.228 10.320 21.788  1.00 14.11 ? 267 ARG C CA  1 
ATOM   6066 C  C   . ARG C 1 289 ? 24.430 11.703 21.173  1.00 14.30 ? 267 ARG C C   1 
ATOM   6067 O  O   . ARG C 1 289 ? 23.767 12.047 20.193  1.00 14.34 ? 267 ARG C O   1 
ATOM   6068 C  CB  . ARG C 1 289 ? 22.905 10.307 22.558  1.00 14.39 ? 267 ARG C CB  1 
ATOM   6069 C  CG  . ARG C 1 289 ? 22.468 8.937  23.064  1.00 14.71 ? 267 ARG C CG  1 
ATOM   6070 C  CD  . ARG C 1 289 ? 21.370 9.071  24.110  1.00 15.03 ? 267 ARG C CD  1 
ATOM   6071 N  NE  . ARG C 1 289 ? 20.297 9.923  23.612  1.00 15.30 ? 267 ARG C NE  1 
ATOM   6072 C  CZ  . ARG C 1 289 ? 19.533 10.735 24.340  1.00 15.84 ? 267 ARG C CZ  1 
ATOM   6073 N  NH1 . ARG C 1 289 ? 19.675 10.834 25.657  1.00 15.93 ? 267 ARG C NH1 1 
ATOM   6074 N  NH2 . ARG C 1 289 ? 18.607 11.465 23.728  1.00 16.29 ? 267 ARG C NH2 1 
ATOM   6075 N  N   . PHE C 1 290 ? 25.326 12.494 21.752  1.00 14.44 ? 268 PHE C N   1 
ATOM   6076 C  CA  . PHE C 1 290 ? 25.513 13.879 21.333  1.00 14.93 ? 268 PHE C CA  1 
ATOM   6077 C  C   . PHE C 1 290 ? 26.869 14.055 20.656  1.00 16.45 ? 268 PHE C C   1 
ATOM   6078 O  O   . PHE C 1 290 ? 27.738 13.189 20.776  1.00 16.81 ? 268 PHE C O   1 
ATOM   6079 C  CB  . PHE C 1 290 ? 25.337 14.796 22.542  1.00 14.31 ? 268 PHE C CB  1 
ATOM   6080 C  CG  . PHE C 1 290 ? 23.974 14.684 23.170  1.00 13.60 ? 268 PHE C CG  1 
ATOM   6081 C  CD1 . PHE C 1 290 ? 22.887 15.337 22.611  1.00 13.29 ? 268 PHE C CD1 1 
ATOM   6082 C  CD2 . PHE C 1 290 ? 23.762 13.888 24.289  1.00 13.23 ? 268 PHE C CD2 1 
ATOM   6083 C  CE1 . PHE C 1 290 ? 21.627 15.221 23.166  1.00 13.01 ? 268 PHE C CE1 1 
ATOM   6084 C  CE2 . PHE C 1 290 ? 22.502 13.769 24.847  1.00 13.14 ? 268 PHE C CE2 1 
ATOM   6085 C  CZ  . PHE C 1 290 ? 21.432 14.434 24.285  1.00 13.12 ? 268 PHE C CZ  1 
ATOM   6086 N  N   . PRO C 1 291 ? 27.043 15.158 19.907  1.00 17.84 ? 269 PRO C N   1 
ATOM   6087 C  CA  . PRO C 1 291 ? 28.338 15.394 19.271  1.00 18.94 ? 269 PRO C CA  1 
ATOM   6088 C  C   . PRO C 1 291 ? 29.465 15.513 20.293  1.00 20.22 ? 269 PRO C C   1 
ATOM   6089 O  O   . PRO C 1 291 ? 29.238 15.951 21.420  1.00 20.66 ? 269 PRO C O   1 
ATOM   6090 C  CB  . PRO C 1 291 ? 28.127 16.721 18.525  1.00 18.92 ? 269 PRO C CB  1 
ATOM   6091 C  CG  . PRO C 1 291 ? 26.655 16.806 18.312  1.00 18.39 ? 269 PRO C CG  1 
ATOM   6092 C  CD  . PRO C 1 291 ? 26.067 16.205 19.556  1.00 18.10 ? 269 PRO C CD  1 
ATOM   6093 N  N   . ALA C 1 292 ? 30.666 15.102 19.900  1.00 22.36 ? 270 ALA C N   1 
ATOM   6094 C  CA  . ALA C 1 292 ? 31.844 15.228 20.752  1.00 24.11 ? 270 ALA C CA  1 
ATOM   6095 C  C   . ALA C 1 292 ? 32.318 16.677 20.782  1.00 25.41 ? 270 ALA C C   1 
ATOM   6096 O  O   . ALA C 1 292 ? 31.855 17.475 21.597  1.00 28.31 ? 270 ALA C O   1 
ATOM   6097 C  CB  . ALA C 1 292 ? 32.955 14.322 20.246  1.00 24.40 ? 270 ALA C CB  1 
HETATM 6098 O  O1  . TLA D 2 .   ? 19.057 50.667 -9.219  1.00 28.04 ? 301 TLA A O1  1 
HETATM 6099 O  O11 . TLA D 2 .   ? 20.611 49.169 -8.832  1.00 27.48 ? 301 TLA A O11 1 
HETATM 6100 C  C1  . TLA D 2 .   ? 20.148 50.325 -8.711  1.00 27.56 ? 301 TLA A C1  1 
HETATM 6101 C  C2  . TLA D 2 .   ? 20.929 51.342 -7.917  1.00 27.13 ? 301 TLA A C2  1 
HETATM 6102 O  O2  . TLA D 2 .   ? 20.231 52.594 -7.908  1.00 26.77 ? 301 TLA A O2  1 
HETATM 6103 C  C3  . TLA D 2 .   ? 22.326 51.546 -8.505  1.00 26.84 ? 301 TLA A C3  1 
HETATM 6104 O  O3  . TLA D 2 .   ? 22.224 51.945 -9.880  1.00 27.54 ? 301 TLA A O3  1 
HETATM 6105 C  C4  . TLA D 2 .   ? 23.066 52.609 -7.741  1.00 26.41 ? 301 TLA A C4  1 
HETATM 6106 O  O4  . TLA D 2 .   ? 23.423 53.645 -8.341  1.00 26.02 ? 301 TLA A O4  1 
HETATM 6107 O  O41 . TLA D 2 .   ? 23.303 52.429 -6.530  1.00 25.90 ? 301 TLA A O41 1 
HETATM 6108 C  C1  . GOL E 3 .   ? 26.542 21.735 22.348  1.00 25.30 ? 302 GOL A C1  1 
HETATM 6109 O  O1  . GOL E 3 .   ? 26.891 22.886 23.123  1.00 25.62 ? 302 GOL A O1  1 
HETATM 6110 C  C2  . GOL E 3 .   ? 27.561 21.535 21.232  1.00 25.46 ? 302 GOL A C2  1 
HETATM 6111 O  O2  . GOL E 3 .   ? 27.680 22.736 20.464  1.00 24.95 ? 302 GOL A O2  1 
HETATM 6112 C  C3  . GOL E 3 .   ? 27.116 20.389 20.327  1.00 25.49 ? 302 GOL A C3  1 
HETATM 6113 O  O3  . GOL E 3 .   ? 27.145 19.148 21.047  1.00 25.90 ? 302 GOL A O3  1 
HETATM 6114 O  O1  . TLA F 2 .   ? -1.680 6.786  34.473  0.50 18.48 ? 601 TLA C O1  1 
HETATM 6115 O  O11 . TLA F 2 .   ? -0.763 8.787  34.491  0.50 17.60 ? 601 TLA C O11 1 
HETATM 6116 C  C1  . TLA F 2 .   ? -1.097 7.737  33.908  0.50 18.34 ? 601 TLA C C1  1 
HETATM 6117 C  C2  . TLA F 2 .   ? -0.757 7.624  32.455  0.50 18.33 ? 601 TLA C C2  1 
HETATM 6118 O  O2  . TLA F 2 .   ? -1.314 6.437  31.878  0.50 18.77 ? 601 TLA C O2  1 
HETATM 6119 C  C3  . TLA F 2 .   ? 0.754  7.603  32.330  0.50 18.31 ? 601 TLA C C3  1 
HETATM 6120 O  O3  . TLA F 2 .   ? 1.278  6.399  32.901  0.50 18.74 ? 601 TLA C O3  1 
HETATM 6121 C  C4  . TLA F 2 .   ? 1.097  7.715  30.878  0.50 18.36 ? 601 TLA C C4  1 
HETATM 6122 O  O4  . TLA F 2 .   ? 1.679  6.763  30.315  0.50 18.53 ? 601 TLA C O4  1 
HETATM 6123 O  O41 . TLA F 2 .   ? 0.767  8.766  30.294  0.50 17.68 ? 601 TLA C O41 1 
HETATM 6124 O  O1  . TLA G 2 .   ? 24.457 38.928 66.638  1.00 23.62 ? 602 TLA C O1  1 
HETATM 6125 O  O11 . TLA G 2 .   ? 23.172 40.035 65.238  1.00 23.67 ? 602 TLA C O11 1 
HETATM 6126 C  C1  . TLA G 2 .   ? 24.277 39.562 65.576  1.00 22.95 ? 602 TLA C C1  1 
HETATM 6127 C  C2  . TLA G 2 .   ? 25.442 39.759 64.656  1.00 22.18 ? 602 TLA C C2  1 
HETATM 6128 O  O2  . TLA G 2 .   ? 26.583 39.077 65.184  1.00 21.71 ? 602 TLA C O2  1 
HETATM 6129 C  C3  . TLA G 2 .   ? 25.772 41.235 64.475  1.00 21.55 ? 602 TLA C C3  1 
HETATM 6130 O  O3  . TLA G 2 .   ? 26.025 41.849 65.748  1.00 22.12 ? 602 TLA C O3  1 
HETATM 6131 C  C4  . TLA G 2 .   ? 26.977 41.340 63.580  1.00 21.07 ? 602 TLA C C4  1 
HETATM 6132 O  O4  . TLA G 2 .   ? 28.011 41.902 64.012  1.00 20.78 ? 602 TLA C O4  1 
HETATM 6133 O  O41 . TLA G 2 .   ? 26.908 40.847 62.428  1.00 19.93 ? 602 TLA C O41 1 
HETATM 6134 C  C1  . GOL H 3 .   ? 11.799 14.324 42.607  1.00 18.82 ? 603 GOL C C1  1 
HETATM 6135 O  O1  . GOL H 3 .   ? 12.817 15.185 43.150  1.00 19.24 ? 603 GOL C O1  1 
HETATM 6136 C  C2  . GOL H 3 .   ? 12.247 13.702 41.281  1.00 18.97 ? 603 GOL C C2  1 
HETATM 6137 O  O2  . GOL H 3 .   ? 13.249 12.705 41.520  1.00 19.64 ? 603 GOL C O2  1 
HETATM 6138 C  C3  . GOL H 3 .   ? 12.840 14.732 40.324  1.00 18.60 ? 603 GOL C C3  1 
HETATM 6139 O  O3  . GOL H 3 .   ? 11.863 15.687 39.891  1.00 18.24 ? 603 GOL C O3  1 
HETATM 6140 O  O   . HOH I 4 .   ? 14.235 45.528 6.506   1.00 11.33 ? 401 HOH A O   1 
HETATM 6141 O  O   . HOH I 4 .   ? 2.041  37.732 24.608  1.00 6.59  ? 402 HOH A O   1 
HETATM 6142 O  O   . HOH I 4 .   ? -0.821 36.295 23.821  1.00 5.34  ? 403 HOH A O   1 
HETATM 6143 O  O   . HOH I 4 .   ? 7.884  44.959 21.472  1.00 9.91  ? 404 HOH A O   1 
HETATM 6144 O  O   . HOH I 4 .   ? 19.759 25.518 2.313   1.00 10.57 ? 405 HOH A O   1 
HETATM 6145 O  O   . HOH I 4 .   ? 4.136  33.970 12.471  1.00 10.19 ? 406 HOH A O   1 
HETATM 6146 O  O   . HOH I 4 .   ? 24.622 33.692 6.961   1.00 6.93  ? 407 HOH A O   1 
HETATM 6147 O  O   . HOH I 4 .   ? 8.895  49.840 8.394   1.00 7.24  ? 408 HOH A O   1 
HETATM 6148 O  O   . HOH I 4 .   ? 7.423  23.998 20.610  1.00 8.46  ? 409 HOH A O   1 
HETATM 6149 O  O   . HOH I 4 .   ? 6.573  44.763 16.139  1.00 5.28  ? 410 HOH A O   1 
HETATM 6150 O  O   . HOH I 4 .   ? 13.574 44.787 16.915  1.00 8.77  ? 411 HOH A O   1 
HETATM 6151 O  O   . HOH I 4 .   ? 7.346  50.365 15.297  1.00 7.16  ? 412 HOH A O   1 
HETATM 6152 O  O   . HOH I 4 .   ? 6.388  28.701 12.391  1.00 9.04  ? 413 HOH A O   1 
HETATM 6153 O  O   . HOH I 4 .   ? 6.206  54.816 3.675   1.00 9.11  ? 414 HOH A O   1 
HETATM 6154 O  O   . HOH I 4 .   ? 19.953 37.284 16.909  1.00 9.18  ? 415 HOH A O   1 
HETATM 6155 O  O   . HOH I 4 .   ? -3.084 52.541 0.322   1.00 9.95  ? 416 HOH A O   1 
HETATM 6156 O  O   . HOH I 4 .   ? 3.309  22.411 8.204   1.00 13.50 ? 417 HOH A O   1 
HETATM 6157 O  O   . HOH I 4 .   ? -4.866 53.695 2.086   1.00 9.66  ? 418 HOH A O   1 
HETATM 6158 O  O   . HOH I 4 .   ? 9.956  48.267 6.466   1.00 12.54 ? 419 HOH A O   1 
HETATM 6159 O  O   . HOH I 4 .   ? 31.882 24.845 8.683   1.00 14.44 ? 420 HOH A O   1 
HETATM 6160 O  O   . HOH I 4 .   ? 14.630 16.600 18.706  1.00 9.27  ? 421 HOH A O   1 
HETATM 6161 O  O   . HOH I 4 .   ? 33.115 40.752 16.337  1.00 14.65 ? 422 HOH A O   1 
HETATM 6162 O  O   . HOH I 4 .   ? 4.886  61.464 7.964   1.00 10.79 ? 423 HOH A O   1 
HETATM 6163 O  O   . HOH I 4 .   ? 2.670  36.018 13.722  1.00 12.26 ? 424 HOH A O   1 
HETATM 6164 O  O   . HOH I 4 .   ? 9.356  52.271 14.780  1.00 9.41  ? 425 HOH A O   1 
HETATM 6165 O  O   . HOH I 4 .   ? 2.752  55.613 2.142   1.00 11.34 ? 426 HOH A O   1 
HETATM 6166 O  O   . HOH I 4 .   ? 16.259 52.298 13.350  1.00 7.53  ? 427 HOH A O   1 
HETATM 6167 O  O   . HOH I 4 .   ? 19.885 39.578 15.208  1.00 8.31  ? 428 HOH A O   1 
HETATM 6168 O  O   . HOH I 4 .   ? 8.590  14.072 25.947  1.00 13.07 ? 429 HOH A O   1 
HETATM 6169 O  O   . HOH I 4 .   ? 10.464 64.654 1.911   1.00 15.39 ? 430 HOH A O   1 
HETATM 6170 O  O   . HOH I 4 .   ? 7.433  29.509 31.374  1.00 6.29  ? 431 HOH A O   1 
HETATM 6171 O  O   . HOH I 4 .   ? 12.833 18.514 17.666  1.00 12.56 ? 432 HOH A O   1 
HETATM 6172 O  O   . HOH I 4 .   ? 15.556 40.369 -3.166  1.00 15.71 ? 433 HOH A O   1 
HETATM 6173 O  O   . HOH I 4 .   ? 10.487 55.245 -4.920  1.00 17.76 ? 434 HOH A O   1 
HETATM 6174 O  O   . HOH I 4 .   ? 8.574  46.536 4.771   1.00 22.25 ? 435 HOH A O   1 
HETATM 6175 O  O   . HOH I 4 .   ? 16.071 59.596 8.942   1.00 11.65 ? 436 HOH A O   1 
HETATM 6176 O  O   . HOH I 4 .   ? 20.915 13.916 15.698  1.00 12.22 ? 437 HOH A O   1 
HETATM 6177 O  O   . HOH I 4 .   ? 26.515 35.531 24.269  1.00 10.52 ? 438 HOH A O   1 
HETATM 6178 O  O   . HOH I 4 .   ? 18.834 37.144 24.844  1.00 10.99 ? 439 HOH A O   1 
HETATM 6179 O  O   . HOH I 4 .   ? 1.675  32.039 31.964  1.00 10.49 ? 440 HOH A O   1 
HETATM 6180 O  O   . HOH I 4 .   ? 11.044 50.203 4.783   1.00 11.46 ? 441 HOH A O   1 
HETATM 6181 O  O   . HOH I 4 .   ? 4.630  16.778 22.679  1.00 16.77 ? 442 HOH A O   1 
HETATM 6182 O  O   . HOH I 4 .   ? 31.687 38.738 23.250  1.00 13.65 ? 443 HOH A O   1 
HETATM 6183 O  O   . HOH I 4 .   ? -0.441 42.217 27.178  1.00 9.63  ? 444 HOH A O   1 
HETATM 6184 O  O   . HOH I 4 .   ? -0.243 36.270 30.510  1.00 10.48 ? 445 HOH A O   1 
HETATM 6185 O  O   . HOH I 4 .   ? 1.134  58.249 2.005   1.00 14.05 ? 446 HOH A O   1 
HETATM 6186 O  O   . HOH I 4 .   ? 11.936 46.525 10.371  1.00 12.85 ? 447 HOH A O   1 
HETATM 6187 O  O   . HOH I 4 .   ? 8.572  53.697 -0.187  1.00 18.31 ? 448 HOH A O   1 
HETATM 6188 O  O   . HOH I 4 .   ? -7.756 50.686 6.758   1.00 13.88 ? 449 HOH A O   1 
HETATM 6189 O  O   . HOH I 4 .   ? 1.441  39.031 32.752  1.00 14.55 ? 450 HOH A O   1 
HETATM 6190 O  O   . HOH I 4 .   ? 7.205  18.331 4.623   1.00 16.60 ? 451 HOH A O   1 
HETATM 6191 O  O   . HOH I 4 .   ? 3.320  36.579 16.450  1.00 13.08 ? 452 HOH A O   1 
HETATM 6192 O  O   . HOH I 4 .   ? 6.642  33.560 -2.970  1.00 16.87 ? 453 HOH A O   1 
HETATM 6193 O  O   . HOH I 4 .   ? -5.127 46.751 3.675   1.00 10.45 ? 454 HOH A O   1 
HETATM 6194 O  O   . HOH I 4 .   ? 22.346 51.037 6.553   1.00 18.02 ? 455 HOH A O   1 
HETATM 6195 O  O   . HOH I 4 .   ? 26.372 32.525 5.196   1.00 13.64 ? 456 HOH A O   1 
HETATM 6196 O  O   . HOH I 4 .   ? 11.336 18.424 4.329   1.00 15.18 ? 457 HOH A O   1 
HETATM 6197 O  O   . HOH I 4 .   ? -1.868 57.995 1.955   1.00 19.01 ? 458 HOH A O   1 
HETATM 6198 O  O   . HOH I 4 .   ? 5.941  14.966 24.508  1.00 17.49 ? 459 HOH A O   1 
HETATM 6199 O  O   . HOH I 4 .   ? 5.424  58.986 8.994   1.00 11.60 ? 460 HOH A O   1 
HETATM 6200 O  O   . HOH I 4 .   ? 8.134  56.157 6.357   1.00 9.79  ? 461 HOH A O   1 
HETATM 6201 O  O   . HOH I 4 .   ? 10.023 59.496 -3.023  1.00 16.42 ? 462 HOH A O   1 
HETATM 6202 O  O   . HOH I 4 .   ? 7.568  64.891 1.930   1.00 21.91 ? 463 HOH A O   1 
HETATM 6203 O  O   . HOH I 4 .   ? -9.917 51.833 3.729   1.00 9.96  ? 464 HOH A O   1 
HETATM 6204 O  O   . HOH I 4 .   ? -0.000 34.194 32.392  0.50 11.20 ? 465 HOH A O   1 
HETATM 6205 O  O   . HOH I 4 .   ? 26.946 50.242 14.771  1.00 17.37 ? 466 HOH A O   1 
HETATM 6206 O  O   . HOH I 4 .   ? 4.185  62.214 4.026   1.00 17.15 ? 467 HOH A O   1 
HETATM 6207 O  O   . HOH I 4 .   ? 17.708 14.316 7.114   1.00 18.91 ? 468 HOH A O   1 
HETATM 6208 O  O   . HOH I 4 .   ? 29.188 19.597 12.083  1.00 17.84 ? 469 HOH A O   1 
HETATM 6209 O  O   . HOH I 4 .   ? 24.907 24.636 8.649   1.00 11.64 ? 470 HOH A O   1 
HETATM 6210 O  O   . HOH I 4 .   ? 3.836  34.072 7.714   1.00 14.30 ? 471 HOH A O   1 
HETATM 6211 O  O   . HOH I 4 .   ? 12.310 47.239 7.624   1.00 17.01 ? 472 HOH A O   1 
HETATM 6212 O  O   . HOH I 4 .   ? 30.825 34.118 21.922  1.00 14.82 ? 473 HOH A O   1 
HETATM 6213 O  O   . HOH I 4 .   ? 26.991 48.774 21.654  1.00 23.13 ? 474 HOH A O   1 
HETATM 6214 O  O   . HOH I 4 .   ? 17.262 29.807 -4.994  1.00 15.77 ? 475 HOH A O   1 
HETATM 6215 O  O   . HOH I 4 .   ? 21.767 43.414 27.054  1.00 16.40 ? 476 HOH A O   1 
HETATM 6216 O  O   . HOH I 4 .   ? 10.657 22.928 1.274   1.00 19.89 ? 477 HOH A O   1 
HETATM 6217 O  O   . HOH I 4 .   ? 20.717 11.390 16.690  1.00 19.47 ? 478 HOH A O   1 
HETATM 6218 O  O   . HOH I 4 .   ? 14.822 64.978 8.992   1.00 16.56 ? 479 HOH A O   1 
HETATM 6219 O  O   . HOH I 4 .   ? 25.464 29.534 2.779   1.00 17.56 ? 480 HOH A O   1 
HETATM 6220 O  O   . HOH I 4 .   ? 34.257 38.061 0.450   1.00 15.71 ? 481 HOH A O   1 
HETATM 6221 O  O   . HOH I 4 .   ? 10.725 41.259 31.365  1.00 13.68 ? 482 HOH A O   1 
HETATM 6222 O  O   . HOH I 4 .   ? -4.272 50.957 -1.704  1.00 20.99 ? 483 HOH A O   1 
HETATM 6223 O  O   . HOH I 4 .   ? 29.227 34.624 24.170  1.00 16.50 ? 484 HOH A O   1 
HETATM 6224 O  O   . HOH I 4 .   ? 22.514 65.103 2.993   1.00 22.63 ? 485 HOH A O   1 
HETATM 6225 O  O   . HOH I 4 .   ? 12.883 64.892 5.668   1.00 21.00 ? 486 HOH A O   1 
HETATM 6226 O  O   . HOH I 4 .   ? 10.367 19.052 18.373  1.00 16.73 ? 487 HOH A O   1 
HETATM 6227 O  O   . HOH I 4 .   ? 4.653  23.693 19.870  1.00 15.75 ? 488 HOH A O   1 
HETATM 6228 O  O   . HOH I 4 .   ? 5.995  21.111 13.601  1.00 13.68 ? 489 HOH A O   1 
HETATM 6229 O  O   . HOH I 4 .   ? 29.960 37.424 25.069  1.00 18.38 ? 490 HOH A O   1 
HETATM 6230 O  O   . HOH I 4 .   ? 0.345  51.862 -3.529  1.00 18.18 ? 491 HOH A O   1 
HETATM 6231 O  O   . HOH I 4 .   ? -0.047 39.941 3.833   1.00 19.19 ? 492 HOH A O   1 
HETATM 6232 O  O   . HOH I 4 .   ? 19.728 9.800  20.706  1.00 16.85 ? 493 HOH A O   1 
HETATM 6233 O  O   . HOH I 4 .   ? 31.376 38.437 5.511   1.00 18.35 ? 494 HOH A O   1 
HETATM 6234 O  O   . HOH I 4 .   ? 0.000  44.942 9.217   1.00 15.02 ? 495 HOH A O   1 
HETATM 6235 O  O   . HOH I 4 .   ? 31.321 27.227 7.619   1.00 22.35 ? 496 HOH A O   1 
HETATM 6236 O  O   . HOH I 4 .   ? 13.526 49.111 5.898   1.00 20.98 ? 497 HOH A O   1 
HETATM 6237 O  O   . HOH I 4 .   ? 0.688  25.012 28.598  1.00 14.22 ? 498 HOH A O   1 
HETATM 6238 O  O   . HOH I 4 .   ? -4.956 43.959 4.173   1.00 16.78 ? 499 HOH A O   1 
HETATM 6239 O  O   . HOH I 4 .   ? 16.279 24.350 -2.700  1.00 16.23 ? 500 HOH A O   1 
HETATM 6240 O  O   . HOH I 4 .   ? 14.172 34.493 20.167  1.00 16.68 ? 501 HOH A O   1 
HETATM 6241 O  O   . HOH I 4 .   ? 0.660  46.438 -1.165  1.00 15.87 ? 502 HOH A O   1 
HETATM 6242 O  O   . HOH I 4 .   ? -2.041 43.945 10.662  1.00 16.99 ? 503 HOH A O   1 
HETATM 6243 O  O   . HOH I 4 .   ? 35.041 34.175 13.014  1.00 24.67 ? 504 HOH A O   1 
HETATM 6244 O  O   . HOH I 4 .   ? 5.058  30.479 20.565  1.00 18.32 ? 505 HOH A O   1 
HETATM 6245 O  O   . HOH I 4 .   ? 1.840  62.771 5.454   1.00 21.11 ? 506 HOH A O   1 
HETATM 6246 O  O   . HOH I 4 .   ? 24.230 56.069 -7.063  1.00 15.19 ? 507 HOH A O   1 
HETATM 6247 O  O   . HOH I 4 .   ? 9.166  39.794 -4.911  1.00 23.49 ? 508 HOH A O   1 
HETATM 6248 O  O   . HOH I 4 .   ? -7.585 47.059 2.355   1.00 22.59 ? 509 HOH A O   1 
HETATM 6249 O  O   . HOH I 4 .   ? 20.956 66.637 9.169   1.00 17.62 ? 510 HOH A O   1 
HETATM 6250 O  O   . HOH I 4 .   ? 5.286  23.894 1.822   1.00 15.94 ? 511 HOH A O   1 
HETATM 6251 O  O   . HOH I 4 .   ? -0.486 38.289 27.321  1.00 16.07 ? 512 HOH A O   1 
HETATM 6252 O  O   . HOH I 4 .   ? 24.516 56.446 8.459   1.00 18.36 ? 513 HOH A O   1 
HETATM 6253 O  O   . HOH I 4 .   ? 18.920 14.908 13.937  1.00 16.95 ? 514 HOH A O   1 
HETATM 6254 O  O   . HOH I 4 .   ? 6.951  17.094 12.442  1.00 16.81 ? 515 HOH A O   1 
HETATM 6255 O  O   . HOH I 4 .   ? 3.692  29.134 13.137  1.00 19.85 ? 516 HOH A O   1 
HETATM 6256 O  O   . HOH I 4 .   ? -0.390 39.709 29.611  1.00 28.34 ? 517 HOH A O   1 
HETATM 6257 O  O   . HOH I 4 .   ? 21.681 13.135 5.984   1.00 24.18 ? 518 HOH A O   1 
HETATM 6258 O  O   . HOH I 4 .   ? 18.119 18.124 0.757   1.00 25.36 ? 519 HOH A O   1 
HETATM 6259 O  O   . HOH I 4 .   ? 9.070  53.893 -2.935  1.00 21.09 ? 520 HOH A O   1 
HETATM 6260 O  O   . HOH I 4 .   ? 15.556 12.373 11.297  1.00 24.92 ? 521 HOH A O   1 
HETATM 6261 O  O   . HOH I 4 .   ? -1.384 46.273 12.473  1.00 28.00 ? 522 HOH A O   1 
HETATM 6262 O  O   . HOH I 4 .   ? 23.225 49.928 -5.327  1.00 24.72 ? 523 HOH A O   1 
HETATM 6263 O  O   . HOH I 4 .   ? 22.731 44.832 -1.908  1.00 27.40 ? 524 HOH A O   1 
HETATM 6264 O  O   . HOH I 4 .   ? 3.985  30.533 1.038   1.00 24.59 ? 525 HOH A O   1 
HETATM 6265 O  O   . HOH I 4 .   ? 17.133 12.744 13.648  1.00 24.30 ? 526 HOH A O   1 
HETATM 6266 O  O   . HOH I 4 .   ? 1.471  38.476 17.368  1.00 18.36 ? 527 HOH A O   1 
HETATM 6267 O  O   . HOH I 4 .   ? 8.727  56.669 0.034   1.00 18.61 ? 528 HOH A O   1 
HETATM 6268 O  O   . HOH I 4 .   ? 2.578  29.462 4.953   1.00 19.26 ? 529 HOH A O   1 
HETATM 6269 O  O   . HOH I 4 .   ? 11.635 40.928 29.082  1.00 19.35 ? 530 HOH A O   1 
HETATM 6270 O  O   . HOH I 4 .   ? -0.906 38.158 19.024  1.00 25.26 ? 531 HOH A O   1 
HETATM 6271 O  O   . HOH I 4 .   ? 0.484  36.780 7.193   1.00 18.22 ? 532 HOH A O   1 
HETATM 6272 O  O   . HOH I 4 .   ? 23.737 30.510 -3.600  1.00 18.25 ? 533 HOH A O   1 
HETATM 6273 O  O   . HOH I 4 .   ? -7.482 53.587 1.080   1.00 23.50 ? 534 HOH A O   1 
HETATM 6274 O  O   . HOH I 4 .   ? -2.156 51.222 12.894  1.00 18.88 ? 535 HOH A O   1 
HETATM 6275 O  O   . HOH I 4 .   ? 5.696  30.801 -2.284  1.00 26.35 ? 536 HOH A O   1 
HETATM 6276 O  O   . HOH I 4 .   ? 6.048  54.244 0.788   1.00 20.15 ? 537 HOH A O   1 
HETATM 6277 O  O   . HOH I 4 .   ? 26.048 49.526 -4.930  1.00 25.77 ? 538 HOH A O   1 
HETATM 6278 O  O   . HOH I 4 .   ? 13.446 44.715 -7.716  1.00 24.49 ? 539 HOH A O   1 
HETATM 6279 O  O   . HOH I 4 .   ? 5.176  27.941 21.458  1.00 21.92 ? 540 HOH A O   1 
HETATM 6280 O  O   . HOH I 4 .   ? 6.396  13.395 8.213   1.00 20.70 ? 541 HOH A O   1 
HETATM 6281 O  O   . HOH I 4 .   ? 7.135  26.703 19.946  1.00 22.12 ? 542 HOH A O   1 
HETATM 6282 O  O   . HOH I 4 .   ? -0.362 50.368 19.036  1.00 13.95 ? 543 HOH A O   1 
HETATM 6283 O  O   . HOH I 4 .   ? -3.699 55.975 3.532   1.00 12.29 ? 544 HOH A O   1 
HETATM 6284 O  O   . HOH I 4 .   ? 4.266  28.915 24.279  1.00 18.01 ? 545 HOH A O   1 
HETATM 6285 O  O   . HOH I 4 .   ? 28.040 60.985 2.672   1.00 22.51 ? 546 HOH A O   1 
HETATM 6286 O  O   . HOH I 4 .   ? 27.353 21.799 5.991   1.00 26.82 ? 547 HOH A O   1 
HETATM 6287 O  O   . HOH I 4 .   ? 32.471 36.503 21.674  1.00 23.01 ? 548 HOH A O   1 
HETATM 6288 O  O   . HOH I 4 .   ? 3.185  24.737 9.701   1.00 19.51 ? 549 HOH A O   1 
HETATM 6289 O  O   . HOH I 4 .   ? 2.941  25.649 2.123   1.00 21.57 ? 550 HOH A O   1 
HETATM 6290 O  O   . HOH I 4 .   ? 26.671 53.545 4.852   1.00 26.68 ? 551 HOH A O   1 
HETATM 6291 O  O   . HOH I 4 .   ? 12.511 31.514 19.182  1.00 23.49 ? 552 HOH A O   1 
HETATM 6292 O  O   . HOH I 4 .   ? 15.005 12.542 18.026  1.00 22.18 ? 553 HOH A O   1 
HETATM 6293 O  O   . HOH I 4 .   ? 22.744 13.352 13.668  1.00 24.94 ? 554 HOH A O   1 
HETATM 6294 O  O   . HOH I 4 .   ? 24.353 62.027 -2.887  1.00 23.70 ? 555 HOH A O   1 
HETATM 6295 O  O   . HOH I 4 .   ? 32.135 42.368 13.058  1.00 23.46 ? 556 HOH A O   1 
HETATM 6296 O  O   . HOH I 4 .   ? 1.081  31.976 25.105  1.00 22.92 ? 557 HOH A O   1 
HETATM 6297 O  O   . HOH I 4 .   ? 9.985  42.783 1.021   1.00 19.92 ? 558 HOH A O   1 
HETATM 6298 O  O   . HOH I 4 .   ? 33.487 40.295 24.591  1.00 20.75 ? 559 HOH A O   1 
HETATM 6299 O  O   . HOH I 4 .   ? 25.807 50.059 24.005  1.00 19.93 ? 560 HOH A O   1 
HETATM 6300 O  O   . HOH I 4 .   ? 9.031  45.829 -6.661  1.00 23.51 ? 561 HOH A O   1 
HETATM 6301 O  O   . HOH I 4 .   ? 31.952 23.117 15.642  1.00 33.85 ? 562 HOH A O   1 
HETATM 6302 O  O   . HOH I 4 .   ? 33.184 44.191 22.110  1.00 28.13 ? 563 HOH A O   1 
HETATM 6303 O  O   . HOH I 4 .   ? 13.807 41.648 -8.692  1.00 24.23 ? 564 HOH A O   1 
HETATM 6304 O  O   . HOH I 4 .   ? 25.232 41.551 -2.857  1.00 19.36 ? 565 HOH A O   1 
HETATM 6305 O  O   . HOH I 4 .   ? 17.742 46.405 0.098   1.00 22.87 ? 566 HOH A O   1 
HETATM 6306 O  O   . HOH I 4 .   ? 15.527 47.374 4.706   1.00 22.58 ? 567 HOH A O   1 
HETATM 6307 O  O   . HOH I 4 .   ? 10.025 14.507 14.886  1.00 24.06 ? 568 HOH A O   1 
HETATM 6308 O  O   . HOH I 4 .   ? 10.565 44.921 -0.618  1.00 22.55 ? 569 HOH A O   1 
HETATM 6309 O  O   . HOH I 4 .   ? 24.001 54.947 13.988  1.00 23.57 ? 570 HOH A O   1 
HETATM 6310 O  O   . HOH I 4 .   ? 20.215 44.826 -8.410  1.00 29.82 ? 571 HOH A O   1 
HETATM 6311 O  O   . HOH I 4 .   ? 19.327 44.713 -11.559 1.00 25.96 ? 572 HOH A O   1 
HETATM 6312 O  O   . HOH I 4 .   ? 15.741 53.016 28.280  1.00 22.80 ? 573 HOH A O   1 
HETATM 6313 O  O   . HOH I 4 .   ? 27.729 56.616 1.987   1.00 24.36 ? 574 HOH A O   1 
HETATM 6314 O  O   . HOH I 4 .   ? 3.740  20.474 16.655  1.00 20.83 ? 575 HOH A O   1 
HETATM 6315 O  O   . HOH I 4 .   ? 13.559 61.447 -8.249  1.00 23.12 ? 576 HOH A O   1 
HETATM 6316 O  O   . HOH I 4 .   ? 3.483  16.312 20.240  1.00 22.07 ? 577 HOH A O   1 
HETATM 6317 O  O   . HOH I 4 .   ? 8.463  28.901 -4.868  1.00 25.39 ? 578 HOH A O   1 
HETATM 6318 O  O   . HOH I 4 .   ? 15.367 32.998 21.959  1.00 25.26 ? 579 HOH A O   1 
HETATM 6319 O  O   . HOH I 4 .   ? 15.683 25.798 -5.004  1.00 23.60 ? 580 HOH A O   1 
HETATM 6320 O  O   . HOH I 4 .   ? 26.957 55.582 -0.600  1.00 23.43 ? 581 HOH A O   1 
HETATM 6321 O  O   . HOH I 4 .   ? 33.157 24.601 13.655  1.00 29.78 ? 582 HOH A O   1 
HETATM 6322 O  O   . HOH I 4 .   ? 20.034 35.535 -7.764  1.00 28.78 ? 583 HOH A O   1 
HETATM 6323 O  O   . HOH I 4 .   ? 11.203 12.382 6.517   1.00 28.98 ? 584 HOH A O   1 
HETATM 6324 O  O   . HOH I 4 .   ? 6.054  41.924 2.917   1.00 22.28 ? 585 HOH A O   1 
HETATM 6325 O  O   . HOH I 4 .   ? 29.997 43.811 28.105  1.00 25.73 ? 586 HOH A O   1 
HETATM 6326 O  O   . HOH I 4 .   ? 0.293  19.721 20.869  1.00 25.14 ? 587 HOH A O   1 
HETATM 6327 O  O   . HOH J 4 .   ? 2.814  49.628 32.857  1.00 6.22  ? 301 HOH B O   1 
HETATM 6328 O  O   . HOH J 4 .   ? 7.734  59.517 22.302  1.00 10.58 ? 302 HOH B O   1 
HETATM 6329 O  O   . HOH J 4 .   ? 18.222 60.158 46.734  1.00 10.99 ? 303 HOH B O   1 
HETATM 6330 O  O   . HOH J 4 .   ? 15.962 51.705 41.029  1.00 9.22  ? 304 HOH B O   1 
HETATM 6331 O  O   . HOH J 4 .   ? 10.382 50.942 47.400  1.00 7.85  ? 305 HOH B O   1 
HETATM 6332 O  O   . HOH J 4 .   ? 15.404 56.637 45.949  1.00 11.77 ? 306 HOH B O   1 
HETATM 6333 O  O   . HOH J 4 .   ? 21.675 54.818 33.712  1.00 9.29  ? 307 HOH B O   1 
HETATM 6334 O  O   . HOH J 4 .   ? 12.893 56.965 50.250  1.00 8.29  ? 308 HOH B O   1 
HETATM 6335 O  O   . HOH J 4 .   ? 2.379  63.570 58.109  1.00 9.57  ? 309 HOH B O   1 
HETATM 6336 O  O   . HOH J 4 .   ? 27.596 64.761 34.487  1.00 8.04  ? 310 HOH B O   1 
HETATM 6337 O  O   . HOH J 4 .   ? 22.003 55.093 36.517  1.00 9.42  ? 311 HOH B O   1 
HETATM 6338 O  O   . HOH J 4 .   ? 28.765 74.576 29.158  1.00 11.97 ? 312 HOH B O   1 
HETATM 6339 O  O   . HOH J 4 .   ? 19.695 50.765 48.839  1.00 8.06  ? 313 HOH B O   1 
HETATM 6340 O  O   . HOH J 4 .   ? 1.626  45.441 42.920  1.00 14.50 ? 314 HOH B O   1 
HETATM 6341 O  O   . HOH J 4 .   ? 9.137  53.002 42.406  1.00 6.71  ? 315 HOH B O   1 
HETATM 6342 O  O   . HOH J 4 .   ? -0.529 63.763 51.775  1.00 10.00 ? 316 HOH B O   1 
HETATM 6343 O  O   . HOH J 4 .   ? 14.085 59.344 49.633  1.00 12.11 ? 317 HOH B O   1 
HETATM 6344 O  O   . HOH J 4 .   ? 9.507  48.299 39.806  1.00 9.59  ? 318 HOH B O   1 
HETATM 6345 O  O   . HOH J 4 .   ? 14.446 64.198 15.803  1.00 9.87  ? 319 HOH B O   1 
HETATM 6346 O  O   . HOH J 4 .   ? 6.511  47.383 21.778  1.00 7.86  ? 320 HOH B O   1 
HETATM 6347 O  O   . HOH J 4 .   ? 29.120 66.764 33.330  1.00 10.20 ? 321 HOH B O   1 
HETATM 6348 O  O   . HOH J 4 .   ? 34.073 45.473 30.606  1.00 20.49 ? 322 HOH B O   1 
HETATM 6349 O  O   . HOH J 4 .   ? 30.993 68.726 35.749  1.00 11.76 ? 323 HOH B O   1 
HETATM 6350 O  O   . HOH J 4 .   ? 1.255  41.902 30.135  1.00 14.55 ? 324 HOH B O   1 
HETATM 6351 O  O   . HOH J 4 .   ? 0.479  61.549 58.491  1.00 10.97 ? 325 HOH B O   1 
HETATM 6352 O  O   . HOH J 4 .   ? 8.157  60.029 59.051  1.00 10.67 ? 326 HOH B O   1 
HETATM 6353 O  O   . HOH J 4 .   ? 1.690  59.144 59.606  1.00 13.40 ? 327 HOH B O   1 
HETATM 6354 O  O   . HOH J 4 .   ? 11.356 58.821 57.136  1.00 11.02 ? 328 HOH B O   1 
HETATM 6355 O  O   . HOH J 4 .   ? 12.636 50.220 49.155  1.00 9.37  ? 329 HOH B O   1 
HETATM 6356 O  O   . HOH J 4 .   ? 19.261 48.220 29.917  1.00 10.99 ? 330 HOH B O   1 
HETATM 6357 O  O   . HOH J 4 .   ? 23.011 73.238 30.628  1.00 9.98  ? 331 HOH B O   1 
HETATM 6358 O  O   . HOH J 4 .   ? 10.159 52.263 58.265  1.00 10.60 ? 332 HOH B O   1 
HETATM 6359 O  O   . HOH J 4 .   ? 13.039 55.709 56.695  1.00 10.84 ? 333 HOH B O   1 
HETATM 6360 O  O   . HOH J 4 .   ? 29.060 68.994 41.916  1.00 23.29 ? 334 HOH B O   1 
HETATM 6361 O  O   . HOH J 4 .   ? 32.297 47.596 30.195  1.00 14.47 ? 335 HOH B O   1 
HETATM 6362 O  O   . HOH J 4 .   ? 7.285  67.155 23.432  1.00 14.33 ? 336 HOH B O   1 
HETATM 6363 O  O   . HOH J 4 .   ? 26.873 48.743 27.600  1.00 10.27 ? 337 HOH B O   1 
HETATM 6364 O  O   . HOH J 4 .   ? 0.383  45.439 35.834  1.00 10.96 ? 338 HOH B O   1 
HETATM 6365 O  O   . HOH J 4 .   ? 16.527 61.928 63.938  1.00 17.91 ? 339 HOH B O   1 
HETATM 6366 O  O   . HOH J 4 .   ? 7.056  65.928 37.488  1.00 15.19 ? 340 HOH B O   1 
HETATM 6367 O  O   . HOH J 4 .   ? 8.300  64.418 30.465  1.00 10.59 ? 341 HOH B O   1 
HETATM 6368 O  O   . HOH J 4 .   ? 16.913 65.698 61.089  1.00 22.13 ? 342 HOH B O   1 
HETATM 6369 O  O   . HOH J 4 .   ? -3.275 59.416 53.932  1.00 13.61 ? 343 HOH B O   1 
HETATM 6370 O  O   . HOH J 4 .   ? 20.699 50.973 57.339  1.00 11.95 ? 344 HOH B O   1 
HETATM 6371 O  O   . HOH J 4 .   ? 13.014 64.401 18.134  1.00 12.01 ? 345 HOH B O   1 
HETATM 6372 O  O   . HOH J 4 .   ? 26.836 45.350 27.955  1.00 13.71 ? 346 HOH B O   1 
HETATM 6373 O  O   . HOH J 4 .   ? 6.978  66.033 20.935  1.00 14.95 ? 347 HOH B O   1 
HETATM 6374 O  O   . HOH J 4 .   ? 3.737  59.631 46.725  1.00 16.22 ? 348 HOH B O   1 
HETATM 6375 O  O   . HOH J 4 .   ? 6.789  58.939 61.644  1.00 14.42 ? 349 HOH B O   1 
HETATM 6376 O  O   . HOH J 4 .   ? 27.439 40.778 34.215  1.00 12.70 ? 350 HOH B O   1 
HETATM 6377 O  O   . HOH J 4 .   ? 22.473 64.937 50.317  1.00 17.98 ? 351 HOH B O   1 
HETATM 6378 O  O   . HOH J 4 .   ? 19.774 60.774 48.959  1.00 17.24 ? 352 HOH B O   1 
HETATM 6379 O  O   . HOH J 4 .   ? 35.084 52.306 35.030  1.00 15.78 ? 353 HOH B O   1 
HETATM 6380 O  O   . HOH J 4 .   ? 0.354  48.463 41.270  1.00 12.85 ? 354 HOH B O   1 
HETATM 6381 O  O   . HOH J 4 .   ? 6.515  61.773 35.206  1.00 12.73 ? 355 HOH B O   1 
HETATM 6382 O  O   . HOH J 4 .   ? 20.878 78.527 25.194  1.00 22.26 ? 356 HOH B O   1 
HETATM 6383 O  O   . HOH J 4 .   ? 4.975  59.846 36.625  1.00 12.97 ? 357 HOH B O   1 
HETATM 6384 O  O   . HOH J 4 .   ? 14.003 75.815 24.750  1.00 16.44 ? 358 HOH B O   1 
HETATM 6385 O  O   . HOH J 4 .   ? 15.692 59.784 51.920  1.00 11.89 ? 359 HOH B O   1 
HETATM 6386 O  O   . HOH J 4 .   ? 0.000  51.286 32.392  0.50 7.16  ? 360 HOH B O   1 
HETATM 6387 O  O   . HOH J 4 .   ? 29.494 49.023 26.580  1.00 15.97 ? 361 HOH B O   1 
HETATM 6388 O  O   . HOH J 4 .   ? 5.586  71.525 27.458  1.00 15.58 ? 362 HOH B O   1 
HETATM 6389 O  O   . HOH J 4 .   ? 16.692 55.141 65.847  1.00 18.61 ? 363 HOH B O   1 
HETATM 6390 O  O   . HOH J 4 .   ? 3.794  61.575 15.447  1.00 15.96 ? 364 HOH B O   1 
HETATM 6391 O  O   . HOH J 4 .   ? 8.948  76.089 31.574  1.00 17.26 ? 365 HOH B O   1 
HETATM 6392 O  O   . HOH J 4 .   ? 15.123 54.012 30.542  1.00 14.44 ? 366 HOH B O   1 
HETATM 6393 O  O   . HOH J 4 .   ? 4.876  60.861 12.854  1.00 16.02 ? 367 HOH B O   1 
HETATM 6394 O  O   . HOH J 4 .   ? 33.261 66.570 28.271  1.00 12.28 ? 368 HOH B O   1 
HETATM 6395 O  O   . HOH J 4 .   ? 9.632  76.230 25.082  1.00 15.33 ? 369 HOH B O   1 
HETATM 6396 O  O   . HOH J 4 .   ? 35.332 63.821 35.435  1.00 17.63 ? 370 HOH B O   1 
HETATM 6397 O  O   . HOH J 4 .   ? 26.763 67.545 25.992  1.00 12.63 ? 371 HOH B O   1 
HETATM 6398 O  O   . HOH J 4 .   ? 8.123  70.171 20.368  1.00 18.15 ? 372 HOH B O   1 
HETATM 6399 O  O   . HOH J 4 .   ? 5.296  69.066 28.914  1.00 19.35 ? 373 HOH B O   1 
HETATM 6400 O  O   . HOH J 4 .   ? 0.930  46.148 24.422  1.00 12.00 ? 374 HOH B O   1 
HETATM 6401 O  O   . HOH J 4 .   ? 22.214 42.886 33.804  1.00 13.12 ? 375 HOH B O   1 
HETATM 6402 O  O   . HOH J 4 .   ? 33.639 66.705 25.203  1.00 15.23 ? 376 HOH B O   1 
HETATM 6403 O  O   . HOH J 4 .   ? 20.887 40.472 37.283  1.00 21.54 ? 377 HOH B O   1 
HETATM 6404 O  O   . HOH J 4 .   ? 26.081 47.238 62.634  1.00 17.26 ? 378 HOH B O   1 
HETATM 6405 O  O   . HOH J 4 .   ? 5.026  67.319 25.026  1.00 20.89 ? 379 HOH B O   1 
HETATM 6406 O  O   . HOH J 4 .   ? 30.737 67.623 31.228  1.00 13.18 ? 380 HOH B O   1 
HETATM 6407 O  O   . HOH J 4 .   ? -0.489 64.827 49.104  1.00 13.79 ? 381 HOH B O   1 
HETATM 6408 O  O   . HOH J 4 .   ? 5.658  67.722 53.028  1.00 19.29 ? 382 HOH B O   1 
HETATM 6409 O  O   . HOH J 4 .   ? 9.798  55.037 63.662  1.00 21.69 ? 383 HOH B O   1 
HETATM 6410 O  O   . HOH J 4 .   ? 30.095 66.677 19.444  1.00 17.61 ? 384 HOH B O   1 
HETATM 6411 O  O   . HOH J 4 .   ? 5.035  60.431 22.865  1.00 17.25 ? 385 HOH B O   1 
HETATM 6412 O  O   . HOH J 4 .   ? 0.101  52.652 44.578  1.00 15.23 ? 386 HOH B O   1 
HETATM 6413 O  O   . HOH J 4 .   ? 19.374 68.665 16.091  1.00 17.43 ? 387 HOH B O   1 
HETATM 6414 O  O   . HOH J 4 .   ? 31.346 51.103 26.947  1.00 20.28 ? 388 HOH B O   1 
HETATM 6415 O  O   . HOH J 4 .   ? 20.283 78.624 32.356  1.00 19.61 ? 389 HOH B O   1 
HETATM 6416 O  O   . HOH J 4 .   ? 27.488 48.048 49.783  1.00 21.85 ? 390 HOH B O   1 
HETATM 6417 O  O   . HOH J 4 .   ? 14.734 81.022 36.599  1.00 31.51 ? 391 HOH B O   1 
HETATM 6418 O  O   . HOH J 4 .   ? 29.795 49.586 44.973  1.00 19.48 ? 392 HOH B O   1 
HETATM 6419 O  O   . HOH J 4 .   ? 14.170 62.021 62.443  1.00 27.03 ? 393 HOH B O   1 
HETATM 6420 O  O   . HOH J 4 .   ? 1.307  66.111 58.062  1.00 18.86 ? 394 HOH B O   1 
HETATM 6421 O  O   . HOH J 4 .   ? 20.960 67.499 13.995  1.00 15.01 ? 395 HOH B O   1 
HETATM 6422 O  O   . HOH J 4 .   ? 14.759 66.635 12.482  1.00 20.49 ? 396 HOH B O   1 
HETATM 6423 O  O   . HOH J 4 .   ? 11.724 75.343 41.892  1.00 19.75 ? 397 HOH B O   1 
HETATM 6424 O  O   . HOH J 4 .   ? 14.674 73.708 47.948  1.00 21.09 ? 398 HOH B O   1 
HETATM 6425 O  O   . HOH J 4 .   ? 33.155 49.833 28.791  1.00 22.67 ? 399 HOH B O   1 
HETATM 6426 O  O   . HOH J 4 .   ? 16.271 58.550 47.853  1.00 14.79 ? 400 HOH B O   1 
HETATM 6427 O  O   . HOH J 4 .   ? 27.503 42.491 28.863  1.00 19.16 ? 401 HOH B O   1 
HETATM 6428 O  O   . HOH J 4 .   ? 6.110  66.972 58.876  1.00 18.84 ? 402 HOH B O   1 
HETATM 6429 O  O   . HOH J 4 .   ? 16.283 72.451 15.599  1.00 24.02 ? 403 HOH B O   1 
HETATM 6430 O  O   . HOH J 4 .   ? 6.668  66.500 40.181  1.00 22.37 ? 404 HOH B O   1 
HETATM 6431 O  O   . HOH J 4 .   ? 20.130 67.985 11.437  1.00 21.43 ? 405 HOH B O   1 
HETATM 6432 O  O   . HOH J 4 .   ? 5.268  57.121 35.726  1.00 16.27 ? 406 HOH B O   1 
HETATM 6433 O  O   . HOH J 4 .   ? 30.957 52.616 49.863  1.00 27.06 ? 407 HOH B O   1 
HETATM 6434 O  O   . HOH J 4 .   ? 6.390  63.179 9.761   1.00 16.83 ? 408 HOH B O   1 
HETATM 6435 O  O   . HOH J 4 .   ? 4.374  65.011 21.450  1.00 26.07 ? 409 HOH B O   1 
HETATM 6436 O  O   . HOH J 4 .   ? 26.654 56.648 50.169  1.00 19.17 ? 410 HOH B O   1 
HETATM 6437 O  O   . HOH J 4 .   ? -2.248 56.130 50.088  1.00 21.30 ? 411 HOH B O   1 
HETATM 6438 O  O   . HOH J 4 .   ? 28.597 75.879 38.407  1.00 16.98 ? 412 HOH B O   1 
HETATM 6439 O  O   . HOH J 4 .   ? 28.836 44.476 40.602  1.00 24.71 ? 413 HOH B O   1 
HETATM 6440 O  O   . HOH J 4 .   ? 22.297 77.726 38.160  1.00 19.44 ? 414 HOH B O   1 
HETATM 6441 O  O   . HOH J 4 .   ? 17.686 70.148 14.546  1.00 24.36 ? 415 HOH B O   1 
HETATM 6442 O  O   . HOH J 4 .   ? 11.441 61.520 58.095  1.00 20.32 ? 416 HOH B O   1 
HETATM 6443 O  O   . HOH J 4 .   ? 13.930 55.312 66.319  1.00 24.04 ? 417 HOH B O   1 
HETATM 6444 O  O   . HOH J 4 .   ? 34.669 54.510 37.599  1.00 18.22 ? 418 HOH B O   1 
HETATM 6445 O  O   . HOH J 4 .   ? 14.510 60.691 60.015  1.00 21.21 ? 419 HOH B O   1 
HETATM 6446 O  O   . HOH J 4 .   ? 19.897 48.486 62.135  1.00 18.49 ? 420 HOH B O   1 
HETATM 6447 O  O   . HOH J 4 .   ? 8.036  75.629 19.302  1.00 23.42 ? 421 HOH B O   1 
HETATM 6448 O  O   . HOH J 4 .   ? 7.110  59.696 11.156  1.00 17.67 ? 422 HOH B O   1 
HETATM 6449 O  O   . HOH J 4 .   ? 14.095 76.579 30.108  1.00 20.20 ? 423 HOH B O   1 
HETATM 6450 O  O   . HOH J 4 .   ? 33.152 70.357 26.767  1.00 22.25 ? 424 HOH B O   1 
HETATM 6451 O  O   . HOH J 4 .   ? 5.774  63.727 30.773  1.00 20.74 ? 425 HOH B O   1 
HETATM 6452 O  O   . HOH J 4 .   ? 1.557  52.131 27.871  1.00 19.50 ? 426 HOH B O   1 
HETATM 6453 O  O   . HOH J 4 .   ? 22.829 74.864 47.069  1.00 30.94 ? 427 HOH B O   1 
HETATM 6454 O  O   . HOH J 4 .   ? 28.489 44.708 60.262  1.00 29.89 ? 428 HOH B O   1 
HETATM 6455 O  O   . HOH J 4 .   ? 27.200 66.448 28.518  1.00 17.17 ? 429 HOH B O   1 
HETATM 6456 O  O   . HOH J 4 .   ? -0.000 47.083 32.392  0.50 17.66 ? 430 HOH B O   1 
HETATM 6457 O  O   . HOH J 4 .   ? 34.085 62.110 22.804  1.00 22.89 ? 431 HOH B O   1 
HETATM 6458 O  O   . HOH J 4 .   ? -2.793 64.999 52.934  1.00 18.79 ? 432 HOH B O   1 
HETATM 6459 O  O   . HOH J 4 .   ? 23.689 76.887 42.168  1.00 20.20 ? 433 HOH B O   1 
HETATM 6460 O  O   . HOH J 4 .   ? 29.307 44.641 49.065  1.00 30.00 ? 434 HOH B O   1 
HETATM 6461 O  O   . HOH J 4 .   ? 1.254  58.868 45.484  1.00 16.34 ? 435 HOH B O   1 
HETATM 6462 O  O   . HOH J 4 .   ? 14.951 64.790 59.070  1.00 21.86 ? 436 HOH B O   1 
HETATM 6463 O  O   . HOH J 4 .   ? 11.900 43.241 32.067  1.00 21.51 ? 437 HOH B O   1 
HETATM 6464 O  O   . HOH J 4 .   ? 18.459 65.535 8.249   1.00 18.05 ? 438 HOH B O   1 
HETATM 6465 O  O   . HOH J 4 .   ? 3.935  65.461 40.689  1.00 21.39 ? 439 HOH B O   1 
HETATM 6466 O  O   . HOH J 4 .   ? 27.532 58.261 17.999  1.00 26.79 ? 440 HOH B O   1 
HETATM 6467 O  O   . HOH J 4 .   ? 12.217 64.520 48.812  1.00 28.02 ? 441 HOH B O   1 
HETATM 6468 O  O   . HOH J 4 .   ? 18.543 51.433 63.945  1.00 22.30 ? 442 HOH B O   1 
HETATM 6469 O  O   . HOH J 4 .   ? 5.981  56.445 28.215  1.00 18.85 ? 443 HOH B O   1 
HETATM 6470 O  O   . HOH J 4 .   ? 27.385 41.985 40.458  1.00 19.78 ? 444 HOH B O   1 
HETATM 6471 O  O   . HOH J 4 .   ? 10.618 63.467 18.715  1.00 16.48 ? 445 HOH B O   1 
HETATM 6472 O  O   . HOH J 4 .   ? 10.381 65.923 46.484  1.00 24.70 ? 446 HOH B O   1 
HETATM 6473 O  O   . HOH J 4 .   ? 4.067  66.658 45.105  1.00 20.10 ? 447 HOH B O   1 
HETATM 6474 O  O   . HOH J 4 .   ? 26.554 68.765 58.243  1.00 32.64 ? 448 HOH B O   1 
HETATM 6475 O  O   . HOH J 4 .   ? 19.366 74.940 18.885  1.00 21.50 ? 449 HOH B O   1 
HETATM 6476 O  O   . HOH J 4 .   ? 14.462 66.843 47.592  1.00 20.16 ? 450 HOH B O   1 
HETATM 6477 O  O   . HOH J 4 .   ? 22.379 63.942 47.792  1.00 21.96 ? 451 HOH B O   1 
HETATM 6478 O  O   . HOH J 4 .   ? 8.070  73.668 37.766  1.00 20.36 ? 452 HOH B O   1 
HETATM 6479 O  O   . HOH J 4 .   ? 17.012 37.502 42.228  1.00 20.83 ? 453 HOH B O   1 
HETATM 6480 O  O   . HOH J 4 .   ? 10.962 78.026 32.752  1.00 22.95 ? 454 HOH B O   1 
HETATM 6481 O  O   . HOH J 4 .   ? 4.427  54.175 24.993  1.00 22.06 ? 455 HOH B O   1 
HETATM 6482 O  O   . HOH J 4 .   ? 37.141 59.933 33.506  1.00 25.08 ? 456 HOH B O   1 
HETATM 6483 O  O   . HOH J 4 .   ? 32.469 61.870 20.515  1.00 31.87 ? 457 HOH B O   1 
HETATM 6484 O  O   . HOH J 4 .   ? 28.804 52.239 53.553  1.00 21.17 ? 458 HOH B O   1 
HETATM 6485 O  O   . HOH J 4 .   ? 13.472 79.216 38.503  1.00 24.55 ? 459 HOH B O   1 
HETATM 6486 O  O   . HOH J 4 .   ? 28.491 53.286 63.906  1.00 24.06 ? 460 HOH B O   1 
HETATM 6487 O  O   . HOH J 4 .   ? 33.363 49.223 59.318  1.00 25.68 ? 461 HOH B O   1 
HETATM 6488 O  O   . HOH J 4 .   ? 6.738  75.326 33.371  1.00 26.06 ? 462 HOH B O   1 
HETATM 6489 O  O   . HOH J 4 .   ? 25.277 71.138 57.382  1.00 30.26 ? 463 HOH B O   1 
HETATM 6490 O  O   . HOH J 4 .   ? 13.400 45.059 30.952  1.00 22.15 ? 464 HOH B O   1 
HETATM 6491 O  O   . HOH J 4 .   ? 5.639  56.882 25.518  1.00 24.92 ? 465 HOH B O   1 
HETATM 6492 O  O   . HOH J 4 .   ? 15.558 62.048 66.691  1.00 26.81 ? 466 HOH B O   1 
HETATM 6493 O  O   . HOH J 4 .   ? 14.255 64.343 50.903  1.00 23.90 ? 467 HOH B O   1 
HETATM 6494 O  O   . HOH J 4 .   ? 23.375 76.021 17.961  1.00 25.55 ? 468 HOH B O   1 
HETATM 6495 O  O   . HOH J 4 .   ? 3.099  64.042 16.424  1.00 22.77 ? 469 HOH B O   1 
HETATM 6496 O  O   . HOH J 4 .   ? 11.539 77.410 37.399  1.00 23.89 ? 470 HOH B O   1 
HETATM 6497 O  O   . HOH J 4 .   ? 20.749 79.199 34.993  1.00 23.49 ? 471 HOH B O   1 
HETATM 6498 O  O   . HOH J 4 .   ? 3.192  55.670 36.998  1.00 25.71 ? 472 HOH B O   1 
HETATM 6499 O  O   . HOH J 4 .   ? 35.913 58.223 40.354  1.00 27.26 ? 473 HOH B O   1 
HETATM 6500 O  O   . HOH J 4 .   ? 20.936 65.478 67.212  1.00 25.13 ? 474 HOH B O   1 
HETATM 6501 O  O   . HOH J 4 .   ? 1.170  62.301 39.424  1.00 27.28 ? 475 HOH B O   1 
HETATM 6502 O  O   . HOH J 4 .   ? 34.756 45.311 59.073  1.00 23.06 ? 476 HOH B O   1 
HETATM 6503 O  O   . HOH J 4 .   ? 14.121 62.443 57.701  1.00 20.30 ? 477 HOH B O   1 
HETATM 6504 O  O   . HOH J 4 .   ? 15.723 76.035 20.425  1.00 28.16 ? 478 HOH B O   1 
HETATM 6505 O  O   . HOH J 4 .   ? 21.996 54.992 58.673  1.00 20.85 ? 479 HOH B O   1 
HETATM 6506 O  O   . HOH J 4 .   ? 12.170 43.784 28.318  1.00 25.45 ? 480 HOH B O   1 
HETATM 6507 O  O   . HOH J 4 .   ? 1.229  59.889 19.127  1.00 21.88 ? 481 HOH B O   1 
HETATM 6508 O  O   . HOH J 4 .   ? 36.678 58.782 24.835  1.00 27.69 ? 482 HOH B O   1 
HETATM 6509 O  O   . HOH J 4 .   ? 1.329  67.144 53.426  1.00 25.53 ? 483 HOH B O   1 
HETATM 6510 O  O   . HOH J 4 .   ? 27.042 78.190 39.480  1.00 19.76 ? 484 HOH B O   1 
HETATM 6511 O  O   . HOH J 4 .   ? 2.154  55.020 44.388  1.00 18.92 ? 485 HOH B O   1 
HETATM 6512 O  O   . HOH J 4 .   ? 36.882 43.513 58.067  1.00 22.36 ? 486 HOH B O   1 
HETATM 6513 O  O   . HOH J 4 .   ? 30.267 71.513 25.893  1.00 25.63 ? 487 HOH B O   1 
HETATM 6514 O  O   . HOH J 4 .   ? 10.618 68.884 16.838  1.00 28.90 ? 488 HOH B O   1 
HETATM 6515 O  O   . HOH J 4 .   ? 1.579  58.660 23.785  1.00 30.30 ? 489 HOH B O   1 
HETATM 6516 O  O   . HOH J 4 .   ? 12.613 77.438 18.764  1.00 30.84 ? 490 HOH B O   1 
HETATM 6517 O  O   . HOH J 4 .   ? 6.344  71.666 35.605  1.00 27.93 ? 491 HOH B O   1 
HETATM 6518 O  O   . HOH J 4 .   ? 23.040 69.309 14.417  1.00 28.02 ? 492 HOH B O   1 
HETATM 6519 O  O   . HOH J 4 .   ? 2.304  56.545 46.694  1.00 25.72 ? 493 HOH B O   1 
HETATM 6520 O  O   . HOH J 4 .   ? 7.605  58.780 25.016  1.00 17.79 ? 494 HOH B O   1 
HETATM 6521 O  O   . HOH J 4 .   ? 18.007 56.891 67.467  1.00 29.64 ? 495 HOH B O   1 
HETATM 6522 O  O   . HOH J 4 .   ? 30.385 46.745 28.319  1.00 20.90 ? 496 HOH B O   1 
HETATM 6523 O  O   . HOH K 4 .   ? 17.487 17.941 39.204  1.00 8.50  ? 701 HOH C O   1 
HETATM 6524 O  O   . HOH K 4 .   ? 8.544  25.982 36.358  1.00 5.33  ? 702 HOH C O   1 
HETATM 6525 O  O   . HOH K 4 .   ? 8.917  22.540 31.866  1.00 7.11  ? 703 HOH C O   1 
HETATM 6526 O  O   . HOH K 4 .   ? 11.511 16.971 35.387  1.00 6.59  ? 704 HOH C O   1 
HETATM 6527 O  O   . HOH K 4 .   ? 10.203 30.709 51.965  1.00 9.29  ? 705 HOH C O   1 
HETATM 6528 O  O   . HOH K 4 .   ? 7.563  27.989 47.740  1.00 11.40 ? 706 HOH C O   1 
HETATM 6529 O  O   . HOH K 4 .   ? 9.173  10.171 33.845  1.00 8.13  ? 707 HOH C O   1 
HETATM 6530 O  O   . HOH K 4 .   ? 9.022  30.550 33.441  1.00 8.56  ? 708 HOH C O   1 
HETATM 6531 O  O   . HOH K 4 .   ? 15.321 27.160 34.816  1.00 8.75  ? 709 HOH C O   1 
HETATM 6532 O  O   . HOH K 4 .   ? 17.879 20.679 29.806  1.00 7.73  ? 710 HOH C O   1 
HETATM 6533 O  O   . HOH K 4 .   ? 10.824 21.215 30.173  1.00 8.80  ? 711 HOH C O   1 
HETATM 6534 O  O   . HOH K 4 .   ? 0.545  7.695  38.745  1.00 10.36 ? 712 HOH C O   1 
HETATM 6535 O  O   . HOH K 4 .   ? 29.358 31.184 54.561  1.00 9.91  ? 713 HOH C O   1 
HETATM 6536 O  O   . HOH K 4 .   ? 12.949 16.144 37.559  1.00 10.55 ? 714 HOH C O   1 
HETATM 6537 O  O   . HOH K 4 .   ? 33.171 37.061 56.652  1.00 10.35 ? 715 HOH C O   1 
HETATM 6538 O  O   . HOH K 4 .   ? 22.256 28.866 39.256  1.00 9.21  ? 716 HOH C O   1 
HETATM 6539 O  O   . HOH K 4 .   ? 28.681 25.255 47.674  1.00 9.55  ? 717 HOH C O   1 
HETATM 6540 O  O   . HOH K 4 .   ? 26.736 37.507 27.055  1.00 13.07 ? 718 HOH C O   1 
HETATM 6541 O  O   . HOH K 4 .   ? 10.418 40.343 51.902  1.00 9.39  ? 719 HOH C O   1 
HETATM 6542 O  O   . HOH K 4 .   ? 4.107  6.557  32.433  1.00 10.67 ? 720 HOH C O   1 
HETATM 6543 O  O   . HOH K 4 .   ? 27.739 39.276 37.399  1.00 11.09 ? 721 HOH C O   1 
HETATM 6544 O  O   . HOH K 4 .   ? 17.165 29.296 63.919  1.00 19.37 ? 722 HOH C O   1 
HETATM 6545 O  O   . HOH K 4 .   ? 3.409  36.479 38.938  1.00 6.29  ? 723 HOH C O   1 
HETATM 6546 O  O   . HOH K 4 .   ? -1.434 13.263 42.369  1.00 11.04 ? 724 HOH C O   1 
HETATM 6547 O  O   . HOH K 4 .   ? 25.161 24.918 57.603  1.00 11.34 ? 725 HOH C O   1 
HETATM 6548 O  O   . HOH K 4 .   ? 7.248  12.539 27.832  1.00 9.02  ? 726 HOH C O   1 
HETATM 6549 O  O   . HOH K 4 .   ? -1.601 8.554  37.163  1.00 8.87  ? 727 HOH C O   1 
HETATM 6550 O  O   . HOH K 4 .   ? 12.977 29.391 64.575  1.00 15.54 ? 728 HOH C O   1 
HETATM 6551 O  O   . HOH K 4 .   ? 35.062 30.523 35.701  1.00 14.48 ? 729 HOH C O   1 
HETATM 6552 O  O   . HOH K 4 .   ? 17.572 13.109 25.811  1.00 12.25 ? 730 HOH C O   1 
HETATM 6553 O  O   . HOH K 4 .   ? 32.439 29.311 57.349  1.00 13.59 ? 731 HOH C O   1 
HETATM 6554 O  O   . HOH K 4 .   ? 15.193 17.875 37.518  1.00 11.75 ? 732 HOH C O   1 
HETATM 6555 O  O   . HOH K 4 .   ? 36.163 31.928 53.157  1.00 10.92 ? 733 HOH C O   1 
HETATM 6556 O  O   . HOH K 4 .   ? 13.726 2.274  32.503  1.00 13.45 ? 734 HOH C O   1 
HETATM 6557 O  O   . HOH K 4 .   ? 35.659 29.363 51.908  1.00 13.54 ? 735 HOH C O   1 
HETATM 6558 O  O   . HOH K 4 .   ? 5.768  27.890 45.637  1.00 12.22 ? 736 HOH C O   1 
HETATM 6559 O  O   . HOH K 4 .   ? 14.511 20.558 36.841  1.00 12.12 ? 737 HOH C O   1 
HETATM 6560 O  O   . HOH K 4 .   ? 14.247 13.869 36.640  1.00 8.13  ? 738 HOH C O   1 
HETATM 6561 O  O   . HOH K 4 .   ? 11.826 36.599 61.902  1.00 16.92 ? 739 HOH C O   1 
HETATM 6562 O  O   . HOH K 4 .   ? 7.810  30.034 57.198  1.00 17.84 ? 740 HOH C O   1 
HETATM 6563 O  O   . HOH K 4 .   ? 22.274 31.472 40.417  1.00 9.17  ? 741 HOH C O   1 
HETATM 6564 O  O   . HOH K 4 .   ? -6.605 10.421 38.498  1.00 11.03 ? 742 HOH C O   1 
HETATM 6565 O  O   . HOH K 4 .   ? 19.952 38.252 36.891  1.00 12.74 ? 743 HOH C O   1 
HETATM 6566 O  O   . HOH K 4 .   ? 27.968 2.734  28.853  1.00 15.20 ? 744 HOH C O   1 
HETATM 6567 O  O   . HOH K 4 .   ? 16.723 41.016 57.264  1.00 12.08 ? 745 HOH C O   1 
HETATM 6568 O  O   . HOH K 4 .   ? 27.701 41.189 31.157  1.00 15.58 ? 746 HOH C O   1 
HETATM 6569 O  O   . HOH K 4 .   ? 16.224 35.096 42.050  1.00 14.36 ? 747 HOH C O   1 
HETATM 6570 O  O   . HOH K 4 .   ? -4.793 13.777 37.896  1.00 12.48 ? 748 HOH C O   1 
HETATM 6571 O  O   . HOH K 4 .   ? 10.586 11.863 31.170  1.00 11.29 ? 749 HOH C O   1 
HETATM 6572 O  O   . HOH K 4 .   ? 0.647  25.102 31.139  1.00 14.86 ? 750 HOH C O   1 
HETATM 6573 O  O   . HOH K 4 .   ? 27.585 30.278 27.121  1.00 19.93 ? 751 HOH C O   1 
HETATM 6574 O  O   . HOH K 4 .   ? 1.627  42.884 33.873  1.00 15.39 ? 752 HOH C O   1 
HETATM 6575 O  O   . HOH K 4 .   ? 18.443 42.964 58.246  1.00 9.93  ? 753 HOH C O   1 
HETATM 6576 O  O   . HOH K 4 .   ? 2.360  45.592 40.228  1.00 11.11 ? 754 HOH C O   1 
HETATM 6577 O  O   . HOH K 4 .   ? 3.092  19.318 40.581  1.00 13.71 ? 755 HOH C O   1 
HETATM 6578 O  O   . HOH K 4 .   ? -1.081 15.007 44.543  1.00 14.77 ? 756 HOH C O   1 
HETATM 6579 O  O   . HOH K 4 .   ? 8.415  30.017 59.872  1.00 13.36 ? 757 HOH C O   1 
HETATM 6580 O  O   . HOH K 4 .   ? 8.434  46.867 41.968  1.00 8.10  ? 758 HOH C O   1 
HETATM 6581 O  O   . HOH K 4 .   ? 32.636 37.286 34.381  1.00 14.42 ? 759 HOH C O   1 
HETATM 6582 O  O   . HOH K 4 .   ? 30.529 39.825 37.796  1.00 15.38 ? 760 HOH C O   1 
HETATM 6583 O  O   . HOH K 4 .   ? -7.720 11.060 41.025  1.00 15.75 ? 761 HOH C O   1 
HETATM 6584 O  O   . HOH K 4 .   ? 21.921 10.268 18.945  1.00 18.94 ? 762 HOH C O   1 
HETATM 6585 O  O   . HOH K 4 .   ? 31.821 39.218 57.933  1.00 12.97 ? 763 HOH C O   1 
HETATM 6586 O  O   . HOH K 4 .   ? 10.324 35.552 57.934  1.00 13.13 ? 764 HOH C O   1 
HETATM 6587 O  O   . HOH K 4 .   ? 11.216 23.974 61.487  1.00 19.11 ? 765 HOH C O   1 
HETATM 6588 O  O   . HOH K 4 .   ? 5.927  29.989 43.657  1.00 13.47 ? 766 HOH C O   1 
HETATM 6589 O  O   . HOH K 4 .   ? 22.634 20.781 61.656  1.00 16.64 ? 767 HOH C O   1 
HETATM 6590 O  O   . HOH K 4 .   ? 12.951 4.023  25.732  1.00 16.44 ? 768 HOH C O   1 
HETATM 6591 O  O   . HOH K 4 .   ? 30.604 25.109 49.691  1.00 19.58 ? 769 HOH C O   1 
HETATM 6592 O  O   . HOH K 4 .   ? 19.359 44.404 61.926  1.00 18.24 ? 770 HOH C O   1 
HETATM 6593 O  O   . HOH K 4 .   ? 14.770 10.445 50.579  1.00 20.08 ? 771 HOH C O   1 
HETATM 6594 O  O   . HOH K 4 .   ? 16.569 15.609 36.541  1.00 13.97 ? 772 HOH C O   1 
HETATM 6595 O  O   . HOH K 4 .   ? 5.814  8.139  34.370  1.00 12.48 ? 773 HOH C O   1 
HETATM 6596 O  O   . HOH K 4 .   ? 26.494 0.419  28.707  1.00 12.88 ? 774 HOH C O   1 
HETATM 6597 O  O   . HOH K 4 .   ? 4.403  17.244 47.519  1.00 17.70 ? 775 HOH C O   1 
HETATM 6598 O  O   . HOH K 4 .   ? -0.366 6.530  41.069  1.00 19.31 ? 776 HOH C O   1 
HETATM 6599 O  O   . HOH K 4 .   ? 7.976  23.866 50.134  1.00 15.07 ? 777 HOH C O   1 
HETATM 6600 O  O   . HOH K 4 .   ? 18.842 15.595 38.466  1.00 14.78 ? 778 HOH C O   1 
HETATM 6601 O  O   . HOH K 4 .   ? -6.010 12.868 42.257  1.00 19.23 ? 779 HOH C O   1 
HETATM 6602 O  O   . HOH K 4 .   ? 12.401 34.827 67.158  1.00 20.15 ? 780 HOH C O   1 
HETATM 6603 O  O   . HOH K 4 .   ? 29.887 38.692 27.809  1.00 19.11 ? 781 HOH C O   1 
HETATM 6604 O  O   . HOH K 4 .   ? 12.637 15.121 55.494  1.00 18.36 ? 782 HOH C O   1 
HETATM 6605 O  O   . HOH K 4 .   ? 24.294 38.253 28.360  1.00 22.81 ? 783 HOH C O   1 
HETATM 6606 O  O   . HOH K 4 .   ? 36.549 36.251 50.493  1.00 21.48 ? 784 HOH C O   1 
HETATM 6607 O  O   . HOH K 4 .   ? 11.526 49.955 57.604  1.00 15.72 ? 785 HOH C O   1 
HETATM 6608 O  O   . HOH K 4 .   ? 1.700  17.693 47.226  1.00 19.51 ? 786 HOH C O   1 
HETATM 6609 O  O   . HOH K 4 .   ? 30.849 39.480 34.765  1.00 21.15 ? 787 HOH C O   1 
HETATM 6610 O  O   . HOH K 4 .   ? 23.811 16.300 57.830  1.00 20.36 ? 788 HOH C O   1 
HETATM 6611 O  O   . HOH K 4 .   ? 32.430 26.423 57.199  1.00 19.99 ? 789 HOH C O   1 
HETATM 6612 O  O   . HOH K 4 .   ? -0.325 29.909 34.194  1.00 12.67 ? 790 HOH C O   1 
HETATM 6613 O  O   . HOH K 4 .   ? 29.410 14.021 31.318  1.00 21.55 ? 791 HOH C O   1 
HETATM 6614 O  O   . HOH K 4 .   ? 26.385 15.225 27.360  1.00 17.78 ? 792 HOH C O   1 
HETATM 6615 O  O   . HOH K 4 .   ? 0.640  17.236 44.732  1.00 15.78 ? 793 HOH C O   1 
HETATM 6616 O  O   . HOH K 4 .   ? -3.557 11.737 43.136  1.00 19.99 ? 794 HOH C O   1 
HETATM 6617 O  O   . HOH K 4 .   ? 10.472 38.282 58.191  1.00 14.89 ? 795 HOH C O   1 
HETATM 6618 O  O   . HOH K 4 .   ? 6.513  40.740 46.379  1.00 20.13 ? 796 HOH C O   1 
HETATM 6619 O  O   . HOH K 4 .   ? 4.895  9.738  44.207  1.00 17.93 ? 797 HOH C O   1 
HETATM 6620 O  O   . HOH K 4 .   ? 24.063 40.068 61.120  1.00 17.20 ? 798 HOH C O   1 
HETATM 6621 O  O   . HOH K 4 .   ? 4.439  5.043  40.757  1.00 19.53 ? 799 HOH C O   1 
HETATM 6622 O  O   . HOH K 4 .   ? 11.351 49.459 61.423  1.00 18.42 ? 800 HOH C O   1 
HETATM 6623 O  O   . HOH K 4 .   ? 21.767 14.685 41.320  1.00 21.46 ? 801 HOH C O   1 
HETATM 6624 O  O   . HOH K 4 .   ? 20.737 38.688 65.300  1.00 23.33 ? 802 HOH C O   1 
HETATM 6625 O  O   . HOH K 4 .   ? 23.560 48.644 62.429  1.00 18.13 ? 803 HOH C O   1 
HETATM 6626 O  O   . HOH K 4 .   ? 11.947 39.524 32.497  1.00 18.66 ? 804 HOH C O   1 
HETATM 6627 O  O   . HOH K 4 .   ? 15.862 10.362 21.342  1.00 17.99 ? 805 HOH C O   1 
HETATM 6628 O  O   . HOH K 4 .   ? 28.879 16.749 30.266  1.00 32.28 ? 806 HOH C O   1 
HETATM 6629 O  O   . HOH K 4 .   ? 25.253 3.490  39.964  1.00 24.54 ? 807 HOH C O   1 
HETATM 6630 O  O   . HOH K 4 .   ? 5.947  49.082 53.420  1.00 19.73 ? 808 HOH C O   1 
HETATM 6631 O  O   . HOH K 4 .   ? 34.160 37.936 32.094  1.00 20.45 ? 809 HOH C O   1 
HETATM 6632 O  O   . HOH K 4 .   ? 18.480 1.495  27.109  1.00 17.46 ? 810 HOH C O   1 
HETATM 6633 O  O   . HOH K 4 .   ? 25.177 44.486 62.799  1.00 19.02 ? 811 HOH C O   1 
HETATM 6634 O  O   . HOH K 4 .   ? 21.835 37.282 30.045  1.00 15.57 ? 812 HOH C O   1 
HETATM 6635 O  O   . HOH K 4 .   ? 15.445 -1.248 33.935  1.00 26.61 ? 813 HOH C O   1 
HETATM 6636 O  O   . HOH K 4 .   ? 25.012 16.166 33.443  1.00 19.05 ? 814 HOH C O   1 
HETATM 6637 O  O   . HOH K 4 .   ? 23.001 -0.089 26.157  1.00 19.01 ? 815 HOH C O   1 
HETATM 6638 O  O   . HOH K 4 .   ? 30.074 16.636 55.291  1.00 20.29 ? 816 HOH C O   1 
HETATM 6639 O  O   . HOH K 4 .   ? 15.157 35.649 44.956  1.00 21.11 ? 817 HOH C O   1 
HETATM 6640 O  O   . HOH K 4 .   ? 32.557 38.462 39.237  1.00 20.33 ? 818 HOH C O   1 
HETATM 6641 O  O   . HOH K 4 .   ? 16.359 24.361 62.196  1.00 28.61 ? 819 HOH C O   1 
HETATM 6642 O  O   . HOH K 4 .   ? 9.667  47.479 60.793  1.00 17.80 ? 820 HOH C O   1 
HETATM 6643 O  O   . HOH K 4 .   ? 24.414 5.954  23.151  1.00 15.26 ? 821 HOH C O   1 
HETATM 6644 O  O   . HOH K 4 .   ? 14.256 14.073 44.960  1.00 15.84 ? 822 HOH C O   1 
HETATM 6645 O  O   . HOH K 4 .   ? 12.117 7.629  36.294  1.00 19.58 ? 823 HOH C O   1 
HETATM 6646 O  O   . HOH K 4 .   ? 0.836  20.996 40.975  1.00 14.84 ? 824 HOH C O   1 
HETATM 6647 O  O   . HOH K 4 .   ? 22.033 41.023 62.996  1.00 17.43 ? 825 HOH C O   1 
HETATM 6648 O  O   . HOH K 4 .   ? 30.455 8.707  25.980  1.00 17.97 ? 826 HOH C O   1 
HETATM 6649 O  O   . HOH K 4 .   ? 15.671 7.018  23.362  1.00 29.18 ? 827 HOH C O   1 
HETATM 6650 O  O   . HOH K 4 .   ? -3.511 18.649 36.838  1.00 20.75 ? 828 HOH C O   1 
HETATM 6651 O  O   . HOH K 4 .   ? 23.286 7.772  18.843  1.00 28.96 ? 829 HOH C O   1 
HETATM 6652 O  O   . HOH K 4 .   ? 4.505  21.625 48.467  1.00 22.01 ? 830 HOH C O   1 
HETATM 6653 O  O   . HOH K 4 .   ? 28.387 23.847 29.214  1.00 14.81 ? 831 HOH C O   1 
HETATM 6654 O  O   . HOH K 4 .   ? 33.770 37.347 36.876  1.00 19.58 ? 832 HOH C O   1 
HETATM 6655 O  O   . HOH K 4 .   ? 34.537 27.452 36.410  1.00 17.29 ? 833 HOH C O   1 
HETATM 6656 O  O   . HOH K 4 .   ? 6.448  6.529  27.807  1.00 20.64 ? 834 HOH C O   1 
HETATM 6657 O  O   . HOH K 4 .   ? 21.716 11.977 40.921  1.00 20.64 ? 835 HOH C O   1 
HETATM 6658 O  O   . HOH K 4 .   ? 14.566 40.212 62.501  1.00 26.09 ? 836 HOH C O   1 
HETATM 6659 O  O   . HOH K 4 .   ? 10.025 3.817  26.015  1.00 24.20 ? 837 HOH C O   1 
HETATM 6660 O  O   . HOH K 4 .   ? 3.755  29.834 41.863  1.00 20.52 ? 838 HOH C O   1 
HETATM 6661 O  O   . HOH K 4 .   ? 7.649  36.850 46.733  1.00 20.64 ? 839 HOH C O   1 
HETATM 6662 O  O   . HOH K 4 .   ? 7.900  45.524 57.614  1.00 14.54 ? 840 HOH C O   1 
HETATM 6663 O  O   . HOH K 4 .   ? -1.172 19.427 38.935  1.00 23.68 ? 841 HOH C O   1 
HETATM 6664 O  O   . HOH K 4 .   ? 9.121  48.055 58.037  1.00 19.13 ? 842 HOH C O   1 
HETATM 6665 O  O   . HOH K 4 .   ? 32.326 20.703 53.813  1.00 24.71 ? 843 HOH C O   1 
HETATM 6666 O  O   . HOH K 4 .   ? 14.164 41.180 56.776  1.00 16.67 ? 844 HOH C O   1 
HETATM 6667 O  O   . HOH K 4 .   ? 30.551 23.755 53.021  1.00 21.30 ? 845 HOH C O   1 
HETATM 6668 O  O   . HOH K 4 .   ? 10.176 16.018 45.397  1.00 20.90 ? 846 HOH C O   1 
HETATM 6669 O  O   . HOH K 4 .   ? 4.691  43.371 54.759  1.00 27.71 ? 847 HOH C O   1 
HETATM 6670 O  O   . HOH K 4 .   ? 17.899 -2.555 32.992  1.00 20.91 ? 848 HOH C O   1 
HETATM 6671 O  O   . HOH K 4 .   ? 23.700 27.139 65.116  1.00 24.15 ? 849 HOH C O   1 
HETATM 6672 O  O   . HOH K 4 .   ? 0.420  10.094 44.385  1.00 20.72 ? 850 HOH C O   1 
HETATM 6673 O  O   . HOH K 4 .   ? 25.940 31.709 25.112  1.00 19.22 ? 851 HOH C O   1 
HETATM 6674 O  O   . HOH K 4 .   ? 23.707 14.165 18.231  1.00 23.51 ? 852 HOH C O   1 
HETATM 6675 O  O   . HOH K 4 .   ? 7.633  23.407 55.557  1.00 26.89 ? 853 HOH C O   1 
HETATM 6676 O  O   . HOH K 4 .   ? 3.966  46.835 54.123  1.00 30.91 ? 854 HOH C O   1 
HETATM 6677 O  O   . HOH K 4 .   ? 13.991 5.975  46.222  1.00 21.74 ? 855 HOH C O   1 
HETATM 6678 O  O   . HOH K 4 .   ? 31.938 28.357 60.400  1.00 23.17 ? 856 HOH C O   1 
HETATM 6679 O  O   . HOH K 4 .   ? 9.234  7.949  35.753  1.00 18.25 ? 857 HOH C O   1 
HETATM 6680 O  O   . HOH K 4 .   ? 12.666 42.511 34.742  1.00 23.39 ? 858 HOH C O   1 
HETATM 6681 O  O   . HOH K 4 .   ? 24.378 12.250 42.445  1.00 32.63 ? 859 HOH C O   1 
HETATM 6682 O  O   . HOH K 4 .   ? 22.332 8.079  50.535  1.00 25.56 ? 860 HOH C O   1 
HETATM 6683 O  O   . HOH K 4 .   ? 19.226 -4.219 28.854  1.00 27.20 ? 861 HOH C O   1 
HETATM 6684 O  O   . HOH K 4 .   ? 34.146 33.756 30.121  1.00 29.25 ? 862 HOH C O   1 
HETATM 6685 O  O   . HOH K 4 .   ? 32.698 41.348 50.501  1.00 26.93 ? 863 HOH C O   1 
HETATM 6686 O  O   . HOH K 4 .   ? 28.776 16.687 58.410  1.00 20.15 ? 864 HOH C O   1 
HETATM 6687 O  O   . HOH K 4 .   ? 14.952 39.575 59.608  1.00 19.56 ? 865 HOH C O   1 
HETATM 6688 O  O   . HOH K 4 .   ? 29.247 8.919  19.808  1.00 31.16 ? 866 HOH C O   1 
HETATM 6689 O  O   . HOH K 4 .   ? 12.075 39.701 56.368  1.00 20.36 ? 867 HOH C O   1 
HETATM 6690 O  O   . HOH K 4 .   ? 40.211 32.813 52.994  1.00 25.15 ? 868 HOH C O   1 
HETATM 6691 O  O   . HOH K 4 .   ? 30.608 15.944 46.436  1.00 23.61 ? 869 HOH C O   1 
HETATM 6692 O  O   . HOH K 4 .   ? 8.791  23.031 60.097  1.00 22.31 ? 870 HOH C O   1 
HETATM 6693 O  O   . HOH K 4 .   ? 25.699 42.577 60.883  1.00 24.54 ? 871 HOH C O   1 
HETATM 6694 O  O   . HOH K 4 .   ? 27.211 11.769 42.827  1.00 30.77 ? 872 HOH C O   1 
HETATM 6695 O  O   . HOH K 4 .   ? 4.125  5.618  29.776  1.00 25.94 ? 873 HOH C O   1 
HETATM 6696 O  O   . HOH K 4 .   ? 29.034 14.258 23.883  1.00 23.84 ? 874 HOH C O   1 
HETATM 6697 O  O   . HOH K 4 .   ? 7.771  38.540 57.466  1.00 24.77 ? 875 HOH C O   1 
HETATM 6698 O  O   . HOH K 4 .   ? 1.746  24.663 46.697  1.00 27.00 ? 876 HOH C O   1 
HETATM 6699 O  O   . HOH K 4 .   ? 3.153  19.674 37.934  1.00 20.54 ? 877 HOH C O   1 
HETATM 6700 O  O   . HOH K 4 .   ? 28.199 4.046  38.681  1.00 33.24 ? 878 HOH C O   1 
HETATM 6701 O  O   . HOH K 4 .   ? 17.150 34.329 68.286  1.00 32.16 ? 879 HOH C O   1 
HETATM 6702 O  O   . HOH K 4 .   ? 15.803 0.203  40.299  1.00 31.24 ? 880 HOH C O   1 
HETATM 6703 O  O   . HOH K 4 .   ? 25.420 20.557 25.730  1.00 26.64 ? 881 HOH C O   1 
# 
