data_8SRW
# 
_entry.id   8SRW 
# 
_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   8SRW         pdb_00008srw 10.2210/pdb8srw/pdb 
WWPDB D_1000274365 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8SRW 
_pdbx_database_status.recvd_initial_deposition_date   2023-05-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'unliganded from of the same enzyme'                        8SRT unspecified 
PDB 'the same enzyme complexed with a different peptide lignad' 8SRU unspecified 
PDB 'the same enzyme complexed with a different peptide ligand' 8SRV unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              john.bruning@adelaide.edu.au 
_pdbx_contact_author.name_first         John 
_pdbx_contact_author.name_last          Bruning 
_pdbx_contact_author.name_mi            B 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6919-1824 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pederick, J.L.' 1 0000-0003-4048-9771 
'Vandborg, B.C.' 2 0000-0002-3234-3089 
'Bruning, J.B.'  3 0000-0002-6919-1824 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Crystal structure of O-acetyl-L-serine sulfhydrylase A (CysK) from Staphylococcus aureus NCTC 8325 complexed with a modified peptide inhibitor
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pederick, J.L.' 1 0000-0003-4048-9771 
primary 'Vandborg, B.C.' 2 0000-0002-3234-3089 
primary 'Bruning, J.B.'  3 0000-0002-6919-1824 
# 
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 'Cysteine synthase' 34257.852 4   ? ? ? ? 
2 polymer syn TYR-MET-NAL-TYR-ILE 785.949   4   ? ? ? ? 
3 water   nat water               18.015    560 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no yes 
;MGHHHHHHMAQKPVDNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSV(LLP)DRIALAMIEKAEREGKIKPGDT
IVEPTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKELKEEHGYFEPQQFEN
PANPEVHELTTGPELLQQFEGKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAG
FIPGTLNTEIYDSIIKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVLPSNGERYLSTPLYSF
DD
;
;MGHHHHHHMAQKPVDNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEP
TSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKELKEEHGYFEPQQFENPANP
EVHELTTGPELLQQFEGKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPG
TLNTEIYDSIIKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVLPSNGERYLSTPLYSFDD
;
A,D,B,C ? 
2 'polypeptide(L)' no yes 'YM(NAL)YI' YMAYI E,F,G,H ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   MET n 
1 10  ALA n 
1 11  GLN n 
1 12  LYS n 
1 13  PRO n 
1 14  VAL n 
1 15  ASP n 
1 16  ASN n 
1 17  ILE n 
1 18  THR n 
1 19  GLN n 
1 20  ILE n 
1 21  ILE n 
1 22  GLY n 
1 23  GLY n 
1 24  THR n 
1 25  PRO n 
1 26  VAL n 
1 27  VAL n 
1 28  LYS n 
1 29  LEU n 
1 30  ARG n 
1 31  ASN n 
1 32  VAL n 
1 33  VAL n 
1 34  ASP n 
1 35  ASP n 
1 36  ASN n 
1 37  ALA n 
1 38  ALA n 
1 39  ASP n 
1 40  VAL n 
1 41  TYR n 
1 42  VAL n 
1 43  LYS n 
1 44  LEU n 
1 45  GLU n 
1 46  TYR n 
1 47  GLN n 
1 48  ASN n 
1 49  PRO n 
1 50  GLY n 
1 51  GLY n 
1 52  SER n 
1 53  VAL n 
1 54  LLP n 
1 55  ASP n 
1 56  ARG n 
1 57  ILE n 
1 58  ALA n 
1 59  LEU n 
1 60  ALA n 
1 61  MET n 
1 62  ILE n 
1 63  GLU n 
1 64  LYS n 
1 65  ALA n 
1 66  GLU n 
1 67  ARG n 
1 68  GLU n 
1 69  GLY n 
1 70  LYS n 
1 71  ILE n 
1 72  LYS n 
1 73  PRO n 
1 74  GLY n 
1 75  ASP n 
1 76  THR n 
1 77  ILE n 
1 78  VAL n 
1 79  GLU n 
1 80  PRO n 
1 81  THR n 
1 82  SER n 
1 83  GLY n 
1 84  ASN n 
1 85  THR n 
1 86  GLY n 
1 87  ILE n 
1 88  GLY n 
1 89  LEU n 
1 90  ALA n 
1 91  PHE n 
1 92  VAL n 
1 93  CYS n 
1 94  ALA n 
1 95  ALA n 
1 96  LYS n 
1 97  GLY n 
1 98  TYR n 
1 99  LYS n 
1 100 ALA n 
1 101 VAL n 
1 102 PHE n 
1 103 THR n 
1 104 MET n 
1 105 PRO n 
1 106 GLU n 
1 107 THR n 
1 108 MET n 
1 109 SER n 
1 110 GLN n 
1 111 GLU n 
1 112 ARG n 
1 113 ARG n 
1 114 ASN n 
1 115 LEU n 
1 116 LEU n 
1 117 LYS n 
1 118 ALA n 
1 119 TYR n 
1 120 GLY n 
1 121 ALA n 
1 122 GLU n 
1 123 LEU n 
1 124 VAL n 
1 125 LEU n 
1 126 THR n 
1 127 PRO n 
1 128 GLY n 
1 129 SER n 
1 130 GLU n 
1 131 ALA n 
1 132 MET n 
1 133 LYS n 
1 134 GLY n 
1 135 ALA n 
1 136 ILE n 
1 137 LYS n 
1 138 LYS n 
1 139 ALA n 
1 140 LYS n 
1 141 GLU n 
1 142 LEU n 
1 143 LYS n 
1 144 GLU n 
1 145 GLU n 
1 146 HIS n 
1 147 GLY n 
1 148 TYR n 
1 149 PHE n 
1 150 GLU n 
1 151 PRO n 
1 152 GLN n 
1 153 GLN n 
1 154 PHE n 
1 155 GLU n 
1 156 ASN n 
1 157 PRO n 
1 158 ALA n 
1 159 ASN n 
1 160 PRO n 
1 161 GLU n 
1 162 VAL n 
1 163 HIS n 
1 164 GLU n 
1 165 LEU n 
1 166 THR n 
1 167 THR n 
1 168 GLY n 
1 169 PRO n 
1 170 GLU n 
1 171 LEU n 
1 172 LEU n 
1 173 GLN n 
1 174 GLN n 
1 175 PHE n 
1 176 GLU n 
1 177 GLY n 
1 178 LYS n 
1 179 THR n 
1 180 ILE n 
1 181 ASP n 
1 182 ALA n 
1 183 PHE n 
1 184 LEU n 
1 185 ALA n 
1 186 GLY n 
1 187 VAL n 
1 188 GLY n 
1 189 THR n 
1 190 GLY n 
1 191 GLY n 
1 192 THR n 
1 193 LEU n 
1 194 SER n 
1 195 GLY n 
1 196 VAL n 
1 197 GLY n 
1 198 LYS n 
1 199 VAL n 
1 200 LEU n 
1 201 LYS n 
1 202 LYS n 
1 203 GLU n 
1 204 TYR n 
1 205 PRO n 
1 206 ASN n 
1 207 ILE n 
1 208 GLU n 
1 209 ILE n 
1 210 VAL n 
1 211 ALA n 
1 212 ILE n 
1 213 GLU n 
1 214 PRO n 
1 215 GLU n 
1 216 ALA n 
1 217 SER n 
1 218 PRO n 
1 219 VAL n 
1 220 LEU n 
1 221 SER n 
1 222 GLY n 
1 223 GLY n 
1 224 GLU n 
1 225 PRO n 
1 226 GLY n 
1 227 PRO n 
1 228 HIS n 
1 229 LYS n 
1 230 LEU n 
1 231 GLN n 
1 232 GLY n 
1 233 LEU n 
1 234 GLY n 
1 235 ALA n 
1 236 GLY n 
1 237 PHE n 
1 238 ILE n 
1 239 PRO n 
1 240 GLY n 
1 241 THR n 
1 242 LEU n 
1 243 ASN n 
1 244 THR n 
1 245 GLU n 
1 246 ILE n 
1 247 TYR n 
1 248 ASP n 
1 249 SER n 
1 250 ILE n 
1 251 ILE n 
1 252 LYS n 
1 253 VAL n 
1 254 GLY n 
1 255 ASN n 
1 256 ASP n 
1 257 THR n 
1 258 ALA n 
1 259 MET n 
1 260 GLU n 
1 261 MET n 
1 262 SER n 
1 263 ARG n 
1 264 ARG n 
1 265 VAL n 
1 266 ALA n 
1 267 LYS n 
1 268 GLU n 
1 269 GLU n 
1 270 GLY n 
1 271 ILE n 
1 272 LEU n 
1 273 ALA n 
1 274 GLY n 
1 275 ILE n 
1 276 SER n 
1 277 SER n 
1 278 GLY n 
1 279 ALA n 
1 280 ALA n 
1 281 ILE n 
1 282 TYR n 
1 283 ALA n 
1 284 ALA n 
1 285 ILE n 
1 286 GLN n 
1 287 LYS n 
1 288 ALA n 
1 289 LYS n 
1 290 GLU n 
1 291 LEU n 
1 292 GLY n 
1 293 LYS n 
1 294 GLY n 
1 295 LYS n 
1 296 THR n 
1 297 VAL n 
1 298 VAL n 
1 299 THR n 
1 300 VAL n 
1 301 LEU n 
1 302 PRO n 
1 303 SER n 
1 304 ASN n 
1 305 GLY n 
1 306 GLU n 
1 307 ARG n 
1 308 TYR n 
1 309 LEU n 
1 310 SER n 
1 311 THR n 
1 312 PRO n 
1 313 LEU n 
1 314 TYR n 
1 315 SER n 
1 316 PHE n 
1 317 ASP n 
1 318 ASP n 
2 1   TYR n 
2 2   MET n 
2 3   NAL n 
2 4   TYR n 
2 5   ILE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   318 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SAOUHSC_00488 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Staphylococcus aureus subsp. aureus NCTC 8325' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     93061 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       5 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                                 
?                                      'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                                                                                
?                                      'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                              
?                                      'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                         
?                                      'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                                
?                                      'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                               
?                                      'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                         
?                                      'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                                                                                 
?                                      'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                               
?                                      'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                                                                                   
?                                      'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                              
?                                      'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                                 
?                                      'C6 H13 N O2'     131.173 
LLP 'L-peptide linking' n '(2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid' 
"N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE" 'C14 H22 N3 O7 P' 375.314 
LYS 'L-peptide linking' y LYSINE                                                                                                  
?                                      'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                                                                                              
?                                      'C5 H11 N O2 S'   149.211 
NAL 'L-peptide linking' n 'BETA-(2-NAPHTHYL)-ALANINE'                                                                             
?                                      'C13 H13 N O2'    215.248 
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 
TYR 'L-peptide linking' y TYROSINE                                                                                                
?                                      'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                                                                                                  
?                                      'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -7  ?   ?   ?   A . n 
A 1 2   GLY 2   -6  ?   ?   ?   A . n 
A 1 3   HIS 3   -5  ?   ?   ?   A . n 
A 1 4   HIS 4   -4  ?   ?   ?   A . n 
A 1 5   HIS 5   -3  ?   ?   ?   A . n 
A 1 6   HIS 6   -2  ?   ?   ?   A . n 
A 1 7   HIS 7   -1  ?   ?   ?   A . n 
A 1 8   HIS 8   0   ?   ?   ?   A . n 
A 1 9   MET 9   1   1   MET MET A . n 
A 1 10  ALA 10  2   2   ALA ALA A . n 
A 1 11  GLN 11  3   3   GLN GLN A . n 
A 1 12  LYS 12  4   4   LYS LYS A . n 
A 1 13  PRO 13  5   5   PRO PRO A . n 
A 1 14  VAL 14  6   6   VAL VAL A . n 
A 1 15  ASP 15  7   7   ASP ASP A . n 
A 1 16  ASN 16  8   8   ASN ASN A . n 
A 1 17  ILE 17  9   9   ILE ILE A . n 
A 1 18  THR 18  10  10  THR THR A . n 
A 1 19  GLN 19  11  11  GLN GLN A . n 
A 1 20  ILE 20  12  12  ILE ILE A . n 
A 1 21  ILE 21  13  13  ILE ILE A . n 
A 1 22  GLY 22  14  14  GLY GLY A . n 
A 1 23  GLY 23  15  15  GLY GLY A . n 
A 1 24  THR 24  16  16  THR THR A . n 
A 1 25  PRO 25  17  17  PRO PRO A . n 
A 1 26  VAL 26  18  18  VAL VAL A . n 
A 1 27  VAL 27  19  19  VAL VAL A . n 
A 1 28  LYS 28  20  20  LYS LYS A . n 
A 1 29  LEU 29  21  21  LEU LEU A . n 
A 1 30  ARG 30  22  22  ARG ARG A . n 
A 1 31  ASN 31  23  23  ASN ASN A . n 
A 1 32  VAL 32  24  24  VAL VAL A . n 
A 1 33  VAL 33  25  25  VAL VAL A . n 
A 1 34  ASP 34  26  26  ASP ASP A . n 
A 1 35  ASP 35  27  27  ASP ASP A . n 
A 1 36  ASN 36  28  28  ASN ASN A . n 
A 1 37  ALA 37  29  29  ALA ALA A . n 
A 1 38  ALA 38  30  30  ALA ALA A . n 
A 1 39  ASP 39  31  31  ASP ASP A . n 
A 1 40  VAL 40  32  32  VAL VAL A . n 
A 1 41  TYR 41  33  33  TYR TYR A . n 
A 1 42  VAL 42  34  34  VAL VAL A . n 
A 1 43  LYS 43  35  35  LYS LYS A . n 
A 1 44  LEU 44  36  36  LEU LEU A . n 
A 1 45  GLU 45  37  37  GLU GLU A . n 
A 1 46  TYR 46  38  38  TYR TYR A . n 
A 1 47  GLN 47  39  39  GLN GLN A . n 
A 1 48  ASN 48  40  40  ASN ASN A . n 
A 1 49  PRO 49  41  41  PRO PRO A . n 
A 1 50  GLY 50  42  42  GLY GLY A . n 
A 1 51  GLY 51  43  43  GLY GLY A . n 
A 1 52  SER 52  44  44  SER SER A . n 
A 1 53  VAL 53  45  45  VAL VAL A . n 
A 1 54  LLP 54  46  46  LLP LLP A . n 
A 1 55  ASP 55  47  47  ASP ASP A . n 
A 1 56  ARG 56  48  48  ARG ARG A . n 
A 1 57  ILE 57  49  49  ILE ILE A . n 
A 1 58  ALA 58  50  50  ALA ALA A . n 
A 1 59  LEU 59  51  51  LEU LEU A . n 
A 1 60  ALA 60  52  52  ALA ALA A . n 
A 1 61  MET 61  53  53  MET MET A . n 
A 1 62  ILE 62  54  54  ILE ILE A . n 
A 1 63  GLU 63  55  55  GLU GLU A . n 
A 1 64  LYS 64  56  56  LYS LYS A . n 
A 1 65  ALA 65  57  57  ALA ALA A . n 
A 1 66  GLU 66  58  58  GLU GLU A . n 
A 1 67  ARG 67  59  59  ARG ARG A . n 
A 1 68  GLU 68  60  60  GLU GLU A . n 
A 1 69  GLY 69  61  61  GLY GLY A . n 
A 1 70  LYS 70  62  62  LYS LYS A . n 
A 1 71  ILE 71  63  63  ILE ILE A . n 
A 1 72  LYS 72  64  64  LYS LYS A . n 
A 1 73  PRO 73  65  65  PRO PRO A . n 
A 1 74  GLY 74  66  66  GLY GLY A . n 
A 1 75  ASP 75  67  67  ASP ASP A . n 
A 1 76  THR 76  68  68  THR THR A . n 
A 1 77  ILE 77  69  69  ILE ILE A . n 
A 1 78  VAL 78  70  70  VAL VAL A . n 
A 1 79  GLU 79  71  71  GLU GLU A . n 
A 1 80  PRO 80  72  72  PRO PRO A . n 
A 1 81  THR 81  73  73  THR THR A . n 
A 1 82  SER 82  74  74  SER SER A . n 
A 1 83  GLY 83  75  75  GLY GLY A . n 
A 1 84  ASN 84  76  76  ASN ASN A . n 
A 1 85  THR 85  77  77  THR THR A . n 
A 1 86  GLY 86  78  78  GLY GLY A . n 
A 1 87  ILE 87  79  79  ILE ILE A . n 
A 1 88  GLY 88  80  80  GLY GLY A . n 
A 1 89  LEU 89  81  81  LEU LEU A . n 
A 1 90  ALA 90  82  82  ALA ALA A . n 
A 1 91  PHE 91  83  83  PHE PHE A . n 
A 1 92  VAL 92  84  84  VAL VAL A . n 
A 1 93  CYS 93  85  85  CYS CYS A . n 
A 1 94  ALA 94  86  86  ALA ALA A . n 
A 1 95  ALA 95  87  87  ALA ALA A . n 
A 1 96  LYS 96  88  88  LYS LYS A . n 
A 1 97  GLY 97  89  89  GLY GLY A . n 
A 1 98  TYR 98  90  90  TYR TYR A . n 
A 1 99  LYS 99  91  91  LYS LYS A . n 
A 1 100 ALA 100 92  92  ALA ALA A . n 
A 1 101 VAL 101 93  93  VAL VAL A . n 
A 1 102 PHE 102 94  94  PHE PHE A . n 
A 1 103 THR 103 95  95  THR THR A . n 
A 1 104 MET 104 96  96  MET MET A . n 
A 1 105 PRO 105 97  97  PRO PRO A . n 
A 1 106 GLU 106 98  98  GLU GLU A . n 
A 1 107 THR 107 99  99  THR THR A . n 
A 1 108 MET 108 100 100 MET MET A . n 
A 1 109 SER 109 101 101 SER SER A . n 
A 1 110 GLN 110 102 102 GLN GLN A . n 
A 1 111 GLU 111 103 103 GLU GLU A . n 
A 1 112 ARG 112 104 104 ARG ARG A . n 
A 1 113 ARG 113 105 105 ARG ARG A . n 
A 1 114 ASN 114 106 106 ASN ASN A . n 
A 1 115 LEU 115 107 107 LEU LEU A . n 
A 1 116 LEU 116 108 108 LEU LEU A . n 
A 1 117 LYS 117 109 109 LYS LYS A . n 
A 1 118 ALA 118 110 110 ALA ALA A . n 
A 1 119 TYR 119 111 111 TYR TYR A . n 
A 1 120 GLY 120 112 112 GLY GLY A . n 
A 1 121 ALA 121 113 113 ALA ALA A . n 
A 1 122 GLU 122 114 114 GLU GLU A . n 
A 1 123 LEU 123 115 115 LEU LEU A . n 
A 1 124 VAL 124 116 116 VAL VAL A . n 
A 1 125 LEU 125 117 117 LEU LEU A . n 
A 1 126 THR 126 118 118 THR THR A . n 
A 1 127 PRO 127 119 119 PRO PRO A . n 
A 1 128 GLY 128 120 120 GLY GLY A . n 
A 1 129 SER 129 121 121 SER SER A . n 
A 1 130 GLU 130 122 122 GLU GLU A . n 
A 1 131 ALA 131 123 123 ALA ALA A . n 
A 1 132 MET 132 124 124 MET MET A . n 
A 1 133 LYS 133 125 125 LYS LYS A . n 
A 1 134 GLY 134 126 126 GLY GLY A . n 
A 1 135 ALA 135 127 127 ALA ALA A . n 
A 1 136 ILE 136 128 128 ILE ILE A . n 
A 1 137 LYS 137 129 129 LYS LYS A . n 
A 1 138 LYS 138 130 130 LYS LYS A . n 
A 1 139 ALA 139 131 131 ALA ALA A . n 
A 1 140 LYS 140 132 132 LYS LYS A . n 
A 1 141 GLU 141 133 133 GLU GLU A . n 
A 1 142 LEU 142 134 134 LEU LEU A . n 
A 1 143 LYS 143 135 135 LYS LYS A . n 
A 1 144 GLU 144 136 136 GLU GLU A . n 
A 1 145 GLU 145 137 137 GLU GLU A . n 
A 1 146 HIS 146 138 138 HIS HIS A . n 
A 1 147 GLY 147 139 139 GLY GLY A . n 
A 1 148 TYR 148 140 140 TYR TYR A . n 
A 1 149 PHE 149 141 141 PHE PHE A . n 
A 1 150 GLU 150 142 142 GLU GLU A . n 
A 1 151 PRO 151 143 143 PRO PRO A . n 
A 1 152 GLN 152 144 144 GLN GLN A . n 
A 1 153 GLN 153 145 145 GLN GLN A . n 
A 1 154 PHE 154 146 146 PHE PHE A . n 
A 1 155 GLU 155 147 147 GLU GLU A . n 
A 1 156 ASN 156 148 148 ASN ASN A . n 
A 1 157 PRO 157 149 149 PRO PRO A . n 
A 1 158 ALA 158 150 150 ALA ALA A . n 
A 1 159 ASN 159 151 151 ASN ASN A . n 
A 1 160 PRO 160 152 152 PRO PRO A . n 
A 1 161 GLU 161 153 153 GLU GLU A . n 
A 1 162 VAL 162 154 154 VAL VAL A . n 
A 1 163 HIS 163 155 155 HIS HIS A . n 
A 1 164 GLU 164 156 156 GLU GLU A . n 
A 1 165 LEU 165 157 157 LEU LEU A . n 
A 1 166 THR 166 158 158 THR THR A . n 
A 1 167 THR 167 159 159 THR THR A . n 
A 1 168 GLY 168 160 160 GLY GLY A . n 
A 1 169 PRO 169 161 161 PRO PRO A . n 
A 1 170 GLU 170 162 162 GLU GLU A . n 
A 1 171 LEU 171 163 163 LEU LEU A . n 
A 1 172 LEU 172 164 164 LEU LEU A . n 
A 1 173 GLN 173 165 165 GLN GLN A . n 
A 1 174 GLN 174 166 166 GLN GLN A . n 
A 1 175 PHE 175 167 167 PHE PHE A . n 
A 1 176 GLU 176 168 168 GLU GLU A . n 
A 1 177 GLY 177 169 169 GLY GLY A . n 
A 1 178 LYS 178 170 170 LYS LYS A . n 
A 1 179 THR 179 171 171 THR THR A . n 
A 1 180 ILE 180 172 172 ILE ILE A . n 
A 1 181 ASP 181 173 173 ASP ASP A . n 
A 1 182 ALA 182 174 174 ALA ALA A . n 
A 1 183 PHE 183 175 175 PHE PHE A . n 
A 1 184 LEU 184 176 176 LEU LEU A . n 
A 1 185 ALA 185 177 177 ALA ALA A . n 
A 1 186 GLY 186 178 178 GLY GLY A . n 
A 1 187 VAL 187 179 179 VAL VAL A . n 
A 1 188 GLY 188 180 180 GLY GLY A . n 
A 1 189 THR 189 181 181 THR THR A . n 
A 1 190 GLY 190 182 182 GLY GLY A . n 
A 1 191 GLY 191 183 183 GLY GLY A . n 
A 1 192 THR 192 184 184 THR THR A . n 
A 1 193 LEU 193 185 185 LEU LEU A . n 
A 1 194 SER 194 186 186 SER SER A . n 
A 1 195 GLY 195 187 187 GLY GLY A . n 
A 1 196 VAL 196 188 188 VAL VAL A . n 
A 1 197 GLY 197 189 189 GLY GLY A . n 
A 1 198 LYS 198 190 190 LYS LYS A . n 
A 1 199 VAL 199 191 191 VAL VAL A . n 
A 1 200 LEU 200 192 192 LEU LEU A . n 
A 1 201 LYS 201 193 193 LYS LYS A . n 
A 1 202 LYS 202 194 194 LYS LYS A . n 
A 1 203 GLU 203 195 195 GLU GLU A . n 
A 1 204 TYR 204 196 196 TYR TYR A . n 
A 1 205 PRO 205 197 197 PRO PRO A . n 
A 1 206 ASN 206 198 198 ASN ASN A . n 
A 1 207 ILE 207 199 199 ILE ILE A . n 
A 1 208 GLU 208 200 200 GLU GLU A . n 
A 1 209 ILE 209 201 201 ILE ILE A . n 
A 1 210 VAL 210 202 202 VAL VAL A . n 
A 1 211 ALA 211 203 203 ALA ALA A . n 
A 1 212 ILE 212 204 204 ILE ILE A . n 
A 1 213 GLU 213 205 205 GLU GLU A . n 
A 1 214 PRO 214 206 206 PRO PRO A . n 
A 1 215 GLU 215 207 207 GLU GLU A . n 
A 1 216 ALA 216 208 208 ALA ALA A . n 
A 1 217 SER 217 209 209 SER SER A . n 
A 1 218 PRO 218 210 210 PRO PRO A . n 
A 1 219 VAL 219 211 211 VAL VAL A . n 
A 1 220 LEU 220 212 212 LEU LEU A . n 
A 1 221 SER 221 213 213 SER SER A . n 
A 1 222 GLY 222 214 214 GLY GLY A . n 
A 1 223 GLY 223 215 215 GLY GLY A . n 
A 1 224 GLU 224 216 216 GLU GLU A . n 
A 1 225 PRO 225 217 217 PRO PRO A . n 
A 1 226 GLY 226 218 218 GLY GLY A . n 
A 1 227 PRO 227 219 219 PRO PRO A . n 
A 1 228 HIS 228 220 220 HIS HIS A . n 
A 1 229 LYS 229 221 221 LYS LYS A . n 
A 1 230 LEU 230 222 222 LEU LEU A . n 
A 1 231 GLN 231 223 223 GLN GLN A . n 
A 1 232 GLY 232 224 224 GLY GLY A . n 
A 1 233 LEU 233 225 225 LEU LEU A . n 
A 1 234 GLY 234 226 226 GLY GLY A . n 
A 1 235 ALA 235 227 227 ALA ALA A . n 
A 1 236 GLY 236 228 228 GLY GLY A . n 
A 1 237 PHE 237 229 229 PHE PHE A . n 
A 1 238 ILE 238 230 230 ILE ILE A . n 
A 1 239 PRO 239 231 231 PRO PRO A . n 
A 1 240 GLY 240 232 232 GLY GLY A . n 
A 1 241 THR 241 233 233 THR THR A . n 
A 1 242 LEU 242 234 234 LEU LEU A . n 
A 1 243 ASN 243 235 235 ASN ASN A . n 
A 1 244 THR 244 236 236 THR THR A . n 
A 1 245 GLU 245 237 237 GLU GLU A . n 
A 1 246 ILE 246 238 238 ILE ILE A . n 
A 1 247 TYR 247 239 239 TYR TYR A . n 
A 1 248 ASP 248 240 240 ASP ASP A . n 
A 1 249 SER 249 241 241 SER SER A . n 
A 1 250 ILE 250 242 242 ILE ILE A . n 
A 1 251 ILE 251 243 243 ILE ILE A . n 
A 1 252 LYS 252 244 244 LYS LYS A . n 
A 1 253 VAL 253 245 245 VAL VAL A . n 
A 1 254 GLY 254 246 246 GLY GLY A . n 
A 1 255 ASN 255 247 247 ASN ASN A . n 
A 1 256 ASP 256 248 248 ASP ASP A . n 
A 1 257 THR 257 249 249 THR THR A . n 
A 1 258 ALA 258 250 250 ALA ALA A . n 
A 1 259 MET 259 251 251 MET MET A . n 
A 1 260 GLU 260 252 252 GLU GLU A . n 
A 1 261 MET 261 253 253 MET MET A . n 
A 1 262 SER 262 254 254 SER SER A . n 
A 1 263 ARG 263 255 255 ARG ARG A . n 
A 1 264 ARG 264 256 256 ARG ARG A . n 
A 1 265 VAL 265 257 257 VAL VAL A . n 
A 1 266 ALA 266 258 258 ALA ALA A . n 
A 1 267 LYS 267 259 259 LYS LYS A . n 
A 1 268 GLU 268 260 260 GLU GLU A . n 
A 1 269 GLU 269 261 261 GLU GLU A . n 
A 1 270 GLY 270 262 262 GLY GLY A . n 
A 1 271 ILE 271 263 263 ILE ILE A . n 
A 1 272 LEU 272 264 264 LEU LEU A . n 
A 1 273 ALA 273 265 265 ALA ALA A . n 
A 1 274 GLY 274 266 266 GLY GLY A . n 
A 1 275 ILE 275 267 267 ILE ILE A . n 
A 1 276 SER 276 268 268 SER SER A . n 
A 1 277 SER 277 269 269 SER SER A . n 
A 1 278 GLY 278 270 270 GLY GLY A . n 
A 1 279 ALA 279 271 271 ALA ALA A . n 
A 1 280 ALA 280 272 272 ALA ALA A . n 
A 1 281 ILE 281 273 273 ILE ILE A . n 
A 1 282 TYR 282 274 274 TYR TYR A . n 
A 1 283 ALA 283 275 275 ALA ALA A . n 
A 1 284 ALA 284 276 276 ALA ALA A . n 
A 1 285 ILE 285 277 277 ILE ILE A . n 
A 1 286 GLN 286 278 278 GLN GLN A . n 
A 1 287 LYS 287 279 279 LYS LYS A . n 
A 1 288 ALA 288 280 280 ALA ALA A . n 
A 1 289 LYS 289 281 281 LYS LYS A . n 
A 1 290 GLU 290 282 282 GLU GLU A . n 
A 1 291 LEU 291 283 283 LEU LEU A . n 
A 1 292 GLY 292 284 284 GLY GLY A . n 
A 1 293 LYS 293 285 285 LYS LYS A . n 
A 1 294 GLY 294 286 286 GLY GLY A . n 
A 1 295 LYS 295 287 287 LYS LYS A . n 
A 1 296 THR 296 288 288 THR THR A . n 
A 1 297 VAL 297 289 289 VAL VAL A . n 
A 1 298 VAL 298 290 290 VAL VAL A . n 
A 1 299 THR 299 291 291 THR THR A . n 
A 1 300 VAL 300 292 292 VAL VAL A . n 
A 1 301 LEU 301 293 293 LEU LEU A . n 
A 1 302 PRO 302 294 294 PRO PRO A . n 
A 1 303 SER 303 295 295 SER SER A . n 
A 1 304 ASN 304 296 296 ASN ASN A . n 
A 1 305 GLY 305 297 297 GLY GLY A . n 
A 1 306 GLU 306 298 298 GLU GLU A . n 
A 1 307 ARG 307 299 299 ARG ARG A . n 
A 1 308 TYR 308 300 300 TYR TYR A . n 
A 1 309 LEU 309 301 301 LEU LEU A . n 
A 1 310 SER 310 302 302 SER SER A . n 
A 1 311 THR 311 303 303 THR THR A . n 
A 1 312 PRO 312 304 304 PRO PRO A . n 
A 1 313 LEU 313 305 305 LEU LEU A . n 
A 1 314 TYR 314 306 306 TYR TYR A . n 
A 1 315 SER 315 307 307 SER SER A . n 
A 1 316 PHE 316 308 ?   ?   ?   A . n 
A 1 317 ASP 317 309 ?   ?   ?   A . n 
A 1 318 ASP 318 310 ?   ?   ?   A . n 
B 1 1   MET 1   -7  ?   ?   ?   D . n 
B 1 2   GLY 2   -6  ?   ?   ?   D . n 
B 1 3   HIS 3   -5  ?   ?   ?   D . n 
B 1 4   HIS 4   -4  ?   ?   ?   D . n 
B 1 5   HIS 5   -3  ?   ?   ?   D . n 
B 1 6   HIS 6   -2  ?   ?   ?   D . n 
B 1 7   HIS 7   -1  ?   ?   ?   D . n 
B 1 8   HIS 8   0   ?   ?   ?   D . n 
B 1 9   MET 9   1   1   MET MET D . n 
B 1 10  ALA 10  2   2   ALA ALA D . n 
B 1 11  GLN 11  3   3   GLN GLN D . n 
B 1 12  LYS 12  4   4   LYS LYS D . n 
B 1 13  PRO 13  5   5   PRO PRO D . n 
B 1 14  VAL 14  6   6   VAL VAL D . n 
B 1 15  ASP 15  7   7   ASP ASP D . n 
B 1 16  ASN 16  8   8   ASN ASN D . n 
B 1 17  ILE 17  9   9   ILE ILE D . n 
B 1 18  THR 18  10  10  THR THR D . n 
B 1 19  GLN 19  11  11  GLN GLN D . n 
B 1 20  ILE 20  12  12  ILE ILE D . n 
B 1 21  ILE 21  13  13  ILE ILE D . n 
B 1 22  GLY 22  14  14  GLY GLY D . n 
B 1 23  GLY 23  15  15  GLY GLY D . n 
B 1 24  THR 24  16  16  THR THR D . n 
B 1 25  PRO 25  17  17  PRO PRO D . n 
B 1 26  VAL 26  18  18  VAL VAL D . n 
B 1 27  VAL 27  19  19  VAL VAL D . n 
B 1 28  LYS 28  20  20  LYS LYS D . n 
B 1 29  LEU 29  21  21  LEU LEU D . n 
B 1 30  ARG 30  22  22  ARG ARG D . n 
B 1 31  ASN 31  23  23  ASN ASN D . n 
B 1 32  VAL 32  24  24  VAL VAL D . n 
B 1 33  VAL 33  25  25  VAL VAL D . n 
B 1 34  ASP 34  26  26  ASP ASP D . n 
B 1 35  ASP 35  27  27  ASP ASP D . n 
B 1 36  ASN 36  28  28  ASN ASN D . n 
B 1 37  ALA 37  29  29  ALA ALA D . n 
B 1 38  ALA 38  30  30  ALA ALA D . n 
B 1 39  ASP 39  31  31  ASP ASP D . n 
B 1 40  VAL 40  32  32  VAL VAL D . n 
B 1 41  TYR 41  33  33  TYR TYR D . n 
B 1 42  VAL 42  34  34  VAL VAL D . n 
B 1 43  LYS 43  35  35  LYS LYS D . n 
B 1 44  LEU 44  36  36  LEU LEU D . n 
B 1 45  GLU 45  37  37  GLU GLU D . n 
B 1 46  TYR 46  38  38  TYR TYR D . n 
B 1 47  GLN 47  39  39  GLN GLN D . n 
B 1 48  ASN 48  40  40  ASN ASN D . n 
B 1 49  PRO 49  41  41  PRO PRO D . n 
B 1 50  GLY 50  42  42  GLY GLY D . n 
B 1 51  GLY 51  43  43  GLY GLY D . n 
B 1 52  SER 52  44  44  SER SER D . n 
B 1 53  VAL 53  45  45  VAL VAL D . n 
B 1 54  LLP 54  46  46  LLP LLP D . n 
B 1 55  ASP 55  47  47  ASP ASP D . n 
B 1 56  ARG 56  48  48  ARG ARG D . n 
B 1 57  ILE 57  49  49  ILE ILE D . n 
B 1 58  ALA 58  50  50  ALA ALA D . n 
B 1 59  LEU 59  51  51  LEU LEU D . n 
B 1 60  ALA 60  52  52  ALA ALA D . n 
B 1 61  MET 61  53  53  MET MET D . n 
B 1 62  ILE 62  54  54  ILE ILE D . n 
B 1 63  GLU 63  55  55  GLU GLU D . n 
B 1 64  LYS 64  56  56  LYS LYS D . n 
B 1 65  ALA 65  57  57  ALA ALA D . n 
B 1 66  GLU 66  58  58  GLU GLU D . n 
B 1 67  ARG 67  59  59  ARG ARG D . n 
B 1 68  GLU 68  60  60  GLU GLU D . n 
B 1 69  GLY 69  61  61  GLY GLY D . n 
B 1 70  LYS 70  62  62  LYS LYS D . n 
B 1 71  ILE 71  63  63  ILE ILE D . n 
B 1 72  LYS 72  64  64  LYS LYS D . n 
B 1 73  PRO 73  65  65  PRO PRO D . n 
B 1 74  GLY 74  66  66  GLY GLY D . n 
B 1 75  ASP 75  67  67  ASP ASP D . n 
B 1 76  THR 76  68  68  THR THR D . n 
B 1 77  ILE 77  69  69  ILE ILE D . n 
B 1 78  VAL 78  70  70  VAL VAL D . n 
B 1 79  GLU 79  71  71  GLU GLU D . n 
B 1 80  PRO 80  72  72  PRO PRO D . n 
B 1 81  THR 81  73  73  THR THR D . n 
B 1 82  SER 82  74  74  SER SER D . n 
B 1 83  GLY 83  75  75  GLY GLY D . n 
B 1 84  ASN 84  76  76  ASN ASN D . n 
B 1 85  THR 85  77  77  THR THR D . n 
B 1 86  GLY 86  78  78  GLY GLY D . n 
B 1 87  ILE 87  79  79  ILE ILE D . n 
B 1 88  GLY 88  80  80  GLY GLY D . n 
B 1 89  LEU 89  81  81  LEU LEU D . n 
B 1 90  ALA 90  82  82  ALA ALA D . n 
B 1 91  PHE 91  83  83  PHE PHE D . n 
B 1 92  VAL 92  84  84  VAL VAL D . n 
B 1 93  CYS 93  85  85  CYS CYS D . n 
B 1 94  ALA 94  86  86  ALA ALA D . n 
B 1 95  ALA 95  87  87  ALA ALA D . n 
B 1 96  LYS 96  88  88  LYS LYS D . n 
B 1 97  GLY 97  89  89  GLY GLY D . n 
B 1 98  TYR 98  90  90  TYR TYR D . n 
B 1 99  LYS 99  91  91  LYS LYS D . n 
B 1 100 ALA 100 92  92  ALA ALA D . n 
B 1 101 VAL 101 93  93  VAL VAL D . n 
B 1 102 PHE 102 94  94  PHE PHE D . n 
B 1 103 THR 103 95  95  THR THR D . n 
B 1 104 MET 104 96  96  MET MET D . n 
B 1 105 PRO 105 97  97  PRO PRO D . n 
B 1 106 GLU 106 98  98  GLU GLU D . n 
B 1 107 THR 107 99  99  THR THR D . n 
B 1 108 MET 108 100 100 MET MET D . n 
B 1 109 SER 109 101 101 SER SER D . n 
B 1 110 GLN 110 102 102 GLN GLN D . n 
B 1 111 GLU 111 103 103 GLU GLU D . n 
B 1 112 ARG 112 104 104 ARG ARG D . n 
B 1 113 ARG 113 105 105 ARG ARG D . n 
B 1 114 ASN 114 106 106 ASN ASN D . n 
B 1 115 LEU 115 107 107 LEU LEU D . n 
B 1 116 LEU 116 108 108 LEU LEU D . n 
B 1 117 LYS 117 109 109 LYS LYS D . n 
B 1 118 ALA 118 110 110 ALA ALA D . n 
B 1 119 TYR 119 111 111 TYR TYR D . n 
B 1 120 GLY 120 112 112 GLY GLY D . n 
B 1 121 ALA 121 113 113 ALA ALA D . n 
B 1 122 GLU 122 114 114 GLU GLU D . n 
B 1 123 LEU 123 115 115 LEU LEU D . n 
B 1 124 VAL 124 116 116 VAL VAL D . n 
B 1 125 LEU 125 117 117 LEU LEU D . n 
B 1 126 THR 126 118 118 THR THR D . n 
B 1 127 PRO 127 119 119 PRO PRO D . n 
B 1 128 GLY 128 120 120 GLY GLY D . n 
B 1 129 SER 129 121 121 SER SER D . n 
B 1 130 GLU 130 122 122 GLU GLU D . n 
B 1 131 ALA 131 123 123 ALA ALA D . n 
B 1 132 MET 132 124 124 MET MET D . n 
B 1 133 LYS 133 125 125 LYS LYS D . n 
B 1 134 GLY 134 126 126 GLY GLY D . n 
B 1 135 ALA 135 127 127 ALA ALA D . n 
B 1 136 ILE 136 128 128 ILE ILE D . n 
B 1 137 LYS 137 129 129 LYS LYS D . n 
B 1 138 LYS 138 130 130 LYS LYS D . n 
B 1 139 ALA 139 131 131 ALA ALA D . n 
B 1 140 LYS 140 132 132 LYS LYS D . n 
B 1 141 GLU 141 133 133 GLU GLU D . n 
B 1 142 LEU 142 134 134 LEU LEU D . n 
B 1 143 LYS 143 135 135 LYS LYS D . n 
B 1 144 GLU 144 136 136 GLU GLU D . n 
B 1 145 GLU 145 137 137 GLU GLU D . n 
B 1 146 HIS 146 138 138 HIS HIS D . n 
B 1 147 GLY 147 139 139 GLY GLY D . n 
B 1 148 TYR 148 140 140 TYR TYR D . n 
B 1 149 PHE 149 141 141 PHE PHE D . n 
B 1 150 GLU 150 142 142 GLU GLU D . n 
B 1 151 PRO 151 143 143 PRO PRO D . n 
B 1 152 GLN 152 144 144 GLN GLN D . n 
B 1 153 GLN 153 145 145 GLN GLN D . n 
B 1 154 PHE 154 146 146 PHE PHE D . n 
B 1 155 GLU 155 147 147 GLU GLU D . n 
B 1 156 ASN 156 148 148 ASN ASN D . n 
B 1 157 PRO 157 149 149 PRO PRO D . n 
B 1 158 ALA 158 150 150 ALA ALA D . n 
B 1 159 ASN 159 151 151 ASN ASN D . n 
B 1 160 PRO 160 152 152 PRO PRO D . n 
B 1 161 GLU 161 153 153 GLU GLU D . n 
B 1 162 VAL 162 154 154 VAL VAL D . n 
B 1 163 HIS 163 155 155 HIS HIS D . n 
B 1 164 GLU 164 156 156 GLU GLU D . n 
B 1 165 LEU 165 157 157 LEU LEU D . n 
B 1 166 THR 166 158 158 THR THR D . n 
B 1 167 THR 167 159 159 THR THR D . n 
B 1 168 GLY 168 160 160 GLY GLY D . n 
B 1 169 PRO 169 161 161 PRO PRO D . n 
B 1 170 GLU 170 162 162 GLU GLU D . n 
B 1 171 LEU 171 163 163 LEU LEU D . n 
B 1 172 LEU 172 164 164 LEU LEU D . n 
B 1 173 GLN 173 165 165 GLN GLN D . n 
B 1 174 GLN 174 166 166 GLN GLN D . n 
B 1 175 PHE 175 167 167 PHE PHE D . n 
B 1 176 GLU 176 168 168 GLU GLU D . n 
B 1 177 GLY 177 169 169 GLY GLY D . n 
B 1 178 LYS 178 170 170 LYS LYS D . n 
B 1 179 THR 179 171 171 THR THR D . n 
B 1 180 ILE 180 172 172 ILE ILE D . n 
B 1 181 ASP 181 173 173 ASP ASP D . n 
B 1 182 ALA 182 174 174 ALA ALA D . n 
B 1 183 PHE 183 175 175 PHE PHE D . n 
B 1 184 LEU 184 176 176 LEU LEU D . n 
B 1 185 ALA 185 177 177 ALA ALA D . n 
B 1 186 GLY 186 178 178 GLY GLY D . n 
B 1 187 VAL 187 179 179 VAL VAL D . n 
B 1 188 GLY 188 180 180 GLY GLY D . n 
B 1 189 THR 189 181 181 THR THR D . n 
B 1 190 GLY 190 182 182 GLY GLY D . n 
B 1 191 GLY 191 183 183 GLY GLY D . n 
B 1 192 THR 192 184 184 THR THR D . n 
B 1 193 LEU 193 185 185 LEU LEU D . n 
B 1 194 SER 194 186 186 SER SER D . n 
B 1 195 GLY 195 187 187 GLY GLY D . n 
B 1 196 VAL 196 188 188 VAL VAL D . n 
B 1 197 GLY 197 189 189 GLY GLY D . n 
B 1 198 LYS 198 190 190 LYS LYS D . n 
B 1 199 VAL 199 191 191 VAL VAL D . n 
B 1 200 LEU 200 192 192 LEU LEU D . n 
B 1 201 LYS 201 193 193 LYS LYS D . n 
B 1 202 LYS 202 194 194 LYS LYS D . n 
B 1 203 GLU 203 195 195 GLU GLU D . n 
B 1 204 TYR 204 196 196 TYR TYR D . n 
B 1 205 PRO 205 197 197 PRO PRO D . n 
B 1 206 ASN 206 198 198 ASN ASN D . n 
B 1 207 ILE 207 199 199 ILE ILE D . n 
B 1 208 GLU 208 200 200 GLU GLU D . n 
B 1 209 ILE 209 201 201 ILE ILE D . n 
B 1 210 VAL 210 202 202 VAL VAL D . n 
B 1 211 ALA 211 203 203 ALA ALA D . n 
B 1 212 ILE 212 204 204 ILE ILE D . n 
B 1 213 GLU 213 205 205 GLU GLU D . n 
B 1 214 PRO 214 206 206 PRO PRO D . n 
B 1 215 GLU 215 207 207 GLU GLU D . n 
B 1 216 ALA 216 208 208 ALA ALA D . n 
B 1 217 SER 217 209 209 SER SER D . n 
B 1 218 PRO 218 210 210 PRO PRO D . n 
B 1 219 VAL 219 211 211 VAL VAL D . n 
B 1 220 LEU 220 212 212 LEU LEU D . n 
B 1 221 SER 221 213 213 SER SER D . n 
B 1 222 GLY 222 214 214 GLY GLY D . n 
B 1 223 GLY 223 215 215 GLY GLY D . n 
B 1 224 GLU 224 216 216 GLU GLU D . n 
B 1 225 PRO 225 217 217 PRO PRO D . n 
B 1 226 GLY 226 218 218 GLY GLY D . n 
B 1 227 PRO 227 219 219 PRO PRO D . n 
B 1 228 HIS 228 220 220 HIS HIS D . n 
B 1 229 LYS 229 221 221 LYS LYS D . n 
B 1 230 LEU 230 222 222 LEU LEU D . n 
B 1 231 GLN 231 223 223 GLN GLN D . n 
B 1 232 GLY 232 224 224 GLY GLY D . n 
B 1 233 LEU 233 225 225 LEU LEU D . n 
B 1 234 GLY 234 226 226 GLY GLY D . n 
B 1 235 ALA 235 227 227 ALA ALA D . n 
B 1 236 GLY 236 228 228 GLY GLY D . n 
B 1 237 PHE 237 229 229 PHE PHE D . n 
B 1 238 ILE 238 230 230 ILE ILE D . n 
B 1 239 PRO 239 231 231 PRO PRO D . n 
B 1 240 GLY 240 232 232 GLY GLY D . n 
B 1 241 THR 241 233 233 THR THR D . n 
B 1 242 LEU 242 234 234 LEU LEU D . n 
B 1 243 ASN 243 235 235 ASN ASN D . n 
B 1 244 THR 244 236 236 THR THR D . n 
B 1 245 GLU 245 237 237 GLU GLU D . n 
B 1 246 ILE 246 238 238 ILE ILE D . n 
B 1 247 TYR 247 239 239 TYR TYR D . n 
B 1 248 ASP 248 240 240 ASP ASP D . n 
B 1 249 SER 249 241 241 SER SER D . n 
B 1 250 ILE 250 242 242 ILE ILE D . n 
B 1 251 ILE 251 243 243 ILE ILE D . n 
B 1 252 LYS 252 244 244 LYS LYS D . n 
B 1 253 VAL 253 245 245 VAL VAL D . n 
B 1 254 GLY 254 246 246 GLY GLY D . n 
B 1 255 ASN 255 247 247 ASN ASN D . n 
B 1 256 ASP 256 248 248 ASP ASP D . n 
B 1 257 THR 257 249 249 THR THR D . n 
B 1 258 ALA 258 250 250 ALA ALA D . n 
B 1 259 MET 259 251 251 MET MET D . n 
B 1 260 GLU 260 252 252 GLU GLU D . n 
B 1 261 MET 261 253 253 MET MET D . n 
B 1 262 SER 262 254 254 SER SER D . n 
B 1 263 ARG 263 255 255 ARG ARG D . n 
B 1 264 ARG 264 256 256 ARG ARG D . n 
B 1 265 VAL 265 257 257 VAL VAL D . n 
B 1 266 ALA 266 258 258 ALA ALA D . n 
B 1 267 LYS 267 259 259 LYS LYS D . n 
B 1 268 GLU 268 260 260 GLU GLU D . n 
B 1 269 GLU 269 261 261 GLU GLU D . n 
B 1 270 GLY 270 262 262 GLY GLY D . n 
B 1 271 ILE 271 263 263 ILE ILE D . n 
B 1 272 LEU 272 264 264 LEU LEU D . n 
B 1 273 ALA 273 265 265 ALA ALA D . n 
B 1 274 GLY 274 266 266 GLY GLY D . n 
B 1 275 ILE 275 267 267 ILE ILE D . n 
B 1 276 SER 276 268 268 SER SER D . n 
B 1 277 SER 277 269 269 SER SER D . n 
B 1 278 GLY 278 270 270 GLY GLY D . n 
B 1 279 ALA 279 271 271 ALA ALA D . n 
B 1 280 ALA 280 272 272 ALA ALA D . n 
B 1 281 ILE 281 273 273 ILE ILE D . n 
B 1 282 TYR 282 274 274 TYR TYR D . n 
B 1 283 ALA 283 275 275 ALA ALA D . n 
B 1 284 ALA 284 276 276 ALA ALA D . n 
B 1 285 ILE 285 277 277 ILE ILE D . n 
B 1 286 GLN 286 278 278 GLN GLN D . n 
B 1 287 LYS 287 279 279 LYS LYS D . n 
B 1 288 ALA 288 280 280 ALA ALA D . n 
B 1 289 LYS 289 281 281 LYS LYS D . n 
B 1 290 GLU 290 282 282 GLU GLU D . n 
B 1 291 LEU 291 283 283 LEU LEU D . n 
B 1 292 GLY 292 284 284 GLY GLY D . n 
B 1 293 LYS 293 285 285 LYS LYS D . n 
B 1 294 GLY 294 286 286 GLY GLY D . n 
B 1 295 LYS 295 287 287 LYS LYS D . n 
B 1 296 THR 296 288 288 THR THR D . n 
B 1 297 VAL 297 289 289 VAL VAL D . n 
B 1 298 VAL 298 290 290 VAL VAL D . n 
B 1 299 THR 299 291 291 THR THR D . n 
B 1 300 VAL 300 292 292 VAL VAL D . n 
B 1 301 LEU 301 293 293 LEU LEU D . n 
B 1 302 PRO 302 294 294 PRO PRO D . n 
B 1 303 SER 303 295 295 SER SER D . n 
B 1 304 ASN 304 296 296 ASN ASN D . n 
B 1 305 GLY 305 297 297 GLY GLY D . n 
B 1 306 GLU 306 298 298 GLU GLU D . n 
B 1 307 ARG 307 299 299 ARG ARG D . n 
B 1 308 TYR 308 300 300 TYR TYR D . n 
B 1 309 LEU 309 301 301 LEU LEU D . n 
B 1 310 SER 310 302 302 SER SER D . n 
B 1 311 THR 311 303 303 THR THR D . n 
B 1 312 PRO 312 304 304 PRO PRO D . n 
B 1 313 LEU 313 305 305 LEU LEU D . n 
B 1 314 TYR 314 306 306 TYR TYR D . n 
B 1 315 SER 315 307 307 SER SER D . n 
B 1 316 PHE 316 308 ?   ?   ?   D . n 
B 1 317 ASP 317 309 ?   ?   ?   D . n 
B 1 318 ASP 318 310 ?   ?   ?   D . n 
C 1 1   MET 1   -7  ?   ?   ?   B . n 
C 1 2   GLY 2   -6  ?   ?   ?   B . n 
C 1 3   HIS 3   -5  ?   ?   ?   B . n 
C 1 4   HIS 4   -4  ?   ?   ?   B . n 
C 1 5   HIS 5   -3  ?   ?   ?   B . n 
C 1 6   HIS 6   -2  ?   ?   ?   B . n 
C 1 7   HIS 7   -1  ?   ?   ?   B . n 
C 1 8   HIS 8   0   ?   ?   ?   B . n 
C 1 9   MET 9   1   1   MET MET B . n 
C 1 10  ALA 10  2   2   ALA ALA B . n 
C 1 11  GLN 11  3   3   GLN GLN B . n 
C 1 12  LYS 12  4   4   LYS LYS B . n 
C 1 13  PRO 13  5   5   PRO PRO B . n 
C 1 14  VAL 14  6   6   VAL VAL B . n 
C 1 15  ASP 15  7   7   ASP ASP B . n 
C 1 16  ASN 16  8   8   ASN ASN B . n 
C 1 17  ILE 17  9   9   ILE ILE B . n 
C 1 18  THR 18  10  10  THR THR B . n 
C 1 19  GLN 19  11  11  GLN GLN B . n 
C 1 20  ILE 20  12  12  ILE ILE B . n 
C 1 21  ILE 21  13  13  ILE ILE B . n 
C 1 22  GLY 22  14  14  GLY GLY B . n 
C 1 23  GLY 23  15  15  GLY GLY B . n 
C 1 24  THR 24  16  16  THR THR B . n 
C 1 25  PRO 25  17  17  PRO PRO B . n 
C 1 26  VAL 26  18  18  VAL VAL B . n 
C 1 27  VAL 27  19  19  VAL VAL B . n 
C 1 28  LYS 28  20  20  LYS LYS B . n 
C 1 29  LEU 29  21  21  LEU LEU B . n 
C 1 30  ARG 30  22  22  ARG ARG B . n 
C 1 31  ASN 31  23  23  ASN ASN B . n 
C 1 32  VAL 32  24  24  VAL VAL B . n 
C 1 33  VAL 33  25  25  VAL VAL B . n 
C 1 34  ASP 34  26  26  ASP ASP B . n 
C 1 35  ASP 35  27  27  ASP ASP B . n 
C 1 36  ASN 36  28  28  ASN ASN B . n 
C 1 37  ALA 37  29  29  ALA ALA B . n 
C 1 38  ALA 38  30  30  ALA ALA B . n 
C 1 39  ASP 39  31  31  ASP ASP B . n 
C 1 40  VAL 40  32  32  VAL VAL B . n 
C 1 41  TYR 41  33  33  TYR TYR B . n 
C 1 42  VAL 42  34  34  VAL VAL B . n 
C 1 43  LYS 43  35  35  LYS LYS B . n 
C 1 44  LEU 44  36  36  LEU LEU B . n 
C 1 45  GLU 45  37  37  GLU GLU B . n 
C 1 46  TYR 46  38  38  TYR TYR B . n 
C 1 47  GLN 47  39  39  GLN GLN B . n 
C 1 48  ASN 48  40  40  ASN ASN B . n 
C 1 49  PRO 49  41  41  PRO PRO B . n 
C 1 50  GLY 50  42  42  GLY GLY B . n 
C 1 51  GLY 51  43  43  GLY GLY B . n 
C 1 52  SER 52  44  44  SER SER B . n 
C 1 53  VAL 53  45  45  VAL VAL B . n 
C 1 54  LLP 54  46  46  LLP LLP B . n 
C 1 55  ASP 55  47  47  ASP ASP B . n 
C 1 56  ARG 56  48  48  ARG ARG B . n 
C 1 57  ILE 57  49  49  ILE ILE B . n 
C 1 58  ALA 58  50  50  ALA ALA B . n 
C 1 59  LEU 59  51  51  LEU LEU B . n 
C 1 60  ALA 60  52  52  ALA ALA B . n 
C 1 61  MET 61  53  53  MET MET B . n 
C 1 62  ILE 62  54  54  ILE ILE B . n 
C 1 63  GLU 63  55  55  GLU GLU B . n 
C 1 64  LYS 64  56  56  LYS LYS B . n 
C 1 65  ALA 65  57  57  ALA ALA B . n 
C 1 66  GLU 66  58  58  GLU GLU B . n 
C 1 67  ARG 67  59  59  ARG ARG B . n 
C 1 68  GLU 68  60  60  GLU GLU B . n 
C 1 69  GLY 69  61  61  GLY GLY B . n 
C 1 70  LYS 70  62  62  LYS LYS B . n 
C 1 71  ILE 71  63  63  ILE ILE B . n 
C 1 72  LYS 72  64  64  LYS LYS B . n 
C 1 73  PRO 73  65  65  PRO PRO B . n 
C 1 74  GLY 74  66  66  GLY GLY B . n 
C 1 75  ASP 75  67  67  ASP ASP B . n 
C 1 76  THR 76  68  68  THR THR B . n 
C 1 77  ILE 77  69  69  ILE ILE B . n 
C 1 78  VAL 78  70  70  VAL VAL B . n 
C 1 79  GLU 79  71  71  GLU GLU B . n 
C 1 80  PRO 80  72  72  PRO PRO B . n 
C 1 81  THR 81  73  73  THR THR B . n 
C 1 82  SER 82  74  74  SER SER B . n 
C 1 83  GLY 83  75  75  GLY GLY B . n 
C 1 84  ASN 84  76  76  ASN ASN B . n 
C 1 85  THR 85  77  77  THR THR B . n 
C 1 86  GLY 86  78  78  GLY GLY B . n 
C 1 87  ILE 87  79  79  ILE ILE B . n 
C 1 88  GLY 88  80  80  GLY GLY B . n 
C 1 89  LEU 89  81  81  LEU LEU B . n 
C 1 90  ALA 90  82  82  ALA ALA B . n 
C 1 91  PHE 91  83  83  PHE PHE B . n 
C 1 92  VAL 92  84  84  VAL VAL B . n 
C 1 93  CYS 93  85  85  CYS CYS B . n 
C 1 94  ALA 94  86  86  ALA ALA B . n 
C 1 95  ALA 95  87  87  ALA ALA B . n 
C 1 96  LYS 96  88  88  LYS LYS B . n 
C 1 97  GLY 97  89  89  GLY GLY B . n 
C 1 98  TYR 98  90  90  TYR TYR B . n 
C 1 99  LYS 99  91  91  LYS LYS B . n 
C 1 100 ALA 100 92  92  ALA ALA B . n 
C 1 101 VAL 101 93  93  VAL VAL B . n 
C 1 102 PHE 102 94  94  PHE PHE B . n 
C 1 103 THR 103 95  95  THR THR B . n 
C 1 104 MET 104 96  96  MET MET B . n 
C 1 105 PRO 105 97  97  PRO PRO B . n 
C 1 106 GLU 106 98  98  GLU GLU B . n 
C 1 107 THR 107 99  99  THR THR B . n 
C 1 108 MET 108 100 100 MET MET B . n 
C 1 109 SER 109 101 101 SER SER B . n 
C 1 110 GLN 110 102 102 GLN GLN B . n 
C 1 111 GLU 111 103 103 GLU GLU B . n 
C 1 112 ARG 112 104 104 ARG ARG B . n 
C 1 113 ARG 113 105 105 ARG ARG B . n 
C 1 114 ASN 114 106 106 ASN ASN B . n 
C 1 115 LEU 115 107 107 LEU LEU B . n 
C 1 116 LEU 116 108 108 LEU LEU B . n 
C 1 117 LYS 117 109 109 LYS LYS B . n 
C 1 118 ALA 118 110 110 ALA ALA B . n 
C 1 119 TYR 119 111 111 TYR TYR B . n 
C 1 120 GLY 120 112 112 GLY GLY B . n 
C 1 121 ALA 121 113 113 ALA ALA B . n 
C 1 122 GLU 122 114 114 GLU GLU B . n 
C 1 123 LEU 123 115 115 LEU LEU B . n 
C 1 124 VAL 124 116 116 VAL VAL B . n 
C 1 125 LEU 125 117 117 LEU LEU B . n 
C 1 126 THR 126 118 118 THR THR B . n 
C 1 127 PRO 127 119 119 PRO PRO B . n 
C 1 128 GLY 128 120 120 GLY GLY B . n 
C 1 129 SER 129 121 121 SER SER B . n 
C 1 130 GLU 130 122 122 GLU GLU B . n 
C 1 131 ALA 131 123 123 ALA ALA B . n 
C 1 132 MET 132 124 124 MET MET B . n 
C 1 133 LYS 133 125 125 LYS LYS B . n 
C 1 134 GLY 134 126 126 GLY GLY B . n 
C 1 135 ALA 135 127 127 ALA ALA B . n 
C 1 136 ILE 136 128 128 ILE ILE B . n 
C 1 137 LYS 137 129 129 LYS LYS B . n 
C 1 138 LYS 138 130 130 LYS LYS B . n 
C 1 139 ALA 139 131 131 ALA ALA B . n 
C 1 140 LYS 140 132 132 LYS LYS B . n 
C 1 141 GLU 141 133 133 GLU GLU B . n 
C 1 142 LEU 142 134 134 LEU LEU B . n 
C 1 143 LYS 143 135 135 LYS LYS B . n 
C 1 144 GLU 144 136 136 GLU GLU B . n 
C 1 145 GLU 145 137 137 GLU GLU B . n 
C 1 146 HIS 146 138 138 HIS HIS B . n 
C 1 147 GLY 147 139 139 GLY GLY B . n 
C 1 148 TYR 148 140 140 TYR TYR B . n 
C 1 149 PHE 149 141 141 PHE PHE B . n 
C 1 150 GLU 150 142 142 GLU GLU B . n 
C 1 151 PRO 151 143 143 PRO PRO B . n 
C 1 152 GLN 152 144 144 GLN GLN B . n 
C 1 153 GLN 153 145 145 GLN GLN B . n 
C 1 154 PHE 154 146 146 PHE PHE B . n 
C 1 155 GLU 155 147 147 GLU GLU B . n 
C 1 156 ASN 156 148 148 ASN ASN B . n 
C 1 157 PRO 157 149 149 PRO PRO B . n 
C 1 158 ALA 158 150 150 ALA ALA B . n 
C 1 159 ASN 159 151 151 ASN ASN B . n 
C 1 160 PRO 160 152 152 PRO PRO B . n 
C 1 161 GLU 161 153 153 GLU GLU B . n 
C 1 162 VAL 162 154 154 VAL VAL B . n 
C 1 163 HIS 163 155 155 HIS HIS B . n 
C 1 164 GLU 164 156 156 GLU GLU B . n 
C 1 165 LEU 165 157 157 LEU LEU B . n 
C 1 166 THR 166 158 158 THR THR B . n 
C 1 167 THR 167 159 159 THR THR B . n 
C 1 168 GLY 168 160 160 GLY GLY B . n 
C 1 169 PRO 169 161 161 PRO PRO B . n 
C 1 170 GLU 170 162 162 GLU GLU B . n 
C 1 171 LEU 171 163 163 LEU LEU B . n 
C 1 172 LEU 172 164 164 LEU LEU B . n 
C 1 173 GLN 173 165 165 GLN GLN B . n 
C 1 174 GLN 174 166 166 GLN GLN B . n 
C 1 175 PHE 175 167 167 PHE PHE B . n 
C 1 176 GLU 176 168 168 GLU GLU B . n 
C 1 177 GLY 177 169 169 GLY GLY B . n 
C 1 178 LYS 178 170 170 LYS LYS B . n 
C 1 179 THR 179 171 171 THR THR B . n 
C 1 180 ILE 180 172 172 ILE ILE B . n 
C 1 181 ASP 181 173 173 ASP ASP B . n 
C 1 182 ALA 182 174 174 ALA ALA B . n 
C 1 183 PHE 183 175 175 PHE PHE B . n 
C 1 184 LEU 184 176 176 LEU LEU B . n 
C 1 185 ALA 185 177 177 ALA ALA B . n 
C 1 186 GLY 186 178 178 GLY GLY B . n 
C 1 187 VAL 187 179 179 VAL VAL B . n 
C 1 188 GLY 188 180 180 GLY GLY B . n 
C 1 189 THR 189 181 181 THR THR B . n 
C 1 190 GLY 190 182 182 GLY GLY B . n 
C 1 191 GLY 191 183 183 GLY GLY B . n 
C 1 192 THR 192 184 184 THR THR B . n 
C 1 193 LEU 193 185 185 LEU LEU B . n 
C 1 194 SER 194 186 186 SER SER B . n 
C 1 195 GLY 195 187 187 GLY GLY B . n 
C 1 196 VAL 196 188 188 VAL VAL B . n 
C 1 197 GLY 197 189 189 GLY GLY B . n 
C 1 198 LYS 198 190 190 LYS LYS B . n 
C 1 199 VAL 199 191 191 VAL VAL B . n 
C 1 200 LEU 200 192 192 LEU LEU B . n 
C 1 201 LYS 201 193 193 LYS LYS B . n 
C 1 202 LYS 202 194 194 LYS LYS B . n 
C 1 203 GLU 203 195 195 GLU GLU B . n 
C 1 204 TYR 204 196 196 TYR TYR B . n 
C 1 205 PRO 205 197 197 PRO PRO B . n 
C 1 206 ASN 206 198 198 ASN ASN B . n 
C 1 207 ILE 207 199 199 ILE ILE B . n 
C 1 208 GLU 208 200 200 GLU GLU B . n 
C 1 209 ILE 209 201 201 ILE ILE B . n 
C 1 210 VAL 210 202 202 VAL VAL B . n 
C 1 211 ALA 211 203 203 ALA ALA B . n 
C 1 212 ILE 212 204 204 ILE ILE B . n 
C 1 213 GLU 213 205 205 GLU GLU B . n 
C 1 214 PRO 214 206 206 PRO PRO B . n 
C 1 215 GLU 215 207 207 GLU GLU B . n 
C 1 216 ALA 216 208 208 ALA ALA B . n 
C 1 217 SER 217 209 209 SER SER B . n 
C 1 218 PRO 218 210 210 PRO PRO B . n 
C 1 219 VAL 219 211 211 VAL VAL B . n 
C 1 220 LEU 220 212 212 LEU LEU B . n 
C 1 221 SER 221 213 213 SER SER B . n 
C 1 222 GLY 222 214 214 GLY GLY B . n 
C 1 223 GLY 223 215 215 GLY GLY B . n 
C 1 224 GLU 224 216 216 GLU GLU B . n 
C 1 225 PRO 225 217 217 PRO PRO B . n 
C 1 226 GLY 226 218 218 GLY GLY B . n 
C 1 227 PRO 227 219 219 PRO PRO B . n 
C 1 228 HIS 228 220 220 HIS HIS B . n 
C 1 229 LYS 229 221 221 LYS LYS B . n 
C 1 230 LEU 230 222 222 LEU LEU B . n 
C 1 231 GLN 231 223 223 GLN GLN B . n 
C 1 232 GLY 232 224 224 GLY GLY B . n 
C 1 233 LEU 233 225 225 LEU LEU B . n 
C 1 234 GLY 234 226 226 GLY GLY B . n 
C 1 235 ALA 235 227 227 ALA ALA B . n 
C 1 236 GLY 236 228 228 GLY GLY B . n 
C 1 237 PHE 237 229 229 PHE PHE B . n 
C 1 238 ILE 238 230 230 ILE ILE B . n 
C 1 239 PRO 239 231 231 PRO PRO B . n 
C 1 240 GLY 240 232 232 GLY GLY B . n 
C 1 241 THR 241 233 233 THR THR B . n 
C 1 242 LEU 242 234 234 LEU LEU B . n 
C 1 243 ASN 243 235 235 ASN ASN B . n 
C 1 244 THR 244 236 236 THR THR B . n 
C 1 245 GLU 245 237 237 GLU GLU B . n 
C 1 246 ILE 246 238 238 ILE ILE B . n 
C 1 247 TYR 247 239 239 TYR TYR B . n 
C 1 248 ASP 248 240 240 ASP ASP B . n 
C 1 249 SER 249 241 241 SER SER B . n 
C 1 250 ILE 250 242 242 ILE ILE B . n 
C 1 251 ILE 251 243 243 ILE ILE B . n 
C 1 252 LYS 252 244 244 LYS LYS B . n 
C 1 253 VAL 253 245 245 VAL VAL B . n 
C 1 254 GLY 254 246 246 GLY GLY B . n 
C 1 255 ASN 255 247 247 ASN ASN B . n 
C 1 256 ASP 256 248 248 ASP ASP B . n 
C 1 257 THR 257 249 249 THR THR B . n 
C 1 258 ALA 258 250 250 ALA ALA B . n 
C 1 259 MET 259 251 251 MET MET B . n 
C 1 260 GLU 260 252 252 GLU GLU B . n 
C 1 261 MET 261 253 253 MET MET B . n 
C 1 262 SER 262 254 254 SER SER B . n 
C 1 263 ARG 263 255 255 ARG ARG B . n 
C 1 264 ARG 264 256 256 ARG ARG B . n 
C 1 265 VAL 265 257 257 VAL VAL B . n 
C 1 266 ALA 266 258 258 ALA ALA B . n 
C 1 267 LYS 267 259 259 LYS LYS B . n 
C 1 268 GLU 268 260 260 GLU GLU B . n 
C 1 269 GLU 269 261 261 GLU GLU B . n 
C 1 270 GLY 270 262 262 GLY GLY B . n 
C 1 271 ILE 271 263 263 ILE ILE B . n 
C 1 272 LEU 272 264 264 LEU LEU B . n 
C 1 273 ALA 273 265 265 ALA ALA B . n 
C 1 274 GLY 274 266 266 GLY GLY B . n 
C 1 275 ILE 275 267 267 ILE ILE B . n 
C 1 276 SER 276 268 268 SER SER B . n 
C 1 277 SER 277 269 269 SER SER B . n 
C 1 278 GLY 278 270 270 GLY GLY B . n 
C 1 279 ALA 279 271 271 ALA ALA B . n 
C 1 280 ALA 280 272 272 ALA ALA B . n 
C 1 281 ILE 281 273 273 ILE ILE B . n 
C 1 282 TYR 282 274 274 TYR TYR B . n 
C 1 283 ALA 283 275 275 ALA ALA B . n 
C 1 284 ALA 284 276 276 ALA ALA B . n 
C 1 285 ILE 285 277 277 ILE ILE B . n 
C 1 286 GLN 286 278 278 GLN GLN B . n 
C 1 287 LYS 287 279 279 LYS LYS B . n 
C 1 288 ALA 288 280 280 ALA ALA B . n 
C 1 289 LYS 289 281 281 LYS LYS B . n 
C 1 290 GLU 290 282 282 GLU GLU B . n 
C 1 291 LEU 291 283 283 LEU LEU B . n 
C 1 292 GLY 292 284 284 GLY GLY B . n 
C 1 293 LYS 293 285 285 LYS LYS B . n 
C 1 294 GLY 294 286 286 GLY GLY B . n 
C 1 295 LYS 295 287 287 LYS LYS B . n 
C 1 296 THR 296 288 288 THR THR B . n 
C 1 297 VAL 297 289 289 VAL VAL B . n 
C 1 298 VAL 298 290 290 VAL VAL B . n 
C 1 299 THR 299 291 291 THR THR B . n 
C 1 300 VAL 300 292 292 VAL VAL B . n 
C 1 301 LEU 301 293 293 LEU LEU B . n 
C 1 302 PRO 302 294 294 PRO PRO B . n 
C 1 303 SER 303 295 295 SER SER B . n 
C 1 304 ASN 304 296 296 ASN ASN B . n 
C 1 305 GLY 305 297 297 GLY GLY B . n 
C 1 306 GLU 306 298 298 GLU GLU B . n 
C 1 307 ARG 307 299 299 ARG ARG B . n 
C 1 308 TYR 308 300 300 TYR TYR B . n 
C 1 309 LEU 309 301 301 LEU LEU B . n 
C 1 310 SER 310 302 302 SER SER B . n 
C 1 311 THR 311 303 303 THR THR B . n 
C 1 312 PRO 312 304 304 PRO PRO B . n 
C 1 313 LEU 313 305 305 LEU LEU B . n 
C 1 314 TYR 314 306 306 TYR TYR B . n 
C 1 315 SER 315 307 307 SER SER B . n 
C 1 316 PHE 316 308 ?   ?   ?   B . n 
C 1 317 ASP 317 309 ?   ?   ?   B . n 
C 1 318 ASP 318 310 ?   ?   ?   B . n 
D 1 1   MET 1   -7  ?   ?   ?   C . n 
D 1 2   GLY 2   -6  ?   ?   ?   C . n 
D 1 3   HIS 3   -5  ?   ?   ?   C . n 
D 1 4   HIS 4   -4  ?   ?   ?   C . n 
D 1 5   HIS 5   -3  ?   ?   ?   C . n 
D 1 6   HIS 6   -2  ?   ?   ?   C . n 
D 1 7   HIS 7   -1  ?   ?   ?   C . n 
D 1 8   HIS 8   0   ?   ?   ?   C . n 
D 1 9   MET 9   1   1   MET MET C . n 
D 1 10  ALA 10  2   2   ALA ALA C . n 
D 1 11  GLN 11  3   3   GLN GLN C . n 
D 1 12  LYS 12  4   4   LYS LYS C . n 
D 1 13  PRO 13  5   5   PRO PRO C . n 
D 1 14  VAL 14  6   6   VAL VAL C . n 
D 1 15  ASP 15  7   7   ASP ASP C . n 
D 1 16  ASN 16  8   8   ASN ASN C . n 
D 1 17  ILE 17  9   9   ILE ILE C . n 
D 1 18  THR 18  10  10  THR THR C . n 
D 1 19  GLN 19  11  11  GLN GLN C . n 
D 1 20  ILE 20  12  12  ILE ILE C . n 
D 1 21  ILE 21  13  13  ILE ILE C . n 
D 1 22  GLY 22  14  14  GLY GLY C . n 
D 1 23  GLY 23  15  15  GLY GLY C . n 
D 1 24  THR 24  16  16  THR THR C . n 
D 1 25  PRO 25  17  17  PRO PRO C . n 
D 1 26  VAL 26  18  18  VAL VAL C . n 
D 1 27  VAL 27  19  19  VAL VAL C . n 
D 1 28  LYS 28  20  20  LYS LYS C . n 
D 1 29  LEU 29  21  21  LEU LEU C . n 
D 1 30  ARG 30  22  22  ARG ARG C . n 
D 1 31  ASN 31  23  23  ASN ASN C . n 
D 1 32  VAL 32  24  24  VAL VAL C . n 
D 1 33  VAL 33  25  25  VAL VAL C . n 
D 1 34  ASP 34  26  26  ASP ASP C . n 
D 1 35  ASP 35  27  27  ASP ASP C . n 
D 1 36  ASN 36  28  28  ASN ASN C . n 
D 1 37  ALA 37  29  29  ALA ALA C . n 
D 1 38  ALA 38  30  30  ALA ALA C . n 
D 1 39  ASP 39  31  31  ASP ASP C . n 
D 1 40  VAL 40  32  32  VAL VAL C . n 
D 1 41  TYR 41  33  33  TYR TYR C . n 
D 1 42  VAL 42  34  34  VAL VAL C . n 
D 1 43  LYS 43  35  35  LYS LYS C . n 
D 1 44  LEU 44  36  36  LEU LEU C . n 
D 1 45  GLU 45  37  37  GLU GLU C . n 
D 1 46  TYR 46  38  38  TYR TYR C . n 
D 1 47  GLN 47  39  39  GLN GLN C . n 
D 1 48  ASN 48  40  40  ASN ASN C . n 
D 1 49  PRO 49  41  41  PRO PRO C . n 
D 1 50  GLY 50  42  42  GLY GLY C . n 
D 1 51  GLY 51  43  43  GLY GLY C . n 
D 1 52  SER 52  44  44  SER SER C . n 
D 1 53  VAL 53  45  45  VAL VAL C . n 
D 1 54  LLP 54  46  46  LLP LLP C . n 
D 1 55  ASP 55  47  47  ASP ASP C . n 
D 1 56  ARG 56  48  48  ARG ARG C . n 
D 1 57  ILE 57  49  49  ILE ILE C . n 
D 1 58  ALA 58  50  50  ALA ALA C . n 
D 1 59  LEU 59  51  51  LEU LEU C . n 
D 1 60  ALA 60  52  52  ALA ALA C . n 
D 1 61  MET 61  53  53  MET MET C . n 
D 1 62  ILE 62  54  54  ILE ILE C . n 
D 1 63  GLU 63  55  55  GLU GLU C . n 
D 1 64  LYS 64  56  56  LYS LYS C . n 
D 1 65  ALA 65  57  57  ALA ALA C . n 
D 1 66  GLU 66  58  58  GLU GLU C . n 
D 1 67  ARG 67  59  59  ARG ARG C . n 
D 1 68  GLU 68  60  60  GLU GLU C . n 
D 1 69  GLY 69  61  61  GLY GLY C . n 
D 1 70  LYS 70  62  62  LYS LYS C . n 
D 1 71  ILE 71  63  63  ILE ILE C . n 
D 1 72  LYS 72  64  64  LYS LYS C . n 
D 1 73  PRO 73  65  65  PRO PRO C . n 
D 1 74  GLY 74  66  66  GLY GLY C . n 
D 1 75  ASP 75  67  67  ASP ASP C . n 
D 1 76  THR 76  68  68  THR THR C . n 
D 1 77  ILE 77  69  69  ILE ILE C . n 
D 1 78  VAL 78  70  70  VAL VAL C . n 
D 1 79  GLU 79  71  71  GLU GLU C . n 
D 1 80  PRO 80  72  72  PRO PRO C . n 
D 1 81  THR 81  73  73  THR THR C . n 
D 1 82  SER 82  74  74  SER SER C . n 
D 1 83  GLY 83  75  75  GLY GLY C . n 
D 1 84  ASN 84  76  76  ASN ASN C . n 
D 1 85  THR 85  77  77  THR THR C . n 
D 1 86  GLY 86  78  78  GLY GLY C . n 
D 1 87  ILE 87  79  79  ILE ILE C . n 
D 1 88  GLY 88  80  80  GLY GLY C . n 
D 1 89  LEU 89  81  81  LEU LEU C . n 
D 1 90  ALA 90  82  82  ALA ALA C . n 
D 1 91  PHE 91  83  83  PHE PHE C . n 
D 1 92  VAL 92  84  84  VAL VAL C . n 
D 1 93  CYS 93  85  85  CYS CYS C . n 
D 1 94  ALA 94  86  86  ALA ALA C . n 
D 1 95  ALA 95  87  87  ALA ALA C . n 
D 1 96  LYS 96  88  88  LYS LYS C . n 
D 1 97  GLY 97  89  89  GLY GLY C . n 
D 1 98  TYR 98  90  90  TYR TYR C . n 
D 1 99  LYS 99  91  91  LYS LYS C . n 
D 1 100 ALA 100 92  92  ALA ALA C . n 
D 1 101 VAL 101 93  93  VAL VAL C . n 
D 1 102 PHE 102 94  94  PHE PHE C . n 
D 1 103 THR 103 95  95  THR THR C . n 
D 1 104 MET 104 96  96  MET MET C . n 
D 1 105 PRO 105 97  97  PRO PRO C . n 
D 1 106 GLU 106 98  98  GLU GLU C . n 
D 1 107 THR 107 99  99  THR THR C . n 
D 1 108 MET 108 100 100 MET MET C . n 
D 1 109 SER 109 101 101 SER SER C . n 
D 1 110 GLN 110 102 102 GLN GLN C . n 
D 1 111 GLU 111 103 103 GLU GLU C . n 
D 1 112 ARG 112 104 104 ARG ARG C . n 
D 1 113 ARG 113 105 105 ARG ARG C . n 
D 1 114 ASN 114 106 106 ASN ASN C . n 
D 1 115 LEU 115 107 107 LEU LEU C . n 
D 1 116 LEU 116 108 108 LEU LEU C . n 
D 1 117 LYS 117 109 109 LYS LYS C . n 
D 1 118 ALA 118 110 110 ALA ALA C . n 
D 1 119 TYR 119 111 111 TYR TYR C . n 
D 1 120 GLY 120 112 112 GLY GLY C . n 
D 1 121 ALA 121 113 113 ALA ALA C . n 
D 1 122 GLU 122 114 114 GLU GLU C . n 
D 1 123 LEU 123 115 115 LEU LEU C . n 
D 1 124 VAL 124 116 116 VAL VAL C . n 
D 1 125 LEU 125 117 117 LEU LEU C . n 
D 1 126 THR 126 118 118 THR THR C . n 
D 1 127 PRO 127 119 119 PRO PRO C . n 
D 1 128 GLY 128 120 120 GLY GLY C . n 
D 1 129 SER 129 121 121 SER SER C . n 
D 1 130 GLU 130 122 122 GLU GLU C . n 
D 1 131 ALA 131 123 123 ALA ALA C . n 
D 1 132 MET 132 124 124 MET MET C . n 
D 1 133 LYS 133 125 125 LYS LYS C . n 
D 1 134 GLY 134 126 126 GLY GLY C . n 
D 1 135 ALA 135 127 127 ALA ALA C . n 
D 1 136 ILE 136 128 128 ILE ILE C . n 
D 1 137 LYS 137 129 129 LYS LYS C . n 
D 1 138 LYS 138 130 130 LYS LYS C . n 
D 1 139 ALA 139 131 131 ALA ALA C . n 
D 1 140 LYS 140 132 132 LYS LYS C . n 
D 1 141 GLU 141 133 133 GLU GLU C . n 
D 1 142 LEU 142 134 134 LEU LEU C . n 
D 1 143 LYS 143 135 135 LYS LYS C . n 
D 1 144 GLU 144 136 136 GLU GLU C . n 
D 1 145 GLU 145 137 137 GLU GLU C . n 
D 1 146 HIS 146 138 138 HIS HIS C . n 
D 1 147 GLY 147 139 139 GLY GLY C . n 
D 1 148 TYR 148 140 140 TYR TYR C . n 
D 1 149 PHE 149 141 141 PHE PHE C . n 
D 1 150 GLU 150 142 142 GLU GLU C . n 
D 1 151 PRO 151 143 143 PRO PRO C . n 
D 1 152 GLN 152 144 144 GLN GLN C . n 
D 1 153 GLN 153 145 145 GLN GLN C . n 
D 1 154 PHE 154 146 146 PHE PHE C . n 
D 1 155 GLU 155 147 147 GLU GLU C . n 
D 1 156 ASN 156 148 148 ASN ASN C . n 
D 1 157 PRO 157 149 149 PRO PRO C . n 
D 1 158 ALA 158 150 150 ALA ALA C . n 
D 1 159 ASN 159 151 151 ASN ASN C . n 
D 1 160 PRO 160 152 152 PRO PRO C . n 
D 1 161 GLU 161 153 153 GLU GLU C . n 
D 1 162 VAL 162 154 154 VAL VAL C . n 
D 1 163 HIS 163 155 155 HIS HIS C . n 
D 1 164 GLU 164 156 156 GLU GLU C . n 
D 1 165 LEU 165 157 157 LEU LEU C . n 
D 1 166 THR 166 158 158 THR THR C . n 
D 1 167 THR 167 159 159 THR THR C . n 
D 1 168 GLY 168 160 160 GLY GLY C . n 
D 1 169 PRO 169 161 161 PRO PRO C . n 
D 1 170 GLU 170 162 162 GLU GLU C . n 
D 1 171 LEU 171 163 163 LEU LEU C . n 
D 1 172 LEU 172 164 164 LEU LEU C . n 
D 1 173 GLN 173 165 165 GLN GLN C . n 
D 1 174 GLN 174 166 166 GLN GLN C . n 
D 1 175 PHE 175 167 167 PHE PHE C . n 
D 1 176 GLU 176 168 168 GLU GLU C . n 
D 1 177 GLY 177 169 169 GLY GLY C . n 
D 1 178 LYS 178 170 170 LYS LYS C . n 
D 1 179 THR 179 171 171 THR THR C . n 
D 1 180 ILE 180 172 172 ILE ILE C . n 
D 1 181 ASP 181 173 173 ASP ASP C . n 
D 1 182 ALA 182 174 174 ALA ALA C . n 
D 1 183 PHE 183 175 175 PHE PHE C . n 
D 1 184 LEU 184 176 176 LEU LEU C . n 
D 1 185 ALA 185 177 177 ALA ALA C . n 
D 1 186 GLY 186 178 178 GLY GLY C . n 
D 1 187 VAL 187 179 179 VAL VAL C . n 
D 1 188 GLY 188 180 180 GLY GLY C . n 
D 1 189 THR 189 181 181 THR THR C . n 
D 1 190 GLY 190 182 182 GLY GLY C . n 
D 1 191 GLY 191 183 183 GLY GLY C . n 
D 1 192 THR 192 184 184 THR THR C . n 
D 1 193 LEU 193 185 185 LEU LEU C . n 
D 1 194 SER 194 186 186 SER SER C . n 
D 1 195 GLY 195 187 187 GLY GLY C . n 
D 1 196 VAL 196 188 188 VAL VAL C . n 
D 1 197 GLY 197 189 189 GLY GLY C . n 
D 1 198 LYS 198 190 190 LYS LYS C . n 
D 1 199 VAL 199 191 191 VAL VAL C . n 
D 1 200 LEU 200 192 192 LEU LEU C . n 
D 1 201 LYS 201 193 193 LYS LYS C . n 
D 1 202 LYS 202 194 194 LYS LYS C . n 
D 1 203 GLU 203 195 195 GLU GLU C . n 
D 1 204 TYR 204 196 196 TYR TYR C . n 
D 1 205 PRO 205 197 197 PRO PRO C . n 
D 1 206 ASN 206 198 198 ASN ASN C . n 
D 1 207 ILE 207 199 199 ILE ILE C . n 
D 1 208 GLU 208 200 200 GLU GLU C . n 
D 1 209 ILE 209 201 201 ILE ILE C . n 
D 1 210 VAL 210 202 202 VAL VAL C . n 
D 1 211 ALA 211 203 203 ALA ALA C . n 
D 1 212 ILE 212 204 204 ILE ILE C . n 
D 1 213 GLU 213 205 205 GLU GLU C . n 
D 1 214 PRO 214 206 206 PRO PRO C . n 
D 1 215 GLU 215 207 207 GLU GLU C . n 
D 1 216 ALA 216 208 208 ALA ALA C . n 
D 1 217 SER 217 209 209 SER SER C . n 
D 1 218 PRO 218 210 210 PRO PRO C . n 
D 1 219 VAL 219 211 211 VAL VAL C . n 
D 1 220 LEU 220 212 212 LEU LEU C . n 
D 1 221 SER 221 213 213 SER SER C . n 
D 1 222 GLY 222 214 214 GLY GLY C . n 
D 1 223 GLY 223 215 215 GLY GLY C . n 
D 1 224 GLU 224 216 216 GLU GLU C . n 
D 1 225 PRO 225 217 217 PRO PRO C . n 
D 1 226 GLY 226 218 218 GLY GLY C . n 
D 1 227 PRO 227 219 219 PRO PRO C . n 
D 1 228 HIS 228 220 220 HIS HIS C . n 
D 1 229 LYS 229 221 221 LYS LYS C . n 
D 1 230 LEU 230 222 222 LEU LEU C . n 
D 1 231 GLN 231 223 223 GLN GLN C . n 
D 1 232 GLY 232 224 224 GLY GLY C . n 
D 1 233 LEU 233 225 225 LEU LEU C . n 
D 1 234 GLY 234 226 226 GLY GLY C . n 
D 1 235 ALA 235 227 227 ALA ALA C . n 
D 1 236 GLY 236 228 228 GLY GLY C . n 
D 1 237 PHE 237 229 229 PHE PHE C . n 
D 1 238 ILE 238 230 230 ILE ILE C . n 
D 1 239 PRO 239 231 231 PRO PRO C . n 
D 1 240 GLY 240 232 232 GLY GLY C . n 
D 1 241 THR 241 233 233 THR THR C . n 
D 1 242 LEU 242 234 234 LEU LEU C . n 
D 1 243 ASN 243 235 235 ASN ASN C . n 
D 1 244 THR 244 236 236 THR THR C . n 
D 1 245 GLU 245 237 237 GLU GLU C . n 
D 1 246 ILE 246 238 238 ILE ILE C . n 
D 1 247 TYR 247 239 239 TYR TYR C . n 
D 1 248 ASP 248 240 240 ASP ASP C . n 
D 1 249 SER 249 241 241 SER SER C . n 
D 1 250 ILE 250 242 242 ILE ILE C . n 
D 1 251 ILE 251 243 243 ILE ILE C . n 
D 1 252 LYS 252 244 244 LYS LYS C . n 
D 1 253 VAL 253 245 245 VAL VAL C . n 
D 1 254 GLY 254 246 246 GLY GLY C . n 
D 1 255 ASN 255 247 247 ASN ASN C . n 
D 1 256 ASP 256 248 248 ASP ASP C . n 
D 1 257 THR 257 249 249 THR THR C . n 
D 1 258 ALA 258 250 250 ALA ALA C . n 
D 1 259 MET 259 251 251 MET MET C . n 
D 1 260 GLU 260 252 252 GLU GLU C . n 
D 1 261 MET 261 253 253 MET MET C . n 
D 1 262 SER 262 254 254 SER SER C . n 
D 1 263 ARG 263 255 255 ARG ARG C . n 
D 1 264 ARG 264 256 256 ARG ARG C . n 
D 1 265 VAL 265 257 257 VAL VAL C . n 
D 1 266 ALA 266 258 258 ALA ALA C . n 
D 1 267 LYS 267 259 259 LYS LYS C . n 
D 1 268 GLU 268 260 260 GLU GLU C . n 
D 1 269 GLU 269 261 261 GLU GLU C . n 
D 1 270 GLY 270 262 262 GLY GLY C . n 
D 1 271 ILE 271 263 263 ILE ILE C . n 
D 1 272 LEU 272 264 264 LEU LEU C . n 
D 1 273 ALA 273 265 265 ALA ALA C . n 
D 1 274 GLY 274 266 266 GLY GLY C . n 
D 1 275 ILE 275 267 267 ILE ILE C . n 
D 1 276 SER 276 268 268 SER SER C . n 
D 1 277 SER 277 269 269 SER SER C . n 
D 1 278 GLY 278 270 270 GLY GLY C . n 
D 1 279 ALA 279 271 271 ALA ALA C . n 
D 1 280 ALA 280 272 272 ALA ALA C . n 
D 1 281 ILE 281 273 273 ILE ILE C . n 
D 1 282 TYR 282 274 274 TYR TYR C . n 
D 1 283 ALA 283 275 275 ALA ALA C . n 
D 1 284 ALA 284 276 276 ALA ALA C . n 
D 1 285 ILE 285 277 277 ILE ILE C . n 
D 1 286 GLN 286 278 278 GLN GLN C . n 
D 1 287 LYS 287 279 279 LYS LYS C . n 
D 1 288 ALA 288 280 280 ALA ALA C . n 
D 1 289 LYS 289 281 281 LYS LYS C . n 
D 1 290 GLU 290 282 282 GLU GLU C . n 
D 1 291 LEU 291 283 283 LEU LEU C . n 
D 1 292 GLY 292 284 284 GLY GLY C . n 
D 1 293 LYS 293 285 285 LYS LYS C . n 
D 1 294 GLY 294 286 286 GLY GLY C . n 
D 1 295 LYS 295 287 287 LYS LYS C . n 
D 1 296 THR 296 288 288 THR THR C . n 
D 1 297 VAL 297 289 289 VAL VAL C . n 
D 1 298 VAL 298 290 290 VAL VAL C . n 
D 1 299 THR 299 291 291 THR THR C . n 
D 1 300 VAL 300 292 292 VAL VAL C . n 
D 1 301 LEU 301 293 293 LEU LEU C . n 
D 1 302 PRO 302 294 294 PRO PRO C . n 
D 1 303 SER 303 295 295 SER SER C . n 
D 1 304 ASN 304 296 296 ASN ASN C . n 
D 1 305 GLY 305 297 297 GLY GLY C . n 
D 1 306 GLU 306 298 298 GLU GLU C . n 
D 1 307 ARG 307 299 299 ARG ARG C . n 
D 1 308 TYR 308 300 300 TYR TYR C . n 
D 1 309 LEU 309 301 301 LEU LEU C . n 
D 1 310 SER 310 302 302 SER SER C . n 
D 1 311 THR 311 303 303 THR THR C . n 
D 1 312 PRO 312 304 304 PRO PRO C . n 
D 1 313 LEU 313 305 305 LEU LEU C . n 
D 1 314 TYR 314 306 306 TYR TYR C . n 
D 1 315 SER 315 307 307 SER SER C . n 
D 1 316 PHE 316 308 ?   ?   ?   C . n 
D 1 317 ASP 317 309 ?   ?   ?   C . n 
D 1 318 ASP 318 310 ?   ?   ?   C . n 
E 2 1   TYR 1   1   1   TYR TYR E . n 
E 2 2   MET 2   2   2   MET MET E . n 
E 2 3   NAL 3   3   3   NAL NAL E . n 
E 2 4   TYR 4   4   4   TYR TYR E . n 
E 2 5   ILE 5   5   5   ILE ILE E . n 
F 2 1   TYR 1   1   1   TYR TYR F . n 
F 2 2   MET 2   2   2   MET MET F . n 
F 2 3   NAL 3   3   3   NAL NAL F . n 
F 2 4   TYR 4   4   4   TYR TYR F . n 
F 2 5   ILE 5   5   5   ILE ILE F . n 
G 2 1   TYR 1   1   1   TYR TYR G . n 
G 2 2   MET 2   2   2   MET MET G . n 
G 2 3   NAL 3   3   3   NAL NAL G . n 
G 2 4   TYR 4   4   4   TYR TYR G . n 
G 2 5   ILE 5   5   5   ILE ILE G . n 
H 2 1   TYR 1   1   1   TYR TYR H . n 
H 2 2   MET 2   2   2   MET MET H . n 
H 2 3   NAL 3   3   3   NAL NAL H . n 
H 2 4   TYR 4   4   4   TYR TYR H . n 
H 2 5   ILE 5   5   5   ILE ILE H . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NAL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NAL 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
I 3 HOH 1   401 160 HOH HOH A . 
I 3 HOH 2   402 213 HOH HOH A . 
I 3 HOH 3   403 226 HOH HOH A . 
I 3 HOH 4   404 510 HOH HOH A . 
I 3 HOH 5   405 461 HOH HOH A . 
I 3 HOH 6   406 161 HOH HOH A . 
I 3 HOH 7   407 552 HOH HOH A . 
I 3 HOH 8   408 28  HOH HOH A . 
I 3 HOH 9   409 475 HOH HOH A . 
I 3 HOH 10  410 164 HOH HOH A . 
I 3 HOH 11  411 242 HOH HOH A . 
I 3 HOH 12  412 135 HOH HOH A . 
I 3 HOH 13  413 86  HOH HOH A . 
I 3 HOH 14  414 186 HOH HOH A . 
I 3 HOH 15  415 20  HOH HOH A . 
I 3 HOH 16  416 34  HOH HOH A . 
I 3 HOH 17  417 220 HOH HOH A . 
I 3 HOH 18  418 7   HOH HOH A . 
I 3 HOH 19  419 425 HOH HOH A . 
I 3 HOH 20  420 4   HOH HOH A . 
I 3 HOH 21  421 254 HOH HOH A . 
I 3 HOH 22  422 350 HOH HOH A . 
I 3 HOH 23  423 272 HOH HOH A . 
I 3 HOH 24  424 448 HOH HOH A . 
I 3 HOH 25  425 57  HOH HOH A . 
I 3 HOH 26  426 187 HOH HOH A . 
I 3 HOH 27  427 188 HOH HOH A . 
I 3 HOH 28  428 134 HOH HOH A . 
I 3 HOH 29  429 281 HOH HOH A . 
I 3 HOH 30  430 241 HOH HOH A . 
I 3 HOH 31  431 66  HOH HOH A . 
I 3 HOH 32  432 196 HOH HOH A . 
I 3 HOH 33  433 125 HOH HOH A . 
I 3 HOH 34  434 275 HOH HOH A . 
I 3 HOH 35  435 14  HOH HOH A . 
I 3 HOH 36  436 194 HOH HOH A . 
I 3 HOH 37  437 147 HOH HOH A . 
I 3 HOH 38  438 58  HOH HOH A . 
I 3 HOH 39  439 77  HOH HOH A . 
I 3 HOH 40  440 30  HOH HOH A . 
I 3 HOH 41  441 84  HOH HOH A . 
I 3 HOH 42  442 63  HOH HOH A . 
I 3 HOH 43  443 394 HOH HOH A . 
I 3 HOH 44  444 446 HOH HOH A . 
I 3 HOH 45  445 129 HOH HOH A . 
I 3 HOH 46  446 112 HOH HOH A . 
I 3 HOH 47  447 55  HOH HOH A . 
I 3 HOH 48  448 144 HOH HOH A . 
I 3 HOH 49  449 185 HOH HOH A . 
I 3 HOH 50  450 369 HOH HOH A . 
I 3 HOH 51  451 49  HOH HOH A . 
I 3 HOH 52  452 32  HOH HOH A . 
I 3 HOH 53  453 427 HOH HOH A . 
I 3 HOH 54  454 534 HOH HOH A . 
I 3 HOH 55  455 22  HOH HOH A . 
I 3 HOH 56  456 172 HOH HOH A . 
I 3 HOH 57  457 6   HOH HOH A . 
I 3 HOH 58  458 126 HOH HOH A . 
I 3 HOH 59  459 46  HOH HOH A . 
I 3 HOH 60  460 236 HOH HOH A . 
I 3 HOH 61  461 142 HOH HOH A . 
I 3 HOH 62  462 245 HOH HOH A . 
I 3 HOH 63  463 41  HOH HOH A . 
I 3 HOH 64  464 382 HOH HOH A . 
I 3 HOH 65  465 83  HOH HOH A . 
I 3 HOH 66  466 368 HOH HOH A . 
I 3 HOH 67  467 75  HOH HOH A . 
I 3 HOH 68  468 486 HOH HOH A . 
I 3 HOH 69  469 524 HOH HOH A . 
I 3 HOH 70  470 24  HOH HOH A . 
I 3 HOH 71  471 90  HOH HOH A . 
I 3 HOH 72  472 76  HOH HOH A . 
I 3 HOH 73  473 397 HOH HOH A . 
I 3 HOH 74  474 252 HOH HOH A . 
I 3 HOH 75  475 79  HOH HOH A . 
I 3 HOH 76  476 113 HOH HOH A . 
I 3 HOH 77  477 117 HOH HOH A . 
I 3 HOH 78  478 308 HOH HOH A . 
I 3 HOH 79  479 529 HOH HOH A . 
I 3 HOH 80  480 298 HOH HOH A . 
I 3 HOH 81  481 18  HOH HOH A . 
I 3 HOH 82  482 471 HOH HOH A . 
I 3 HOH 83  483 219 HOH HOH A . 
I 3 HOH 84  484 412 HOH HOH A . 
I 3 HOH 85  485 251 HOH HOH A . 
I 3 HOH 86  486 82  HOH HOH A . 
I 3 HOH 87  487 481 HOH HOH A . 
I 3 HOH 88  488 420 HOH HOH A . 
I 3 HOH 89  489 150 HOH HOH A . 
I 3 HOH 90  490 483 HOH HOH A . 
I 3 HOH 91  491 366 HOH HOH A . 
I 3 HOH 92  492 224 HOH HOH A . 
I 3 HOH 93  493 333 HOH HOH A . 
I 3 HOH 94  494 434 HOH HOH A . 
I 3 HOH 95  495 527 HOH HOH A . 
I 3 HOH 96  496 198 HOH HOH A . 
I 3 HOH 97  497 560 HOH HOH A . 
I 3 HOH 98  498 530 HOH HOH A . 
I 3 HOH 99  499 559 HOH HOH A . 
I 3 HOH 100 500 286 HOH HOH A . 
I 3 HOH 101 501 78  HOH HOH A . 
I 3 HOH 102 502 373 HOH HOH A . 
I 3 HOH 103 503 315 HOH HOH A . 
I 3 HOH 104 504 523 HOH HOH A . 
I 3 HOH 105 505 557 HOH HOH A . 
I 3 HOH 106 506 311 HOH HOH A . 
I 3 HOH 107 507 152 HOH HOH A . 
I 3 HOH 108 508 553 HOH HOH A . 
I 3 HOH 109 509 387 HOH HOH A . 
I 3 HOH 110 510 87  HOH HOH A . 
I 3 HOH 111 511 536 HOH HOH A . 
I 3 HOH 112 512 318 HOH HOH A . 
I 3 HOH 113 513 136 HOH HOH A . 
I 3 HOH 114 514 379 HOH HOH A . 
I 3 HOH 115 515 554 HOH HOH A . 
I 3 HOH 116 516 71  HOH HOH A . 
I 3 HOH 117 517 445 HOH HOH A . 
I 3 HOH 118 518 182 HOH HOH A . 
I 3 HOH 119 519 489 HOH HOH A . 
I 3 HOH 120 520 197 HOH HOH A . 
I 3 HOH 121 521 464 HOH HOH A . 
I 3 HOH 122 522 431 HOH HOH A . 
I 3 HOH 123 523 268 HOH HOH A . 
I 3 HOH 124 524 322 HOH HOH A . 
I 3 HOH 125 525 507 HOH HOH A . 
I 3 HOH 126 526 271 HOH HOH A . 
I 3 HOH 127 527 287 HOH HOH A . 
I 3 HOH 128 528 419 HOH HOH A . 
I 3 HOH 129 529 566 HOH HOH A . 
I 3 HOH 130 530 277 HOH HOH A . 
I 3 HOH 131 531 327 HOH HOH A . 
I 3 HOH 132 532 479 HOH HOH A . 
I 3 HOH 133 533 437 HOH HOH A . 
I 3 HOH 134 534 258 HOH HOH A . 
I 3 HOH 135 535 398 HOH HOH A . 
I 3 HOH 136 536 468 HOH HOH A . 
I 3 HOH 137 537 138 HOH HOH A . 
I 3 HOH 138 538 493 HOH HOH A . 
I 3 HOH 139 539 550 HOH HOH A . 
I 3 HOH 140 540 540 HOH HOH A . 
I 3 HOH 141 541 225 HOH HOH A . 
I 3 HOH 142 542 522 HOH HOH A . 
I 3 HOH 143 543 421 HOH HOH A . 
I 3 HOH 144 544 109 HOH HOH A . 
I 3 HOH 145 545 453 HOH HOH A . 
I 3 HOH 146 546 299 HOH HOH A . 
I 3 HOH 147 547 491 HOH HOH A . 
I 3 HOH 148 548 291 HOH HOH A . 
I 3 HOH 149 549 564 HOH HOH A . 
I 3 HOH 150 550 303 HOH HOH A . 
I 3 HOH 151 551 538 HOH HOH A . 
I 3 HOH 152 552 192 HOH HOH A . 
I 3 HOH 153 553 497 HOH HOH A . 
I 3 HOH 154 554 393 HOH HOH A . 
I 3 HOH 155 555 307 HOH HOH A . 
I 3 HOH 156 556 504 HOH HOH A . 
I 3 HOH 157 557 177 HOH HOH A . 
I 3 HOH 158 558 462 HOH HOH A . 
I 3 HOH 159 559 263 HOH HOH A . 
J 3 HOH 1   401 345 HOH HOH D . 
J 3 HOH 2   402 432 HOH HOH D . 
J 3 HOH 3   403 484 HOH HOH D . 
J 3 HOH 4   404 151 HOH HOH D . 
J 3 HOH 5   405 256 HOH HOH D . 
J 3 HOH 6   406 454 HOH HOH D . 
J 3 HOH 7   407 155 HOH HOH D . 
J 3 HOH 8   408 1   HOH HOH D . 
J 3 HOH 9   409 178 HOH HOH D . 
J 3 HOH 10  410 33  HOH HOH D . 
J 3 HOH 11  411 430 HOH HOH D . 
J 3 HOH 12  412 107 HOH HOH D . 
J 3 HOH 13  413 12  HOH HOH D . 
J 3 HOH 14  414 244 HOH HOH D . 
J 3 HOH 15  415 191 HOH HOH D . 
J 3 HOH 16  416 203 HOH HOH D . 
J 3 HOH 17  417 38  HOH HOH D . 
J 3 HOH 18  418 44  HOH HOH D . 
J 3 HOH 19  419 54  HOH HOH D . 
J 3 HOH 20  420 5   HOH HOH D . 
J 3 HOH 21  421 357 HOH HOH D . 
J 3 HOH 22  422 511 HOH HOH D . 
J 3 HOH 23  423 183 HOH HOH D . 
J 3 HOH 24  424 358 HOH HOH D . 
J 3 HOH 25  425 284 HOH HOH D . 
J 3 HOH 26  426 347 HOH HOH D . 
J 3 HOH 27  427 137 HOH HOH D . 
J 3 HOH 28  428 503 HOH HOH D . 
J 3 HOH 29  429 60  HOH HOH D . 
J 3 HOH 30  430 499 HOH HOH D . 
J 3 HOH 31  431 13  HOH HOH D . 
J 3 HOH 32  432 105 HOH HOH D . 
J 3 HOH 33  433 104 HOH HOH D . 
J 3 HOH 34  434 228 HOH HOH D . 
J 3 HOH 35  435 447 HOH HOH D . 
J 3 HOH 36  436 52  HOH HOH D . 
J 3 HOH 37  437 16  HOH HOH D . 
J 3 HOH 38  438 262 HOH HOH D . 
J 3 HOH 39  439 154 HOH HOH D . 
J 3 HOH 40  440 210 HOH HOH D . 
J 3 HOH 41  441 248 HOH HOH D . 
J 3 HOH 42  442 338 HOH HOH D . 
J 3 HOH 43  443 148 HOH HOH D . 
J 3 HOH 44  444 273 HOH HOH D . 
J 3 HOH 45  445 302 HOH HOH D . 
J 3 HOH 46  446 163 HOH HOH D . 
J 3 HOH 47  447 342 HOH HOH D . 
J 3 HOH 48  448 92  HOH HOH D . 
J 3 HOH 49  449 337 HOH HOH D . 
J 3 HOH 50  450 168 HOH HOH D . 
J 3 HOH 51  451 97  HOH HOH D . 
J 3 HOH 52  452 361 HOH HOH D . 
J 3 HOH 53  453 516 HOH HOH D . 
J 3 HOH 54  454 324 HOH HOH D . 
J 3 HOH 55  455 184 HOH HOH D . 
J 3 HOH 56  456 452 HOH HOH D . 
J 3 HOH 57  457 528 HOH HOH D . 
J 3 HOH 58  458 23  HOH HOH D . 
J 3 HOH 59  459 175 HOH HOH D . 
J 3 HOH 60  460 211 HOH HOH D . 
J 3 HOH 61  461 120 HOH HOH D . 
J 3 HOH 62  462 344 HOH HOH D . 
J 3 HOH 63  463 349 HOH HOH D . 
J 3 HOH 64  464 199 HOH HOH D . 
J 3 HOH 65  465 255 HOH HOH D . 
J 3 HOH 66  466 305 HOH HOH D . 
J 3 HOH 67  467 404 HOH HOH D . 
J 3 HOH 68  468 162 HOH HOH D . 
J 3 HOH 69  469 505 HOH HOH D . 
J 3 HOH 70  470 207 HOH HOH D . 
J 3 HOH 71  471 119 HOH HOH D . 
J 3 HOH 72  472 424 HOH HOH D . 
J 3 HOH 73  473 354 HOH HOH D . 
J 3 HOH 74  474 300 HOH HOH D . 
J 3 HOH 75  475 94  HOH HOH D . 
J 3 HOH 76  476 375 HOH HOH D . 
J 3 HOH 77  477 365 HOH HOH D . 
J 3 HOH 78  478 304 HOH HOH D . 
J 3 HOH 79  479 313 HOH HOH D . 
J 3 HOH 80  480 396 HOH HOH D . 
J 3 HOH 81  481 329 HOH HOH D . 
J 3 HOH 82  482 267 HOH HOH D . 
J 3 HOH 83  483 326 HOH HOH D . 
J 3 HOH 84  484 202 HOH HOH D . 
J 3 HOH 85  485 400 HOH HOH D . 
J 3 HOH 86  486 543 HOH HOH D . 
J 3 HOH 87  487 91  HOH HOH D . 
J 3 HOH 88  488 47  HOH HOH D . 
J 3 HOH 89  489 473 HOH HOH D . 
J 3 HOH 90  490 482 HOH HOH D . 
J 3 HOH 91  491 306 HOH HOH D . 
J 3 HOH 92  492 293 HOH HOH D . 
J 3 HOH 93  493 169 HOH HOH D . 
J 3 HOH 94  494 416 HOH HOH D . 
J 3 HOH 95  495 295 HOH HOH D . 
J 3 HOH 96  496 158 HOH HOH D . 
J 3 HOH 97  497 124 HOH HOH D . 
J 3 HOH 98  498 562 HOH HOH D . 
J 3 HOH 99  499 496 HOH HOH D . 
J 3 HOH 100 500 253 HOH HOH D . 
J 3 HOH 101 501 246 HOH HOH D . 
J 3 HOH 102 502 556 HOH HOH D . 
J 3 HOH 103 503 381 HOH HOH D . 
J 3 HOH 104 504 456 HOH HOH D . 
J 3 HOH 105 505 278 HOH HOH D . 
J 3 HOH 106 506 336 HOH HOH D . 
J 3 HOH 107 507 370 HOH HOH D . 
J 3 HOH 108 508 351 HOH HOH D . 
J 3 HOH 109 509 520 HOH HOH D . 
J 3 HOH 110 510 487 HOH HOH D . 
J 3 HOH 111 511 40  HOH HOH D . 
J 3 HOH 112 512 116 HOH HOH D . 
J 3 HOH 113 513 451 HOH HOH D . 
J 3 HOH 114 514 438 HOH HOH D . 
J 3 HOH 115 515 346 HOH HOH D . 
J 3 HOH 116 516 294 HOH HOH D . 
J 3 HOH 117 517 127 HOH HOH D . 
J 3 HOH 118 518 518 HOH HOH D . 
J 3 HOH 119 519 399 HOH HOH D . 
J 3 HOH 120 520 490 HOH HOH D . 
J 3 HOH 121 521 260 HOH HOH D . 
J 3 HOH 122 522 189 HOH HOH D . 
J 3 HOH 123 523 521 HOH HOH D . 
J 3 HOH 124 524 406 HOH HOH D . 
J 3 HOH 125 525 362 HOH HOH D . 
J 3 HOH 126 526 383 HOH HOH D . 
J 3 HOH 127 527 515 HOH HOH D . 
J 3 HOH 128 528 317 HOH HOH D . 
J 3 HOH 129 529 391 HOH HOH D . 
J 3 HOH 130 530 111 HOH HOH D . 
J 3 HOH 131 531 340 HOH HOH D . 
J 3 HOH 132 532 513 HOH HOH D . 
J 3 HOH 133 533 355 HOH HOH D . 
J 3 HOH 134 534 292 HOH HOH D . 
J 3 HOH 135 535 563 HOH HOH D . 
J 3 HOH 136 536 539 HOH HOH D . 
J 3 HOH 137 537 123 HOH HOH D . 
J 3 HOH 138 538 509 HOH HOH D . 
J 3 HOH 139 539 433 HOH HOH D . 
J 3 HOH 140 540 532 HOH HOH D . 
K 3 HOH 1   401 545 HOH HOH B . 
K 3 HOH 2   402 176 HOH HOH B . 
K 3 HOH 3   403 441 HOH HOH B . 
K 3 HOH 4   404 3   HOH HOH B . 
K 3 HOH 5   405 80  HOH HOH B . 
K 3 HOH 6   406 343 HOH HOH B . 
K 3 HOH 7   407 201 HOH HOH B . 
K 3 HOH 8   408 478 HOH HOH B . 
K 3 HOH 9   409 449 HOH HOH B . 
K 3 HOH 10  410 95  HOH HOH B . 
K 3 HOH 11  411 193 HOH HOH B . 
K 3 HOH 12  412 171 HOH HOH B . 
K 3 HOH 13  413 103 HOH HOH B . 
K 3 HOH 14  414 339 HOH HOH B . 
K 3 HOH 15  415 141 HOH HOH B . 
K 3 HOH 16  416 214 HOH HOH B . 
K 3 HOH 17  417 247 HOH HOH B . 
K 3 HOH 18  418 386 HOH HOH B . 
K 3 HOH 19  419 371 HOH HOH B . 
K 3 HOH 20  420 156 HOH HOH B . 
K 3 HOH 21  421 166 HOH HOH B . 
K 3 HOH 22  422 9   HOH HOH B . 
K 3 HOH 23  423 270 HOH HOH B . 
K 3 HOH 24  424 37  HOH HOH B . 
K 3 HOH 25  425 69  HOH HOH B . 
K 3 HOH 26  426 36  HOH HOH B . 
K 3 HOH 27  427 204 HOH HOH B . 
K 3 HOH 28  428 53  HOH HOH B . 
K 3 HOH 29  429 8   HOH HOH B . 
K 3 HOH 30  430 364 HOH HOH B . 
K 3 HOH 31  431 88  HOH HOH B . 
K 3 HOH 32  432 10  HOH HOH B . 
K 3 HOH 33  433 43  HOH HOH B . 
K 3 HOH 34  434 231 HOH HOH B . 
K 3 HOH 35  435 48  HOH HOH B . 
K 3 HOH 36  436 128 HOH HOH B . 
K 3 HOH 37  437 283 HOH HOH B . 
K 3 HOH 38  438 174 HOH HOH B . 
K 3 HOH 39  439 348 HOH HOH B . 
K 3 HOH 40  440 276 HOH HOH B . 
K 3 HOH 41  441 118 HOH HOH B . 
K 3 HOH 42  442 474 HOH HOH B . 
K 3 HOH 43  443 221 HOH HOH B . 
K 3 HOH 44  444 100 HOH HOH B . 
K 3 HOH 45  445 429 HOH HOH B . 
K 3 HOH 46  446 237 HOH HOH B . 
K 3 HOH 47  447 558 HOH HOH B . 
K 3 HOH 48  448 26  HOH HOH B . 
K 3 HOH 49  449 280 HOH HOH B . 
K 3 HOH 50  450 74  HOH HOH B . 
K 3 HOH 51  451 378 HOH HOH B . 
K 3 HOH 52  452 217 HOH HOH B . 
K 3 HOH 53  453 309 HOH HOH B . 
K 3 HOH 54  454 2   HOH HOH B . 
K 3 HOH 55  455 145 HOH HOH B . 
K 3 HOH 56  456 165 HOH HOH B . 
K 3 HOH 57  457 257 HOH HOH B . 
K 3 HOH 58  458 238 HOH HOH B . 
K 3 HOH 59  459 133 HOH HOH B . 
K 3 HOH 60  460 21  HOH HOH B . 
K 3 HOH 61  461 70  HOH HOH B . 
K 3 HOH 62  462 132 HOH HOH B . 
K 3 HOH 63  463 477 HOH HOH B . 
K 3 HOH 64  464 17  HOH HOH B . 
K 3 HOH 65  465 239 HOH HOH B . 
K 3 HOH 66  466 205 HOH HOH B . 
K 3 HOH 67  467 439 HOH HOH B . 
K 3 HOH 68  468 39  HOH HOH B . 
K 3 HOH 69  469 149 HOH HOH B . 
K 3 HOH 70  470 312 HOH HOH B . 
K 3 HOH 71  471 56  HOH HOH B . 
K 3 HOH 72  472 422 HOH HOH B . 
K 3 HOH 73  473 310 HOH HOH B . 
K 3 HOH 74  474 289 HOH HOH B . 
K 3 HOH 75  475 363 HOH HOH B . 
K 3 HOH 76  476 181 HOH HOH B . 
K 3 HOH 77  477 62  HOH HOH B . 
K 3 HOH 78  478 170 HOH HOH B . 
K 3 HOH 79  479 108 HOH HOH B . 
K 3 HOH 80  480 167 HOH HOH B . 
K 3 HOH 81  481 323 HOH HOH B . 
K 3 HOH 82  482 115 HOH HOH B . 
K 3 HOH 83  483 35  HOH HOH B . 
K 3 HOH 84  484 218 HOH HOH B . 
K 3 HOH 85  485 59  HOH HOH B . 
K 3 HOH 86  486 402 HOH HOH B . 
K 3 HOH 87  487 101 HOH HOH B . 
K 3 HOH 88  488 114 HOH HOH B . 
K 3 HOH 89  489 85  HOH HOH B . 
K 3 HOH 90  490 288 HOH HOH B . 
K 3 HOH 91  491 501 HOH HOH B . 
K 3 HOH 92  492 458 HOH HOH B . 
K 3 HOH 93  493 265 HOH HOH B . 
K 3 HOH 94  494 465 HOH HOH B . 
K 3 HOH 95  495 195 HOH HOH B . 
K 3 HOH 96  496 223 HOH HOH B . 
K 3 HOH 97  497 31  HOH HOH B . 
K 3 HOH 98  498 325 HOH HOH B . 
K 3 HOH 99  499 384 HOH HOH B . 
K 3 HOH 100 500 341 HOH HOH B . 
K 3 HOH 101 501 335 HOH HOH B . 
K 3 HOH 102 502 190 HOH HOH B . 
K 3 HOH 103 503 426 HOH HOH B . 
K 3 HOH 104 504 240 HOH HOH B . 
K 3 HOH 105 505 65  HOH HOH B . 
K 3 HOH 106 506 546 HOH HOH B . 
K 3 HOH 107 507 264 HOH HOH B . 
K 3 HOH 108 508 535 HOH HOH B . 
K 3 HOH 109 509 457 HOH HOH B . 
K 3 HOH 110 510 525 HOH HOH B . 
K 3 HOH 111 511 321 HOH HOH B . 
K 3 HOH 112 512 130 HOH HOH B . 
K 3 HOH 113 513 230 HOH HOH B . 
K 3 HOH 114 514 450 HOH HOH B . 
K 3 HOH 115 515 435 HOH HOH B . 
K 3 HOH 116 516 440 HOH HOH B . 
K 3 HOH 117 517 232 HOH HOH B . 
K 3 HOH 118 518 542 HOH HOH B . 
K 3 HOH 119 519 519 HOH HOH B . 
K 3 HOH 120 520 460 HOH HOH B . 
K 3 HOH 121 521 356 HOH HOH B . 
K 3 HOH 122 522 212 HOH HOH B . 
K 3 HOH 123 523 414 HOH HOH B . 
K 3 HOH 124 524 551 HOH HOH B . 
K 3 HOH 125 525 139 HOH HOH B . 
K 3 HOH 126 526 418 HOH HOH B . 
K 3 HOH 127 527 274 HOH HOH B . 
K 3 HOH 128 528 157 HOH HOH B . 
K 3 HOH 129 529 492 HOH HOH B . 
K 3 HOH 130 530 208 HOH HOH B . 
K 3 HOH 131 531 249 HOH HOH B . 
K 3 HOH 132 532 297 HOH HOH B . 
K 3 HOH 133 533 506 HOH HOH B . 
K 3 HOH 134 534 415 HOH HOH B . 
K 3 HOH 135 535 235 HOH HOH B . 
K 3 HOH 136 536 488 HOH HOH B . 
K 3 HOH 137 537 102 HOH HOH B . 
K 3 HOH 138 538 407 HOH HOH B . 
K 3 HOH 139 539 395 HOH HOH B . 
K 3 HOH 140 540 209 HOH HOH B . 
K 3 HOH 141 541 301 HOH HOH B . 
K 3 HOH 142 542 320 HOH HOH B . 
K 3 HOH 143 543 549 HOH HOH B . 
L 3 HOH 1   401 227 HOH HOH C . 
L 3 HOH 2   402 269 HOH HOH C . 
L 3 HOH 3   403 442 HOH HOH C . 
L 3 HOH 4   404 498 HOH HOH C . 
L 3 HOH 5   405 401 HOH HOH C . 
L 3 HOH 6   406 514 HOH HOH C . 
L 3 HOH 7   407 143 HOH HOH C . 
L 3 HOH 8   408 234 HOH HOH C . 
L 3 HOH 9   409 261 HOH HOH C . 
L 3 HOH 10  410 106 HOH HOH C . 
L 3 HOH 11  411 19  HOH HOH C . 
L 3 HOH 12  412 485 HOH HOH C . 
L 3 HOH 13  413 390 HOH HOH C . 
L 3 HOH 14  414 405 HOH HOH C . 
L 3 HOH 15  415 374 HOH HOH C . 
L 3 HOH 16  416 508 HOH HOH C . 
L 3 HOH 17  417 200 HOH HOH C . 
L 3 HOH 18  418 215 HOH HOH C . 
L 3 HOH 19  419 72  HOH HOH C . 
L 3 HOH 20  420 99  HOH HOH C . 
L 3 HOH 21  421 89  HOH HOH C . 
L 3 HOH 22  422 266 HOH HOH C . 
L 3 HOH 23  423 61  HOH HOH C . 
L 3 HOH 24  424 467 HOH HOH C . 
L 3 HOH 25  425 180 HOH HOH C . 
L 3 HOH 26  426 29  HOH HOH C . 
L 3 HOH 27  427 68  HOH HOH C . 
L 3 HOH 28  428 11  HOH HOH C . 
L 3 HOH 29  429 45  HOH HOH C . 
L 3 HOH 30  430 319 HOH HOH C . 
L 3 HOH 31  431 466 HOH HOH C . 
L 3 HOH 32  432 531 HOH HOH C . 
L 3 HOH 33  433 537 HOH HOH C . 
L 3 HOH 34  434 98  HOH HOH C . 
L 3 HOH 35  435 15  HOH HOH C . 
L 3 HOH 36  436 334 HOH HOH C . 
L 3 HOH 37  437 411 HOH HOH C . 
L 3 HOH 38  438 131 HOH HOH C . 
L 3 HOH 39  439 331 HOH HOH C . 
L 3 HOH 40  440 233 HOH HOH C . 
L 3 HOH 41  441 42  HOH HOH C . 
L 3 HOH 42  442 463 HOH HOH C . 
L 3 HOH 43  443 316 HOH HOH C . 
L 3 HOH 44  444 173 HOH HOH C . 
L 3 HOH 45  445 392 HOH HOH C . 
L 3 HOH 46  446 50  HOH HOH C . 
L 3 HOH 47  447 206 HOH HOH C . 
L 3 HOH 48  448 470 HOH HOH C . 
L 3 HOH 49  449 179 HOH HOH C . 
L 3 HOH 50  450 64  HOH HOH C . 
L 3 HOH 51  451 443 HOH HOH C . 
L 3 HOH 52  452 455 HOH HOH C . 
L 3 HOH 53  453 314 HOH HOH C . 
L 3 HOH 54  454 122 HOH HOH C . 
L 3 HOH 55  455 285 HOH HOH C . 
L 3 HOH 56  456 216 HOH HOH C . 
L 3 HOH 57  457 328 HOH HOH C . 
L 3 HOH 58  458 544 HOH HOH C . 
L 3 HOH 59  459 121 HOH HOH C . 
L 3 HOH 60  460 385 HOH HOH C . 
L 3 HOH 61  461 480 HOH HOH C . 
L 3 HOH 62  462 140 HOH HOH C . 
L 3 HOH 63  463 282 HOH HOH C . 
L 3 HOH 64  464 526 HOH HOH C . 
L 3 HOH 65  465 353 HOH HOH C . 
L 3 HOH 66  466 146 HOH HOH C . 
L 3 HOH 67  467 561 HOH HOH C . 
L 3 HOH 68  468 459 HOH HOH C . 
L 3 HOH 69  469 548 HOH HOH C . 
L 3 HOH 70  470 279 HOH HOH C . 
L 3 HOH 71  471 259 HOH HOH C . 
L 3 HOH 72  472 500 HOH HOH C . 
L 3 HOH 73  473 352 HOH HOH C . 
L 3 HOH 74  474 413 HOH HOH C . 
L 3 HOH 75  475 250 HOH HOH C . 
L 3 HOH 76  476 472 HOH HOH C . 
L 3 HOH 77  477 332 HOH HOH C . 
L 3 HOH 78  478 403 HOH HOH C . 
L 3 HOH 79  479 377 HOH HOH C . 
L 3 HOH 80  480 533 HOH HOH C . 
L 3 HOH 81  481 517 HOH HOH C . 
L 3 HOH 82  482 96  HOH HOH C . 
L 3 HOH 83  483 409 HOH HOH C . 
L 3 HOH 84  484 296 HOH HOH C . 
L 3 HOH 85  485 541 HOH HOH C . 
L 3 HOH 86  486 243 HOH HOH C . 
L 3 HOH 87  487 469 HOH HOH C . 
L 3 HOH 88  488 423 HOH HOH C . 
L 3 HOH 89  489 376 HOH HOH C . 
L 3 HOH 90  490 389 HOH HOH C . 
L 3 HOH 91  491 153 HOH HOH C . 
L 3 HOH 92  492 359 HOH HOH C . 
L 3 HOH 93  493 388 HOH HOH C . 
L 3 HOH 94  494 380 HOH HOH C . 
L 3 HOH 95  495 360 HOH HOH C . 
L 3 HOH 96  496 495 HOH HOH C . 
L 3 HOH 97  497 512 HOH HOH C . 
L 3 HOH 98  498 436 HOH HOH C . 
L 3 HOH 99  499 410 HOH HOH C . 
L 3 HOH 100 500 502 HOH HOH C . 
L 3 HOH 101 501 372 HOH HOH C . 
L 3 HOH 102 502 417 HOH HOH C . 
L 3 HOH 103 503 476 HOH HOH C . 
L 3 HOH 104 504 290 HOH HOH C . 
L 3 HOH 105 505 408 HOH HOH C . 
M 3 HOH 1   101 27  HOH HOH E . 
M 3 HOH 2   102 51  HOH HOH E . 
M 3 HOH 3   103 555 HOH HOH E . 
M 3 HOH 4   104 565 HOH HOH E . 
N 3 HOH 1   101 229 HOH HOH F . 
N 3 HOH 2   102 110 HOH HOH F . 
N 3 HOH 3   103 81  HOH HOH F . 
N 3 HOH 4   104 159 HOH HOH F . 
N 3 HOH 5   105 367 HOH HOH F . 
O 3 HOH 1   101 25  HOH HOH G . 
P 3 HOH 1   101 93  HOH HOH H . 
P 3 HOH 2   102 67  HOH HOH H . 
P 3 HOH 3   103 330 HOH HOH H . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 103 ? CG  ? A GLU 111 CG  
2  1 Y 1 A GLU 103 ? CD  ? A GLU 111 CD  
3  1 Y 1 A GLU 103 ? OE1 ? A GLU 111 OE1 
4  1 Y 1 A GLU 103 ? OE2 ? A GLU 111 OE2 
5  1 Y 1 A LYS 125 ? CG  ? A LYS 133 CG  
6  1 Y 1 A LYS 125 ? CD  ? A LYS 133 CD  
7  1 Y 1 A LYS 125 ? CE  ? A LYS 133 CE  
8  1 Y 1 A LYS 125 ? NZ  ? A LYS 133 NZ  
9  1 Y 1 A GLU 133 ? CG  ? A GLU 141 CG  
10 1 Y 1 A GLU 133 ? CD  ? A GLU 141 CD  
11 1 Y 1 A GLU 133 ? OE1 ? A GLU 141 OE1 
12 1 Y 1 A GLU 133 ? OE2 ? A GLU 141 OE2 
13 1 Y 1 A LYS 221 ? CG  ? A LYS 229 CG  
14 1 Y 1 A LYS 221 ? CD  ? A LYS 229 CD  
15 1 Y 1 A LYS 221 ? CE  ? A LYS 229 CE  
16 1 Y 1 A LYS 221 ? NZ  ? A LYS 229 NZ  
17 1 Y 1 D ASP 27  ? CG  ? B ASP 35  CG  
18 1 Y 1 D ASP 27  ? OD1 ? B ASP 35  OD1 
19 1 Y 1 D ASP 27  ? OD2 ? B ASP 35  OD2 
20 1 Y 1 D GLU 103 ? CG  ? B GLU 111 CG  
21 1 Y 1 D GLU 103 ? CD  ? B GLU 111 CD  
22 1 Y 1 D GLU 103 ? OE1 ? B GLU 111 OE1 
23 1 Y 1 D GLU 103 ? OE2 ? B GLU 111 OE2 
24 1 Y 1 D GLU 252 ? CG  ? B GLU 260 CG  
25 1 Y 1 D GLU 252 ? CD  ? B GLU 260 CD  
26 1 Y 1 D GLU 252 ? OE1 ? B GLU 260 OE1 
27 1 Y 1 D GLU 252 ? OE2 ? B GLU 260 OE2 
28 1 Y 1 D LYS 287 ? CG  ? B LYS 295 CG  
29 1 Y 1 D LYS 287 ? CD  ? B LYS 295 CD  
30 1 Y 1 D LYS 287 ? CE  ? B LYS 295 CE  
31 1 Y 1 D LYS 287 ? NZ  ? B LYS 295 NZ  
32 1 Y 1 B LYS 64  ? CG  ? C LYS 72  CG  
33 1 Y 1 B LYS 64  ? CD  ? C LYS 72  CD  
34 1 Y 1 B LYS 64  ? CE  ? C LYS 72  CE  
35 1 Y 1 B LYS 64  ? NZ  ? C LYS 72  NZ  
36 1 Y 1 B LYS 125 ? CG  ? C LYS 133 CG  
37 1 Y 1 B LYS 125 ? CD  ? C LYS 133 CD  
38 1 Y 1 B LYS 125 ? CE  ? C LYS 133 CE  
39 1 Y 1 B LYS 125 ? NZ  ? C LYS 133 NZ  
40 1 Y 1 B LYS 130 ? CE  ? C LYS 138 CE  
41 1 Y 1 B LYS 130 ? NZ  ? C LYS 138 NZ  
42 1 Y 1 B GLU 252 ? CG  ? C GLU 260 CG  
43 1 Y 1 B GLU 252 ? CD  ? C GLU 260 CD  
44 1 Y 1 B GLU 252 ? OE1 ? C GLU 260 OE1 
45 1 Y 1 B GLU 252 ? OE2 ? C GLU 260 OE2 
46 1 Y 1 B LYS 259 ? CG  ? C LYS 267 CG  
47 1 Y 1 B LYS 259 ? CD  ? C LYS 267 CD  
48 1 Y 1 B LYS 259 ? CE  ? C LYS 267 CE  
49 1 Y 1 B LYS 259 ? NZ  ? C LYS 267 NZ  
50 1 Y 1 C ASP 27  ? CG  ? D ASP 35  CG  
51 1 Y 1 C ASP 27  ? OD1 ? D ASP 35  OD1 
52 1 Y 1 C ASP 27  ? OD2 ? D ASP 35  OD2 
53 1 Y 1 C LYS 64  ? CG  ? D LYS 72  CG  
54 1 Y 1 C LYS 64  ? CD  ? D LYS 72  CD  
55 1 Y 1 C LYS 64  ? CE  ? D LYS 72  CE  
56 1 Y 1 C LYS 64  ? NZ  ? D LYS 72  NZ  
57 1 Y 1 C GLU 103 ? CG  ? D GLU 111 CG  
58 1 Y 1 C GLU 103 ? CD  ? D GLU 111 CD  
59 1 Y 1 C GLU 103 ? OE1 ? D GLU 111 OE1 
60 1 Y 1 C GLU 103 ? OE2 ? D GLU 111 OE2 
61 1 Y 1 C LYS 125 ? CG  ? D LYS 133 CG  
62 1 Y 1 C LYS 125 ? CD  ? D LYS 133 CD  
63 1 Y 1 C LYS 125 ? CE  ? D LYS 133 CE  
64 1 Y 1 C LYS 125 ? NZ  ? D LYS 133 NZ  
65 1 Y 1 C LYS 130 ? CE  ? D LYS 138 CE  
66 1 Y 1 C LYS 130 ? NZ  ? D LYS 138 NZ  
67 1 Y 1 C GLU 137 ? CG  ? D GLU 145 CG  
68 1 Y 1 C GLU 137 ? CD  ? D GLU 145 CD  
69 1 Y 1 C GLU 137 ? OE1 ? D GLU 145 OE1 
70 1 Y 1 C GLU 137 ? OE2 ? D GLU 145 OE2 
71 1 Y 1 C GLU 252 ? CG  ? D GLU 260 CG  
72 1 Y 1 C GLU 252 ? CD  ? D GLU 260 CD  
73 1 Y 1 C GLU 252 ? OE1 ? D GLU 260 OE1 
74 1 Y 1 C GLU 252 ? OE2 ? D GLU 260 OE2 
75 1 Y 1 E TYR 1   ? CG  ? E TYR 1   CG  
76 1 Y 1 E TYR 1   ? CD1 ? E TYR 1   CD1 
77 1 Y 1 E TYR 1   ? CD2 ? E TYR 1   CD2 
78 1 Y 1 E TYR 1   ? CE1 ? E TYR 1   CE1 
79 1 Y 1 E TYR 1   ? CE2 ? E TYR 1   CE2 
80 1 Y 1 E TYR 1   ? CZ  ? E TYR 1   CZ  
81 1 Y 1 E TYR 1   ? OH  ? E TYR 1   OH  
82 1 Y 1 G TYR 1   ? CG  ? G TYR 1   CG  
83 1 Y 1 G TYR 1   ? CD1 ? G TYR 1   CD1 
84 1 Y 1 G TYR 1   ? CD2 ? G TYR 1   CD2 
85 1 Y 1 G TYR 1   ? CE1 ? G TYR 1   CE1 
86 1 Y 1 G TYR 1   ? CE2 ? G TYR 1   CE2 
87 1 Y 1 G TYR 1   ? CZ  ? G TYR 1   CZ  
88 1 Y 1 G TYR 1   ? OH  ? G TYR 1   OH  
89 1 Y 1 H TYR 1   ? CG  ? H TYR 1   CG  
90 1 Y 1 H TYR 1   ? CD1 ? H TYR 1   CD1 
91 1 Y 1 H TYR 1   ? CD2 ? H TYR 1   CD2 
92 1 Y 1 H TYR 1   ? CE1 ? H TYR 1   CE1 
93 1 Y 1 H TYR 1   ? CE2 ? H TYR 1   CE2 
94 1 Y 1 H TYR 1   ? CZ  ? H TYR 1   CZ  
95 1 Y 1 H TYR 1   ? OH  ? H TYR 1   OH  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.71 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8SRW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     65.927 
_cell.length_a_esd                 ? 
_cell.length_b                     119.714 
_cell.length_b_esd                 ? 
_cell.length_c                     84.657 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8SRW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8SRW 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.79 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2 M ammonium acetate, 0.1 M HEPES pH 7.5, 22-25% PEG 3350.
Drops contained:
1ul 25 mg/ml CysK, 1 ul well solution, 0.4 ul CysK seed stock (1/100 dilution)
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9537 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9537 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX1 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8SRW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.15 
_reflns.d_resolution_low                               39.90 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     70305 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.230 
_reflns.pdbx_Rpim_I_all                                0.086 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       494112 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.213 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.15 
_reflns_shell.d_res_low                                     2.20 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           32948 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4569 
_reflns_shell.percent_possible_obs                          99.9 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               7.2 
_reflns_shell.pdbx_chi_squared                              0.91 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               1.994 
_reflns_shell.pdbx_Rpim_I_all                               0.738 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.425 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.850 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8SRW 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.15 
_refine.ls_d_res_low                             39.50 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     70237 
_refine.ls_number_reflns_R_free                  3517 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.56 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1956 
_refine.ls_R_factor_R_free                       0.2355 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1935 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      8SRT 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.68 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.27 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.15 
_refine_hist.d_res_low                        39.50 
_refine_hist.number_atoms_solvent             560 
_refine_hist.number_atoms_total               9909 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        9349 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002 ? 9506  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.517 ? 12863 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.451 ? 1358  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042 ? 1456  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 1667  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.15 2.18  . . 142 2689 100.00 . . . . 0.2801 . . . . . . . . . . . 0.3005 
'X-RAY DIFFRACTION' 2.18 2.21  . . 138 2678 100.00 . . . . 0.2821 . . . . . . . . . . . 0.3182 
'X-RAY DIFFRACTION' 2.21 2.24  . . 143 2649 100.00 . . . . 0.2848 . . . . . . . . . . . 0.3343 
'X-RAY DIFFRACTION' 2.24 2.28  . . 138 2686 100.00 . . . . 0.2606 . . . . . . . . . . . 0.3503 
'X-RAY DIFFRACTION' 2.28 2.32  . . 114 2679 100.00 . . . . 0.2615 . . . . . . . . . . . 0.2773 
'X-RAY DIFFRACTION' 2.32 2.36  . . 148 2709 99.00  . . . . 0.2547 . . . . . . . . . . . 0.2922 
'X-RAY DIFFRACTION' 2.36 2.40  . . 161 2576 100.00 . . . . 0.2526 . . . . . . . . . . . 0.2905 
'X-RAY DIFFRACTION' 2.40 2.44  . . 129 2700 99.00  . . . . 0.2401 . . . . . . . . . . . 0.3090 
'X-RAY DIFFRACTION' 2.44 2.49  . . 133 2632 99.00  . . . . 0.2444 . . . . . . . . . . . 0.2724 
'X-RAY DIFFRACTION' 2.49 2.55  . . 137 2679 99.00  . . . . 0.2344 . . . . . . . . . . . 0.2719 
'X-RAY DIFFRACTION' 2.55 2.61  . . 134 2627 99.00  . . . . 0.2304 . . . . . . . . . . . 0.3183 
'X-RAY DIFFRACTION' 2.61 2.67  . . 151 2614 98.00  . . . . 0.2320 . . . . . . . . . . . 0.2634 
'X-RAY DIFFRACTION' 2.67 2.75  . . 142 2671 100.00 . . . . 0.2272 . . . . . . . . . . . 0.2840 
'X-RAY DIFFRACTION' 2.75 2.83  . . 153 2667 100.00 . . . . 0.2107 . . . . . . . . . . . 0.2517 
'X-RAY DIFFRACTION' 2.83 2.92  . . 127 2692 100.00 . . . . 0.2143 . . . . . . . . . . . 0.2613 
'X-RAY DIFFRACTION' 2.92 3.02  . . 129 2687 100.00 . . . . 0.2112 . . . . . . . . . . . 0.2859 
'X-RAY DIFFRACTION' 3.02 3.14  . . 143 2674 100.00 . . . . 0.2080 . . . . . . . . . . . 0.2439 
'X-RAY DIFFRACTION' 3.14 3.29  . . 135 2682 100.00 . . . . 0.1966 . . . . . . . . . . . 0.2268 
'X-RAY DIFFRACTION' 3.29 3.46  . . 137 2663 100.00 . . . . 0.1890 . . . . . . . . . . . 0.2209 
'X-RAY DIFFRACTION' 3.46 3.68  . . 149 2692 100.00 . . . . 0.1680 . . . . . . . . . . . 0.2039 
'X-RAY DIFFRACTION' 3.68 3.96  . . 139 2665 100.00 . . . . 0.1579 . . . . . . . . . . . 0.1893 
'X-RAY DIFFRACTION' 3.96 4.36  . . 129 2678 100.00 . . . . 0.1484 . . . . . . . . . . . 0.1974 
'X-RAY DIFFRACTION' 4.36 4.99  . . 151 2650 98.00  . . . . 0.1424 . . . . . . . . . . . 0.1901 
'X-RAY DIFFRACTION' 4.99 6.28  . . 137 2664 99.00  . . . . 0.1754 . . . . . . . . . . . 0.2295 
'X-RAY DIFFRACTION' 6.28 39.50 . . 178 2717 100.00 . . . . 0.1580 . . . . . . . . . . . 0.1909 
# 
_struct.entry_id                     8SRW 
_struct.title                        
;Crystal structure of O-acetyl-L-serine sulfhydrylase A (CysK) from Staphylococcus aureus NCTC 8325 complexed with a modified peptide inhibitor
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8SRW 
_struct_keywords.text            'Pyridoxal-phosphate dependent enzyme, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Q2G0Q8_STAA8 Q2G0Q8 ? 1 
;MAQKPVDNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIG
LAFVCAAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKELKEEHGYFEPQQFENPANPEVHELTTG
PELLQQFEGKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTEIYD
SIIKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVLPSNGERYLSTPLYSFDD
;
1 
2 PDB 8SRW         8SRW   ? 2 ? 1 
# 
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 8SRW A 9 ? 318 ? Q2G0Q8 1 ? 310 ? 1 310 
2 1 8SRW D 9 ? 318 ? Q2G0Q8 1 ? 310 ? 1 310 
3 1 8SRW B 9 ? 318 ? Q2G0Q8 1 ? 310 ? 1 310 
4 1 8SRW C 9 ? 318 ? Q2G0Q8 1 ? 310 ? 1 310 
5 2 8SRW E 1 ? 5   ? 8SRW   1 ? 5   ? 1 5   
6 2 8SRW F 1 ? 5   ? 8SRW   1 ? 5   ? 1 5   
7 2 8SRW G 1 ? 5   ? 8SRW   1 ? 5   ? 1 5   
8 2 8SRW H 1 ? 5   ? 8SRW   1 ? 5   ? 1 5   
# 
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 8SRW MET A 1 ? UNP Q2G0Q8 ? ? 'expression tag' -7 1  
1 8SRW GLY A 2 ? UNP Q2G0Q8 ? ? 'expression tag' -6 2  
1 8SRW HIS A 3 ? UNP Q2G0Q8 ? ? 'expression tag' -5 3  
1 8SRW HIS A 4 ? UNP Q2G0Q8 ? ? 'expression tag' -4 4  
1 8SRW HIS A 5 ? UNP Q2G0Q8 ? ? 'expression tag' -3 5  
1 8SRW HIS A 6 ? UNP Q2G0Q8 ? ? 'expression tag' -2 6  
1 8SRW HIS A 7 ? UNP Q2G0Q8 ? ? 'expression tag' -1 7  
1 8SRW HIS A 8 ? UNP Q2G0Q8 ? ? 'expression tag' 0  8  
2 8SRW MET D 1 ? UNP Q2G0Q8 ? ? 'expression tag' -7 9  
2 8SRW GLY D 2 ? UNP Q2G0Q8 ? ? 'expression tag' -6 10 
2 8SRW HIS D 3 ? UNP Q2G0Q8 ? ? 'expression tag' -5 11 
2 8SRW HIS D 4 ? UNP Q2G0Q8 ? ? 'expression tag' -4 12 
2 8SRW HIS D 5 ? UNP Q2G0Q8 ? ? 'expression tag' -3 13 
2 8SRW HIS D 6 ? UNP Q2G0Q8 ? ? 'expression tag' -2 14 
2 8SRW HIS D 7 ? UNP Q2G0Q8 ? ? 'expression tag' -1 15 
2 8SRW HIS D 8 ? UNP Q2G0Q8 ? ? 'expression tag' 0  16 
3 8SRW MET B 1 ? UNP Q2G0Q8 ? ? 'expression tag' -7 17 
3 8SRW GLY B 2 ? UNP Q2G0Q8 ? ? 'expression tag' -6 18 
3 8SRW HIS B 3 ? UNP Q2G0Q8 ? ? 'expression tag' -5 19 
3 8SRW HIS B 4 ? UNP Q2G0Q8 ? ? 'expression tag' -4 20 
3 8SRW HIS B 5 ? UNP Q2G0Q8 ? ? 'expression tag' -3 21 
3 8SRW HIS B 6 ? UNP Q2G0Q8 ? ? 'expression tag' -2 22 
3 8SRW HIS B 7 ? UNP Q2G0Q8 ? ? 'expression tag' -1 23 
3 8SRW HIS B 8 ? UNP Q2G0Q8 ? ? 'expression tag' 0  24 
4 8SRW MET C 1 ? UNP Q2G0Q8 ? ? 'expression tag' -7 25 
4 8SRW GLY C 2 ? UNP Q2G0Q8 ? ? 'expression tag' -6 26 
4 8SRW HIS C 3 ? UNP Q2G0Q8 ? ? 'expression tag' -5 27 
4 8SRW HIS C 4 ? UNP Q2G0Q8 ? ? 'expression tag' -4 28 
4 8SRW HIS C 5 ? UNP Q2G0Q8 ? ? 'expression tag' -3 29 
4 8SRW HIS C 6 ? UNP Q2G0Q8 ? ? 'expression tag' -2 30 
4 8SRW HIS C 7 ? UNP Q2G0Q8 ? ? 'expression tag' -1 31 
4 8SRW HIS C 8 ? UNP Q2G0Q8 ? ? 'expression tag' 0  32 
# 
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 tetrameric 4 
2 author_and_software_defined_assembly PISA tetrameric 4 
# 
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)' 7370  ? 
1 MORE         -21   ? 
1 'SSA (A^2)'  22050 ? 
2 'ABSA (A^2)' 7240  ? 
2 MORE         -19   ? 
2 'SSA (A^2)'  21670 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,I,J,M,N 
2 1 C,D,G,H,K,L,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 16  ? ILE A 21  ? ASN A 8   ILE A 13  5 ? 6  
HELX_P HELX_P2  AA2 TYR A 46  ? ASN A 48  ? TYR A 38  ASN A 40  5 ? 3  
HELX_P HELX_P3  AA3 VAL A 53  ? GLU A 68  ? VAL A 45  GLU A 60  1 ? 16 
HELX_P HELX_P4  AA4 GLY A 83  ? GLY A 97  ? GLY A 75  GLY A 89  1 ? 15 
HELX_P HELX_P5  AA5 SER A 109 ? TYR A 119 ? SER A 101 TYR A 111 1 ? 11 
HELX_P HELX_P6  AA6 PRO A 127 ? SER A 129 ? PRO A 119 SER A 121 5 ? 3  
HELX_P HELX_P7  AA7 GLU A 130 ? GLY A 147 ? GLU A 122 GLY A 139 1 ? 18 
HELX_P HELX_P8  AA8 PRO A 157 ? THR A 166 ? PRO A 149 THR A 158 1 ? 10 
HELX_P HELX_P9  AA9 THR A 166 ? PHE A 175 ? THR A 158 PHE A 167 1 ? 10 
HELX_P HELX_P10 AB1 GLY A 190 ? TYR A 204 ? GLY A 182 TYR A 196 1 ? 15 
HELX_P HELX_P11 AB2 GLY A 254 ? GLY A 270 ? GLY A 246 GLY A 262 1 ? 17 
HELX_P HELX_P12 AB3 GLY A 274 ? GLY A 292 ? GLY A 266 GLY A 284 1 ? 19 
HELX_P HELX_P13 AB4 ASN A 304 ? LEU A 309 ? ASN A 296 LEU A 301 5 ? 6  
HELX_P HELX_P14 AB5 ASN B 16  ? ILE B 21  ? ASN D 8   ILE D 13  5 ? 6  
HELX_P HELX_P15 AB6 TYR B 46  ? ASN B 48  ? TYR D 38  ASN D 40  5 ? 3  
HELX_P HELX_P16 AB7 VAL B 53  ? GLU B 68  ? VAL D 45  GLU D 60  1 ? 16 
HELX_P HELX_P17 AB8 GLY B 83  ? GLY B 97  ? GLY D 75  GLY D 89  1 ? 15 
HELX_P HELX_P18 AB9 SER B 109 ? TYR B 119 ? SER D 101 TYR D 111 1 ? 11 
HELX_P HELX_P19 AC1 PRO B 127 ? SER B 129 ? PRO D 119 SER D 121 5 ? 3  
HELX_P HELX_P20 AC2 GLU B 130 ? GLY B 147 ? GLU D 122 GLY D 139 1 ? 18 
HELX_P HELX_P21 AC3 PRO B 157 ? THR B 166 ? PRO D 149 THR D 158 1 ? 10 
HELX_P HELX_P22 AC4 THR B 166 ? PHE B 175 ? THR D 158 PHE D 167 1 ? 10 
HELX_P HELX_P23 AC5 GLY B 190 ? TYR B 204 ? GLY D 182 TYR D 196 1 ? 15 
HELX_P HELX_P24 AC6 GLY B 254 ? GLY B 270 ? GLY D 246 GLY D 262 1 ? 17 
HELX_P HELX_P25 AC7 GLY B 274 ? GLY B 292 ? GLY D 266 GLY D 284 1 ? 19 
HELX_P HELX_P26 AC8 ASN B 304 ? LEU B 309 ? ASN D 296 LEU D 301 5 ? 6  
HELX_P HELX_P27 AC9 ASN C 16  ? ILE C 21  ? ASN B 8   ILE B 13  5 ? 6  
HELX_P HELX_P28 AD1 TYR C 46  ? ASN C 48  ? TYR B 38  ASN B 40  5 ? 3  
HELX_P HELX_P29 AD2 VAL C 53  ? GLU C 68  ? VAL B 45  GLU B 60  1 ? 16 
HELX_P HELX_P30 AD3 GLY C 83  ? GLY C 97  ? GLY B 75  GLY B 89  1 ? 15 
HELX_P HELX_P31 AD4 SER C 109 ? TYR C 119 ? SER B 101 TYR B 111 1 ? 11 
HELX_P HELX_P32 AD5 PRO C 127 ? SER C 129 ? PRO B 119 SER B 121 5 ? 3  
HELX_P HELX_P33 AD6 GLU C 130 ? GLY C 147 ? GLU B 122 GLY B 139 1 ? 18 
HELX_P HELX_P34 AD7 PRO C 157 ? THR C 166 ? PRO B 149 THR B 158 1 ? 10 
HELX_P HELX_P35 AD8 THR C 166 ? PHE C 175 ? THR B 158 PHE B 167 1 ? 10 
HELX_P HELX_P36 AD9 GLY C 190 ? TYR C 204 ? GLY B 182 TYR B 196 1 ? 15 
HELX_P HELX_P37 AE1 GLY C 254 ? GLY C 270 ? GLY B 246 GLY B 262 1 ? 17 
HELX_P HELX_P38 AE2 GLY C 274 ? GLY C 292 ? GLY B 266 GLY B 284 1 ? 19 
HELX_P HELX_P39 AE3 ASN C 304 ? LEU C 309 ? ASN B 296 LEU B 301 5 ? 6  
HELX_P HELX_P40 AE4 ASN D 16  ? ILE D 21  ? ASN C 8   ILE C 13  5 ? 6  
HELX_P HELX_P41 AE5 TYR D 46  ? ASN D 48  ? TYR C 38  ASN C 40  5 ? 3  
HELX_P HELX_P42 AE6 VAL D 53  ? GLU D 68  ? VAL C 45  GLU C 60  1 ? 16 
HELX_P HELX_P43 AE7 GLY D 83  ? GLY D 97  ? GLY C 75  GLY C 89  1 ? 15 
HELX_P HELX_P44 AE8 SER D 109 ? TYR D 119 ? SER C 101 TYR C 111 1 ? 11 
HELX_P HELX_P45 AE9 PRO D 127 ? SER D 129 ? PRO C 119 SER C 121 5 ? 3  
HELX_P HELX_P46 AF1 GLU D 130 ? GLY D 147 ? GLU C 122 GLY C 139 1 ? 18 
HELX_P HELX_P47 AF2 PRO D 157 ? THR D 166 ? PRO C 149 THR C 158 1 ? 10 
HELX_P HELX_P48 AF3 THR D 166 ? PHE D 175 ? THR C 158 PHE C 167 1 ? 10 
HELX_P HELX_P49 AF4 GLY D 190 ? TYR D 204 ? GLY C 182 TYR C 196 1 ? 15 
HELX_P HELX_P50 AF5 GLY D 254 ? GLY D 270 ? GLY C 246 GLY C 262 1 ? 17 
HELX_P HELX_P51 AF6 GLY D 274 ? GLY D 292 ? GLY C 266 GLY C 284 1 ? 19 
HELX_P HELX_P52 AF7 ASN D 304 ? LEU D 309 ? ASN C 296 LEU C 301 5 ? 6  
HELX_P HELX_P53 AF8 THR D 311 ? SER D 315 ? THR C 303 SER C 307 5 ? 5  
# 
_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 VAL 53 C ? ? ? 1_555 A LLP 54 N ? ? A VAL 45 A LLP 46 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale2  covale both ? A LLP 54 C ? ? ? 1_555 A ASP 55 N ? ? A LLP 46 A ASP 47 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale3  covale both ? B VAL 53 C ? ? ? 1_555 B LLP 54 N ? ? D VAL 45 D LLP 46 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale4  covale both ? B LLP 54 C ? ? ? 1_555 B ASP 55 N ? ? D LLP 46 D ASP 47 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale5  covale both ? C VAL 53 C ? ? ? 1_555 C LLP 54 N ? ? B VAL 45 B LLP 46 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale6  covale both ? C LLP 54 C ? ? ? 1_555 C ASP 55 N ? ? B LLP 46 B ASP 47 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale7  covale both ? D VAL 53 C ? ? ? 1_555 D LLP 54 N ? ? C VAL 45 C LLP 46 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale8  covale both ? D LLP 54 C ? ? ? 1_555 D ASP 55 N ? ? C LLP 46 C ASP 47 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale9  covale both ? E MET 2  C ? ? ? 1_555 E NAL 3  N ? ? E MET 2  E NAL 3  1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale10 covale both ? E NAL 3  C ? ? ? 1_555 E TYR 4  N ? ? E NAL 3  E TYR 4  1_555 ? ? ? ? ? ? ? 1.431 ? ? 
covale11 covale both ? F MET 2  C ? ? ? 1_555 F NAL 3  N ? ? F MET 2  F NAL 3  1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale12 covale both ? F NAL 3  C ? ? ? 1_555 F TYR 4  N ? ? F NAL 3  F TYR 4  1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale13 covale both ? G MET 2  C ? ? ? 1_555 G NAL 3  N ? ? G MET 2  G NAL 3  1_555 ? ? ? ? ? ? ? 1.431 ? ? 
covale14 covale both ? G NAL 3  C ? ? ? 1_555 G TYR 4  N ? ? G NAL 3  G TYR 4  1_555 ? ? ? ? ? ? ? 1.431 ? ? 
covale15 covale both ? H MET 2  C ? ? ? 1_555 H NAL 3  N ? ? H MET 2  H NAL 3  1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale16 covale both ? H NAL 3  C ? ? ? 1_555 H TYR 4  N ? ? H NAL 3  H TYR 4  1_555 ? ? ? ? ? ? ? 1.430 ? ? 
# 
_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 LLP A 54 ? . . . . LLP A 46 ? 1_555 . . . . . . . LYS 1 LLP 'Pyridoxal phosphate' 'Named protein modification' 
2 LLP B 54 ? . . . . LLP D 46 ? 1_555 . . . . . . . LYS 1 LLP 'Pyridoxal phosphate' 'Named protein modification' 
3 LLP C 54 ? . . . . LLP B 46 ? 1_555 . . . . . . . LYS 1 LLP 'Pyridoxal phosphate' 'Named protein modification' 
4 LLP D 54 ? . . . . LLP C 46 ? 1_555 . . . . . . . LYS 1 LLP 'Pyridoxal phosphate' 'Named protein modification' 
5 NAL E 3  ? . . . . NAL E 3  ? 1_555 . . . . . . . ?   1 NAL None                  'Non-standard residue'       
6 NAL F 3  ? . . . . NAL F 3  ? 1_555 . . . . . . . ?   1 NAL None                  'Non-standard residue'       
7 NAL G 3  ? . . . . NAL G 3  ? 1_555 . . . . . . . ?   1 NAL None                  'Non-standard residue'       
8 NAL H 3  ? . . . . NAL H 3  ? 1_555 . . . . . . . ?   1 NAL None                  'Non-standard residue'       
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 6 ? 
AA4 ? 3 ? 
AA5 ? 6 ? 
AA6 ? 3 ? 
AA7 ? 6 ? 
AA8 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 26  ? LYS A 28  ? VAL A 18  LYS A 20  
AA1 2 ASP A 39  ? LEU A 44  ? ASP A 31  LEU A 36  
AA1 3 THR A 296 ? LEU A 301 ? THR A 288 LEU A 293 
AA1 4 ALA A 182 ? GLY A 186 ? ALA A 174 GLY A 178 
AA1 5 GLU A 208 ? PRO A 214 ? GLU A 200 PRO A 206 
AA1 6 SER A 249 ? VAL A 253 ? SER A 241 VAL A 245 
AA2 1 THR A 76  ? PRO A 80  ? THR A 68  PRO A 72  
AA2 2 LYS A 99  ? PRO A 105 ? LYS A 91  PRO A 97  
AA2 3 GLU A 122 ? THR A 126 ? GLU A 114 THR A 118 
AA3 1 VAL B 26  ? LYS B 28  ? VAL D 18  LYS D 20  
AA3 2 ASP B 39  ? LEU B 44  ? ASP D 31  LEU D 36  
AA3 3 THR B 296 ? LEU B 301 ? THR D 288 LEU D 293 
AA3 4 ALA B 182 ? GLY B 186 ? ALA D 174 GLY D 178 
AA3 5 GLU B 208 ? PRO B 214 ? GLU D 200 PRO D 206 
AA3 6 SER B 249 ? VAL B 253 ? SER D 241 VAL D 245 
AA4 1 THR B 76  ? PRO B 80  ? THR D 68  PRO D 72  
AA4 2 LYS B 99  ? PRO B 105 ? LYS D 91  PRO D 97  
AA4 3 GLU B 122 ? THR B 126 ? GLU D 114 THR D 118 
AA5 1 VAL C 26  ? LYS C 28  ? VAL B 18  LYS B 20  
AA5 2 ASP C 39  ? LEU C 44  ? ASP B 31  LEU B 36  
AA5 3 THR C 296 ? LEU C 301 ? THR B 288 LEU B 293 
AA5 4 ALA C 182 ? GLY C 186 ? ALA B 174 GLY B 178 
AA5 5 GLU C 208 ? PRO C 214 ? GLU B 200 PRO B 206 
AA5 6 SER C 249 ? VAL C 253 ? SER B 241 VAL B 245 
AA6 1 THR C 76  ? PRO C 80  ? THR B 68  PRO B 72  
AA6 2 LYS C 99  ? PRO C 105 ? LYS B 91  PRO B 97  
AA6 3 GLU C 122 ? THR C 126 ? GLU B 114 THR B 118 
AA7 1 VAL D 26  ? LYS D 28  ? VAL C 18  LYS C 20  
AA7 2 ASP D 39  ? LEU D 44  ? ASP C 31  LEU C 36  
AA7 3 THR D 296 ? LEU D 301 ? THR C 288 LEU C 293 
AA7 4 ALA D 182 ? GLY D 186 ? ALA C 174 GLY C 178 
AA7 5 GLU D 208 ? PRO D 214 ? GLU C 200 PRO C 206 
AA7 6 SER D 249 ? VAL D 253 ? SER C 241 VAL C 245 
AA8 1 THR D 76  ? PRO D 80  ? THR C 68  PRO C 72  
AA8 2 LYS D 99  ? PRO D 105 ? LYS C 91  PRO C 97  
AA8 3 GLU D 122 ? THR D 126 ? GLU C 114 THR C 118 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 27  ? N VAL A 19  O VAL A 42  ? O VAL A 34  
AA1 2 3 N TYR A 41  ? N TYR A 33  O VAL A 297 ? O VAL A 289 
AA1 3 4 O VAL A 298 ? O VAL A 290 N LEU A 184 ? N LEU A 176 
AA1 4 5 N PHE A 183 ? N PHE A 175 O VAL A 210 ? O VAL A 202 
AA1 5 6 N ALA A 211 ? N ALA A 203 O ILE A 251 ? O ILE A 243 
AA2 1 2 N ILE A 77  ? N ILE A 69  O LYS A 99  ? O LYS A 91  
AA2 2 3 N ALA A 100 ? N ALA A 92  O GLU A 122 ? O GLU A 114 
AA3 1 2 N VAL B 27  ? N VAL D 19  O VAL B 42  ? O VAL D 34  
AA3 2 3 N ASP B 39  ? N ASP D 31  O VAL B 297 ? O VAL D 289 
AA3 3 4 O VAL B 298 ? O VAL D 290 N ALA B 182 ? N ALA D 174 
AA3 4 5 N PHE B 183 ? N PHE D 175 O VAL B 210 ? O VAL D 202 
AA3 5 6 N ALA B 211 ? N ALA D 203 O ILE B 251 ? O ILE D 243 
AA4 1 2 N ILE B 77  ? N ILE D 69  O LYS B 99  ? O LYS D 91  
AA4 2 3 N ALA B 100 ? N ALA D 92  O GLU B 122 ? O GLU D 114 
AA5 1 2 N VAL C 27  ? N VAL B 19  O VAL C 42  ? O VAL B 34  
AA5 2 3 N TYR C 41  ? N TYR B 33  O VAL C 297 ? O VAL B 289 
AA5 3 4 O VAL C 298 ? O VAL B 290 N ALA C 182 ? N ALA B 174 
AA5 4 5 N PHE C 183 ? N PHE B 175 O GLU C 208 ? O GLU B 200 
AA5 5 6 N ALA C 211 ? N ALA B 203 O ILE C 251 ? O ILE B 243 
AA6 1 2 N ILE C 77  ? N ILE B 69  O LYS C 99  ? O LYS B 91  
AA6 2 3 N ALA C 100 ? N ALA B 92  O GLU C 122 ? O GLU B 114 
AA7 1 2 N VAL D 27  ? N VAL C 19  O VAL D 42  ? O VAL C 34  
AA7 2 3 N TYR D 41  ? N TYR C 33  O VAL D 297 ? O VAL C 289 
AA7 3 4 O VAL D 298 ? O VAL C 290 N ALA D 182 ? N ALA C 174 
AA7 4 5 N PHE D 183 ? N PHE C 175 O GLU D 208 ? O GLU C 200 
AA7 5 6 N ALA D 211 ? N ALA C 203 O ILE D 251 ? O ILE C 243 
AA8 1 2 N ILE D 77  ? N ILE C 69  O LYS D 99  ? O LYS C 91  
AA8 2 3 N MET D 104 ? N MET C 96  O THR D 126 ? O THR C 118 
# 
_pdbx_entry_details.entry_id                   8SRW 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C  E NAL 3 ? ? N E TYR 4 ? ? CA E TYR 4 ? ? 136.74 121.70 15.04  2.50 Y 
2 1 O  F MET 2 ? ? C F MET 2 ? ? N  F NAL 3 ? ? 98.38  122.70 -24.32 1.60 Y 
3 1 O  F NAL 3 ? ? C F NAL 3 ? ? N  F TYR 4 ? ? 106.36 122.70 -16.34 1.60 Y 
4 1 CA G MET 2 ? ? C G MET 2 ? ? N  G NAL 3 ? ? 94.91  117.20 -22.29 2.20 Y 
5 1 O  G MET 2 ? ? C G MET 2 ? ? N  G NAL 3 ? ? 140.06 122.70 17.36  1.60 Y 
6 1 O  G NAL 3 ? ? C G NAL 3 ? ? N  G TYR 4 ? ? 109.89 122.70 -12.81 1.60 Y 
7 1 C  G NAL 3 ? ? N G TYR 4 ? ? CA G TYR 4 ? ? 141.85 121.70 20.15  2.50 Y 
8 1 O  H NAL 3 ? ? C H NAL 3 ? ? N  H TYR 4 ? ? 112.93 122.70 -9.77  1.60 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 ALA A 123 ? ? 51.65   -135.93 
2  1 GLN A 144 ? ? 60.91   80.56   
3  1 THR A 158 ? ? -122.84 -61.82  
4  1 PRO A 304 ? ? -59.87  -7.55   
5  1 GLU D 98  ? ? -67.21  2.21    
6  1 ALA D 123 ? ? 52.53   -138.52 
7  1 GLN D 144 ? ? 57.39   79.17   
8  1 THR D 158 ? ? -121.56 -62.69  
9  1 THR D 236 ? ? -69.16  0.01    
10 1 PRO D 304 ? ? -69.90  0.76    
11 1 ALA B 123 ? ? 53.84   -134.33 
12 1 GLN B 144 ? ? 55.84   80.69   
13 1 THR B 158 ? ? -123.08 -65.39  
14 1 ALA C 123 ? ? 52.50   -136.65 
15 1 GLN C 144 ? ? 58.10   81.55   
16 1 THR C 158 ? ? -124.48 -64.65  
17 1 PRO C 304 ? ? -68.25  1.37    
18 1 TYR G 4   ? ? -151.06 71.36   
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 MET E 2 ? ? NAL E 3 ? ? 147.51 
2 1 MET G 2 ? ? NAL G 3 ? ? 144.43 
3 1 MET H 2 ? ? NAL H 3 ? ? 147.56 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 NAL E 3 ? ? -13.90 
2 1 MET F 2 ? ? 26.73  
3 1 NAL F 3 ? ? -15.25 
4 1 NAL G 3 ? ? -18.80 
5 1 NAL H 3 ? ? -18.67 
# 
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 LLP 54 A LLP 46 ? LYS 'modified residue' 
2 B LLP 54 D LLP 46 ? LYS 'modified residue' 
3 C LLP 54 B LLP 46 ? LYS 'modified residue' 
4 D LLP 54 C LLP 46 ? LYS 'modified residue' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 559 ? 6.04 . 
2 1 O ? D HOH 540 ? 6.34 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -7  ? A MET 1   
2  1 Y 1 A GLY -6  ? A GLY 2   
3  1 Y 1 A HIS -5  ? A HIS 3   
4  1 Y 1 A HIS -4  ? A HIS 4   
5  1 Y 1 A HIS -3  ? A HIS 5   
6  1 Y 1 A HIS -2  ? A HIS 6   
7  1 Y 1 A HIS -1  ? A HIS 7   
8  1 Y 1 A HIS 0   ? A HIS 8   
9  1 Y 1 A PHE 308 ? A PHE 316 
10 1 Y 1 A ASP 309 ? A ASP 317 
11 1 Y 1 A ASP 310 ? A ASP 318 
12 1 Y 1 D MET -7  ? B MET 1   
13 1 Y 1 D GLY -6  ? B GLY 2   
14 1 Y 1 D HIS -5  ? B HIS 3   
15 1 Y 1 D HIS -4  ? B HIS 4   
16 1 Y 1 D HIS -3  ? B HIS 5   
17 1 Y 1 D HIS -2  ? B HIS 6   
18 1 Y 1 D HIS -1  ? B HIS 7   
19 1 Y 1 D HIS 0   ? B HIS 8   
20 1 Y 1 D PHE 308 ? B PHE 316 
21 1 Y 1 D ASP 309 ? B ASP 317 
22 1 Y 1 D ASP 310 ? B ASP 318 
23 1 Y 1 B MET -7  ? C MET 1   
24 1 Y 1 B GLY -6  ? C GLY 2   
25 1 Y 1 B HIS -5  ? C HIS 3   
26 1 Y 1 B HIS -4  ? C HIS 4   
27 1 Y 1 B HIS -3  ? C HIS 5   
28 1 Y 1 B HIS -2  ? C HIS 6   
29 1 Y 1 B HIS -1  ? C HIS 7   
30 1 Y 1 B HIS 0   ? C HIS 8   
31 1 Y 1 B PHE 308 ? C PHE 316 
32 1 Y 1 B ASP 309 ? C ASP 317 
33 1 Y 1 B ASP 310 ? C ASP 318 
34 1 Y 1 C MET -7  ? D MET 1   
35 1 Y 1 C GLY -6  ? D GLY 2   
36 1 Y 1 C HIS -5  ? D HIS 3   
37 1 Y 1 C HIS -4  ? D HIS 4   
38 1 Y 1 C HIS -3  ? D HIS 5   
39 1 Y 1 C HIS -2  ? D HIS 6   
40 1 Y 1 C HIS -1  ? D HIS 7   
41 1 Y 1 C HIS 0   ? D HIS 8   
42 1 Y 1 C PHE 308 ? D PHE 316 
43 1 Y 1 C ASP 309 ? D ASP 317 
44 1 Y 1 C ASP 310 ? D ASP 318 
# 
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 
HIS N      N N N 137 
HIS CA     C N S 138 
HIS C      C N N 139 
HIS O      O N N 140 
HIS CB     C N N 141 
HIS CG     C Y N 142 
HIS ND1    N Y N 143 
HIS CD2    C Y N 144 
HIS CE1    C Y N 145 
HIS NE2    N Y N 146 
HIS OXT    O N N 147 
HIS H      H N N 148 
HIS H2     H N N 149 
HIS HA     H N N 150 
HIS HB2    H N N 151 
HIS HB3    H N N 152 
HIS HD1    H N N 153 
HIS HD2    H N N 154 
HIS HE1    H N N 155 
HIS HE2    H N N 156 
HIS HXT    H N N 157 
HOH O      O N N 158 
HOH H1     H N N 159 
HOH H2     H N N 160 
ILE N      N N N 161 
ILE CA     C N S 162 
ILE C      C N N 163 
ILE O      O N N 164 
ILE CB     C N S 165 
ILE CG1    C N N 166 
ILE CG2    C N N 167 
ILE CD1    C N N 168 
ILE OXT    O N N 169 
ILE H      H N N 170 
ILE H2     H N N 171 
ILE HA     H N N 172 
ILE HB     H N N 173 
ILE HG12   H N N 174 
ILE HG13   H N N 175 
ILE HG21   H N N 176 
ILE HG22   H N N 177 
ILE HG23   H N N 178 
ILE HD11   H N N 179 
ILE HD12   H N N 180 
ILE HD13   H N N 181 
ILE HXT    H N N 182 
LEU N      N N N 183 
LEU CA     C N S 184 
LEU C      C N N 185 
LEU O      O N N 186 
LEU CB     C N N 187 
LEU CG     C N N 188 
LEU CD1    C N N 189 
LEU CD2    C N N 190 
LEU OXT    O N N 191 
LEU H      H N N 192 
LEU H2     H N N 193 
LEU HA     H N N 194 
LEU HB2    H N N 195 
LEU HB3    H N N 196 
LEU HG     H N N 197 
LEU HD11   H N N 198 
LEU HD12   H N N 199 
LEU HD13   H N N 200 
LEU HD21   H N N 201 
LEU HD22   H N N 202 
LEU HD23   H N N 203 
LEU HXT    H N N 204 
LLP N1     N Y N 205 
LLP C2     C Y N 206 
LLP "C2'"  C N N 207 
LLP C3     C Y N 208 
LLP O3     O N N 209 
LLP C4     C Y N 210 
LLP "C4'"  C N N 211 
LLP C5     C Y N 212 
LLP C6     C Y N 213 
LLP "C5'"  C N N 214 
LLP OP4    O N N 215 
LLP P      P N N 216 
LLP OP1    O N N 217 
LLP OP2    O N N 218 
LLP OP3    O N N 219 
LLP N      N N N 220 
LLP CA     C N S 221 
LLP CB     C N N 222 
LLP CG     C N N 223 
LLP CD     C N N 224 
LLP CE     C N N 225 
LLP NZ     N N N 226 
LLP C      C N N 227 
LLP O      O N N 228 
LLP OXT    O N N 229 
LLP "H2'1" H N N 230 
LLP "H2'2" H N N 231 
LLP "H2'3" H N N 232 
LLP HO3    H N N 233 
LLP "H4'1" H N N 234 
LLP H6     H N N 235 
LLP "H5'1" H N N 236 
LLP "H5'2" H N N 237 
LLP HOP2   H N N 238 
LLP HOP3   H N N 239 
LLP H      H N N 240 
LLP H2     H N N 241 
LLP HA     H N N 242 
LLP HB2    H N N 243 
LLP HB3    H N N 244 
LLP HG2    H N N 245 
LLP HG3    H N N 246 
LLP HD2    H N N 247 
LLP HD3    H N N 248 
LLP HE2    H N N 249 
LLP HE3    H N N 250 
LLP HXT    H N N 251 
LYS N      N N N 252 
LYS CA     C N S 253 
LYS C      C N N 254 
LYS O      O N N 255 
LYS CB     C N N 256 
LYS CG     C N N 257 
LYS CD     C N N 258 
LYS CE     C N N 259 
LYS NZ     N N N 260 
LYS OXT    O N N 261 
LYS H      H N N 262 
LYS H2     H N N 263 
LYS HA     H N N 264 
LYS HB2    H N N 265 
LYS HB3    H N N 266 
LYS HG2    H N N 267 
LYS HG3    H N N 268 
LYS HD2    H N N 269 
LYS HD3    H N N 270 
LYS HE2    H N N 271 
LYS HE3    H N N 272 
LYS HZ1    H N N 273 
LYS HZ2    H N N 274 
LYS HZ3    H N N 275 
LYS HXT    H N N 276 
MET N      N N N 277 
MET CA     C N S 278 
MET C      C N N 279 
MET O      O N N 280 
MET CB     C N N 281 
MET CG     C N N 282 
MET SD     S N N 283 
MET CE     C N N 284 
MET OXT    O N N 285 
MET H      H N N 286 
MET H2     H N N 287 
MET HA     H N N 288 
MET HB2    H N N 289 
MET HB3    H N N 290 
MET HG2    H N N 291 
MET HG3    H N N 292 
MET HE1    H N N 293 
MET HE2    H N N 294 
MET HE3    H N N 295 
MET HXT    H N N 296 
NAL C1     C Y N 297 
NAL C2     C Y N 298 
NAL C3     C Y N 299 
NAL C4     C Y N 300 
NAL C4A    C Y N 301 
NAL C5     C Y N 302 
NAL C6     C Y N 303 
NAL C7     C Y N 304 
NAL C8     C Y N 305 
NAL C8A    C Y N 306 
NAL C9     C N N 307 
NAL CA     C N S 308 
NAL C      C N N 309 
NAL N      N N N 310 
NAL O      O N N 311 
NAL OXT    O N N 312 
NAL H1     H N N 313 
NAL H3     H N N 314 
NAL H4     H N N 315 
NAL H5     H N N 316 
NAL H6     H N N 317 
NAL H7     H N N 318 
NAL H8     H N N 319 
NAL H91    H N N 320 
NAL H92    H N N 321 
NAL HA     H N N 322 
NAL H      H N N 323 
NAL H2     H N N 324 
NAL HXT    H N N 325 
PHE N      N N N 326 
PHE CA     C N S 327 
PHE C      C N N 328 
PHE O      O N N 329 
PHE CB     C N N 330 
PHE CG     C Y N 331 
PHE CD1    C Y N 332 
PHE CD2    C Y N 333 
PHE CE1    C Y N 334 
PHE CE2    C Y N 335 
PHE CZ     C Y N 336 
PHE OXT    O N N 337 
PHE H      H N N 338 
PHE H2     H N N 339 
PHE HA     H N N 340 
PHE HB2    H N N 341 
PHE HB3    H N N 342 
PHE HD1    H N N 343 
PHE HD2    H N N 344 
PHE HE1    H N N 345 
PHE HE2    H N N 346 
PHE HZ     H N N 347 
PHE HXT    H N N 348 
PRO N      N N N 349 
PRO CA     C N S 350 
PRO C      C N N 351 
PRO O      O N N 352 
PRO CB     C N N 353 
PRO CG     C N N 354 
PRO CD     C N N 355 
PRO OXT    O N N 356 
PRO H      H N N 357 
PRO HA     H N N 358 
PRO HB2    H N N 359 
PRO HB3    H N N 360 
PRO HG2    H N N 361 
PRO HG3    H N N 362 
PRO HD2    H N N 363 
PRO HD3    H N N 364 
PRO HXT    H N N 365 
SER N      N N N 366 
SER CA     C N S 367 
SER C      C N N 368 
SER O      O N N 369 
SER CB     C N N 370 
SER OG     O N N 371 
SER OXT    O N N 372 
SER H      H N N 373 
SER H2     H N N 374 
SER HA     H N N 375 
SER HB2    H N N 376 
SER HB3    H N N 377 
SER HG     H N N 378 
SER HXT    H N N 379 
THR N      N N N 380 
THR CA     C N S 381 
THR C      C N N 382 
THR O      O N N 383 
THR CB     C N R 384 
THR OG1    O N N 385 
THR CG2    C N N 386 
THR OXT    O N N 387 
THR H      H N N 388 
THR H2     H N N 389 
THR HA     H N N 390 
THR HB     H N N 391 
THR HG1    H N N 392 
THR HG21   H N N 393 
THR HG22   H N N 394 
THR HG23   H N N 395 
THR HXT    H N N 396 
TYR N      N N N 397 
TYR CA     C N S 398 
TYR C      C N N 399 
TYR O      O N N 400 
TYR CB     C N N 401 
TYR CG     C Y N 402 
TYR CD1    C Y N 403 
TYR CD2    C Y N 404 
TYR CE1    C Y N 405 
TYR CE2    C Y N 406 
TYR CZ     C Y N 407 
TYR OH     O N N 408 
TYR OXT    O N N 409 
TYR H      H N N 410 
TYR H2     H N N 411 
TYR HA     H N N 412 
TYR HB2    H N N 413 
TYR HB3    H N N 414 
TYR HD1    H N N 415 
TYR HD2    H N N 416 
TYR HE1    H N N 417 
TYR HE2    H N N 418 
TYR HH     H N N 419 
TYR HXT    H N N 420 
VAL N      N N N 421 
VAL CA     C N S 422 
VAL C      C N N 423 
VAL O      O N N 424 
VAL CB     C N N 425 
VAL CG1    C N N 426 
VAL CG2    C N N 427 
VAL OXT    O N N 428 
VAL H      H N N 429 
VAL H2     H N N 430 
VAL HA     H N N 431 
VAL HB     H N N 432 
VAL HG11   H N N 433 
VAL HG12   H N N 434 
VAL HG13   H N N 435 
VAL HG21   H N N 436 
VAL HG22   H N N 437 
VAL HG23   H N N 438 
VAL HXT    H N N 439 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LLP N1    C2     doub Y N 194 
LLP N1    C6     sing Y N 195 
LLP C2    "C2'"  sing N N 196 
LLP C2    C3     sing Y N 197 
LLP C3    O3     sing N N 198 
LLP C3    C4     doub Y N 199 
LLP C4    "C4'"  sing N N 200 
LLP C4    C5     sing Y N 201 
LLP "C4'" NZ     doub N N 202 
LLP C5    C6     doub Y N 203 
LLP C5    "C5'"  sing N N 204 
LLP "C5'" OP4    sing N N 205 
LLP OP4   P      sing N N 206 
LLP P     OP1    doub N N 207 
LLP P     OP2    sing N N 208 
LLP P     OP3    sing N N 209 
LLP N     CA     sing N N 210 
LLP CA    CB     sing N N 211 
LLP CA    C      sing N N 212 
LLP CB    CG     sing N N 213 
LLP CG    CD     sing N N 214 
LLP CD    CE     sing N N 215 
LLP CE    NZ     sing N N 216 
LLP C     O      doub N N 217 
LLP C     OXT    sing N N 218 
LLP "C2'" "H2'1" sing N N 219 
LLP "C2'" "H2'2" sing N N 220 
LLP "C2'" "H2'3" sing N N 221 
LLP O3    HO3    sing N N 222 
LLP "C4'" "H4'1" sing N N 223 
LLP C6    H6     sing N N 224 
LLP "C5'" "H5'1" sing N N 225 
LLP "C5'" "H5'2" sing N N 226 
LLP OP2   HOP2   sing N N 227 
LLP OP3   HOP3   sing N N 228 
LLP N     H      sing N N 229 
LLP N     H2     sing N N 230 
LLP CA    HA     sing N N 231 
LLP CB    HB2    sing N N 232 
LLP CB    HB3    sing N N 233 
LLP CG    HG2    sing N N 234 
LLP CG    HG3    sing N N 235 
LLP CD    HD2    sing N N 236 
LLP CD    HD3    sing N N 237 
LLP CE    HE2    sing N N 238 
LLP CE    HE3    sing N N 239 
LLP OXT   HXT    sing N N 240 
LYS N     CA     sing N N 241 
LYS N     H      sing N N 242 
LYS N     H2     sing N N 243 
LYS CA    C      sing N N 244 
LYS CA    CB     sing N N 245 
LYS CA    HA     sing N N 246 
LYS C     O      doub N N 247 
LYS C     OXT    sing N N 248 
LYS CB    CG     sing N N 249 
LYS CB    HB2    sing N N 250 
LYS CB    HB3    sing N N 251 
LYS CG    CD     sing N N 252 
LYS CG    HG2    sing N N 253 
LYS CG    HG3    sing N N 254 
LYS CD    CE     sing N N 255 
LYS CD    HD2    sing N N 256 
LYS CD    HD3    sing N N 257 
LYS CE    NZ     sing N N 258 
LYS CE    HE2    sing N N 259 
LYS CE    HE3    sing N N 260 
LYS NZ    HZ1    sing N N 261 
LYS NZ    HZ2    sing N N 262 
LYS NZ    HZ3    sing N N 263 
LYS OXT   HXT    sing N N 264 
MET N     CA     sing N N 265 
MET N     H      sing N N 266 
MET N     H2     sing N N 267 
MET CA    C      sing N N 268 
MET CA    CB     sing N N 269 
MET CA    HA     sing N N 270 
MET C     O      doub N N 271 
MET C     OXT    sing N N 272 
MET CB    CG     sing N N 273 
MET CB    HB2    sing N N 274 
MET CB    HB3    sing N N 275 
MET CG    SD     sing N N 276 
MET CG    HG2    sing N N 277 
MET CG    HG3    sing N N 278 
MET SD    CE     sing N N 279 
MET CE    HE1    sing N N 280 
MET CE    HE2    sing N N 281 
MET CE    HE3    sing N N 282 
MET OXT   HXT    sing N N 283 
NAL C6    C5     doub Y N 284 
NAL C6    C7     sing Y N 285 
NAL C5    C4A    sing Y N 286 
NAL C7    C8     doub Y N 287 
NAL C4A   C4     doub Y N 288 
NAL C4A   C8A    sing Y N 289 
NAL C8    C8A    sing Y N 290 
NAL C4    C3     sing Y N 291 
NAL C8A   C1     doub Y N 292 
NAL C3    C2     doub Y N 293 
NAL C1    C2     sing Y N 294 
NAL C2    C9     sing N N 295 
NAL C9    CA     sing N N 296 
NAL CA    N      sing N N 297 
NAL CA    C      sing N N 298 
NAL C     O      doub N N 299 
NAL C     OXT    sing N N 300 
NAL C1    H1     sing N N 301 
NAL C3    H3     sing N N 302 
NAL C4    H4     sing N N 303 
NAL C5    H5     sing N N 304 
NAL C6    H6     sing N N 305 
NAL C7    H7     sing N N 306 
NAL C8    H8     sing N N 307 
NAL C9    H91    sing N N 308 
NAL C9    H92    sing N N 309 
NAL CA    HA     sing N N 310 
NAL N     H      sing N N 311 
NAL N     H2     sing N N 312 
NAL OXT   HXT    sing N N 313 
PHE N     CA     sing N N 314 
PHE N     H      sing N N 315 
PHE N     H2     sing N N 316 
PHE CA    C      sing N N 317 
PHE CA    CB     sing N N 318 
PHE CA    HA     sing N N 319 
PHE C     O      doub N N 320 
PHE C     OXT    sing N N 321 
PHE CB    CG     sing N N 322 
PHE CB    HB2    sing N N 323 
PHE CB    HB3    sing N N 324 
PHE CG    CD1    doub Y N 325 
PHE CG    CD2    sing Y N 326 
PHE CD1   CE1    sing Y N 327 
PHE CD1   HD1    sing N N 328 
PHE CD2   CE2    doub Y N 329 
PHE CD2   HD2    sing N N 330 
PHE CE1   CZ     doub Y N 331 
PHE CE1   HE1    sing N N 332 
PHE CE2   CZ     sing Y N 333 
PHE CE2   HE2    sing N N 334 
PHE CZ    HZ     sing N N 335 
PHE OXT   HXT    sing N N 336 
PRO N     CA     sing N N 337 
PRO N     CD     sing N N 338 
PRO N     H      sing N N 339 
PRO CA    C      sing N N 340 
PRO CA    CB     sing N N 341 
PRO CA    HA     sing N N 342 
PRO C     O      doub N N 343 
PRO C     OXT    sing N N 344 
PRO CB    CG     sing N N 345 
PRO CB    HB2    sing N N 346 
PRO CB    HB3    sing N N 347 
PRO CG    CD     sing N N 348 
PRO CG    HG2    sing N N 349 
PRO CG    HG3    sing N N 350 
PRO CD    HD2    sing N N 351 
PRO CD    HD3    sing N N 352 
PRO OXT   HXT    sing N N 353 
SER N     CA     sing N N 354 
SER N     H      sing N N 355 
SER N     H2     sing N N 356 
SER CA    C      sing N N 357 
SER CA    CB     sing N N 358 
SER CA    HA     sing N N 359 
SER C     O      doub N N 360 
SER C     OXT    sing N N 361 
SER CB    OG     sing N N 362 
SER CB    HB2    sing N N 363 
SER CB    HB3    sing N N 364 
SER OG    HG     sing N N 365 
SER OXT   HXT    sing N N 366 
THR N     CA     sing N N 367 
THR N     H      sing N N 368 
THR N     H2     sing N N 369 
THR CA    C      sing N N 370 
THR CA    CB     sing N N 371 
THR CA    HA     sing N N 372 
THR C     O      doub N N 373 
THR C     OXT    sing N N 374 
THR CB    OG1    sing N N 375 
THR CB    CG2    sing N N 376 
THR CB    HB     sing N N 377 
THR OG1   HG1    sing N N 378 
THR CG2   HG21   sing N N 379 
THR CG2   HG22   sing N N 380 
THR CG2   HG23   sing N N 381 
THR OXT   HXT    sing N N 382 
TYR N     CA     sing N N 383 
TYR N     H      sing N N 384 
TYR N     H2     sing N N 385 
TYR CA    C      sing N N 386 
TYR CA    CB     sing N N 387 
TYR CA    HA     sing N N 388 
TYR C     O      doub N N 389 
TYR C     OXT    sing N N 390 
TYR CB    CG     sing N N 391 
TYR CB    HB2    sing N N 392 
TYR CB    HB3    sing N N 393 
TYR CG    CD1    doub Y N 394 
TYR CG    CD2    sing Y N 395 
TYR CD1   CE1    sing Y N 396 
TYR CD1   HD1    sing N N 397 
TYR CD2   CE2    doub Y N 398 
TYR CD2   HD2    sing N N 399 
TYR CE1   CZ     doub Y N 400 
TYR CE1   HE1    sing N N 401 
TYR CE2   CZ     sing Y N 402 
TYR CE2   HE2    sing N N 403 
TYR CZ    OH     sing N N 404 
TYR OH    HH     sing N N 405 
TYR OXT   HXT    sing N N 406 
VAL N     CA     sing N N 407 
VAL N     H      sing N N 408 
VAL N     H2     sing N N 409 
VAL CA    C      sing N N 410 
VAL CA    CB     sing N N 411 
VAL CA    HA     sing N N 412 
VAL C     O      doub N N 413 
VAL C     OXT    sing N N 414 
VAL CB    CG1    sing N N 415 
VAL CB    CG2    sing N N 416 
VAL CB    HB     sing N N 417 
VAL CG1   HG11   sing N N 418 
VAL CG1   HG12   sing N N 419 
VAL CG1   HG13   sing N N 420 
VAL CG2   HG21   sing N N 421 
VAL CG2   HG22   sing N N 422 
VAL CG2   HG23   sing N N 423 
VAL OXT   HXT    sing N N 424 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8SRT 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8SRW 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.015168 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002324 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008353 
_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]   0.011950 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . MET A 1 9   ? 31.388  6.841   4.887   1.00 71.66 ?  1   MET A N     1 
ATOM   2    C CA    . MET A 1 9   ? 32.787  6.526   5.147   1.00 68.50 ?  1   MET A CA    1 
ATOM   3    C C     . MET A 1 9   ? 33.122  6.718   6.622   1.00 62.50 ?  1   MET A C     1 
ATOM   4    O O     . MET A 1 9   ? 32.958  7.808   7.171   1.00 61.53 ?  1   MET A O     1 
ATOM   5    C CB    . MET A 1 9   ? 33.708  7.393   4.284   1.00 69.42 ?  1   MET A CB    1 
ATOM   6    C CG    . MET A 1 9   ? 34.072  6.786   2.936   1.00 71.75 ?  1   MET A CG    1 
ATOM   7    S SD    . MET A 1 9   ? 35.816  7.020   2.532   1.00 84.66 ?  1   MET A SD    1 
ATOM   8    C CE    . MET A 1 9   ? 35.994  8.783   2.790   1.00 73.60 ?  1   MET A CE    1 
ATOM   9    N N     . ALA A 1 10  ? 33.594  5.650   7.256   1.00 53.56 ?  2   ALA A N     1 
ATOM   10   C CA    . ALA A 1 10  ? 33.975  5.709   8.657   1.00 46.51 ?  2   ALA A CA    1 
ATOM   11   C C     . ALA A 1 10  ? 35.406  6.209   8.805   1.00 48.19 ?  2   ALA A C     1 
ATOM   12   O O     . ALA A 1 10  ? 36.255  6.007   7.931   1.00 48.18 ?  2   ALA A O     1 
ATOM   13   C CB    . ALA A 1 10  ? 33.835  4.334   9.311   1.00 37.63 ?  2   ALA A CB    1 
ATOM   14   N N     . GLN A 1 11  ? 35.665  6.872   9.927   1.00 45.71 ?  3   GLN A N     1 
ATOM   15   C CA    . GLN A 1 11  ? 37.008  7.345   10.227  1.00 46.48 ?  3   GLN A CA    1 
ATOM   16   C C     . GLN A 1 11  ? 37.943  6.166   10.470  1.00 44.05 ?  3   GLN A C     1 
ATOM   17   O O     . GLN A 1 11  ? 37.553  5.158   11.066  1.00 38.20 ?  3   GLN A O     1 
ATOM   18   C CB    . GLN A 1 11  ? 36.979  8.259   11.451  1.00 43.79 ?  3   GLN A CB    1 
ATOM   19   C CG    . GLN A 1 11  ? 38.230  9.093   11.645  1.00 45.02 ?  3   GLN A CG    1 
ATOM   20   C CD    . GLN A 1 11  ? 38.101  10.079  12.790  1.00 52.65 ?  3   GLN A CD    1 
ATOM   21   O OE1   . GLN A 1 11  ? 37.031  10.643  13.023  1.00 54.21 ?  3   GLN A OE1   1 
ATOM   22   N NE2   . GLN A 1 11  ? 39.195  10.290  13.514  1.00 48.71 ?  3   GLN A NE2   1 
ATOM   23   N N     . LYS A 1 12  ? 39.181  6.291   9.994   1.00 39.15 ?  4   LYS A N     1 
ATOM   24   C CA    . LYS A 1 12  ? 40.176  5.264   10.254  1.00 35.04 ?  4   LYS A CA    1 
ATOM   25   C C     . LYS A 1 12  ? 40.430  5.165   11.759  1.00 36.71 ?  4   LYS A C     1 
ATOM   26   O O     . LYS A 1 12  ? 40.246  6.144   12.489  1.00 36.13 ?  4   LYS A O     1 
ATOM   27   C CB    . LYS A 1 12  ? 41.475  5.575   9.510   1.00 40.95 ?  4   LYS A CB    1 
ATOM   28   C CG    . LYS A 1 12  ? 41.417  5.270   8.020   1.00 43.01 ?  4   LYS A CG    1 
ATOM   29   C CD    . LYS A 1 12  ? 41.230  3.781   7.760   1.00 41.09 ?  4   LYS A CD    1 
ATOM   30   C CE    . LYS A 1 12  ? 42.253  3.255   6.766   1.00 49.10 ?  4   LYS A CE    1 
ATOM   31   N NZ    . LYS A 1 12  ? 42.557  1.812   6.989   1.00 51.87 ?  4   LYS A NZ    1 
ATOM   32   N N     . PRO A 1 13  ? 40.837  3.993   12.252  1.00 34.26 ?  5   PRO A N     1 
ATOM   33   C CA    . PRO A 1 13  ? 40.952  3.804   13.704  1.00 31.99 ?  5   PRO A CA    1 
ATOM   34   C C     . PRO A 1 13  ? 41.906  4.805   14.342  1.00 38.32 ?  5   PRO A C     1 
ATOM   35   O O     . PRO A 1 13  ? 42.880  5.251   13.731  1.00 40.48 ?  5   PRO A O     1 
ATOM   36   C CB    . PRO A 1 13  ? 41.477  2.369   13.835  1.00 29.72 ?  5   PRO A CB    1 
ATOM   37   C CG    . PRO A 1 13  ? 41.066  1.700   12.568  1.00 32.73 ?  5   PRO A CG    1 
ATOM   38   C CD    . PRO A 1 13  ? 41.140  2.757   11.510  1.00 36.37 ?  5   PRO A CD    1 
ATOM   39   N N     . VAL A 1 14  ? 41.602  5.161   15.589  1.00 35.12 ?  6   VAL A N     1 
ATOM   40   C CA    . VAL A 1 14  ? 42.360  6.155   16.335  1.00 38.08 ?  6   VAL A CA    1 
ATOM   41   C C     . VAL A 1 14  ? 42.904  5.513   17.605  1.00 34.79 ?  6   VAL A C     1 
ATOM   42   O O     . VAL A 1 14  ? 42.458  4.447   18.036  1.00 32.82 ?  6   VAL A O     1 
ATOM   43   C CB    . VAL A 1 14  ? 41.514  7.401   16.672  1.00 32.42 ?  6   VAL A CB    1 
ATOM   44   C CG1   . VAL A 1 14  ? 40.898  7.984   15.408  1.00 38.13 ?  6   VAL A CG1   1 
ATOM   45   C CG2   . VAL A 1 14  ? 40.433  7.052   17.681  1.00 33.06 ?  6   VAL A CG2   1 
ATOM   46   N N     . ASP A 1 15  ? 43.888  6.185   18.204  1.00 34.14 ?  7   ASP A N     1 
ATOM   47   C CA    . ASP A 1 15  ? 44.538  5.689   19.410  1.00 34.31 ?  7   ASP A CA    1 
ATOM   48   C C     . ASP A 1 15  ? 43.831  6.132   20.683  1.00 33.84 ?  7   ASP A C     1 
ATOM   49   O O     . ASP A 1 15  ? 43.900  5.429   21.698  1.00 33.52 ?  7   ASP A O     1 
ATOM   50   C CB    . ASP A 1 15  ? 45.997  6.158   19.456  1.00 43.34 ?  7   ASP A CB    1 
ATOM   51   C CG    . ASP A 1 15  ? 46.913  5.312   18.588  1.00 47.70 ?  7   ASP A CG    1 
ATOM   52   O OD1   . ASP A 1 15  ? 47.088  4.111   18.888  1.00 52.53 ?  7   ASP A OD1   1 
ATOM   53   O OD2   . ASP A 1 15  ? 47.460  5.852   17.602  1.00 49.14 ?  7   ASP A OD2   1 
ATOM   54   N N     . ASN A 1 16  ? 43.150  7.275   20.653  1.00 30.99 ?  8   ASN A N     1 
ATOM   55   C CA    . ASN A 1 16  ? 42.528  7.838   21.841  1.00 33.36 ?  8   ASN A CA    1 
ATOM   56   C C     . ASN A 1 16  ? 41.138  8.344   21.487  1.00 31.86 ?  8   ASN A C     1 
ATOM   57   O O     . ASN A 1 16  ? 40.913  8.834   20.376  1.00 31.09 ?  8   ASN A O     1 
ATOM   58   C CB    . ASN A 1 16  ? 43.383  8.975   22.419  1.00 29.91 ?  8   ASN A CB    1 
ATOM   59   C CG    . ASN A 1 16  ? 42.840  9.505   23.727  1.00 34.00 ?  8   ASN A CG    1 
ATOM   60   O OD1   . ASN A 1 16  ? 41.859  10.245  23.752  1.00 37.40 ?  8   ASN A OD1   1 
ATOM   61   N ND2   . ASN A 1 16  ? 43.476  9.124   24.828  1.00 36.81 ?  8   ASN A ND2   1 
ATOM   62   N N     . ILE A 1 17  ? 40.209  8.229   22.441  1.00 31.43 ?  9   ILE A N     1 
ATOM   63   C CA    . ILE A 1 17  ? 38.820  8.615   22.192  1.00 37.33 ?  9   ILE A CA    1 
ATOM   64   C C     . ILE A 1 17  ? 38.699  10.106  21.897  1.00 36.98 ?  9   ILE A C     1 
ATOM   65   O O     . ILE A 1 17  ? 37.776  10.533  21.191  1.00 38.18 ?  9   ILE A O     1 
ATOM   66   C CB    . ILE A 1 17  ? 37.935  8.190   23.385  1.00 30.32 ?  9   ILE A CB    1 
ATOM   67   C CG1   . ILE A 1 17  ? 36.479  8.603   23.171  1.00 32.92 ?  9   ILE A CG1   1 
ATOM   68   C CG2   . ILE A 1 17  ? 38.453  8.779   24.670  1.00 32.62 ?  9   ILE A CG2   1 
ATOM   69   C CD1   . ILE A 1 17  ? 35.776  7.800   22.130  1.00 33.35 ?  9   ILE A CD1   1 
ATOM   70   N N     . THR A 1 18  ? 39.624  10.923  22.409  1.00 31.81 ?  10  THR A N     1 
ATOM   71   C CA    . THR A 1 18  ? 39.565  12.358  22.150  1.00 32.30 ?  10  THR A CA    1 
ATOM   72   C C     . THR A 1 18  ? 39.878  12.711  20.703  1.00 31.74 ?  10  THR A C     1 
ATOM   73   O O     . THR A 1 18  ? 39.575  13.829  20.275  1.00 30.38 ?  10  THR A O     1 
ATOM   74   C CB    . THR A 1 18  ? 40.526  13.115  23.068  1.00 35.15 ?  10  THR A CB    1 
ATOM   75   O OG1   . THR A 1 18  ? 41.871  12.684  22.818  1.00 31.22 ?  10  THR A OG1   1 
ATOM   76   C CG2   . THR A 1 18  ? 40.165  12.896  24.530  1.00 30.21 ?  10  THR A CG2   1 
ATOM   77   N N     . GLN A 1 19  ? 40.476  11.791  19.943  1.00 34.35 ?  11  GLN A N     1 
ATOM   78   C CA    . GLN A 1 19  ? 40.813  12.064  18.551  1.00 35.45 ?  11  GLN A CA    1 
ATOM   79   C C     . GLN A 1 19  ? 39.592  12.134  17.644  1.00 39.71 ?  11  GLN A C     1 
ATOM   80   O O     . GLN A 1 19  ? 39.736  12.489  16.470  1.00 33.25 ?  11  GLN A O     1 
ATOM   81   C CB    . GLN A 1 19  ? 41.785  11.006  18.021  1.00 34.48 ?  11  GLN A CB    1 
ATOM   82   C CG    . GLN A 1 19  ? 43.224  11.183  18.490  1.00 36.90 ?  11  GLN A CG    1 
ATOM   83   C CD    . GLN A 1 19  ? 44.127  10.037  18.066  1.00 40.68 ?  11  GLN A CD    1 
ATOM   84   O OE1   . GLN A 1 19  ? 44.220  9.015   18.746  1.00 45.60 ?  11  GLN A OE1   1 
ATOM   85   N NE2   . GLN A 1 19  ? 44.801  10.206  16.933  1.00 45.14 ?  11  GLN A NE2   1 
ATOM   86   N N     . ILE A 1 20  ? 38.406  11.802  18.144  1.00 38.45 ?  12  ILE A N     1 
ATOM   87   C CA    . ILE A 1 20  ? 37.186  11.889  17.355  1.00 40.41 ?  12  ILE A CA    1 
ATOM   88   C C     . ILE A 1 20  ? 36.272  13.000  17.870  1.00 37.00 ?  12  ILE A C     1 
ATOM   89   O O     . ILE A 1 20  ? 35.073  12.999  17.590  1.00 33.97 ?  12  ILE A O     1 
ATOM   90   C CB    . ILE A 1 20  ? 36.460  10.534  17.292  1.00 39.02 ?  12  ILE A CB    1 
ATOM   91   C CG1   . ILE A 1 20  ? 35.960  10.114  18.673  1.00 31.37 ?  12  ILE A CG1   1 
ATOM   92   C CG2   . ILE A 1 20  ? 37.379  9.467   16.726  1.00 38.56 ?  12  ILE A CG2   1 
ATOM   93   C CD1   . ILE A 1 20  ? 34.559  9.548   18.658  1.00 38.61 ?  12  ILE A CD1   1 
ATOM   94   N N     . ILE A 1 21  ? 36.823  13.953  18.617  1.00 29.05 ?  13  ILE A N     1 
ATOM   95   C CA    . ILE A 1 21  ? 36.073  15.139  19.011  1.00 29.74 ?  13  ILE A CA    1 
ATOM   96   C C     . ILE A 1 21  ? 36.021  16.096  17.829  1.00 30.17 ?  13  ILE A C     1 
ATOM   97   O O     . ILE A 1 21  ? 37.038  16.350  17.173  1.00 26.11 ?  13  ILE A O     1 
ATOM   98   C CB    . ILE A 1 21  ? 36.708  15.806  20.241  1.00 30.22 ?  13  ILE A CB    1 
ATOM   99   C CG1   . ILE A 1 21  ? 36.606  14.886  21.459  1.00 25.13 ?  13  ILE A CG1   1 
ATOM   100  C CG2   . ILE A 1 21  ? 36.047  17.153  20.525  1.00 22.41 ?  13  ILE A CG2   1 
ATOM   101  C CD1   . ILE A 1 21  ? 37.323  15.414  22.674  1.00 27.03 ?  13  ILE A CD1   1 
ATOM   102  N N     . GLY A 1 22  ? 34.836  16.618  17.545  1.00 25.73 ?  14  GLY A N     1 
ATOM   103  C CA    . GLY A 1 22  ? 34.657  17.534  16.439  1.00 24.02 ?  14  GLY A CA    1 
ATOM   104  C C     . GLY A 1 22  ? 34.143  16.843  15.192  1.00 28.83 ?  14  GLY A C     1 
ATOM   105  O O     . GLY A 1 22  ? 33.798  15.658  15.185  1.00 24.21 ?  14  GLY A O     1 
ATOM   106  N N     . GLY A 1 23  ? 34.104  17.620  14.111  1.00 29.26 ?  15  GLY A N     1 
ATOM   107  C CA    . GLY A 1 23  ? 33.574  17.144  12.848  1.00 26.81 ?  15  GLY A CA    1 
ATOM   108  C C     . GLY A 1 23  ? 32.130  16.705  12.963  1.00 29.12 ?  15  GLY A C     1 
ATOM   109  O O     . GLY A 1 23  ? 31.777  15.589  12.570  1.00 33.81 ?  15  GLY A O     1 
ATOM   110  N N     . THR A 1 24  ? 31.283  17.578  13.500  1.00 27.81 ?  16  THR A N     1 
ATOM   111  C CA    . THR A 1 24  ? 29.914  17.202  13.813  1.00 26.68 ?  16  THR A CA    1 
ATOM   112  C C     . THR A 1 24  ? 28.986  17.471  12.631  1.00 25.58 ?  16  THR A C     1 
ATOM   113  O O     . THR A 1 24  ? 29.206  18.410  11.858  1.00 23.49 ?  16  THR A O     1 
ATOM   114  C CB    . THR A 1 24  ? 29.421  17.967  15.038  1.00 27.41 ?  16  THR A CB    1 
ATOM   115  O OG1   . THR A 1 24  ? 29.636  19.369  14.847  1.00 22.68 ?  16  THR A OG1   1 
ATOM   116  C CG2   . THR A 1 24  ? 30.175  17.512  16.278  1.00 23.16 ?  16  THR A CG2   1 
ATOM   117  N N     . PRO A 1 25  ? 27.946  16.653  12.481  1.00 22.81 ?  17  PRO A N     1 
ATOM   118  C CA    . PRO A 1 25  ? 27.063  16.774  11.318  1.00 27.36 ?  17  PRO A CA    1 
ATOM   119  C C     . PRO A 1 25  ? 26.073  17.923  11.445  1.00 26.49 ?  17  PRO A C     1 
ATOM   120  O O     . PRO A 1 25  ? 25.792  18.434  12.532  1.00 27.91 ?  17  PRO A O     1 
ATOM   121  C CB    . PRO A 1 25  ? 26.331  15.427  11.294  1.00 28.02 ?  17  PRO A CB    1 
ATOM   122  C CG    . PRO A 1 25  ? 26.313  14.996  12.716  1.00 30.19 ?  17  PRO A CG    1 
ATOM   123  C CD    . PRO A 1 25  ? 27.605  15.486  13.315  1.00 25.35 ?  17  PRO A CD    1 
ATOM   124  N N     . VAL A 1 26  ? 25.534  18.312  10.289  1.00 27.15 ?  18  VAL A N     1 
ATOM   125  C CA    . VAL A 1 26  ? 24.541  19.373  10.174  1.00 24.92 ?  18  VAL A CA    1 
ATOM   126  C C     . VAL A 1 26  ? 23.304  18.800  9.496   1.00 29.43 ?  18  VAL A C     1 
ATOM   127  O O     . VAL A 1 26  ? 23.412  18.046  8.522   1.00 28.11 ?  18  VAL A O     1 
ATOM   128  C CB    . VAL A 1 26  ? 25.090  20.581  9.385   1.00 25.42 ?  18  VAL A CB    1 
ATOM   129  C CG1   . VAL A 1 26  ? 23.973  21.561  9.049   1.00 25.15 ?  18  VAL A CG1   1 
ATOM   130  C CG2   . VAL A 1 26  ? 26.189  21.273  10.174  1.00 24.32 ?  18  VAL A CG2   1 
ATOM   131  N N     . VAL A 1 27  ? 22.128  19.155  10.014  1.00 29.67 ?  19  VAL A N     1 
ATOM   132  C CA    . VAL A 1 27  ? 20.860  18.644  9.508   1.00 27.81 ?  19  VAL A CA    1 
ATOM   133  C C     . VAL A 1 27  ? 19.950  19.818  9.173   1.00 30.11 ?  19  VAL A C     1 
ATOM   134  O O     . VAL A 1 27  ? 19.843  20.771  9.954   1.00 31.56 ?  19  VAL A O     1 
ATOM   135  C CB    . VAL A 1 27  ? 20.180  17.702  10.521  1.00 30.17 ?  19  VAL A CB    1 
ATOM   136  C CG1   . VAL A 1 27  ? 18.879  17.155  9.952   1.00 25.57 ?  19  VAL A CG1   1 
ATOM   137  C CG2   . VAL A 1 27  ? 21.117  16.563  10.894  1.00 24.55 ?  19  VAL A CG2   1 
ATOM   138  N N     . LYS A 1 28  ? 19.303  19.749  8.012   1.00 30.86 ?  20  LYS A N     1 
ATOM   139  C CA    . LYS A 1 28  ? 18.307  20.736  7.622   1.00 31.03 ?  20  LYS A CA    1 
ATOM   140  C C     . LYS A 1 28  ? 16.955  20.382  8.230   1.00 27.89 ?  20  LYS A C     1 
ATOM   141  O O     . LYS A 1 28  ? 16.548  19.216  8.235   1.00 32.59 ?  20  LYS A O     1 
ATOM   142  C CB    . LYS A 1 28  ? 18.197  20.801  6.097   1.00 31.98 ?  20  LYS A CB    1 
ATOM   143  C CG    . LYS A 1 28  ? 17.195  21.817  5.568   1.00 31.19 ?  20  LYS A CG    1 
ATOM   144  C CD    . LYS A 1 28  ? 17.151  21.794  4.044   1.00 34.68 ?  20  LYS A CD    1 
ATOM   145  C CE    . LYS A 1 28  ? 16.368  22.973  3.481   1.00 40.93 ?  20  LYS A CE    1 
ATOM   146  N NZ    . LYS A 1 28  ? 14.982  23.050  4.024   1.00 42.47 ?  20  LYS A NZ    1 
ATOM   147  N N     . LEU A 1 29  ? 16.262  21.393  8.750   1.00 28.77 ?  21  LEU A N     1 
ATOM   148  C CA    . LEU A 1 29  ? 14.952  21.175  9.348   1.00 33.25 ?  21  LEU A CA    1 
ATOM   149  C C     . LEU A 1 29  ? 13.877  21.177  8.270   1.00 30.93 ?  21  LEU A C     1 
ATOM   150  O O     . LEU A 1 29  ? 13.930  21.965  7.323   1.00 33.81 ?  21  LEU A O     1 
ATOM   151  C CB    . LEU A 1 29  ? 14.657  22.245  10.400  1.00 26.68 ?  21  LEU A CB    1 
ATOM   152  C CG    . LEU A 1 29  ? 15.646  22.301  11.568  1.00 28.70 ?  21  LEU A CG    1 
ATOM   153  C CD1   . LEU A 1 29  ? 15.206  23.321  12.606  1.00 21.14 ?  21  LEU A CD1   1 
ATOM   154  C CD2   . LEU A 1 29  ? 15.818  20.925  12.199  1.00 26.45 ?  21  LEU A CD2   1 
ATOM   155  N N     . ARG A 1 30  ? 12.897  20.286  8.417   1.00 29.77 ?  22  ARG A N     1 
ATOM   156  C CA    . ARG A 1 30  ? 11.908  20.053  7.372   1.00 28.86 ?  22  ARG A CA    1 
ATOM   157  C C     . ARG A 1 30  ? 10.479  20.389  7.769   1.00 36.44 ?  22  ARG A C     1 
ATOM   158  O O     . ARG A 1 30  ? 9.692   20.767  6.899   1.00 32.45 ?  22  ARG A O     1 
ATOM   159  C CB    . ARG A 1 30  ? 11.947  18.584  6.920   1.00 33.15 ?  22  ARG A CB    1 
ATOM   160  C CG    . ARG A 1 30  ? 13.267  18.138  6.318   1.00 32.68 ?  22  ARG A CG    1 
ATOM   161  C CD    . ARG A 1 30  ? 13.303  16.625  6.171   1.00 31.68 ?  22  ARG A CD    1 
ATOM   162  N NE    . ARG A 1 30  ? 13.604  15.977  7.441   1.00 30.56 ?  22  ARG A NE    1 
ATOM   163  C CZ    . ARG A 1 30  ? 12.739  15.256  8.141   1.00 35.33 ?  22  ARG A CZ    1 
ATOM   164  N NH1   . ARG A 1 30  ? 11.504  15.049  7.713   1.00 40.24 ?  22  ARG A NH1   1 
ATOM   165  N NH2   . ARG A 1 30  ? 13.121  14.730  9.302   1.00 38.21 ?  22  ARG A NH2   1 
ATOM   166  N N     . ASN A 1 31  ? 10.116  20.262  9.042   1.00 28.52 ?  23  ASN A N     1 
ATOM   167  C CA    . ASN A 1 31  ? 8.717   20.334  9.439   1.00 35.40 ?  23  ASN A CA    1 
ATOM   168  C C     . ASN A 1 31  ? 8.400   21.433  10.440  1.00 37.91 ?  23  ASN A C     1 
ATOM   169  O O     . ASN A 1 31  ? 7.289   21.967  10.407  1.00 34.90 ?  23  ASN A O     1 
ATOM   170  C CB    . ASN A 1 31  ? 8.267   18.986  10.020  1.00 36.31 ?  23  ASN A CB    1 
ATOM   171  C CG    . ASN A 1 31  ? 8.403   17.851  9.023   1.00 40.21 ?  23  ASN A CG    1 
ATOM   172  O OD1   . ASN A 1 31  ? 7.889   17.926  7.908   1.00 36.80 ?  23  ASN A OD1   1 
ATOM   173  N ND2   . ASN A 1 31  ? 9.106   16.795  9.418   1.00 38.79 ?  23  ASN A ND2   1 
ATOM   174  N N     . VAL A 1 32  ? 9.330   21.787  11.331  1.00 31.18 ?  24  VAL A N     1 
ATOM   175  C CA    . VAL A 1 32  ? 9.039   22.812  12.332  1.00 32.41 ?  24  VAL A CA    1 
ATOM   176  C C     . VAL A 1 32  ? 9.134   24.224  11.780  1.00 36.11 ?  24  VAL A C     1 
ATOM   177  O O     . VAL A 1 32  ? 8.725   25.173  12.461  1.00 37.76 ?  24  VAL A O     1 
ATOM   178  C CB    . VAL A 1 32  ? 9.977   22.682  13.547  1.00 36.42 ?  24  VAL A CB    1 
ATOM   179  C CG1   . VAL A 1 32  ? 9.739   21.359  14.260  1.00 31.35 ?  24  VAL A CG1   1 
ATOM   180  C CG2   . VAL A 1 32  ? 11.431  22.816  13.119  1.00 31.20 ?  24  VAL A CG2   1 
ATOM   181  N N     . VAL A 1 33  ? 9.654   24.394  10.566  1.00 26.67 ?  25  VAL A N     1 
ATOM   182  C CA    . VAL A 1 33  ? 9.813   25.702  9.945   1.00 39.68 ?  25  VAL A CA    1 
ATOM   183  C C     . VAL A 1 33  ? 9.086   25.690  8.607   1.00 45.49 ?  25  VAL A C     1 
ATOM   184  O O     . VAL A 1 33  ? 9.165   24.712  7.855   1.00 42.72 ?  25  VAL A O     1 
ATOM   185  C CB    . VAL A 1 33  ? 11.305  26.067  9.777   1.00 40.44 ?  25  VAL A CB    1 
ATOM   186  C CG1   . VAL A 1 33  ? 12.143  24.814  9.568   1.00 31.87 ?  25  VAL A CG1   1 
ATOM   187  C CG2   . VAL A 1 33  ? 11.508  27.057  8.637   1.00 37.90 ?  25  VAL A CG2   1 
ATOM   188  N N     . ASP A 1 34  ? 8.370   26.776  8.320   1.00 46.41 ?  26  ASP A N     1 
ATOM   189  C CA    . ASP A 1 34  ? 7.536   26.862  7.132   1.00 58.14 ?  26  ASP A CA    1 
ATOM   190  C C     . ASP A 1 34  ? 8.377   26.836  5.856   1.00 58.88 ?  26  ASP A C     1 
ATOM   191  O O     . ASP A 1 34  ? 9.577   27.130  5.855   1.00 49.28 ?  26  ASP A O     1 
ATOM   192  C CB    . ASP A 1 34  ? 6.690   28.134  7.172   1.00 56.14 ?  26  ASP A CB    1 
ATOM   193  C CG    . ASP A 1 34  ? 5.491   28.068  6.248   1.00 64.60 ?  26  ASP A CG    1 
ATOM   194  O OD1   . ASP A 1 34  ? 5.385   27.092  5.477   1.00 69.70 ?  26  ASP A OD1   1 
ATOM   195  O OD2   . ASP A 1 34  ? 4.654   28.995  6.293   1.00 71.98 ?  26  ASP A OD2   1 
ATOM   196  N N     . ASP A 1 35  ? 7.717   26.479  4.750   1.00 60.33 ?  27  ASP A N     1 
ATOM   197  C CA    . ASP A 1 35  ? 8.377   26.460  3.451   1.00 63.20 ?  27  ASP A CA    1 
ATOM   198  C C     . ASP A 1 35  ? 8.647   27.860  2.915   1.00 59.70 ?  27  ASP A C     1 
ATOM   199  O O     . ASP A 1 35  ? 9.524   28.022  2.061   1.00 52.30 ?  27  ASP A O     1 
ATOM   200  C CB    . ASP A 1 35  ? 7.539   25.672  2.439   1.00 72.47 ?  27  ASP A CB    1 
ATOM   201  C CG    . ASP A 1 35  ? 6.173   25.287  2.981   1.00 73.88 ?  27  ASP A CG    1 
ATOM   202  O OD1   . ASP A 1 35  ? 6.065   24.221  3.624   1.00 66.22 ?  27  ASP A OD1   1 
ATOM   203  O OD2   . ASP A 1 35  ? 5.205   26.047  2.758   1.00 66.60 ?  27  ASP A OD2   1 
ATOM   204  N N     . ASN A 1 36  ? 7.918   28.871  3.388   1.00 55.48 ?  28  ASN A N     1 
ATOM   205  C CA    . ASN A 1 36  ? 8.138   30.249  2.969   1.00 56.48 ?  28  ASN A CA    1 
ATOM   206  C C     . ASN A 1 36  ? 9.102   30.995  3.885   1.00 48.81 ?  28  ASN A C     1 
ATOM   207  O O     . ASN A 1 36  ? 9.306   32.199  3.704   1.00 42.90 ?  28  ASN A O     1 
ATOM   208  C CB    . ASN A 1 36  ? 6.806   30.999  2.882   1.00 60.99 ?  28  ASN A CB    1 
ATOM   209  C CG    . ASN A 1 36  ? 5.996   30.903  4.157   1.00 63.01 ?  28  ASN A CG    1 
ATOM   210  O OD1   . ASN A 1 36  ? 6.422   31.367  5.214   1.00 65.40 ?  28  ASN A OD1   1 
ATOM   211  N ND2   . ASN A 1 36  ? 4.813   30.305  4.061   1.00 63.11 ?  28  ASN A ND2   1 
ATOM   212  N N     . ALA A 1 37  ? 9.690   30.311  4.858   1.00 42.57 ?  29  ALA A N     1 
ATOM   213  C CA    . ALA A 1 37  ? 10.771  30.856  5.662   1.00 42.82 ?  29  ALA A CA    1 
ATOM   214  C C     . ALA A 1 37  ? 12.116  30.414  5.092   1.00 39.93 ?  29  ALA A C     1 
ATOM   215  O O     . ALA A 1 37  ? 12.194  29.595  4.174   1.00 34.72 ?  29  ALA A O     1 
ATOM   216  C CB    . ALA A 1 37  ? 10.634  30.415  7.121   1.00 39.26 ?  29  ALA A CB    1 
ATOM   217  N N     . ALA A 1 38  ? 13.186  30.969  5.655   1.00 34.01 ?  30  ALA A N     1 
ATOM   218  C CA    . ALA A 1 38  ? 14.523  30.590  5.228   1.00 37.68 ?  30  ALA A CA    1 
ATOM   219  C C     . ALA A 1 38  ? 14.841  29.162  5.663   1.00 35.36 ?  30  ALA A C     1 
ATOM   220  O O     . ALA A 1 38  ? 14.237  28.612  6.588   1.00 36.67 ?  30  ALA A O     1 
ATOM   221  C CB    . ALA A 1 38  ? 15.564  31.554  5.797   1.00 34.10 ?  30  ALA A CB    1 
ATOM   222  N N     . ASP A 1 39  ? 15.802  28.555  4.971   1.00 37.12 ?  31  ASP A N     1 
ATOM   223  C CA    . ASP A 1 39  ? 16.291  27.247  5.380   1.00 33.26 ?  31  ASP A CA    1 
ATOM   224  C C     . ASP A 1 39  ? 16.983  27.350  6.733   1.00 33.59 ?  31  ASP A C     1 
ATOM   225  O O     . ASP A 1 39  ? 17.698  28.316  7.012   1.00 32.49 ?  31  ASP A O     1 
ATOM   226  C CB    . ASP A 1 39  ? 17.254  26.683  4.335   1.00 35.50 ?  31  ASP A CB    1 
ATOM   227  C CG    . ASP A 1 39  ? 16.578  26.414  3.007   1.00 33.31 ?  31  ASP A CG    1 
ATOM   228  O OD1   . ASP A 1 39  ? 15.341  26.254  2.989   1.00 39.71 ?  31  ASP A OD1   1 
ATOM   229  O OD2   . ASP A 1 39  ? 17.287  26.355  1.981   1.00 39.17 ?  31  ASP A OD2   1 
ATOM   230  N N     . VAL A 1 40  ? 16.759  26.352  7.583   1.00 33.14 ?  32  VAL A N     1 
ATOM   231  C CA    . VAL A 1 40  ? 17.327  26.323  8.925   1.00 29.59 ?  32  VAL A CA    1 
ATOM   232  C C     . VAL A 1 40  ? 18.162  25.059  9.061   1.00 27.44 ?  32  VAL A C     1 
ATOM   233  O O     . VAL A 1 40  ? 17.643  23.945  8.913   1.00 26.03 ?  32  VAL A O     1 
ATOM   234  C CB    . VAL A 1 40  ? 16.242  26.378  10.010  1.00 24.62 ?  32  VAL A CB    1 
ATOM   235  C CG1   . VAL A 1 40  ? 16.884  26.382  11.388  1.00 24.06 ?  32  VAL A CG1   1 
ATOM   236  C CG2   . VAL A 1 40  ? 15.362  27.600  9.818   1.00 30.31 ?  32  VAL A CG2   1 
ATOM   237  N N     . TYR A 1 41  ? 19.449  25.232  9.347   1.00 25.96 ?  33  TYR A N     1 
ATOM   238  C CA    . TYR A 1 41  ? 20.382  24.130  9.526   1.00 24.63 ?  33  TYR A CA    1 
ATOM   239  C C     . TYR A 1 41  ? 20.872  24.120  10.966  1.00 24.05 ?  33  TYR A C     1 
ATOM   240  O O     . TYR A 1 41  ? 21.171  25.174  11.536  1.00 27.39 ?  33  TYR A O     1 
ATOM   241  C CB    . TYR A 1 41  ? 21.568  24.253  8.566   1.00 26.85 ?  33  TYR A CB    1 
ATOM   242  C CG    . TYR A 1 41  ? 21.194  24.120  7.106   1.00 29.62 ?  33  TYR A CG    1 
ATOM   243  C CD1   . TYR A 1 41  ? 20.822  25.232  6.360   1.00 30.25 ?  33  TYR A CD1   1 
ATOM   244  C CD2   . TYR A 1 41  ? 21.223  22.886  6.469   1.00 32.31 ?  33  TYR A CD2   1 
ATOM   245  C CE1   . TYR A 1 41  ? 20.481  25.117  5.024   1.00 32.58 ?  33  TYR A CE1   1 
ATOM   246  C CE2   . TYR A 1 41  ? 20.886  22.762  5.133   1.00 34.02 ?  33  TYR A CE2   1 
ATOM   247  C CZ    . TYR A 1 41  ? 20.515  23.880  4.416   1.00 33.42 ?  33  TYR A CZ    1 
ATOM   248  O OH    . TYR A 1 41  ? 20.179  23.757  3.088   1.00 38.69 ?  33  TYR A OH    1 
ATOM   249  N N     . VAL A 1 42  ? 20.950  22.928  11.554  1.00 25.35 ?  34  VAL A N     1 
ATOM   250  C CA    . VAL A 1 42  ? 21.362  22.756  12.942  1.00 26.23 ?  34  VAL A CA    1 
ATOM   251  C C     . VAL A 1 42  ? 22.583  21.843  12.980  1.00 24.73 ?  34  VAL A C     1 
ATOM   252  O O     . VAL A 1 42  ? 22.613  20.805  12.309  1.00 28.09 ?  34  VAL A O     1 
ATOM   253  C CB    . VAL A 1 42  ? 20.219  22.198  13.814  1.00 25.10 ?  34  VAL A CB    1 
ATOM   254  C CG1   . VAL A 1 42  ? 19.060  23.181  13.860  1.00 25.24 ?  34  VAL A CG1   1 
ATOM   255  C CG2   . VAL A 1 42  ? 19.730  20.856  13.293  1.00 25.82 ?  34  VAL A CG2   1 
ATOM   256  N N     . LYS A 1 43  ? 23.593  22.242  13.748  1.00 23.94 ?  35  LYS A N     1 
ATOM   257  C CA    . LYS A 1 43  ? 24.818  21.471  13.920  1.00 21.96 ?  35  LYS A CA    1 
ATOM   258  C C     . LYS A 1 43  ? 24.702  20.674  15.215  1.00 27.94 ?  35  LYS A C     1 
ATOM   259  O O     . LYS A 1 43  ? 24.521  21.254  16.292  1.00 26.20 ?  35  LYS A O     1 
ATOM   260  C CB    . LYS A 1 43  ? 26.038  22.393  13.949  1.00 27.49 ?  35  LYS A CB    1 
ATOM   261  C CG    . LYS A 1 43  ? 27.391  21.703  13.802  1.00 25.74 ?  35  LYS A CG    1 
ATOM   262  C CD    . LYS A 1 43  ? 28.466  22.714  13.403  1.00 20.72 ?  35  LYS A CD    1 
ATOM   263  C CE    . LYS A 1 43  ? 29.866  22.119  13.448  1.00 25.88 ?  35  LYS A CE    1 
ATOM   264  N NZ    . LYS A 1 43  ? 30.006  20.935  12.551  1.00 24.14 ?  35  LYS A NZ    1 
ATOM   265  N N     . LEU A 1 44  ? 24.794  19.350  15.109  1.00 25.68 ?  36  LEU A N     1 
ATOM   266  C CA    . LEU A 1 44  ? 24.538  18.462  16.243  1.00 27.86 ?  36  LEU A CA    1 
ATOM   267  C C     . LEU A 1 44  ? 25.835  18.273  17.017  1.00 29.44 ?  36  LEU A C     1 
ATOM   268  O O     . LEU A 1 44  ? 26.614  17.355  16.755  1.00 26.08 ?  36  LEU A O     1 
ATOM   269  C CB    . LEU A 1 44  ? 23.977  17.133  15.761  1.00 26.16 ?  36  LEU A CB    1 
ATOM   270  C CG    . LEU A 1 44  ? 22.905  17.235  14.681  1.00 28.47 ?  36  LEU A CG    1 
ATOM   271  C CD1   . LEU A 1 44  ? 22.641  15.864  14.118  1.00 30.16 ?  36  LEU A CD1   1 
ATOM   272  C CD2   . LEU A 1 44  ? 21.629  17.843  15.240  1.00 23.60 ?  36  LEU A CD2   1 
ATOM   273  N N     . GLU A 1 45  ? 26.067  19.151  17.994  1.00 26.04 ?  37  GLU A N     1 
ATOM   274  C CA    . GLU A 1 45  ? 27.282  19.044  18.790  1.00 27.87 ?  37  GLU A CA    1 
ATOM   275  C C     . GLU A 1 45  ? 27.216  17.924  19.817  1.00 30.29 ?  37  GLU A C     1 
ATOM   276  O O     . GLU A 1 45  ? 28.240  17.618  20.438  1.00 25.16 ?  37  GLU A O     1 
ATOM   277  C CB    . GLU A 1 45  ? 27.576  20.374  19.480  1.00 23.24 ?  37  GLU A CB    1 
ATOM   278  C CG    . GLU A 1 45  ? 28.172  21.414  18.546  1.00 22.27 ?  37  GLU A CG    1 
ATOM   279  C CD    . GLU A 1 45  ? 29.557  21.029  18.058  1.00 27.55 ?  37  GLU A CD    1 
ATOM   280  O OE1   . GLU A 1 45  ? 30.401  20.648  18.897  1.00 24.60 ?  37  GLU A OE1   1 
ATOM   281  O OE2   . GLU A 1 45  ? 29.803  21.106  16.834  1.00 24.13 ?  37  GLU A OE2   1 
ATOM   282  N N     . TYR A 1 46  ? 26.053  17.302  20.009  1.00 24.78 ?  38  TYR A N     1 
ATOM   283  C CA    . TYR A 1 46  ? 25.983  16.134  20.872  1.00 23.95 ?  38  TYR A CA    1 
ATOM   284  C C     . TYR A 1 46  ? 26.536  14.882  20.204  1.00 25.95 ?  38  TYR A C     1 
ATOM   285  O O     . TYR A 1 46  ? 26.652  13.844  20.864  1.00 25.66 ?  38  TYR A O     1 
ATOM   286  C CB    . TYR A 1 46  ? 24.541  15.898  21.338  1.00 29.29 ?  38  TYR A CB    1 
ATOM   287  C CG    . TYR A 1 46  ? 23.515  15.718  20.238  1.00 25.45 ?  38  TYR A CG    1 
ATOM   288  C CD1   . TYR A 1 46  ? 23.429  14.528  19.527  1.00 23.40 ?  38  TYR A CD1   1 
ATOM   289  C CD2   . TYR A 1 46  ? 22.611  16.728  19.935  1.00 26.67 ?  38  TYR A CD2   1 
ATOM   290  C CE1   . TYR A 1 46  ? 22.488  14.355  18.533  1.00 25.63 ?  38  TYR A CE1   1 
ATOM   291  C CE2   . TYR A 1 46  ? 21.662  16.563  18.941  1.00 27.86 ?  38  TYR A CE2   1 
ATOM   292  C CZ    . TYR A 1 46  ? 21.607  15.373  18.244  1.00 28.66 ?  38  TYR A CZ    1 
ATOM   293  O OH    . TYR A 1 46  ? 20.668  15.198  17.254  1.00 24.64 ?  38  TYR A OH    1 
ATOM   294  N N     . GLN A 1 47  ? 26.878  14.955  18.916  1.00 27.08 ?  39  GLN A N     1 
ATOM   295  C CA    . GLN A 1 47  ? 27.556  13.849  18.256  1.00 24.33 ?  39  GLN A CA    1 
ATOM   296  C C     . GLN A 1 47  ? 29.012  13.719  18.684  1.00 26.39 ?  39  GLN A C     1 
ATOM   297  O O     . GLN A 1 47  ? 29.655  12.724  18.334  1.00 27.50 ?  39  GLN A O     1 
ATOM   298  C CB    . GLN A 1 47  ? 27.461  14.010  16.738  1.00 27.56 ?  39  GLN A CB    1 
ATOM   299  C CG    . GLN A 1 47  ? 26.112  13.607  16.166  1.00 25.39 ?  39  GLN A CG    1 
ATOM   300  C CD    . GLN A 1 47  ? 25.770  12.159  16.461  1.00 26.88 ?  39  GLN A CD    1 
ATOM   301  O OE1   . GLN A 1 47  ? 25.131  11.851  17.469  1.00 26.40 ?  39  GLN A OE1   1 
ATOM   302  N NE2   . GLN A 1 47  ? 26.199  11.260  15.583  1.00 27.62 ?  39  GLN A NE2   1 
ATOM   303  N N     . ASN A 1 48  ? 29.545  14.694  19.419  1.00 24.80 ?  40  ASN A N     1 
ATOM   304  C CA    . ASN A 1 48  ? 30.853  14.531  20.031  1.00 25.96 ?  40  ASN A CA    1 
ATOM   305  C C     . ASN A 1 48  ? 30.822  13.328  20.976  1.00 27.96 ?  40  ASN A C     1 
ATOM   306  O O     . ASN A 1 48  ? 29.785  13.038  21.582  1.00 24.54 ?  40  ASN A O     1 
ATOM   307  C CB    . ASN A 1 48  ? 31.248  15.799  20.790  1.00 21.34 ?  40  ASN A CB    1 
ATOM   308  C CG    . ASN A 1 48  ? 31.673  16.934  19.867  1.00 25.35 ?  40  ASN A CG    1 
ATOM   309  O OD1   . ASN A 1 48  ? 32.575  16.777  19.043  1.00 23.88 ?  40  ASN A OD1   1 
ATOM   310  N ND2   . ASN A 1 48  ? 31.028  18.087  20.012  1.00 25.96 ?  40  ASN A ND2   1 
ATOM   311  N N     . PRO A 1 49  ? 31.941  12.606  21.119  1.00 26.56 ?  41  PRO A N     1 
ATOM   312  C CA    . PRO A 1 49  ? 31.900  11.346  21.887  1.00 26.66 ?  41  PRO A CA    1 
ATOM   313  C C     . PRO A 1 49  ? 31.454  11.511  23.332  1.00 25.86 ?  41  PRO A C     1 
ATOM   314  O O     . PRO A 1 49  ? 30.856  10.584  23.892  1.00 25.47 ?  41  PRO A O     1 
ATOM   315  C CB    . PRO A 1 49  ? 33.346  10.839  21.803  1.00 21.35 ?  41  PRO A CB    1 
ATOM   316  C CG    . PRO A 1 49  ? 34.162  12.055  21.508  1.00 26.68 ?  41  PRO A CG    1 
ATOM   317  C CD    . PRO A 1 49  ? 33.294  12.893  20.615  1.00 26.51 ?  41  PRO A CD    1 
ATOM   318  N N     . GLY A 1 50  ? 31.724  12.656  23.958  1.00 26.52 ?  42  GLY A N     1 
ATOM   319  C CA    . GLY A 1 50  ? 31.255  12.874  25.314  1.00 27.05 ?  42  GLY A CA    1 
ATOM   320  C C     . GLY A 1 50  ? 29.825  13.347  25.424  1.00 29.48 ?  42  GLY A C     1 
ATOM   321  O O     . GLY A 1 50  ? 29.290  13.404  26.536  1.00 25.36 ?  42  GLY A O     1 
ATOM   322  N N     . GLY A 1 51  ? 29.204  13.706  24.303  1.00 26.16 ?  43  GLY A N     1 
ATOM   323  C CA    . GLY A 1 51  ? 27.787  14.005  24.266  1.00 28.40 ?  43  GLY A CA    1 
ATOM   324  C C     . GLY A 1 51  ? 27.402  15.468  24.272  1.00 31.17 ?  43  GLY A C     1 
ATOM   325  O O     . GLY A 1 51  ? 26.210  15.768  24.392  1.00 25.60 ?  43  GLY A O     1 
ATOM   326  N N     . SER A 1 52  ? 28.356  16.386  24.143  1.00 26.96 ?  44  SER A N     1 
ATOM   327  C CA    . SER A 1 52  ? 28.028  17.805  24.179  1.00 27.22 ?  44  SER A CA    1 
ATOM   328  C C     . SER A 1 52  ? 29.139  18.599  23.507  1.00 29.38 ?  44  SER A C     1 
ATOM   329  O O     . SER A 1 52  ? 30.228  18.085  23.237  1.00 27.95 ?  44  SER A O     1 
ATOM   330  C CB    . SER A 1 52  ? 27.807  18.292  25.617  1.00 25.48 ?  44  SER A CB    1 
ATOM   331  O OG    . SER A 1 52  ? 28.945  18.978  26.110  1.00 27.09 ?  44  SER A OG    1 
ATOM   332  N N     . VAL A 1 53  ? 28.845  19.869  23.253  1.00 25.51 ?  45  VAL A N     1 
ATOM   333  C CA    . VAL A 1 53  ? 29.789  20.810  22.664  1.00 27.43 ?  45  VAL A CA    1 
ATOM   334  C C     . VAL A 1 53  ? 31.002  21.023  23.575  1.00 25.52 ?  45  VAL A C     1 
ATOM   335  O O     . VAL A 1 53  ? 32.075  21.416  23.114  1.00 27.58 ?  45  VAL A O     1 
ATOM   336  C CB    . VAL A 1 53  ? 29.086  22.151  22.360  1.00 24.48 ?  45  VAL A CB    1 
ATOM   337  C CG1   . VAL A 1 53  ? 28.690  22.851  23.652  1.00 24.62 ?  45  VAL A CG1   1 
ATOM   338  C CG2   . VAL A 1 53  ? 29.961  23.048  21.495  1.00 22.02 ?  45  VAL A CG2   1 
HETATM 339  N N1    . LLP A 1 54  ? 23.886  24.806  25.844  0.98 26.21 ?  46  LLP A N1    1 
HETATM 340  C C2    . LLP A 1 54  ? 24.459  23.868  26.598  0.98 28.58 ?  46  LLP A C2    1 
HETATM 341  C "C2'" . LLP A 1 54  ? 23.657  22.583  26.959  0.98 24.66 ?  46  LLP A "C2'" 1 
HETATM 342  C C3    . LLP A 1 54  ? 25.791  24.049  27.064  0.98 30.26 ?  46  LLP A C3    1 
HETATM 343  O O3    . LLP A 1 54  ? 26.384  23.056  27.857  0.98 29.82 ?  46  LLP A O3    1 
HETATM 344  C C4    . LLP A 1 54  ? 26.491  25.191  26.733  0.98 29.01 ?  46  LLP A C4    1 
HETATM 345  C "C4'" . LLP A 1 54  ? 28.000  25.385  27.276  0.98 29.24 ?  46  LLP A "C4'" 1 
HETATM 346  C C5    . LLP A 1 54  ? 25.900  26.149  25.959  0.98 29.60 ?  46  LLP A C5    1 
HETATM 347  C C6    . LLP A 1 54  ? 24.588  25.967  25.505  0.98 25.66 ?  46  LLP A C6    1 
HETATM 348  C "C5'" . LLP A 1 54  ? 26.634  27.467  25.559  0.98 25.93 ?  46  LLP A "C5'" 1 
HETATM 349  O OP4   . LLP A 1 54  ? 27.799  27.224  24.804  0.98 27.13 ?  46  LLP A OP4   1 
HETATM 350  P P     . LLP A 1 54  ? 28.931  28.263  24.951  0.98 29.68 ?  46  LLP A P     1 
HETATM 351  O OP1   . LLP A 1 54  ? 29.552  28.115  26.348  0.98 24.16 ?  46  LLP A OP1   1 
HETATM 352  O OP2   . LLP A 1 54  ? 28.367  29.621  24.803  0.98 22.46 ?  46  LLP A OP2   1 
HETATM 353  O OP3   . LLP A 1 54  ? 29.972  28.036  23.910  0.98 24.04 ?  46  LLP A OP3   1 
HETATM 354  N N     . LLP A 1 54  ? 30.836  20.746  24.866  0.98 23.33 ?  46  LLP A N     1 
HETATM 355  C CA    . LLP A 1 54  ? 31.903  20.974  25.853  0.98 26.47 ?  46  LLP A CA    1 
HETATM 356  C CB    . LLP A 1 54  ? 31.353  20.812  27.246  0.98 23.51 ?  46  LLP A CB    1 
HETATM 357  C CG    . LLP A 1 54  ? 30.308  21.899  27.501  0.98 26.86 ?  46  LLP A CG    1 
HETATM 358  C CD    . LLP A 1 54  ? 30.938  23.284  27.288  0.98 26.16 ?  46  LLP A CD    1 
HETATM 359  C CE    . LLP A 1 54  ? 30.017  24.359  27.898  0.98 26.06 ?  46  LLP A CE    1 
HETATM 360  N NZ    . LLP A 1 54  ? 28.626  24.116  27.490  0.98 28.38 ?  46  LLP A NZ    1 
HETATM 361  C C     . LLP A 1 54  ? 33.060  20.056  25.652  0.98 27.64 ?  46  LLP A C     1 
HETATM 362  O O     . LLP A 1 54  ? 34.119  20.296  26.214  0.98 25.90 ?  46  LLP A O     1 
ATOM   363  N N     . ASP A 1 55  ? 32.870  18.997  24.868  1.00 26.02 ?  47  ASP A N     1 
ATOM   364  C CA    . ASP A 1 55  ? 33.963  18.107  24.481  1.00 23.14 ?  47  ASP A CA    1 
ATOM   365  C C     . ASP A 1 55  ? 35.107  18.902  23.868  1.00 28.02 ?  47  ASP A C     1 
ATOM   366  O O     . ASP A 1 55  ? 36.279  18.648  24.146  1.00 24.49 ?  47  ASP A O     1 
ATOM   367  C CB    . ASP A 1 55  ? 33.487  17.058  23.476  1.00 26.08 ?  47  ASP A CB    1 
ATOM   368  C CG    . ASP A 1 55  ? 32.839  15.858  24.133  1.00 27.93 ?  47  ASP A CG    1 
ATOM   369  O OD1   . ASP A 1 55  ? 32.381  15.965  25.290  1.00 31.29 ?  47  ASP A OD1   1 
ATOM   370  O OD2   . ASP A 1 55  ? 32.792  14.798  23.473  1.00 28.71 ?  47  ASP A OD2   1 
ATOM   371  N N     . ARG A 1 56  ? 34.737  19.870  23.027  1.00 27.91 ?  48  ARG A N     1 
ATOM   372  C CA    . ARG A 1 56  ? 35.725  20.668  22.309  1.00 29.09 ?  48  ARG A CA    1 
ATOM   373  C C     . ARG A 1 56  ? 36.575  21.492  23.267  1.00 25.36 ?  48  ARG A C     1 
ATOM   374  O O     . ARG A 1 56  ? 37.810  21.456  23.210  1.00 23.90 ?  48  ARG A O     1 
ATOM   375  C CB    . ARG A 1 56  ? 35.020  21.578  21.303  1.00 25.41 ?  48  ARG A CB    1 
ATOM   376  C CG    . ARG A 1 56  ? 34.366  20.851  20.139  1.00 27.43 ?  48  ARG A CG    1 
ATOM   377  C CD    . ARG A 1 56  ? 33.762  21.847  19.164  1.00 24.06 ?  48  ARG A CD    1 
ATOM   378  N NE    . ARG A 1 56  ? 32.944  21.210  18.139  1.00 22.09 ?  48  ARG A NE    1 
ATOM   379  C CZ    . ARG A 1 56  ? 33.376  20.900  16.924  1.00 25.36 ?  48  ARG A CZ    1 
ATOM   380  N NH1   . ARG A 1 56  ? 34.624  21.134  16.552  1.00 21.05 ?  48  ARG A NH1   1 
ATOM   381  N NH2   . ARG A 1 56  ? 32.534  20.341  16.059  1.00 23.27 ?  48  ARG A NH2   1 
ATOM   382  N N     . ILE A 1 57  ? 35.929  22.250  24.155  1.00 25.02 ?  49  ILE A N     1 
ATOM   383  C CA    . ILE A 1 57  ? 36.678  23.153  25.023  1.00 27.56 ?  49  ILE A CA    1 
ATOM   384  C C     . ILE A 1 57  ? 37.381  22.388  26.138  1.00 27.65 ?  49  ILE A C     1 
ATOM   385  O O     . ILE A 1 57  ? 38.423  22.830  26.634  1.00 21.84 ?  49  ILE A O     1 
ATOM   386  C CB    . ILE A 1 57  ? 35.758  24.255  25.580  1.00 23.14 ?  49  ILE A CB    1 
ATOM   387  C CG1   . ILE A 1 57  ? 34.841  23.715  26.682  1.00 27.82 ?  49  ILE A CG1   1 
ATOM   388  C CG2   . ILE A 1 57  ? 34.943  24.875  24.454  1.00 19.86 ?  49  ILE A CG2   1 
ATOM   389  C CD1   . ILE A 1 57  ? 34.274  24.796  27.590  1.00 24.36 ?  49  ILE A CD1   1 
ATOM   390  N N     . ALA A 1 58  ? 36.846  21.236  26.544  1.00 24.70 ?  50  ALA A N     1 
ATOM   391  C CA    . ALA A 1 58  ? 37.529  20.425  27.546  1.00 25.38 ?  50  ALA A CA    1 
ATOM   392  C C     . ALA A 1 58  ? 38.872  19.933  27.020  1.00 28.01 ?  50  ALA A C     1 
ATOM   393  O O     . ALA A 1 58  ? 39.894  20.024  27.708  1.00 26.01 ?  50  ALA A O     1 
ATOM   394  C CB    . ALA A 1 58  ? 36.645  19.251  27.965  1.00 25.05 ?  50  ALA A CB    1 
ATOM   395  N N     . LEU A 1 59  ? 38.887  19.412  25.790  1.00 29.63 ?  51  LEU A N     1 
ATOM   396  C CA    . LEU A 1 59  ? 40.142  18.986  25.180  1.00 26.66 ?  51  LEU A CA    1 
ATOM   397  C C     . LEU A 1 59  ? 41.053  20.173  24.899  1.00 29.50 ?  51  LEU A C     1 
ATOM   398  O O     . LEU A 1 59  ? 42.271  20.090  25.097  1.00 29.98 ?  51  LEU A O     1 
ATOM   399  C CB    . LEU A 1 59  ? 39.863  18.216  23.890  1.00 23.36 ?  51  LEU A CB    1 
ATOM   400  C CG    . LEU A 1 59  ? 41.106  17.756  23.126  1.00 33.19 ?  51  LEU A CG    1 
ATOM   401  C CD1   . LEU A 1 59  ? 41.930  16.790  23.966  1.00 31.15 ?  51  LEU A CD1   1 
ATOM   402  C CD2   . LEU A 1 59  ? 40.721  17.131  21.795  1.00 32.83 ?  51  LEU A CD2   1 
ATOM   403  N N     . ALA A 1 60  ? 40.481  21.287  24.437  1.00 27.62 ?  52  ALA A N     1 
ATOM   404  C CA    . ALA A 1 60  ? 41.291  22.449  24.091  1.00 31.41 ?  52  ALA A CA    1 
ATOM   405  C C     . ALA A 1 60  ? 41.969  23.041  25.319  1.00 25.83 ?  52  ALA A C     1 
ATOM   406  O O     . ALA A 1 60  ? 43.153  23.393  25.274  1.00 27.30 ?  52  ALA A O     1 
ATOM   407  C CB    . ALA A 1 60  ? 40.425  23.502  23.402  1.00 25.62 ?  52  ALA A CB    1 
ATOM   408  N N     . MET A 1 61  ? 41.236  23.160  26.427  1.00 26.08 ?  53  MET A N     1 
ATOM   409  C CA    . MET A 1 61  ? 41.808  23.767  27.624  1.00 23.55 ?  53  MET A CA    1 
ATOM   410  C C     . MET A 1 61  ? 42.901  22.893  28.229  1.00 27.53 ?  53  MET A C     1 
ATOM   411  O O     . MET A 1 61  ? 43.862  23.417  28.802  1.00 30.19 ?  53  MET A O     1 
ATOM   412  C CB    . MET A 1 61  ? 40.707  24.045  28.650  1.00 25.91 ?  53  MET A CB    1 
ATOM   413  C CG    . MET A 1 61  ? 39.983  25.370  28.435  1.00 27.59 ?  53  MET A CG    1 
ATOM   414  S SD    . MET A 1 61  ? 38.699  25.695  29.662  1.00 28.69 ?  53  MET A SD    1 
ATOM   415  C CE    . MET A 1 61  ? 37.568  24.339  29.361  1.00 20.89 ?  53  MET A CE    1 
ATOM   416  N N     . ILE A 1 62  ? 42.780  21.568  28.104  1.00 29.07 ?  54  ILE A N     1 
ATOM   417  C CA    . ILE A 1 62  ? 43.813  20.676  28.624  1.00 25.68 ?  54  ILE A CA    1 
ATOM   418  C C     . ILE A 1 62  ? 45.045  20.713  27.728  1.00 30.11 ?  54  ILE A C     1 
ATOM   419  O O     . ILE A 1 62  ? 46.181  20.796  28.209  1.00 28.58 ?  54  ILE A O     1 
ATOM   420  C CB    . ILE A 1 62  ? 43.265  19.245  28.770  1.00 31.45 ?  54  ILE A CB    1 
ATOM   421  C CG1   . ILE A 1 62  ? 42.311  19.155  29.963  1.00 33.15 ?  54  ILE A CG1   1 
ATOM   422  C CG2   . ILE A 1 62  ? 44.406  18.242  28.914  1.00 30.52 ?  54  ILE A CG2   1 
ATOM   423  C CD1   . ILE A 1 62  ? 42.984  19.369  31.303  1.00 37.14 ?  54  ILE A CD1   1 
ATOM   424  N N     . GLU A 1 63  ? 44.837  20.658  26.410  1.00 28.60 ?  55  GLU A N     1 
ATOM   425  C CA    . GLU A 1 63  ? 45.962  20.693  25.481  1.00 26.97 ?  55  GLU A CA    1 
ATOM   426  C C     . GLU A 1 63  ? 46.728  22.005  25.593  1.00 31.21 ?  55  GLU A C     1 
ATOM   427  O O     . GLU A 1 63  ? 47.961  22.021  25.497  1.00 31.65 ?  55  GLU A O     1 
ATOM   428  C CB    . GLU A 1 63  ? 45.468  20.478  24.050  1.00 26.72 ?  55  GLU A CB    1 
ATOM   429  C CG    . GLU A 1 63  ? 45.084  19.040  23.730  1.00 28.37 ?  55  GLU A CG    1 
ATOM   430  C CD    . GLU A 1 63  ? 44.539  18.881  22.321  1.00 30.70 ?  55  GLU A CD    1 
ATOM   431  O OE1   . GLU A 1 63  ? 44.196  19.905  21.693  1.00 31.34 ?  55  GLU A OE1   1 
ATOM   432  O OE2   . GLU A 1 63  ? 44.453  17.730  21.840  1.00 29.45 ?  55  GLU A OE2   1 
ATOM   433  N N     . LYS A 1 64  ? 46.016  23.115  25.802  1.00 29.50 ?  56  LYS A N     1 
ATOM   434  C CA    . LYS A 1 64  ? 46.679  24.406  25.964  1.00 27.98 ?  56  LYS A CA    1 
ATOM   435  C C     . LYS A 1 64  ? 47.592  24.404  27.185  1.00 31.67 ?  56  LYS A C     1 
ATOM   436  O O     . LYS A 1 64  ? 48.754  24.823  27.107  1.00 30.29 ?  56  LYS A O     1 
ATOM   437  C CB    . LYS A 1 64  ? 45.635  25.518  26.073  1.00 29.87 ?  56  LYS A CB    1 
ATOM   438  C CG    . LYS A 1 64  ? 46.222  26.886  26.384  1.00 31.78 ?  56  LYS A CG    1 
ATOM   439  C CD    . LYS A 1 64  ? 45.152  27.965  26.415  1.00 34.18 ?  56  LYS A CD    1 
ATOM   440  C CE    . LYS A 1 64  ? 45.758  29.330  26.709  1.00 40.10 ?  56  LYS A CE    1 
ATOM   441  N NZ    . LYS A 1 64  ? 45.579  29.715  28.139  1.00 37.18 ?  56  LYS A NZ    1 
ATOM   442  N N     . ALA A 1 65  ? 47.080  23.934  28.326  1.00 26.17 ?  57  ALA A N     1 
ATOM   443  C CA    . ALA A 1 65  ? 47.903  23.862  29.529  1.00 28.67 ?  57  ALA A CA    1 
ATOM   444  C C     . ALA A 1 65  ? 49.038  22.858  29.374  1.00 33.81 ?  57  ALA A C     1 
ATOM   445  O O     . ALA A 1 65  ? 50.068  22.981  30.047  1.00 29.10 ?  57  ALA A O     1 
ATOM   446  C CB    . ALA A 1 65  ? 47.038  23.510  30.738  1.00 23.57 ?  57  ALA A CB    1 
ATOM   447  N N     . GLU A 1 66  ? 48.874  21.864  28.497  1.00 31.81 ?  58  GLU A N     1 
ATOM   448  C CA    . GLU A 1 66  ? 49.956  20.919  28.237  1.00 28.08 ?  58  GLU A CA    1 
ATOM   449  C C     . GLU A 1 66  ? 51.075  21.574  27.439  1.00 31.17 ?  58  GLU A C     1 
ATOM   450  O O     . GLU A 1 66  ? 52.257  21.436  27.776  1.00 27.50 ?  58  GLU A O     1 
ATOM   451  C CB    . GLU A 1 66  ? 49.421  19.696  27.495  1.00 23.61 ?  58  GLU A CB    1 
ATOM   452  C CG    . GLU A 1 66  ? 48.675  18.722  28.376  1.00 28.62 ?  58  GLU A CG    1 
ATOM   453  C CD    . GLU A 1 66  ? 48.209  17.496  27.622  1.00 29.63 ?  58  GLU A CD    1 
ATOM   454  O OE1   . GLU A 1 66  ? 47.908  17.616  26.415  1.00 33.76 ?  58  GLU A OE1   1 
ATOM   455  O OE2   . GLU A 1 66  ? 48.142  16.409  28.237  1.00 33.39 ?  58  GLU A OE2   1 
ATOM   456  N N     . ARG A 1 67  ? 50.719  22.290  26.369  1.00 27.35 ?  59  ARG A N     1 
ATOM   457  C CA    . ARG A 1 67  ? 51.722  22.947  25.539  1.00 31.64 ?  59  ARG A CA    1 
ATOM   458  C C     . ARG A 1 67  ? 52.463  24.045  26.289  1.00 34.96 ?  59  ARG A C     1 
ATOM   459  O O     . ARG A 1 67  ? 53.558  24.434  25.871  1.00 38.02 ?  59  ARG A O     1 
ATOM   460  C CB    . ARG A 1 67  ? 51.068  23.531  24.286  1.00 37.72 ?  59  ARG A CB    1 
ATOM   461  C CG    . ARG A 1 67  ? 50.311  22.519  23.440  1.00 42.54 ?  59  ARG A CG    1 
ATOM   462  C CD    . ARG A 1 67  ? 50.129  23.021  22.012  1.00 46.11 ?  59  ARG A CD    1 
ATOM   463  N NE    . ARG A 1 67  ? 49.411  24.290  21.957  1.00 57.13 ?  59  ARG A NE    1 
ATOM   464  C CZ    . ARG A 1 67  ? 48.091  24.410  22.009  1.00 54.53 ?  59  ARG A CZ    1 
ATOM   465  N NH1   . ARG A 1 67  ? 47.303  23.352  22.112  1.00 44.82 ?  59  ARG A NH1   1 
ATOM   466  N NH2   . ARG A 1 67  ? 47.548  25.623  21.953  1.00 52.12 ?  59  ARG A NH2   1 
ATOM   467  N N     . GLU A 1 68  ? 51.897  24.551  27.382  1.00 31.46 ?  60  GLU A N     1 
ATOM   468  C CA    . GLU A 1 68  ? 52.510  25.620  28.155  1.00 33.33 ?  60  GLU A CA    1 
ATOM   469  C C     . GLU A 1 68  ? 53.287  25.115  29.362  1.00 35.64 ?  60  GLU A C     1 
ATOM   470  O O     . GLU A 1 68  ? 53.837  25.928  30.111  1.00 38.20 ?  60  GLU A O     1 
ATOM   471  C CB    . GLU A 1 68  ? 51.440  26.614  28.614  1.00 32.46 ?  60  GLU A CB    1 
ATOM   472  C CG    . GLU A 1 68  ? 50.909  27.493  27.501  1.00 30.54 ?  60  GLU A CG    1 
ATOM   473  C CD    . GLU A 1 68  ? 49.539  28.048  27.811  1.00 29.81 ?  60  GLU A CD    1 
ATOM   474  O OE1   . GLU A 1 68  ? 49.093  27.924  28.972  1.00 27.82 ?  60  GLU A OE1   1 
ATOM   475  O OE2   . GLU A 1 68  ? 48.907  28.605  26.891  1.00 29.74 ?  60  GLU A OE2   1 
ATOM   476  N N     . GLY A 1 69  ? 53.350  23.802  29.568  1.00 36.44 ?  61  GLY A N     1 
ATOM   477  C CA    . GLY A 1 69  ? 54.038  23.270  30.725  1.00 33.30 ?  61  GLY A CA    1 
ATOM   478  C C     . GLY A 1 69  ? 53.337  23.495  32.043  1.00 36.74 ?  61  GLY A C     1 
ATOM   479  O O     . GLY A 1 69  ? 53.955  23.309  33.095  1.00 32.33 ?  61  GLY A O     1 
ATOM   480  N N     . LYS A 1 70  ? 52.065  23.893  32.023  1.00 33.26 ?  62  LYS A N     1 
ATOM   481  C CA    . LYS A 1 70  ? 51.337  24.114  33.266  1.00 27.92 ?  62  LYS A CA    1 
ATOM   482  C C     . LYS A 1 70  ? 50.895  22.806  33.910  1.00 29.87 ?  62  LYS A C     1 
ATOM   483  O O     . LYS A 1 70  ? 50.852  22.710  35.141  1.00 28.88 ?  62  LYS A O     1 
ATOM   484  C CB    . LYS A 1 70  ? 50.125  25.012  33.011  1.00 27.56 ?  62  LYS A CB    1 
ATOM   485  C CG    . LYS A 1 70  ? 50.482  26.420  32.564  1.00 25.18 ?  62  LYS A CG    1 
ATOM   486  C CD    . LYS A 1 70  ? 49.255  27.313  32.547  1.00 35.10 ?  62  LYS A CD    1 
ATOM   487  C CE    . LYS A 1 70  ? 49.636  28.780  32.613  1.00 32.18 ?  62  LYS A CE    1 
ATOM   488  N NZ    . LYS A 1 70  ? 50.015  29.316  31.277  1.00 33.31 ?  62  LYS A NZ    1 
ATOM   489  N N     . ILE A 1 71  ? 50.558  21.796  33.104  1.00 30.78 ?  63  ILE A N     1 
ATOM   490  C CA    . ILE A 1 71  ? 50.123  20.500  33.608  1.00 31.45 ?  63  ILE A CA    1 
ATOM   491  C C     . ILE A 1 71  ? 50.792  19.398  32.800  1.00 32.26 ?  63  ILE A C     1 
ATOM   492  O O     . ILE A 1 71  ? 51.275  19.613  31.686  1.00 30.78 ?  63  ILE A O     1 
ATOM   493  C CB    . ILE A 1 71  ? 48.585  20.323  33.557  1.00 31.82 ?  63  ILE A CB    1 
ATOM   494  C CG1   . ILE A 1 71  ? 48.096  20.286  32.107  1.00 27.19 ?  63  ILE A CG1   1 
ATOM   495  C CG2   . ILE A 1 71  ? 47.884  21.417  34.337  1.00 27.77 ?  63  ILE A CG2   1 
ATOM   496  C CD1   . ILE A 1 71  ? 46.605  20.049  31.970  1.00 33.74 ?  63  ILE A CD1   1 
ATOM   497  N N     . LYS A 1 72  ? 50.810  18.203  33.383  1.00 33.72 ?  64  LYS A N     1 
ATOM   498  C CA    . LYS A 1 72  ? 51.289  17.001  32.717  1.00 38.09 ?  64  LYS A CA    1 
ATOM   499  C C     . LYS A 1 72  ? 50.453  15.835  33.216  1.00 31.91 ?  64  LYS A C     1 
ATOM   500  O O     . LYS A 1 72  ? 49.896  15.911  34.318  1.00 32.05 ?  64  LYS A O     1 
ATOM   501  C CB    . LYS A 1 72  ? 52.782  16.755  32.985  1.00 28.32 ?  64  LYS A CB    1 
ATOM   502  C CG    . LYS A 1 72  ? 53.139  16.570  34.451  1.00 33.63 ?  64  LYS A CG    1 
ATOM   503  C CD    . LYS A 1 72  ? 54.587  16.122  34.620  1.00 52.53 ?  64  LYS A CD    1 
ATOM   504  C CE    . LYS A 1 72  ? 55.503  16.791  33.605  1.00 51.22 ?  64  LYS A CE    1 
ATOM   505  N NZ    . LYS A 1 72  ? 56.823  17.165  34.186  1.00 63.45 ?  64  LYS A NZ    1 
ATOM   506  N N     . PRO A 1 73  ? 50.316  14.765  32.427  1.00 32.13 ?  65  PRO A N     1 
ATOM   507  C CA    . PRO A 1 73  ? 49.481  13.634  32.851  1.00 29.61 ?  65  PRO A CA    1 
ATOM   508  C C     . PRO A 1 73  ? 49.836  13.160  34.254  1.00 33.07 ?  65  PRO A C     1 
ATOM   509  O O     . PRO A 1 73  ? 51.009  13.056  34.621  1.00 33.03 ?  65  PRO A O     1 
ATOM   510  C CB    . PRO A 1 73  ? 49.787  12.566  31.799  1.00 31.68 ?  65  PRO A CB    1 
ATOM   511  C CG    . PRO A 1 73  ? 50.045  13.355  30.572  1.00 29.20 ?  65  PRO A CG    1 
ATOM   512  C CD    . PRO A 1 73  ? 50.772  14.606  31.034  1.00 37.54 ?  65  PRO A CD    1 
ATOM   513  N N     . GLY A 1 74  ? 48.801  12.882  35.044  1.00 31.43 ?  66  GLY A N     1 
ATOM   514  C CA    . GLY A 1 74  ? 48.940  12.598  36.451  1.00 26.55 ?  66  GLY A CA    1 
ATOM   515  C C     . GLY A 1 74  ? 48.573  13.759  37.351  1.00 29.86 ?  66  GLY A C     1 
ATOM   516  O O     . GLY A 1 74  ? 48.341  13.553  38.548  1.00 33.55 ?  66  GLY A O     1 
ATOM   517  N N     . ASP A 1 75  ? 48.516  14.968  36.801  1.00 31.39 ?  67  ASP A N     1 
ATOM   518  C CA    . ASP A 1 75  ? 48.114  16.146  37.548  1.00 33.00 ?  67  ASP A CA    1 
ATOM   519  C C     . ASP A 1 75  ? 46.607  16.143  37.781  1.00 33.06 ?  67  ASP A C     1 
ATOM   520  O O     . ASP A 1 75  ? 45.855  15.368  37.183  1.00 31.15 ?  67  ASP A O     1 
ATOM   521  C CB    . ASP A 1 75  ? 48.530  17.416  36.809  1.00 26.36 ?  67  ASP A CB    1 
ATOM   522  C CG    . ASP A 1 75  ? 50.012  17.679  36.909  1.00 36.02 ?  67  ASP A CG    1 
ATOM   523  O OD1   . ASP A 1 75  ? 50.643  17.114  37.826  1.00 32.26 ?  67  ASP A OD1   1 
ATOM   524  O OD2   . ASP A 1 75  ? 50.546  18.444  36.081  1.00 33.87 ?  67  ASP A OD2   1 
ATOM   525  N N     . THR A 1 76  ? 46.169  17.034  38.665  1.00 34.59 ?  68  THR A N     1 
ATOM   526  C CA    . THR A 1 76  ? 44.769  17.149  39.046  1.00 32.51 ?  68  THR A CA    1 
ATOM   527  C C     . THR A 1 76  ? 44.223  18.498  38.606  1.00 32.97 ?  68  THR A C     1 
ATOM   528  O O     . THR A 1 76  ? 44.826  19.540  38.887  1.00 29.20 ?  68  THR A O     1 
ATOM   529  C CB    . THR A 1 76  ? 44.591  16.992  40.555  1.00 32.17 ?  68  THR A CB    1 
ATOM   530  O OG1   . THR A 1 76  ? 45.202  15.770  40.987  1.00 35.01 ?  68  THR A OG1   1 
ATOM   531  C CG2   . THR A 1 76  ? 43.108  16.970  40.909  1.00 30.45 ?  68  THR A CG2   1 
ATOM   532  N N     . ILE A 1 77  ? 43.078  18.471  37.926  1.00 32.31 ?  69  ILE A N     1 
ATOM   533  C CA    . ILE A 1 77  ? 42.370  19.678  37.523  1.00 31.11 ?  69  ILE A CA    1 
ATOM   534  C C     . ILE A 1 77  ? 41.157  19.844  38.424  1.00 31.42 ?  69  ILE A C     1 
ATOM   535  O O     . ILE A 1 77  ? 40.594  18.868  38.934  1.00 31.21 ?  69  ILE A O     1 
ATOM   536  C CB    . ILE A 1 77  ? 41.996  19.650  36.016  1.00 38.07 ?  69  ILE A CB    1 
ATOM   537  C CG1   . ILE A 1 77  ? 40.852  18.674  35.671  1.00 39.34 ?  69  ILE A CG1   1 
ATOM   538  C CG2   . ILE A 1 77  ? 43.224  19.363  35.173  1.00 36.10 ?  69  ILE A CG2   1 
ATOM   539  C CD1   . ILE A 1 77  ? 39.444  19.225  35.844  1.00 36.10 ?  69  ILE A CD1   1 
ATOM   540  N N     . VAL A 1 78  ? 40.767  21.094  38.649  1.00 27.33 ?  70  VAL A N     1 
ATOM   541  C CA    . VAL A 1 78  ? 39.577  21.407  39.427  1.00 30.06 ?  70  VAL A CA    1 
ATOM   542  C C     . VAL A 1 78  ? 38.779  22.465  38.678  1.00 31.63 ?  70  VAL A C     1 
ATOM   543  O O     . VAL A 1 78  ? 39.352  23.364  38.052  1.00 28.80 ?  70  VAL A O     1 
ATOM   544  C CB    . VAL A 1 78  ? 39.925  21.875  40.857  1.00 31.32 ?  70  VAL A CB    1 
ATOM   545  C CG1   . VAL A 1 78  ? 40.662  23.207  40.837  1.00 29.95 ?  70  VAL A CG1   1 
ATOM   546  C CG2   . VAL A 1 78  ? 38.667  21.951  41.717  1.00 29.96 ?  70  VAL A CG2   1 
ATOM   547  N N     . GLU A 1 79  ? 37.451  22.342  38.721  1.00 29.28 ?  71  GLU A N     1 
ATOM   548  C CA    . GLU A 1 79  ? 36.595  23.286  38.028  1.00 32.26 ?  71  GLU A CA    1 
ATOM   549  C C     . GLU A 1 79  ? 35.242  23.380  38.718  1.00 29.25 ?  71  GLU A C     1 
ATOM   550  O O     . GLU A 1 79  ? 34.643  22.337  39.027  1.00 29.21 ?  71  GLU A O     1 
ATOM   551  C CB    . GLU A 1 79  ? 36.397  22.901  36.559  1.00 27.61 ?  71  GLU A CB    1 
ATOM   552  C CG    . GLU A 1 79  ? 35.611  23.924  35.744  1.00 28.45 ?  71  GLU A CG    1 
ATOM   553  C CD    . GLU A 1 79  ? 36.407  25.185  35.444  1.00 31.09 ?  71  GLU A CD    1 
ATOM   554  O OE1   . GLU A 1 79  ? 37.609  25.229  35.777  1.00 27.81 ?  71  GLU A OE1   1 
ATOM   555  O OE2   . GLU A 1 79  ? 35.828  26.134  34.875  1.00 31.02 ?  71  GLU A OE2   1 
ATOM   556  N N     . PRO A 1 80  ? 34.749  24.588  38.976  1.00 27.06 ?  72  PRO A N     1 
ATOM   557  C CA    . PRO A 1 80  ? 33.385  24.757  39.493  1.00 28.03 ?  72  PRO A CA    1 
ATOM   558  C C     . PRO A 1 80  ? 32.379  24.711  38.354  1.00 31.48 ?  72  PRO A C     1 
ATOM   559  O O     . PRO A 1 80  ? 32.290  25.637  37.542  1.00 28.18 ?  72  PRO A O     1 
ATOM   560  C CB    . PRO A 1 80  ? 33.439  26.139  40.160  1.00 31.23 ?  72  PRO A CB    1 
ATOM   561  C CG    . PRO A 1 80  ? 34.478  26.888  39.374  1.00 29.93 ?  72  PRO A CG    1 
ATOM   562  C CD    . PRO A 1 80  ? 35.456  25.873  38.827  1.00 27.40 ?  72  PRO A CD    1 
ATOM   563  N N     . THR A 1 81  ? 31.620  23.622  38.287  1.00 26.74 ?  73  THR A N     1 
ATOM   564  C CA    . THR A 1 81  ? 30.745  23.395  37.149  1.00 28.22 ?  73  THR A CA    1 
ATOM   565  C C     . THR A 1 81  ? 29.542  22.570  37.570  1.00 31.66 ?  73  THR A C     1 
ATOM   566  O O     . THR A 1 81  ? 29.666  21.624  38.353  1.00 29.51 ?  73  THR A O     1 
ATOM   567  C CB    . THR A 1 81  ? 31.483  22.686  36.010  1.00 28.84 ?  73  THR A CB    1 
ATOM   568  O OG1   . THR A 1 81  ? 30.532  22.193  35.057  1.00 30.77 ?  73  THR A OG1   1 
ATOM   569  C CG2   . THR A 1 81  ? 32.318  21.533  36.554  1.00 23.28 ?  73  THR A CG2   1 
ATOM   570  N N     . SER A 1 82  ? 28.380  22.936  37.033  1.00 31.05 ?  74  SER A N     1 
ATOM   571  C CA    . SER A 1 82  ? 27.141  22.201  37.247  1.00 34.34 ?  74  SER A CA    1 
ATOM   572  C C     . SER A 1 82  ? 26.508  21.779  35.927  1.00 39.80 ?  74  SER A C     1 
ATOM   573  O O     . SER A 1 82  ? 25.300  21.529  35.873  1.00 43.13 ?  74  SER A O     1 
ATOM   574  C CB    . SER A 1 82  ? 26.160  23.041  38.063  1.00 40.01 ?  74  SER A CB    1 
ATOM   575  O OG    . SER A 1 82  ? 26.059  24.353  37.533  1.00 37.85 ?  74  SER A OG    1 
ATOM   576  N N     . GLY A 1 83  ? 27.297  21.701  34.858  1.00 32.14 ?  75  GLY A N     1 
ATOM   577  C CA    . GLY A 1 83  ? 26.754  21.390  33.552  1.00 31.65 ?  75  GLY A CA    1 
ATOM   578  C C     . GLY A 1 83  ? 27.636  20.501  32.700  1.00 29.85 ?  75  GLY A C     1 
ATOM   579  O O     . GLY A 1 83  ? 28.337  19.624  33.214  1.00 29.47 ?  75  GLY A O     1 
ATOM   580  N N     . ASN A 1 84  ? 27.614  20.729  31.386  1.00 28.61 ?  76  ASN A N     1 
ATOM   581  C CA    . ASN A 1 84  ? 28.300  19.836  30.461  1.00 26.06 ?  76  ASN A CA    1 
ATOM   582  C C     . ASN A 1 84  ? 29.812  20.013  30.482  1.00 27.53 ?  76  ASN A C     1 
ATOM   583  O O     . ASN A 1 84  ? 30.530  19.124  30.012  1.00 28.38 ?  76  ASN A O     1 
ATOM   584  C CB    . ASN A 1 84  ? 27.769  20.048  29.046  1.00 26.29 ?  76  ASN A CB    1 
ATOM   585  C CG    . ASN A 1 84  ? 26.367  19.517  28.873  1.00 26.08 ?  76  ASN A CG    1 
ATOM   586  O OD1   . ASN A 1 84  ? 26.076  18.377  29.230  1.00 25.15 ?  76  ASN A OD1   1 
ATOM   587  N ND2   . ASN A 1 84  ? 25.483  20.347  28.338  1.00 25.12 ?  76  ASN A ND2   1 
ATOM   588  N N     . THR A 1 85  ? 30.312  21.135  31.004  1.00 26.20 ?  77  THR A N     1 
ATOM   589  C CA    . THR A 1 85  ? 31.757  21.307  31.108  1.00 26.55 ?  77  THR A CA    1 
ATOM   590  C C     . THR A 1 85  ? 32.360  20.276  32.055  1.00 27.37 ?  77  THR A C     1 
ATOM   591  O O     . THR A 1 85  ? 33.421  19.707  31.773  1.00 25.86 ?  77  THR A O     1 
ATOM   592  C CB    . THR A 1 85  ? 32.090  22.729  31.563  1.00 27.04 ?  77  THR A CB    1 
ATOM   593  O OG1   . THR A 1 85  ? 31.874  23.640  30.478  1.00 24.16 ?  77  THR A OG1   1 
ATOM   594  C CG2   . THR A 1 85  ? 33.544  22.828  32.007  1.00 23.74 ?  77  THR A CG2   1 
ATOM   595  N N     . GLY A 1 86  ? 31.687  20.010  33.177  1.00 27.75 ?  78  GLY A N     1 
ATOM   596  C CA    . GLY A 1 86  ? 32.153  18.966  34.074  1.00 28.81 ?  78  GLY A CA    1 
ATOM   597  C C     . GLY A 1 86  ? 32.157  17.598  33.419  1.00 28.87 ?  78  GLY A C     1 
ATOM   598  O O     . GLY A 1 86  ? 33.093  16.816  33.598  1.00 26.89 ?  78  GLY A O     1 
ATOM   599  N N     . ILE A 1 87  ? 31.110  17.294  32.650  1.00 28.93 ?  79  ILE A N     1 
ATOM   600  C CA    . ILE A 1 87  ? 31.073  16.039  31.904  1.00 29.59 ?  79  ILE A CA    1 
ATOM   601  C C     . ILE A 1 87  ? 32.204  15.996  30.885  1.00 28.25 ?  79  ILE A C     1 
ATOM   602  O O     . ILE A 1 87  ? 32.932  15.002  30.777  1.00 27.57 ?  79  ILE A O     1 
ATOM   603  C CB    . ILE A 1 87  ? 29.704  15.856  31.228  1.00 26.27 ?  79  ILE A CB    1 
ATOM   604  C CG1   . ILE A 1 87  ? 28.589  15.850  32.273  1.00 26.49 ?  79  ILE A CG1   1 
ATOM   605  C CG2   . ILE A 1 87  ? 29.688  14.580  30.403  1.00 19.62 ?  79  ILE A CG2   1 
ATOM   606  C CD1   . ILE A 1 87  ? 27.204  15.890  31.675  1.00 28.32 ?  79  ILE A CD1   1 
ATOM   607  N N     . GLY A 1 88  ? 32.366  17.077  30.119  1.00 25.29 ?  80  GLY A N     1 
ATOM   608  C CA    . GLY A 1 88  ? 33.430  17.113  29.129  1.00 24.54 ?  80  GLY A CA    1 
ATOM   609  C C     . GLY A 1 88  ? 34.810  17.006  29.748  1.00 29.35 ?  80  GLY A C     1 
ATOM   610  O O     . GLY A 1 88  ? 35.683  16.310  29.224  1.00 27.95 ?  80  GLY A O     1 
ATOM   611  N N     . LEU A 1 89  ? 35.027  17.691  30.873  1.00 24.01 ?  81  LEU A N     1 
ATOM   612  C CA    . LEU A 1 89  ? 36.334  17.629  31.518  1.00 26.21 ?  81  LEU A CA    1 
ATOM   613  C C     . LEU A 1 89  ? 36.581  16.260  32.139  1.00 28.73 ?  81  LEU A C     1 
ATOM   614  O O     . LEU A 1 89  ? 37.674  15.702  31.996  1.00 25.72 ?  81  LEU A O     1 
ATOM   615  C CB    . LEU A 1 89  ? 36.463  18.736  32.565  1.00 26.55 ?  81  LEU A CB    1 
ATOM   616  C CG    . LEU A 1 89  ? 36.767  20.131  32.015  1.00 28.58 ?  81  LEU A CG    1 
ATOM   617  C CD1   . LEU A 1 89  ? 36.734  21.161  33.131  1.00 24.17 ?  81  LEU A CD1   1 
ATOM   618  C CD2   . LEU A 1 89  ? 38.111  20.154  31.297  1.00 27.65 ?  81  LEU A CD2   1 
ATOM   619  N N     . ALA A 1 90  ? 35.581  15.699  32.828  1.00 26.91 ?  82  ALA A N     1 
ATOM   620  C CA    . ALA A 1 90  ? 35.729  14.348  33.365  1.00 31.44 ?  82  ALA A CA    1 
ATOM   621  C C     . ALA A 1 90  ? 36.003  13.346  32.253  1.00 30.68 ?  82  ALA A C     1 
ATOM   622  O O     . ALA A 1 90  ? 36.818  12.429  32.416  1.00 27.69 ?  82  ALA A O     1 
ATOM   623  C CB    . ALA A 1 90  ? 34.477  13.947  34.147  1.00 30.41 ?  82  ALA A CB    1 
ATOM   624  N N     . PHE A 1 91  ? 35.330  13.511  31.114  1.00 29.54 ?  83  PHE A N     1 
ATOM   625  C CA    . PHE A 1 91  ? 35.574  12.661  29.955  1.00 26.46 ?  83  PHE A CA    1 
ATOM   626  C C     . PHE A 1 91  ? 37.009  12.813  29.460  1.00 27.92 ?  83  PHE A C     1 
ATOM   627  O O     . PHE A 1 91  ? 37.744  11.827  29.327  1.00 27.80 ?  83  PHE A O     1 
ATOM   628  C CB    . PHE A 1 91  ? 34.566  13.010  28.856  1.00 27.35 ?  83  PHE A CB    1 
ATOM   629  C CG    . PHE A 1 91  ? 34.952  12.527  27.487  1.00 25.24 ?  83  PHE A CG    1 
ATOM   630  C CD1   . PHE A 1 91  ? 35.346  11.216  27.267  1.00 24.38 ?  83  PHE A CD1   1 
ATOM   631  C CD2   . PHE A 1 91  ? 34.910  13.397  26.410  1.00 26.63 ?  83  PHE A CD2   1 
ATOM   632  C CE1   . PHE A 1 91  ? 35.694  10.789  25.999  1.00 26.11 ?  83  PHE A CE1   1 
ATOM   633  C CE2   . PHE A 1 91  ? 35.255  12.976  25.144  1.00 21.07 ?  83  PHE A CE2   1 
ATOM   634  C CZ    . PHE A 1 91  ? 35.648  11.670  24.937  1.00 25.32 ?  83  PHE A CZ    1 
ATOM   635  N N     . VAL A 1 92  ? 37.429  14.051  29.191  1.00 25.71 ?  84  VAL A N     1 
ATOM   636  C CA    . VAL A 1 92  ? 38.750  14.279  28.608  1.00 29.15 ?  84  VAL A CA    1 
ATOM   637  C C     . VAL A 1 92  ? 39.850  13.887  29.590  1.00 27.95 ?  84  VAL A C     1 
ATOM   638  O O     . VAL A 1 92  ? 40.864  13.294  29.201  1.00 29.00 ?  84  VAL A O     1 
ATOM   639  C CB    . VAL A 1 92  ? 38.879  15.745  28.150  1.00 26.65 ?  84  VAL A CB    1 
ATOM   640  C CG1   . VAL A 1 92  ? 40.341  16.130  27.969  1.00 30.60 ?  84  VAL A CG1   1 
ATOM   641  C CG2   . VAL A 1 92  ? 38.107  15.957  26.854  1.00 21.38 ?  84  VAL A CG2   1 
ATOM   642  N N     . CYS A 1 93  ? 39.662  14.193  30.878  1.00 26.66 ?  85  CYS A N     1 
ATOM   643  C CA    . CYS A 1 93  ? 40.678  13.858  31.875  1.00 31.36 ?  85  CYS A CA    1 
ATOM   644  C C     . CYS A 1 93  ? 40.871  12.351  31.995  1.00 32.59 ?  85  CYS A C     1 
ATOM   645  O O     . CYS A 1 93  ? 41.992  11.879  32.221  1.00 32.74 ?  85  CYS A O     1 
ATOM   646  C CB    . CYS A 1 93  ? 40.304  14.454  33.231  1.00 29.32 ?  85  CYS A CB    1 
ATOM   647  S SG    . CYS A 1 93  ? 40.522  16.236  33.333  1.00 32.92 ?  85  CYS A SG    1 
ATOM   648  N N     . ALA A 1 94  ? 39.789  11.579  31.862  1.00 28.92 ?  86  ALA A N     1 
ATOM   649  C CA    . ALA A 1 94  ? 39.918  10.126  31.881  1.00 29.51 ?  86  ALA A CA    1 
ATOM   650  C C     . ALA A 1 94  ? 40.670  9.627   30.655  1.00 33.31 ?  86  ALA A C     1 
ATOM   651  O O     . ALA A 1 94  ? 41.468  8.686   30.744  1.00 31.50 ?  86  ALA A O     1 
ATOM   652  C CB    . ALA A 1 94  ? 38.537  9.475   31.962  1.00 31.04 ?  86  ALA A CB    1 
ATOM   653  N N     . ALA A 1 95  ? 40.436  10.257  29.504  1.00 25.72 ?  87  ALA A N     1 
ATOM   654  C CA    . ALA A 1 95  ? 41.038  9.806   28.258  1.00 32.56 ?  87  ALA A CA    1 
ATOM   655  C C     . ALA A 1 95  ? 42.511  10.167  28.150  1.00 32.48 ?  87  ALA A C     1 
ATOM   656  O O     . ALA A 1 95  ? 43.241  9.514   27.397  1.00 31.13 ?  87  ALA A O     1 
ATOM   657  C CB    . ALA A 1 95  ? 40.278  10.401  27.078  1.00 29.90 ?  87  ALA A CB    1 
ATOM   658  N N     . LYS A 1 96  ? 42.964  11.185  28.875  1.00 33.27 ?  88  LYS A N     1 
ATOM   659  C CA    . LYS A 1 96  ? 44.319  11.686  28.723  1.00 32.60 ?  88  LYS A CA    1 
ATOM   660  C C     . LYS A 1 96  ? 45.171  11.513  29.973  1.00 36.08 ?  88  LYS A C     1 
ATOM   661  O O     . LYS A 1 96  ? 46.330  11.946  29.979  1.00 35.46 ?  88  LYS A O     1 
ATOM   662  C CB    . LYS A 1 96  ? 44.285  13.163  28.307  1.00 29.29 ?  88  LYS A CB    1 
ATOM   663  C CG    . LYS A 1 96  ? 43.957  13.369  26.830  1.00 33.63 ?  88  LYS A CG    1 
ATOM   664  C CD    . LYS A 1 96  ? 43.887  14.844  26.473  1.00 34.82 ?  88  LYS A CD    1 
ATOM   665  C CE    . LYS A 1 96  ? 45.251  15.502  26.579  1.00 33.50 ?  88  LYS A CE    1 
ATOM   666  N NZ    . LYS A 1 96  ? 46.071  15.262  25.362  1.00 32.25 ?  88  LYS A NZ    1 
ATOM   667  N N     . GLY A 1 97  ? 44.640  10.896  31.026  1.00 32.69 ?  89  GLY A N     1 
ATOM   668  C CA    . GLY A 1 97  ? 45.442  10.550  32.183  1.00 32.09 ?  89  GLY A CA    1 
ATOM   669  C C     . GLY A 1 97  ? 45.550  11.634  33.234  1.00 34.20 ?  89  GLY A C     1 
ATOM   670  O O     . GLY A 1 97  ? 46.633  11.872  33.778  1.00 35.98 ?  89  GLY A O     1 
ATOM   671  N N     . TYR A 1 98  ? 44.437  12.293  33.538  1.00 32.09 ?  90  TYR A N     1 
ATOM   672  C CA    . TYR A 1 98  ? 44.400  13.330  34.555  1.00 29.38 ?  90  TYR A CA    1 
ATOM   673  C C     . TYR A 1 98  ? 43.365  12.986  35.614  1.00 32.47 ?  90  TYR A C     1 
ATOM   674  O O     . TYR A 1 98  ? 42.377  12.298  35.343  1.00 33.13 ?  90  TYR A O     1 
ATOM   675  C CB    . TYR A 1 98  ? 44.075  14.699  33.950  1.00 26.57 ?  90  TYR A CB    1 
ATOM   676  C CG    . TYR A 1 98  ? 45.193  15.282  33.123  1.00 31.49 ?  90  TYR A CG    1 
ATOM   677  C CD1   . TYR A 1 98  ? 45.303  14.996  31.769  1.00 29.72 ?  90  TYR A CD1   1 
ATOM   678  C CD2   . TYR A 1 98  ? 46.144  16.113  33.698  1.00 32.00 ?  90  TYR A CD2   1 
ATOM   679  C CE1   . TYR A 1 98  ? 46.327  15.526  31.010  1.00 32.76 ?  90  TYR A CE1   1 
ATOM   680  C CE2   . TYR A 1 98  ? 47.170  16.648  32.948  1.00 32.98 ?  90  TYR A CE2   1 
ATOM   681  C CZ    . TYR A 1 98  ? 47.257  16.351  31.605  1.00 30.82 ?  90  TYR A CZ    1 
ATOM   682  O OH    . TYR A 1 98  ? 48.279  16.881  30.857  1.00 30.40 ?  90  TYR A OH    1 
ATOM   683  N N     . LYS A 1 99  ? 43.608  13.470  36.829  1.00 31.87 ?  91  LYS A N     1 
ATOM   684  C CA    . LYS A 1 99  ? 42.618  13.419  37.891  1.00 29.34 ?  91  LYS A CA    1 
ATOM   685  C C     . LYS A 1 99  ? 41.732  14.653  37.810  1.00 28.55 ?  91  LYS A C     1 
ATOM   686  O O     . LYS A 1 99  ? 42.207  15.755  37.518  1.00 32.61 ?  91  LYS A O     1 
ATOM   687  C CB    . LYS A 1 99  ? 43.288  13.337  39.263  1.00 33.94 ?  91  LYS A CB    1 
ATOM   688  C CG    . LYS A 1 99  ? 44.388  12.295  39.351  1.00 39.49 ?  91  LYS A CG    1 
ATOM   689  C CD    . LYS A 1 99  ? 44.580  11.806  40.776  1.00 40.92 ?  91  LYS A CD    1 
ATOM   690  C CE    . LYS A 1 99  ? 45.897  11.060  40.919  1.00 51.22 ?  91  LYS A CE    1 
ATOM   691  N NZ    . LYS A 1 99  ? 46.042  10.406  42.250  1.00 48.22 ?  91  LYS A NZ    1 
ATOM   692  N N     . ALA A 1 100 ? 40.442  14.463  38.063  1.00 32.63 ?  92  ALA A N     1 
ATOM   693  C CA    . ALA A 1 100 ? 39.453  15.522  37.928  1.00 35.30 ?  92  ALA A CA    1 
ATOM   694  C C     . ALA A 1 100 ? 38.713  15.711  39.242  1.00 28.85 ?  92  ALA A C     1 
ATOM   695  O O     . ALA A 1 100 ? 38.214  14.742  39.825  1.00 31.06 ?  92  ALA A O     1 
ATOM   696  C CB    . ALA A 1 100 ? 38.457  15.206  36.806  1.00 28.05 ?  92  ALA A CB    1 
ATOM   697  N N     . VAL A 1 101 ? 38.646  16.958  39.701  1.00 27.57 ?  93  VAL A N     1 
ATOM   698  C CA    . VAL A 1 101 ? 37.857  17.346  40.863  1.00 31.91 ?  93  VAL A CA    1 
ATOM   699  C C     . VAL A 1 101 ? 36.880  18.424  40.417  1.00 32.66 ?  93  VAL A C     1 
ATOM   700  O O     . VAL A 1 101 ? 37.277  19.395  39.764  1.00 29.18 ?  93  VAL A O     1 
ATOM   701  C CB    . VAL A 1 101 ? 38.742  17.854  42.016  1.00 40.01 ?  93  VAL A CB    1 
ATOM   702  C CG1   . VAL A 1 101 ? 37.888  18.240  43.216  1.00 37.16 ?  93  VAL A CG1   1 
ATOM   703  C CG2   . VAL A 1 101 ? 39.766  16.800  42.403  1.00 29.48 ?  93  VAL A CG2   1 
ATOM   704  N N     . PHE A 1 102 ? 35.608  18.249  40.756  1.00 29.62 ?  94  PHE A N     1 
ATOM   705  C CA    . PHE A 1 102 ? 34.571  19.201  40.391  1.00 31.46 ?  94  PHE A CA    1 
ATOM   706  C C     . PHE A 1 102 ? 33.821  19.644  41.636  1.00 32.61 ?  94  PHE A C     1 
ATOM   707  O O     . PHE A 1 102 ? 33.528  18.831  42.519  1.00 30.38 ?  94  PHE A O     1 
ATOM   708  C CB    . PHE A 1 102 ? 33.602  18.599  39.371  1.00 29.62 ?  94  PHE A CB    1 
ATOM   709  C CG    . PHE A 1 102 ? 34.265  18.177  38.095  1.00 30.61 ?  94  PHE A CG    1 
ATOM   710  C CD1   . PHE A 1 102 ? 34.943  19.100  37.318  1.00 26.74 ?  94  PHE A CD1   1 
ATOM   711  C CD2   . PHE A 1 102 ? 34.224  16.857  37.680  1.00 28.99 ?  94  PHE A CD2   1 
ATOM   712  C CE1   . PHE A 1 102 ? 35.562  18.718  36.145  1.00 30.53 ?  94  PHE A CE1   1 
ATOM   713  C CE2   . PHE A 1 102 ? 34.842  16.469  36.509  1.00 28.85 ?  94  PHE A CE2   1 
ATOM   714  C CZ    . PHE A 1 102 ? 35.512  17.399  35.739  1.00 27.55 ?  94  PHE A CZ    1 
ATOM   715  N N     . THR A 1 103 ? 33.535  20.939  41.711  1.00 28.17 ?  95  THR A N     1 
ATOM   716  C CA    . THR A 1 103 ? 32.737  21.509  42.783  1.00 31.70 ?  95  THR A CA    1 
ATOM   717  C C     . THR A 1 103 ? 31.394  21.953  42.222  1.00 29.70 ?  95  THR A C     1 
ATOM   718  O O     . THR A 1 103 ? 31.325  22.510  41.122  1.00 28.64 ?  95  THR A O     1 
ATOM   719  C CB    . THR A 1 103 ? 33.447  22.694  43.444  1.00 30.82 ?  95  THR A CB    1 
ATOM   720  O OG1   . THR A 1 103 ? 33.781  23.670  42.452  1.00 27.23 ?  95  THR A OG1   1 
ATOM   721  C CG2   . THR A 1 103 ? 34.719  22.231  44.141  1.00 26.26 ?  95  THR A CG2   1 
ATOM   722  N N     . MET A 1 104 ? 30.333  21.697  42.978  1.00 29.69 ?  96  MET A N     1 
ATOM   723  C CA    . MET A 1 104 ? 28.981  22.018  42.547  1.00 33.87 ?  96  MET A CA    1 
ATOM   724  C C     . MET A 1 104 ? 28.075  22.001  43.768  1.00 33.31 ?  96  MET A C     1 
ATOM   725  O O     . MET A 1 104 ? 28.398  21.356  44.773  1.00 29.79 ?  96  MET A O     1 
ATOM   726  C CB    . MET A 1 104 ? 28.481  21.020  41.492  1.00 34.27 ?  96  MET A CB    1 
ATOM   727  C CG    . MET A 1 104 ? 28.100  19.667  42.064  1.00 36.11 ?  96  MET A CG    1 
ATOM   728  S SD    . MET A 1 104 ? 28.870  18.290  41.199  1.00 41.69 ?  96  MET A SD    1 
ATOM   729  C CE    . MET A 1 104 ? 30.557  18.428  41.767  1.00 36.62 ?  96  MET A CE    1 
ATOM   730  N N     . PRO A 1 105 ? 26.945  22.707  43.721  1.00 35.68 ?  97  PRO A N     1 
ATOM   731  C CA    . PRO A 1 105 ? 26.011  22.659  44.851  1.00 37.93 ?  97  PRO A CA    1 
ATOM   732  C C     . PRO A 1 105 ? 25.512  21.243  45.089  1.00 39.01 ?  97  PRO A C     1 
ATOM   733  O O     . PRO A 1 105 ? 25.399  20.435  44.165  1.00 35.69 ?  97  PRO A O     1 
ATOM   734  C CB    . PRO A 1 105 ? 24.871  23.589  44.420  1.00 34.68 ?  97  PRO A CB    1 
ATOM   735  C CG    . PRO A 1 105 ? 25.432  24.439  43.343  1.00 35.78 ?  97  PRO A CG    1 
ATOM   736  C CD    . PRO A 1 105 ? 26.535  23.673  42.688  1.00 38.65 ?  97  PRO A CD    1 
ATOM   737  N N     . GLU A 1 106 ? 25.213  20.950  46.357  1.00 40.19 ?  98  GLU A N     1 
ATOM   738  C CA    . GLU A 1 106 ? 24.683  19.645  46.732  1.00 41.36 ?  98  GLU A CA    1 
ATOM   739  C C     . GLU A 1 106 ? 23.319  19.366  46.112  1.00 43.23 ?  98  GLU A C     1 
ATOM   740  O O     . GLU A 1 106 ? 22.806  18.251  46.259  1.00 42.62 ?  98  GLU A O     1 
ATOM   741  C CB    . GLU A 1 106 ? 24.598  19.547  48.257  1.00 40.72 ?  98  GLU A CB    1 
ATOM   742  C CG    . GLU A 1 106 ? 23.617  20.531  48.879  1.00 36.81 ?  98  GLU A CG    1 
ATOM   743  C CD    . GLU A 1 106 ? 23.886  20.790  50.350  1.00 43.07 ?  98  GLU A CD    1 
ATOM   744  O OE1   . GLU A 1 106 ? 24.354  19.866  51.048  1.00 47.06 ?  98  GLU A OE1   1 
ATOM   745  O OE2   . GLU A 1 106 ? 23.626  21.924  50.807  1.00 40.06 ?  98  GLU A OE2   1 
ATOM   746  N N     . THR A 1 107 ? 22.728  20.342  45.421  1.00 39.57 ?  99  THR A N     1 
ATOM   747  C CA    . THR A 1 107 ? 21.416  20.190  44.808  1.00 41.53 ?  99  THR A CA    1 
ATOM   748  C C     . THR A 1 107 ? 21.446  19.372  43.523  1.00 43.04 ?  99  THR A C     1 
ATOM   749  O O     . THR A 1 107 ? 20.378  19.066  42.982  1.00 39.90 ?  99  THR A O     1 
ATOM   750  C CB    . THR A 1 107 ? 20.814  21.567  44.511  1.00 35.93 ?  99  THR A CB    1 
ATOM   751  O OG1   . THR A 1 107 ? 21.795  22.389  43.865  1.00 56.24 ?  99  THR A OG1   1 
ATOM   752  C CG2   . THR A 1 107 ? 20.377  22.240  45.801  1.00 47.03 ?  99  THR A CG2   1 
ATOM   753  N N     . MET A 1 108 ? 22.627  19.016  43.026  1.00 37.84 ?  100 MET A N     1 
ATOM   754  C CA    . MET A 1 108 ? 22.722  18.302  41.762  1.00 38.19 ?  100 MET A CA    1 
ATOM   755  C C     . MET A 1 108 ? 22.125  16.904  41.876  1.00 41.22 ?  100 MET A C     1 
ATOM   756  O O     . MET A 1 108 ? 22.126  16.286  42.944  1.00 45.15 ?  100 MET A O     1 
ATOM   757  C CB    . MET A 1 108 ? 24.177  18.217  41.307  1.00 43.31 ?  100 MET A CB    1 
ATOM   758  C CG    . MET A 1 108 ? 24.825  19.567  41.065  1.00 42.83 ?  100 MET A CG    1 
ATOM   759  S SD    . MET A 1 108 ? 24.022  20.483  39.743  1.00 47.02 ?  100 MET A SD    1 
ATOM   760  C CE    . MET A 1 108 ? 24.687  19.618  38.325  1.00 40.81 ?  100 MET A CE    1 
ATOM   761  N N     . SER A 1 109 ? 21.609  16.409  40.754  1.00 40.55 ?  101 SER A N     1 
ATOM   762  C CA    . SER A 1 109 ? 20.961  15.108  40.726  1.00 41.97 ?  101 SER A CA    1 
ATOM   763  C C     . SER A 1 109 ? 21.974  13.992  40.963  1.00 43.46 ?  101 SER A C     1 
ATOM   764  O O     . SER A 1 109 ? 23.179  14.147  40.748  1.00 45.18 ?  101 SER A O     1 
ATOM   765  C CB    . SER A 1 109 ? 20.253  14.888  39.388  1.00 45.93 ?  101 SER A CB    1 
ATOM   766  O OG    . SER A 1 109 ? 21.151  15.030  38.301  1.00 46.32 ?  101 SER A OG    1 
ATOM   767  N N     . GLN A 1 110 ? 21.463  12.846  41.420  1.00 40.26 ?  102 GLN A N     1 
ATOM   768  C CA    . GLN A 1 110 ? 22.322  11.681  41.599  1.00 47.12 ?  102 GLN A CA    1 
ATOM   769  C C     . GLN A 1 110 ? 22.731  11.082  40.260  1.00 46.75 ?  102 GLN A C     1 
ATOM   770  O O     . GLN A 1 110 ? 23.797  10.463  40.159  1.00 43.14 ?  102 GLN A O     1 
ATOM   771  C CB    . GLN A 1 110 ? 21.618  10.633  42.462  1.00 51.18 ?  102 GLN A CB    1 
ATOM   772  C CG    . GLN A 1 110 ? 22.507  9.471   42.879  1.00 47.40 ?  102 GLN A CG    1 
ATOM   773  C CD    . GLN A 1 110 ? 23.666  9.913   43.750  1.00 47.49 ?  102 GLN A CD    1 
ATOM   774  O OE1   . GLN A 1 110 ? 23.472  10.365  44.877  1.00 55.91 ?  102 GLN A OE1   1 
ATOM   775  N NE2   . GLN A 1 110 ? 24.881  9.787   43.227  1.00 46.45 ?  102 GLN A NE2   1 
ATOM   776  N N     . GLU A 1 111 ? 21.901  11.254  39.228  1.00 43.56 ?  103 GLU A N     1 
ATOM   777  C CA    . GLU A 1 111 ? 22.270  10.798  37.892  1.00 42.29 ?  103 GLU A CA    1 
ATOM   778  C C     . GLU A 1 111 ? 23.483  11.562  37.374  1.00 41.39 ?  103 GLU A C     1 
ATOM   779  O O     . GLU A 1 111 ? 24.438  10.965  36.864  1.00 42.99 ?  103 GLU A O     1 
ATOM   780  C CB    . GLU A 1 111 ? 21.084  10.952  36.940  1.00 45.77 ?  103 GLU A CB    1 
ATOM   781  N N     . ARG A 1 112 ? 23.461  12.892  37.502  1.00 36.43 ?  104 ARG A N     1 
ATOM   782  C CA    . ARG A 1 112 ? 24.610  13.700  37.105  1.00 40.04 ?  104 ARG A CA    1 
ATOM   783  C C     . ARG A 1 112 ? 25.848  13.329  37.911  1.00 37.00 ?  104 ARG A C     1 
ATOM   784  O O     . ARG A 1 112 ? 26.960  13.277  37.371  1.00 44.50 ?  104 ARG A O     1 
ATOM   785  C CB    . ARG A 1 112 ? 24.291  15.186  37.275  1.00 40.95 ?  104 ARG A CB    1 
ATOM   786  C CG    . ARG A 1 112 ? 25.291  16.116  36.609  1.00 50.45 ?  104 ARG A CG    1 
ATOM   787  C CD    . ARG A 1 112 ? 25.404  15.826  35.124  1.00 46.48 ?  104 ARG A CD    1 
ATOM   788  N NE    . ARG A 1 112 ? 24.476  16.641  34.350  1.00 48.24 ?  104 ARG A NE    1 
ATOM   789  C CZ    . ARG A 1 112 ? 23.509  16.150  33.588  1.00 53.80 ?  104 ARG A CZ    1 
ATOM   790  N NH1   . ARG A 1 112 ? 23.316  14.846  33.472  1.00 51.95 ?  104 ARG A NH1   1 
ATOM   791  N NH2   . ARG A 1 112 ? 22.712  16.987  32.930  1.00 53.74 ?  104 ARG A NH2   1 
ATOM   792  N N     . ARG A 1 113 ? 25.673  13.069  39.208  1.00 35.93 ?  105 ARG A N     1 
ATOM   793  C CA    . ARG A 1 113 ? 26.794  12.657  40.047  1.00 40.03 ?  105 ARG A CA    1 
ATOM   794  C C     . ARG A 1 113 ? 27.405  11.351  39.558  1.00 37.77 ?  105 ARG A C     1 
ATOM   795  O O     . ARG A 1 113 ? 28.633  11.225  39.471  1.00 37.42 ?  105 ARG A O     1 
ATOM   796  C CB    . ARG A 1 113 ? 26.325  12.511  41.491  1.00 41.87 ?  105 ARG A CB    1 
ATOM   797  C CG    . ARG A 1 113 ? 26.163  13.810  42.248  1.00 41.28 ?  105 ARG A CG    1 
ATOM   798  C CD    . ARG A 1 113 ? 25.549  13.499  43.601  1.00 43.82 ?  105 ARG A CD    1 
ATOM   799  N NE    . ARG A 1 113 ? 24.777  14.608  44.146  1.00 45.58 ?  105 ARG A NE    1 
ATOM   800  C CZ    . ARG A 1 113 ? 24.587  14.816  45.442  1.00 49.05 ?  105 ARG A CZ    1 
ATOM   801  N NH1   . ARG A 1 113 ? 25.027  13.960  46.353  1.00 51.20 ?  105 ARG A NH1   1 
ATOM   802  N NH2   . ARG A 1 113 ? 23.922  15.899  45.835  1.00 48.17 ?  105 ARG A NH2   1 
ATOM   803  N N     . ASN A 1 114 ? 26.562  10.366  39.240  1.00 39.69 ?  106 ASN A N     1 
ATOM   804  C CA    . ASN A 1 114 ? 27.063  9.071   38.792  1.00 38.51 ?  106 ASN A CA    1 
ATOM   805  C C     . ASN A 1 114 ? 27.770  9.185   37.448  1.00 37.47 ?  106 ASN A C     1 
ATOM   806  O O     . ASN A 1 114 ? 28.751  8.475   37.193  1.00 36.37 ?  106 ASN A O     1 
ATOM   807  C CB    . ASN A 1 114 ? 25.913  8.071   38.712  1.00 45.08 ?  106 ASN A CB    1 
ATOM   808  C CG    . ASN A 1 114 ? 25.395  7.670   40.078  1.00 46.91 ?  106 ASN A CG    1 
ATOM   809  O OD1   . ASN A 1 114 ? 26.122  7.715   41.070  1.00 50.59 ?  106 ASN A OD1   1 
ATOM   810  N ND2   . ASN A 1 114 ? 24.128  7.277   40.136  1.00 49.08 ?  106 ASN A ND2   1 
ATOM   811  N N     . LEU A 1 115 ? 27.283  10.069  36.574  1.00 33.82 ?  107 LEU A N     1 
ATOM   812  C CA    . LEU A 1 115 ? 27.942  10.285  35.290  1.00 33.15 ?  107 LEU A CA    1 
ATOM   813  C C     . LEU A 1 115 ? 29.368  10.784  35.486  1.00 34.00 ?  107 LEU A C     1 
ATOM   814  O O     . LEU A 1 115 ? 30.311  10.255  34.887  1.00 33.48 ?  107 LEU A O     1 
ATOM   815  C CB    . LEU A 1 115 ? 27.132  11.273  34.447  1.00 35.63 ?  107 LEU A CB    1 
ATOM   816  C CG    . LEU A 1 115 ? 27.672  11.623  33.057  1.00 33.02 ?  107 LEU A CG    1 
ATOM   817  C CD1   . LEU A 1 115 ? 28.148  10.382  32.325  1.00 30.86 ?  107 LEU A CD1   1 
ATOM   818  C CD2   . LEU A 1 115 ? 26.617  12.350  32.238  1.00 35.09 ?  107 LEU A CD2   1 
ATOM   819  N N     . LEU A 1 116 ? 29.545  11.803  36.330  1.00 34.95 ?  108 LEU A N     1 
ATOM   820  C CA    . LEU A 1 116 ? 30.884  12.321  36.590  1.00 33.26 ?  108 LEU A CA    1 
ATOM   821  C C     . LEU A 1 116 ? 31.746  11.284  37.298  1.00 32.96 ?  108 LEU A C     1 
ATOM   822  O O     . LEU A 1 116 ? 32.939  11.147  37.002  1.00 31.59 ?  108 LEU A O     1 
ATOM   823  C CB    . LEU A 1 116 ? 30.799  13.602  37.418  1.00 30.99 ?  108 LEU A CB    1 
ATOM   824  C CG    . LEU A 1 116 ? 29.934  14.719  36.835  1.00 33.25 ?  108 LEU A CG    1 
ATOM   825  C CD1   . LEU A 1 116 ? 29.687  15.790  37.879  1.00 30.44 ?  108 LEU A CD1   1 
ATOM   826  C CD2   . LEU A 1 116 ? 30.589  15.314  35.599  1.00 31.72 ?  108 LEU A CD2   1 
ATOM   827  N N     . LYS A 1 117 ? 31.155  10.536  38.234  1.00 32.19 ?  109 LYS A N     1 
ATOM   828  C CA    . LYS A 1 117 ? 31.915  9.529   38.964  1.00 34.95 ?  109 LYS A CA    1 
ATOM   829  C C     . LYS A 1 117 ? 32.264  8.336   38.085  1.00 36.99 ?  109 LYS A C     1 
ATOM   830  O O     . LYS A 1 117 ? 33.280  7.673   38.321  1.00 31.30 ?  109 LYS A O     1 
ATOM   831  C CB    . LYS A 1 117 ? 31.131  9.076   40.195  1.00 30.82 ?  109 LYS A CB    1 
ATOM   832  C CG    . LYS A 1 117 ? 31.167  10.072  41.343  1.00 36.66 ?  109 LYS A CG    1 
ATOM   833  C CD    . LYS A 1 117 ? 30.762  9.425   42.657  1.00 45.89 ?  109 LYS A CD    1 
ATOM   834  C CE    . LYS A 1 117 ? 29.258  9.499   42.873  1.00 44.63 ?  109 LYS A CE    1 
ATOM   835  N NZ    . LYS A 1 117 ? 28.917  9.859   44.278  1.00 55.26 ?  109 LYS A NZ    1 
ATOM   836  N N     . ALA A 1 118 ? 31.443  8.046   37.072  1.00 33.91 ?  110 ALA A N     1 
ATOM   837  C CA    . ALA A 1 118 ? 31.739  6.924   36.186  1.00 37.81 ?  110 ALA A CA    1 
ATOM   838  C C     . ALA A 1 118 ? 33.031  7.147   35.413  1.00 36.04 ?  110 ALA A C     1 
ATOM   839  O O     . ALA A 1 118 ? 33.730  6.183   35.081  1.00 28.99 ?  110 ALA A O     1 
ATOM   840  C CB    . ALA A 1 118 ? 30.576  6.692   35.222  1.00 34.75 ?  110 ALA A CB    1 
ATOM   841  N N     . TYR A 1 119 ? 33.362  8.402   35.116  1.00 33.74 ?  111 TYR A N     1 
ATOM   842  C CA    . TYR A 1 119 ? 34.616  8.731   34.453  1.00 34.51 ?  111 TYR A CA    1 
ATOM   843  C C     . TYR A 1 119 ? 35.802  8.754   35.409  1.00 34.33 ?  111 TYR A C     1 
ATOM   844  O O     . TYR A 1 119 ? 36.929  9.000   34.966  1.00 34.67 ?  111 TYR A O     1 
ATOM   845  C CB    . TYR A 1 119 ? 34.498  10.084  33.747  1.00 26.77 ?  111 TYR A CB    1 
ATOM   846  C CG    . TYR A 1 119 ? 33.887  10.012  32.366  1.00 31.68 ?  111 TYR A CG    1 
ATOM   847  C CD1   . TYR A 1 119 ? 34.457  9.224   31.375  1.00 29.83 ?  111 TYR A CD1   1 
ATOM   848  C CD2   . TYR A 1 119 ? 32.747  10.741  32.048  1.00 27.63 ?  111 TYR A CD2   1 
ATOM   849  C CE1   . TYR A 1 119 ? 33.906  9.157   30.109  1.00 29.51 ?  111 TYR A CE1   1 
ATOM   850  C CE2   . TYR A 1 119 ? 32.189  10.681  30.783  1.00 29.38 ?  111 TYR A CE2   1 
ATOM   851  C CZ    . TYR A 1 119 ? 32.774  9.887   29.818  1.00 32.64 ?  111 TYR A CZ    1 
ATOM   852  O OH    . TYR A 1 119 ? 32.224  9.825   28.558  1.00 31.01 ?  111 TYR A OH    1 
ATOM   853  N N     . GLY A 1 120 ? 35.580  8.509   36.698  1.00 33.60 ?  112 GLY A N     1 
ATOM   854  C CA    . GLY A 1 120 ? 36.646  8.512   37.676  1.00 28.36 ?  112 GLY A CA    1 
ATOM   855  C C     . GLY A 1 120 ? 36.894  9.835   38.362  1.00 34.92 ?  112 GLY A C     1 
ATOM   856  O O     . GLY A 1 120 ? 37.913  9.976   39.047  1.00 28.18 ?  112 GLY A O     1 
ATOM   857  N N     . ALA A 1 121 ? 36.000  10.806  38.206  1.00 30.64 ?  113 ALA A N     1 
ATOM   858  C CA    . ALA A 1 121 ? 36.197  12.112  38.809  1.00 30.85 ?  113 ALA A CA    1 
ATOM   859  C C     . ALA A 1 121 ? 35.731  12.114  40.264  1.00 34.00 ?  113 ALA A C     1 
ATOM   860  O O     . ALA A 1 121 ? 34.915  11.291  40.687  1.00 34.50 ?  113 ALA A O     1 
ATOM   861  C CB    . ALA A 1 121 ? 35.453  13.188  38.016  1.00 26.36 ?  113 ALA A CB    1 
ATOM   862  N N     . GLU A 1 122 ? 36.275  13.055  41.033  1.00 33.23 ?  114 GLU A N     1 
ATOM   863  C CA    . GLU A 1 122 ? 35.890  13.266  42.421  1.00 34.57 ?  114 GLU A CA    1 
ATOM   864  C C     . GLU A 1 122 ? 34.967  14.474  42.514  1.00 34.50 ?  114 GLU A C     1 
ATOM   865  O O     . GLU A 1 122 ? 35.191  15.492  41.852  1.00 36.08 ?  114 GLU A O     1 
ATOM   866  C CB    . GLU A 1 122 ? 37.122  13.471  43.307  1.00 38.87 ?  114 GLU A CB    1 
ATOM   867  C CG    . GLU A 1 122 ? 36.816  13.839  44.758  1.00 47.73 ?  114 GLU A CG    1 
ATOM   868  C CD    . GLU A 1 122 ? 37.982  14.532  45.448  1.00 58.95 ?  114 GLU A CD    1 
ATOM   869  O OE1   . GLU A 1 122 ? 37.844  14.906  46.634  1.00 68.58 ?  114 GLU A OE1   1 
ATOM   870  O OE2   . GLU A 1 122 ? 39.039  14.702  44.805  1.00 61.40 ?  114 GLU A OE2   1 
ATOM   871  N N     . LEU A 1 123 ? 33.927  14.355  43.333  1.00 29.52 ?  115 LEU A N     1 
ATOM   872  C CA    . LEU A 1 123 ? 32.924  15.399  43.485  1.00 34.93 ?  115 LEU A CA    1 
ATOM   873  C C     . LEU A 1 123 ? 33.058  16.066  44.847  1.00 35.94 ?  115 LEU A C     1 
ATOM   874  O O     . LEU A 1 123 ? 33.255  15.393  45.864  1.00 34.15 ?  115 LEU A O     1 
ATOM   875  C CB    . LEU A 1 123 ? 31.513  14.832  43.319  1.00 37.03 ?  115 LEU A CB    1 
ATOM   876  C CG    . LEU A 1 123 ? 31.238  14.152  41.978  1.00 33.49 ?  115 LEU A CG    1 
ATOM   877  C CD1   . LEU A 1 123 ? 29.755  13.886  41.812  1.00 39.70 ?  115 LEU A CD1   1 
ATOM   878  C CD2   . LEU A 1 123 ? 31.766  14.998  40.832  1.00 36.84 ?  115 LEU A CD2   1 
ATOM   879  N N     . VAL A 1 124 ? 32.953  17.392  44.856  1.00 34.22 ?  116 VAL A N     1 
ATOM   880  C CA    . VAL A 1 124 ? 33.028  18.195  46.072  1.00 29.46 ?  116 VAL A CA    1 
ATOM   881  C C     . VAL A 1 124 ? 31.765  19.042  46.108  1.00 33.85 ?  116 VAL A C     1 
ATOM   882  O O     . VAL A 1 124 ? 31.641  20.020  45.363  1.00 35.46 ?  116 VAL A O     1 
ATOM   883  C CB    . VAL A 1 124 ? 34.281  19.074  46.123  1.00 35.57 ?  116 VAL A CB    1 
ATOM   884  C CG1   . VAL A 1 124 ? 34.201  20.035  47.298  1.00 28.27 ?  116 VAL A CG1   1 
ATOM   885  C CG2   . VAL A 1 124 ? 35.530  18.212  46.211  1.00 31.23 ?  116 VAL A CG2   1 
ATOM   886  N N     . LEU A 1 125 ? 30.829  18.677  46.973  1.00 29.64 ?  117 LEU A N     1 
ATOM   887  C CA    . LEU A 1 125 ? 29.537  19.342  47.029  1.00 33.60 ?  117 LEU A CA    1 
ATOM   888  C C     . LEU A 1 125 ? 29.584  20.533  47.973  1.00 36.52 ?  117 LEU A C     1 
ATOM   889  O O     . LEU A 1 125 ? 30.111  20.437  49.086  1.00 39.57 ?  117 LEU A O     1 
ATOM   890  C CB    . LEU A 1 125 ? 28.458  18.368  47.477  1.00 34.22 ?  117 LEU A CB    1 
ATOM   891  C CG    . LEU A 1 125 ? 28.422  17.037  46.745  1.00 36.98 ?  117 LEU A CG    1 
ATOM   892  C CD1   . LEU A 1 125 ? 27.229  16.281  47.257  1.00 44.11 ?  117 LEU A CD1   1 
ATOM   893  C CD2   . LEU A 1 125 ? 28.330  17.259  45.242  1.00 34.10 ?  117 LEU A CD2   1 
ATOM   894  N N     . THR A 1 126 ? 29.010  21.638  47.533  1.00 33.54 ?  118 THR A N     1 
ATOM   895  C CA    . THR A 1 126 ? 28.931  22.866  48.296  1.00 35.67 ?  118 THR A CA    1 
ATOM   896  C C     . THR A 1 126 ? 27.495  23.121  48.736  1.00 34.85 ?  118 THR A C     1 
ATOM   897  O O     . THR A 1 126 ? 26.558  22.520  48.199  1.00 34.64 ?  118 THR A O     1 
ATOM   898  C CB    . THR A 1 126 ? 29.447  24.041  47.453  1.00 35.39 ?  118 THR A CB    1 
ATOM   899  O OG1   . THR A 1 126 ? 28.613  24.208  46.300  1.00 34.64 ?  118 THR A OG1   1 
ATOM   900  C CG2   . THR A 1 126 ? 30.877  23.775  47.008  1.00 37.35 ?  118 THR A CG2   1 
ATOM   901  N N     . PRO A 1 127 ? 27.286  23.979  49.735  1.00 33.06 ?  119 PRO A N     1 
ATOM   902  C CA    . PRO A 1 127 ? 25.917  24.265  50.186  1.00 33.37 ?  119 PRO A CA    1 
ATOM   903  C C     . PRO A 1 127 ? 25.020  24.711  49.040  1.00 38.31 ?  119 PRO A C     1 
ATOM   904  O O     . PRO A 1 127 ? 25.379  25.585  48.246  1.00 41.27 ?  119 PRO A O     1 
ATOM   905  C CB    . PRO A 1 127 ? 26.102  25.381  51.223  1.00 37.27 ?  119 PRO A CB    1 
ATOM   906  C CG    . PRO A 1 127 ? 27.575  25.610  51.363  1.00 46.12 ?  119 PRO A CG    1 
ATOM   907  C CD    . PRO A 1 127 ? 28.300  24.519  50.656  1.00 38.19 ?  119 PRO A CD    1 
ATOM   908  N N     . GLY A 1 128 ? 23.845  24.083  48.949  1.00 42.40 ?  120 GLY A N     1 
ATOM   909  C CA    . GLY A 1 128 ? 22.904  24.445  47.902  1.00 36.87 ?  120 GLY A CA    1 
ATOM   910  C C     . GLY A 1 128 ? 22.440  25.885  48.008  1.00 40.27 ?  120 GLY A C     1 
ATOM   911  O O     . GLY A 1 128 ? 22.180  26.539  46.995  1.00 42.47 ?  120 GLY A O     1 
ATOM   912  N N     . SER A 1 129 ? 22.340  26.401  49.237  1.00 47.05 ?  121 SER A N     1 
ATOM   913  C CA    . SER A 1 129 ? 21.942  27.789  49.437  1.00 50.59 ?  121 SER A CA    1 
ATOM   914  C C     . SER A 1 129 ? 22.938  28.771  48.833  1.00 48.00 ?  121 SER A C     1 
ATOM   915  O O     . SER A 1 129 ? 22.574  29.923  48.571  1.00 45.95 ?  121 SER A O     1 
ATOM   916  C CB    . SER A 1 129 ? 21.769  28.071  50.929  1.00 53.56 ?  121 SER A CB    1 
ATOM   917  O OG    . SER A 1 129 ? 22.914  28.716  51.459  1.00 69.53 ?  121 SER A OG    1 
ATOM   918  N N     . GLU A 1 130 ? 24.178  28.345  48.602  1.00 42.89 ?  122 GLU A N     1 
ATOM   919  C CA    . GLU A 1 130 ? 25.207  29.211  48.047  1.00 44.69 ?  122 GLU A CA    1 
ATOM   920  C C     . GLU A 1 130 ? 25.297  29.134  46.528  1.00 43.14 ?  122 GLU A C     1 
ATOM   921  O O     . GLU A 1 130 ? 26.103  29.862  45.936  1.00 38.44 ?  122 GLU A O     1 
ATOM   922  C CB    . GLU A 1 130 ? 26.566  28.869  48.662  1.00 42.21 ?  122 GLU A CB    1 
ATOM   923  C CG    . GLU A 1 130 ? 26.695  29.275  50.115  1.00 52.00 ?  122 GLU A CG    1 
ATOM   924  C CD    . GLU A 1 130 ? 27.532  30.524  50.293  1.00 66.46 ?  122 GLU A CD    1 
ATOM   925  O OE1   . GLU A 1 130 ? 28.774  30.428  50.207  1.00 67.86 ?  122 GLU A OE1   1 
ATOM   926  O OE2   . GLU A 1 130 ? 26.943  31.603  50.518  1.00 65.08 ?  122 GLU A OE2   1 
ATOM   927  N N     . ALA A 1 131 ? 24.493  28.274  45.892  1.00 40.00 ?  123 ALA A N     1 
ATOM   928  C CA    . ALA A 1 131 ? 24.434  28.147  44.438  1.00 35.79 ?  123 ALA A CA    1 
ATOM   929  C C     . ALA A 1 131 ? 25.831  27.954  43.852  1.00 37.10 ?  123 ALA A C     1 
ATOM   930  O O     . ALA A 1 131 ? 26.625  27.175  44.388  1.00 39.24 ?  123 ALA A O     1 
ATOM   931  C CB    . ALA A 1 131 ? 23.731  29.362  43.829  1.00 35.07 ?  123 ALA A CB    1 
ATOM   932  N N     . MET A 1 132 ? 26.152  28.650  42.759  1.00 32.13 ?  124 MET A N     1 
ATOM   933  C CA    . MET A 1 132 ? 27.487  28.517  42.181  1.00 35.09 ?  124 MET A CA    1 
ATOM   934  C C     . MET A 1 132 ? 28.504  29.430  42.841  1.00 37.29 ?  124 MET A C     1 
ATOM   935  O O     . MET A 1 132 ? 29.708  29.248  42.627  1.00 35.71 ?  124 MET A O     1 
ATOM   936  C CB    . MET A 1 132 ? 27.454  28.801  40.682  1.00 31.71 ?  124 MET A CB    1 
ATOM   937  C CG    . MET A 1 132 ? 26.510  27.911  39.916  1.00 35.54 ?  124 MET A CG    1 
ATOM   938  S SD    . MET A 1 132 ? 27.101  26.213  39.759  1.00 34.53 ?  124 MET A SD    1 
ATOM   939  C CE    . MET A 1 132 ? 28.881  26.434  39.712  1.00 31.83 ?  124 MET A CE    1 
ATOM   940  N N     . LYS A 1 133 ? 28.045  30.419  43.609  1.00 35.50 ?  125 LYS A N     1 
ATOM   941  C CA    . LYS A 1 133 ? 28.964  31.225  44.403  1.00 37.01 ?  125 LYS A CA    1 
ATOM   942  C C     . LYS A 1 133 ? 29.729  30.355  45.393  1.00 38.20 ?  125 LYS A C     1 
ATOM   943  O O     . LYS A 1 133 ? 30.930  30.554  45.607  1.00 36.76 ?  125 LYS A O     1 
ATOM   944  C CB    . LYS A 1 133 ? 28.194  32.328  45.132  1.00 33.29 ?  125 LYS A CB    1 
ATOM   945  N N     . GLY A 1 134 ? 29.053  29.373  45.991  1.00 36.90 ?  126 GLY A N     1 
ATOM   946  C CA    . GLY A 1 134 ? 29.735  28.469  46.902  1.00 41.45 ?  126 GLY A CA    1 
ATOM   947  C C     . GLY A 1 134 ? 30.667  27.507  46.189  1.00 39.52 ?  126 GLY A C     1 
ATOM   948  O O     . GLY A 1 134 ? 31.754  27.201  46.685  1.00 34.15 ?  126 GLY A O     1 
ATOM   949  N N     . ALA A 1 135 ? 30.253  27.013  45.018  1.00 38.09 ?  127 ALA A N     1 
ATOM   950  C CA    . ALA A 1 135 ? 31.111  26.117  44.247  1.00 33.62 ?  127 ALA A CA    1 
ATOM   951  C C     . ALA A 1 135 ? 32.350  26.841  43.737  1.00 33.81 ?  127 ALA A C     1 
ATOM   952  O O     . ALA A 1 135 ? 33.445  26.267  43.709  1.00 36.63 ?  127 ALA A O     1 
ATOM   953  C CB    . ALA A 1 135 ? 30.330  25.512  43.082  1.00 34.14 ?  127 ALA A CB    1 
ATOM   954  N N     . ILE A 1 136 ? 32.195  28.098  43.320  1.00 34.82 ?  128 ILE A N     1 
ATOM   955  C CA    . ILE A 1 136 ? 33.343  28.884  42.877  1.00 35.20 ?  128 ILE A CA    1 
ATOM   956  C C     . ILE A 1 136 ? 34.325  29.075  44.026  1.00 35.91 ?  128 ILE A C     1 
ATOM   957  O O     . ILE A 1 136 ? 35.543  28.941  43.854  1.00 38.37 ?  128 ILE A O     1 
ATOM   958  C CB    . ILE A 1 136 ? 32.876  30.232  42.300  1.00 33.99 ?  128 ILE A CB    1 
ATOM   959  C CG1   . ILE A 1 136 ? 32.207  30.027  40.939  1.00 39.77 ?  128 ILE A CG1   1 
ATOM   960  C CG2   . ILE A 1 136 ? 34.041  31.202  42.181  1.00 31.89 ?  128 ILE A CG2   1 
ATOM   961  C CD1   . ILE A 1 136 ? 31.706  31.305  40.313  1.00 37.49 ?  128 ILE A CD1   1 
ATOM   962  N N     . LYS A 1 137 ? 33.805  29.380  45.220  1.00 32.31 ?  129 LYS A N     1 
ATOM   963  C CA    . LYS A 1 137 ? 34.664  29.579  46.384  1.00 35.15 ?  129 LYS A CA    1 
ATOM   964  C C     . LYS A 1 137 ? 35.469  28.321  46.687  1.00 35.49 ?  129 LYS A C     1 
ATOM   965  O O     . LYS A 1 137 ? 36.694  28.377  46.845  1.00 34.50 ?  129 LYS A O     1 
ATOM   966  C CB    . LYS A 1 137 ? 33.817  29.999  47.594  1.00 35.48 ?  129 LYS A CB    1 
ATOM   967  C CG    . LYS A 1 137 ? 34.602  30.344  48.877  1.00 47.21 ?  129 LYS A CG    1 
ATOM   968  C CD    . LYS A 1 137 ? 34.955  29.119  49.727  1.00 47.33 ?  129 LYS A CD    1 
ATOM   969  C CE    . LYS A 1 137 ? 36.076  29.418  50.711  1.00 55.87 ?  129 LYS A CE    1 
ATOM   970  N NZ    . LYS A 1 137 ? 36.913  28.210  50.946  1.00 45.44 ?  129 LYS A NZ    1 
ATOM   971  N N     . LYS A 1 138 ? 34.794  27.173  46.761  1.00 33.96 ?  130 LYS A N     1 
ATOM   972  C CA    . LYS A 1 138 ? 35.478  25.932  47.107  1.00 36.71 ?  130 LYS A CA    1 
ATOM   973  C C     . LYS A 1 138 ? 36.496  25.543  46.039  1.00 34.88 ?  130 LYS A C     1 
ATOM   974  O O     . LYS A 1 138 ? 37.563  25.002  46.356  1.00 39.13 ?  130 LYS A O     1 
ATOM   975  C CB    . LYS A 1 138 ? 34.452  24.817  47.317  1.00 35.68 ?  130 LYS A CB    1 
ATOM   976  C CG    . LYS A 1 138 ? 35.055  23.476  47.682  1.00 33.02 ?  130 LYS A CG    1 
ATOM   977  C CD    . LYS A 1 138 ? 36.029  23.601  48.839  1.00 38.71 ?  130 LYS A CD    1 
ATOM   978  C CE    . LYS A 1 138 ? 35.314  23.556  50.175  1.00 43.43 ?  130 LYS A CE    1 
ATOM   979  N NZ    . LYS A 1 138 ? 36.041  22.687  51.141  1.00 47.10 ?  130 LYS A NZ    1 
ATOM   980  N N     . ALA A 1 139 ? 36.189  25.819  44.768  1.00 31.06 ?  131 ALA A N     1 
ATOM   981  C CA    . ALA A 1 139 ? 37.136  25.515  43.700  1.00 34.66 ?  131 ALA A CA    1 
ATOM   982  C C     . ALA A 1 139 ? 38.418  26.325  43.853  1.00 36.36 ?  131 ALA A C     1 
ATOM   983  O O     . ALA A 1 139 ? 39.522  25.789  43.696  1.00 31.43 ?  131 ALA A O     1 
ATOM   984  C CB    . ALA A 1 139 ? 36.493  25.772  42.338  1.00 26.59 ?  131 ALA A CB    1 
ATOM   985  N N     . LYS A 1 140 ? 38.294  27.617  44.167  1.00 30.22 ?  132 LYS A N     1 
ATOM   986  C CA    . LYS A 1 140 ? 39.484  28.438  44.375  1.00 34.06 ?  132 LYS A CA    1 
ATOM   987  C C     . LYS A 1 140 ? 40.272  27.965  45.591  1.00 41.04 ?  132 LYS A C     1 
ATOM   988  O O     . LYS A 1 140 ? 41.509  27.961  45.575  1.00 33.13 ?  132 LYS A O     1 
ATOM   989  C CB    . LYS A 1 140 ? 39.095  29.908  44.533  1.00 39.72 ?  132 LYS A CB    1 
ATOM   990  C CG    . LYS A 1 140 ? 40.270  30.829  44.840  1.00 44.08 ?  132 LYS A CG    1 
ATOM   991  C CD    . LYS A 1 140 ? 39.949  32.276  44.496  1.00 53.55 ?  132 LYS A CD    1 
ATOM   992  C CE    . LYS A 1 140 ? 39.794  33.117  45.755  1.00 55.65 ?  132 LYS A CE    1 
ATOM   993  N NZ    . LYS A 1 140 ? 40.965  32.977  46.662  1.00 57.58 ?  132 LYS A NZ    1 
ATOM   994  N N     . GLU A 1 141 ? 39.570  27.566  46.655  1.00 31.72 ?  133 GLU A N     1 
ATOM   995  C CA    . GLU A 1 141 ? 40.242  27.076  47.855  1.00 41.13 ?  133 GLU A CA    1 
ATOM   996  C C     . GLU A 1 141 ? 41.019  25.797  47.565  1.00 40.53 ?  133 GLU A C     1 
ATOM   997  O O     . GLU A 1 141 ? 42.181  25.658  47.963  1.00 34.22 ?  133 GLU A O     1 
ATOM   998  C CB    . GLU A 1 141 ? 39.221  26.847  48.970  1.00 32.03 ?  133 GLU A CB    1 
ATOM   999  N N     . LEU A 1 142 ? 40.388  24.847  46.871  1.00 38.91 ?  134 LEU A N     1 
ATOM   1000 C CA    . LEU A 1 142 ? 41.087  23.624  46.490  1.00 36.83 ?  134 LEU A CA    1 
ATOM   1001 C C     . LEU A 1 142 ? 42.261  23.926  45.568  1.00 34.69 ?  134 LEU A C     1 
ATOM   1002 O O     . LEU A 1 142 ? 43.315  23.284  45.660  1.00 36.67 ?  134 LEU A O     1 
ATOM   1003 C CB    . LEU A 1 142 ? 40.116  22.652  45.820  1.00 33.34 ?  134 LEU A CB    1 
ATOM   1004 C CG    . LEU A 1 142 ? 39.011  22.067  46.699  1.00 36.45 ?  134 LEU A CG    1 
ATOM   1005 C CD1   . LEU A 1 142 ? 38.217  21.032  45.918  1.00 33.62 ?  134 LEU A CD1   1 
ATOM   1006 C CD2   . LEU A 1 142 ? 39.591  21.460  47.967  1.00 32.95 ?  134 LEU A CD2   1 
ATOM   1007 N N     . LYS A 1 143 ? 42.096  24.902  44.672  1.00 36.56 ?  135 LYS A N     1 
ATOM   1008 C CA    . LYS A 1 143 ? 43.188  25.305  43.791  1.00 33.77 ?  135 LYS A CA    1 
ATOM   1009 C C     . LYS A 1 143 ? 44.387  25.799  44.590  1.00 36.13 ?  135 LYS A C     1 
ATOM   1010 O O     . LYS A 1 143 ? 45.525  25.378  44.353  1.00 41.07 ?  135 LYS A O     1 
ATOM   1011 C CB    . LYS A 1 143 ? 42.702  26.388  42.828  1.00 35.88 ?  135 LYS A CB    1 
ATOM   1012 C CG    . LYS A 1 143 ? 43.736  26.855  41.818  1.00 33.56 ?  135 LYS A CG    1 
ATOM   1013 C CD    . LYS A 1 143 ? 43.176  27.981  40.956  1.00 45.41 ?  135 LYS A CD    1 
ATOM   1014 C CE    . LYS A 1 143 ? 43.807  29.324  41.304  1.00 54.50 ?  135 LYS A CE    1 
ATOM   1015 N NZ    . LYS A 1 143 ? 45.292  29.264  41.271  1.00 62.10 ?  135 LYS A NZ    1 
ATOM   1016 N N     . GLU A 1 144 ? 44.147  26.691  45.551  1.00 36.32 ?  136 GLU A N     1 
ATOM   1017 C CA    . GLU A 1 144 ? 45.247  27.298  46.292  1.00 37.83 ?  136 GLU A CA    1 
ATOM   1018 C C     . GLU A 1 144 ? 45.875  26.309  47.267  1.00 37.33 ?  136 GLU A C     1 
ATOM   1019 O O     . GLU A 1 144 ? 47.102  26.167  47.318  1.00 36.75 ?  136 GLU A O     1 
ATOM   1020 C CB    . GLU A 1 144 ? 44.752  28.544  47.029  1.00 37.16 ?  136 GLU A CB    1 
ATOM   1021 C CG    . GLU A 1 144 ? 44.978  29.842  46.274  1.00 49.47 ?  136 GLU A CG    1 
ATOM   1022 C CD    . GLU A 1 144 ? 43.804  30.798  46.389  1.00 65.54 ?  136 GLU A CD    1 
ATOM   1023 O OE1   . GLU A 1 144 ? 43.659  31.676  45.511  1.00 60.63 ?  136 GLU A OE1   1 
ATOM   1024 O OE2   . GLU A 1 144 ? 43.025  30.669  47.359  1.00 61.31 ?  136 GLU A OE2   1 
ATOM   1025 N N     . GLU A 1 145 ? 45.050  25.607  48.044  1.00 37.33 ?  137 GLU A N     1 
ATOM   1026 C CA    . GLU A 1 145 ? 45.568  24.784  49.130  1.00 42.24 ?  137 GLU A CA    1 
ATOM   1027 C C     . GLU A 1 145 ? 46.170  23.467  48.660  1.00 43.94 ?  137 GLU A C     1 
ATOM   1028 O O     . GLU A 1 145 ? 47.002  22.897  49.374  1.00 41.48 ?  137 GLU A O     1 
ATOM   1029 C CB    . GLU A 1 145 ? 44.467  24.499  50.155  1.00 45.01 ?  137 GLU A CB    1 
ATOM   1030 C CG    . GLU A 1 145 ? 43.865  25.747  50.781  1.00 47.11 ?  137 GLU A CG    1 
ATOM   1031 C CD    . GLU A 1 145 ? 42.719  25.432  51.722  1.00 58.05 ?  137 GLU A CD    1 
ATOM   1032 O OE1   . GLU A 1 145 ? 42.236  26.359  52.407  1.00 64.15 ?  137 GLU A OE1   1 
ATOM   1033 O OE2   . GLU A 1 145 ? 42.303  24.255  51.778  1.00 62.20 ?  137 GLU A OE2   1 
ATOM   1034 N N     . HIS A 1 146 ? 45.779  22.968  47.488  1.00 38.93 ?  138 HIS A N     1 
ATOM   1035 C CA    . HIS A 1 146 ? 46.237  21.665  47.029  1.00 38.78 ?  138 HIS A CA    1 
ATOM   1036 C C     . HIS A 1 146 ? 46.903  21.695  45.659  1.00 35.61 ?  138 HIS A C     1 
ATOM   1037 O O     . HIS A 1 146 ? 47.419  20.661  45.219  1.00 40.90 ?  138 HIS A O     1 
ATOM   1038 C CB    . HIS A 1 146 ? 45.068  20.669  47.026  1.00 42.22 ?  138 HIS A CB    1 
ATOM   1039 C CG    . HIS A 1 146 ? 44.456  20.457  48.378  1.00 41.49 ?  138 HIS A CG    1 
ATOM   1040 N ND1   . HIS A 1 146 ? 43.113  20.640  48.626  1.00 43.52 ?  138 HIS A ND1   1 
ATOM   1041 C CD2   . HIS A 1 146 ? 45.009  20.088  49.558  1.00 40.46 ?  138 HIS A CD2   1 
ATOM   1042 C CE1   . HIS A 1 146 ? 42.864  20.388  49.900  1.00 43.87 ?  138 HIS A CE1   1 
ATOM   1043 N NE2   . HIS A 1 146 ? 43.998  20.051  50.487  1.00 47.74 ?  138 HIS A NE2   1 
ATOM   1044 N N     . GLY A 1 147 ? 46.913  22.838  44.978  1.00 35.65 ?  139 GLY A N     1 
ATOM   1045 C CA    . GLY A 1 147 ? 47.674  22.975  43.752  1.00 36.35 ?  139 GLY A CA    1 
ATOM   1046 C C     . GLY A 1 147 ? 47.027  22.421  42.504  1.00 35.74 ?  139 GLY A C     1 
ATOM   1047 O O     . GLY A 1 147 ? 47.735  22.132  41.533  1.00 33.10 ?  139 GLY A O     1 
ATOM   1048 N N     . TYR A 1 148 ? 45.707  22.262  42.491  1.00 36.49 ?  140 TYR A N     1 
ATOM   1049 C CA    . TYR A 1 148 ? 45.035  21.783  41.293  1.00 32.72 ?  140 TYR A CA    1 
ATOM   1050 C C     . TYR A 1 148 ? 45.008  22.873  40.227  1.00 29.38 ?  140 TYR A C     1 
ATOM   1051 O O     . TYR A 1 148 ? 44.962  24.068  40.527  1.00 31.58 ?  140 TYR A O     1 
ATOM   1052 C CB    . TYR A 1 148 ? 43.604  21.344  41.605  1.00 31.26 ?  140 TYR A CB    1 
ATOM   1053 C CG    . TYR A 1 148 ? 43.455  20.345  42.732  1.00 36.83 ?  140 TYR A CG    1 
ATOM   1054 C CD1   . TYR A 1 148 ? 44.479  19.464  43.056  1.00 37.97 ?  140 TYR A CD1   1 
ATOM   1055 C CD2   . TYR A 1 148 ? 42.277  20.278  43.467  1.00 36.10 ?  140 TYR A CD2   1 
ATOM   1056 C CE1   . TYR A 1 148 ? 44.336  18.549  44.085  1.00 34.49 ?  140 TYR A CE1   1 
ATOM   1057 C CE2   . TYR A 1 148 ? 42.125  19.368  44.495  1.00 40.47 ?  140 TYR A CE2   1 
ATOM   1058 C CZ    . TYR A 1 148 ? 43.157  18.506  44.800  1.00 35.72 ?  140 TYR A CZ    1 
ATOM   1059 O OH    . TYR A 1 148 ? 43.008  17.599  45.824  1.00 32.15 ?  140 TYR A OH    1 
ATOM   1060 N N     . PHE A 1 149 ? 45.035  22.448  38.968  1.00 27.26 ?  141 PHE A N     1 
ATOM   1061 C CA    . PHE A 1 149 ? 44.898  23.379  37.857  1.00 31.12 ?  141 PHE A CA    1 
ATOM   1062 C C     . PHE A 1 149 ? 43.425  23.687  37.623  1.00 28.61 ?  141 PHE A C     1 
ATOM   1063 O O     . PHE A 1 149 ? 42.596  22.776  37.554  1.00 27.02 ?  141 PHE A O     1 
ATOM   1064 C CB    . PHE A 1 149 ? 45.523  22.796  36.592  1.00 27.13 ?  141 PHE A CB    1 
ATOM   1065 C CG    . PHE A 1 149 ? 45.372  23.673  35.380  1.00 28.70 ?  141 PHE A CG    1 
ATOM   1066 C CD1   . PHE A 1 149 ? 46.152  24.808  35.225  1.00 27.27 ?  141 PHE A CD1   1 
ATOM   1067 C CD2   . PHE A 1 149 ? 44.444  23.365  34.397  1.00 32.31 ?  141 PHE A CD2   1 
ATOM   1068 C CE1   . PHE A 1 149 ? 46.014  25.617  34.109  1.00 27.72 ?  141 PHE A CE1   1 
ATOM   1069 C CE2   . PHE A 1 149 ? 44.299  24.170  33.280  1.00 26.85 ?  141 PHE A CE2   1 
ATOM   1070 C CZ    . PHE A 1 149 ? 45.085  25.298  33.136  1.00 31.30 ?  141 PHE A CZ    1 
ATOM   1071 N N     . GLU A 1 150 ? 43.098  24.968  37.502  1.00 27.52 ?  142 GLU A N     1 
ATOM   1072 C CA    . GLU A 1 150 ? 41.716  25.365  37.269  1.00 28.67 ?  142 GLU A CA    1 
ATOM   1073 C C     . GLU A 1 150 ? 41.578  25.892  35.849  1.00 28.41 ?  142 GLU A C     1 
ATOM   1074 O O     . GLU A 1 150 ? 42.108  26.972  35.542  1.00 34.16 ?  142 GLU A O     1 
ATOM   1075 C CB    . GLU A 1 150 ? 41.275  26.420  38.282  1.00 30.83 ?  142 GLU A CB    1 
ATOM   1076 C CG    . GLU A 1 150 ? 39.786  26.687  38.260  1.00 31.08 ?  142 GLU A CG    1 
ATOM   1077 C CD    . GLU A 1 150 ? 39.388  27.869  39.114  1.00 37.83 ?  142 GLU A CD    1 
ATOM   1078 O OE1   . GLU A 1 150 ? 40.262  28.704  39.433  1.00 41.68 ?  142 GLU A OE1   1 
ATOM   1079 O OE2   . GLU A 1 150 ? 38.195  27.956  39.470  1.00 37.36 ?  142 GLU A OE2   1 
ATOM   1080 N N     . PRO A 1 151 ? 40.904  25.167  34.948  1.00 27.42 ?  143 PRO A N     1 
ATOM   1081 C CA    . PRO A 1 151 ? 40.825  25.633  33.551  1.00 25.96 ?  143 PRO A CA    1 
ATOM   1082 C C     . PRO A 1 151 ? 40.123  26.970  33.387  1.00 32.85 ?  143 PRO A C     1 
ATOM   1083 O O     . PRO A 1 151 ? 40.503  27.753  32.506  1.00 27.34 ?  143 PRO A O     1 
ATOM   1084 C CB    . PRO A 1 151 ? 40.060  24.501  32.848  1.00 30.57 ?  143 PRO A CB    1 
ATOM   1085 C CG    . PRO A 1 151 ? 40.237  23.304  33.719  1.00 32.30 ?  143 PRO A CG    1 
ATOM   1086 C CD    . PRO A 1 151 ? 40.369  23.806  35.122  1.00 26.19 ?  143 PRO A CD    1 
ATOM   1087 N N     . GLN A 1 152 ? 39.105  27.249  34.207  1.00 28.50 ?  144 GLN A N     1 
ATOM   1088 C CA    . GLN A 1 152 ? 38.355  28.503  34.158  1.00 29.93 ?  144 GLN A CA    1 
ATOM   1089 C C     . GLN A 1 152 ? 37.680  28.679  32.802  1.00 28.16 ?  144 GLN A C     1 
ATOM   1090 O O     . GLN A 1 152 ? 38.176  29.408  31.936  1.00 26.29 ?  144 GLN A O     1 
ATOM   1091 C CB    . GLN A 1 152 ? 39.271  29.691  34.474  1.00 32.00 ?  144 GLN A CB    1 
ATOM   1092 C CG    . GLN A 1 152 ? 39.529  29.892  35.959  1.00 35.91 ?  144 GLN A CG    1 
ATOM   1093 C CD    . GLN A 1 152 ? 40.688  30.830  36.225  1.00 38.49 ?  144 GLN A CD    1 
ATOM   1094 O OE1   . GLN A 1 152 ? 40.718  31.955  35.725  1.00 42.19 ?  144 GLN A OE1   1 
ATOM   1095 N NE2   . GLN A 1 152 ? 41.652  30.371  37.018  1.00 44.90 ?  144 GLN A NE2   1 
ATOM   1096 N N     . GLN A 1 153 ? 36.534  28.017  32.624  1.00 29.66 ?  145 GLN A N     1 
ATOM   1097 C CA    . GLN A 1 153 ? 35.858  27.982  31.332  1.00 25.89 ?  145 GLN A CA    1 
ATOM   1098 C C     . GLN A 1 153 ? 35.319  29.340  30.901  1.00 24.79 ?  145 GLN A C     1 
ATOM   1099 O O     . GLN A 1 153 ? 35.053  29.537  29.710  1.00 26.94 ?  145 GLN A O     1 
ATOM   1100 C CB    . GLN A 1 153 ? 34.721  26.964  31.380  1.00 22.86 ?  145 GLN A CB    1 
ATOM   1101 C CG    . GLN A 1 153 ? 33.683  27.252  32.448  1.00 28.75 ?  145 GLN A CG    1 
ATOM   1102 C CD    . GLN A 1 153 ? 32.455  26.389  32.290  1.00 28.88 ?  145 GLN A CD    1 
ATOM   1103 O OE1   . GLN A 1 153 ? 32.018  26.117  31.173  1.00 30.02 ?  145 GLN A OE1   1 
ATOM   1104 N NE2   . GLN A 1 153 ? 31.901  25.935  33.408  1.00 29.91 ?  145 GLN A NE2   1 
ATOM   1105 N N     . PHE A 1 154 ? 35.149  30.277  31.830  1.00 25.14 ?  146 PHE A N     1 
ATOM   1106 C CA    . PHE A 1 154 ? 34.627  31.593  31.492  1.00 27.01 ?  146 PHE A CA    1 
ATOM   1107 C C     . PHE A 1 154 ? 35.718  32.608  31.179  1.00 28.26 ?  146 PHE A C     1 
ATOM   1108 O O     . PHE A 1 154 ? 35.399  33.738  30.795  1.00 27.73 ?  146 PHE A O     1 
ATOM   1109 C CB    . PHE A 1 154 ? 33.749  32.120  32.630  1.00 26.19 ?  146 PHE A CB    1 
ATOM   1110 C CG    . PHE A 1 154 ? 32.462  31.364  32.799  1.00 24.79 ?  146 PHE A CG    1 
ATOM   1111 C CD1   . PHE A 1 154 ? 31.396  31.582  31.940  1.00 25.49 ?  146 PHE A CD1   1 
ATOM   1112 C CD2   . PHE A 1 154 ? 32.316  30.437  33.818  1.00 22.25 ?  146 PHE A CD2   1 
ATOM   1113 C CE1   . PHE A 1 154 ? 30.205  30.889  32.094  1.00 24.82 ?  146 PHE A CE1   1 
ATOM   1114 C CE2   . PHE A 1 154 ? 31.129  29.741  33.979  1.00 29.11 ?  146 PHE A CE2   1 
ATOM   1115 C CZ    . PHE A 1 154 ? 30.072  29.968  33.116  1.00 30.22 ?  146 PHE A CZ    1 
ATOM   1116 N N     . GLU A 1 155 ? 36.990  32.238  31.333  1.00 26.93 ?  147 GLU A N     1 
ATOM   1117 C CA    . GLU A 1 155 ? 38.097  33.133  31.028  1.00 30.75 ?  147 GLU A CA    1 
ATOM   1118 C C     . GLU A 1 155 ? 39.136  32.522  30.102  1.00 30.12 ?  147 GLU A C     1 
ATOM   1119 O O     . GLU A 1 155 ? 39.962  33.265  29.561  1.00 33.35 ?  147 GLU A O     1 
ATOM   1120 C CB    . GLU A 1 155 ? 38.800  33.583  32.320  1.00 26.75 ?  147 GLU A CB    1 
ATOM   1121 C CG    . GLU A 1 155 ? 37.886  34.189  33.377  1.00 27.40 ?  147 GLU A CG    1 
ATOM   1122 C CD    . GLU A 1 155 ? 37.357  35.559  32.993  1.00 38.58 ?  147 GLU A CD    1 
ATOM   1123 O OE1   . GLU A 1 155 ? 37.906  36.176  32.054  1.00 41.89 ?  147 GLU A OE1   1 
ATOM   1124 O OE2   . GLU A 1 155 ? 36.390  36.022  33.635  1.00 40.58 ?  147 GLU A OE2   1 
ATOM   1125 N N     . ASN A 1 156 ? 39.121  31.212  29.898  1.00 30.71 ?  148 ASN A N     1 
ATOM   1126 C CA    . ASN A 1 156 ? 40.187  30.546  29.161  1.00 25.44 ?  148 ASN A CA    1 
ATOM   1127 C C     . ASN A 1 156 ? 40.043  30.813  27.669  1.00 24.01 ?  148 ASN A C     1 
ATOM   1128 O O     . ASN A 1 156 ? 39.024  30.435  27.080  1.00 31.77 ?  148 ASN A O     1 
ATOM   1129 C CB    . ASN A 1 156 ? 40.158  29.051  29.435  1.00 25.79 ?  148 ASN A CB    1 
ATOM   1130 C CG    . ASN A 1 156 ? 41.473  28.378  29.122  1.00 28.29 ?  148 ASN A CG    1 
ATOM   1131 O OD1   . ASN A 1 156 ? 42.061  28.595  28.063  1.00 28.23 ?  148 ASN A OD1   1 
ATOM   1132 N ND2   . ASN A 1 156 ? 41.952  27.561  30.052  1.00 25.26 ?  148 ASN A ND2   1 
ATOM   1133 N N     . PRO A 1 157 ? 41.033  31.430  27.018  1.00 28.16 ?  149 PRO A N     1 
ATOM   1134 C CA    . PRO A 1 157 ? 40.890  31.731  25.583  1.00 25.39 ?  149 PRO A CA    1 
ATOM   1135 C C     . PRO A 1 157 ? 40.869  30.499  24.697  1.00 26.32 ?  149 PRO A C     1 
ATOM   1136 O O     . PRO A 1 157 ? 40.450  30.605  23.539  1.00 23.09 ?  149 PRO A O     1 
ATOM   1137 C CB    . PRO A 1 157 ? 42.107  32.612  25.276  1.00 31.13 ?  149 PRO A CB    1 
ATOM   1138 C CG    . PRO A 1 157 ? 43.087  32.354  26.369  1.00 28.77 ?  149 PRO A CG    1 
ATOM   1139 C CD    . PRO A 1 157 ? 42.361  31.780  27.551  1.00 30.43 ?  149 PRO A CD    1 
ATOM   1140 N N     . ALA A 1 158 ? 41.312  29.341  25.192  1.00 25.68 ?  150 ALA A N     1 
ATOM   1141 C CA    . ALA A 1 158 ? 41.185  28.109  24.423  1.00 25.64 ?  150 ALA A CA    1 
ATOM   1142 C C     . ALA A 1 158 ? 39.728  27.739  24.186  1.00 27.09 ?  150 ALA A C     1 
ATOM   1143 O O     . ALA A 1 158 ? 39.430  26.997  23.245  1.00 25.38 ?  150 ALA A O     1 
ATOM   1144 C CB    . ALA A 1 158 ? 41.903  26.964  25.136  1.00 24.31 ?  150 ALA A CB    1 
ATOM   1145 N N     . ASN A 1 159 ? 38.818  28.242  25.020  1.00 25.30 ?  151 ASN A N     1 
ATOM   1146 C CA    . ASN A 1 159 ? 37.394  27.963  24.840  1.00 24.29 ?  151 ASN A CA    1 
ATOM   1147 C C     . ASN A 1 159 ? 36.878  28.552  23.532  1.00 25.09 ?  151 ASN A C     1 
ATOM   1148 O O     . ASN A 1 159 ? 36.397  27.785  22.682  1.00 23.16 ?  151 ASN A O     1 
ATOM   1149 C CB    . ASN A 1 159 ? 36.635  28.446  26.085  1.00 24.41 ?  151 ASN A CB    1 
ATOM   1150 C CG    . ASN A 1 159 ? 35.122  28.299  25.970  1.00 22.91 ?  151 ASN A CG    1 
ATOM   1151 O OD1   . ASN A 1 159 ? 34.573  27.998  24.911  1.00 21.99 ?  151 ASN A OD1   1 
ATOM   1152 N ND2   . ASN A 1 159 ? 34.440  28.518  27.086  1.00 21.51 ?  151 ASN A ND2   1 
ATOM   1153 N N     . PRO A 1 160 ? 36.949  29.869  23.286  1.00 24.53 ?  152 PRO A N     1 
ATOM   1154 C CA    . PRO A 1 160 ? 36.491  30.369  21.981  1.00 24.88 ?  152 PRO A CA    1 
ATOM   1155 C C     . PRO A 1 160 ? 37.457  30.067  20.849  1.00 28.31 ?  152 PRO A C     1 
ATOM   1156 O O     . PRO A 1 160 ? 37.041  30.092  19.684  1.00 23.42 ?  152 PRO A O     1 
ATOM   1157 C CB    . PRO A 1 160 ? 36.352  31.879  22.210  1.00 25.69 ?  152 PRO A CB    1 
ATOM   1158 C CG    . PRO A 1 160 ? 37.356  32.182  23.243  1.00 26.00 ?  152 PRO A CG    1 
ATOM   1159 C CD    . PRO A 1 160 ? 37.415  30.974  24.145  1.00 27.18 ?  152 PRO A CD    1 
ATOM   1160 N N     . GLU A 1 161 ? 38.724  29.770  21.154  1.00 23.13 ?  153 GLU A N     1 
ATOM   1161 C CA    . GLU A 1 161 ? 39.703  29.509  20.102  1.00 26.64 ?  153 GLU A CA    1 
ATOM   1162 C C     . GLU A 1 161 ? 39.438  28.176  19.412  1.00 22.69 ?  153 GLU A C     1 
ATOM   1163 O O     . GLU A 1 161 ? 39.568  28.071  18.187  1.00 24.30 ?  153 GLU A O     1 
ATOM   1164 C CB    . GLU A 1 161 ? 41.119  29.545  20.680  1.00 27.35 ?  153 GLU A CB    1 
ATOM   1165 C CG    . GLU A 1 161 ? 42.212  29.125  19.704  1.00 30.69 ?  153 GLU A CG    1 
ATOM   1166 C CD    . GLU A 1 161 ? 43.576  29.000  20.360  1.00 38.79 ?  153 GLU A CD    1 
ATOM   1167 O OE1   . GLU A 1 161 ? 43.770  28.069  21.171  1.00 43.42 ?  153 GLU A OE1   1 
ATOM   1168 O OE2   . GLU A 1 161 ? 44.458  29.833  20.061  1.00 43.15 ?  153 GLU A OE2   1 
ATOM   1169 N N     . VAL A 1 162 ? 39.064  27.147  20.177  1.00 21.29 ?  154 VAL A N     1 
ATOM   1170 C CA    . VAL A 1 162 ? 38.791  25.850  19.565  1.00 25.53 ?  154 VAL A CA    1 
ATOM   1171 C C     . VAL A 1 162 ? 37.590  25.935  18.628  1.00 23.41 ?  154 VAL A C     1 
ATOM   1172 O O     . VAL A 1 162 ? 37.523  25.209  17.629  1.00 27.23 ?  154 VAL A O     1 
ATOM   1173 C CB    . VAL A 1 162 ? 38.600  24.770  20.647  1.00 26.48 ?  154 VAL A CB    1 
ATOM   1174 C CG1   . VAL A 1 162 ? 37.310  24.988  21.425  1.00 25.27 ?  154 VAL A CG1   1 
ATOM   1175 C CG2   . VAL A 1 162 ? 38.634  23.378  20.030  1.00 28.42 ?  154 VAL A CG2   1 
ATOM   1176 N N     . HIS A 1 163 ? 36.633  26.819  18.917  1.00 20.57 ?  155 HIS A N     1 
ATOM   1177 C CA    . HIS A 1 163 ? 35.542  27.040  17.973  1.00 23.11 ?  155 HIS A CA    1 
ATOM   1178 C C     . HIS A 1 163 ? 36.030  27.819  16.762  1.00 21.18 ?  155 HIS A C     1 
ATOM   1179 O O     . HIS A 1 163 ? 35.565  27.594  15.638  1.00 26.88 ?  155 HIS A O     1 
ATOM   1180 C CB    . HIS A 1 163 ? 34.389  27.773  18.658  1.00 22.24 ?  155 HIS A CB    1 
ATOM   1181 C CG    . HIS A 1 163 ? 33.711  26.966  19.719  1.00 21.31 ?  155 HIS A CG    1 
ATOM   1182 N ND1   . HIS A 1 163 ? 32.968  25.840  19.438  1.00 21.71 ?  155 HIS A ND1   1 
ATOM   1183 C CD2   . HIS A 1 163 ? 33.678  27.113  21.065  1.00 21.94 ?  155 HIS A CD2   1 
ATOM   1184 C CE1   . HIS A 1 163 ? 32.500  25.332  20.565  1.00 23.67 ?  155 HIS A CE1   1 
ATOM   1185 N NE2   . HIS A 1 163 ? 32.916  26.086  21.566  1.00 20.64 ?  155 HIS A NE2   1 
ATOM   1186 N N     . GLU A 1 164 ? 36.974  28.735  16.974  1.00 21.20 ?  156 GLU A N     1 
ATOM   1187 C CA    . GLU A 1 164 ? 37.580  29.455  15.863  1.00 22.68 ?  156 GLU A CA    1 
ATOM   1188 C C     . GLU A 1 164 ? 38.429  28.534  14.995  1.00 23.83 ?  156 GLU A C     1 
ATOM   1189 O O     . GLU A 1 164 ? 38.579  28.781  13.793  1.00 24.87 ?  156 GLU A O     1 
ATOM   1190 C CB    . GLU A 1 164 ? 38.411  30.618  16.406  1.00 24.65 ?  156 GLU A CB    1 
ATOM   1191 C CG    . GLU A 1 164 ? 39.267  31.340  15.386  1.00 26.68 ?  156 GLU A CG    1 
ATOM   1192 C CD    . GLU A 1 164 ? 40.170  32.374  16.028  1.00 33.53 ?  156 GLU A CD    1 
ATOM   1193 O OE1   . GLU A 1 164 ? 39.959  32.690  17.219  1.00 33.02 ?  156 GLU A OE1   1 
ATOM   1194 O OE2   . GLU A 1 164 ? 41.089  32.871  15.345  1.00 37.64 ?  156 GLU A OE2   1 
ATOM   1195 N N     . LEU A 1 165 ? 38.974  27.463  15.572  1.00 22.39 ?  157 LEU A N     1 
ATOM   1196 C CA    . LEU A 1 165 ? 39.850  26.569  14.824  1.00 24.16 ?  157 LEU A CA    1 
ATOM   1197 C C     . LEU A 1 165 ? 39.130  25.360  14.244  1.00 28.05 ?  157 LEU A C     1 
ATOM   1198 O O     . LEU A 1 165 ? 39.562  24.833  13.212  1.00 24.15 ?  157 LEU A O     1 
ATOM   1199 C CB    . LEU A 1 165 ? 40.998  26.084  15.714  1.00 26.59 ?  157 LEU A CB    1 
ATOM   1200 C CG    . LEU A 1 165 ? 42.005  27.121  16.203  1.00 29.52 ?  157 LEU A CG    1 
ATOM   1201 C CD1   . LEU A 1 165 ? 43.032  26.452  17.097  1.00 29.25 ?  157 LEU A CD1   1 
ATOM   1202 C CD2   . LEU A 1 165 ? 42.678  27.800  15.024  1.00 30.93 ?  157 LEU A CD2   1 
ATOM   1203 N N     . THR A 1 166 ? 38.048  24.902  14.878  1.00 23.81 ?  158 THR A N     1 
ATOM   1204 C CA    . THR A 1 166 ? 37.379  23.668  14.474  1.00 23.08 ?  158 THR A CA    1 
ATOM   1205 C C     . THR A 1 166 ? 35.909  23.883  14.136  1.00 26.06 ?  158 THR A C     1 
ATOM   1206 O O     . THR A 1 166 ? 35.512  23.642  12.992  1.00 24.25 ?  158 THR A O     1 
ATOM   1207 C CB    . THR A 1 166 ? 37.526  22.599  15.569  1.00 28.44 ?  158 THR A CB    1 
ATOM   1208 O OG1   . THR A 1 166 ? 36.980  23.085  16.803  1.00 30.29 ?  158 THR A OG1   1 
ATOM   1209 C CG2   . THR A 1 166 ? 38.991  22.239  15.774  1.00 27.36 ?  158 THR A CG2   1 
ATOM   1210 N N     . THR A 1 167 ? 35.086  24.328  15.092  1.00 25.28 ?  159 THR A N     1 
ATOM   1211 C CA    . THR A 1 167 ? 33.647  24.433  14.849  1.00 26.11 ?  159 THR A CA    1 
ATOM   1212 C C     . THR A 1 167 ? 33.350  25.357  13.675  1.00 25.61 ?  159 THR A C     1 
ATOM   1213 O O     . THR A 1 167 ? 32.560  25.016  12.787  1.00 25.52 ?  159 THR A O     1 
ATOM   1214 C CB    . THR A 1 167 ? 32.927  24.929  16.105  1.00 24.77 ?  159 THR A CB    1 
ATOM   1215 O OG1   . THR A 1 167 ? 33.525  24.351  17.272  1.00 25.22 ?  159 THR A OG1   1 
ATOM   1216 C CG2   . THR A 1 167 ? 31.448  24.546  16.057  1.00 21.52 ?  159 THR A CG2   1 
ATOM   1217 N N     . GLY A 1 168 ? 33.976  26.531  13.655  1.00 26.81 ?  160 GLY A N     1 
ATOM   1218 C CA    . GLY A 1 168 ? 33.791  27.489  12.590  1.00 22.78 ?  160 GLY A CA    1 
ATOM   1219 C C     . GLY A 1 168 ? 34.209  26.966  11.229  1.00 27.00 ?  160 GLY A C     1 
ATOM   1220 O O     . GLY A 1 168 ? 33.403  26.906  10.295  1.00 29.01 ?  160 GLY A O     1 
ATOM   1221 N N     . PRO A 1 169 ? 35.486  26.589  11.085  1.00 29.28 ?  161 PRO A N     1 
ATOM   1222 C CA    . PRO A 1 169 ? 35.940  26.056  9.788   1.00 27.08 ?  161 PRO A CA    1 
ATOM   1223 C C     . PRO A 1 169 ? 35.147  24.851  9.312   1.00 28.23 ?  161 PRO A C     1 
ATOM   1224 O O     . PRO A 1 169 ? 34.968  24.680  8.100   1.00 27.83 ?  161 PRO A O     1 
ATOM   1225 C CB    . PRO A 1 169 ? 37.408  25.704  10.053  1.00 26.74 ?  161 PRO A CB    1 
ATOM   1226 C CG    . PRO A 1 169 ? 37.820  26.610  11.149  1.00 24.33 ?  161 PRO A CG    1 
ATOM   1227 C CD    . PRO A 1 169 ? 36.609  26.817  12.013  1.00 26.35 ?  161 PRO A CD    1 
ATOM   1228 N N     . GLU A 1 170 ? 34.676  24.002  10.229  1.00 28.54 ?  162 GLU A N     1 
ATOM   1229 C CA    . GLU A 1 170 ? 33.785  22.915  9.836   1.00 31.26 ?  162 GLU A CA    1 
ATOM   1230 C C     . GLU A 1 170 ? 32.556  23.456  9.120   1.00 30.26 ?  162 GLU A C     1 
ATOM   1231 O O     . GLU A 1 170 ? 32.160  22.948  8.065   1.00 32.80 ?  162 GLU A O     1 
ATOM   1232 C CB    . GLU A 1 170 ? 33.368  22.100  11.061  1.00 26.38 ?  162 GLU A CB    1 
ATOM   1233 C CG    . GLU A 1 170 ? 34.407  21.119  11.551  1.00 33.62 ?  162 GLU A CG    1 
ATOM   1234 C CD    . GLU A 1 170 ? 34.076  20.581  12.926  1.00 28.96 ?  162 GLU A CD    1 
ATOM   1235 O OE1   . GLU A 1 170 ? 32.874  20.451  13.242  1.00 30.62 ?  162 GLU A OE1   1 
ATOM   1236 O OE2   . GLU A 1 170 ? 35.016  20.291  13.692  1.00 27.12 ?  162 GLU A OE2   1 
ATOM   1237 N N     . LEU A 1 171 ? 31.945  24.503  9.679   1.00 30.18 ?  163 LEU A N     1 
ATOM   1238 C CA    . LEU A 1 171 ? 30.760  25.089  9.061   1.00 30.21 ?  163 LEU A CA    1 
ATOM   1239 C C     . LEU A 1 171 ? 31.098  25.758  7.734   1.00 31.15 ?  163 LEU A C     1 
ATOM   1240 O O     . LEU A 1 171 ? 30.302  25.706  6.789   1.00 32.52 ?  163 LEU A O     1 
ATOM   1241 C CB    . LEU A 1 171 ? 30.115  26.090  10.018  1.00 27.49 ?  163 LEU A CB    1 
ATOM   1242 C CG    . LEU A 1 171 ? 29.237  25.494  11.119  1.00 26.78 ?  163 LEU A CG    1 
ATOM   1243 C CD1   . LEU A 1 171 ? 28.903  26.543  12.169  1.00 26.81 ?  163 LEU A CD1   1 
ATOM   1244 C CD2   . LEU A 1 171 ? 27.969  24.904  10.524  1.00 29.90 ?  163 LEU A CD2   1 
ATOM   1245 N N     . LEU A 1 172 ? 32.267  26.400  7.648   1.00 29.82 ?  164 LEU A N     1 
ATOM   1246 C CA    . LEU A 1 172 ? 32.698  27.004  6.390   1.00 30.37 ?  164 LEU A CA    1 
ATOM   1247 C C     . LEU A 1 172 ? 32.731  25.972  5.272   1.00 36.48 ?  164 LEU A C     1 
ATOM   1248 O O     . LEU A 1 172 ? 32.195  26.196  4.181   1.00 33.00 ?  164 LEU A O     1 
ATOM   1249 C CB    . LEU A 1 172 ? 34.077  27.645  6.554   1.00 34.40 ?  164 LEU A CB    1 
ATOM   1250 C CG    . LEU A 1 172 ? 34.168  29.008  7.232   1.00 35.54 ?  164 LEU A CG    1 
ATOM   1251 C CD1   . LEU A 1 172 ? 35.539  29.612  6.978   1.00 36.20 ?  164 LEU A CD1   1 
ATOM   1252 C CD2   . LEU A 1 172 ? 33.072  29.925  6.724   1.00 34.94 ?  164 LEU A CD2   1 
ATOM   1253 N N     . GLN A 1 173 ? 33.359  24.826  5.534   1.00 34.36 ?  165 GLN A N     1 
ATOM   1254 C CA    . GLN A 1 173 ? 33.429  23.780  4.525   1.00 36.23 ?  165 GLN A CA    1 
ATOM   1255 C C     . GLN A 1 173 ? 32.094  23.058  4.371   1.00 34.15 ?  165 GLN A C     1 
ATOM   1256 O O     . GLN A 1 173 ? 31.786  22.560  3.283   1.00 36.82 ?  165 GLN A O     1 
ATOM   1257 C CB    . GLN A 1 173 ? 34.547  22.796  4.873   1.00 38.78 ?  165 GLN A CB    1 
ATOM   1258 C CG    . GLN A 1 173 ? 34.093  21.639  5.730   1.00 48.18 ?  165 GLN A CG    1 
ATOM   1259 C CD    . GLN A 1 173 ? 35.079  20.498  5.746   1.00 57.81 ?  165 GLN A CD    1 
ATOM   1260 O OE1   . GLN A 1 173 ? 36.293  20.700  5.709   1.00 64.45 ?  165 GLN A OE1   1 
ATOM   1261 N NE2   . GLN A 1 173 ? 34.555  19.281  5.753   1.00 62.33 ?  165 GLN A NE2   1 
ATOM   1262 N N     . GLN A 1 174 ? 31.283  23.000  5.433   1.00 33.70 ?  166 GLN A N     1 
ATOM   1263 C CA    . GLN A 1 174 ? 29.967  22.383  5.315   1.00 33.89 ?  166 GLN A CA    1 
ATOM   1264 C C     . GLN A 1 174 ? 29.020  23.227  4.475   1.00 29.62 ?  166 GLN A C     1 
ATOM   1265 O O     . GLN A 1 174 ? 28.064  22.689  3.909   1.00 32.32 ?  166 GLN A O     1 
ATOM   1266 C CB    . GLN A 1 174 ? 29.364  22.136  6.700   1.00 28.03 ?  166 GLN A CB    1 
ATOM   1267 C CG    . GLN A 1 174 ? 29.848  20.856  7.374   1.00 32.84 ?  166 GLN A CG    1 
ATOM   1268 C CD    . GLN A 1 174 ? 29.490  20.794  8.849   1.00 27.66 ?  166 GLN A CD    1 
ATOM   1269 O OE1   . GLN A 1 174 ? 29.681  21.759  9.588   1.00 26.67 ?  166 GLN A OE1   1 
ATOM   1270 N NE2   . GLN A 1 174 ? 28.972  19.651  9.285   1.00 30.36 ?  166 GLN A NE2   1 
ATOM   1271 N N     . PHE A 1 175 ? 29.270  24.527  4.374   1.00 32.84 ?  167 PHE A N     1 
ATOM   1272 C CA    . PHE A 1 175 ? 28.462  25.436  3.573   1.00 33.77 ?  167 PHE A CA    1 
ATOM   1273 C C     . PHE A 1 175 ? 29.298  26.061  2.466   1.00 36.56 ?  167 PHE A C     1 
ATOM   1274 O O     . PHE A 1 175 ? 29.147  27.237  2.131   1.00 34.97 ?  167 PHE A O     1 
ATOM   1275 C CB    . PHE A 1 175 ? 27.817  26.502  4.454   1.00 32.12 ?  167 PHE A CB    1 
ATOM   1276 C CG    . PHE A 1 175 ? 26.683  25.982  5.289   1.00 35.78 ?  167 PHE A CG    1 
ATOM   1277 C CD1   . PHE A 1 175 ? 26.924  25.415  6.531   1.00 34.81 ?  167 PHE A CD1   1 
ATOM   1278 C CD2   . PHE A 1 175 ? 25.380  26.039  4.825   1.00 36.06 ?  167 PHE A CD2   1 
ATOM   1279 C CE1   . PHE A 1 175 ? 25.881  24.923  7.301   1.00 34.17 ?  167 PHE A CE1   1 
ATOM   1280 C CE2   . PHE A 1 175 ? 24.333  25.551  5.589   1.00 35.32 ?  167 PHE A CE2   1 
ATOM   1281 C CZ    . PHE A 1 175 ? 24.584  24.990  6.828   1.00 39.64 ?  167 PHE A CZ    1 
ATOM   1282 N N     . GLU A 1 176 ? 30.201  25.264  1.898   1.00 42.24 ?  168 GLU A N     1 
ATOM   1283 C CA    . GLU A 1 176 ? 31.021  25.710  0.780   1.00 41.50 ?  168 GLU A CA    1 
ATOM   1284 C C     . GLU A 1 176 ? 30.142  26.041  -0.418  1.00 44.46 ?  168 GLU A C     1 
ATOM   1285 O O     . GLU A 1 176 ? 29.273  25.253  -0.804  1.00 42.38 ?  168 GLU A O     1 
ATOM   1286 C CB    . GLU A 1 176 ? 32.035  24.627  0.408   1.00 44.60 ?  168 GLU A CB    1 
ATOM   1287 C CG    . GLU A 1 176 ? 33.141  25.095  -0.522  1.00 53.68 ?  168 GLU A CG    1 
ATOM   1288 C CD    . GLU A 1 176 ? 34.429  25.406  0.212   1.00 63.15 ?  168 GLU A CD    1 
ATOM   1289 O OE1   . GLU A 1 176 ? 35.213  24.463  0.452   1.00 65.64 ?  168 GLU A OE1   1 
ATOM   1290 O OE2   . GLU A 1 176 ? 34.664  26.587  0.545   1.00 66.54 ?  168 GLU A OE2   1 
ATOM   1291 N N     . GLY A 1 177 ? 30.362  27.216  -1.001  1.00 42.22 ?  169 GLY A N     1 
ATOM   1292 C CA    . GLY A 1 177 ? 29.562  27.661  -2.122  1.00 44.30 ?  169 GLY A CA    1 
ATOM   1293 C C     . GLY A 1 177 ? 28.152  28.086  -1.781  1.00 46.64 ?  169 GLY A C     1 
ATOM   1294 O O     . GLY A 1 177 ? 27.391  28.432  -2.693  1.00 47.68 ?  169 GLY A O     1 
ATOM   1295 N N     . LYS A 1 178 ? 27.773  28.069  -0.507  1.00 45.20 ?  170 LYS A N     1 
ATOM   1296 C CA    . LYS A 1 178 ? 26.457  28.499  -0.063  1.00 38.98 ?  170 LYS A CA    1 
ATOM   1297 C C     . LYS A 1 178 ? 26.614  29.653  0.916   1.00 42.16 ?  170 LYS A C     1 
ATOM   1298 O O     . LYS A 1 178 ? 27.501  29.633  1.775   1.00 46.03 ?  170 LYS A O     1 
ATOM   1299 C CB    . LYS A 1 178 ? 25.691  27.348  0.595   1.00 42.66 ?  170 LYS A CB    1 
ATOM   1300 C CG    . LYS A 1 178 ? 24.181  27.484  0.531   1.00 46.24 ?  170 LYS A CG    1 
ATOM   1301 C CD    . LYS A 1 178 ? 23.518  26.720  1.666   1.00 50.97 ?  170 LYS A CD    1 
ATOM   1302 C CE    . LYS A 1 178 ? 23.106  25.322  1.232   1.00 49.28 ?  170 LYS A CE    1 
ATOM   1303 N NZ    . LYS A 1 178 ? 22.098  25.345  0.137   1.00 45.16 ?  170 LYS A NZ    1 
ATOM   1304 N N     . THR A 1 179 ? 25.756  30.660  0.782   1.00 42.28 ?  171 THR A N     1 
ATOM   1305 C CA    . THR A 1 179 ? 25.835  31.854  1.614   1.00 39.84 ?  171 THR A CA    1 
ATOM   1306 C C     . THR A 1 179 ? 25.017  31.655  2.883   1.00 40.13 ?  171 THR A C     1 
ATOM   1307 O O     . THR A 1 179 ? 23.806  31.418  2.816   1.00 38.37 ?  171 THR A O     1 
ATOM   1308 C CB    . THR A 1 179 ? 25.344  33.087  0.855   1.00 37.68 ?  171 THR A CB    1 
ATOM   1309 O OG1   . THR A 1 179 ? 24.247  32.724  0.007   1.00 56.06 ?  171 THR A OG1   1 
ATOM   1310 C CG2   . THR A 1 179 ? 26.464  33.677  0.014   1.00 40.93 ?  171 THR A CG2   1 
ATOM   1311 N N     . ILE A 1 180 ? 25.679  31.749  4.031   1.00 39.05 ?  172 ILE A N     1 
ATOM   1312 C CA    . ILE A 1 180 ? 25.001  31.755  5.321   1.00 32.77 ?  172 ILE A CA    1 
ATOM   1313 C C     . ILE A 1 180 ? 24.619  33.193  5.639   1.00 28.76 ?  172 ILE A C     1 
ATOM   1314 O O     . ILE A 1 180 ? 25.487  34.067  5.741   1.00 32.86 ?  172 ILE A O     1 
ATOM   1315 C CB    . ILE A 1 180 ? 25.887  31.162  6.427   1.00 31.19 ?  172 ILE A CB    1 
ATOM   1316 C CG1   . ILE A 1 180 ? 26.405  29.782  6.023   1.00 30.61 ?  172 ILE A CG1   1 
ATOM   1317 C CG2   . ILE A 1 180 ? 25.114  31.080  7.733   1.00 28.29 ?  172 ILE A CG2   1 
ATOM   1318 C CD1   . ILE A 1 180 ? 27.230  29.111  7.098   1.00 30.26 ?  172 ILE A CD1   1 
ATOM   1319 N N     . ASP A 1 181 ? 23.321  33.440  5.791   1.00 30.07 ?  173 ASP A N     1 
ATOM   1320 C CA    . ASP A 1 181 ? 22.829  34.792  6.009   1.00 29.13 ?  173 ASP A CA    1 
ATOM   1321 C C     . ASP A 1 181 ? 22.784  35.175  7.482   1.00 29.43 ?  173 ASP A C     1 
ATOM   1322 O O     . ASP A 1 181 ? 22.864  36.366  7.805   1.00 29.84 ?  173 ASP A O     1 
ATOM   1323 C CB    . ASP A 1 181 ? 21.440  34.944  5.385   1.00 31.75 ?  173 ASP A CB    1 
ATOM   1324 C CG    . ASP A 1 181 ? 21.443  34.662  3.895   1.00 37.48 ?  173 ASP A CG    1 
ATOM   1325 O OD1   . ASP A 1 181 ? 21.931  35.515  3.123   1.00 39.92 ?  173 ASP A OD1   1 
ATOM   1326 O OD2   . ASP A 1 181 ? 20.974  33.577  3.494   1.00 37.49 ?  173 ASP A OD2   1 
ATOM   1327 N N     . ALA A 1 182 ? 22.671  34.198  8.379   1.00 29.50 ?  174 ALA A N     1 
ATOM   1328 C CA    . ALA A 1 182 ? 22.648  34.468  9.809   1.00 27.81 ?  174 ALA A CA    1 
ATOM   1329 C C     . ALA A 1 182 ? 23.096  33.227  10.564  1.00 28.28 ?  174 ALA A C     1 
ATOM   1330 O O     . ALA A 1 182 ? 22.675  32.112  10.247  1.00 28.56 ?  174 ALA A O     1 
ATOM   1331 C CB    . ALA A 1 182 ? 21.252  34.891  10.283  1.00 22.83 ?  174 ALA A CB    1 
ATOM   1332 N N     . PHE A 1 183 ? 23.958  33.431  11.557  1.00 26.82 ?  175 PHE A N     1 
ATOM   1333 C CA    . PHE A 1 183 ? 24.324  32.390  12.506  1.00 25.79 ?  175 PHE A CA    1 
ATOM   1334 C C     . PHE A 1 183 ? 23.865  32.811  13.893  1.00 26.64 ?  175 PHE A C     1 
ATOM   1335 O O     . PHE A 1 183 ? 24.097  33.951  14.311  1.00 25.47 ?  175 PHE A O     1 
ATOM   1336 C CB    . PHE A 1 183 ? 25.830  32.119  12.505  1.00 25.80 ?  175 PHE A CB    1 
ATOM   1337 C CG    . PHE A 1 183 ? 26.253  31.104  13.528  1.00 26.86 ?  175 PHE A CG    1 
ATOM   1338 C CD1   . PHE A 1 183 ? 26.115  29.750  13.273  1.00 24.38 ?  175 PHE A CD1   1 
ATOM   1339 C CD2   . PHE A 1 183 ? 26.771  31.503  14.749  1.00 24.63 ?  175 PHE A CD2   1 
ATOM   1340 C CE1   . PHE A 1 183 ? 26.491  28.812  14.214  1.00 28.06 ?  175 PHE A CE1   1 
ATOM   1341 C CE2   . PHE A 1 183 ? 27.150  30.569  15.695  1.00 27.89 ?  175 PHE A CE2   1 
ATOM   1342 C CZ    . PHE A 1 183 ? 27.009  29.222  15.427  1.00 26.09 ?  175 PHE A CZ    1 
ATOM   1343 N N     . LEU A 1 184 ? 23.215  31.891  14.600  1.00 26.28 ?  176 LEU A N     1 
ATOM   1344 C CA    . LEU A 1 184 ? 22.661  32.147  15.920  1.00 29.48 ?  176 LEU A CA    1 
ATOM   1345 C C     . LEU A 1 184 ? 23.140  31.063  16.872  1.00 27.70 ?  176 LEU A C     1 
ATOM   1346 O O     . LEU A 1 184 ? 23.215  29.889  16.497  1.00 29.60 ?  176 LEU A O     1 
ATOM   1347 C CB    . LEU A 1 184 ? 21.123  32.181  15.888  1.00 28.88 ?  176 LEU A CB    1 
ATOM   1348 C CG    . LEU A 1 184 ? 20.427  33.047  14.829  1.00 33.17 ?  176 LEU A CG    1 
ATOM   1349 C CD1   . LEU A 1 184 ? 20.271  32.305  13.514  1.00 29.51 ?  176 LEU A CD1   1 
ATOM   1350 C CD2   . LEU A 1 184 ? 19.068  33.523  15.327  1.00 26.24 ?  176 LEU A CD2   1 
ATOM   1351 N N     . ALA A 1 185 ? 23.466  31.455  18.101  1.00 24.25 ?  177 ALA A N     1 
ATOM   1352 C CA    . ALA A 1 185 ? 23.950  30.505  19.091  1.00 23.39 ?  177 ALA A CA    1 
ATOM   1353 C C     . ALA A 1 185 ? 23.631  31.013  20.488  1.00 28.46 ?  177 ALA A C     1 
ATOM   1354 O O     . ALA A 1 185 ? 23.807  32.199  20.780  1.00 26.57 ?  177 ALA A O     1 
ATOM   1355 C CB    . ALA A 1 185 ? 25.459  30.271  18.949  1.00 20.08 ?  177 ALA A CB    1 
ATOM   1356 N N     . GLY A 1 186 ? 23.156  30.111  21.343  1.00 28.59 ?  178 GLY A N     1 
ATOM   1357 C CA    . GLY A 1 186 ? 22.996  30.447  22.743  1.00 21.63 ?  178 GLY A CA    1 
ATOM   1358 C C     . GLY A 1 186 ? 24.335  30.706  23.405  1.00 28.42 ?  178 GLY A C     1 
ATOM   1359 O O     . GLY A 1 186 ? 25.360  30.127  23.045  1.00 23.89 ?  178 GLY A O     1 
ATOM   1360 N N     . VAL A 1 187 ? 24.326  31.598  24.390  1.00 24.51 ?  179 VAL A N     1 
ATOM   1361 C CA    . VAL A 1 187 ? 25.545  32.045  25.055  1.00 25.56 ?  179 VAL A CA    1 
ATOM   1362 C C     . VAL A 1 187 ? 25.552  31.486  26.471  1.00 22.55 ?  179 VAL A C     1 
ATOM   1363 O O     . VAL A 1 187 ? 24.750  31.896  27.319  1.00 23.26 ?  179 VAL A O     1 
ATOM   1364 C CB    . VAL A 1 187 ? 25.664  33.575  25.065  1.00 25.59 ?  179 VAL A CB    1 
ATOM   1365 C CG1   . VAL A 1 187 ? 26.790  34.010  25.993  1.00 23.53 ?  179 VAL A CG1   1 
ATOM   1366 C CG2   . VAL A 1 187 ? 25.900  34.096  23.657  1.00 21.09 ?  179 VAL A CG2   1 
ATOM   1367 N N     . GLY A 1 188 ? 26.457  30.546  26.725  1.00 23.55 ?  180 GLY A N     1 
ATOM   1368 C CA    . GLY A 1 188 ? 26.742  30.109  28.076  1.00 22.88 ?  180 GLY A CA    1 
ATOM   1369 C C     . GLY A 1 188 ? 28.054  30.712  28.525  1.00 24.86 ?  180 GLY A C     1 
ATOM   1370 O O     . GLY A 1 188 ? 28.074  31.700  29.264  1.00 25.69 ?  180 GLY A O     1 
ATOM   1371 N N     . THR A 1 189 ? 29.165  30.131  28.071  1.00 23.65 ?  181 THR A N     1 
ATOM   1372 C CA    . THR A 1 189 ? 30.451  30.799  28.202  1.00 24.02 ?  181 THR A CA    1 
ATOM   1373 C C     . THR A 1 189 ? 30.668  31.832  27.106  1.00 26.04 ?  181 THR A C     1 
ATOM   1374 O O     . THR A 1 189 ? 31.477  32.748  27.285  1.00 27.39 ?  181 THR A O     1 
ATOM   1375 C CB    . THR A 1 189 ? 31.597  29.786  28.168  1.00 23.58 ?  181 THR A CB    1 
ATOM   1376 O OG1   . THR A 1 189 ? 31.701  29.226  26.854  1.00 22.45 ?  181 THR A OG1   1 
ATOM   1377 C CG2   . THR A 1 189 ? 31.353  28.665  29.166  1.00 27.18 ?  181 THR A CG2   1 
ATOM   1378 N N     . GLY A 1 190 ? 29.961  31.706  25.985  1.00 25.24 ?  182 GLY A N     1 
ATOM   1379 C CA    . GLY A 1 190 ? 30.158  32.570  24.844  1.00 25.45 ?  182 GLY A CA    1 
ATOM   1380 C C     . GLY A 1 190 ? 31.203  32.094  23.860  1.00 23.34 ?  182 GLY A C     1 
ATOM   1381 O O     . GLY A 1 190 ? 31.428  32.769  22.846  1.00 22.08 ?  182 GLY A O     1 
ATOM   1382 N N     . GLY A 1 191 ? 31.842  30.951  24.120  1.00 23.28 ?  183 GLY A N     1 
ATOM   1383 C CA    . GLY A 1 191 ? 32.916  30.500  23.250  1.00 22.74 ?  183 GLY A CA    1 
ATOM   1384 C C     . GLY A 1 191 ? 32.436  30.097  21.869  1.00 24.67 ?  183 GLY A C     1 
ATOM   1385 O O     . GLY A 1 191 ? 33.105  30.368  20.868  1.00 21.62 ?  183 GLY A O     1 
ATOM   1386 N N     . THR A 1 192 ? 31.274  29.444  21.792  1.00 25.86 ?  184 THR A N     1 
ATOM   1387 C CA    . THR A 1 192 ? 30.755  29.005  20.500  1.00 23.11 ?  184 THR A CA    1 
ATOM   1388 C C     . THR A 1 192 ? 30.409  30.195  19.614  1.00 24.44 ?  184 THR A C     1 
ATOM   1389 O O     . THR A 1 192 ? 30.835  30.266  18.456  1.00 23.68 ?  184 THR A O     1 
ATOM   1390 C CB    . THR A 1 192 ? 29.526  28.116  20.696  1.00 26.24 ?  184 THR A CB    1 
ATOM   1391 O OG1   . THR A 1 192 ? 29.862  27.008  21.541  1.00 22.95 ?  184 THR A OG1   1 
ATOM   1392 C CG2   . THR A 1 192 ? 29.025  27.602  19.353  1.00 20.77 ?  184 THR A CG2   1 
ATOM   1393 N N     . LEU A 1 193 ? 29.632  31.141  20.144  1.00 29.03 ?  185 LEU A N     1 
ATOM   1394 C CA    . LEU A 1 193 ? 29.236  32.301  19.352  1.00 26.56 ?  185 LEU A CA    1 
ATOM   1395 C C     . LEU A 1 193 ? 30.444  33.130  18.933  1.00 25.82 ?  185 LEU A C     1 
ATOM   1396 O O     . LEU A 1 193 ? 30.509  33.615  17.797  1.00 27.00 ?  185 LEU A O     1 
ATOM   1397 C CB    . LEU A 1 193 ? 28.250  33.160  20.140  1.00 25.15 ?  185 LEU A CB    1 
ATOM   1398 C CG    . LEU A 1 193 ? 27.633  34.315  19.350  1.00 26.68 ?  185 LEU A CG    1 
ATOM   1399 C CD1   . LEU A 1 193 ? 26.584  33.810  18.363  1.00 25.90 ?  185 LEU A CD1   1 
ATOM   1400 C CD2   . LEU A 1 193 ? 27.051  35.351  20.294  1.00 24.33 ?  185 LEU A CD2   1 
ATOM   1401 N N     . SER A 1 194 ? 31.412  33.303  19.836  1.00 28.64 ?  186 SER A N     1 
ATOM   1402 C CA    . SER A 1 194 ? 32.574  34.133  19.531  1.00 27.39 ?  186 SER A CA    1 
ATOM   1403 C C     . SER A 1 194 ? 33.470  33.470  18.494  1.00 23.13 ?  186 SER A C     1 
ATOM   1404 O O     . SER A 1 194 ? 33.838  34.090  17.489  1.00 26.35 ?  186 SER A O     1 
ATOM   1405 C CB    . SER A 1 194 ? 33.359  34.425  20.811  1.00 27.14 ?  186 SER A CB    1 
ATOM   1406 O OG    . SER A 1 194 ? 32.592  35.194  21.721  1.00 27.70 ?  186 SER A OG    1 
ATOM   1407 N N     . GLY A 1 195 ? 33.830  32.206  18.721  1.00 28.16 ?  187 GLY A N     1 
ATOM   1408 C CA    . GLY A 1 195 ? 34.740  31.531  17.809  1.00 22.84 ?  187 GLY A CA    1 
ATOM   1409 C C     . GLY A 1 195 ? 34.133  31.303  16.437  1.00 26.94 ?  187 GLY A C     1 
ATOM   1410 O O     . GLY A 1 195 ? 34.765  31.574  15.413  1.00 22.86 ?  187 GLY A O     1 
ATOM   1411 N N     . VAL A 1 196 ? 32.898  30.799  16.397  1.00 24.54 ?  188 VAL A N     1 
ATOM   1412 C CA    . VAL A 1 196 ? 32.244  30.566  15.114  1.00 26.02 ?  188 VAL A CA    1 
ATOM   1413 C C     . VAL A 1 196 ? 31.907  31.889  14.440  1.00 27.02 ?  188 VAL A C     1 
ATOM   1414 O O     . VAL A 1 196 ? 32.077  32.043  13.224  1.00 29.45 ?  188 VAL A O     1 
ATOM   1415 C CB    . VAL A 1 196 ? 30.990  29.690  15.295  1.00 24.43 ?  188 VAL A CB    1 
ATOM   1416 C CG1   . VAL A 1 196 ? 30.238  29.563  13.978  1.00 26.11 ?  188 VAL A CG1   1 
ATOM   1417 C CG2   . VAL A 1 196 ? 31.369  28.319  15.832  1.00 20.29 ?  188 VAL A CG2   1 
ATOM   1418 N N     . GLY A 1 197 ? 31.439  32.868  15.218  1.00 26.48 ?  189 GLY A N     1 
ATOM   1419 C CA    . GLY A 1 197 ? 31.050  34.145  14.637  1.00 28.89 ?  189 GLY A CA    1 
ATOM   1420 C C     . GLY A 1 197 ? 32.204  34.873  13.976  1.00 30.68 ?  189 GLY A C     1 
ATOM   1421 O O     . GLY A 1 197 ? 32.047  35.456  12.900  1.00 30.56 ?  189 GLY A O     1 
ATOM   1422 N N     . LYS A 1 198 ? 33.378  34.857  14.612  1.00 29.67 ?  190 LYS A N     1 
ATOM   1423 C CA    . LYS A 1 198 ? 34.554  35.481  14.013  1.00 29.40 ?  190 LYS A CA    1 
ATOM   1424 C C     . LYS A 1 198 ? 34.902  34.826  12.683  1.00 31.80 ?  190 LYS A C     1 
ATOM   1425 O O     . LYS A 1 198 ? 35.179  35.510  11.690  1.00 28.78 ?  190 LYS A O     1 
ATOM   1426 C CB    . LYS A 1 198 ? 35.741  35.399  14.973  1.00 32.84 ?  190 LYS A CB    1 
ATOM   1427 C CG    . LYS A 1 198 ? 37.080  35.667  14.302  1.00 31.44 ?  190 LYS A CG    1 
ATOM   1428 C CD    . LYS A 1 198 ? 38.253  35.260  15.179  1.00 32.67 ?  190 LYS A CD    1 
ATOM   1429 C CE    . LYS A 1 198 ? 38.303  36.063  16.468  1.00 29.65 ?  190 LYS A CE    1 
ATOM   1430 N NZ    . LYS A 1 198 ? 39.441  35.639  17.330  1.00 33.59 ?  190 LYS A NZ    1 
ATOM   1431 N N     . VAL A 1 199 ? 34.893  33.493  12.647  1.00 28.55 ?  191 VAL A N     1 
ATOM   1432 C CA    . VAL A 1 199 ? 35.267  32.774  11.434  1.00 30.95 ?  191 VAL A CA    1 
ATOM   1433 C C     . VAL A 1 199 ? 34.242  33.013  10.333  1.00 33.95 ?  191 VAL A C     1 
ATOM   1434 O O     . VAL A 1 199 ? 34.599  33.189  9.161   1.00 33.28 ?  191 VAL A O     1 
ATOM   1435 C CB    . VAL A 1 199 ? 35.436  31.276  11.745  1.00 33.24 ?  191 VAL A CB    1 
ATOM   1436 C CG1   . VAL A 1 199 ? 35.476  30.457  10.467  1.00 28.68 ?  191 VAL A CG1   1 
ATOM   1437 C CG2   . VAL A 1 199 ? 36.691  31.050  12.567  1.00 28.78 ?  191 VAL A CG2   1 
ATOM   1438 N N     . LEU A 1 200 ? 32.957  33.041  10.690  1.00 32.81 ?  192 LEU A N     1 
ATOM   1439 C CA    . LEU A 1 200 ? 31.918  33.203  9.678   1.00 31.23 ?  192 LEU A CA    1 
ATOM   1440 C C     . LEU A 1 200 ? 31.879  34.629  9.142   1.00 30.68 ?  192 LEU A C     1 
ATOM   1441 O O     . LEU A 1 200 ? 31.609  34.842  7.955   1.00 32.35 ?  192 LEU A O     1 
ATOM   1442 C CB    . LEU A 1 200 ? 30.558  32.808  10.254  1.00 26.54 ?  192 LEU A CB    1 
ATOM   1443 C CG    . LEU A 1 200 ? 30.347  31.337  10.630  1.00 33.05 ?  192 LEU A CG    1 
ATOM   1444 C CD1   . LEU A 1 200 ? 28.870  30.980  10.591  1.00 27.12 ?  192 LEU A CD1   1 
ATOM   1445 C CD2   . LEU A 1 200 ? 31.145  30.399  9.735   1.00 28.11 ?  192 LEU A CD2   1 
ATOM   1446 N N     . LYS A 1 201 ? 32.146  35.620  9.997   1.00 29.45 ?  193 LYS A N     1 
ATOM   1447 C CA    . LYS A 1 201 ? 32.111  37.010  9.550   1.00 35.67 ?  193 LYS A CA    1 
ATOM   1448 C C     . LYS A 1 201 ? 33.187  37.286  8.506   1.00 40.18 ?  193 LYS A C     1 
ATOM   1449 O O     . LYS A 1 201 ? 32.972  38.076  7.578   1.00 38.34 ?  193 LYS A O     1 
ATOM   1450 C CB    . LYS A 1 201 ? 32.270  37.953  10.743  1.00 31.54 ?  193 LYS A CB    1 
ATOM   1451 C CG    . LYS A 1 201 ? 30.954  38.423  11.340  1.00 39.59 ?  193 LYS A CG    1 
ATOM   1452 C CD    . LYS A 1 201 ? 31.185  39.427  12.458  1.00 40.81 ?  193 LYS A CD    1 
ATOM   1453 C CE    . LYS A 1 201 ? 30.423  40.719  12.208  1.00 46.48 ?  193 LYS A CE    1 
ATOM   1454 N NZ    . LYS A 1 201 ? 28.957  40.495  12.072  1.00 49.12 ?  193 LYS A NZ    1 
ATOM   1455 N N     . LYS A 1 202 ? 34.351  36.648  8.641   1.00 33.54 ?  194 LYS A N     1 
ATOM   1456 C CA    . LYS A 1 202 ? 35.421  36.848  7.669   1.00 37.73 ?  194 LYS A CA    1 
ATOM   1457 C C     . LYS A 1 202 ? 35.027  36.322  6.294   1.00 36.35 ?  194 LYS A C     1 
ATOM   1458 O O     . LYS A 1 202 ? 35.348  36.936  5.269   1.00 42.29 ?  194 LYS A O     1 
ATOM   1459 C CB    . LYS A 1 202 ? 36.704  36.174  8.155   1.00 36.63 ?  194 LYS A CB    1 
ATOM   1460 C CG    . LYS A 1 202 ? 37.656  37.110  8.884   1.00 41.61 ?  194 LYS A CG    1 
ATOM   1461 C CD    . LYS A 1 202 ? 38.096  36.536  10.222  1.00 45.17 ?  194 LYS A CD    1 
ATOM   1462 C CE    . LYS A 1 202 ? 39.061  35.376  10.037  1.00 46.03 ?  194 LYS A CE    1 
ATOM   1463 N NZ    . LYS A 1 202 ? 39.296  34.629  11.306  1.00 46.55 ?  194 LYS A NZ    1 
ATOM   1464 N N     . GLU A 1 203 ? 34.327  35.188  6.251   1.00 34.28 ?  195 GLU A N     1 
ATOM   1465 C CA    . GLU A 1 203 ? 33.933  34.607  4.972   1.00 35.54 ?  195 GLU A CA    1 
ATOM   1466 C C     . GLU A 1 203 ? 32.666  35.253  4.426   1.00 30.98 ?  195 GLU A C     1 
ATOM   1467 O O     . GLU A 1 203 ? 32.587  35.553  3.230   1.00 33.57 ?  195 GLU A O     1 
ATOM   1468 C CB    . GLU A 1 203 ? 33.740  33.098  5.121   1.00 30.27 ?  195 GLU A CB    1 
ATOM   1469 C CG    . GLU A 1 203 ? 33.414  32.384  3.821   1.00 39.40 ?  195 GLU A CG    1 
ATOM   1470 C CD    . GLU A 1 203 ? 34.641  32.133  2.968   1.00 40.21 ?  195 GLU A CD    1 
ATOM   1471 O OE1   . GLU A 1 203 ? 35.759  32.472  3.412   1.00 41.61 ?  195 GLU A OE1   1 
ATOM   1472 O OE2   . GLU A 1 203 ? 34.490  31.596  1.850   1.00 43.61 ?  195 GLU A OE2   1 
ATOM   1473 N N     . TYR A 1 204 ? 31.666  35.471  5.282   1.00 32.76 ?  196 TYR A N     1 
ATOM   1474 C CA    . TYR A 1 204 ? 30.396  36.077  4.888   1.00 33.31 ?  196 TYR A CA    1 
ATOM   1475 C C     . TYR A 1 204 ? 30.287  37.451  5.537   1.00 37.66 ?  196 TYR A C     1 
ATOM   1476 O O     . TYR A 1 204 ? 29.781  37.576  6.662   1.00 38.69 ?  196 TYR A O     1 
ATOM   1477 C CB    . TYR A 1 204 ? 29.218  35.188  5.292   1.00 29.76 ?  196 TYR A CB    1 
ATOM   1478 C CG    . TYR A 1 204 ? 29.295  33.785  4.733   1.00 35.81 ?  196 TYR A CG    1 
ATOM   1479 C CD1   . TYR A 1 204 ? 29.006  33.529  3.399   1.00 30.46 ?  196 TYR A CD1   1 
ATOM   1480 C CD2   . TYR A 1 204 ? 29.654  32.715  5.542   1.00 33.07 ?  196 TYR A CD2   1 
ATOM   1481 C CE1   . TYR A 1 204 ? 29.077  32.248  2.888   1.00 35.16 ?  196 TYR A CE1   1 
ATOM   1482 C CE2   . TYR A 1 204 ? 29.726  31.432  5.040   1.00 28.86 ?  196 TYR A CE2   1 
ATOM   1483 C CZ    . TYR A 1 204 ? 29.436  31.204  3.713   1.00 35.48 ?  196 TYR A CZ    1 
ATOM   1484 O OH    . TYR A 1 204 ? 29.506  29.925  3.212   1.00 37.67 ?  196 TYR A OH    1 
ATOM   1485 N N     . PRO A 1 205 ? 30.742  38.515  4.870   1.00 42.62 ?  197 PRO A N     1 
ATOM   1486 C CA    . PRO A 1 205 ? 30.751  39.840  5.512   1.00 42.05 ?  197 PRO A CA    1 
ATOM   1487 C C     . PRO A 1 205 ? 29.367  40.416  5.765   1.00 39.66 ?  197 PRO A C     1 
ATOM   1488 O O     . PRO A 1 205 ? 29.242  41.326  6.593   1.00 45.49 ?  197 PRO A O     1 
ATOM   1489 C CB    . PRO A 1 205 ? 31.542  40.712  4.524   1.00 42.85 ?  197 PRO A CB    1 
ATOM   1490 C CG    . PRO A 1 205 ? 32.137  39.765  3.519   1.00 41.77 ?  197 PRO A CG    1 
ATOM   1491 C CD    . PRO A 1 205 ? 31.284  38.548  3.504   1.00 41.01 ?  197 PRO A CD    1 
ATOM   1492 N N     . ASN A 1 206 ? 28.331  39.929  5.084   1.00 39.99 ?  198 ASN A N     1 
ATOM   1493 C CA    . ASN A 1 206 ? 26.969  40.397  5.307   1.00 44.28 ?  198 ASN A CA    1 
ATOM   1494 C C     . ASN A 1 206 ? 26.208  39.545  6.313   1.00 42.01 ?  198 ASN A C     1 
ATOM   1495 O O     . ASN A 1 206 ? 25.015  39.783  6.527   1.00 46.72 ?  198 ASN A O     1 
ATOM   1496 C CB    . ASN A 1 206 ? 26.191  40.429  3.987   1.00 45.39 ?  198 ASN A CB    1 
ATOM   1497 C CG    . ASN A 1 206 ? 26.837  41.324  2.953   1.00 44.72 ?  198 ASN A CG    1 
ATOM   1498 O OD1   . ASN A 1 206 ? 27.492  42.309  3.290   1.00 45.64 ?  198 ASN A OD1   1 
ATOM   1499 N ND2   . ASN A 1 206 ? 26.648  40.990  1.682   1.00 53.46 ?  198 ASN A ND2   1 
ATOM   1500 N N     . ILE A 1 207 ? 26.863  38.562  6.931   1.00 36.59 ?  199 ILE A N     1 
ATOM   1501 C CA    . ILE A 1 207 ? 26.171  37.668  7.849   1.00 35.28 ?  199 ILE A CA    1 
ATOM   1502 C C     . ILE A 1 207 ? 25.749  38.430  9.101   1.00 34.37 ?  199 ILE A C     1 
ATOM   1503 O O     . ILE A 1 207 ? 26.416  39.376  9.545   1.00 37.19 ?  199 ILE A O     1 
ATOM   1504 C CB    . ILE A 1 207 ? 27.058  36.460  8.203   1.00 38.12 ?  199 ILE A CB    1 
ATOM   1505 C CG1   . ILE A 1 207 ? 26.204  35.293  8.696   1.00 31.70 ?  199 ILE A CG1   1 
ATOM   1506 C CG2   . ILE A 1 207 ? 28.093  36.829  9.260   1.00 38.03 ?  199 ILE A CG2   1 
ATOM   1507 C CD1   . ILE A 1 207 ? 27.017  34.112  9.176   1.00 31.52 ?  199 ILE A CD1   1 
ATOM   1508 N N     . GLU A 1 208 ? 24.612  38.030  9.662   1.00 30.74 ?  200 GLU A N     1 
ATOM   1509 C CA    . GLU A 1 208 ? 24.166  38.517  10.960  1.00 32.83 ?  200 GLU A CA    1 
ATOM   1510 C C     . GLU A 1 208 ? 24.508  37.477  12.017  1.00 25.70 ?  200 GLU A C     1 
ATOM   1511 O O     . GLU A 1 208 ? 24.197  36.293  11.853  1.00 31.41 ?  200 GLU A O     1 
ATOM   1512 C CB    . GLU A 1 208 ? 22.663  38.802  10.975  1.00 32.51 ?  200 GLU A CB    1 
ATOM   1513 C CG    . GLU A 1 208 ? 22.220  39.620  12.185  1.00 35.64 ?  200 GLU A CG    1 
ATOM   1514 C CD    . GLU A 1 208 ? 20.709  39.713  12.337  1.00 38.75 ?  200 GLU A CD    1 
ATOM   1515 O OE1   . GLU A 1 208 ? 19.976  39.290  11.417  1.00 37.12 ?  200 GLU A OE1   1 
ATOM   1516 O OE2   . GLU A 1 208 ? 20.252  40.204  13.392  1.00 35.18 ?  200 GLU A OE2   1 
ATOM   1517 N N     . ILE A 1 209 ? 25.151  37.919  13.091  1.00 30.80 ?  201 ILE A N     1 
ATOM   1518 C CA    . ILE A 1 209 ? 25.500  37.060  14.215  1.00 32.07 ?  201 ILE A CA    1 
ATOM   1519 C C     . ILE A 1 209 ? 24.561  37.411  15.359  1.00 29.26 ?  201 ILE A C     1 
ATOM   1520 O O     . ILE A 1 209 ? 24.492  38.573  15.779  1.00 30.04 ?  201 ILE A O     1 
ATOM   1521 C CB    . ILE A 1 209 ? 26.970  37.229  14.623  1.00 27.63 ?  201 ILE A CB    1 
ATOM   1522 C CG1   . ILE A 1 209 ? 27.880  37.051  13.403  1.00 30.78 ?  201 ILE A CG1   1 
ATOM   1523 C CG2   . ILE A 1 209 ? 27.337  36.246  15.723  1.00 26.86 ?  201 ILE A CG2   1 
ATOM   1524 C CD1   . ILE A 1 209 ? 27.839  35.658  12.796  1.00 25.27 ?  201 ILE A CD1   1 
ATOM   1525 N N     . VAL A 1 210 ? 23.830  36.415  15.854  1.00 26.12 ?  202 VAL A N     1 
ATOM   1526 C CA    . VAL A 1 210 ? 22.784  36.621  16.847  1.00 29.03 ?  202 VAL A CA    1 
ATOM   1527 C C     . VAL A 1 210 ? 23.137  35.845  18.107  1.00 28.21 ?  202 VAL A C     1 
ATOM   1528 O O     . VAL A 1 210 ? 23.431  34.645  18.044  1.00 25.41 ?  202 VAL A O     1 
ATOM   1529 C CB    . VAL A 1 210 ? 21.405  36.190  16.315  1.00 30.61 ?  202 VAL A CB    1 
ATOM   1530 C CG1   . VAL A 1 210 ? 20.316  36.548  17.311  1.00 29.19 ?  202 VAL A CG1   1 
ATOM   1531 C CG2   . VAL A 1 210 ? 21.132  36.828  14.960  1.00 28.46 ?  202 VAL A CG2   1 
ATOM   1532 N N     . ALA A 1 211 ? 23.103  36.530  19.247  1.00 28.78 ?  203 ALA A N     1 
ATOM   1533 C CA    . ALA A 1 211 ? 23.259  35.888  20.541  1.00 24.26 ?  203 ALA A CA    1 
ATOM   1534 C C     . ALA A 1 211 ? 21.889  35.555  21.112  1.00 27.05 ?  203 ALA A C     1 
ATOM   1535 O O     . ALA A 1 211 ? 20.949  36.347  21.005  1.00 25.18 ?  203 ALA A O     1 
ATOM   1536 C CB    . ALA A 1 211 ? 24.023  36.793  21.508  1.00 24.52 ?  203 ALA A CB    1 
ATOM   1537 N N     . ILE A 1 212 ? 21.778  34.375  21.714  1.00 27.83 ?  204 ILE A N     1 
ATOM   1538 C CA    . ILE A 1 212 ? 20.543  33.922  22.343  1.00 23.49 ?  204 ILE A CA    1 
ATOM   1539 C C     . ILE A 1 212 ? 20.788  33.809  23.840  1.00 22.41 ?  204 ILE A C     1 
ATOM   1540 O O     . ILE A 1 212 ? 21.771  33.194  24.270  1.00 22.20 ?  204 ILE A O     1 
ATOM   1541 C CB    . ILE A 1 212 ? 20.067  32.582  21.757  1.00 25.24 ?  204 ILE A CB    1 
ATOM   1542 C CG1   . ILE A 1 212 ? 19.664  32.757  20.291  1.00 27.34 ?  204 ILE A CG1   1 
ATOM   1543 C CG2   . ILE A 1 212 ? 18.905  32.027  22.568  1.00 26.57 ?  204 ILE A CG2   1 
ATOM   1544 C CD1   . ILE A 1 212 ? 20.096  31.614  19.398  1.00 30.67 ?  204 ILE A CD1   1 
ATOM   1545 N N     . GLU A 1 213 ? 19.905  34.407  24.627  1.00 23.25 ?  205 GLU A N     1 
ATOM   1546 C CA    . GLU A 1 213 ? 19.999  34.402  26.077  1.00 22.49 ?  205 GLU A CA    1 
ATOM   1547 C C     . GLU A 1 213 ? 18.595  34.297  26.650  1.00 27.35 ?  205 GLU A C     1 
ATOM   1548 O O     . GLU A 1 213 ? 17.618  34.634  25.973  1.00 28.47 ?  205 GLU A O     1 
ATOM   1549 C CB    . GLU A 1 213 ? 20.705  35.663  26.595  1.00 24.60 ?  205 GLU A CB    1 
ATOM   1550 C CG    . GLU A 1 213 ? 19.858  36.921  26.579  1.00 29.96 ?  205 GLU A CG    1 
ATOM   1551 C CD    . GLU A 1 213 ? 20.586  38.115  27.168  1.00 34.16 ?  205 GLU A CD    1 
ATOM   1552 O OE1   . GLU A 1 213 ? 21.579  37.909  27.899  1.00 31.12 ?  205 GLU A OE1   1 
ATOM   1553 O OE2   . GLU A 1 213 ? 20.165  39.261  26.902  1.00 35.10 ?  205 GLU A OE2   1 
ATOM   1554 N N     . PRO A 1 214 ? 18.459  33.818  27.888  1.00 27.71 ?  206 PRO A N     1 
ATOM   1555 C CA    . PRO A 1 214 ? 17.116  33.643  28.455  1.00 29.63 ?  206 PRO A CA    1 
ATOM   1556 C C     . PRO A 1 214 ? 16.429  34.975  28.707  1.00 31.62 ?  206 PRO A C     1 
ATOM   1557 O O     . PRO A 1 214 ? 17.041  35.934  29.183  1.00 26.91 ?  206 PRO A O     1 
ATOM   1558 C CB    . PRO A 1 214 ? 17.370  32.890  29.769  1.00 26.18 ?  206 PRO A CB    1 
ATOM   1559 C CG    . PRO A 1 214 ? 18.785  32.417  29.703  1.00 29.62 ?  206 PRO A CG    1 
ATOM   1560 C CD    . PRO A 1 214 ? 19.508  33.375  28.822  1.00 33.15 ?  206 PRO A CD    1 
ATOM   1561 N N     . GLU A 1 215 ? 15.135  35.020  28.378  1.00 35.19 ?  207 GLU A N     1 
ATOM   1562 C CA    . GLU A 1 215 ? 14.325  36.192  28.688  1.00 30.20 ?  207 GLU A CA    1 
ATOM   1563 C C     . GLU A 1 215 ? 14.269  36.447  30.190  1.00 28.58 ?  207 GLU A C     1 
ATOM   1564 O O     . GLU A 1 215 ? 14.121  37.596  30.620  1.00 31.36 ?  207 GLU A O     1 
ATOM   1565 C CB    . GLU A 1 215 ? 12.915  36.013  28.120  1.00 32.70 ?  207 GLU A CB    1 
ATOM   1566 C CG    . GLU A 1 215 ? 12.015  37.230  28.269  1.00 45.36 ?  207 GLU A CG    1 
ATOM   1567 C CD    . GLU A 1 215 ? 10.645  37.028  27.650  1.00 40.64 ?  207 GLU A CD    1 
ATOM   1568 O OE1   . GLU A 1 215 ? 10.280  37.802  26.738  1.00 35.40 ?  207 GLU A OE1   1 
ATOM   1569 O OE2   . GLU A 1 215 ? 9.931   36.092  28.072  1.00 39.36 ?  207 GLU A OE2   1 
ATOM   1570 N N     . ALA A 1 216 ? 14.396  35.393  30.999  1.00 32.24 ?  208 ALA A N     1 
ATOM   1571 C CA    . ALA A 1 216 ? 14.387  35.521  32.450  1.00 29.50 ?  208 ALA A CA    1 
ATOM   1572 C C     . ALA A 1 216 ? 15.718  35.999  33.018  1.00 31.85 ?  208 ALA A C     1 
ATOM   1573 O O     . ALA A 1 216 ? 15.784  36.314  34.211  1.00 35.18 ?  208 ALA A O     1 
ATOM   1574 C CB    . ALA A 1 216 ? 14.007  34.184  33.090  1.00 33.76 ?  208 ALA A CB    1 
ATOM   1575 N N     . SER A 1 217 ? 16.775  36.054  32.206  1.00 32.98 ?  209 SER A N     1 
ATOM   1576 C CA    . SER A 1 217 ? 18.068  36.589  32.639  1.00 34.26 ?  209 SER A CA    1 
ATOM   1577 C C     . SER A 1 217 ? 18.724  37.297  31.462  1.00 34.54 ?  209 SER A C     1 
ATOM   1578 O O     . SER A 1 217 ? 19.733  36.836  30.915  1.00 30.07 ?  209 SER A O     1 
ATOM   1579 C CB    . SER A 1 217 ? 18.961  35.477  33.186  1.00 30.16 ?  209 SER A CB    1 
ATOM   1580 O OG    . SER A 1 217 ? 20.195  35.996  33.649  1.00 38.06 ?  209 SER A OG    1 
ATOM   1581 N N     . PRO A 1 218 ? 18.171  38.442  31.044  1.00 35.76 ?  210 PRO A N     1 
ATOM   1582 C CA    . PRO A 1 218 ? 18.660  39.134  29.832  1.00 36.62 ?  210 PRO A CA    1 
ATOM   1583 C C     . PRO A 1 218 ? 19.828  40.073  30.119  1.00 33.21 ?  210 PRO A C     1 
ATOM   1584 O O     . PRO A 1 218 ? 19.733  41.303  30.007  1.00 32.83 ?  210 PRO A O     1 
ATOM   1585 C CB    . PRO A 1 218 ? 17.410  39.881  29.366  1.00 36.66 ?  210 PRO A CB    1 
ATOM   1586 C CG    . PRO A 1 218 ? 16.710  40.241  30.646  1.00 33.48 ?  210 PRO A CG    1 
ATOM   1587 C CD    . PRO A 1 218 ? 17.051  39.171  31.668  1.00 34.23 ?  210 PRO A CD    1 
ATOM   1588 N N     . VAL A 1 219 ? 20.970  39.488  30.484  1.00 35.42 ?  211 VAL A N     1 
ATOM   1589 C CA    . VAL A 1 219 ? 22.113  40.295  30.898  1.00 33.49 ?  211 VAL A CA    1 
ATOM   1590 C C     . VAL A 1 219 ? 22.775  40.955  29.695  1.00 35.81 ?  211 VAL A C     1 
ATOM   1591 O O     . VAL A 1 219 ? 23.114  42.144  29.733  1.00 32.46 ?  211 VAL A O     1 
ATOM   1592 C CB    . VAL A 1 219 ? 23.109  39.440  31.700  1.00 35.52 ?  211 VAL A CB    1 
ATOM   1593 C CG1   . VAL A 1 219 ? 24.500  40.059  31.663  1.00 30.40 ?  211 VAL A CG1   1 
ATOM   1594 C CG2   . VAL A 1 219 ? 22.627  39.282  33.132  1.00 32.02 ?  211 VAL A CG2   1 
ATOM   1595 N N     . LEU A 1 220 ? 22.977  40.200  28.611  1.00 33.21 ?  212 LEU A N     1 
ATOM   1596 C CA    . LEU A 1 220 ? 23.542  40.797  27.405  1.00 34.79 ?  212 LEU A CA    1 
ATOM   1597 C C     . LEU A 1 220 ? 22.641  41.891  26.851  1.00 36.58 ?  212 LEU A C     1 
ATOM   1598 O O     . LEU A 1 220 ? 23.130  42.845  26.235  1.00 32.51 ?  212 LEU A O     1 
ATOM   1599 C CB    . LEU A 1 220 ? 23.788  39.725  26.341  1.00 33.45 ?  212 LEU A CB    1 
ATOM   1600 C CG    . LEU A 1 220 ? 24.537  38.460  26.757  1.00 35.51 ?  212 LEU A CG    1 
ATOM   1601 C CD1   . LEU A 1 220 ? 24.815  37.602  25.534  1.00 28.11 ?  212 LEU A CD1   1 
ATOM   1602 C CD2   . LEU A 1 220 ? 25.826  38.804  27.485  1.00 33.00 ?  212 LEU A CD2   1 
ATOM   1603 N N     . SER A 1 221 ? 21.329  41.775  27.064  1.00 34.82 ?  213 SER A N     1 
ATOM   1604 C CA    . SER A 1 221 ? 20.413  42.817  26.621  1.00 32.90 ?  213 SER A CA    1 
ATOM   1605 C C     . SER A 1 221 ? 20.461  44.047  27.518  1.00 34.30 ?  213 SER A C     1 
ATOM   1606 O O     . SER A 1 221 ? 19.977  45.110  27.118  1.00 36.48 ?  213 SER A O     1 
ATOM   1607 C CB    . SER A 1 221 ? 18.988  42.266  26.559  1.00 29.12 ?  213 SER A CB    1 
ATOM   1608 O OG    . SER A 1 221 ? 18.873  41.282  25.546  1.00 30.55 ?  213 SER A OG    1 
ATOM   1609 N N     . GLY A 1 222 ? 21.036  43.929  28.714  1.00 38.27 ?  214 GLY A N     1 
ATOM   1610 C CA    . GLY A 1 222 ? 21.129  45.037  29.645  1.00 35.85 ?  214 GLY A CA    1 
ATOM   1611 C C     . GLY A 1 222 ? 20.291  44.894  30.895  1.00 39.14 ?  214 GLY A C     1 
ATOM   1612 O O     . GLY A 1 222 ? 20.367  45.765  31.770  1.00 43.29 ?  214 GLY A O     1 
ATOM   1613 N N     . GLY A 1 223 ? 19.494  43.833  31.011  1.00 37.27 ?  215 GLY A N     1 
ATOM   1614 C CA    . GLY A 1 223 ? 18.678  43.624  32.185  1.00 34.48 ?  215 GLY A CA    1 
ATOM   1615 C C     . GLY A 1 223 ? 19.468  43.053  33.347  1.00 45.21 ?  215 GLY A C     1 
ATOM   1616 O O     . GLY A 1 223 ? 20.685  42.872  33.292  1.00 44.06 ?  215 GLY A O     1 
ATOM   1617 N N     . GLU A 1 224 ? 18.740  42.766  34.432  1.00 47.90 ?  216 GLU A N     1 
ATOM   1618 C CA    . GLU A 1 224 ? 19.353  42.213  35.627  1.00 48.72 ?  216 GLU A CA    1 
ATOM   1619 C C     . GLU A 1 224 ? 19.343  40.690  35.570  1.00 43.33 ?  216 GLU A C     1 
ATOM   1620 O O     . GLU A 1 224 ? 18.483  40.092  34.914  1.00 40.20 ?  216 GLU A O     1 
ATOM   1621 C CB    . GLU A 1 224 ? 18.608  42.683  36.876  1.00 46.02 ?  216 GLU A CB    1 
ATOM   1622 C CG    . GLU A 1 224 ? 18.855  44.141  37.240  1.00 50.59 ?  216 GLU A CG    1 
ATOM   1623 C CD    . GLU A 1 224 ? 20.303  44.560  37.047  1.00 69.11 ?  216 GLU A CD    1 
ATOM   1624 O OE1   . GLU A 1 224 ? 20.596  45.254  36.049  1.00 61.24 ?  216 GLU A OE1   1 
ATOM   1625 O OE2   . GLU A 1 224 ? 21.149  44.199  37.893  1.00 73.98 ?  216 GLU A OE2   1 
ATOM   1626 N N     . PRO A 1 225 ? 20.299  40.038  36.231  1.00 45.31 ?  217 PRO A N     1 
ATOM   1627 C CA    . PRO A 1 225 ? 20.295  38.572  36.260  1.00 35.83 ?  217 PRO A CA    1 
ATOM   1628 C C     . PRO A 1 225 ? 19.070  38.040  36.988  1.00 37.42 ?  217 PRO A C     1 
ATOM   1629 O O     . PRO A 1 225 ? 18.562  38.651  37.931  1.00 41.19 ?  217 PRO A O     1 
ATOM   1630 C CB    . PRO A 1 225 ? 21.586  38.222  37.010  1.00 33.23 ?  217 PRO A CB    1 
ATOM   1631 C CG    . PRO A 1 225 ? 22.427  39.455  36.957  1.00 35.91 ?  217 PRO A CG    1 
ATOM   1632 C CD    . PRO A 1 225 ? 21.487  40.613  36.882  1.00 39.04 ?  217 PRO A CD    1 
ATOM   1633 N N     . GLY A 1 226 ? 18.597  36.881  36.536  1.00 34.16 ?  218 GLY A N     1 
ATOM   1634 C CA    . GLY A 1 226 ? 17.429  36.263  37.113  1.00 32.83 ?  218 GLY A CA    1 
ATOM   1635 C C     . GLY A 1 226 ? 17.445  34.757  36.961  1.00 37.72 ?  218 GLY A C     1 
ATOM   1636 O O     . GLY A 1 226 ? 18.167  34.199  36.128  1.00 35.50 ?  218 GLY A O     1 
ATOM   1637 N N     . PRO A 1 227 ? 16.654  34.067  37.780  1.00 37.54 ?  219 PRO A N     1 
ATOM   1638 C CA    . PRO A 1 227 ? 16.566  32.608  37.656  1.00 38.57 ?  219 PRO A CA    1 
ATOM   1639 C C     . PRO A 1 227 ? 15.857  32.206  36.372  1.00 36.61 ?  219 PRO A C     1 
ATOM   1640 O O     . PRO A 1 227 ? 14.860  32.811  35.973  1.00 36.97 ?  219 PRO A O     1 
ATOM   1641 C CB    . PRO A 1 227 ? 15.760  32.194  38.893  1.00 41.54 ?  219 PRO A CB    1 
ATOM   1642 C CG    . PRO A 1 227 ? 14.985  33.421  39.263  1.00 40.31 ?  219 PRO A CG    1 
ATOM   1643 C CD    . PRO A 1 227 ? 15.874  34.578  38.919  1.00 38.29 ?  219 PRO A CD    1 
ATOM   1644 N N     . HIS A 1 228 ? 16.386  31.171  35.725  1.00 33.32 ?  220 HIS A N     1 
ATOM   1645 C CA    . HIS A 1 228 ? 15.824  30.670  34.480  1.00 33.51 ?  220 HIS A CA    1 
ATOM   1646 C C     . HIS A 1 228 ? 16.047  29.166  34.419  1.00 34.91 ?  220 HIS A C     1 
ATOM   1647 O O     . HIS A 1 228 ? 16.699  28.578  35.286  1.00 27.21 ?  220 HIS A O     1 
ATOM   1648 C CB    . HIS A 1 228 ? 16.444  31.372  33.267  1.00 34.17 ?  220 HIS A CB    1 
ATOM   1649 C CG    . HIS A 1 228 ? 17.902  31.084  33.087  1.00 32.01 ?  220 HIS A CG    1 
ATOM   1650 N ND1   . HIS A 1 228 ? 18.363  29.986  32.394  1.00 31.68 ?  220 HIS A ND1   1 
ATOM   1651 C CD2   . HIS A 1 228 ? 19.001  31.747  33.518  1.00 30.87 ?  220 HIS A CD2   1 
ATOM   1652 C CE1   . HIS A 1 228 ? 19.684  29.986  32.403  1.00 30.55 ?  220 HIS A CE1   1 
ATOM   1653 N NE2   . HIS A 1 228 ? 20.096  31.043  33.079  1.00 30.67 ?  220 HIS A NE2   1 
ATOM   1654 N N     . LYS A 1 229 ? 15.497  28.543  33.378  1.00 30.22 ?  221 LYS A N     1 
ATOM   1655 C CA    . LYS A 1 229 ? 15.576  27.097  33.213  1.00 32.96 ?  221 LYS A CA    1 
ATOM   1656 C C     . LYS A 1 229 ? 16.304  26.687  31.939  1.00 34.22 ?  221 LYS A C     1 
ATOM   1657 O O     . LYS A 1 229 ? 16.307  25.498  31.598  1.00 37.49 ?  221 LYS A O     1 
ATOM   1658 C CB    . LYS A 1 229 ? 14.172  26.482  33.233  1.00 31.15 ?  221 LYS A CB    1 
ATOM   1659 N N     . LEU A 1 230 ? 16.923  27.631  31.230  1.00 31.84 ?  222 LEU A N     1 
ATOM   1660 C CA    . LEU A 1 230 ? 17.653  27.324  29.999  1.00 29.39 ?  222 LEU A CA    1 
ATOM   1661 C C     . LEU A 1 230 ? 19.045  26.821  30.376  1.00 30.31 ?  222 LEU A C     1 
ATOM   1662 O O     . LEU A 1 230 ? 20.035  27.558  30.372  1.00 30.99 ?  222 LEU A O     1 
ATOM   1663 C CB    . LEU A 1 230 ? 17.719  28.546  29.089  1.00 28.06 ?  222 LEU A CB    1 
ATOM   1664 C CG    . LEU A 1 230 ? 16.403  29.224  28.699  1.00 32.34 ?  222 LEU A CG    1 
ATOM   1665 C CD1   . LEU A 1 230 ? 16.590  30.112  27.474  1.00 26.79 ?  222 LEU A CD1   1 
ATOM   1666 C CD2   . LEU A 1 230 ? 15.305  28.200  28.451  1.00 33.22 ?  222 LEU A CD2   1 
ATOM   1667 N N     . GLN A 1 231 ? 19.108  25.531  30.714  1.00 27.91 ?  223 GLN A N     1 
ATOM   1668 C CA    . GLN A 1 231 ? 20.366  24.905  31.105  1.00 34.13 ?  223 GLN A CA    1 
ATOM   1669 C C     . GLN A 1 231 ? 21.415  25.076  30.017  1.00 30.76 ?  223 GLN A C     1 
ATOM   1670 O O     . GLN A 1 231 ? 21.169  24.782  28.845  1.00 29.05 ?  223 GLN A O     1 
ATOM   1671 C CB    . GLN A 1 231 ? 20.149  23.419  31.391  1.00 32.56 ?  223 GLN A CB    1 
ATOM   1672 C CG    . GLN A 1 231 ? 19.448  23.119  32.702  1.00 37.12 ?  223 GLN A CG    1 
ATOM   1673 C CD    . GLN A 1 231 ? 19.579  21.663  33.101  1.00 41.53 ?  223 GLN A CD    1 
ATOM   1674 O OE1   . GLN A 1 231 ? 20.604  21.029  32.845  1.00 43.94 ?  223 GLN A OE1   1 
ATOM   1675 N NE2   . GLN A 1 231 ? 18.541  21.124  33.729  1.00 48.92 ?  223 GLN A NE2   1 
ATOM   1676 N N     . GLY A 1 232 ? 22.590  25.558  30.417  1.00 35.77 ?  224 GLY A N     1 
ATOM   1677 C CA    . GLY A 1 232 ? 23.665  25.845  29.497  1.00 30.71 ?  224 GLY A CA    1 
ATOM   1678 C C     . GLY A 1 232 ? 23.789  27.301  29.100  1.00 31.91 ?  224 GLY A C     1 
ATOM   1679 O O     . GLY A 1 232 ? 24.817  27.681  28.529  1.00 31.50 ?  224 GLY A O     1 
ATOM   1680 N N     . LEU A 1 233 ? 22.783  28.122  29.384  1.00 26.47 ?  225 LEU A N     1 
ATOM   1681 C CA    . LEU A 1 233 ? 22.788  29.539  29.038  1.00 27.53 ?  225 LEU A CA    1 
ATOM   1682 C C     . LEU A 1 233 ? 22.629  30.382  30.303  1.00 25.68 ?  225 LEU A C     1 
ATOM   1683 O O     . LEU A 1 233 ? 22.554  29.862  31.419  1.00 24.12 ?  225 LEU A O     1 
ATOM   1684 C CB    . LEU A 1 233 ? 21.675  29.857  28.033  1.00 29.00 ?  225 LEU A CB    1 
ATOM   1685 C CG    . LEU A 1 233 ? 21.565  28.947  26.808  1.00 28.08 ?  225 LEU A CG    1 
ATOM   1686 C CD1   . LEU A 1 233 ? 20.409  29.375  25.915  1.00 22.97 ?  225 LEU A CD1   1 
ATOM   1687 C CD2   . LEU A 1 233 ? 22.869  28.952  26.034  1.00 25.99 ?  225 LEU A CD2   1 
ATOM   1688 N N     . GLY A 1 234 ? 22.586  31.700  30.112  1.00 25.38 ?  226 GLY A N     1 
ATOM   1689 C CA    . GLY A 1 234 ? 22.292  32.631  31.184  1.00 28.03 ?  226 GLY A CA    1 
ATOM   1690 C C     . GLY A 1 234 ? 23.175  32.507  32.409  1.00 25.98 ?  226 GLY A C     1 
ATOM   1691 O O     . GLY A 1 234 ? 22.690  32.212  33.506  1.00 26.78 ?  226 GLY A O     1 
ATOM   1692 N N     . ALA A 1 235 ? 24.478  32.734  32.234  1.00 28.23 ?  227 ALA A N     1 
ATOM   1693 C CA    . ALA A 1 235 ? 25.405  32.656  33.356  1.00 27.62 ?  227 ALA A CA    1 
ATOM   1694 C C     . ALA A 1 235 ? 25.202  33.784  34.358  1.00 29.14 ?  227 ALA A C     1 
ATOM   1695 O O     . ALA A 1 235 ? 25.684  33.683  35.491  1.00 31.18 ?  227 ALA A O     1 
ATOM   1696 C CB    . ALA A 1 235 ? 26.848  32.664  32.848  1.00 23.68 ?  227 ALA A CB    1 
ATOM   1697 N N     . GLY A 1 236 ? 24.502  34.847  33.972  1.00 26.30 ?  228 GLY A N     1 
ATOM   1698 C CA    . GLY A 1 236 ? 24.256  35.961  34.861  1.00 30.75 ?  228 GLY A CA    1 
ATOM   1699 C C     . GLY A 1 236 ? 25.308  37.045  34.847  1.00 29.58 ?  228 GLY A C     1 
ATOM   1700 O O     . GLY A 1 236 ? 25.249  37.952  35.686  1.00 27.27 ?  228 GLY A O     1 
ATOM   1701 N N     . PHE A 1 237 ? 26.267  36.983  33.930  1.00 29.45 ?  229 PHE A N     1 
ATOM   1702 C CA    . PHE A 1 237 ? 27.306  37.999  33.830  1.00 31.78 ?  229 PHE A CA    1 
ATOM   1703 C C     . PHE A 1 237 ? 27.865  37.974  32.413  1.00 22.84 ?  229 PHE A C     1 
ATOM   1704 O O     . PHE A 1 237 ? 27.398  37.223  31.552  1.00 28.02 ?  229 PHE A O     1 
ATOM   1705 C CB    . PHE A 1 237 ? 28.404  37.778  34.878  1.00 23.04 ?  229 PHE A CB    1 
ATOM   1706 C CG    . PHE A 1 237 ? 29.078  36.437  34.783  1.00 24.32 ?  229 PHE A CG    1 
ATOM   1707 C CD1   . PHE A 1 237 ? 30.183  36.257  33.968  1.00 29.11 ?  229 PHE A CD1   1 
ATOM   1708 C CD2   . PHE A 1 237 ? 28.610  35.358  35.515  1.00 25.34 ?  229 PHE A CD2   1 
ATOM   1709 C CE1   . PHE A 1 237 ? 30.806  35.027  33.880  1.00 29.47 ?  229 PHE A CE1   1 
ATOM   1710 C CE2   . PHE A 1 237 ? 29.230  34.125  35.431  1.00 32.21 ?  229 PHE A CE2   1 
ATOM   1711 C CZ    . PHE A 1 237 ? 30.329  33.960  34.612  1.00 25.94 ?  229 PHE A CZ    1 
ATOM   1712 N N     . ILE A 1 238 ? 28.871  38.809  32.178  1.00 27.93 ?  230 ILE A N     1 
ATOM   1713 C CA    . ILE A 1 238 ? 29.557  38.866  30.891  1.00 28.67 ?  230 ILE A CA    1 
ATOM   1714 C C     . ILE A 1 238 ? 30.827  38.030  30.989  1.00 33.10 ?  230 ILE A C     1 
ATOM   1715 O O     . ILE A 1 238 ? 31.815  38.477  31.592  1.00 27.57 ?  230 ILE A O     1 
ATOM   1716 C CB    . ILE A 1 238 ? 29.877  40.314  30.489  1.00 31.05 ?  230 ILE A CB    1 
ATOM   1717 C CG1   . ILE A 1 238 ? 28.622  41.187  30.588  1.00 29.79 ?  230 ILE A CG1   1 
ATOM   1718 C CG2   . ILE A 1 238 ? 30.489  40.358  29.096  1.00 28.42 ?  230 ILE A CG2   1 
ATOM   1719 C CD1   . ILE A 1 238 ? 27.815  41.253  29.316  1.00 35.77 ?  230 ILE A CD1   1 
ATOM   1720 N N     . PRO A 1 239 ? 30.853  36.824  30.425  1.00 29.44 ?  231 PRO A N     1 
ATOM   1721 C CA    . PRO A 1 239 ? 32.053  35.991  30.536  1.00 28.26 ?  231 PRO A CA    1 
ATOM   1722 C C     . PRO A 1 239 ? 33.214  36.576  29.751  1.00 29.56 ?  231 PRO A C     1 
ATOM   1723 O O     . PRO A 1 239 ? 33.041  37.171  28.684  1.00 28.64 ?  231 PRO A O     1 
ATOM   1724 C CB    . PRO A 1 239 ? 31.610  34.644  29.948  1.00 32.52 ?  231 PRO A CB    1 
ATOM   1725 C CG    . PRO A 1 239 ? 30.106  34.703  29.901  1.00 29.17 ?  231 PRO A CG    1 
ATOM   1726 C CD    . PRO A 1 239 ? 29.783  36.145  29.679  1.00 31.07 ?  231 PRO A CD    1 
ATOM   1727 N N     . GLY A 1 240 ? 34.416  36.400  30.304  1.00 28.69 ?  232 GLY A N     1 
ATOM   1728 C CA    . GLY A 1 240 ? 35.624  36.815  29.615  1.00 28.87 ?  232 GLY A CA    1 
ATOM   1729 C C     . GLY A 1 240 ? 35.819  36.148  28.269  1.00 28.27 ?  232 GLY A C     1 
ATOM   1730 O O     . GLY A 1 240 ? 36.482  36.717  27.393  1.00 30.62 ?  232 GLY A O     1 
ATOM   1731 N N     . THR A 1 241 ? 35.253  34.955  28.083  1.00 23.52 ?  233 THR A N     1 
ATOM   1732 C CA    . THR A 1 241 ? 35.342  34.231  26.820  1.00 26.12 ?  233 THR A CA    1 
ATOM   1733 C C     . THR A 1 241 ? 34.329  34.709  25.788  1.00 27.68 ?  233 THR A C     1 
ATOM   1734 O O     . THR A 1 241 ? 34.328  34.199  24.662  1.00 27.48 ?  233 THR A O     1 
ATOM   1735 C CB    . THR A 1 241 ? 35.151  32.729  27.052  1.00 25.41 ?  233 THR A CB    1 
ATOM   1736 O OG1   . THR A 1 241 ? 34.084  32.517  27.984  1.00 25.85 ?  233 THR A OG1   1 
ATOM   1737 C CG2   . THR A 1 241 ? 36.419  32.111  27.610  1.00 21.76 ?  233 THR A CG2   1 
ATOM   1738 N N     . LEU A 1 242 ? 33.469  35.661  26.141  1.00 26.38 ?  234 LEU A N     1 
ATOM   1739 C CA    . LEU A 1 242 ? 32.459  36.187  25.232  1.00 26.02 ?  234 LEU A CA    1 
ATOM   1740 C C     . LEU A 1 242 ? 32.973  37.467  24.587  1.00 28.31 ?  234 LEU A C     1 
ATOM   1741 O O     . LEU A 1 242 ? 33.271  38.444  25.283  1.00 28.75 ?  234 LEU A O     1 
ATOM   1742 C CB    . LEU A 1 242 ? 31.147  36.455  25.967  1.00 23.05 ?  234 LEU A CB    1 
ATOM   1743 C CG    . LEU A 1 242 ? 30.087  37.185  25.139  1.00 26.30 ?  234 LEU A CG    1 
ATOM   1744 C CD1   . LEU A 1 242 ? 29.674  36.350  23.935  1.00 24.17 ?  234 LEU A CD1   1 
ATOM   1745 C CD2   . LEU A 1 242 ? 28.883  37.531  25.993  1.00 33.74 ?  234 LEU A CD2   1 
ATOM   1746 N N     . ASN A 1 243 ? 33.075  37.457  23.262  1.00 28.13 ?  235 ASN A N     1 
ATOM   1747 C CA    . ASN A 1 243 ? 33.390  38.658  22.493  1.00 35.96 ?  235 ASN A CA    1 
ATOM   1748 C C     . ASN A 1 243 ? 32.098  39.449  22.333  1.00 32.18 ?  235 ASN A C     1 
ATOM   1749 O O     . ASN A 1 243 ? 31.263  39.134  21.484  1.00 28.33 ?  235 ASN A O     1 
ATOM   1750 C CB    . ASN A 1 243 ? 33.995  38.282  21.144  1.00 31.52 ?  235 ASN A CB    1 
ATOM   1751 C CG    . ASN A 1 243 ? 34.350  39.490  20.299  1.00 32.59 ?  235 ASN A CG    1 
ATOM   1752 O OD1   . ASN A 1 243 ? 34.318  40.627  20.769  1.00 32.38 ?  235 ASN A OD1   1 
ATOM   1753 N ND2   . ASN A 1 243 ? 34.690  39.246  19.040  1.00 28.88 ?  235 ASN A ND2   1 
ATOM   1754 N N     . THR A 1 244 ? 31.922  40.483  23.158  1.00 30.85 ?  236 THR A N     1 
ATOM   1755 C CA    . THR A 1 244 ? 30.682  41.250  23.136  1.00 36.07 ?  236 THR A CA    1 
ATOM   1756 C C     . THR A 1 244 ? 30.515  42.080  21.868  1.00 33.50 ?  236 THR A C     1 
ATOM   1757 O O     . THR A 1 244 ? 29.435  42.642  21.659  1.00 39.22 ?  236 THR A O     1 
ATOM   1758 C CB    . THR A 1 244 ? 30.600  42.161  24.363  1.00 31.60 ?  236 THR A CB    1 
ATOM   1759 O OG1   . THR A 1 244 ? 31.787  42.959  24.455  1.00 32.75 ?  236 THR A OG1   1 
ATOM   1760 C CG2   . THR A 1 244 ? 30.447  41.327  25.626  1.00 26.70 ?  236 THR A CG2   1 
ATOM   1761 N N     . GLU A 1 245 ? 31.539  42.164  21.022  1.00 33.78 ?  237 GLU A N     1 
ATOM   1762 C CA    . GLU A 1 245 ? 31.461  42.887  19.761  1.00 32.21 ?  237 GLU A CA    1 
ATOM   1763 C C     . GLU A 1 245 ? 31.103  41.988  18.581  1.00 35.61 ?  237 GLU A C     1 
ATOM   1764 O O     . GLU A 1 245 ? 30.993  42.485  17.455  1.00 37.31 ?  237 GLU A O     1 
ATOM   1765 C CB    . GLU A 1 245 ? 32.790  43.596  19.472  1.00 33.71 ?  237 GLU A CB    1 
ATOM   1766 C CG    . GLU A 1 245 ? 33.222  44.607  20.527  1.00 38.19 ?  237 GLU A CG    1 
ATOM   1767 C CD    . GLU A 1 245 ? 32.136  45.612  20.855  1.00 51.35 ?  237 GLU A CD    1 
ATOM   1768 O OE1   . GLU A 1 245 ? 31.755  46.392  19.955  1.00 49.40 ?  237 GLU A OE1   1 
ATOM   1769 O OE2   . GLU A 1 245 ? 31.667  45.626  22.013  1.00 50.48 ?  237 GLU A OE2   1 
ATOM   1770 N N     . ILE A 1 246 ? 30.903  40.690  18.807  1.00 29.63 ?  238 ILE A N     1 
ATOM   1771 C CA    . ILE A 1 246 ? 30.744  39.759  17.697  1.00 32.28 ?  238 ILE A CA    1 
ATOM   1772 C C     . ILE A 1 246 ? 29.297  39.658  17.209  1.00 28.95 ?  238 ILE A C     1 
ATOM   1773 O O     . ILE A 1 246 ? 29.067  39.351  16.034  1.00 31.07 ?  238 ILE A O     1 
ATOM   1774 C CB    . ILE A 1 246 ? 31.285  38.369  18.086  1.00 27.93 ?  238 ILE A CB    1 
ATOM   1775 C CG1   . ILE A 1 246 ? 31.582  37.551  16.827  1.00 29.55 ?  238 ILE A CG1   1 
ATOM   1776 C CG2   . ILE A 1 246 ? 30.289  37.614  18.956  1.00 25.37 ?  238 ILE A CG2   1 
ATOM   1777 C CD1   . ILE A 1 246 ? 32.758  38.073  16.041  1.00 29.18 ?  238 ILE A CD1   1 
ATOM   1778 N N     . TYR A 1 247 ? 28.310  39.903  18.070  1.00 31.58 ?  239 TYR A N     1 
ATOM   1779 C CA    . TYR A 1 247 ? 26.916  39.698  17.703  1.00 30.10 ?  239 TYR A CA    1 
ATOM   1780 C C     . TYR A 1 247 ? 26.260  41.017  17.324  1.00 36.37 ?  239 TYR A C     1 
ATOM   1781 O O     . TYR A 1 247 ? 26.435  42.033  18.004  1.00 33.08 ?  239 TYR A O     1 
ATOM   1782 C CB    . TYR A 1 247 ? 26.121  39.033  18.829  1.00 28.01 ?  239 TYR A CB    1 
ATOM   1783 C CG    . TYR A 1 247 ? 26.372  39.572  20.219  1.00 33.05 ?  239 TYR A CG    1 
ATOM   1784 C CD1   . TYR A 1 247 ? 27.372  39.036  21.016  1.00 31.14 ?  239 TYR A CD1   1 
ATOM   1785 C CD2   . TYR A 1 247 ? 25.590  40.594  20.747  1.00 32.41 ?  239 TYR A CD2   1 
ATOM   1786 C CE1   . TYR A 1 247 ? 27.602  39.509  22.289  1.00 29.38 ?  239 TYR A CE1   1 
ATOM   1787 C CE2   . TYR A 1 247 ? 25.814  41.077  22.026  1.00 29.85 ?  239 TYR A CE2   1 
ATOM   1788 C CZ    . TYR A 1 247 ? 26.824  40.528  22.791  1.00 29.86 ?  239 TYR A CZ    1 
ATOM   1789 O OH    . TYR A 1 247 ? 27.062  40.994  24.064  1.00 31.49 ?  239 TYR A OH    1 
ATOM   1790 N N     . ASP A 1 248 ? 25.495  40.986  16.230  1.00 34.29 ?  240 ASP A N     1 
ATOM   1791 C CA    . ASP A 1 248 ? 24.780  42.162  15.752  1.00 31.48 ?  240 ASP A CA    1 
ATOM   1792 C C     . ASP A 1 248 ? 23.449  42.370  16.460  1.00 34.95 ?  240 ASP A C     1 
ATOM   1793 O O     . ASP A 1 248 ? 22.910  43.481  16.417  1.00 38.28 ?  240 ASP A O     1 
ATOM   1794 C CB    . ASP A 1 248 ? 24.539  42.058  14.242  1.00 32.86 ?  240 ASP A CB    1 
ATOM   1795 C CG    . ASP A 1 248 ? 25.802  41.735  13.471  1.00 32.94 ?  240 ASP A CG    1 
ATOM   1796 O OD1   . ASP A 1 248 ? 26.668  42.626  13.342  1.00 36.70 ?  240 ASP A OD1   1 
ATOM   1797 O OD2   . ASP A 1 248 ? 25.927  40.589  12.989  1.00 37.01 ?  240 ASP A OD2   1 
ATOM   1798 N N     . SER A 1 249 ? 22.911  41.338  17.104  1.00 32.75 ?  241 SER A N     1 
ATOM   1799 C CA    . SER A 1 249 ? 21.615  41.441  17.759  1.00 31.51 ?  241 SER A CA    1 
ATOM   1800 C C     . SER A 1 249 ? 21.488  40.320  18.781  1.00 33.35 ?  241 SER A C     1 
ATOM   1801 O O     . SER A 1 249 ? 22.276  39.371  18.799  1.00 32.67 ?  241 SER A O     1 
ATOM   1802 C CB    . SER A 1 249 ? 20.471  41.389  16.742  1.00 25.51 ?  241 SER A CB    1 
ATOM   1803 O OG    . SER A 1 249 ? 20.457  40.149  16.056  1.00 32.51 ?  241 SER A OG    1 
ATOM   1804 N N     . ILE A 1 250 ? 20.477  40.447  19.636  1.00 28.06 ?  242 ILE A N     1 
ATOM   1805 C CA    . ILE A 1 250 ? 20.183  39.484  20.688  1.00 26.01 ?  242 ILE A CA    1 
ATOM   1806 C C     . ILE A 1 250 ? 18.729  39.058  20.552  1.00 36.64 ?  242 ILE A C     1 
ATOM   1807 O O     . ILE A 1 250 ? 17.854  39.888  20.276  1.00 33.48 ?  242 ILE A O     1 
ATOM   1808 C CB    . ILE A 1 250 ? 20.450  40.075  22.088  1.00 28.79 ?  242 ILE A CB    1 
ATOM   1809 C CG1   . ILE A 1 250 ? 21.921  40.469  22.235  1.00 30.23 ?  242 ILE A CG1   1 
ATOM   1810 C CG2   . ILE A 1 250 ? 20.049  39.093  23.181  1.00 31.47 ?  242 ILE A CG2   1 
ATOM   1811 C CD1   . ILE A 1 250 ? 22.183  41.394  23.399  1.00 30.02 ?  242 ILE A CD1   1 
ATOM   1812 N N     . ILE A 1 251 ? 18.472  37.766  20.734  1.00 34.11 ?  243 ILE A N     1 
ATOM   1813 C CA    . ILE A 1 251 ? 17.120  37.221  20.745  1.00 34.42 ?  243 ILE A CA    1 
ATOM   1814 C C     . ILE A 1 251 ? 16.897  36.529  22.082  1.00 37.54 ?  243 ILE A C     1 
ATOM   1815 O O     . ILE A 1 251 ? 17.669  35.641  22.465  1.00 33.20 ?  243 ILE A O     1 
ATOM   1816 C CB    . ILE A 1 251 ? 16.879  36.251  19.574  1.00 30.03 ?  243 ILE A CB    1 
ATOM   1817 C CG1   . ILE A 1 251 ? 16.779  37.018  18.252  1.00 29.83 ?  243 ILE A CG1   1 
ATOM   1818 C CG2   . ILE A 1 251 ? 15.613  35.443  19.805  1.00 28.35 ?  243 ILE A CG2   1 
ATOM   1819 C CD1   . ILE A 1 251 ? 16.746  36.123  17.026  1.00 33.39 ?  243 ILE A CD1   1 
ATOM   1820 N N     . LYS A 1 252 ? 15.848  36.938  22.789  1.00 32.45 ?  244 LYS A N     1 
ATOM   1821 C CA    . LYS A 1 252 ? 15.524  36.408  24.105  1.00 32.23 ?  244 LYS A CA    1 
ATOM   1822 C C     . LYS A 1 252 ? 14.481  35.304  23.984  1.00 32.90 ?  244 LYS A C     1 
ATOM   1823 O O     . LYS A 1 252 ? 13.516  35.427  23.222  1.00 33.50 ?  244 LYS A O     1 
ATOM   1824 C CB    . LYS A 1 252 ? 15.011  37.520  25.022  1.00 34.84 ?  244 LYS A CB    1 
ATOM   1825 C CG    . LYS A 1 252 ? 16.066  38.556  25.372  1.00 33.89 ?  244 LYS A CG    1 
ATOM   1826 C CD    . LYS A 1 252 ? 15.548  39.555  26.393  1.00 40.73 ?  244 LYS A CD    1 
ATOM   1827 C CE    . LYS A 1 252 ? 14.958  40.789  25.728  1.00 39.56 ?  244 LYS A CE    1 
ATOM   1828 N NZ    . LYS A 1 252 ? 14.032  41.524  26.636  1.00 50.03 ?  244 LYS A NZ    1 
ATOM   1829 N N     . VAL A 1 253 ? 14.681  34.224  24.738  1.00 30.59 ?  245 VAL A N     1 
ATOM   1830 C CA    . VAL A 1 253 ? 13.813  33.053  24.685  1.00 35.72 ?  245 VAL A CA    1 
ATOM   1831 C C     . VAL A 1 253 ? 13.323  32.740  26.091  1.00 31.66 ?  245 VAL A C     1 
ATOM   1832 O O     . VAL A 1 253 ? 14.121  32.688  27.034  1.00 28.61 ?  245 VAL A O     1 
ATOM   1833 C CB    . VAL A 1 253 ? 14.536  31.832  24.081  1.00 31.98 ?  245 VAL A CB    1 
ATOM   1834 C CG1   . VAL A 1 253 ? 13.592  30.641  23.998  1.00 29.59 ?  245 VAL A CG1   1 
ATOM   1835 C CG2   . VAL A 1 253 ? 15.097  32.170  22.707  1.00 25.53 ?  245 VAL A CG2   1 
ATOM   1836 N N     . GLY A 1 254 ? 12.013  32.528  26.231  1.00 32.54 ?  246 GLY A N     1 
ATOM   1837 C CA    . GLY A 1 254 ? 11.447  32.158  27.510  1.00 29.90 ?  246 GLY A CA    1 
ATOM   1838 C C     . GLY A 1 254 ? 11.653  30.690  27.842  1.00 28.24 ?  246 GLY A C     1 
ATOM   1839 O O     . GLY A 1 254 ? 12.038  29.878  27.000  1.00 32.99 ?  246 GLY A O     1 
ATOM   1840 N N     . ASN A 1 255 ? 11.381  30.355  29.107  1.00 26.41 ?  247 ASN A N     1 
ATOM   1841 C CA    . ASN A 1 255 ? 11.585  28.991  29.587  1.00 30.50 ?  247 ASN A CA    1 
ATOM   1842 C C     . ASN A 1 255 ? 10.710  28.000  28.826  1.00 33.93 ?  247 ASN A C     1 
ATOM   1843 O O     . ASN A 1 255 ? 11.213  27.063  28.195  1.00 30.93 ?  247 ASN A O     1 
ATOM   1844 C CB    . ASN A 1 255 ? 11.299  28.914  31.091  1.00 32.10 ?  247 ASN A CB    1 
ATOM   1845 C CG    . ASN A 1 255 ? 12.371  29.588  31.932  1.00 39.29 ?  247 ASN A CG    1 
ATOM   1846 O OD1   . ASN A 1 255 ? 13.525  29.699  31.519  1.00 39.73 ?  247 ASN A OD1   1 
ATOM   1847 N ND2   . ASN A 1 255 ? 11.992  30.037  33.123  1.00 37.84 ?  247 ASN A ND2   1 
ATOM   1848 N N     . ASP A 1 256 ? 9.388   28.198  28.872  1.00 33.70 ?  248 ASP A N     1 
ATOM   1849 C CA    . ASP A 1 256 ? 8.466   27.250  28.253  1.00 34.82 ?  248 ASP A CA    1 
ATOM   1850 C C     . ASP A 1 256 ? 8.627   27.203  26.738  1.00 28.60 ?  248 ASP A C     1 
ATOM   1851 O O     . ASP A 1 256 ? 8.406   26.151  26.127  1.00 32.67 ?  248 ASP A O     1 
ATOM   1852 C CB    . ASP A 1 256 ? 7.024   27.605  28.621  1.00 33.30 ?  248 ASP A CB    1 
ATOM   1853 C CG    . ASP A 1 256 ? 6.753   27.486  30.111  1.00 37.73 ?  248 ASP A CG    1 
ATOM   1854 O OD1   . ASP A 1 256 ? 6.983   26.397  30.677  1.00 44.10 ?  248 ASP A OD1   1 
ATOM   1855 O OD2   . ASP A 1 256 ? 6.307   28.484  30.718  1.00 38.23 ?  248 ASP A OD2   1 
ATOM   1856 N N     . THR A 1 257 ? 9.008   28.324  26.119  1.00 28.35 ?  249 THR A N     1 
ATOM   1857 C CA    . THR A 1 257 ? 9.200   28.351  24.671  1.00 31.21 ?  249 THR A CA    1 
ATOM   1858 C C     . THR A 1 257 ? 10.282  27.367  24.242  1.00 33.28 ?  249 THR A C     1 
ATOM   1859 O O     . THR A 1 257 ? 10.104  26.606  23.283  1.00 29.23 ?  249 THR A O     1 
ATOM   1860 C CB    . THR A 1 257 ? 9.558   29.767  24.219  1.00 33.10 ?  249 THR A CB    1 
ATOM   1861 O OG1   . THR A 1 257 ? 8.439   30.637  24.425  1.00 34.92 ?  249 THR A OG1   1 
ATOM   1862 C CG2   . THR A 1 257 ? 9.943   29.778  22.746  1.00 34.62 ?  249 THR A CG2   1 
ATOM   1863 N N     . ALA A 1 258 ? 11.416  27.370  24.947  1.00 35.04 ?  250 ALA A N     1 
ATOM   1864 C CA    . ALA A 1 258 ? 12.507  26.465  24.603  1.00 25.46 ?  250 ALA A CA    1 
ATOM   1865 C C     . ALA A 1 258 ? 12.103  25.009  24.797  1.00 26.92 ?  250 ALA A C     1 
ATOM   1866 O O     . ALA A 1 258 ? 12.426  24.154  23.965  1.00 27.60 ?  250 ALA A O     1 
ATOM   1867 C CB    . ALA A 1 258 ? 13.746  26.795  25.435  1.00 24.06 ?  250 ALA A CB    1 
ATOM   1868 N N     . MET A 1 259 ? 11.396  24.705  25.889  1.00 25.44 ?  251 MET A N     1 
ATOM   1869 C CA    . MET A 1 259 ? 10.969  23.328  26.124  1.00 30.67 ?  251 MET A CA    1 
ATOM   1870 C C     . MET A 1 259 ? 10.028  22.848  25.026  1.00 32.26 ?  251 MET A C     1 
ATOM   1871 O O     . MET A 1 259 ? 10.193  21.745  24.492  1.00 30.22 ?  251 MET A O     1 
ATOM   1872 C CB    . MET A 1 259 ? 10.295  23.194  27.491  1.00 32.45 ?  251 MET A CB    1 
ATOM   1873 C CG    . MET A 1 259 ? 10.976  23.908  28.642  1.00 43.78 ?  251 MET A CG    1 
ATOM   1874 S SD    . MET A 1 259 ? 11.070  22.845  30.098  1.00 59.24 ?  251 MET A SD    1 
ATOM   1875 C CE    . MET A 1 259 ? 11.714  23.987  31.316  1.00 50.19 ?  251 MET A CE    1 
ATOM   1876 N N     . GLU A 1 260 ? 9.030   23.665  24.674  1.00 33.29 ?  252 GLU A N     1 
ATOM   1877 C CA    . GLU A 1 260 ? 8.056   23.245  23.673  1.00 38.84 ?  252 GLU A CA    1 
ATOM   1878 C C     . GLU A 1 260 ? 8.693   23.105  22.296  1.00 31.36 ?  252 GLU A C     1 
ATOM   1879 O O     . GLU A 1 260 ? 8.278   22.247  21.507  1.00 33.65 ?  252 GLU A O     1 
ATOM   1880 C CB    . GLU A 1 260 ? 6.887   24.233  23.629  1.00 41.32 ?  252 GLU A CB    1 
ATOM   1881 C CG    . GLU A 1 260 ? 5.785   23.976  24.664  1.00 44.49 ?  252 GLU A CG    1 
ATOM   1882 C CD    . GLU A 1 260 ? 5.196   22.571  24.622  1.00 55.70 ?  252 GLU A CD    1 
ATOM   1883 O OE1   . GLU A 1 260 ? 5.354   21.860  23.605  1.00 51.46 ?  252 GLU A OE1   1 
ATOM   1884 O OE2   . GLU A 1 260 ? 4.568   22.173  25.626  1.00 59.02 ?  252 GLU A OE2   1 
ATOM   1885 N N     . MET A 1 261 ? 9.698   23.931  21.991  1.00 27.55 ?  253 MET A N     1 
ATOM   1886 C CA    . MET A 1 261 ? 10.412  23.783  20.727  1.00 26.26 ?  253 MET A CA    1 
ATOM   1887 C C     . MET A 1 261 ? 11.191  22.475  20.687  1.00 28.86 ?  253 MET A C     1 
ATOM   1888 O O     . MET A 1 261 ? 11.206  21.784  19.660  1.00 29.84 ?  253 MET A O     1 
ATOM   1889 C CB    . MET A 1 261 ? 11.349  24.971  20.509  1.00 29.98 ?  253 MET A CB    1 
ATOM   1890 C CG    . MET A 1 261 ? 11.829  25.110  19.078  1.00 30.87 ?  253 MET A CG    1 
ATOM   1891 S SD    . MET A 1 261 ? 10.462  25.408  17.943  1.00 41.55 ?  253 MET A SD    1 
ATOM   1892 C CE    . MET A 1 261 ? 10.783  24.157  16.709  1.00 30.59 ?  253 MET A CE    1 
ATOM   1893 N N     . SER A 1 262 ? 11.841  22.116  21.799  1.00 28.98 ?  254 SER A N     1 
ATOM   1894 C CA    . SER A 1 262 ? 12.595  20.867  21.844  1.00 31.32 ?  254 SER A CA    1 
ATOM   1895 C C     . SER A 1 262 ? 11.678  19.662  21.674  1.00 30.27 ?  254 SER A C     1 
ATOM   1896 O O     . SER A 1 262 ? 12.039  18.687  21.003  1.00 29.09 ?  254 SER A O     1 
ATOM   1897 C CB    . SER A 1 262 ? 13.370  20.767  23.157  1.00 28.76 ?  254 SER A CB    1 
ATOM   1898 O OG    . SER A 1 262 ? 14.570  21.517  23.103  1.00 31.41 ?  254 SER A OG    1 
ATOM   1899 N N     . ARG A 1 263 ? 10.487  19.709  22.279  1.00 28.40 ?  255 ARG A N     1 
ATOM   1900 C CA    . ARG A 1 263 ? 9.534   18.615  22.122  1.00 28.67 ?  255 ARG A CA    1 
ATOM   1901 C C     . ARG A 1 263 ? 9.038   18.519  20.686  1.00 24.42 ?  255 ARG A C     1 
ATOM   1902 O O     . ARG A 1 263 ? 8.900   17.416  20.143  1.00 27.07 ?  255 ARG A O     1 
ATOM   1903 C CB    . ARG A 1 263 ? 8.359   18.799  23.080  1.00 33.93 ?  255 ARG A CB    1 
ATOM   1904 C CG    . ARG A 1 263 ? 8.710   18.632  24.547  1.00 34.48 ?  255 ARG A CG    1 
ATOM   1905 C CD    . ARG A 1 263 ? 7.600   19.174  25.430  1.00 36.43 ?  255 ARG A CD    1 
ATOM   1906 N NE    . ARG A 1 263 ? 7.967   19.168  26.840  1.00 47.27 ?  255 ARG A NE    1 
ATOM   1907 C CZ    . ARG A 1 263 ? 7.391   19.924  27.765  1.00 54.21 ?  255 ARG A CZ    1 
ATOM   1908 N NH1   . ARG A 1 263 ? 6.412   20.762  27.462  1.00 46.83 ?  255 ARG A NH1   1 
ATOM   1909 N NH2   . ARG A 1 263 ? 7.807   19.838  29.025  1.00 55.44 ?  255 ARG A NH2   1 
ATOM   1910 N N     . ARG A 1 264 ? 8.754   19.663  20.058  1.00 25.21 ?  256 ARG A N     1 
ATOM   1911 C CA    . ARG A 1 264 ? 8.360   19.664  18.653  1.00 26.80 ?  256 ARG A CA    1 
ATOM   1912 C C     . ARG A 1 264 ? 9.464   19.093  17.774  1.00 29.63 ?  256 ARG A C     1 
ATOM   1913 O O     . ARG A 1 264 ? 9.215   18.231  16.924  1.00 31.53 ?  256 ARG A O     1 
ATOM   1914 C CB    . ARG A 1 264 ? 8.009   21.082  18.207  1.00 33.52 ?  256 ARG A CB    1 
ATOM   1915 C CG    . ARG A 1 264 ? 6.563   21.469  18.415  1.00 38.33 ?  256 ARG A CG    1 
ATOM   1916 C CD    . ARG A 1 264 ? 6.193   22.636  17.519  1.00 37.76 ?  256 ARG A CD    1 
ATOM   1917 N NE    . ARG A 1 264 ? 5.945   22.214  16.146  1.00 49.52 ?  256 ARG A NE    1 
ATOM   1918 C CZ    . ARG A 1 264 ? 6.119   22.989  15.084  1.00 45.73 ?  256 ARG A CZ    1 
ATOM   1919 N NH1   . ARG A 1 264 ? 6.561   24.230  15.201  1.00 42.06 ?  256 ARG A NH1   1 
ATOM   1920 N NH2   . ARG A 1 264 ? 5.843   22.507  13.875  1.00 40.54 ?  256 ARG A NH2   1 
ATOM   1921 N N     . VAL A 1 265 ? 10.696  19.568  17.967  1.00 27.99 ?  257 VAL A N     1 
ATOM   1922 C CA    . VAL A 1 265 ? 11.812  19.106  17.147  1.00 25.50 ?  257 VAL A CA    1 
ATOM   1923 C C     . VAL A 1 265 ? 12.024  17.609  17.329  1.00 26.66 ?  257 VAL A C     1 
ATOM   1924 O O     . VAL A 1 265 ? 12.326  16.887  16.371  1.00 26.31 ?  257 VAL A O     1 
ATOM   1925 C CB    . VAL A 1 265 ? 13.082  19.910  17.485  1.00 28.66 ?  257 VAL A CB    1 
ATOM   1926 C CG1   . VAL A 1 265 ? 14.324  19.202  16.975  1.00 24.42 ?  257 VAL A CG1   1 
ATOM   1927 C CG2   . VAL A 1 265 ? 12.989  21.307  16.899  1.00 27.67 ?  257 VAL A CG2   1 
ATOM   1928 N N     . ALA A 1 266 ? 11.849  17.116  18.558  1.00 27.45 ?  258 ALA A N     1 
ATOM   1929 C CA    . ALA A 1 266 ? 12.021  15.691  18.817  1.00 24.93 ?  258 ALA A CA    1 
ATOM   1930 C C     . ALA A 1 266 ? 10.944  14.864  18.127  1.00 28.99 ?  258 ALA A C     1 
ATOM   1931 O O     . ALA A 1 266 ? 11.237  13.810  17.552  1.00 30.72 ?  258 ALA A O     1 
ATOM   1932 C CB    . ALA A 1 266 ? 12.017  15.428  20.323  1.00 28.47 ?  258 ALA A CB    1 
ATOM   1933 N N     . LYS A 1 267 ? 9.693   15.328  18.165  1.00 28.41 ?  259 LYS A N     1 
ATOM   1934 C CA    . LYS A 1 267 ? 8.597   14.549  17.599  1.00 26.56 ?  259 LYS A CA    1 
ATOM   1935 C C     . LYS A 1 267 ? 8.461   14.734  16.093  1.00 28.53 ?  259 LYS A C     1 
ATOM   1936 O O     . LYS A 1 267 ? 8.010   13.813  15.402  1.00 30.19 ?  259 LYS A O     1 
ATOM   1937 C CB    . LYS A 1 267 ? 7.281   14.918  18.286  1.00 28.92 ?  259 LYS A CB    1 
ATOM   1938 C CG    . LYS A 1 267 ? 7.231   14.588  19.766  1.00 31.18 ?  259 LYS A CG    1 
ATOM   1939 C CD    . LYS A 1 267 ? 5.874   14.935  20.357  1.00 33.90 ?  259 LYS A CD    1 
ATOM   1940 C CE    . LYS A 1 267 ? 5.778   14.502  21.810  1.00 40.13 ?  259 LYS A CE    1 
ATOM   1941 N NZ    . LYS A 1 267 ? 4.386   14.598  22.327  1.00 45.38 ?  259 LYS A NZ    1 
ATOM   1942 N N     . GLU A 1 268 ? 8.841   15.900  15.563  1.00 29.56 ?  260 GLU A N     1 
ATOM   1943 C CA    . GLU A 1 268 ? 8.604   16.217  14.161  1.00 29.87 ?  260 GLU A CA    1 
ATOM   1944 C C     . GLU A 1 268 ? 9.847   16.156  13.286  1.00 33.81 ?  260 GLU A C     1 
ATOM   1945 O O     . GLU A 1 268 ? 9.712   16.123  12.059  1.00 31.26 ?  260 GLU A O     1 
ATOM   1946 C CB    . GLU A 1 268 ? 7.973   17.610  14.031  1.00 30.99 ?  260 GLU A CB    1 
ATOM   1947 C CG    . GLU A 1 268 ? 6.541   17.660  14.528  1.00 30.29 ?  260 GLU A CG    1 
ATOM   1948 C CD    . GLU A 1 268 ? 5.988   19.067  14.592  1.00 33.55 ?  260 GLU A CD    1 
ATOM   1949 O OE1   . GLU A 1 268 ? 6.271   19.868  13.677  1.00 41.43 ?  260 GLU A OE1   1 
ATOM   1950 O OE2   . GLU A 1 268 ? 5.266   19.371  15.564  1.00 48.13 ?  260 GLU A OE2   1 
ATOM   1951 N N     . GLU A 1 269 ? 11.043  16.143  13.873  1.00 32.92 ?  261 GLU A N     1 
ATOM   1952 C CA    . GLU A 1 269 ? 12.275  15.997  13.114  1.00 31.86 ?  261 GLU A CA    1 
ATOM   1953 C C     . GLU A 1 269 ? 13.082  14.769  13.499  1.00 29.69 ?  261 GLU A C     1 
ATOM   1954 O O     . GLU A 1 269 ? 14.024  14.422  12.778  1.00 31.57 ?  261 GLU A O     1 
ATOM   1955 C CB    . GLU A 1 269 ? 13.170  17.236  13.279  1.00 25.99 ?  261 GLU A CB    1 
ATOM   1956 C CG    . GLU A 1 269 ? 12.461  18.563  13.098  1.00 29.31 ?  261 GLU A CG    1 
ATOM   1957 C CD    . GLU A 1 269 ? 12.291  18.938  11.640  1.00 30.86 ?  261 GLU A CD    1 
ATOM   1958 O OE1   . GLU A 1 269 ? 13.079  18.452  10.800  1.00 32.98 ?  261 GLU A OE1   1 
ATOM   1959 O OE2   . GLU A 1 269 ? 11.373  19.726  11.332  1.00 32.47 ?  261 GLU A OE2   1 
ATOM   1960 N N     . GLY A 1 270 ? 12.750  14.105  14.603  1.00 28.56 ?  262 GLY A N     1 
ATOM   1961 C CA    . GLY A 1 270 ? 13.573  13.018  15.086  1.00 27.02 ?  262 GLY A CA    1 
ATOM   1962 C C     . GLY A 1 270 ? 14.855  13.452  15.753  1.00 28.52 ?  262 GLY A C     1 
ATOM   1963 O O     . GLY A 1 270 ? 15.703  12.604  16.045  1.00 29.83 ?  262 GLY A O     1 
ATOM   1964 N N     . ILE A 1 271 ? 15.023  14.746  16.004  1.00 29.57 ?  263 ILE A N     1 
ATOM   1965 C CA    . ILE A 1 271 ? 16.217  15.289  16.638  1.00 25.50 ?  263 ILE A CA    1 
ATOM   1966 C C     . ILE A 1 271 ? 15.889  15.536  18.105  1.00 29.32 ?  263 ILE A C     1 
ATOM   1967 O O     . ILE A 1 271 ? 15.120  16.445  18.434  1.00 23.84 ?  263 ILE A O     1 
ATOM   1968 C CB    . ILE A 1 271 ? 16.682  16.577  15.946  1.00 23.70 ?  263 ILE A CB    1 
ATOM   1969 C CG1   . ILE A 1 271 ? 16.995  16.301  14.474  1.00 22.06 ?  263 ILE A CG1   1 
ATOM   1970 C CG2   . ILE A 1 271 ? 17.890  17.160  16.661  1.00 24.89 ?  263 ILE A CG2   1 
ATOM   1971 C CD1   . ILE A 1 271 ? 17.278  17.547  13.671  1.00 25.07 ?  263 ILE A CD1   1 
ATOM   1972 N N     . LEU A 1 272 ? 16.470  14.728  18.989  1.00 25.97 ?  264 LEU A N     1 
ATOM   1973 C CA    . LEU A 1 272 ? 16.230  14.820  20.425  1.00 26.83 ?  264 LEU A CA    1 
ATOM   1974 C C     . LEU A 1 272 ? 17.377  15.595  21.065  1.00 25.90 ?  264 LEU A C     1 
ATOM   1975 O O     . LEU A 1 272 ? 18.488  15.071  21.207  1.00 25.27 ?  264 LEU A O     1 
ATOM   1976 C CB    . LEU A 1 272 ? 16.100  13.429  21.040  1.00 21.96 ?  264 LEU A CB    1 
ATOM   1977 C CG    . LEU A 1 272 ? 15.813  13.420  22.539  1.00 29.07 ?  264 LEU A CG    1 
ATOM   1978 C CD1   . LEU A 1 272 ? 14.413  13.943  22.806  1.00 30.63 ?  264 LEU A CD1   1 
ATOM   1979 C CD2   . LEU A 1 272 ? 15.988  12.029  23.101  1.00 28.57 ?  264 LEU A CD2   1 
ATOM   1980 N N     . ALA A 1 273 ? 17.105  16.835  21.464  1.00 24.29 ?  265 ALA A N     1 
ATOM   1981 C CA    . ALA A 1 273 ? 18.129  17.738  21.963  1.00 28.80 ?  265 ALA A CA    1 
ATOM   1982 C C     . ALA A 1 273 ? 17.673  18.385  23.265  1.00 28.75 ?  265 ALA A C     1 
ATOM   1983 O O     . ALA A 1 273 ? 16.518  18.261  23.680  1.00 26.29 ?  265 ALA A O     1 
ATOM   1984 C CB    . ALA A 1 273 ? 18.473  18.804  20.917  1.00 22.83 ?  265 ALA A CB    1 
ATOM   1985 N N     . GLY A 1 274 ? 18.605  19.087  23.911  1.00 27.34 ?  266 GLY A N     1 
ATOM   1986 C CA    . GLY A 1 274 ? 18.349  19.704  25.194  1.00 27.67 ?  266 GLY A CA    1 
ATOM   1987 C C     . GLY A 1 274 ? 17.541  20.985  25.092  1.00 31.11 ?  266 GLY A C     1 
ATOM   1988 O O     . GLY A 1 274 ? 17.110  21.412  24.021  1.00 26.04 ?  266 GLY A O     1 
ATOM   1989 N N     . ILE A 1 275 ? 17.340  21.614  26.253  1.00 29.21 ?  267 ILE A N     1 
ATOM   1990 C CA    . ILE A 1 275 ? 16.491  22.800  26.312  1.00 30.82 ?  267 ILE A CA    1 
ATOM   1991 C C     . ILE A 1 275 ? 17.157  23.982  25.617  1.00 29.80 ?  267 ILE A C     1 
ATOM   1992 O O     . ILE A 1 275 ? 16.486  24.788  24.960  1.00 30.79 ?  267 ILE A O     1 
ATOM   1993 C CB    . ILE A 1 275 ? 16.120  23.127  27.771  1.00 30.78 ?  267 ILE A CB    1 
ATOM   1994 C CG1   . ILE A 1 275 ? 15.154  24.311  27.817  1.00 37.26 ?  267 ILE A CG1   1 
ATOM   1995 C CG2   . ILE A 1 275 ? 17.358  23.396  28.614  1.00 34.20 ?  267 ILE A CG2   1 
ATOM   1996 C CD1   . ILE A 1 275 ? 14.494  24.492  29.152  1.00 41.11 ?  267 ILE A CD1   1 
ATOM   1997 N N     . SER A 1 276 ? 18.481  24.108  25.744  1.00 26.15 ?  268 SER A N     1 
ATOM   1998 C CA    . SER A 1 276 ? 19.180  25.196  25.069  1.00 24.29 ?  268 SER A CA    1 
ATOM   1999 C C     . SER A 1 276 ? 19.088  25.057  23.557  1.00 23.26 ?  268 SER A C     1 
ATOM   2000 O O     . SER A 1 276 ? 19.076  26.063  22.839  1.00 23.23 ?  268 SER A O     1 
ATOM   2001 C CB    . SER A 1 276 ? 20.641  25.238  25.510  1.00 24.98 ?  268 SER A CB    1 
ATOM   2002 O OG    . SER A 1 276 ? 21.424  24.356  24.725  1.00 29.81 ?  268 SER A OG    1 
ATOM   2003 N N     . SER A 1 277 ? 19.021  23.822  23.056  1.00 22.71 ?  269 SER A N     1 
ATOM   2004 C CA    . SER A 1 277 ? 18.855  23.619  21.623  1.00 26.01 ?  269 SER A CA    1 
ATOM   2005 C C     . SER A 1 277 ? 17.469  24.045  21.161  1.00 28.14 ?  269 SER A C     1 
ATOM   2006 O O     . SER A 1 277 ? 17.315  24.540  20.039  1.00 26.98 ?  269 SER A O     1 
ATOM   2007 C CB    . SER A 1 277 ? 19.106  22.156  21.271  1.00 25.87 ?  269 SER A CB    1 
ATOM   2008 O OG    . SER A 1 277 ? 20.385  21.729  21.703  1.00 25.91 ?  269 SER A OG    1 
ATOM   2009 N N     . GLY A 1 278 ? 16.453  23.854  22.007  1.00 27.27 ?  270 GLY A N     1 
ATOM   2010 C CA    . GLY A 1 278 ? 15.131  24.362  21.685  1.00 26.97 ?  270 GLY A CA    1 
ATOM   2011 C C     . GLY A 1 278 ? 15.099  25.876  21.608  1.00 28.48 ?  270 GLY A C     1 
ATOM   2012 O O     . GLY A 1 278 ? 14.474  26.449  20.712  1.00 27.10 ?  270 GLY A O     1 
ATOM   2013 N N     . ALA A 1 279 ? 15.777  26.547  22.545  1.00 27.90 ?  271 ALA A N     1 
ATOM   2014 C CA    . ALA A 1 279 ? 15.888  27.999  22.472  1.00 27.63 ?  271 ALA A CA    1 
ATOM   2015 C C     . ALA A 1 279 ? 16.622  28.428  21.209  1.00 29.04 ?  271 ALA A C     1 
ATOM   2016 O O     . ALA A 1 279 ? 16.280  29.446  20.597  1.00 25.86 ?  271 ALA A O     1 
ATOM   2017 C CB    . ALA A 1 279 ? 16.595  28.536  23.716  1.00 24.55 ?  271 ALA A CB    1 
ATOM   2018 N N     . ALA A 1 280 ? 17.630  27.655  20.797  1.00 27.39 ?  272 ALA A N     1 
ATOM   2019 C CA    . ALA A 1 280 ? 18.374  27.994  19.589  1.00 28.39 ?  272 ALA A CA    1 
ATOM   2020 C C     . ALA A 1 280 ? 17.523  27.798  18.341  1.00 28.03 ?  272 ALA A C     1 
ATOM   2021 O O     . ALA A 1 280 ? 17.550  28.633  17.429  1.00 26.49 ?  272 ALA A O     1 
ATOM   2022 C CB    . ALA A 1 280 ? 19.650  27.156  19.505  1.00 27.80 ?  272 ALA A CB    1 
ATOM   2023 N N     . ILE A 1 281 ? 16.760  26.705  18.281  1.00 28.60 ?  273 ILE A N     1 
ATOM   2024 C CA    . ILE A 1 281 ? 15.946  26.438  17.100  1.00 28.36 ?  273 ILE A CA    1 
ATOM   2025 C C     . ILE A 1 281 ? 14.783  27.421  17.014  1.00 27.71 ?  273 ILE A C     1 
ATOM   2026 O O     . ILE A 1 281 ? 14.431  27.887  15.924  1.00 28.19 ?  273 ILE A O     1 
ATOM   2027 C CB    . ILE A 1 281 ? 15.467  24.975  17.101  1.00 28.48 ?  273 ILE A CB    1 
ATOM   2028 C CG1   . ILE A 1 281 ? 16.655  24.037  16.887  1.00 26.76 ?  273 ILE A CG1   1 
ATOM   2029 C CG2   . ILE A 1 281 ? 14.411  24.750  16.029  1.00 25.56 ?  273 ILE A CG2   1 
ATOM   2030 C CD1   . ILE A 1 281 ? 16.351  22.585  17.167  1.00 23.46 ?  273 ILE A CD1   1 
ATOM   2031 N N     . TYR A 1 282 ? 14.173  27.757  18.154  1.00 27.79 ?  274 TYR A N     1 
ATOM   2032 C CA    . TYR A 1 282 ? 13.108  28.756  18.148  1.00 28.68 ?  274 TYR A CA    1 
ATOM   2033 C C     . TYR A 1 282 ? 13.618  30.094  17.632  1.00 29.72 ?  274 TYR A C     1 
ATOM   2034 O O     . TYR A 1 282 ? 12.973  30.742  16.800  1.00 31.79 ?  274 TYR A O     1 
ATOM   2035 C CB    . TYR A 1 282 ? 12.515  28.920  19.549  1.00 27.04 ?  274 TYR A CB    1 
ATOM   2036 C CG    . TYR A 1 282 ? 11.624  30.139  19.674  1.00 33.26 ?  274 TYR A CG    1 
ATOM   2037 C CD1   . TYR A 1 282 ? 10.302  30.101  19.249  1.00 34.59 ?  274 TYR A CD1   1 
ATOM   2038 C CD2   . TYR A 1 282 ? 12.106  31.328  20.211  1.00 30.99 ?  274 TYR A CD2   1 
ATOM   2039 C CE1   . TYR A 1 282 ? 9.485   31.213  19.356  1.00 36.35 ?  274 TYR A CE1   1 
ATOM   2040 C CE2   . TYR A 1 282 ? 11.297  32.444  20.320  1.00 33.22 ?  274 TYR A CE2   1 
ATOM   2041 C CZ    . TYR A 1 282 ? 9.987   32.381  19.892  1.00 38.97 ?  274 TYR A CZ    1 
ATOM   2042 O OH    . TYR A 1 282 ? 9.178   33.490  20.000  1.00 43.35 ?  274 TYR A OH    1 
ATOM   2043 N N     . ALA A 1 283 ? 14.779  30.528  18.126  1.00 29.40 ?  275 ALA A N     1 
ATOM   2044 C CA    . ALA A 1 283 ? 15.355  31.788  17.671  1.00 29.92 ?  275 ALA A CA    1 
ATOM   2045 C C     . ALA A 1 283 ? 15.748  31.716  16.203  1.00 29.26 ?  275 ALA A C     1 
ATOM   2046 O O     . ALA A 1 283 ? 15.619  32.704  15.471  1.00 29.72 ?  275 ALA A O     1 
ATOM   2047 C CB    . ALA A 1 283 ? 16.563  32.152  18.533  1.00 27.20 ?  275 ALA A CB    1 
ATOM   2048 N N     . ALA A 1 284 ? 16.228  30.555  15.754  1.00 26.10 ?  276 ALA A N     1 
ATOM   2049 C CA    . ALA A 1 284 ? 16.597  30.405  14.351  1.00 28.75 ?  276 ALA A CA    1 
ATOM   2050 C C     . ALA A 1 284 ? 15.374  30.504  13.448  1.00 28.16 ?  276 ALA A C     1 
ATOM   2051 O O     . ALA A 1 284 ? 15.437  31.104  12.369  1.00 30.18 ?  276 ALA A O     1 
ATOM   2052 C CB    . ALA A 1 284 ? 17.320  29.076  14.135  1.00 29.08 ?  276 ALA A CB    1 
ATOM   2053 N N     . ILE A 1 285 ? 14.251  29.924  13.876  1.00 27.77 ?  277 ILE A N     1 
ATOM   2054 C CA    . ILE A 1 285 ? 13.032  29.971  13.074  1.00 29.37 ?  277 ILE A CA    1 
ATOM   2055 C C     . ILE A 1 285 ? 12.501  31.398  12.991  1.00 31.93 ?  277 ILE A C     1 
ATOM   2056 O O     . ILE A 1 285 ? 12.097  31.864  11.919  1.00 32.83 ?  277 ILE A O     1 
ATOM   2057 C CB    . ILE A 1 285 ? 11.978  29.005  13.644  1.00 29.50 ?  277 ILE A CB    1 
ATOM   2058 C CG1   . ILE A 1 285 ? 12.428  27.557  13.449  1.00 22.66 ?  277 ILE A CG1   1 
ATOM   2059 C CG2   . ILE A 1 285 ? 10.625  29.235  12.986  1.00 32.68 ?  277 ILE A CG2   1 
ATOM   2060 C CD1   . ILE A 1 285 ? 11.492  26.542  14.054  1.00 25.97 ?  277 ILE A CD1   1 
ATOM   2061 N N     . GLN A 1 286 ? 12.491  32.110  14.123  1.00 37.26 ?  278 GLN A N     1 
ATOM   2062 C CA    . GLN A 1 286 ? 12.075  33.510  14.118  1.00 33.29 ?  278 GLN A CA    1 
ATOM   2063 C C     . GLN A 1 286 ? 12.930  34.332  13.163  1.00 35.69 ?  278 GLN A C     1 
ATOM   2064 O O     . GLN A 1 286 ? 12.412  35.174  12.419  1.00 33.23 ?  278 GLN A O     1 
ATOM   2065 C CB    . GLN A 1 286 ? 12.150  34.085  15.533  1.00 27.48 ?  278 GLN A CB    1 
ATOM   2066 C CG    . GLN A 1 286 ? 11.866  35.576  15.617  1.00 34.62 ?  278 GLN A CG    1 
ATOM   2067 C CD    . GLN A 1 286 ? 12.222  36.160  16.972  1.00 39.61 ?  278 GLN A CD    1 
ATOM   2068 O OE1   . GLN A 1 286 ? 12.964  37.140  17.064  1.00 42.21 ?  278 GLN A OE1   1 
ATOM   2069 N NE2   . GLN A 1 286 ? 11.693  35.560  18.033  1.00 42.93 ?  278 GLN A NE2   1 
ATOM   2070 N N     . LYS A 1 287 ? 14.243  34.097  13.166  1.00 30.46 ?  279 LYS A N     1 
ATOM   2071 C CA    . LYS A 1 287 ? 15.116  34.773  12.212  1.00 30.85 ?  279 LYS A CA    1 
ATOM   2072 C C     . LYS A 1 287 ? 14.852  34.294  10.790  1.00 36.00 ?  279 LYS A C     1 
ATOM   2073 O O     . LYS A 1 287 ? 14.928  35.082  9.839   1.00 35.23 ?  279 LYS A O     1 
ATOM   2074 C CB    . LYS A 1 287 ? 16.579  34.551  12.597  1.00 31.84 ?  279 LYS A CB    1 
ATOM   2075 C CG    . LYS A 1 287 ? 17.581  35.186  11.647  1.00 28.69 ?  279 LYS A CG    1 
ATOM   2076 C CD    . LYS A 1 287 ? 17.485  36.703  11.665  1.00 37.09 ?  279 LYS A CD    1 
ATOM   2077 C CE    . LYS A 1 287 ? 17.623  37.251  13.075  1.00 34.06 ?  279 LYS A CE    1 
ATOM   2078 N NZ    . LYS A 1 287 ? 17.526  38.734  13.092  1.00 36.81 ?  279 LYS A NZ    1 
ATOM   2079 N N     . ALA A 1 288 ? 14.533  33.008  10.623  1.00 29.79 ?  280 ALA A N     1 
ATOM   2080 C CA    . ALA A 1 288 ? 14.245  32.486  9.291   1.00 34.65 ?  280 ALA A CA    1 
ATOM   2081 C C     . ALA A 1 288 ? 12.986  33.117  8.709   1.00 36.44 ?  280 ALA A C     1 
ATOM   2082 O O     . ALA A 1 288 ? 12.912  33.374  7.502   1.00 35.05 ?  280 ALA A O     1 
ATOM   2083 C CB    . ALA A 1 288 ? 14.108  30.965  9.340   1.00 31.46 ?  280 ALA A CB    1 
ATOM   2084 N N     . LYS A 1 289 ? 11.982  33.371  9.551   1.00 34.07 ?  281 LYS A N     1 
ATOM   2085 C CA    . LYS A 1 289 ? 10.773  34.031  9.074   1.00 43.16 ?  281 LYS A CA    1 
ATOM   2086 C C     . LYS A 1 289 ? 11.041  35.478  8.685   1.00 38.70 ?  281 LYS A C     1 
ATOM   2087 O O     . LYS A 1 289 ? 10.412  35.995  7.755   1.00 38.89 ?  281 LYS A O     1 
ATOM   2088 C CB    . LYS A 1 289 ? 9.678   33.957  10.138  1.00 40.18 ?  281 LYS A CB    1 
ATOM   2089 C CG    . LYS A 1 289 ? 8.924   32.639  10.149  1.00 35.82 ?  281 LYS A CG    1 
ATOM   2090 C CD    . LYS A 1 289 ? 8.760   32.101  11.559  1.00 37.22 ?  281 LYS A CD    1 
ATOM   2091 C CE    . LYS A 1 289 ? 7.879   33.009  12.399  1.00 45.55 ?  281 LYS A CE    1 
ATOM   2092 N NZ    . LYS A 1 289 ? 6.830   32.239  13.124  1.00 48.69 ?  281 LYS A NZ    1 
ATOM   2093 N N     . GLU A 1 290 ? 11.967  36.144  9.377   1.00 42.24 ?  282 GLU A N     1 
ATOM   2094 C CA    . GLU A 1 290 ? 12.324  37.510  9.010   1.00 38.44 ?  282 GLU A CA    1 
ATOM   2095 C C     . GLU A 1 290 ? 13.115  37.540  7.708   1.00 41.07 ?  282 GLU A C     1 
ATOM   2096 O O     . GLU A 1 290 ? 12.927  38.439  6.880   1.00 40.65 ?  282 GLU A O     1 
ATOM   2097 C CB    . GLU A 1 290 ? 13.122  38.165  10.139  1.00 37.48 ?  282 GLU A CB    1 
ATOM   2098 C CG    . GLU A 1 290 ? 13.821  39.459  9.745   1.00 46.31 ?  282 GLU A CG    1 
ATOM   2099 C CD    . GLU A 1 290 ? 15.001  39.792  10.643  1.00 47.19 ?  282 GLU A CD    1 
ATOM   2100 O OE1   . GLU A 1 290 ? 14.962  39.442  11.843  1.00 38.14 ?  282 GLU A OE1   1 
ATOM   2101 O OE2   . GLU A 1 290 ? 15.974  40.400  10.146  1.00 52.37 ?  282 GLU A OE2   1 
ATOM   2102 N N     . LEU A 1 291 ? 13.995  36.558  7.504   1.00 38.44 ?  283 LEU A N     1 
ATOM   2103 C CA    . LEU A 1 291 ? 14.848  36.557  6.320   1.00 35.06 ?  283 LEU A CA    1 
ATOM   2104 C C     . LEU A 1 291 ? 14.081  36.140  5.072   1.00 39.61 ?  283 LEU A C     1 
ATOM   2105 O O     . LEU A 1 291 ? 14.264  36.733  4.004   1.00 37.79 ?  283 LEU A O     1 
ATOM   2106 C CB    . LEU A 1 291 ? 16.047  35.639  6.542   1.00 40.29 ?  283 LEU A CB    1 
ATOM   2107 C CG    . LEU A 1 291 ? 17.248  36.294  7.225   1.00 39.25 ?  283 LEU A CG    1 
ATOM   2108 C CD1   . LEU A 1 291 ? 18.342  35.270  7.473   1.00 34.43 ?  283 LEU A CD1   1 
ATOM   2109 C CD2   . LEU A 1 291 ? 17.771  37.457  6.398   1.00 36.34 ?  283 LEU A CD2   1 
ATOM   2110 N N     . GLY A 1 292 ? 13.235  35.122  5.182   1.00 36.08 ?  284 GLY A N     1 
ATOM   2111 C CA    . GLY A 1 292 ? 12.381  34.718  4.086   1.00 35.60 ?  284 GLY A CA    1 
ATOM   2112 C C     . GLY A 1 292 ? 12.966  33.596  3.249   1.00 39.95 ?  284 GLY A C     1 
ATOM   2113 O O     . GLY A 1 292 ? 14.117  33.183  3.402   1.00 40.05 ?  284 GLY A O     1 
ATOM   2114 N N     . LYS A 1 293 ? 12.134  33.102  2.334   1.00 36.45 ?  285 LYS A N     1 
ATOM   2115 C CA    . LYS A 1 293 ? 12.507  31.982  1.480   1.00 38.05 ?  285 LYS A CA    1 
ATOM   2116 C C     . LYS A 1 293 ? 13.756  32.309  0.669   1.00 43.60 ?  285 LYS A C     1 
ATOM   2117 O O     . LYS A 1 293 ? 13.931  33.434  0.191   1.00 43.16 ?  285 LYS A O     1 
ATOM   2118 C CB    . LYS A 1 293 ? 11.346  31.637  0.544   1.00 43.23 ?  285 LYS A CB    1 
ATOM   2119 C CG    . LYS A 1 293 ? 11.623  30.531  -0.460  1.00 47.00 ?  285 LYS A CG    1 
ATOM   2120 C CD    . LYS A 1 293 ? 10.326  30.093  -1.132  1.00 56.05 ?  285 LYS A CD    1 
ATOM   2121 C CE    . LYS A 1 293 ? 10.078  28.599  -0.991  1.00 60.67 ?  285 LYS A CE    1 
ATOM   2122 N NZ    . LYS A 1 293 ? 9.359   28.044  -2.177  1.00 60.62 ?  285 LYS A NZ    1 
ATOM   2123 N N     . GLY A 1 294 ? 14.633  31.314  0.523   1.00 40.69 ?  286 GLY A N     1 
ATOM   2124 C CA    . GLY A 1 294 ? 15.859  31.443  -0.226  1.00 44.80 ?  286 GLY A CA    1 
ATOM   2125 C C     . GLY A 1 294 ? 17.094  31.676  0.623   1.00 42.84 ?  286 GLY A C     1 
ATOM   2126 O O     . GLY A 1 294 ? 18.198  31.301  0.210   1.00 47.01 ?  286 GLY A O     1 
ATOM   2127 N N     . LYS A 1 295 ? 16.938  32.288  1.794   1.00 41.24 ?  287 LYS A N     1 
ATOM   2128 C CA    . LYS A 1 295 ? 18.066  32.566  2.667   1.00 36.11 ?  287 LYS A CA    1 
ATOM   2129 C C     . LYS A 1 295 ? 18.441  31.324  3.478   1.00 37.99 ?  287 LYS A C     1 
ATOM   2130 O O     . LYS A 1 295 ? 17.766  30.292  3.438   1.00 32.66 ?  287 LYS A O     1 
ATOM   2131 C CB    . LYS A 1 295 ? 17.747  33.744  3.585   1.00 36.12 ?  287 LYS A CB    1 
ATOM   2132 C CG    . LYS A 1 295 ? 17.332  35.003  2.837   1.00 36.28 ?  287 LYS A CG    1 
ATOM   2133 C CD    . LYS A 1 295 ? 18.537  35.690  2.209   1.00 43.00 ?  287 LYS A CD    1 
ATOM   2134 C CE    . LYS A 1 295 ? 18.130  36.569  1.036   1.00 50.32 ?  287 LYS A CE    1 
ATOM   2135 N NZ    . LYS A 1 295 ? 18.159  35.822  -0.252  1.00 54.08 ?  287 LYS A NZ    1 
ATOM   2136 N N     . THR A 1 296 ? 19.540  31.433  4.224   1.00 36.41 ?  288 THR A N     1 
ATOM   2137 C CA    . THR A 1 296 ? 20.099  30.306  4.960   1.00 31.82 ?  288 THR A CA    1 
ATOM   2138 C C     . THR A 1 296 ? 20.376  30.721  6.397   1.00 32.30 ?  288 THR A C     1 
ATOM   2139 O O     . THR A 1 296 ? 20.987  31.767  6.639   1.00 30.76 ?  288 THR A O     1 
ATOM   2140 C CB    . THR A 1 296 ? 21.384  29.799  4.295   1.00 38.26 ?  288 THR A CB    1 
ATOM   2141 O OG1   . THR A 1 296 ? 21.093  29.368  2.960   1.00 36.88 ?  288 THR A OG1   1 
ATOM   2142 C CG2   . THR A 1 296 ? 21.974  28.637  5.079   1.00 32.98 ?  288 THR A CG2   1 
ATOM   2143 N N     . VAL A 1 297 ? 19.931  29.897  7.344   1.00 33.51 ?  289 VAL A N     1 
ATOM   2144 C CA    . VAL A 1 297 ? 20.068  30.162  8.771   1.00 30.34 ?  289 VAL A CA    1 
ATOM   2145 C C     . VAL A 1 297 ? 20.697  28.942  9.433   1.00 28.69 ?  289 VAL A C     1 
ATOM   2146 O O     . VAL A 1 297 ? 20.267  27.808  9.191   1.00 25.69 ?  289 VAL A O     1 
ATOM   2147 C CB    . VAL A 1 297 ? 18.709  30.500  9.414   1.00 30.02 ?  289 VAL A CB    1 
ATOM   2148 C CG1   . VAL A 1 297 ? 18.786  30.401  10.922  1.00 26.71 ?  289 VAL A CG1   1 
ATOM   2149 C CG2   . VAL A 1 297 ? 18.265  31.894  8.997   1.00 31.40 ?  289 VAL A CG2   1 
ATOM   2150 N N     . VAL A 1 298 ? 21.715  29.171  10.260  1.00 25.05 ?  290 VAL A N     1 
ATOM   2151 C CA    . VAL A 1 298 ? 22.469  28.099  10.898  1.00 24.58 ?  290 VAL A CA    1 
ATOM   2152 C C     . VAL A 1 298 ? 22.518  28.346  12.400  1.00 25.40 ?  290 VAL A C     1 
ATOM   2153 O O     . VAL A 1 298 ? 22.741  29.477  12.847  1.00 26.55 ?  290 VAL A O     1 
ATOM   2154 C CB    . VAL A 1 298 ? 23.897  27.990  10.322  1.00 24.59 ?  290 VAL A CB    1 
ATOM   2155 C CG1   . VAL A 1 298 ? 24.688  26.906  11.043  1.00 24.87 ?  290 VAL A CG1   1 
ATOM   2156 C CG2   . VAL A 1 298 ? 23.849  27.725  8.828   1.00 31.31 ?  290 VAL A CG2   1 
ATOM   2157 N N     . THR A 1 299 ? 22.314  27.284  13.179  1.00 25.75 ?  291 THR A N     1 
ATOM   2158 C CA    . THR A 1 299 ? 22.452  27.342  14.626  1.00 22.53 ?  291 THR A CA    1 
ATOM   2159 C C     . THR A 1 299 ? 23.118  26.058  15.113  1.00 24.66 ?  291 THR A C     1 
ATOM   2160 O O     . THR A 1 299 ? 23.377  25.131  14.337  1.00 23.82 ?  291 THR A O     1 
ATOM   2161 C CB    . THR A 1 299 ? 21.097  27.564  15.308  1.00 24.58 ?  291 THR A CB    1 
ATOM   2162 O OG1   . THR A 1 299 ? 21.308  27.923  16.679  1.00 24.24 ?  291 THR A OG1   1 
ATOM   2163 C CG2   . THR A 1 299 ? 20.253  26.305  15.242  1.00 23.73 ?  291 THR A CG2   1 
ATOM   2164 N N     . VAL A 1 300 ? 23.395  26.009  16.415  1.00 24.47 ?  292 VAL A N     1 
ATOM   2165 C CA    . VAL A 1 300 ? 24.138  24.918  17.036  1.00 23.24 ?  292 VAL A CA    1 
ATOM   2166 C C     . VAL A 1 300 ? 23.263  24.274  18.103  1.00 25.32 ?  292 VAL A C     1 
ATOM   2167 O O     . VAL A 1 300 ? 22.651  24.975  18.916  1.00 26.25 ?  292 VAL A O     1 
ATOM   2168 C CB    . VAL A 1 300 ? 25.461  25.419  17.649  1.00 26.53 ?  292 VAL A CB    1 
ATOM   2169 C CG1   . VAL A 1 300 ? 25.987  24.431  18.682  1.00 23.06 ?  292 VAL A CG1   1 
ATOM   2170 C CG2   . VAL A 1 300 ? 26.495  25.672  16.560  1.00 23.07 ?  292 VAL A CG2   1 
ATOM   2171 N N     . LEU A 1 301 ? 23.210  22.938  18.101  1.00 25.40 ?  293 LEU A N     1 
ATOM   2172 C CA    . LEU A 1 301 ? 22.524  22.195  19.149  1.00 31.47 ?  293 LEU A CA    1 
ATOM   2173 C C     . LEU A 1 301 ? 23.556  21.653  20.128  1.00 28.56 ?  293 LEU A C     1 
ATOM   2174 O O     . LEU A 1 301 ? 24.269  20.694  19.793  1.00 26.91 ?  293 LEU A O     1 
ATOM   2175 C CB    . LEU A 1 301 ? 21.696  21.056  18.556  1.00 24.90 ?  293 LEU A CB    1 
ATOM   2176 C CG    . LEU A 1 301 ? 20.743  21.407  17.410  1.00 28.14 ?  293 LEU A CG    1 
ATOM   2177 C CD1   . LEU A 1 301 ? 19.744  20.285  17.180  1.00 22.76 ?  293 LEU A CD1   1 
ATOM   2178 C CD2   . LEU A 1 301 ? 20.016  22.715  17.681  1.00 23.16 ?  293 LEU A CD2   1 
ATOM   2179 N N     . PRO A 1 302 ? 23.674  22.218  21.333  1.00 26.67 ?  294 PRO A N     1 
ATOM   2180 C CA    . PRO A 1 302 ? 24.827  21.875  22.184  1.00 25.73 ?  294 PRO A CA    1 
ATOM   2181 C C     . PRO A 1 302 ? 24.773  20.486  22.797  1.00 25.14 ?  294 PRO A C     1 
ATOM   2182 O O     . PRO A 1 302 ? 25.822  19.841  22.921  1.00 19.71 ?  294 PRO A O     1 
ATOM   2183 C CB    . PRO A 1 302 ? 24.792  22.973  23.257  1.00 27.62 ?  294 PRO A CB    1 
ATOM   2184 C CG    . PRO A 1 302 ? 24.093  24.115  22.587  1.00 25.09 ?  294 PRO A CG    1 
ATOM   2185 C CD    . PRO A 1 302 ? 23.004  23.439  21.809  1.00 28.35 ?  294 PRO A CD    1 
ATOM   2186 N N     . SER A 1 303 ? 23.598  19.998  23.197  1.00 24.09 ?  295 SER A N     1 
ATOM   2187 C CA    . SER A 1 303 ? 23.525  18.743  23.932  1.00 26.26 ?  295 SER A CA    1 
ATOM   2188 C C     . SER A 1 303 ? 22.292  17.951  23.516  1.00 27.99 ?  295 SER A C     1 
ATOM   2189 O O     . SER A 1 303 ? 21.377  18.465  22.867  1.00 25.73 ?  295 SER A O     1 
ATOM   2190 C CB    . SER A 1 303 ? 23.512  18.986  25.445  1.00 26.31 ?  295 SER A CB    1 
ATOM   2191 O OG    . SER A 1 303 ? 22.386  19.757  25.821  1.00 27.99 ?  295 SER A OG    1 
ATOM   2192 N N     . ASN A 1 304 ? 22.277  16.683  23.922  1.00 27.38 ?  296 ASN A N     1 
ATOM   2193 C CA    . ASN A 1 304 ? 21.224  15.740  23.580  1.00 26.60 ?  296 ASN A CA    1 
ATOM   2194 C C     . ASN A 1 304 ? 20.145  15.703  24.658  1.00 30.41 ?  296 ASN A C     1 
ATOM   2195 O O     . ASN A 1 304 ? 20.420  15.869  25.850  1.00 27.13 ?  296 ASN A O     1 
ATOM   2196 C CB    . ASN A 1 304 ? 21.810  14.339  23.390  1.00 25.48 ?  296 ASN A CB    1 
ATOM   2197 C CG    . ASN A 1 304 ? 20.875  13.412  22.647  1.00 31.32 ?  296 ASN A CG    1 
ATOM   2198 O OD1   . ASN A 1 304 ? 19.981  12.808  23.239  1.00 29.81 ?  296 ASN A OD1   1 
ATOM   2199 N ND2   . ASN A 1 304 ? 21.080  13.289  21.342  1.00 31.25 ?  296 ASN A ND2   1 
ATOM   2200 N N     . GLY A 1 305 ? 18.907  15.460  24.222  1.00 27.90 ?  297 GLY A N     1 
ATOM   2201 C CA    . GLY A 1 305 ? 17.774  15.409  25.132  1.00 27.59 ?  297 GLY A CA    1 
ATOM   2202 C C     . GLY A 1 305 ? 17.819  14.270  26.130  1.00 29.76 ?  297 GLY A C     1 
ATOM   2203 O O     . GLY A 1 305 ? 17.208  14.374  27.200  1.00 30.65 ?  297 GLY A O     1 
ATOM   2204 N N     . GLU A 1 306 ? 18.524  13.182  25.805  1.00 32.62 ?  298 GLU A N     1 
ATOM   2205 C CA    . GLU A 1 306 ? 18.609  12.058  26.734  1.00 27.37 ?  298 GLU A CA    1 
ATOM   2206 C C     . GLU A 1 306 ? 19.299  12.459  28.033  1.00 36.39 ?  298 GLU A C     1 
ATOM   2207 O O     . GLU A 1 306 ? 19.082  11.831  29.077  1.00 31.95 ?  298 GLU A O     1 
ATOM   2208 C CB    . GLU A 1 306 ? 19.346  10.888  26.078  1.00 30.77 ?  298 GLU A CB    1 
ATOM   2209 C CG    . GLU A 1 306 ? 19.358  9.591   26.876  1.00 32.78 ?  298 GLU A CG    1 
ATOM   2210 C CD    . GLU A 1 306 ? 19.907  8.424   26.071  1.00 31.81 ?  298 GLU A CD    1 
ATOM   2211 O OE1   . GLU A 1 306 ? 20.002  8.555   24.833  1.00 33.03 ?  298 GLU A OE1   1 
ATOM   2212 O OE2   . GLU A 1 306 ? 20.245  7.380   26.670  1.00 30.70 ?  298 GLU A OE2   1 
ATOM   2213 N N     . ARG A 1 307 ? 20.124  13.505  27.990  1.00 35.85 ?  299 ARG A N     1 
ATOM   2214 C CA    . ARG A 1 307 ? 20.769  14.024  29.187  1.00 32.04 ?  299 ARG A CA    1 
ATOM   2215 C C     . ARG A 1 307 ? 19.795  14.772  30.092  1.00 36.98 ?  299 ARG A C     1 
ATOM   2216 O O     . ARG A 1 307 ? 20.153  15.105  31.227  1.00 36.54 ?  299 ARG A O     1 
ATOM   2217 C CB    . ARG A 1 307 ? 21.936  14.927  28.771  1.00 27.73 ?  299 ARG A CB    1 
ATOM   2218 C CG    . ARG A 1 307 ? 22.832  15.397  29.898  1.00 30.14 ?  299 ARG A CG    1 
ATOM   2219 C CD    . ARG A 1 307 ? 24.183  15.834  29.370  1.00 29.26 ?  299 ARG A CD    1 
ATOM   2220 N NE    . ARG A 1 307 ? 24.985  14.704  28.918  1.00 26.42 ?  299 ARG A NE    1 
ATOM   2221 C CZ    . ARG A 1 307 ? 26.196  14.810  28.388  1.00 27.20 ?  299 ARG A CZ    1 
ATOM   2222 N NH1   . ARG A 1 307 ? 26.772  15.987  28.210  1.00 22.38 ?  299 ARG A NH1   1 
ATOM   2223 N NH2   . ARG A 1 307 ? 26.844  13.706  28.026  1.00 23.27 ?  299 ARG A NH2   1 
ATOM   2224 N N     . TYR A 1 308 ? 18.564  15.010  29.636  1.00 37.90 ?  300 TYR A N     1 
ATOM   2225 C CA    . TYR A 1 308 ? 17.596  15.816  30.370  1.00 35.07 ?  300 TYR A CA    1 
ATOM   2226 C C     . TYR A 1 308 ? 16.306  15.056  30.661  1.00 43.78 ?  300 TYR A C     1 
ATOM   2227 O O     . TYR A 1 308 ? 15.254  15.679  30.834  1.00 43.53 ?  300 TYR A O     1 
ATOM   2228 C CB    . TYR A 1 308 ? 17.290  17.098  29.595  1.00 34.87 ?  300 TYR A CB    1 
ATOM   2229 C CG    . TYR A 1 308 ? 18.522  17.898  29.241  1.00 40.77 ?  300 TYR A CG    1 
ATOM   2230 C CD1   . TYR A 1 308 ? 19.011  18.874  30.097  1.00 41.34 ?  300 TYR A CD1   1 
ATOM   2231 C CD2   . TYR A 1 308 ? 19.205  17.668  28.054  1.00 33.88 ?  300 TYR A CD2   1 
ATOM   2232 C CE1   . TYR A 1 308 ? 20.139  19.605  29.779  1.00 43.34 ?  300 TYR A CE1   1 
ATOM   2233 C CE2   . TYR A 1 308 ? 20.338  18.392  27.728  1.00 36.64 ?  300 TYR A CE2   1 
ATOM   2234 C CZ    . TYR A 1 308 ? 20.799  19.360  28.594  1.00 36.09 ?  300 TYR A CZ    1 
ATOM   2235 O OH    . TYR A 1 308 ? 21.924  20.088  28.280  1.00 36.17 ?  300 TYR A OH    1 
ATOM   2236 N N     . LEU A 1 309 ? 16.360  13.722  30.723  1.00 42.28 ?  301 LEU A N     1 
ATOM   2237 C CA    . LEU A 1 309 ? 15.148  12.944  30.967  1.00 46.49 ?  301 LEU A CA    1 
ATOM   2238 C C     . LEU A 1 309 ? 14.598  13.145  32.373  1.00 42.97 ?  301 LEU A C     1 
ATOM   2239 O O     . LEU A 1 309 ? 13.439  12.799  32.624  1.00 50.49 ?  301 LEU A O     1 
ATOM   2240 C CB    . LEU A 1 309 ? 15.407  11.455  30.724  1.00 40.55 ?  301 LEU A CB    1 
ATOM   2241 C CG    . LEU A 1 309 ? 15.998  11.047  29.372  1.00 40.70 ?  301 LEU A CG    1 
ATOM   2242 C CD1   . LEU A 1 309 ? 16.107  9.533   29.264  1.00 40.35 ?  301 LEU A CD1   1 
ATOM   2243 C CD2   . LEU A 1 309 ? 15.156  11.605  28.235  1.00 38.04 ?  301 LEU A CD2   1 
ATOM   2244 N N     . SER A 1 310 ? 15.395  13.692  33.291  1.00 49.81 ?  302 SER A N     1 
ATOM   2245 C CA    . SER A 1 310 ? 14.969  13.912  34.667  1.00 48.23 ?  302 SER A CA    1 
ATOM   2246 C C     . SER A 1 310 ? 14.672  15.379  34.953  1.00 51.02 ?  302 SER A C     1 
ATOM   2247 O O     . SER A 1 310 ? 14.632  15.788  36.117  1.00 51.14 ?  302 SER A O     1 
ATOM   2248 C CB    . SER A 1 310 ? 16.022  13.379  35.638  1.00 54.60 ?  302 SER A CB    1 
ATOM   2249 O OG    . SER A 1 310 ? 15.708  12.055  36.030  1.00 68.18 ?  302 SER A OG    1 
ATOM   2250 N N     . THR A 1 311 ? 14.471  16.175  33.917  1.00 38.37 ?  303 THR A N     1 
ATOM   2251 C CA    . THR A 1 311 ? 14.031  17.552  34.021  1.00 41.18 ?  303 THR A CA    1 
ATOM   2252 C C     . THR A 1 311 ? 12.608  17.678  33.497  1.00 43.86 ?  303 THR A C     1 
ATOM   2253 O O     . THR A 1 311 ? 12.090  16.769  32.839  1.00 47.22 ?  303 THR A O     1 
ATOM   2254 C CB    . THR A 1 311 ? 14.969  18.473  33.230  1.00 43.16 ?  303 THR A CB    1 
ATOM   2255 O OG1   . THR A 1 311 ? 14.805  18.235  31.827  1.00 42.27 ?  303 THR A OG1   1 
ATOM   2256 C CG2   . THR A 1 311 ? 16.415  18.223  33.620  1.00 43.52 ?  303 THR A CG2   1 
ATOM   2257 N N     . PRO A 1 312 ? 11.930  18.794  33.786  1.00 46.65 ?  304 PRO A N     1 
ATOM   2258 C CA    . PRO A 1 312 ? 10.590  19.007  33.210  1.00 44.43 ?  304 PRO A CA    1 
ATOM   2259 C C     . PRO A 1 312 ? 10.566  19.030  31.686  1.00 45.55 ?  304 PRO A C     1 
ATOM   2260 O O     . PRO A 1 312 ? 9.471   19.061  31.109  1.00 42.43 ?  304 PRO A O     1 
ATOM   2261 C CB    . PRO A 1 312 ? 10.161  20.368  33.784  1.00 35.67 ?  304 PRO A CB    1 
ATOM   2262 C CG    . PRO A 1 312 ? 11.333  20.892  34.562  1.00 48.21 ?  304 PRO A CG    1 
ATOM   2263 C CD    . PRO A 1 312 ? 12.222  19.743  34.872  1.00 42.50 ?  304 PRO A CD    1 
ATOM   2264 N N     . LEU A 1 313 ? 11.726  19.016  31.022  1.00 39.46 ?  305 LEU A N     1 
ATOM   2265 C CA    . LEU A 1 313 ? 11.753  19.081  29.563  1.00 41.54 ?  305 LEU A CA    1 
ATOM   2266 C C     . LEU A 1 313 ? 11.053  17.881  28.935  1.00 42.21 ?  305 LEU A C     1 
ATOM   2267 O O     . LEU A 1 313 ? 10.296  18.032  27.969  1.00 40.73 ?  305 LEU A O     1 
ATOM   2268 C CB    . LEU A 1 313 ? 13.200  19.175  29.072  1.00 39.38 ?  305 LEU A CB    1 
ATOM   2269 C CG    . LEU A 1 313 ? 13.450  19.121  27.561  1.00 35.10 ?  305 LEU A CG    1 
ATOM   2270 C CD1   . LEU A 1 313 ? 12.595  20.141  26.824  1.00 35.85 ?  305 LEU A CD1   1 
ATOM   2271 C CD2   . LEU A 1 313 ? 14.924  19.331  27.245  1.00 31.03 ?  305 LEU A CD2   1 
ATOM   2272 N N     . TYR A 1 314 ? 11.287  16.680  29.470  1.00 38.61 ?  306 TYR A N     1 
ATOM   2273 C CA    . TYR A 1 314 ? 10.728  15.465  28.890  1.00 41.56 ?  306 TYR A CA    1 
ATOM   2274 C C     . TYR A 1 314 ? 10.020  14.603  29.929  1.00 47.29 ?  306 TYR A C     1 
ATOM   2275 O O     . TYR A 1 314 ? 9.904   13.388  29.743  1.00 46.05 ?  306 TYR A O     1 
ATOM   2276 C CB    . TYR A 1 314 ? 11.819  14.654  28.185  1.00 36.23 ?  306 TYR A CB    1 
ATOM   2277 C CG    . TYR A 1 314 ? 12.383  15.338  26.960  1.00 35.04 ?  306 TYR A CG    1 
ATOM   2278 C CD1   . TYR A 1 314 ? 11.547  15.787  25.944  1.00 34.01 ?  306 TYR A CD1   1 
ATOM   2279 C CD2   . TYR A 1 314 ? 13.750  15.539  26.818  1.00 32.70 ?  306 TYR A CD2   1 
ATOM   2280 C CE1   . TYR A 1 314 ? 12.055  16.415  24.822  1.00 32.06 ?  306 TYR A CE1   1 
ATOM   2281 C CE2   . TYR A 1 314 ? 14.269  16.167  25.699  1.00 30.61 ?  306 TYR A CE2   1 
ATOM   2282 C CZ    . TYR A 1 314 ? 13.416  16.604  24.706  1.00 35.18 ?  306 TYR A CZ    1 
ATOM   2283 O OH    . TYR A 1 314 ? 13.924  17.228  23.589  1.00 30.35 ?  306 TYR A OH    1 
ATOM   2284 N N     . SER A 1 315 ? 9.541   15.200  31.015  1.00 49.38 ?  307 SER A N     1 
ATOM   2285 C CA    . SER A 1 315 ? 8.827   14.451  32.040  1.00 51.24 ?  307 SER A CA    1 
ATOM   2286 C C     . SER A 1 315 ? 7.387   14.937  32.161  1.00 53.58 ?  307 SER A C     1 
ATOM   2287 O O     . SER A 1 315 ? 7.138   16.082  32.538  1.00 64.04 ?  307 SER A O     1 
ATOM   2288 C CB    . SER A 1 315 ? 9.543   14.567  33.388  1.00 47.60 ?  307 SER A CB    1 
ATOM   2289 O OG    . SER A 1 315 ? 8.669   15.046  34.395  1.00 59.46 ?  307 SER A OG    1 
ATOM   2290 N N     . MET B 1 9   ? 37.070  19.005  9.004   1.00 61.42 ?  1   MET D N     1 
ATOM   2291 C CA    . MET B 1 9   ? 36.437  18.062  8.088   1.00 63.25 ?  1   MET D CA    1 
ATOM   2292 C C     . MET B 1 9   ? 35.227  17.384  8.727   1.00 60.64 ?  1   MET D C     1 
ATOM   2293 O O     . MET B 1 9   ? 35.368  16.584  9.653   1.00 59.18 ?  1   MET D O     1 
ATOM   2294 C CB    . MET B 1 9   ? 37.446  17.008  7.624   1.00 62.69 ?  1   MET D CB    1 
ATOM   2295 C CG    . MET B 1 9   ? 36.846  15.880  6.789   1.00 70.15 ?  1   MET D CG    1 
ATOM   2296 S SD    . MET B 1 9   ? 37.158  16.060  5.019   1.00 82.16 ?  1   MET D SD    1 
ATOM   2297 C CE    . MET B 1 9   ? 35.531  16.499  4.409   1.00 62.96 ?  1   MET D CE    1 
ATOM   2298 N N     . ALA B 1 10  ? 34.040  17.709  8.220   1.00 62.02 ?  2   ALA D N     1 
ATOM   2299 C CA    . ALA B 1 10  ? 32.785  17.147  8.693   1.00 50.73 ?  2   ALA D CA    1 
ATOM   2300 C C     . ALA B 1 10  ? 31.924  16.759  7.498   1.00 46.19 ?  2   ALA D C     1 
ATOM   2301 O O     . ALA B 1 10  ? 32.243  17.069  6.347   1.00 49.12 ?  2   ALA D O     1 
ATOM   2302 C CB    . ALA B 1 10  ? 32.034  18.135  9.595   1.00 32.89 ?  2   ALA D CB    1 
ATOM   2303 N N     . GLN B 1 11  ? 30.817  16.078  7.781   1.00 43.01 ?  3   GLN D N     1 
ATOM   2304 C CA    . GLN B 1 11  ? 29.905  15.644  6.732   1.00 37.62 ?  3   GLN D CA    1 
ATOM   2305 C C     . GLN B 1 11  ? 29.071  16.814  6.224   1.00 35.54 ?  3   GLN D C     1 
ATOM   2306 O O     . GLN B 1 11  ? 28.680  17.698  6.991   1.00 36.13 ?  3   GLN D O     1 
ATOM   2307 C CB    . GLN B 1 11  ? 28.984  14.535  7.243   1.00 40.64 ?  3   GLN D CB    1 
ATOM   2308 C CG    . GLN B 1 11  ? 29.682  13.496  8.101   1.00 52.63 ?  3   GLN D CG    1 
ATOM   2309 C CD    . GLN B 1 11  ? 28.709  12.628  8.876   1.00 60.72 ?  3   GLN D CD    1 
ATOM   2310 O OE1   . GLN B 1 11  ? 27.656  12.247  8.364   1.00 54.79 ?  3   GLN D OE1   1 
ATOM   2311 N NE2   . GLN B 1 11  ? 29.059  12.311  10.118  1.00 51.09 ?  3   GLN D NE2   1 
ATOM   2312 N N     . LYS B 1 12  ? 28.798  16.809  4.918   1.00 40.84 ?  4   LYS D N     1 
ATOM   2313 C CA    . LYS B 1 12  ? 27.977  17.845  4.317   1.00 39.40 ?  4   LYS D CA    1 
ATOM   2314 C C     . LYS B 1 12  ? 26.558  17.783  4.884   1.00 33.01 ?  4   LYS D C     1 
ATOM   2315 O O     . LYS B 1 12  ? 26.117  16.735  5.363   1.00 36.23 ?  4   LYS D O     1 
ATOM   2316 C CB    . LYS B 1 12  ? 27.957  17.686  2.796   1.00 36.88 ?  4   LYS D CB    1 
ATOM   2317 C CG    . LYS B 1 12  ? 29.282  18.015  2.123   1.00 39.13 ?  4   LYS D CG    1 
ATOM   2318 C CD    . LYS B 1 12  ? 29.484  19.517  1.989   1.00 40.21 ?  4   LYS D CD    1 
ATOM   2319 C CE    . LYS B 1 12  ? 30.916  19.848  1.598   1.00 41.05 ?  4   LYS D CE    1 
ATOM   2320 N NZ    . LYS B 1 12  ? 30.991  20.517  0.269   1.00 49.56 ?  4   LYS D NZ    1 
ATOM   2321 N N     . PRO B 1 13  ? 25.831  18.902  4.856   1.00 37.13 ?  5   PRO D N     1 
ATOM   2322 C CA    . PRO B 1 13  ? 24.488  18.921  5.450   1.00 31.29 ?  5   PRO D CA    1 
ATOM   2323 C C     . PRO B 1 13  ? 23.564  17.906  4.790   1.00 31.50 ?  5   PRO D C     1 
ATOM   2324 O O     . PRO B 1 13  ? 23.593  17.707  3.574   1.00 36.02 ?  5   PRO D O     1 
ATOM   2325 C CB    . PRO B 1 13  ? 24.011  20.357  5.205   1.00 29.53 ?  5   PRO D CB    1 
ATOM   2326 C CG    . PRO B 1 13  ? 25.261  21.152  5.039   1.00 34.37 ?  5   PRO D CG    1 
ATOM   2327 C CD    . PRO B 1 13  ? 26.239  20.233  4.374   1.00 34.55 ?  5   PRO D CD    1 
ATOM   2328 N N     . VAL B 1 14  ? 22.741  17.260  5.615   1.00 26.56 ?  6   VAL D N     1 
ATOM   2329 C CA    . VAL B 1 14  ? 21.797  16.249  5.162   1.00 29.19 ?  6   VAL D CA    1 
ATOM   2330 C C     . VAL B 1 14  ? 20.380  16.734  5.440   1.00 29.40 ?  6   VAL D C     1 
ATOM   2331 O O     . VAL B 1 14  ? 20.144  17.602  6.283   1.00 29.27 ?  6   VAL D O     1 
ATOM   2332 C CB    . VAL B 1 14  ? 22.047  14.880  5.829   1.00 27.28 ?  6   VAL D CB    1 
ATOM   2333 C CG1   . VAL B 1 14  ? 23.469  14.410  5.562   1.00 28.88 ?  6   VAL D CG1   1 
ATOM   2334 C CG2   . VAL B 1 14  ? 21.788  14.968  7.324   1.00 29.58 ?  6   VAL D CG2   1 
ATOM   2335 N N     . ASP B 1 15  ? 19.426  16.155  4.706   1.00 33.26 ?  7   ASP D N     1 
ATOM   2336 C CA    . ASP B 1 15  ? 18.029  16.547  4.851   1.00 30.88 ?  7   ASP D CA    1 
ATOM   2337 C C     . ASP B 1 15  ? 17.385  15.934  6.088   1.00 31.77 ?  7   ASP D C     1 
ATOM   2338 O O     . ASP B 1 15  ? 16.480  16.539  6.674   1.00 28.76 ?  7   ASP D O     1 
ATOM   2339 C CB    . ASP B 1 15  ? 17.233  16.138  3.608   1.00 34.97 ?  7   ASP D CB    1 
ATOM   2340 C CG    . ASP B 1 15  ? 17.378  17.125  2.463   1.00 45.22 ?  7   ASP D CG    1 
ATOM   2341 O OD1   . ASP B 1 15  ? 17.406  18.348  2.719   1.00 45.16 ?  7   ASP D OD1   1 
ATOM   2342 O OD2   . ASP B 1 15  ? 17.463  16.673  1.301   1.00 53.36 ?  7   ASP D OD2   1 
ATOM   2343 N N     . ASN B 1 16  ? 17.836  14.751  6.498   1.00 31.98 ?  8   ASN D N     1 
ATOM   2344 C CA    . ASN B 1 16  ? 17.163  13.976  7.529   1.00 31.71 ?  8   ASN D CA    1 
ATOM   2345 C C     . ASN B 1 16  ? 18.192  13.428  8.507   1.00 29.77 ?  8   ASN D C     1 
ATOM   2346 O O     . ASN B 1 16  ? 19.309  13.083  8.115   1.00 30.16 ?  8   ASN D O     1 
ATOM   2347 C CB    . ASN B 1 16  ? 16.358  12.828  6.905   1.00 25.51 ?  8   ASN D CB    1 
ATOM   2348 C CG    . ASN B 1 16  ? 15.395  12.190  7.881   1.00 26.61 ?  8   ASN D CG    1 
ATOM   2349 O OD1   . ASN B 1 16  ? 15.799  11.464  8.788   1.00 27.97 ?  8   ASN D OD1   1 
ATOM   2350 N ND2   . ASN B 1 16  ? 14.108  12.450  7.692   1.00 36.31 ?  8   ASN D ND2   1 
ATOM   2351 N N     . ILE B 1 17  ? 17.803  13.338  9.782   1.00 27.82 ?  9   ILE D N     1 
ATOM   2352 C CA    . ILE B 1 17  ? 18.726  12.879  10.817  1.00 29.63 ?  9   ILE D CA    1 
ATOM   2353 C C     . ILE B 1 17  ? 19.151  11.435  10.579  1.00 31.10 ?  9   ILE D C     1 
ATOM   2354 O O     . ILE B 1 17  ? 20.273  11.045  10.925  1.00 30.30 ?  9   ILE D O     1 
ATOM   2355 C CB    . ILE B 1 17  ? 18.094  13.070  12.213  1.00 26.55 ?  9   ILE D CB    1 
ATOM   2356 C CG1   . ILE B 1 17  ? 19.032  12.577  13.316  1.00 32.66 ?  9   ILE D CG1   1 
ATOM   2357 C CG2   . ILE B 1 17  ? 16.764  12.356  12.305  1.00 28.96 ?  9   ILE D CG2   1 
ATOM   2358 C CD1   . ILE B 1 17  ? 20.315  13.339  13.408  1.00 31.83 ?  9   ILE D CD1   1 
ATOM   2359 N N     . THR B 1 18  ? 18.282  10.623  9.972   1.00 27.32 ?  10  THR D N     1 
ATOM   2360 C CA    . THR B 1 18  ? 18.637  9.233   9.711   1.00 29.93 ?  10  THR D CA    1 
ATOM   2361 C C     . THR B 1 18  ? 19.780  9.100   8.713   1.00 28.92 ?  10  THR D C     1 
ATOM   2362 O O     . THR B 1 18  ? 20.406  8.037   8.644   1.00 28.14 ?  10  THR D O     1 
ATOM   2363 C CB    . THR B 1 18  ? 17.418  8.458   9.203   1.00 31.98 ?  10  THR D CB    1 
ATOM   2364 O OG1   . THR B 1 18  ? 17.007  8.983   7.932   1.00 32.76 ?  10  THR D OG1   1 
ATOM   2365 C CG2   . THR B 1 18  ? 16.271  8.567   10.191  1.00 28.23 ?  10  THR D CG2   1 
ATOM   2366 N N     . GLN B 1 19  ? 20.076  10.154  7.950   1.00 31.17 ?  11  GLN D N     1 
ATOM   2367 C CA    . GLN B 1 19  ? 21.098  10.073  6.916   1.00 34.22 ?  11  GLN D CA    1 
ATOM   2368 C C     . GLN B 1 19  ? 22.509  10.012  7.480   1.00 35.22 ?  11  GLN D C     1 
ATOM   2369 O O     . GLN B 1 19  ? 23.448  9.745   6.721   1.00 36.90 ?  11  GLN D O     1 
ATOM   2370 C CB    . GLN B 1 19  ? 20.980  11.258  5.960   1.00 33.38 ?  11  GLN D CB    1 
ATOM   2371 C CG    . GLN B 1 19  ? 19.790  11.171  5.025   1.00 31.01 ?  11  GLN D CG    1 
ATOM   2372 C CD    . GLN B 1 19  ? 19.832  12.221  3.940   1.00 38.28 ?  11  GLN D CD    1 
ATOM   2373 O OE1   . GLN B 1 19  ? 19.111  13.216  3.995   1.00 41.79 ?  11  GLN D OE1   1 
ATOM   2374 N NE2   . GLN B 1 19  ? 20.686  12.008  2.944   1.00 41.91 ?  11  GLN D NE2   1 
ATOM   2375 N N     . ILE B 1 20  ? 22.691  10.261  8.775   1.00 32.35 ?  12  ILE D N     1 
ATOM   2376 C CA    . ILE B 1 20  ? 24.014  10.181  9.374   1.00 38.44 ?  12  ILE D CA    1 
ATOM   2377 C C     . ILE B 1 20  ? 24.121  8.994   10.326  1.00 34.75 ?  12  ILE D C     1 
ATOM   2378 O O     . ILE B 1 20  ? 25.109  8.873   11.060  1.00 29.05 ?  12  ILE D O     1 
ATOM   2379 C CB    . ILE B 1 20  ? 24.436  11.525  10.025  1.00 42.87 ?  12  ILE D CB    1 
ATOM   2380 C CG1   . ILE B 1 20  ? 23.534  12.018  11.179  1.00 40.02 ?  12  ILE D CG1   1 
ATOM   2381 C CG2   . ILE B 1 20  ? 24.494  12.633  8.953   1.00 42.43 ?  12  ILE D CG2   1 
ATOM   2382 C CD1   . ILE B 1 20  ? 23.781  11.393  12.553  1.00 37.40 ?  12  ILE D CD1   1 
ATOM   2383 N N     . ILE B 1 21  ? 23.138  8.085   10.292  1.00 27.90 ?  13  ILE D N     1 
ATOM   2384 C CA    . ILE B 1 21  ? 23.290  6.770   10.904  1.00 26.14 ?  13  ILE D CA    1 
ATOM   2385 C C     . ILE B 1 21  ? 24.388  6.006   10.181  1.00 26.60 ?  13  ILE D C     1 
ATOM   2386 O O     . ILE B 1 21  ? 24.419  5.946   8.946   1.00 29.17 ?  13  ILE D O     1 
ATOM   2387 C CB    . ILE B 1 21  ? 21.963  5.994   10.854  1.00 24.40 ?  13  ILE D CB    1 
ATOM   2388 C CG1   . ILE B 1 21  ? 20.911  6.646   11.749  1.00 26.83 ?  13  ILE D CG1   1 
ATOM   2389 C CG2   . ILE B 1 21  ? 22.177  4.539   11.247  1.00 28.87 ?  13  ILE D CG2   1 
ATOM   2390 C CD1   . ILE B 1 21  ? 19.524  6.064   11.580  1.00 26.47 ?  13  ILE D CD1   1 
ATOM   2391 N N     . GLY B 1 22  ? 25.296  5.417   10.948  1.00 25.65 ?  14  GLY D N     1 
ATOM   2392 C CA    . GLY B 1 22  ? 26.367  4.614   10.392  1.00 30.78 ?  14  GLY D CA    1 
ATOM   2393 C C     . GLY B 1 22  ? 27.690  5.353   10.380  1.00 26.62 ?  14  GLY D C     1 
ATOM   2394 O O     . GLY B 1 22  ? 27.815  6.500   10.822  1.00 29.11 ?  14  GLY D O     1 
ATOM   2395 N N     . GLY B 1 23  ? 28.696  4.662   9.852   1.00 31.96 ?  15  GLY D N     1 
ATOM   2396 C CA    . GLY B 1 23  ? 30.040  5.201   9.787   1.00 30.52 ?  15  GLY D CA    1 
ATOM   2397 C C     . GLY B 1 23  ? 30.623  5.500   11.152  1.00 28.03 ?  15  GLY D C     1 
ATOM   2398 O O     . GLY B 1 23  ? 31.143  6.594   11.386  1.00 29.96 ?  15  GLY D O     1 
ATOM   2399 N N     . THR B 1 24  ? 30.543  4.533   12.060  1.00 28.76 ?  16  THR D N     1 
ATOM   2400 C CA    . THR B 1 24  ? 30.979  4.743   13.431  1.00 28.78 ?  16  THR D CA    1 
ATOM   2401 C C     . THR B 1 24  ? 32.490  4.543   13.560  1.00 31.83 ?  16  THR D C     1 
ATOM   2402 O O     . THR B 1 24  ? 33.074  3.704   12.869  1.00 30.75 ?  16  THR D O     1 
ATOM   2403 C CB    . THR B 1 24  ? 30.243  3.792   14.369  1.00 29.84 ?  16  THR D CB    1 
ATOM   2404 O OG1   . THR B 1 24  ? 30.515  2.436   13.998  1.00 28.60 ?  16  THR D OG1   1 
ATOM   2405 C CG2   . THR B 1 24  ? 28.739  4.040   14.301  1.00 27.42 ?  16  THR D CG2   1 
ATOM   2406 N N     . PRO B 1 25  ? 33.143  5.300   14.438  1.00 30.57 ?  17  PRO D N     1 
ATOM   2407 C CA    . PRO B 1 25  ? 34.603  5.230   14.542  1.00 35.25 ?  17  PRO D CA    1 
ATOM   2408 C C     . PRO B 1 25  ? 35.062  4.011   15.334  1.00 34.45 ?  17  PRO D C     1 
ATOM   2409 O O     . PRO B 1 25  ? 34.274  3.288   15.944  1.00 33.44 ?  17  PRO D O     1 
ATOM   2410 C CB    . PRO B 1 25  ? 34.966  6.531   15.263  1.00 33.52 ?  17  PRO D CB    1 
ATOM   2411 C CG    . PRO B 1 25  ? 33.768  6.847   16.093  1.00 32.60 ?  17  PRO D CG    1 
ATOM   2412 C CD    . PRO B 1 25  ? 32.561  6.241   15.413  1.00 28.25 ?  17  PRO D CD    1 
ATOM   2413 N N     . VAL B 1 26  ? 36.378  3.796   15.306  1.00 29.89 ?  18  VAL D N     1 
ATOM   2414 C CA    . VAL B 1 26  ? 37.025  2.688   15.998  1.00 30.03 ?  18  VAL D CA    1 
ATOM   2415 C C     . VAL B 1 26  ? 38.176  3.240   16.829  1.00 35.16 ?  18  VAL D C     1 
ATOM   2416 O O     . VAL B 1 26  ? 38.937  4.096   16.362  1.00 35.17 ?  18  VAL D O     1 
ATOM   2417 C CB    . VAL B 1 26  ? 37.526  1.615   15.007  1.00 33.61 ?  18  VAL D CB    1 
ATOM   2418 C CG1   . VAL B 1 26  ? 38.405  0.601   15.714  1.00 32.92 ?  18  VAL D CG1   1 
ATOM   2419 C CG2   . VAL B 1 26  ? 36.348  0.922   14.338  1.00 30.24 ?  18  VAL D CG2   1 
ATOM   2420 N N     . VAL B 1 27  ? 38.299  2.757   18.064  1.00 30.63 ?  19  VAL D N     1 
ATOM   2421 C CA    . VAL B 1 27  ? 39.320  3.225   18.992  1.00 35.32 ?  19  VAL D CA    1 
ATOM   2422 C C     . VAL B 1 27  ? 40.129  2.033   19.486  1.00 35.32 ?  19  VAL D C     1 
ATOM   2423 O O     . VAL B 1 27  ? 39.570  0.975   19.796  1.00 31.57 ?  19  VAL D O     1 
ATOM   2424 C CB    . VAL B 1 27  ? 38.701  3.991   20.180  1.00 32.70 ?  19  VAL D CB    1 
ATOM   2425 C CG1   . VAL B 1 27  ? 39.789  4.487   21.123  1.00 28.28 ?  19  VAL D CG1   1 
ATOM   2426 C CG2   . VAL B 1 27  ? 37.856  5.152   19.680  1.00 30.09 ?  19  VAL D CG2   1 
ATOM   2427 N N     . LYS B 1 28  ? 41.448  2.207   19.548  1.00 33.34 ?  20  LYS D N     1 
ATOM   2428 C CA    . LYS B 1 28  ? 42.330  1.208   20.134  1.00 31.54 ?  20  LYS D CA    1 
ATOM   2429 C C     . LYS B 1 28  ? 42.395  1.396   21.644  1.00 28.68 ?  20  LYS D C     1 
ATOM   2430 O O     . LYS B 1 28  ? 42.548  2.521   22.131  1.00 31.12 ?  20  LYS D O     1 
ATOM   2431 C CB    . LYS B 1 28  ? 43.730  1.316   19.528  1.00 32.02 ?  20  LYS D CB    1 
ATOM   2432 C CG    . LYS B 1 28  ? 44.716  0.264   20.021  1.00 37.42 ?  20  LYS D CG    1 
ATOM   2433 C CD    . LYS B 1 28  ? 46.009  0.302   19.214  1.00 38.72 ?  20  LYS D CD    1 
ATOM   2434 C CE    . LYS B 1 28  ? 47.078  -0.596  19.821  1.00 43.37 ?  20  LYS D CE    1 
ATOM   2435 N NZ    . LYS B 1 28  ? 47.651  -0.027  21.076  1.00 48.86 ?  20  LYS D NZ    1 
ATOM   2436 N N     . LEU B 1 29  ? 42.275  0.296   22.384  1.00 33.78 ?  21  LEU D N     1 
ATOM   2437 C CA    . LEU B 1 29  ? 42.420  0.342   23.832  1.00 28.85 ?  21  LEU D CA    1 
ATOM   2438 C C     . LEU B 1 29  ? 43.900  0.378   24.196  1.00 36.87 ?  21  LEU D C     1 
ATOM   2439 O O     . LEU B 1 29  ? 44.704  -0.376  23.637  1.00 33.86 ?  21  LEU D O     1 
ATOM   2440 C CB    . LEU B 1 29  ? 41.737  -0.859  24.484  1.00 35.59 ?  21  LEU D CB    1 
ATOM   2441 C CG    . LEU B 1 29  ? 40.273  -1.103  24.117  1.00 36.35 ?  21  LEU D CG    1 
ATOM   2442 C CD1   . LEU B 1 29  ? 39.732  -2.326  24.845  1.00 30.91 ?  21  LEU D CD1   1 
ATOM   2443 C CD2   . LEU B 1 29  ? 39.429  0.124   24.426  1.00 27.26 ?  21  LEU D CD2   1 
ATOM   2444 N N     . ARG B 1 30  ? 44.257  1.259   25.130  1.00 36.70 ?  22  ARG D N     1 
ATOM   2445 C CA    . ARG B 1 30  ? 45.646  1.458   25.515  1.00 41.07 ?  22  ARG D CA    1 
ATOM   2446 C C     . ARG B 1 30  ? 45.988  0.926   26.897  1.00 39.34 ?  22  ARG D C     1 
ATOM   2447 O O     . ARG B 1 30  ? 47.104  0.442   27.094  1.00 40.92 ?  22  ARG D O     1 
ATOM   2448 C CB    . ARG B 1 30  ? 46.006  2.950   25.472  1.00 33.91 ?  22  ARG D CB    1 
ATOM   2449 C CG    . ARG B 1 30  ? 45.558  3.693   24.222  1.00 38.56 ?  22  ARG D CG    1 
ATOM   2450 C CD    . ARG B 1 30  ? 45.578  5.201   24.457  1.00 40.52 ?  22  ARG D CD    1 
ATOM   2451 N NE    . ARG B 1 30  ? 44.327  5.683   25.031  1.00 40.67 ?  22  ARG D NE    1 
ATOM   2452 C CZ    . ARG B 1 30  ? 44.236  6.357   26.171  1.00 42.37 ?  22  ARG D CZ    1 
ATOM   2453 N NH1   . ARG B 1 30  ? 45.308  6.649   26.889  1.00 42.46 ?  22  ARG D NH1   1 
ATOM   2454 N NH2   . ARG B 1 30  ? 43.038  6.743   26.603  1.00 43.62 ?  22  ARG D NH2   1 
ATOM   2455 N N     . ASN B 1 31  ? 45.065  0.995   27.853  1.00 38.16 ?  23  ASN D N     1 
ATOM   2456 C CA    . ASN B 1 31  ? 45.387  0.770   29.258  1.00 37.65 ?  23  ASN D CA    1 
ATOM   2457 C C     . ASN B 1 31  ? 44.842  -0.532  29.826  1.00 42.00 ?  23  ASN D C     1 
ATOM   2458 O O     . ASN B 1 31  ? 45.545  -1.203  30.586  1.00 41.43 ?  23  ASN D O     1 
ATOM   2459 C CB    . ASN B 1 31  ? 44.874  1.945   30.101  1.00 31.39 ?  23  ASN D CB    1 
ATOM   2460 C CG    . ASN B 1 31  ? 45.698  3.204   29.900  1.00 43.34 ?  23  ASN D CG    1 
ATOM   2461 O OD1   . ASN B 1 31  ? 46.925  3.173   29.977  1.00 42.20 ?  23  ASN D OD1   1 
ATOM   2462 N ND2   . ASN B 1 31  ? 45.027  4.318   29.630  1.00 36.25 ?  23  ASN D ND2   1 
ATOM   2463 N N     . VAL B 1 32  ? 43.608  -0.919  29.486  1.00 38.98 ?  24  VAL D N     1 
ATOM   2464 C CA    . VAL B 1 32  ? 43.011  -2.114  30.083  1.00 43.04 ?  24  VAL D CA    1 
ATOM   2465 C C     . VAL B 1 32  ? 43.536  -3.407  29.483  1.00 40.39 ?  24  VAL D C     1 
ATOM   2466 O O     . VAL B 1 32  ? 43.168  -4.489  29.959  1.00 41.98 ?  24  VAL D O     1 
ATOM   2467 C CB    . VAL B 1 32  ? 41.474  -2.105  29.952  1.00 43.48 ?  24  VAL D CB    1 
ATOM   2468 C CG1   . VAL B 1 32  ? 40.872  -1.021  30.835  1.00 40.42 ?  24  VAL D CG1   1 
ATOM   2469 C CG2   . VAL B 1 32  ? 41.067  -1.920  28.501  1.00 35.32 ?  24  VAL D CG2   1 
ATOM   2470 N N     . VAL B 1 33  ? 44.380  -3.334  28.456  1.00 42.57 ?  25  VAL D N     1 
ATOM   2471 C CA    . VAL B 1 33  ? 44.955  -4.509  27.814  1.00 43.93 ?  25  VAL D CA    1 
ATOM   2472 C C     . VAL B 1 33  ? 46.473  -4.387  27.853  1.00 51.09 ?  25  VAL D C     1 
ATOM   2473 O O     . VAL B 1 33  ? 47.024  -3.295  27.673  1.00 49.86 ?  25  VAL D O     1 
ATOM   2474 C CB    . VAL B 1 33  ? 44.446  -4.675  26.365  1.00 51.37 ?  25  VAL D CB    1 
ATOM   2475 C CG1   . VAL B 1 33  ? 44.696  -3.409  25.556  1.00 47.26 ?  25  VAL D CG1   1 
ATOM   2476 C CG2   . VAL B 1 33  ? 45.084  -5.890  25.697  1.00 47.52 ?  25  VAL D CG2   1 
ATOM   2477 N N     . ASP B 1 34  ? 47.144  -5.507  28.108  1.00 55.85 ?  26  ASP D N     1 
ATOM   2478 C CA    . ASP B 1 34  ? 48.594  -5.523  28.210  1.00 58.52 ?  26  ASP D CA    1 
ATOM   2479 C C     . ASP B 1 34  ? 49.233  -5.338  26.837  1.00 58.79 ?  26  ASP D C     1 
ATOM   2480 O O     . ASP B 1 34  ? 48.638  -5.632  25.796  1.00 57.81 ?  26  ASP D O     1 
ATOM   2481 C CB    . ASP B 1 34  ? 49.068  -6.838  28.835  1.00 63.28 ?  26  ASP D CB    1 
ATOM   2482 C CG    . ASP B 1 34  ? 50.514  -6.784  29.311  1.00 72.19 ?  26  ASP D CG    1 
ATOM   2483 O OD1   . ASP B 1 34  ? 51.340  -6.086  28.684  1.00 73.77 ?  26  ASP D OD1   1 
ATOM   2484 O OD2   . ASP B 1 34  ? 50.826  -7.448  30.320  1.00 80.62 ?  26  ASP D OD2   1 
ATOM   2485 N N     . ASP B 1 35  ? 50.474  -4.846  26.846  1.00 64.79 ?  27  ASP D N     1 
ATOM   2486 C CA    . ASP B 1 35  ? 51.264  -4.773  25.624  1.00 63.99 ?  27  ASP D CA    1 
ATOM   2487 C C     . ASP B 1 35  ? 51.704  -6.146  25.131  1.00 59.90 ?  27  ASP D C     1 
ATOM   2488 O O     . ASP B 1 35  ? 52.240  -6.245  24.022  1.00 58.77 ?  27  ASP D O     1 
ATOM   2489 C CB    . ASP B 1 35  ? 52.492  -3.885  25.845  1.00 60.64 ?  27  ASP D CB    1 
ATOM   2490 N N     . ASN B 1 36  ? 51.491  -7.197  25.921  1.00 55.40 ?  28  ASN D N     1 
ATOM   2491 C CA    . ASN B 1 36  ? 51.837  -8.559  25.543  1.00 57.87 ?  28  ASN D CA    1 
ATOM   2492 C C     . ASN B 1 36  ? 50.660  -9.329  24.962  1.00 59.52 ?  28  ASN D C     1 
ATOM   2493 O O     . ASN B 1 36  ? 50.818  -10.502 24.608  1.00 56.82 ?  28  ASN D O     1 
ATOM   2494 C CB    . ASN B 1 36  ? 52.403  -9.311  26.750  1.00 66.74 ?  28  ASN D CB    1 
ATOM   2495 C CG    . ASN B 1 36  ? 53.849  -8.957  27.028  1.00 73.74 ?  28  ASN D CG    1 
ATOM   2496 O OD1   . ASN B 1 36  ? 54.703  -9.053  26.146  1.00 81.50 ?  28  ASN D OD1   1 
ATOM   2497 N ND2   . ASN B 1 36  ? 54.131  -8.536  28.256  1.00 75.54 ?  28  ASN D ND2   1 
ATOM   2498 N N     . ALA B 1 37  ? 49.491  -8.708  24.866  1.00 51.47 ?  29  ALA D N     1 
ATOM   2499 C CA    . ALA B 1 37  ? 48.332  -9.297  24.215  1.00 49.34 ?  29  ALA D CA    1 
ATOM   2500 C C     . ALA B 1 37  ? 48.147  -8.679  22.835  1.00 45.25 ?  29  ALA D C     1 
ATOM   2501 O O     . ALA B 1 37  ? 48.859  -7.754  22.438  1.00 48.90 ?  29  ALA D O     1 
ATOM   2502 C CB    . ALA B 1 37  ? 47.073  -9.101  25.066  1.00 44.00 ?  29  ALA D CB    1 
ATOM   2503 N N     . ALA B 1 38  ? 47.176  -9.206  22.098  1.00 43.84 ?  30  ALA D N     1 
ATOM   2504 C CA    . ALA B 1 38  ? 46.858  -8.645  20.796  1.00 41.77 ?  30  ALA D CA    1 
ATOM   2505 C C     . ALA B 1 38  ? 46.274  -7.244  20.950  1.00 40.85 ?  30  ALA D C     1 
ATOM   2506 O O     . ALA B 1 38  ? 45.813  -6.845  22.023  1.00 35.96 ?  30  ALA D O     1 
ATOM   2507 C CB    . ALA B 1 38  ? 45.876  -9.546  20.049  1.00 39.89 ?  30  ALA D CB    1 
ATOM   2508 N N     . ASP B 1 39  ? 46.306  -6.488  19.856  1.00 41.95 ?  31  ASP D N     1 
ATOM   2509 C CA    . ASP B 1 39  ? 45.662  -5.184  19.842  1.00 42.60 ?  31  ASP D CA    1 
ATOM   2510 C C     . ASP B 1 39  ? 44.147  -5.346  19.831  1.00 40.92 ?  31  ASP D C     1 
ATOM   2511 O O     . ASP B 1 39  ? 43.598  -6.159  19.081  1.00 39.03 ?  31  ASP D O     1 
ATOM   2512 C CB    . ASP B 1 39  ? 46.117  -4.376  18.628  1.00 37.69 ?  31  ASP D CB    1 
ATOM   2513 C CG    . ASP B 1 39  ? 47.575  -3.973  18.712  1.00 43.29 ?  31  ASP D CG    1 
ATOM   2514 O OD1   . ASP B 1 39  ? 48.120  -3.938  19.835  1.00 44.28 ?  31  ASP D OD1   1 
ATOM   2515 O OD2   . ASP B 1 39  ? 48.175  -3.687  17.655  1.00 40.21 ?  31  ASP D OD2   1 
ATOM   2516 N N     . VAL B 1 40  ? 43.472  -4.575  20.676  1.00 37.85 ?  32  VAL D N     1 
ATOM   2517 C CA    . VAL B 1 40  ? 42.020  -4.620  20.795  1.00 39.04 ?  32  VAL D CA    1 
ATOM   2518 C C     . VAL B 1 40  ? 41.463  -3.302  20.280  1.00 37.43 ?  32  VAL D C     1 
ATOM   2519 O O     . VAL B 1 40  ? 41.811  -2.229  20.790  1.00 34.57 ?  32  VAL D O     1 
ATOM   2520 C CB    . VAL B 1 40  ? 41.573  -4.876  22.241  1.00 39.30 ?  32  VAL D CB    1 
ATOM   2521 C CG1   . VAL B 1 40  ? 40.056  -4.952  22.313  1.00 34.84 ?  32  VAL D CG1   1 
ATOM   2522 C CG2   . VAL B 1 40  ? 42.203  -6.151  22.772  1.00 40.12 ?  32  VAL D CG2   1 
ATOM   2523 N N     . TYR B 1 41  ? 40.600  -3.384  19.273  1.00 31.61 ?  33  TYR D N     1 
ATOM   2524 C CA    . TYR B 1 41  ? 39.931  -2.227  18.698  1.00 28.33 ?  33  TYR D CA    1 
ATOM   2525 C C     . TYR B 1 41  ? 38.431  -2.348  18.927  1.00 29.43 ?  33  TYR D C     1 
ATOM   2526 O O     . TYR B 1 41  ? 37.854  -3.425  18.752  1.00 32.90 ?  33  TYR D O     1 
ATOM   2527 C CB    . TYR B 1 41  ? 40.225  -2.116  17.202  1.00 31.11 ?  33  TYR D CB    1 
ATOM   2528 C CG    . TYR B 1 41  ? 41.661  -1.775  16.869  1.00 39.28 ?  33  TYR D CG    1 
ATOM   2529 C CD1   . TYR B 1 41  ? 42.070  -0.454  16.744  1.00 35.72 ?  33  TYR D CD1   1 
ATOM   2530 C CD2   . TYR B 1 41  ? 42.606  -2.775  16.676  1.00 40.39 ?  33  TYR D CD2   1 
ATOM   2531 C CE1   . TYR B 1 41  ? 43.378  -0.138  16.433  1.00 35.13 ?  33  TYR D CE1   1 
ATOM   2532 C CE2   . TYR B 1 41  ? 43.918  -2.467  16.368  1.00 37.20 ?  33  TYR D CE2   1 
ATOM   2533 C CZ    . TYR B 1 41  ? 44.298  -1.148  16.249  1.00 41.42 ?  33  TYR D CZ    1 
ATOM   2534 O OH    . TYR B 1 41  ? 45.601  -0.834  15.942  1.00 41.04 ?  33  TYR D OH    1 
ATOM   2535 N N     . VAL B 1 42  ? 37.798  -1.244  19.320  1.00 28.01 ?  34  VAL D N     1 
ATOM   2536 C CA    . VAL B 1 42  ? 36.370  -1.222  19.610  1.00 28.33 ?  34  VAL D CA    1 
ATOM   2537 C C     . VAL B 1 42  ? 35.680  -0.255  18.658  1.00 32.50 ?  34  VAL D C     1 
ATOM   2538 O O     . VAL B 1 42  ? 36.172  0.852   18.414  1.00 31.86 ?  34  VAL D O     1 
ATOM   2539 C CB    . VAL B 1 42  ? 36.087  -0.842  21.082  1.00 28.34 ?  34  VAL D CB    1 
ATOM   2540 C CG1   . VAL B 1 42  ? 36.593  -1.928  22.014  1.00 24.92 ?  34  VAL D CG1   1 
ATOM   2541 C CG2   . VAL B 1 42  ? 36.725  0.497   21.432  1.00 25.46 ?  34  VAL D CG2   1 
ATOM   2542 N N     . LYS B 1 43  ? 34.543  -0.683  18.116  1.00 28.70 ?  35  LYS D N     1 
ATOM   2543 C CA    . LYS B 1 43  ? 33.723  0.146   17.242  1.00 31.53 ?  35  LYS D CA    1 
ATOM   2544 C C     . LYS B 1 43  ? 32.596  0.764   18.060  1.00 30.13 ?  35  LYS D C     1 
ATOM   2545 O O     . LYS B 1 43  ? 31.830  0.047   18.713  1.00 31.31 ?  35  LYS D O     1 
ATOM   2546 C CB    . LYS B 1 43  ? 33.160  -0.678  16.082  1.00 31.91 ?  35  LYS D CB    1 
ATOM   2547 C CG    . LYS B 1 43  ? 32.695  0.140   14.888  1.00 26.62 ?  35  LYS D CG    1 
ATOM   2548 C CD    . LYS B 1 43  ? 32.602  -0.735  13.645  1.00 29.06 ?  35  LYS D CD    1 
ATOM   2549 C CE    . LYS B 1 43  ? 31.674  -0.140  12.596  1.00 29.34 ?  35  LYS D CE    1 
ATOM   2550 N NZ    . LYS B 1 43  ? 32.194  1.145   12.049  1.00 26.44 ?  35  LYS D NZ    1 
ATOM   2551 N N     . LEU B 1 44  ? 32.499  2.091   18.017  1.00 29.80 ?  36  LEU D N     1 
ATOM   2552 C CA    . LEU B 1 44  ? 31.607  2.848   18.895  1.00 31.23 ?  36  LEU D CA    1 
ATOM   2553 C C     . LEU B 1 44  ? 30.253  3.009   18.218  1.00 29.97 ?  36  LEU D C     1 
ATOM   2554 O O     . LEU B 1 44  ? 29.998  3.992   17.521  1.00 29.11 ?  36  LEU D O     1 
ATOM   2555 C CB    . LEU B 1 44  ? 32.219  4.202   19.222  1.00 32.45 ?  36  LEU D CB    1 
ATOM   2556 C CG    . LEU B 1 44  ? 33.678  4.178   19.665  1.00 30.83 ?  36  LEU D CG    1 
ATOM   2557 C CD1   . LEU B 1 44  ? 34.079  5.566   20.077  1.00 36.72 ?  36  LEU D CD1   1 
ATOM   2558 C CD2   . LEU B 1 44  ? 33.891  3.195   20.805  1.00 30.36 ?  36  LEU D CD2   1 
ATOM   2559 N N     . GLU B 1 45  ? 29.362  2.044   18.442  1.00 29.57 ?  37  GLU D N     1 
ATOM   2560 C CA    . GLU B 1 45  ? 28.034  2.110   17.847  1.00 32.36 ?  37  GLU D CA    1 
ATOM   2561 C C     . GLU B 1 45  ? 27.091  3.053   18.585  1.00 29.46 ?  37  GLU D C     1 
ATOM   2562 O O     . GLU B 1 45  ? 26.005  3.339   18.067  1.00 30.14 ?  37  GLU D O     1 
ATOM   2563 C CB    . GLU B 1 45  ? 27.416  0.713   17.769  1.00 32.10 ?  37  GLU D CB    1 
ATOM   2564 C CG    . GLU B 1 45  ? 28.006  -0.137  16.658  1.00 31.46 ?  37  GLU D CG    1 
ATOM   2565 C CD    . GLU B 1 45  ? 27.796  0.478   15.289  1.00 27.38 ?  37  GLU D CD    1 
ATOM   2566 O OE1   . GLU B 1 45  ? 26.636  0.788   14.947  1.00 27.95 ?  37  GLU D OE1   1 
ATOM   2567 O OE2   . GLU B 1 45  ? 28.792  0.659   14.557  1.00 27.15 ?  37  GLU D OE2   1 
ATOM   2568 N N     . TYR B 1 46  ? 27.466  3.542   19.769  1.00 27.01 ?  38  TYR D N     1 
ATOM   2569 C CA    . TYR B 1 46  ? 26.691  4.596   20.410  1.00 31.24 ?  38  TYR D CA    1 
ATOM   2570 C C     . TYR B 1 46  ? 26.912  5.954   19.757  1.00 29.29 ?  38  TYR D C     1 
ATOM   2571 O O     . TYR B 1 46  ? 26.208  6.911   20.097  1.00 27.66 ?  38  TYR D O     1 
ATOM   2572 C CB    . TYR B 1 46  ? 27.011  4.672   21.911  1.00 25.27 ?  38  TYR D CB    1 
ATOM   2573 C CG    . TYR B 1 46  ? 28.475  4.860   22.258  1.00 29.11 ?  38  TYR D CG    1 
ATOM   2574 C CD1   . TYR B 1 46  ? 29.118  6.072   22.036  1.00 27.27 ?  38  TYR D CD1   1 
ATOM   2575 C CD2   . TYR B 1 46  ? 29.211  3.826   22.826  1.00 31.00 ?  38  TYR D CD2   1 
ATOM   2576 C CE1   . TYR B 1 46  ? 30.451  6.247   22.355  1.00 30.40 ?  38  TYR D CE1   1 
ATOM   2577 C CE2   . TYR B 1 46  ? 30.547  3.992   23.150  1.00 27.40 ?  38  TYR D CE2   1 
ATOM   2578 C CZ    . TYR B 1 46  ? 31.160  5.205   22.912  1.00 29.87 ?  38  TYR D CZ    1 
ATOM   2579 O OH    . TYR B 1 46  ? 32.486  5.384   23.229  1.00 35.63 ?  38  TYR D OH    1 
ATOM   2580 N N     . GLN B 1 47  ? 27.870  6.057   18.834  1.00 28.14 ?  39  GLN D N     1 
ATOM   2581 C CA    . GLN B 1 47  ? 28.066  7.278   18.064  1.00 29.04 ?  39  GLN D CA    1 
ATOM   2582 C C     . GLN B 1 47  ? 26.955  7.515   17.051  1.00 26.77 ?  39  GLN D C     1 
ATOM   2583 O O     . GLN B 1 47  ? 26.878  8.613   16.490  1.00 24.19 ?  39  GLN D O     1 
ATOM   2584 C CB    . GLN B 1 47  ? 29.417  7.237   17.350  1.00 27.29 ?  39  GLN D CB    1 
ATOM   2585 C CG    . GLN B 1 47  ? 30.588  7.665   18.218  1.00 22.84 ?  39  GLN D CG    1 
ATOM   2586 C CD    . GLN B 1 47  ? 30.506  9.122   18.627  1.00 35.03 ?  39  GLN D CD    1 
ATOM   2587 O OE1   . GLN B 1 47  ? 29.996  9.452   19.699  1.00 29.79 ?  39  GLN D OE1   1 
ATOM   2588 N NE2   . GLN B 1 47  ? 31.010  10.005  17.773  1.00 38.42 ?  39  GLN D NE2   1 
ATOM   2589 N N     . ASN B 1 48  ? 26.106  6.522   16.799  1.00 25.48 ?  40  ASN D N     1 
ATOM   2590 C CA    . ASN B 1 48  ? 24.939  6.732   15.960  1.00 27.30 ?  40  ASN D CA    1 
ATOM   2591 C C     . ASN B 1 48  ? 24.025  7.787   16.591  1.00 26.91 ?  40  ASN D C     1 
ATOM   2592 O O     . ASN B 1 48  ? 24.002  7.944   17.817  1.00 27.27 ?  40  ASN D O     1 
ATOM   2593 C CB    . ASN B 1 48  ? 24.188  5.414   15.770  1.00 28.62 ?  40  ASN D CB    1 
ATOM   2594 C CG    . ASN B 1 48  ? 24.830  4.520   14.720  1.00 28.13 ?  40  ASN D CG    1 
ATOM   2595 O OD1   . ASN B 1 48  ? 25.185  4.973   13.631  1.00 26.93 ?  40  ASN D OD1   1 
ATOM   2596 N ND2   . ASN B 1 48  ? 24.979  3.241   15.047  1.00 29.07 ?  40  ASN D ND2   1 
ATOM   2597 N N     . PRO B 1 49  ? 23.250  8.518   15.774  1.00 28.83 ?  41  PRO D N     1 
ATOM   2598 C CA    . PRO B 1 49  ? 22.477  9.655   16.314  1.00 28.43 ?  41  PRO D CA    1 
ATOM   2599 C C     . PRO B 1 49  ? 21.531  9.262   17.430  1.00 27.86 ?  41  PRO D C     1 
ATOM   2600 O O     . PRO B 1 49  ? 21.416  9.988   18.425  1.00 32.45 ?  41  PRO D O     1 
ATOM   2601 C CB    . PRO B 1 49  ? 21.713  10.175  15.084  1.00 33.19 ?  41  PRO D CB    1 
ATOM   2602 C CG    . PRO B 1 49  ? 21.683  9.039   14.148  1.00 31.66 ?  41  PRO D CG    1 
ATOM   2603 C CD    . PRO B 1 49  ? 22.961  8.290   14.349  1.00 26.56 ?  41  PRO D CD    1 
ATOM   2604 N N     . GLY B 1 50  ? 20.861  8.117   17.296  1.00 23.24 ?  42  GLY D N     1 
ATOM   2605 C CA    . GLY B 1 50  ? 19.968  7.631   18.326  1.00 26.15 ?  42  GLY D CA    1 
ATOM   2606 C C     . GLY B 1 50  ? 20.654  7.078   19.549  1.00 26.25 ?  42  GLY D C     1 
ATOM   2607 O O     . GLY B 1 50  ? 19.998  6.856   20.572  1.00 26.29 ?  42  GLY D O     1 
ATOM   2608 N N     . GLY B 1 51  ? 21.958  6.843   19.461  1.00 27.12 ?  43  GLY D N     1 
ATOM   2609 C CA    . GLY B 1 51  ? 22.753  6.484   20.610  1.00 25.75 ?  43  GLY D CA    1 
ATOM   2610 C C     . GLY B 1 51  ? 23.102  5.022   20.757  1.00 29.55 ?  43  GLY D C     1 
ATOM   2611 O O     . GLY B 1 51  ? 23.643  4.643   21.800  1.00 29.88 ?  43  GLY D O     1 
ATOM   2612 N N     . SER B 1 52  ? 22.824  4.187   19.759  1.00 28.33 ?  44  SER D N     1 
ATOM   2613 C CA    . SER B 1 52  ? 23.128  2.768   19.888  1.00 29.97 ?  44  SER D CA    1 
ATOM   2614 C C     . SER B 1 52  ? 23.198  2.129   18.506  1.00 31.61 ?  44  SER D C     1 
ATOM   2615 O O     . SER B 1 52  ? 22.961  2.775   17.481  1.00 30.19 ?  44  SER D O     1 
ATOM   2616 C CB    . SER B 1 52  ? 22.093  2.057   20.764  1.00 27.14 ?  44  SER D CB    1 
ATOM   2617 O OG    . SER B 1 52  ? 21.038  1.539   19.974  1.00 28.05 ?  44  SER D OG    1 
ATOM   2618 N N     . VAL B 1 53  ? 23.521  0.839   18.499  1.00 27.71 ?  45  VAL D N     1 
ATOM   2619 C CA    . VAL B 1 53  ? 23.641  0.045   17.283  1.00 30.62 ?  45  VAL D CA    1 
ATOM   2620 C C     . VAL B 1 53  ? 22.281  -0.148  16.620  1.00 27.65 ?  45  VAL D C     1 
ATOM   2621 O O     . VAL B 1 53  ? 22.193  -0.364  15.411  1.00 26.35 ?  45  VAL D O     1 
ATOM   2622 C CB    . VAL B 1 53  ? 24.308  -1.321  17.591  1.00 28.66 ?  45  VAL D CB    1 
ATOM   2623 C CG1   . VAL B 1 53  ? 23.412  -2.175  18.480  1.00 27.63 ?  45  VAL D CG1   1 
ATOM   2624 C CG2   . VAL B 1 53  ? 24.653  -2.062  16.306  1.00 25.16 ?  45  VAL D CG2   1 
HETATM 2625 N N1    . LLP B 1 54  ? 24.071  -4.816  23.343  1.00 30.41 ?  46  LLP D N1    1 
HETATM 2626 C C2    . LLP B 1 54  ? 23.071  -3.936  23.320  1.00 30.41 ?  46  LLP D C2    1 
HETATM 2627 C "C2'" . LLP B 1 54  ? 23.022  -2.780  24.362  1.00 31.00 ?  46  LLP D "C2'" 1 
HETATM 2628 C C3    . LLP B 1 54  ? 22.044  -4.049  22.347  1.00 30.57 ?  46  LLP D C3    1 
HETATM 2629 O O3    . LLP B 1 54  ? 21.011  -3.104  22.357  1.00 30.58 ?  46  LLP D O3    1 
HETATM 2630 C C4    . LLP B 1 54  ? 22.073  -5.065  21.413  1.00 33.61 ?  46  LLP D C4    1 
HETATM 2631 C "C4'" . LLP B 1 54  ? 20.891  -5.181  20.316  1.00 32.21 ?  46  LLP D "C4'" 1 
HETATM 2632 C C5    . LLP B 1 54  ? 23.100  -5.967  21.434  1.00 34.83 ?  46  LLP D C5    1 
HETATM 2633 C C6    . LLP B 1 54  ? 24.107  -5.850  22.401  1.00 32.44 ?  46  LLP D C6    1 
HETATM 2634 C "C5'" . LLP B 1 54  ? 23.202  -7.153  20.421  1.00 31.22 ?  46  LLP D "C5'" 1 
HETATM 2635 O OP4   . LLP B 1 54  ? 23.195  -6.742  19.072  1.00 30.77 ?  46  LLP D OP4   1 
HETATM 2636 P P     . LLP B 1 54  ? 22.518  -7.702  18.068  1.00 35.51 ?  46  LLP D P     1 
HETATM 2637 O OP1   . LLP B 1 54  ? 20.998  -7.644  18.267  1.00 30.18 ?  46  LLP D OP1   1 
HETATM 2638 O OP2   . LLP B 1 54  ? 22.986  -9.081  18.319  1.00 32.60 ?  46  LLP D OP2   1 
HETATM 2639 O OP3   . LLP B 1 54  ? 22.856  -7.307  16.672  1.00 30.88 ?  46  LLP D OP3   1 
HETATM 2640 N N     . LLP B 1 54  ? 21.218  -0.045  17.412  1.00 29.18 ?  46  LLP D N     1 
HETATM 2641 C CA    . LLP B 1 54  ? 19.859  -0.324  16.926  1.00 29.87 ?  46  LLP D CA    1 
HETATM 2642 C CB    . LLP B 1 54  ? 18.913  -0.412  18.095  1.00 31.97 ?  46  LLP D CB    1 
HETATM 2643 C CG    . LLP B 1 54  ? 19.325  -1.580  18.994  1.00 27.10 ?  46  LLP D CG    1 
HETATM 2644 C CD    . LLP B 1 54  ? 19.237  -2.895  18.203  1.00 26.32 ?  46  LLP D CD    1 
HETATM 2645 C CE    . LLP B 1 54  ? 19.135  -4.079  19.184  1.00 25.98 ?  46  LLP D CE    1 
HETATM 2646 N NZ    . LLP B 1 54  ? 20.178  -3.944  20.211  1.00 36.35 ?  46  LLP D NZ    1 
HETATM 2647 C C     . LLP B 1 54  ? 19.394  0.709   15.956  1.00 29.41 ?  46  LLP D C     1 
HETATM 2648 O O     . LLP B 1 54  ? 18.363  0.527   15.326  1.00 30.63 ?  46  LLP D O     1 
ATOM   2649 N N     . ASP B 1 55  ? 20.139  1.804   15.834  1.00 31.87 ?  47  ASP D N     1 
ATOM   2650 C CA    . ASP B 1 55  ? 19.865  2.812   14.815  1.00 29.57 ?  47  ASP D CA    1 
ATOM   2651 C C     . ASP B 1 55  ? 19.857  2.187   13.427  1.00 30.61 ?  47  ASP D C     1 
ATOM   2652 O O     . ASP B 1 55  ? 18.991  2.482   12.604  1.00 23.91 ?  47  ASP D O     1 
ATOM   2653 C CB    . ASP B 1 55  ? 20.905  3.934   14.860  1.00 28.76 ?  47  ASP D CB    1 
ATOM   2654 C CG    . ASP B 1 55  ? 20.624  4.953   15.942  1.00 28.14 ?  47  ASP D CG    1 
ATOM   2655 O OD1   . ASP B 1 55  ? 19.966  4.605   16.943  1.00 30.65 ?  47  ASP D OD1   1 
ATOM   2656 O OD2   . ASP B 1 55  ? 21.060  6.113   15.784  1.00 30.40 ?  47  ASP D OD2   1 
ATOM   2657 N N     . ARG B 1 56  ? 20.839  1.317   13.183  1.00 28.11 ?  48  ARG D N     1 
ATOM   2658 C CA    . ARG B 1 56  ? 20.995  0.712   11.864  1.00 24.74 ?  48  ARG D CA    1 
ATOM   2659 C C     . ARG B 1 56  ? 19.807  -0.177  11.516  1.00 27.07 ?  48  ARG D C     1 
ATOM   2660 O O     . ARG B 1 56  ? 19.260  -0.097  10.409  1.00 28.21 ?  48  ARG D O     1 
ATOM   2661 C CB    . ARG B 1 56  ? 22.292  -0.093  11.810  1.00 30.48 ?  48  ARG D CB    1 
ATOM   2662 C CG    . ARG B 1 56  ? 23.553  0.698   12.116  1.00 29.47 ?  48  ARG D CG    1 
ATOM   2663 C CD    . ARG B 1 56  ? 24.774  -0.189  11.953  1.00 30.80 ?  48  ARG D CD    1 
ATOM   2664 N NE    . ARG B 1 56  ? 26.021  0.487   12.290  1.00 28.87 ?  48  ARG D NE    1 
ATOM   2665 C CZ    . ARG B 1 56  ? 26.894  0.934   11.397  1.00 31.67 ?  48  ARG D CZ    1 
ATOM   2666 N NH1   . ARG B 1 56  ? 26.681  0.803   10.098  1.00 25.14 ?  48  ARG D NH1   1 
ATOM   2667 N NH2   . ARG B 1 56  ? 28.008  1.527   11.819  1.00 30.00 ?  48  ARG D NH2   1 
ATOM   2668 N N     . ILE B 1 57  ? 19.398  -1.040  12.448  1.00 27.11 ?  49  ILE D N     1 
ATOM   2669 C CA    . ILE B 1 57  ? 18.333  -1.988  12.138  1.00 25.14 ?  49  ILE D CA    1 
ATOM   2670 C C     . ILE B 1 57  ? 16.964  -1.323  12.220  1.00 31.12 ?  49  ILE D C     1 
ATOM   2671 O O     . ILE B 1 57  ? 16.025  -1.752  11.542  1.00 31.19 ?  49  ILE D O     1 
ATOM   2672 C CB    . ILE B 1 57  ? 18.419  -3.227  13.048  1.00 27.23 ?  49  ILE D CB    1 
ATOM   2673 C CG1   . ILE B 1 57  ? 17.885  -2.930  14.450  1.00 29.91 ?  49  ILE D CG1   1 
ATOM   2674 C CG2   . ILE B 1 57  ? 19.851  -3.737  13.112  1.00 23.33 ?  49  ILE D CG2   1 
ATOM   2675 C CD1   . ILE B 1 57  ? 17.541  -4.176  15.235  1.00 28.94 ?  49  ILE D CD1   1 
ATOM   2676 N N     . ALA B 1 58  ? 16.819  -0.272  13.028  1.00 27.52 ?  50  ALA D N     1 
ATOM   2677 C CA    . ALA B 1 58  ? 15.573  0.485   13.010  1.00 32.42 ?  50  ALA D CA    1 
ATOM   2678 C C     . ALA B 1 58  ? 15.366  1.138   11.650  1.00 35.32 ?  50  ALA D C     1 
ATOM   2679 O O     . ALA B 1 58  ? 14.271  1.081   11.078  1.00 26.67 ?  50  ALA D O     1 
ATOM   2680 C CB    . ALA B 1 58  ? 15.572  1.532   14.123  1.00 28.98 ?  50  ALA D CB    1 
ATOM   2681 N N     . LEU B 1 59  ? 16.422  1.744   11.105  1.00 27.62 ?  51  LEU D N     1 
ATOM   2682 C CA    . LEU B 1 59  ? 16.330  2.342   9.778   1.00 29.99 ?  51  LEU D CA    1 
ATOM   2683 C C     . LEU B 1 59  ? 16.088  1.283   8.710   1.00 29.24 ?  51  LEU D C     1 
ATOM   2684 O O     . LEU B 1 59  ? 15.295  1.495   7.785   1.00 30.62 ?  51  LEU D O     1 
ATOM   2685 C CB    . LEU B 1 59  ? 17.606  3.124   9.470   1.00 28.57 ?  51  LEU D CB    1 
ATOM   2686 C CG    . LEU B 1 59  ? 17.611  3.898   8.153   1.00 29.44 ?  51  LEU D CG    1 
ATOM   2687 C CD1   . LEU B 1 59  ? 16.486  4.924   8.123   1.00 26.63 ?  51  LEU D CD1   1 
ATOM   2688 C CD2   . LEU B 1 59  ? 18.959  4.558   7.939   1.00 29.26 ?  51  LEU D CD2   1 
ATOM   2689 N N     . ALA B 1 60  ? 16.757  0.134   8.826   1.00 25.95 ?  52  ALA D N     1 
ATOM   2690 C CA    . ALA B 1 60  ? 16.672  -0.886  7.786   1.00 27.47 ?  52  ALA D CA    1 
ATOM   2691 C C     . ALA B 1 60  ? 15.272  -1.480  7.703   1.00 26.49 ?  52  ALA D C     1 
ATOM   2692 O O     . ALA B 1 60  ? 14.709  -1.619  6.611   1.00 28.43 ?  52  ALA D O     1 
ATOM   2693 C CB    . ALA B 1 60  ? 17.705  -1.983  8.040   1.00 27.18 ?  52  ALA D CB    1 
ATOM   2694 N N     . MET B 1 61  ? 14.693  -1.842  8.850   1.00 27.70 ?  53  MET D N     1 
ATOM   2695 C CA    . MET B 1 61  ? 13.376  -2.473  8.839   1.00 30.99 ?  53  MET D CA    1 
ATOM   2696 C C     . MET B 1 61  ? 12.281  -1.505  8.408   1.00 30.91 ?  53  MET D C     1 
ATOM   2697 O O     . MET B 1 61  ? 11.286  -1.930  7.812   1.00 32.39 ?  53  MET D O     1 
ATOM   2698 C CB    . MET B 1 61  ? 13.057  -3.059  10.215  1.00 27.20 ?  53  MET D CB    1 
ATOM   2699 C CG    . MET B 1 61  ? 14.088  -4.058  10.712  1.00 23.50 ?  53  MET D CG    1 
ATOM   2700 S SD    . MET B 1 61  ? 13.618  -4.858  12.258  1.00 28.68 ?  53  MET D SD    1 
ATOM   2701 C CE    . MET B 1 61  ? 14.256  -3.687  13.452  1.00 31.93 ?  53  MET D CE    1 
ATOM   2702 N N     . ILE B 1 62  ? 12.437  -0.212  8.696   1.00 29.76 ?  54  ILE D N     1 
ATOM   2703 C CA    . ILE B 1 62  ? 11.441  0.759   8.256   1.00 30.59 ?  54  ILE D CA    1 
ATOM   2704 C C     . ILE B 1 62  ? 11.628  1.094   6.781   1.00 29.20 ?  54  ILE D C     1 
ATOM   2705 O O     . ILE B 1 62  ? 10.653  1.193   6.029   1.00 28.73 ?  54  ILE D O     1 
ATOM   2706 C CB    . ILE B 1 62  ? 11.494  2.020   9.137   1.00 29.82 ?  54  ILE D CB    1 
ATOM   2707 C CG1   . ILE B 1 62  ? 11.154  1.671   10.588  1.00 30.41 ?  54  ILE D CG1   1 
ATOM   2708 C CG2   . ILE B 1 62  ? 10.552  3.091   8.598   1.00 27.47 ?  54  ILE D CG2   1 
ATOM   2709 C CD1   . ILE B 1 62  ? 9.682   1.404   10.836  1.00 32.59 ?  54  ILE D CD1   1 
ATOM   2710 N N     . GLU B 1 63  ? 12.877  1.272   6.342   1.00 29.73 ?  55  GLU D N     1 
ATOM   2711 C CA    . GLU B 1 63  ? 13.132  1.530   4.928   1.00 35.42 ?  55  GLU D CA    1 
ATOM   2712 C C     . GLU B 1 63  ? 12.680  0.359   4.065   1.00 29.39 ?  55  GLU D C     1 
ATOM   2713 O O     . GLU B 1 63  ? 12.206  0.554   2.940   1.00 33.20 ?  55  GLU D O     1 
ATOM   2714 C CB    . GLU B 1 63  ? 14.617  1.815   4.704   1.00 30.06 ?  55  GLU D CB    1 
ATOM   2715 C CG    . GLU B 1 63  ? 15.015  3.263   4.918   1.00 29.96 ?  55  GLU D CG    1 
ATOM   2716 C CD    . GLU B 1 63  ? 16.489  3.505   4.650   1.00 36.63 ?  55  GLU D CD    1 
ATOM   2717 O OE1   . GLU B 1 63  ? 17.200  2.537   4.307   1.00 40.55 ?  55  GLU D OE1   1 
ATOM   2718 O OE2   . GLU B 1 63  ? 16.938  4.663   4.779   1.00 40.95 ?  55  GLU D OE2   1 
ATOM   2719 N N     . LYS B 1 64  ? 12.817  -0.866  4.578   1.00 31.40 ?  56  LYS D N     1 
ATOM   2720 C CA    . LYS B 1 64  ? 12.372  -2.044  3.841   1.00 32.85 ?  56  LYS D CA    1 
ATOM   2721 C C     . LYS B 1 64  ? 10.858  -2.040  3.664   1.00 33.12 ?  56  LYS D C     1 
ATOM   2722 O O     . LYS B 1 64  ? 10.349  -2.134  2.542   1.00 30.32 ?  56  LYS D O     1 
ATOM   2723 C CB    . LYS B 1 64  ? 12.830  -3.312  4.565   1.00 33.46 ?  56  LYS D CB    1 
ATOM   2724 C CG    . LYS B 1 64  ? 12.734  -4.577  3.734   1.00 35.01 ?  56  LYS D CG    1 
ATOM   2725 C CD    . LYS B 1 64  ? 12.418  -5.776  4.611   1.00 39.83 ?  56  LYS D CD    1 
ATOM   2726 C CE    . LYS B 1 64  ? 12.773  -7.082  3.922   1.00 35.42 ?  56  LYS D CE    1 
ATOM   2727 N NZ    . LYS B 1 64  ? 12.650  -8.237  4.851   1.00 42.87 ?  56  LYS D NZ    1 
ATOM   2728 N N     . ALA B 1 65  ? 10.119  -1.932  4.771   1.00 30.10 ?  57  ALA D N     1 
ATOM   2729 C CA    . ALA B 1 65  ? 8.663   -1.878  4.686   1.00 34.16 ?  57  ALA D CA    1 
ATOM   2730 C C     . ALA B 1 65  ? 8.193   -0.668  3.891   1.00 31.84 ?  57  ALA D C     1 
ATOM   2731 O O     . ALA B 1 65  ? 7.165   -0.736  3.209   1.00 30.36 ?  57  ALA D O     1 
ATOM   2732 C CB    . ALA B 1 65  ? 8.053   -1.860  6.086   1.00 29.10 ?  57  ALA D CB    1 
ATOM   2733 N N     . GLU B 1 66  ? 8.924   0.445   3.973   1.00 30.26 ?  58  GLU D N     1 
ATOM   2734 C CA    . GLU B 1 66  ? 8.596   1.616   3.166   1.00 30.63 ?  58  GLU D CA    1 
ATOM   2735 C C     . GLU B 1 66  ? 8.774   1.321   1.683   1.00 31.79 ?  58  GLU D C     1 
ATOM   2736 O O     . GLU B 1 66  ? 7.885   1.596   0.869   1.00 34.08 ?  58  GLU D O     1 
ATOM   2737 C CB    . GLU B 1 66  ? 9.476   2.794   3.580   1.00 30.12 ?  58  GLU D CB    1 
ATOM   2738 C CG    . GLU B 1 66  ? 8.977   4.147   3.126   1.00 30.77 ?  58  GLU D CG    1 
ATOM   2739 C CD    . GLU B 1 66  ? 9.786   5.277   3.724   1.00 37.59 ?  58  GLU D CD    1 
ATOM   2740 O OE1   . GLU B 1 66  ? 11.009  5.322   3.473   1.00 33.28 ?  58  GLU D OE1   1 
ATOM   2741 O OE2   . GLU B 1 66  ? 9.208   6.110   4.454   1.00 36.06 ?  58  GLU D OE2   1 
ATOM   2742 N N     . ARG B 1 67  ? 9.929   0.762   1.317   1.00 32.94 ?  59  ARG D N     1 
ATOM   2743 C CA    . ARG B 1 67  ? 10.209  0.453   -0.080  1.00 35.96 ?  59  ARG D CA    1 
ATOM   2744 C C     . ARG B 1 67  ? 9.234   -0.584  -0.626  1.00 33.33 ?  59  ARG D C     1 
ATOM   2745 O O     . ARG B 1 67  ? 8.793   -0.488  -1.777  1.00 33.08 ?  59  ARG D O     1 
ATOM   2746 C CB    . ARG B 1 67  ? 11.653  -0.032  -0.212  1.00 33.45 ?  59  ARG D CB    1 
ATOM   2747 C CG    . ARG B 1 67  ? 12.030  -0.616  -1.559  1.00 37.23 ?  59  ARG D CG    1 
ATOM   2748 C CD    . ARG B 1 67  ? 13.522  -0.947  -1.616  1.00 44.29 ?  59  ARG D CD    1 
ATOM   2749 N NE    . ARG B 1 67  ? 13.994  -1.648  -0.425  1.00 41.78 ?  59  ARG D NE    1 
ATOM   2750 C CZ    . ARG B 1 67  ? 14.712  -1.090  0.542   1.00 48.52 ?  59  ARG D CZ    1 
ATOM   2751 N NH1   . ARG B 1 67  ? 15.064  0.185   0.496   1.00 52.20 ?  59  ARG D NH1   1 
ATOM   2752 N NH2   . ARG B 1 67  ? 15.082  -1.830  1.584   1.00 43.01 ?  59  ARG D NH2   1 
ATOM   2753 N N     . GLU B 1 68  ? 8.880   -1.581  0.188   1.00 33.68 ?  60  GLU D N     1 
ATOM   2754 C CA    . GLU B 1 68  ? 7.930   -2.597  -0.247  1.00 34.78 ?  60  GLU D CA    1 
ATOM   2755 C C     . GLU B 1 68  ? 6.516   -2.054  -0.383  1.00 37.02 ?  60  GLU D C     1 
ATOM   2756 O O     . GLU B 1 68  ? 5.698   -2.660  -1.083  1.00 34.94 ?  60  GLU D O     1 
ATOM   2757 C CB    . GLU B 1 68  ? 7.935   -3.771  0.729   1.00 33.42 ?  60  GLU D CB    1 
ATOM   2758 C CG    . GLU B 1 68  ? 9.227   -4.557  0.738   1.00 30.56 ?  60  GLU D CG    1 
ATOM   2759 C CD    . GLU B 1 68  ? 9.242   -5.621  1.812   1.00 38.73 ?  60  GLU D CD    1 
ATOM   2760 O OE1   . GLU B 1 68  ? 8.656   -5.383  2.889   1.00 38.76 ?  60  GLU D OE1   1 
ATOM   2761 O OE2   . GLU B 1 68  ? 9.831   -6.697  1.580   1.00 45.32 ?  60  GLU D OE2   1 
ATOM   2762 N N     . GLY B 1 69  ? 6.212   -0.933  0.264   1.00 39.85 ?  61  GLY D N     1 
ATOM   2763 C CA    . GLY B 1 69  ? 4.872   -0.393  0.263   1.00 28.82 ?  61  GLY D CA    1 
ATOM   2764 C C     . GLY B 1 69  ? 4.002   -0.856  1.409   1.00 33.17 ?  61  GLY D C     1 
ATOM   2765 O O     . GLY B 1 69  ? 2.821   -0.488  1.455   1.00 34.37 ?  61  GLY D O     1 
ATOM   2766 N N     . LYS B 1 70  ? 4.544   -1.654  2.334   1.00 32.44 ?  62  LYS D N     1 
ATOM   2767 C CA    . LYS B 1 70  ? 3.763   -2.089  3.486   1.00 32.84 ?  62  LYS D CA    1 
ATOM   2768 C C     . LYS B 1 70  ? 3.370   -0.912  4.367   1.00 37.40 ?  62  LYS D C     1 
ATOM   2769 O O     . LYS B 1 70  ? 2.322   -0.947  5.021   1.00 33.55 ?  62  LYS D O     1 
ATOM   2770 C CB    . LYS B 1 70  ? 4.548   -3.120  4.299   1.00 35.34 ?  62  LYS D CB    1 
ATOM   2771 C CG    . LYS B 1 70  ? 4.287   -4.563  3.892   1.00 38.24 ?  62  LYS D CG    1 
ATOM   2772 C CD    . LYS B 1 70  ? 5.266   -5.518  4.561   1.00 35.65 ?  62  LYS D CD    1 
ATOM   2773 C CE    . LYS B 1 70  ? 5.785   -6.562  3.585   1.00 40.56 ?  62  LYS D CE    1 
ATOM   2774 N NZ    . LYS B 1 70  ? 5.235   -7.917  3.867   1.00 47.28 ?  62  LYS D NZ    1 
ATOM   2775 N N     . ILE B 1 71  ? 4.193   0.133   4.401   1.00 34.24 ?  63  ILE D N     1 
ATOM   2776 C CA    . ILE B 1 71  ? 3.903   1.335   5.170   1.00 33.20 ?  63  ILE D CA    1 
ATOM   2777 C C     . ILE B 1 71  ? 4.212   2.556   4.318   1.00 33.54 ?  63  ILE D C     1 
ATOM   2778 O O     . ILE B 1 71  ? 5.044   2.513   3.406   1.00 32.72 ?  63  ILE D O     1 
ATOM   2779 C CB    . ILE B 1 71  ? 4.703   1.395   6.491   1.00 29.69 ?  63  ILE D CB    1 
ATOM   2780 C CG1   . ILE B 1 71  ? 6.205   1.343   6.209   1.00 35.57 ?  63  ILE D CG1   1 
ATOM   2781 C CG2   . ILE B 1 71  ? 4.276   0.279   7.433   1.00 28.80 ?  63  ILE D CG2   1 
ATOM   2782 C CD1   . ILE B 1 71  ? 7.069   1.607   7.422   1.00 31.51 ?  63  ILE D CD1   1 
ATOM   2783 N N     . LYS B 1 72  ? 3.523   3.651   4.620   1.00 35.15 ?  64  LYS D N     1 
ATOM   2784 C CA    . LYS B 1 72  ? 3.817   4.967   4.079   1.00 35.16 ?  64  LYS D CA    1 
ATOM   2785 C C     . LYS B 1 72  ? 3.584   5.981   5.187   1.00 32.62 ?  64  LYS D C     1 
ATOM   2786 O O     . LYS B 1 72  ? 2.812   5.712   6.115   1.00 37.61 ?  64  LYS D O     1 
ATOM   2787 C CB    . LYS B 1 72  ? 2.951   5.295   2.850   1.00 38.60 ?  64  LYS D CB    1 
ATOM   2788 C CG    . LYS B 1 72  ? 1.450   5.248   3.092   1.00 38.33 ?  64  LYS D CG    1 
ATOM   2789 C CD    . LYS B 1 72  ? 0.678   5.379   1.782   1.00 41.40 ?  64  LYS D CD    1 
ATOM   2790 C CE    . LYS B 1 72  ? -0.816  5.155   1.980   1.00 45.59 ?  64  LYS D CE    1 
ATOM   2791 N NZ    . LYS B 1 72  ? -1.372  5.980   3.092   1.00 49.96 ?  64  LYS D NZ    1 
ATOM   2792 N N     . PRO B 1 73  ? 4.276   7.138   5.144   1.00 29.93 ?  65  PRO D N     1 
ATOM   2793 C CA    . PRO B 1 73  ? 4.164   8.123   6.233   1.00 36.75 ?  65  PRO D CA    1 
ATOM   2794 C C     . PRO B 1 73  ? 2.747   8.353   6.735   1.00 39.21 ?  65  PRO D C     1 
ATOM   2795 O O     . PRO B 1 73  ? 1.825   8.573   5.942   1.00 37.18 ?  65  PRO D O     1 
ATOM   2796 C CB    . PRO B 1 73  ? 4.736   9.396   5.597   1.00 36.09 ?  65  PRO D CB    1 
ATOM   2797 C CG    . PRO B 1 73  ? 5.751   8.890   4.622   1.00 33.91 ?  65  PRO D CG    1 
ATOM   2798 C CD    . PRO B 1 73  ? 5.339   7.499   4.189   1.00 38.12 ?  65  PRO D CD    1 
ATOM   2799 N N     . GLY B 1 74  ? 2.572   8.303   8.053   1.00 38.66 ?  66  GLY D N     1 
ATOM   2800 C CA    . GLY B 1 74  ? 1.270   8.322   8.683   1.00 32.26 ?  66  GLY D CA    1 
ATOM   2801 C C     . GLY B 1 74  ? 0.848   6.986   9.258   1.00 34.66 ?  66  GLY D C     1 
ATOM   2802 O O     . GLY B 1 74  ? 0.001   6.953   10.161  1.00 34.63 ?  66  GLY D O     1 
ATOM   2803 N N     . ASP B 1 75  ? 1.415   5.887   8.765   1.00 32.98 ?  67  ASP D N     1 
ATOM   2804 C CA    . ASP B 1 75  ? 1.080   4.565   9.270   1.00 29.02 ?  67  ASP D CA    1 
ATOM   2805 C C     . ASP B 1 75  ? 1.708   4.343   10.645  1.00 34.08 ?  67  ASP D C     1 
ATOM   2806 O O     . ASP B 1 75  ? 2.541   5.121   11.119  1.00 31.44 ?  67  ASP D O     1 
ATOM   2807 C CB    . ASP B 1 75  ? 1.540   3.487   8.291   1.00 29.36 ?  67  ASP D CB    1 
ATOM   2808 C CG    . ASP B 1 75  ? 0.596   3.324   7.120   1.00 35.39 ?  67  ASP D CG    1 
ATOM   2809 O OD1   . ASP B 1 75  ? -0.557  3.799   7.210   1.00 31.74 ?  67  ASP D OD1   1 
ATOM   2810 O OD2   . ASP B 1 75  ? 1.004   2.720   6.105   1.00 37.23 ?  67  ASP D OD2   1 
ATOM   2811 N N     . THR B 1 76  ? 1.301   3.252   11.289  1.00 27.27 ?  68  THR D N     1 
ATOM   2812 C CA    . THR B 1 76  ? 1.718   2.938   12.648  1.00 35.01 ?  68  THR D CA    1 
ATOM   2813 C C     . THR B 1 76  ? 2.456   1.607   12.662  1.00 31.25 ?  68  THR D C     1 
ATOM   2814 O O     . THR B 1 76  ? 1.997   0.632   12.057  1.00 37.17 ?  68  THR D O     1 
ATOM   2815 C CB    . THR B 1 76  ? 0.513   2.877   13.593  1.00 38.19 ?  68  THR D CB    1 
ATOM   2816 O OG1   . THR B 1 76  ? -0.034  4.191   13.754  1.00 37.36 ?  68  THR D OG1   1 
ATOM   2817 C CG2   . THR B 1 76  ? 0.928   2.345   14.956  1.00 30.60 ?  68  THR D CG2   1 
ATOM   2818 N N     . ILE B 1 77  ? 3.597   1.574   13.344  1.00 32.77 ?  69  ILE D N     1 
ATOM   2819 C CA    . ILE B 1 77  ? 4.343   0.344   13.574  1.00 35.54 ?  69  ILE D CA    1 
ATOM   2820 C C     . ILE B 1 77  ? 4.194   -0.043  15.039  1.00 34.72 ?  69  ILE D C     1 
ATOM   2821 O O     . ILE B 1 77  ? 3.980   0.807   15.910  1.00 31.80 ?  69  ILE D O     1 
ATOM   2822 C CB    . ILE B 1 77  ? 5.832   0.486   13.184  1.00 32.99 ?  69  ILE D CB    1 
ATOM   2823 C CG1   . ILE B 1 77  ? 6.574   1.400   14.164  1.00 30.34 ?  69  ILE D CG1   1 
ATOM   2824 C CG2   . ILE B 1 77  ? 5.969   1.002   11.760  1.00 34.44 ?  69  ILE D CG2   1 
ATOM   2825 C CD1   . ILE B 1 77  ? 7.467   0.660   15.143  1.00 34.15 ?  69  ILE D CD1   1 
ATOM   2826 N N     . VAL B 1 78  ? 4.300   -1.342  15.309  1.00 30.44 ?  70  VAL D N     1 
ATOM   2827 C CA    . VAL B 1 78  ? 4.240   -1.862  16.669  1.00 31.78 ?  70  VAL D CA    1 
ATOM   2828 C C     . VAL B 1 78  ? 5.364   -2.872  16.855  1.00 29.65 ?  70  VAL D C     1 
ATOM   2829 O O     . VAL B 1 78  ? 5.678   -3.644  15.943  1.00 34.15 ?  70  VAL D O     1 
ATOM   2830 C CB    . VAL B 1 78  ? 2.860   -2.483  16.987  1.00 32.77 ?  70  VAL D CB    1 
ATOM   2831 C CG1   . VAL B 1 78  ? 2.632   -3.768  16.202  1.00 35.00 ?  70  VAL D CG1   1 
ATOM   2832 C CG2   . VAL B 1 78  ? 2.720   -2.730  18.484  1.00 31.21 ?  70  VAL D CG2   1 
ATOM   2833 N N     . GLU B 1 79  ? 5.990   -2.848  18.033  1.00 33.42 ?  71  GLU D N     1 
ATOM   2834 C CA    . GLU B 1 79  ? 7.091   -3.751  18.312  1.00 31.35 ?  71  GLU D CA    1 
ATOM   2835 C C     . GLU B 1 79  ? 7.188   -3.985  19.812  1.00 30.32 ?  71  GLU D C     1 
ATOM   2836 O O     . GLU B 1 79  ? 7.162   -3.013  20.583  1.00 30.59 ?  71  GLU D O     1 
ATOM   2837 C CB    . GLU B 1 79  ? 8.426   -3.214  17.790  1.00 28.93 ?  71  GLU D CB    1 
ATOM   2838 C CG    . GLU B 1 79  ? 9.603   -4.160  18.001  1.00 34.06 ?  71  GLU D CG    1 
ATOM   2839 C CD    . GLU B 1 79  ? 9.675   -5.257  16.954  1.00 33.22 ?  71  GLU D CD    1 
ATOM   2840 O OE1   . GLU B 1 79  ? 8.838   -5.253  16.029  1.00 35.34 ?  71  GLU D OE1   1 
ATOM   2841 O OE2   . GLU B 1 79  ? 10.568  -6.126  17.056  1.00 34.10 ?  71  GLU D OE2   1 
ATOM   2842 N N     . PRO B 1 80  ? 7.299   -5.229  20.249  1.00 33.39 ?  72  PRO D N     1 
ATOM   2843 C CA    . PRO B 1 80  ? 7.555   -5.500  21.667  1.00 28.36 ?  72  PRO D CA    1 
ATOM   2844 C C     . PRO B 1 80  ? 9.040   -5.364  21.959  1.00 33.09 ?  72  PRO D C     1 
ATOM   2845 O O     . PRO B 1 80  ? 9.865   -6.121  21.439  1.00 32.51 ?  72  PRO D O     1 
ATOM   2846 C CB    . PRO B 1 80  ? 7.051   -6.940  21.836  1.00 28.62 ?  72  PRO D CB    1 
ATOM   2847 C CG    . PRO B 1 80  ? 7.319   -7.566  20.500  1.00 29.32 ?  72  PRO D CG    1 
ATOM   2848 C CD    . PRO B 1 80  ? 7.199   -6.466  19.457  1.00 28.33 ?  72  PRO D CD    1 
ATOM   2849 N N     . THR B 1 81  ? 9.393   -4.365  22.762  1.00 33.92 ?  73  THR D N     1 
ATOM   2850 C CA    . THR B 1 81  ? 10.797  -4.059  22.980  1.00 32.85 ?  73  THR D CA    1 
ATOM   2851 C C     . THR B 1 81  ? 10.986  -3.433  24.352  1.00 36.38 ?  73  THR D C     1 
ATOM   2852 O O     . THR B 1 81  ? 10.194  -2.590  24.781  1.00 30.14 ?  73  THR D O     1 
ATOM   2853 C CB    . THR B 1 81  ? 11.350  -3.129  21.889  1.00 30.15 ?  73  THR D CB    1 
ATOM   2854 O OG1   . THR B 1 81  ? 12.615  -2.600  22.301  1.00 34.83 ?  73  THR D OG1   1 
ATOM   2855 C CG2   . THR B 1 81  ? 10.383  -1.989  21.607  1.00 29.99 ?  73  THR D CG2   1 
ATOM   2856 N N     . SER B 1 82  ? 12.048  -3.859  25.028  1.00 32.74 ?  74  SER D N     1 
ATOM   2857 C CA    . SER B 1 82  ? 12.403  -3.351  26.340  1.00 32.21 ?  74  SER D CA    1 
ATOM   2858 C C     . SER B 1 82  ? 13.754  -2.652  26.348  1.00 36.72 ?  74  SER D C     1 
ATOM   2859 O O     . SER B 1 82  ? 14.191  -2.189  27.409  1.00 36.75 ?  74  SER D O     1 
ATOM   2860 C CB    . SER B 1 82  ? 12.408  -4.496  27.363  1.00 36.00 ?  74  SER D CB    1 
ATOM   2861 O OG    . SER B 1 82  ? 13.005  -5.659  26.812  1.00 39.30 ?  74  SER D OG    1 
ATOM   2862 N N     . GLY B 1 83  ? 14.423  -2.557  25.202  1.00 31.67 ?  75  GLY D N     1 
ATOM   2863 C CA    . GLY B 1 83  ? 15.752  -1.985  25.162  1.00 33.74 ?  75  GLY D CA    1 
ATOM   2864 C C     . GLY B 1 83  ? 15.987  -0.980  24.055  1.00 30.93 ?  75  GLY D C     1 
ATOM   2865 O O     . GLY B 1 83  ? 15.133  -0.137  23.765  1.00 30.84 ?  75  GLY D O     1 
ATOM   2866 N N     . ASN B 1 84  ? 17.158  -1.071  23.423  1.00 24.34 ?  76  ASN D N     1 
ATOM   2867 C CA    . ASN B 1 84  ? 17.593  -0.062  22.467  1.00 26.06 ?  76  ASN D CA    1 
ATOM   2868 C C     . ASN B 1 84  ? 16.843  -0.124  21.145  1.00 26.41 ?  76  ASN D C     1 
ATOM   2869 O O     . ASN B 1 84  ? 16.917  0.835   20.368  1.00 28.30 ?  76  ASN D O     1 
ATOM   2870 C CB    . ASN B 1 84  ? 19.094  -0.202  22.222  1.00 26.41 ?  76  ASN D CB    1 
ATOM   2871 C CG    . ASN B 1 84  ? 19.916  0.298   23.384  1.00 27.71 ?  76  ASN D CG    1 
ATOM   2872 O OD1   . ASN B 1 84  ? 19.595  1.319   23.988  1.00 26.10 ?  76  ASN D OD1   1 
ATOM   2873 N ND2   . ASN B 1 84  ? 20.983  -0.416  23.706  1.00 25.70 ?  76  ASN D ND2   1 
ATOM   2874 N N     . THR B 1 85  ? 16.132  -1.218  20.867  1.00 25.02 ?  77  THR D N     1 
ATOM   2875 C CA    . THR B 1 85  ? 15.331  -1.275  19.650  1.00 29.83 ?  77  THR D CA    1 
ATOM   2876 C C     . THR B 1 85  ? 14.132  -0.337  19.734  1.00 29.85 ?  77  THR D C     1 
ATOM   2877 O O     . THR B 1 85  ? 13.751  0.274   18.728  1.00 27.44 ?  77  THR D O     1 
ATOM   2878 C CB    . THR B 1 85  ? 14.892  -2.716  19.383  1.00 31.59 ?  77  THR D CB    1 
ATOM   2879 O OG1   . THR B 1 85  ? 15.989  -3.447  18.822  1.00 33.05 ?  77  THR D OG1   1 
ATOM   2880 C CG2   . THR B 1 85  ? 13.717  -2.768  18.420  1.00 34.00 ?  77  THR D CG2   1 
ATOM   2881 N N     . GLY B 1 86  ? 13.543  -0.187  20.922  1.00 26.69 ?  78  GLY D N     1 
ATOM   2882 C CA    . GLY B 1 86  ? 12.467  0.776   21.081  1.00 26.41 ?  78  GLY D CA    1 
ATOM   2883 C C     . GLY B 1 86  ? 12.934  2.205   20.888  1.00 27.11 ?  78  GLY D C     1 
ATOM   2884 O O     . GLY B 1 86  ? 12.245  3.015   20.262  1.00 33.19 ?  78  GLY D O     1 
ATOM   2885 N N     . ILE B 1 87  ? 14.111  2.536   21.425  1.00 28.08 ?  79  ILE D N     1 
ATOM   2886 C CA    . ILE B 1 87  ? 14.673  3.869   21.229  1.00 31.12 ?  79  ILE D CA    1 
ATOM   2887 C C     . ILE B 1 87  ? 14.972  4.103   19.753  1.00 30.08 ?  79  ILE D C     1 
ATOM   2888 O O     . ILE B 1 87  ? 14.634  5.151   19.190  1.00 28.01 ?  79  ILE D O     1 
ATOM   2889 C CB    . ILE B 1 87  ? 15.932  4.051   22.096  1.00 26.00 ?  79  ILE D CB    1 
ATOM   2890 C CG1   . ILE B 1 87  ? 15.587  3.890   23.578  1.00 27.82 ?  79  ILE D CG1   1 
ATOM   2891 C CG2   . ILE B 1 87  ? 16.562  5.408   21.844  1.00 26.16 ?  79  ILE D CG2   1 
ATOM   2892 C CD1   . ILE B 1 87  ? 16.780  3.574   24.451  1.00 30.31 ?  79  ILE D CD1   1 
ATOM   2893 N N     . GLY B 1 88  ? 15.604  3.122   19.104  1.00 26.21 ?  80  GLY D N     1 
ATOM   2894 C CA    . GLY B 1 88  ? 15.923  3.270   17.693  1.00 31.48 ?  80  GLY D CA    1 
ATOM   2895 C C     . GLY B 1 88  ? 14.690  3.395   16.819  1.00 26.86 ?  80  GLY D C     1 
ATOM   2896 O O     . GLY B 1 88  ? 14.647  4.222   15.906  1.00 25.96 ?  80  GLY D O     1 
ATOM   2897 N N     . LEU B 1 89  ? 13.672  2.572   17.081  1.00 30.51 ?  81  LEU D N     1 
ATOM   2898 C CA    . LEU B 1 89  ? 12.455  2.641   16.278  1.00 25.49 ?  81  LEU D CA    1 
ATOM   2899 C C     . LEU B 1 89  ? 11.685  3.927   16.550  1.00 24.89 ?  81  LEU D C     1 
ATOM   2900 O O     . LEU B 1 89  ? 11.139  4.533   15.622  1.00 29.80 ?  81  LEU D O     1 
ATOM   2901 C CB    . LEU B 1 89  ? 11.577  1.416   16.535  1.00 30.96 ?  81  LEU D CB    1 
ATOM   2902 C CG    . LEU B 1 89  ? 12.004  0.136   15.810  1.00 25.63 ?  81  LEU D CG    1 
ATOM   2903 C CD1   . LEU B 1 89  ? 11.285  -1.086  16.367  1.00 28.95 ?  81  LEU D CD1   1 
ATOM   2904 C CD2   . LEU B 1 89  ? 11.771  0.269   14.314  1.00 30.06 ?  81  LEU D CD2   1 
ATOM   2905 N N     . ALA B 1 90  ? 11.629  4.360   17.811  1.00 24.44 ?  82  ALA D N     1 
ATOM   2906 C CA    . ALA B 1 90  ? 11.012  5.648   18.119  1.00 25.55 ?  82  ALA D CA    1 
ATOM   2907 C C     . ALA B 1 90  ? 11.757  6.784   17.430  1.00 30.40 ?  82  ALA D C     1 
ATOM   2908 O O     . ALA B 1 90  ? 11.142  7.695   16.862  1.00 30.05 ?  82  ALA D O     1 
ATOM   2909 C CB    . ALA B 1 90  ? 10.975  5.867   19.631  1.00 26.78 ?  82  ALA D CB    1 
ATOM   2910 N N     . PHE B 1 91  ? 13.090  6.738   17.473  1.00 28.26 ?  83  PHE D N     1 
ATOM   2911 C CA    . PHE B 1 91  ? 13.914  7.757   16.829  1.00 26.60 ?  83  PHE D CA    1 
ATOM   2912 C C     . PHE B 1 91  ? 13.668  7.797   15.323  1.00 26.63 ?  83  PHE D C     1 
ATOM   2913 O O     . PHE B 1 91  ? 13.475  8.872   14.742  1.00 29.23 ?  83  PHE D O     1 
ATOM   2914 C CB    . PHE B 1 91  ? 15.386  7.481   17.147  1.00 26.22 ?  83  PHE D CB    1 
ATOM   2915 C CG    . PHE B 1 91  ? 16.361  8.109   16.188  1.00 27.08 ?  83  PHE D CG    1 
ATOM   2916 C CD1   . PHE B 1 91  ? 16.338  9.469   15.926  1.00 29.79 ?  83  PHE D CD1   1 
ATOM   2917 C CD2   . PHE B 1 91  ? 17.319  7.328   15.562  1.00 33.12 ?  83  PHE D CD2   1 
ATOM   2918 C CE1   . PHE B 1 91  ? 17.245  10.032  15.047  1.00 33.19 ?  83  PHE D CE1   1 
ATOM   2919 C CE2   . PHE B 1 91  ? 18.227  7.884   14.685  1.00 29.52 ?  83  PHE D CE2   1 
ATOM   2920 C CZ    . PHE B 1 91  ? 18.190  9.239   14.426  1.00 31.94 ?  83  PHE D CZ    1 
ATOM   2921 N N     . VAL B 1 92  ? 13.664  6.631   14.672  1.00 26.38 ?  84  VAL D N     1 
ATOM   2922 C CA    . VAL B 1 92  ? 13.538  6.594   13.217  1.00 27.84 ?  84  VAL D CA    1 
ATOM   2923 C C     . VAL B 1 92  ? 12.116  6.933   12.784  1.00 30.55 ?  84  VAL D C     1 
ATOM   2924 O O     . VAL B 1 92  ? 11.908  7.594   11.758  1.00 31.25 ?  84  VAL D O     1 
ATOM   2925 C CB    . VAL B 1 92  ? 13.988  5.222   12.683  1.00 32.93 ?  84  VAL D CB    1 
ATOM   2926 C CG1   . VAL B 1 92  ? 13.565  5.041   11.232  1.00 29.24 ?  84  VAL D CG1   1 
ATOM   2927 C CG2   . VAL B 1 92  ? 15.494  5.069   12.824  1.00 33.97 ?  84  VAL D CG2   1 
ATOM   2928 N N     . CYS B 1 93  ? 11.116  6.489   13.550  1.00 27.56 ?  85  CYS D N     1 
ATOM   2929 C CA    . CYS B 1 93  ? 9.725   6.763   13.193  1.00 29.38 ?  85  CYS D CA    1 
ATOM   2930 C C     . CYS B 1 93  ? 9.434   8.258   13.208  1.00 29.40 ?  85  CYS D C     1 
ATOM   2931 O O     . CYS B 1 93  ? 8.807   8.789   12.284  1.00 28.00 ?  85  CYS D O     1 
ATOM   2932 C CB    . CYS B 1 93  ? 8.779   6.023   14.138  1.00 23.81 ?  85  CYS D CB    1 
ATOM   2933 S SG    . CYS B 1 93  ? 8.632   4.258   13.793  1.00 30.87 ?  85  CYS D SG    1 
ATOM   2934 N N     . ALA B 1 94  ? 9.876   8.956   14.258  1.00 27.73 ?  86  ALA D N     1 
ATOM   2935 C CA    . ALA B 1 94  ? 9.685   10.401  14.310  1.00 29.23 ?  86  ALA D CA    1 
ATOM   2936 C C     . ALA B 1 94  ? 10.443  11.094  13.186  1.00 29.37 ?  86  ALA D C     1 
ATOM   2937 O O     . ALA B 1 94  ? 9.995   12.122  12.662  1.00 28.48 ?  86  ALA D O     1 
ATOM   2938 C CB    . ALA B 1 94  ? 10.127  10.944  15.670  1.00 28.02 ?  86  ALA D CB    1 
ATOM   2939 N N     . ALA B 1 95  ? 11.589  10.537  12.792  1.00 34.52 ?  87  ALA D N     1 
ATOM   2940 C CA    . ALA B 1 95  ? 12.390  11.151  11.742  1.00 29.54 ?  87  ALA D CA    1 
ATOM   2941 C C     . ALA B 1 95  ? 11.777  10.944  10.364  1.00 32.68 ?  87  ALA D C     1 
ATOM   2942 O O     . ALA B 1 95  ? 11.917  11.807  9.490   1.00 31.95 ?  87  ALA D O     1 
ATOM   2943 C CB    . ALA B 1 95  ? 13.807  10.588  11.775  1.00 30.71 ?  87  ALA D CB    1 
ATOM   2944 N N     . LYS B 1 96  ? 11.102  9.817   10.150  1.00 27.02 ?  88  LYS D N     1 
ATOM   2945 C CA    . LYS B 1 96  ? 10.551  9.472   8.848   1.00 29.21 ?  88  LYS D CA    1 
ATOM   2946 C C     . LYS B 1 96  ? 9.044   9.670   8.766   1.00 29.87 ?  88  LYS D C     1 
ATOM   2947 O O     . LYS B 1 96  ? 8.446   9.345   7.736   1.00 32.27 ?  88  LYS D O     1 
ATOM   2948 C CB    . LYS B 1 96  ? 10.910  8.025   8.495   1.00 28.83 ?  88  LYS D CB    1 
ATOM   2949 C CG    . LYS B 1 96  ? 12.377  7.837   8.138   1.00 28.37 ?  88  LYS D CG    1 
ATOM   2950 C CD    . LYS B 1 96  ? 12.672  6.415   7.701   1.00 30.48 ?  88  LYS D CD    1 
ATOM   2951 C CE    . LYS B 1 96  ? 12.098  6.145   6.324   1.00 37.96 ?  88  LYS D CE    1 
ATOM   2952 N NZ    . LYS B 1 96  ? 12.937  6.722   5.235   1.00 25.99 ?  88  LYS D NZ    1 
ATOM   2953 N N     . GLY B 1 97  ? 8.419   10.192  9.815   1.00 30.17 ?  89  GLY D N     1 
ATOM   2954 C CA    . GLY B 1 97  ? 7.000   10.490  9.770   1.00 28.17 ?  89  GLY D CA    1 
ATOM   2955 C C     . GLY B 1 97  ? 6.093   9.307   10.017  1.00 30.13 ?  89  GLY D C     1 
ATOM   2956 O O     . GLY B 1 97  ? 5.032   9.203   9.390   1.00 33.65 ?  89  GLY D O     1 
ATOM   2957 N N     . TYR B 1 98  ? 6.475   8.410   10.921  1.00 28.86 ?  90  TYR D N     1 
ATOM   2958 C CA    . TYR B 1 98  ? 5.681   7.235   11.240  1.00 28.34 ?  90  TYR D CA    1 
ATOM   2959 C C     . TYR B 1 98  ? 5.262   7.263   12.702  1.00 27.59 ?  90  TYR D C     1 
ATOM   2960 O O     . TYR B 1 98  ? 5.997   7.745   13.568  1.00 31.06 ?  90  TYR D O     1 
ATOM   2961 C CB    . TYR B 1 98  ? 6.455   5.948   10.950  1.00 26.55 ?  90  TYR D CB    1 
ATOM   2962 C CG    . TYR B 1 98  ? 6.633   5.680   9.478   1.00 34.36 ?  90  TYR D CG    1 
ATOM   2963 C CD1   . TYR B 1 98  ? 5.595   5.155   8.723   1.00 29.50 ?  90  TYR D CD1   1 
ATOM   2964 C CD2   . TYR B 1 98  ? 7.832   5.967   8.840   1.00 26.24 ?  90  TYR D CD2   1 
ATOM   2965 C CE1   . TYR B 1 98  ? 5.749   4.913   7.378   1.00 30.63 ?  90  TYR D CE1   1 
ATOM   2966 C CE2   . TYR B 1 98  ? 7.993   5.729   7.492   1.00 30.19 ?  90  TYR D CE2   1 
ATOM   2967 C CZ    . TYR B 1 98  ? 6.949   5.203   6.768   1.00 32.60 ?  90  TYR D CZ    1 
ATOM   2968 O OH    . TYR B 1 98  ? 7.101   4.964   5.425   1.00 33.75 ?  90  TYR D OH    1 
ATOM   2969 N N     . LYS B 1 99  ? 4.068   6.744   12.964  1.00 30.09 ?  91  LYS D N     1 
ATOM   2970 C CA    . LYS B 1 99  ? 3.580   6.586   14.324  1.00 30.26 ?  91  LYS D CA    1 
ATOM   2971 C C     . LYS B 1 99  ? 4.119   5.284   14.902  1.00 30.46 ?  91  LYS D C     1 
ATOM   2972 O O     . LYS B 1 99  ? 4.237   4.280   14.193  1.00 35.78 ?  91  LYS D O     1 
ATOM   2973 C CB    . LYS B 1 99  ? 2.051   6.596   14.357  1.00 33.25 ?  91  LYS D CB    1 
ATOM   2974 C CG    . LYS B 1 99  ? 1.466   7.357   15.537  1.00 42.37 ?  91  LYS D CG    1 
ATOM   2975 C CD    . LYS B 1 99  ? 0.007   7.000   15.774  1.00 54.39 ?  91  LYS D CD    1 
ATOM   2976 C CE    . LYS B 1 99  ? -0.451  7.450   17.155  1.00 59.10 ?  91  LYS D CE    1 
ATOM   2977 N NZ    . LYS B 1 99  ? 0.393   6.875   18.241  1.00 45.92 ?  91  LYS D NZ    1 
ATOM   2978 N N     . ALA B 1 100 ? 4.457   5.307   16.189  1.00 31.28 ?  92  ALA D N     1 
ATOM   2979 C CA    . ALA B 1 100 ? 5.120   4.182   16.834  1.00 32.63 ?  92  ALA D CA    1 
ATOM   2980 C C     . ALA B 1 100 ? 4.364   3.775   18.089  1.00 32.18 ?  92  ALA D C     1 
ATOM   2981 O O     . ALA B 1 100 ? 4.018   4.626   18.915  1.00 30.87 ?  92  ALA D O     1 
ATOM   2982 C CB    . ALA B 1 100 ? 6.572   4.524   17.185  1.00 28.25 ?  92  ALA D CB    1 
ATOM   2983 N N     . VAL B 1 101 ? 4.114   2.475   18.226  1.00 31.86 ?  93  VAL D N     1 
ATOM   2984 C CA    . VAL B 1 101 ? 3.537   1.885   19.428  1.00 31.80 ?  93  VAL D CA    1 
ATOM   2985 C C     . VAL B 1 101 ? 4.481   0.796   19.916  1.00 33.53 ?  93  VAL D C     1 
ATOM   2986 O O     . VAL B 1 101 ? 4.872   -0.085  19.141  1.00 29.12 ?  93  VAL D O     1 
ATOM   2987 C CB    . VAL B 1 101 ? 2.131   1.312   19.171  1.00 31.83 ?  93  VAL D CB    1 
ATOM   2988 C CG1   . VAL B 1 101 ? 1.594   0.643   20.427  1.00 31.31 ?  93  VAL D CG1   1 
ATOM   2989 C CG2   . VAL B 1 101 ? 1.189   2.406   18.700  1.00 32.08 ?  93  VAL D CG2   1 
ATOM   2990 N N     . PHE B 1 102 ? 4.853   0.857   21.190  1.00 29.67 ?  94  PHE D N     1 
ATOM   2991 C CA    . PHE B 1 102 ? 5.742   -0.128  21.790  1.00 31.02 ?  94  PHE D CA    1 
ATOM   2992 C C     . PHE B 1 102 ? 5.066   -0.746  23.003  1.00 33.75 ?  94  PHE D C     1 
ATOM   2993 O O     . PHE B 1 102 ? 4.547   -0.027  23.864  1.00 34.48 ?  94  PHE D O     1 
ATOM   2994 C CB    . PHE B 1 102 ? 7.081   0.499   22.190  1.00 34.80 ?  94  PHE D CB    1 
ATOM   2995 C CG    . PHE B 1 102 ? 7.794   1.186   21.059  1.00 30.02 ?  94  PHE D CG    1 
ATOM   2996 C CD1   . PHE B 1 102 ? 8.276   0.458   19.984  1.00 29.65 ?  94  PHE D CD1   1 
ATOM   2997 C CD2   . PHE B 1 102 ? 7.996   2.556   21.078  1.00 28.24 ?  94  PHE D CD2   1 
ATOM   2998 C CE1   . PHE B 1 102 ? 8.937   1.084   18.944  1.00 25.42 ?  94  PHE D CE1   1 
ATOM   2999 C CE2   . PHE B 1 102 ? 8.658   3.187   20.039  1.00 29.97 ?  94  PHE D CE2   1 
ATOM   3000 C CZ    . PHE B 1 102 ? 9.128   2.450   18.972  1.00 22.59 ?  94  PHE D CZ    1 
ATOM   3001 N N     . THR B 1 103 ? 5.068   -2.073  23.064  1.00 28.89 ?  95  THR D N     1 
ATOM   3002 C CA    . THR B 1 103 ? 4.549   -2.806  24.208  1.00 32.73 ?  95  THR D CA    1 
ATOM   3003 C C     . THR B 1 103 ? 5.717   -3.279  25.061  1.00 33.95 ?  95  THR D C     1 
ATOM   3004 O O     . THR B 1 103 ? 6.707   -3.798  24.535  1.00 34.32 ?  95  THR D O     1 
ATOM   3005 C CB    . THR B 1 103 ? 3.694   -3.994  23.762  1.00 28.67 ?  95  THR D CB    1 
ATOM   3006 O OG1   . THR B 1 103 ? 4.499   -4.915  23.017  1.00 28.87 ?  95  THR D OG1   1 
ATOM   3007 C CG2   . THR B 1 103 ? 2.543   -3.522  22.889  1.00 25.90 ?  95  THR D CG2   1 
ATOM   3008 N N     . MET B 1 104 ? 5.604   -3.085  26.369  1.00 35.94 ?  96  MET D N     1 
ATOM   3009 C CA    . MET B 1 104 ? 6.652   -3.449  27.309  1.00 34.33 ?  96  MET D CA    1 
ATOM   3010 C C     . MET B 1 104 ? 5.998   -3.824  28.626  1.00 34.73 ?  96  MET D C     1 
ATOM   3011 O O     . MET B 1 104 ? 4.847   -3.449  28.880  1.00 35.13 ?  96  MET D O     1 
ATOM   3012 C CB    . MET B 1 104 ? 7.639   -2.294  27.522  1.00 33.45 ?  96  MET D CB    1 
ATOM   3013 C CG    . MET B 1 104 ? 6.962   -0.955  27.718  1.00 32.28 ?  96  MET D CG    1 
ATOM   3014 S SD    . MET B 1 104 ? 8.002   0.421   27.215  1.00 40.42 ?  96  MET D SD    1 
ATOM   3015 C CE    . MET B 1 104 ? 7.088   0.983   25.788  1.00 43.41 ?  96  MET D CE    1 
ATOM   3016 N N     . PRO B 1 105 ? 6.698   -4.562  29.486  1.00 34.47 ?  97  PRO D N     1 
ATOM   3017 C CA    . PRO B 1 105 ? 6.181   -4.773  30.841  1.00 31.88 ?  97  PRO D CA    1 
ATOM   3018 C C     . PRO B 1 105 ? 6.103   -3.456  31.594  1.00 33.26 ?  97  PRO D C     1 
ATOM   3019 O O     . PRO B 1 105 ? 6.913   -2.548  31.391  1.00 32.19 ?  97  PRO D O     1 
ATOM   3020 C CB    . PRO B 1 105 ? 7.202   -5.726  31.478  1.00 31.94 ?  97  PRO D CB    1 
ATOM   3021 C CG    . PRO B 1 105 ? 8.050   -6.231  30.362  1.00 37.23 ?  97  PRO D CG    1 
ATOM   3022 C CD    . PRO B 1 105 ? 7.985   -5.239  29.258  1.00 37.66 ?  97  PRO D CD    1 
ATOM   3023 N N     . GLU B 1 106 ? 5.112   -3.354  32.478  1.00 34.38 ?  98  GLU D N     1 
ATOM   3024 C CA    . GLU B 1 106 ? 4.971   -2.138  33.269  1.00 40.14 ?  98  GLU D CA    1 
ATOM   3025 C C     . GLU B 1 106 ? 6.113   -1.937  34.259  1.00 36.95 ?  98  GLU D C     1 
ATOM   3026 O O     . GLU B 1 106 ? 6.089   -0.957  35.012  1.00 40.27 ?  98  GLU D O     1 
ATOM   3027 C CB    . GLU B 1 106 ? 3.632   -2.146  34.007  1.00 34.66 ?  98  GLU D CB    1 
ATOM   3028 C CG    . GLU B 1 106 ? 3.522   -3.210  35.079  1.00 36.89 ?  98  GLU D CG    1 
ATOM   3029 C CD    . GLU B 1 106 ? 2.093   -3.654  35.305  1.00 45.90 ?  98  GLU D CD    1 
ATOM   3030 O OE1   . GLU B 1 106 ? 1.176   -2.837  35.074  1.00 45.91 ?  98  GLU D OE1   1 
ATOM   3031 O OE2   . GLU B 1 106 ? 1.887   -4.816  35.715  1.00 37.15 ?  98  GLU D OE2   1 
ATOM   3032 N N     . THR B 1 107 ? 7.106   -2.828  34.270  1.00 37.46 ?  99  THR D N     1 
ATOM   3033 C CA    . THR B 1 107 ? 8.285   -2.706  35.117  1.00 39.18 ?  99  THR D CA    1 
ATOM   3034 C C     . THR B 1 107 ? 9.342   -1.772  34.539  1.00 36.46 ?  99  THR D C     1 
ATOM   3035 O O     . THR B 1 107 ? 10.364  -1.543  35.195  1.00 39.68 ?  99  THR D O     1 
ATOM   3036 C CB    . THR B 1 107 ? 8.913   -4.085  35.350  1.00 36.34 ?  99  THR D CB    1 
ATOM   3037 O OG1   . THR B 1 107 ? 9.094   -4.747  34.092  1.00 37.48 ?  99  THR D OG1   1 
ATOM   3038 C CG2   . THR B 1 107 ? 8.021   -4.939  36.238  1.00 37.57 ?  99  THR D CG2   1 
ATOM   3039 N N     . MET B 1 108 ? 9.131   -1.235  33.340  1.00 40.37 ?  100 MET D N     1 
ATOM   3040 C CA    . MET B 1 108 ? 10.133  -0.392  32.705  1.00 43.42 ?  100 MET D CA    1 
ATOM   3041 C C     . MET B 1 108 ? 10.203  0.967   33.386  1.00 41.03 ?  100 MET D C     1 
ATOM   3042 O O     . MET B 1 108 ? 9.181   1.539   33.776  1.00 35.00 ?  100 MET D O     1 
ATOM   3043 C CB    . MET B 1 108 ? 9.827   -0.222  31.217  1.00 35.56 ?  100 MET D CB    1 
ATOM   3044 C CG    . MET B 1 108 ? 9.874   -1.526  30.435  1.00 36.77 ?  100 MET D CG    1 
ATOM   3045 S SD    . MET B 1 108 ? 11.523  -2.131  29.998  1.00 47.16 ?  100 MET D SD    1 
ATOM   3046 C CE    . MET B 1 108 ? 12.550  -0.672  30.195  1.00 45.76 ?  100 MET D CE    1 
ATOM   3047 N N     . SER B 1 109 ? 11.424  1.483   33.514  1.00 41.33 ?  101 SER D N     1 
ATOM   3048 C CA    . SER B 1 109 ? 11.668  2.705   34.267  1.00 34.66 ?  101 SER D CA    1 
ATOM   3049 C C     . SER B 1 109 ? 10.907  3.885   33.675  1.00 40.79 ?  101 SER D C     1 
ATOM   3050 O O     . SER B 1 109 ? 10.608  3.929   32.479  1.00 37.69 ?  101 SER D O     1 
ATOM   3051 C CB    . SER B 1 109 ? 13.166  3.013   34.296  1.00 37.26 ?  101 SER D CB    1 
ATOM   3052 O OG    . SER B 1 109 ? 13.553  3.765   33.159  1.00 32.41 ?  101 SER D OG    1 
ATOM   3053 N N     . GLN B 1 110 ? 10.591  4.853   34.539  1.00 41.60 ?  102 GLN D N     1 
ATOM   3054 C CA    . GLN B 1 110 ? 9.954   6.081   34.077  1.00 40.85 ?  102 GLN D CA    1 
ATOM   3055 C C     . GLN B 1 110 ? 10.884  6.882   33.175  1.00 40.56 ?  102 GLN D C     1 
ATOM   3056 O O     . GLN B 1 110 ? 10.416  7.567   32.257  1.00 40.29 ?  102 GLN D O     1 
ATOM   3057 C CB    . GLN B 1 110 ? 9.505   6.921   35.275  1.00 40.09 ?  102 GLN D CB    1 
ATOM   3058 C CG    . GLN B 1 110 ? 8.825   8.227   34.903  1.00 45.07 ?  102 GLN D CG    1 
ATOM   3059 C CD    . GLN B 1 110 ? 7.414   8.020   34.388  1.00 48.12 ?  102 GLN D CD    1 
ATOM   3060 O OE1   . GLN B 1 110 ? 6.569   7.446   35.074  1.00 50.97 ?  102 GLN D OE1   1 
ATOM   3061 N NE2   . GLN B 1 110 ? 7.154   8.487   33.171  1.00 45.91 ?  102 GLN D NE2   1 
ATOM   3062 N N     . GLU B 1 111 ? 12.197  6.802   33.410  1.00 37.71 ?  103 GLU D N     1 
ATOM   3063 C CA    . GLU B 1 111 ? 13.146  7.475   32.529  1.00 37.35 ?  103 GLU D CA    1 
ATOM   3064 C C     . GLU B 1 111 ? 13.070  6.921   31.111  1.00 36.20 ?  103 GLU D C     1 
ATOM   3065 O O     . GLU B 1 111 ? 13.121  7.681   30.136  1.00 42.34 ?  103 GLU D O     1 
ATOM   3066 C CB    . GLU B 1 111 ? 14.565  7.341   33.086  1.00 36.00 ?  103 GLU D CB    1 
ATOM   3067 N N     . ARG B 1 112 ? 12.936  5.599   30.977  1.00 35.93 ?  104 ARG D N     1 
ATOM   3068 C CA    . ARG B 1 112 ? 12.828  4.990   29.654  1.00 33.32 ?  104 ARG D CA    1 
ATOM   3069 C C     . ARG B 1 112 ? 11.538  5.412   28.964  1.00 35.91 ?  104 ARG D C     1 
ATOM   3070 O O     . ARG B 1 112 ? 11.540  5.759   27.776  1.00 36.02 ?  104 ARG D O     1 
ATOM   3071 C CB    . ARG B 1 112 ? 12.903  3.467   29.770  1.00 35.45 ?  104 ARG D CB    1 
ATOM   3072 C CG    . ARG B 1 112 ? 12.951  2.741   28.433  1.00 43.64 ?  104 ARG D CG    1 
ATOM   3073 C CD    . ARG B 1 112 ? 13.859  3.469   27.444  1.00 39.74 ?  104 ARG D CD    1 
ATOM   3074 N NE    . ARG B 1 112 ? 15.283  3.336   27.739  1.00 36.31 ?  104 ARG D NE    1 
ATOM   3075 C CZ    . ARG B 1 112 ? 15.931  2.190   27.913  1.00 34.26 ?  104 ARG D CZ    1 
ATOM   3076 N NH1   . ARG B 1 112 ? 15.346  1.019   27.714  1.00 35.54 ?  104 ARG D NH1   1 
ATOM   3077 N NH2   . ARG B 1 112 ? 17.214  2.219   28.261  1.00 37.85 ?  104 ARG D NH2   1 
ATOM   3078 N N     . ARG B 1 113 ? 10.421  5.383   29.698  1.00 36.95 ?  105 ARG D N     1 
ATOM   3079 C CA    . ARG B 1 113 ? 9.153   5.849   29.146  1.00 31.95 ?  105 ARG D CA    1 
ATOM   3080 C C     . ARG B 1 113 ? 9.267   7.280   28.640  1.00 36.13 ?  105 ARG D C     1 
ATOM   3081 O O     . ARG B 1 113 ? 8.769   7.605   27.556  1.00 33.40 ?  105 ARG D O     1 
ATOM   3082 C CB    . ARG B 1 113 ? 8.048   5.754   30.199  1.00 38.08 ?  105 ARG D CB    1 
ATOM   3083 C CG    . ARG B 1 113 ? 7.785   4.361   30.740  1.00 36.25 ?  105 ARG D CG    1 
ATOM   3084 C CD    . ARG B 1 113 ? 7.094   4.446   32.091  1.00 36.78 ?  105 ARG D CD    1 
ATOM   3085 N NE    . ARG B 1 113 ? 6.744   3.138   32.631  1.00 45.31 ?  105 ARG D NE    1 
ATOM   3086 C CZ    . ARG B 1 113 ? 5.571   2.848   33.176  1.00 44.23 ?  105 ARG D CZ    1 
ATOM   3087 N NH1   . ARG B 1 113 ? 4.611   3.753   33.272  1.00 43.87 ?  105 ARG D NH1   1 
ATOM   3088 N NH2   . ARG B 1 113 ? 5.356   1.619   33.639  1.00 43.40 ?  105 ARG D NH2   1 
ATOM   3089 N N     . ASN B 1 114 ? 9.928   8.146   29.412  1.00 39.19 ?  106 ASN D N     1 
ATOM   3090 C CA    . ASN B 1 114 ? 10.080  9.539   29.008  1.00 39.03 ?  106 ASN D CA    1 
ATOM   3091 C C     . ASN B 1 114 ? 10.894  9.656   27.726  1.00 33.21 ?  106 ASN D C     1 
ATOM   3092 O O     . ASN B 1 114 ? 10.599  10.498  26.869  1.00 32.19 ?  106 ASN D O     1 
ATOM   3093 C CB    . ASN B 1 114 ? 10.740  10.337  30.133  1.00 38.47 ?  106 ASN D CB    1 
ATOM   3094 C CG    . ASN B 1 114 ? 9.836   10.508  31.339  1.00 40.25 ?  106 ASN D CG    1 
ATOM   3095 O OD1   . ASN B 1 114 ? 8.633   10.257  31.273  1.00 43.77 ?  106 ASN D OD1   1 
ATOM   3096 N ND2   . ASN B 1 114 ? 10.418  10.932  32.454  1.00 46.87 ?  106 ASN D ND2   1 
ATOM   3097 N N     . LEU B 1 115 ? 11.923  8.819   27.577  1.00 33.71 ?  107 LEU D N     1 
ATOM   3098 C CA    . LEU B 1 115 ? 12.746  8.854   26.372  1.00 28.42 ?  107 LEU D CA    1 
ATOM   3099 C C     . LEU B 1 115 ? 11.933  8.471   25.141  1.00 32.80 ?  107 LEU D C     1 
ATOM   3100 O O     . LEU B 1 115 ? 11.988  9.149   24.109  1.00 28.50 ?  107 LEU D O     1 
ATOM   3101 C CB    . LEU B 1 115 ? 13.951  7.926   26.541  1.00 33.03 ?  107 LEU D CB    1 
ATOM   3102 C CG    . LEU B 1 115 ? 14.873  7.734   25.336  1.00 29.28 ?  107 LEU D CG    1 
ATOM   3103 C CD1   . LEU B 1 115 ? 15.327  9.069   24.801  1.00 31.61 ?  107 LEU D CD1   1 
ATOM   3104 C CD2   . LEU B 1 115 ? 16.074  6.890   25.716  1.00 27.56 ?  107 LEU D CD2   1 
ATOM   3105 N N     . LEU B 1 116 ? 11.165  7.384   25.237  1.00 30.12 ?  108 LEU D N     1 
ATOM   3106 C CA    . LEU B 1 116 ? 10.359  6.939   24.104  1.00 25.20 ?  108 LEU D CA    1 
ATOM   3107 C C     . LEU B 1 116 ? 9.266   7.949   23.776  1.00 29.47 ?  108 LEU D C     1 
ATOM   3108 O O     . LEU B 1 116 ? 9.072   8.312   22.609  1.00 26.55 ?  108 LEU D O     1 
ATOM   3109 C CB    . LEU B 1 116 ? 9.755   5.566   24.403  1.00 27.01 ?  108 LEU D CB    1 
ATOM   3110 C CG    . LEU B 1 116 ? 10.744  4.427   24.647  1.00 28.41 ?  108 LEU D CG    1 
ATOM   3111 C CD1   . LEU B 1 116 ? 10.007  3.154   25.026  1.00 32.86 ?  108 LEU D CD1   1 
ATOM   3112 C CD2   . LEU B 1 116 ? 11.615  4.201   23.424  1.00 29.56 ?  108 LEU D CD2   1 
ATOM   3113 N N     . LYS B 1 117 ? 8.541   8.419   24.795  1.00 30.40 ?  109 LYS D N     1 
ATOM   3114 C CA    . LYS B 1 117 ? 7.458   9.367   24.552  1.00 34.04 ?  109 LYS D CA    1 
ATOM   3115 C C     . LYS B 1 117 ? 7.980   10.700  24.028  1.00 31.78 ?  109 LYS D C     1 
ATOM   3116 O O     . LYS B 1 117 ? 7.244   11.425  23.349  1.00 30.51 ?  109 LYS D O     1 
ATOM   3117 C CB    . LYS B 1 117 ? 6.641   9.576   25.828  1.00 32.32 ?  109 LYS D CB    1 
ATOM   3118 C CG    . LYS B 1 117 ? 5.752   8.396   26.198  1.00 33.25 ?  109 LYS D CG    1 
ATOM   3119 C CD    . LYS B 1 117 ? 5.707   8.185   27.704  1.00 41.00 ?  109 LYS D CD    1 
ATOM   3120 C CE    . LYS B 1 117 ? 4.561   8.951   28.340  1.00 46.03 ?  109 LYS D CE    1 
ATOM   3121 N NZ    . LYS B 1 117 ? 4.655   8.946   29.826  1.00 51.61 ?  109 LYS D NZ    1 
ATOM   3122 N N     . ALA B 1 118 ? 9.238   11.038  24.325  1.00 29.52 ?  110 ALA D N     1 
ATOM   3123 C CA    . ALA B 1 118 ? 9.818   12.265  23.790  1.00 30.37 ?  110 ALA D CA    1 
ATOM   3124 C C     . ALA B 1 118 ? 9.877   12.239  22.268  1.00 34.11 ?  110 ALA D C     1 
ATOM   3125 O O     . ALA B 1 118 ? 9.763   13.289  21.624  1.00 33.18 ?  110 ALA D O     1 
ATOM   3126 C CB    . ALA B 1 118 ? 11.214  12.486  24.373  1.00 27.04 ?  110 ALA D CB    1 
ATOM   3127 N N     . TYR B 1 119 ? 10.053  11.057  21.677  1.00 29.70 ?  111 TYR D N     1 
ATOM   3128 C CA    . TYR B 1 119 ? 10.015  10.881  20.231  1.00 31.04 ?  111 TYR D CA    1 
ATOM   3129 C C     . TYR B 1 119 ? 8.595   10.789  19.687  1.00 29.96 ?  111 TYR D C     1 
ATOM   3130 O O     . TYR B 1 119 ? 8.421   10.532  18.491  1.00 27.89 ?  111 TYR D O     1 
ATOM   3131 C CB    . TYR B 1 119 ? 10.795  9.627   19.828  1.00 25.86 ?  111 TYR D CB    1 
ATOM   3132 C CG    . TYR B 1 119 ? 12.296  9.794   19.839  1.00 27.83 ?  111 TYR D CG    1 
ATOM   3133 C CD1   . TYR B 1 119 ? 12.928  10.638  18.934  1.00 23.16 ?  111 TYR D CD1   1 
ATOM   3134 C CD2   . TYR B 1 119 ? 13.084  9.100   20.748  1.00 26.86 ?  111 TYR D CD2   1 
ATOM   3135 C CE1   . TYR B 1 119 ? 14.303  10.791  18.939  1.00 27.74 ?  111 TYR D CE1   1 
ATOM   3136 C CE2   . TYR B 1 119 ? 14.459  9.246   20.760  1.00 25.09 ?  111 TYR D CE2   1 
ATOM   3137 C CZ    . TYR B 1 119 ? 15.063  10.091  19.854  1.00 27.54 ?  111 TYR D CZ    1 
ATOM   3138 O OH    . TYR B 1 119 ? 16.432  10.237  19.866  1.00 31.10 ?  111 TYR D OH    1 
ATOM   3139 N N     . GLY B 1 120 ? 7.585   10.982  20.533  1.00 29.93 ?  112 GLY D N     1 
ATOM   3140 C CA    . GLY B 1 120 ? 6.202   10.878  20.124  1.00 27.31 ?  112 GLY D CA    1 
ATOM   3141 C C     . GLY B 1 120 ? 5.626   9.480   20.166  1.00 29.10 ?  112 GLY D C     1 
ATOM   3142 O O     . GLY B 1 120 ? 4.479   9.288   19.740  1.00 32.34 ?  112 GLY D O     1 
ATOM   3143 N N     . ALA B 1 121 ? 6.377   8.503   20.668  1.00 33.73 ?  113 ALA D N     1 
ATOM   3144 C CA    . ALA B 1 121 ? 5.917   7.123   20.675  1.00 32.67 ?  113 ALA D CA    1 
ATOM   3145 C C     . ALA B 1 121 ? 4.773   6.929   21.664  1.00 29.93 ?  113 ALA D C     1 
ATOM   3146 O O     . ALA B 1 121 ? 4.677   7.616   22.685  1.00 34.11 ?  113 ALA D O     1 
ATOM   3147 C CB    . ALA B 1 121 ? 7.068   6.182   21.026  1.00 29.76 ?  113 ALA D CB    1 
ATOM   3148 N N     . GLU B 1 122 ? 3.900   5.978   21.345  1.00 32.34 ?  114 GLU D N     1 
ATOM   3149 C CA    . GLU B 1 122 ? 2.822   5.565   22.232  1.00 30.42 ?  114 GLU D CA    1 
ATOM   3150 C C     . GLU B 1 122 ? 3.213   4.263   22.917  1.00 34.93 ?  114 GLU D C     1 
ATOM   3151 O O     . GLU B 1 122 ? 3.659   3.319   22.256  1.00 33.61 ?  114 GLU D O     1 
ATOM   3152 C CB    . GLU B 1 122 ? 1.514   5.388   21.459  1.00 37.61 ?  114 GLU D CB    1 
ATOM   3153 C CG    . GLU B 1 122 ? 0.274   5.346   22.338  1.00 41.22 ?  114 GLU D CG    1 
ATOM   3154 C CD    . GLU B 1 122 ? -0.790  4.407   21.800  1.00 51.43 ?  114 GLU D CD    1 
ATOM   3155 O OE1   . GLU B 1 122 ? -1.386  3.659   22.604  1.00 52.43 ?  114 GLU D OE1   1 
ATOM   3156 O OE2   . GLU B 1 122 ? -1.030  4.417   20.574  1.00 57.03 ?  114 GLU D OE2   1 
ATOM   3157 N N     . LEU B 1 123 ? 3.051   4.215   24.235  1.00 29.32 ?  115 LEU D N     1 
ATOM   3158 C CA    . LEU B 1 123 ? 3.452   3.065   25.031  1.00 34.12 ?  115 LEU D CA    1 
ATOM   3159 C C     . LEU B 1 123 ? 2.222   2.299   25.494  1.00 35.04 ?  115 LEU D C     1 
ATOM   3160 O O     . LEU B 1 123 ? 1.236   2.896   25.935  1.00 34.09 ?  115 LEU D O     1 
ATOM   3161 C CB    . LEU B 1 123 ? 4.283   3.489   26.245  1.00 31.25 ?  115 LEU D CB    1 
ATOM   3162 C CG    . LEU B 1 123 ? 5.409   4.509   26.052  1.00 28.07 ?  115 LEU D CG    1 
ATOM   3163 C CD1   . LEU B 1 123 ? 6.343   4.479   27.248  1.00 31.00 ?  115 LEU D CD1   1 
ATOM   3164 C CD2   . LEU B 1 123 ? 6.183   4.276   24.763  1.00 30.18 ?  115 LEU D CD2   1 
ATOM   3165 N N     . VAL B 1 124 ? 2.286   0.977   25.387  1.00 31.91 ?  116 VAL D N     1 
ATOM   3166 C CA    . VAL B 1 124 ? 1.228   0.089   25.855  1.00 33.54 ?  116 VAL D CA    1 
ATOM   3167 C C     . VAL B 1 124 ? 1.866   -0.825  26.892  1.00 35.14 ?  116 VAL D C     1 
ATOM   3168 O O     . VAL B 1 124 ? 2.594   -1.762  26.546  1.00 32.09 ?  116 VAL D O     1 
ATOM   3169 C CB    . VAL B 1 124 ? 0.590   -0.713  24.717  1.00 31.01 ?  116 VAL D CB    1 
ATOM   3170 C CG1   . VAL B 1 124 ? -0.347  -1.777  25.276  1.00 33.85 ?  116 VAL D CG1   1 
ATOM   3171 C CG2   . VAL B 1 124 ? -0.155  0.217   23.777  1.00 27.02 ?  116 VAL D CG2   1 
ATOM   3172 N N     . LEU B 1 125 ? 1.605   -0.552  28.164  1.00 32.14 ?  117 LEU D N     1 
ATOM   3173 C CA    . LEU B 1 125 ? 2.211   -1.321  29.238  1.00 33.32 ?  117 LEU D CA    1 
ATOM   3174 C C     . LEU B 1 125 ? 1.467   -2.634  29.444  1.00 36.33 ?  117 LEU D C     1 
ATOM   3175 O O     . LEU B 1 125 ? 0.235   -2.675  29.466  1.00 35.57 ?  117 LEU D O     1 
ATOM   3176 C CB    . LEU B 1 125 ? 2.228   -0.505  30.527  1.00 34.12 ?  117 LEU D CB    1 
ATOM   3177 C CG    . LEU B 1 125 ? 2.914   0.853   30.376  1.00 29.89 ?  117 LEU D CG    1 
ATOM   3178 C CD1   . LEU B 1 125 ? 2.612   1.735   31.570  1.00 41.00 ?  117 LEU D CD1   1 
ATOM   3179 C CD2   . LEU B 1 125 ? 4.418   0.686   30.189  1.00 29.79 ?  117 LEU D CD2   1 
ATOM   3180 N N     . THR B 1 126 ? 2.231   -3.707  29.587  1.00 34.39 ?  118 THR D N     1 
ATOM   3181 C CA    . THR B 1 126 ? 1.749   -5.068  29.749  1.00 33.90 ?  118 THR D CA    1 
ATOM   3182 C C     . THR B 1 126 ? 2.098   -5.567  31.146  1.00 36.05 ?  118 THR D C     1 
ATOM   3183 O O     . THR B 1 126 ? 2.943   -4.973  31.828  1.00 33.58 ?  118 THR D O     1 
ATOM   3184 C CB    . THR B 1 126 ? 2.371   -5.992  28.688  1.00 34.54 ?  118 THR D CB    1 
ATOM   3185 O OG1   . THR B 1 126 ? 3.795   -6.009  28.845  1.00 34.24 ?  118 THR D OG1   1 
ATOM   3186 C CG2   . THR B 1 126 ? 2.025   -5.500  27.300  1.00 35.91 ?  118 THR D CG2   1 
ATOM   3187 N N     . PRO B 1 127 ? 1.462   -6.645  31.609  1.00 38.74 ?  119 PRO D N     1 
ATOM   3188 C CA    . PRO B 1 127 ? 1.726   -7.137  32.969  1.00 36.04 ?  119 PRO D CA    1 
ATOM   3189 C C     . PRO B 1 127 ? 3.209   -7.350  33.240  1.00 31.08 ?  119 PRO D C     1 
ATOM   3190 O O     . PRO B 1 127 ? 3.927   -7.961  32.445  1.00 33.79 ?  119 PRO D O     1 
ATOM   3191 C CB    . PRO B 1 127 ? 0.949   -8.456  33.017  1.00 30.55 ?  119 PRO D CB    1 
ATOM   3192 C CG    . PRO B 1 127 ? -0.177  -8.252  32.069  1.00 31.56 ?  119 PRO D CG    1 
ATOM   3193 C CD    . PRO B 1 127 ? 0.354   -7.381  30.968  1.00 35.64 ?  119 PRO D CD    1 
ATOM   3194 N N     . GLY B 1 128 ? 3.666   -6.831  34.381  1.00 33.82 ?  120 GLY D N     1 
ATOM   3195 C CA    . GLY B 1 128 ? 5.069   -6.970  34.734  1.00 31.99 ?  120 GLY D CA    1 
ATOM   3196 C C     . GLY B 1 128 ? 5.472   -8.414  34.957  1.00 34.64 ?  120 GLY D C     1 
ATOM   3197 O O     . GLY B 1 128 ? 6.589   -8.816  34.626  1.00 33.71 ?  120 GLY D O     1 
ATOM   3198 N N     . SER B 1 129 ? 4.561   -9.218  35.513  1.00 31.93 ?  121 SER D N     1 
ATOM   3199 C CA    . SER B 1 129 ? 4.856   -10.624 35.760  1.00 32.98 ?  121 SER D CA    1 
ATOM   3200 C C     . SER B 1 129 ? 5.045   -11.414 34.473  1.00 34.41 ?  121 SER D C     1 
ATOM   3201 O O     . SER B 1 129 ? 5.723   -12.447 34.491  1.00 36.90 ?  121 SER D O     1 
ATOM   3202 C CB    . SER B 1 129 ? 3.742   -11.254 36.595  1.00 31.35 ?  121 SER D CB    1 
ATOM   3203 O OG    . SER B 1 129 ? 2.468   -10.960 36.049  1.00 29.85 ?  121 SER D OG    1 
ATOM   3204 N N     . GLU B 1 130 ? 4.467   -10.959 33.362  1.00 31.25 ?  122 GLU D N     1 
ATOM   3205 C CA    . GLU B 1 130 ? 4.579   -11.665 32.094  1.00 33.32 ?  122 GLU D CA    1 
ATOM   3206 C C     . GLU B 1 130 ? 5.841   -11.309 31.320  1.00 35.52 ?  122 GLU D C     1 
ATOM   3207 O O     . GLU B 1 130 ? 6.115   -11.942 30.295  1.00 32.20 ?  122 GLU D O     1 
ATOM   3208 C CB    . GLU B 1 130 ? 3.349   -11.387 31.227  1.00 29.10 ?  122 GLU D CB    1 
ATOM   3209 C CG    . GLU B 1 130 ? 2.055   -11.951 31.795  1.00 35.65 ?  122 GLU D CG    1 
ATOM   3210 C CD    . GLU B 1 130 ? 2.050   -13.466 31.850  1.00 35.63 ?  122 GLU D CD    1 
ATOM   3211 O OE1   . GLU B 1 130 ? 2.690   -14.099 30.983  1.00 33.76 ?  122 GLU D OE1   1 
ATOM   3212 O OE2   . GLU B 1 130 ? 1.407   -14.026 32.763  1.00 34.52 ?  122 GLU D OE2   1 
ATOM   3213 N N     . ALA B 1 131 ? 6.605   -10.317 31.784  1.00 29.98 ?  123 ALA D N     1 
ATOM   3214 C CA    . ALA B 1 131 ? 7.870   -9.924  31.171  1.00 33.19 ?  123 ALA D CA    1 
ATOM   3215 C C     . ALA B 1 131 ? 7.719   -9.656  29.678  1.00 33.07 ?  123 ALA D C     1 
ATOM   3216 O O     . ALA B 1 131 ? 6.735   -9.046  29.246  1.00 30.55 ?  123 ALA D O     1 
ATOM   3217 C CB    . ALA B 1 131 ? 8.936   -10.996 31.411  1.00 28.64 ?  123 ALA D CB    1 
ATOM   3218 N N     . MET B 1 132 ? 8.691   -10.112 28.884  1.00 27.48 ?  124 MET D N     1 
ATOM   3219 C CA    . MET B 1 132 ? 8.644   -9.895  27.444  1.00 30.89 ?  124 MET D CA    1 
ATOM   3220 C C     . MET B 1 132 ? 7.616   -10.785 26.760  1.00 35.98 ?  124 MET D C     1 
ATOM   3221 O O     . MET B 1 132 ? 7.188   -10.470 25.644  1.00 33.76 ?  124 MET D O     1 
ATOM   3222 C CB    . MET B 1 132 ? 10.027  -10.133 26.836  1.00 32.19 ?  124 MET D CB    1 
ATOM   3223 C CG    . MET B 1 132 ? 10.983  -8.962  26.995  1.00 37.09 ?  124 MET D CG    1 
ATOM   3224 S SD    . MET B 1 132 ? 10.148  -7.379  27.209  1.00 37.61 ?  124 MET D SD    1 
ATOM   3225 C CE    . MET B 1 132 ? 9.856   -6.925  25.501  1.00 31.57 ?  124 MET D CE    1 
ATOM   3226 N N     . LYS B 1 133 ? 7.216   -11.885 27.401  1.00 32.30 ?  125 LYS D N     1 
ATOM   3227 C CA    . LYS B 1 133 ? 6.177   -12.742 26.837  1.00 36.43 ?  125 LYS D CA    1 
ATOM   3228 C C     . LYS B 1 133 ? 4.862   -11.984 26.700  1.00 33.13 ?  125 LYS D C     1 
ATOM   3229 O O     . LYS B 1 133 ? 4.187   -12.068 25.667  1.00 32.51 ?  125 LYS D O     1 
ATOM   3230 C CB    . LYS B 1 133 ? 6.000   -13.983 27.712  1.00 40.17 ?  125 LYS D CB    1 
ATOM   3231 C CG    . LYS B 1 133 ? 4.849   -14.888 27.311  1.00 36.96 ?  125 LYS D CG    1 
ATOM   3232 C CD    . LYS B 1 133 ? 4.793   -16.104 28.220  1.00 49.42 ?  125 LYS D CD    1 
ATOM   3233 C CE    . LYS B 1 133 ? 3.670   -17.049 27.835  1.00 47.78 ?  125 LYS D CE    1 
ATOM   3234 N NZ    . LYS B 1 133 ? 3.670   -18.259 28.704  1.00 55.85 ?  125 LYS D NZ    1 
ATOM   3235 N N     . GLY B 1 134 ? 4.483   -11.232 27.737  1.00 31.32 ?  126 GLY D N     1 
ATOM   3236 C CA    . GLY B 1 134 ? 3.264   -10.446 27.669  1.00 34.65 ?  126 GLY D CA    1 
ATOM   3237 C C     . GLY B 1 134 ? 3.340   -9.308  26.671  1.00 33.84 ?  126 GLY D C     1 
ATOM   3238 O O     . GLY B 1 134 ? 2.327   -8.945  26.063  1.00 31.85 ?  126 GLY D O     1 
ATOM   3239 N N     . ALA B 1 135 ? 4.531   -8.730  26.490  1.00 32.45 ?  127 ALA D N     1 
ATOM   3240 C CA    . ALA B 1 135 ? 4.699   -7.675  25.496  1.00 32.56 ?  127 ALA D CA    1 
ATOM   3241 C C     . ALA B 1 135 ? 4.575   -8.226  24.081  1.00 27.79 ?  127 ALA D C     1 
ATOM   3242 O O     . ALA B 1 135 ? 3.947   -7.601  23.218  1.00 32.12 ?  127 ALA D O     1 
ATOM   3243 C CB    . ALA B 1 135 ? 6.049   -6.984  25.685  1.00 33.98 ?  127 ALA D CB    1 
ATOM   3244 N N     . ILE B 1 136 ? 5.174   -9.389  23.821  1.00 28.19 ?  128 ILE D N     1 
ATOM   3245 C CA    . ILE B 1 136 ? 5.027   -10.020 22.513  1.00 30.52 ?  128 ILE D CA    1 
ATOM   3246 C C     . ILE B 1 136 ? 3.564   -10.342 22.247  1.00 34.70 ?  128 ILE D C     1 
ATOM   3247 O O     . ILE B 1 136 ? 3.049   -10.113 21.146  1.00 33.54 ?  128 ILE D O     1 
ATOM   3248 C CB    . ILE B 1 136 ? 5.909   -11.279 22.423  1.00 32.21 ?  128 ILE D CB    1 
ATOM   3249 C CG1   . ILE B 1 136 ? 7.363   -10.892 22.157  1.00 32.01 ?  128 ILE D CG1   1 
ATOM   3250 C CG2   . ILE B 1 136 ? 5.397   -12.224 21.347  1.00 26.53 ?  128 ILE D CG2   1 
ATOM   3251 C CD1   . ILE B 1 136 ? 8.347   -11.962 22.552  1.00 29.23 ?  128 ILE D CD1   1 
ATOM   3252 N N     . LYS B 1 137 ? 2.869   -10.861 23.261  1.00 33.13 ?  129 LYS D N     1 
ATOM   3253 C CA    . LYS B 1 137 ? 1.461   -11.209 23.105  1.00 32.72 ?  129 LYS D CA    1 
ATOM   3254 C C     . LYS B 1 137 ? 0.614   -9.980  22.798  1.00 36.06 ?  129 LYS D C     1 
ATOM   3255 O O     . LYS B 1 137 ? -0.309  -10.043 21.977  1.00 40.38 ?  129 LYS D O     1 
ATOM   3256 C CB    . LYS B 1 137 ? 0.962   -11.905 24.372  1.00 37.63 ?  129 LYS D CB    1 
ATOM   3257 C CG    . LYS B 1 137 ? -0.502  -12.300 24.344  1.00 42.57 ?  129 LYS D CG    1 
ATOM   3258 C CD    . LYS B 1 137 ? -0.839  -13.212 25.514  1.00 46.30 ?  129 LYS D CD    1 
ATOM   3259 C CE    . LYS B 1 137 ? -2.315  -13.574 25.534  1.00 45.86 ?  129 LYS D CE    1 
ATOM   3260 N NZ    . LYS B 1 137 ? -3.084  -12.689 26.455  1.00 51.42 ?  129 LYS D NZ    1 
ATOM   3261 N N     . LYS B 1 138 ? 0.915   -8.852  23.446  1.00 34.05 ?  130 LYS D N     1 
ATOM   3262 C CA    . LYS B 1 138 ? 0.119   -7.646  23.241  1.00 32.62 ?  130 LYS D CA    1 
ATOM   3263 C C     . LYS B 1 138 ? 0.386   -7.028  21.875  1.00 31.68 ?  130 LYS D C     1 
ATOM   3264 O O     . LYS B 1 138 ? -0.540  -6.531  21.222  1.00 33.55 ?  130 LYS D O     1 
ATOM   3265 C CB    . LYS B 1 138 ? 0.404   -6.635  24.348  1.00 33.24 ?  130 LYS D CB    1 
ATOM   3266 C CG    . LYS B 1 138 ? -0.408  -5.358  24.242  1.00 31.50 ?  130 LYS D CG    1 
ATOM   3267 C CD    . LYS B 1 138 ? -1.818  -5.572  24.760  1.00 36.55 ?  130 LYS D CD    1 
ATOM   3268 C CE    . LYS B 1 138 ? -2.837  -4.881  23.872  1.00 40.48 ?  130 LYS D CE    1 
ATOM   3269 N NZ    . LYS B 1 138 ? -4.231  -5.024  24.380  1.00 52.10 ?  130 LYS D NZ    1 
ATOM   3270 N N     . ALA B 1 139 ? 1.646   -7.036  21.432  1.00 29.37 ?  131 ALA D N     1 
ATOM   3271 C CA    . ALA B 1 139 ? 1.965   -6.510  20.109  1.00 32.07 ?  131 ALA D CA    1 
ATOM   3272 C C     . ALA B 1 139 ? 1.263   -7.303  19.013  1.00 34.88 ?  131 ALA D C     1 
ATOM   3273 O O     . ALA B 1 139 ? 0.773   -6.725  18.036  1.00 32.80 ?  131 ALA D O     1 
ATOM   3274 C CB    . ALA B 1 139 ? 3.477   -6.515  19.888  1.00 30.04 ?  131 ALA D CB    1 
ATOM   3275 N N     . LYS B 1 140 ? 1.213   -8.631  19.151  1.00 35.38 ?  132 LYS D N     1 
ATOM   3276 C CA    . LYS B 1 140 ? 0.485   -9.440  18.180  1.00 37.23 ?  132 LYS D CA    1 
ATOM   3277 C C     . LYS B 1 140 ? -0.996  -9.093  18.170  1.00 40.13 ?  132 LYS D C     1 
ATOM   3278 O O     . LYS B 1 140 ? -1.628  -9.071  17.110  1.00 41.18 ?  132 LYS D O     1 
ATOM   3279 C CB    . LYS B 1 140 ? 0.679   -10.924 18.477  1.00 44.48 ?  132 LYS D CB    1 
ATOM   3280 C CG    . LYS B 1 140 ? 2.106   -11.404 18.297  1.00 44.15 ?  132 LYS D CG    1 
ATOM   3281 C CD    . LYS B 1 140 ? 2.626   -11.163 16.872  1.00 43.70 ?  132 LYS D CD    1 
ATOM   3282 C CE    . LYS B 1 140 ? 4.046   -11.693 16.715  1.00 45.82 ?  132 LYS D CE    1 
ATOM   3283 N NZ    . LYS B 1 140 ? 4.207   -13.029 17.368  1.00 50.38 ?  132 LYS D NZ    1 
ATOM   3284 N N     . GLU B 1 141 ? -1.568  -8.823  19.342  1.00 37.95 ?  133 GLU D N     1 
ATOM   3285 C CA    . GLU B 1 141 ? -2.989  -8.502  19.407  1.00 37.89 ?  133 GLU D CA    1 
ATOM   3286 C C     . GLU B 1 141 ? -3.296  -7.178  18.717  1.00 40.84 ?  133 GLU D C     1 
ATOM   3287 O O     . GLU B 1 141 ? -4.283  -7.072  17.980  1.00 40.54 ?  133 GLU D O     1 
ATOM   3288 C CB    . GLU B 1 141 ? -3.457  -8.474  20.862  1.00 37.93 ?  133 GLU D CB    1 
ATOM   3289 C CG    . GLU B 1 141 ? -3.696  -9.853  21.450  1.00 41.58 ?  133 GLU D CG    1 
ATOM   3290 C CD    . GLU B 1 141 ? -3.788  -9.836  22.961  1.00 40.76 ?  133 GLU D CD    1 
ATOM   3291 O OE1   . GLU B 1 141 ? -4.222  -8.809  23.524  1.00 50.20 ?  133 GLU D OE1   1 
ATOM   3292 O OE2   . GLU B 1 141 ? -3.420  -10.851 23.587  1.00 46.10 ?  133 GLU D OE2   1 
ATOM   3293 N N     . LEU B 1 142 ? -2.468  -6.156  18.943  1.00 35.55 ?  134 LEU D N     1 
ATOM   3294 C CA    . LEU B 1 142 ? -2.677  -4.880  18.266  1.00 39.27 ?  134 LEU D CA    1 
ATOM   3295 C C     . LEU B 1 142 ? -2.427  -4.989  16.768  1.00 37.40 ?  134 LEU D C     1 
ATOM   3296 O O     . LEU B 1 142 ? -3.045  -4.263  15.982  1.00 38.45 ?  134 LEU D O     1 
ATOM   3297 C CB    . LEU B 1 142 ? -1.773  -3.807  18.871  1.00 40.33 ?  134 LEU D CB    1 
ATOM   3298 C CG    . LEU B 1 142 ? -1.993  -3.470  20.345  1.00 34.21 ?  134 LEU D CG    1 
ATOM   3299 C CD1   . LEU B 1 142 ? -0.812  -2.687  20.897  1.00 27.27 ?  134 LEU D CD1   1 
ATOM   3300 C CD2   . LEU B 1 142 ? -3.284  -2.691  20.525  1.00 38.34 ?  134 LEU D CD2   1 
ATOM   3301 N N     . LYS B 1 143 ? -1.524  -5.882  16.358  1.00 36.60 ?  135 LYS D N     1 
ATOM   3302 C CA    . LYS B 1 143 ? -1.218  -6.033  14.940  1.00 45.84 ?  135 LYS D CA    1 
ATOM   3303 C C     . LYS B 1 143 ? -2.388  -6.659  14.193  1.00 47.19 ?  135 LYS D C     1 
ATOM   3304 O O     . LYS B 1 143 ? -2.694  -6.270  13.061  1.00 44.89 ?  135 LYS D O     1 
ATOM   3305 C CB    . LYS B 1 143 ? 0.051   -6.872  14.778  1.00 42.16 ?  135 LYS D CB    1 
ATOM   3306 C CG    . LYS B 1 143 ? 0.186   -7.618  13.458  1.00 48.59 ?  135 LYS D CG    1 
ATOM   3307 C CD    . LYS B 1 143 ? 1.472   -8.439  13.438  1.00 43.81 ?  135 LYS D CD    1 
ATOM   3308 C CE    . LYS B 1 143 ? 1.826   -8.927  12.040  1.00 50.33 ?  135 LYS D CE    1 
ATOM   3309 N NZ    . LYS B 1 143 ? 2.803   -10.056 12.085  1.00 54.41 ?  135 LYS D NZ    1 
ATOM   3310 N N     . GLU B 1 144 ? -3.063  -7.623  14.816  1.00 45.12 ?  136 GLU D N     1 
ATOM   3311 C CA    . GLU B 1 144 ? -4.209  -8.248  14.166  1.00 46.87 ?  136 GLU D CA    1 
ATOM   3312 C C     . GLU B 1 144 ? -5.446  -7.359  14.239  1.00 48.05 ?  136 GLU D C     1 
ATOM   3313 O O     . GLU B 1 144 ? -6.270  -7.354  13.317  1.00 50.97 ?  136 GLU D O     1 
ATOM   3314 C CB    . GLU B 1 144 ? -4.492  -9.612  14.799  1.00 47.80 ?  136 GLU D CB    1 
ATOM   3315 C CG    . GLU B 1 144 ? -3.785  -10.827 14.171  1.00 59.03 ?  136 GLU D CG    1 
ATOM   3316 C CD    . GLU B 1 144 ? -2.257  -10.784 14.153  1.00 65.46 ?  136 GLU D CD    1 
ATOM   3317 O OE1   . GLU B 1 144 ? -1.643  -9.799  14.620  1.00 78.58 ?  136 GLU D OE1   1 
ATOM   3318 O OE2   . GLU B 1 144 ? -1.658  -11.756 13.660  1.00 72.58 ?  136 GLU D OE2   1 
ATOM   3319 N N     . GLU B 1 145 ? -5.598  -6.603  15.327  1.00 42.60 ?  137 GLU D N     1 
ATOM   3320 C CA    . GLU B 1 145 ? -6.806  -5.807  15.506  1.00 45.13 ?  137 GLU D CA    1 
ATOM   3321 C C     . GLU B 1 145 ? -6.760  -4.517  14.693  1.00 49.76 ?  137 GLU D C     1 
ATOM   3322 O O     . GLU B 1 145 ? -7.780  -4.098  14.133  1.00 49.66 ?  137 GLU D O     1 
ATOM   3323 C CB    . GLU B 1 145 ? -7.010  -5.502  16.991  1.00 40.38 ?  137 GLU D CB    1 
ATOM   3324 C CG    . GLU B 1 145 ? -7.860  -4.281  17.270  1.00 49.98 ?  137 GLU D CG    1 
ATOM   3325 C CD    . GLU B 1 145 ? -8.338  -4.229  18.705  1.00 57.61 ?  137 GLU D CD    1 
ATOM   3326 O OE1   . GLU B 1 145 ? -7.658  -4.807  19.581  1.00 59.32 ?  137 GLU D OE1   1 
ATOM   3327 O OE2   . GLU B 1 145 ? -9.390  -3.606  18.957  1.00 65.28 ?  137 GLU D OE2   1 
ATOM   3328 N N     . HIS B 1 146 ? -5.590  -3.881  14.603  1.00 43.54 ?  138 HIS D N     1 
ATOM   3329 C CA    . HIS B 1 146 ? -5.464  -2.595  13.931  1.00 40.88 ?  138 HIS D CA    1 
ATOM   3330 C C     . HIS B 1 146 ? -4.660  -2.641  12.639  1.00 43.21 ?  138 HIS D C     1 
ATOM   3331 O O     . HIS B 1 146 ? -4.644  -1.643  11.910  1.00 45.00 ?  138 HIS D O     1 
ATOM   3332 C CB    . HIS B 1 146 ? -4.824  -1.562  14.870  1.00 45.27 ?  138 HIS D CB    1 
ATOM   3333 C CG    . HIS B 1 146 ? -5.632  -1.274  16.095  1.00 47.90 ?  138 HIS D CG    1 
ATOM   3334 N ND1   . HIS B 1 146 ? -5.436  -1.932  17.290  1.00 46.97 ?  138 HIS D ND1   1 
ATOM   3335 C CD2   . HIS B 1 146 ? -6.647  -0.404  16.307  1.00 46.41 ?  138 HIS D CD2   1 
ATOM   3336 C CE1   . HIS B 1 146 ? -6.290  -1.473  18.188  1.00 43.42 ?  138 HIS D CE1   1 
ATOM   3337 N NE2   . HIS B 1 146 ? -7.038  -0.547  17.616  1.00 52.47 ?  138 HIS D NE2   1 
ATOM   3338 N N     . GLY B 1 147 ? -3.995  -3.752  12.335  1.00 39.96 ?  139 GLY D N     1 
ATOM   3339 C CA    . GLY B 1 147 ? -3.209  -3.823  11.118  1.00 38.92 ?  139 GLY D CA    1 
ATOM   3340 C C     . GLY B 1 147 ? -1.902  -3.063  11.169  1.00 41.98 ?  139 GLY D C     1 
ATOM   3341 O O     . GLY B 1 147 ? -1.395  -2.648  10.122  1.00 40.67 ?  139 GLY D O     1 
ATOM   3342 N N     . TYR B 1 148 ? -1.347  -2.859  12.362  1.00 43.19 ?  140 TYR D N     1 
ATOM   3343 C CA    . TYR B 1 148 ? -0.044  -2.219  12.478  1.00 39.41 ?  140 TYR D CA    1 
ATOM   3344 C C     . TYR B 1 148 ? 1.030   -3.093  11.842  1.00 33.59 ?  140 TYR D C     1 
ATOM   3345 O O     . TYR B 1 148 ? 0.911   -4.319  11.783  1.00 39.63 ?  140 TYR D O     1 
ATOM   3346 C CB    . TYR B 1 148 ? 0.308   -1.970  13.947  1.00 40.31 ?  140 TYR D CB    1 
ATOM   3347 C CG    . TYR B 1 148 ? -0.633  -1.051  14.694  1.00 37.32 ?  140 TYR D CG    1 
ATOM   3348 C CD1   . TYR B 1 148 ? -1.411  -0.117  14.023  1.00 37.33 ?  140 TYR D CD1   1 
ATOM   3349 C CD2   . TYR B 1 148 ? -0.740  -1.121  16.078  1.00 40.55 ?  140 TYR D CD2   1 
ATOM   3350 C CE1   . TYR B 1 148 ? -2.268  0.724   14.712  1.00 40.53 ?  140 TYR D CE1   1 
ATOM   3351 C CE2   . TYR B 1 148 ? -1.595  -0.288  16.773  1.00 37.23 ?  140 TYR D CE2   1 
ATOM   3352 C CZ    . TYR B 1 148 ? -2.357  0.632   16.086  1.00 43.15 ?  140 TYR D CZ    1 
ATOM   3353 O OH    . TYR B 1 148 ? -3.208  1.462   16.779  1.00 43.46 ?  140 TYR D OH    1 
ATOM   3354 N N     . PHE B 1 149 ? 2.093   -2.449  11.365  1.00 35.97 ?  141 PHE D N     1 
ATOM   3355 C CA    . PHE B 1 149 ? 3.259   -3.178  10.886  1.00 35.59 ?  141 PHE D CA    1 
ATOM   3356 C C     . PHE B 1 149 ? 4.143   -3.572  12.062  1.00 35.97 ?  141 PHE D C     1 
ATOM   3357 O O     . PHE B 1 149 ? 4.442   -2.747  12.931  1.00 33.40 ?  141 PHE D O     1 
ATOM   3358 C CB    . PHE B 1 149 ? 4.064   -2.341  9.895   1.00 32.19 ?  141 PHE D CB    1 
ATOM   3359 C CG    . PHE B 1 149 ? 5.317   -3.019  9.421   1.00 32.36 ?  141 PHE D CG    1 
ATOM   3360 C CD1   . PHE B 1 149 ? 5.250   -4.180  8.671   1.00 36.23 ?  141 PHE D CD1   1 
ATOM   3361 C CD2   . PHE B 1 149 ? 6.562   -2.514  9.755   1.00 32.88 ?  141 PHE D CD2   1 
ATOM   3362 C CE1   . PHE B 1 149 ? 6.399   -4.813  8.244   1.00 31.61 ?  141 PHE D CE1   1 
ATOM   3363 C CE2   . PHE B 1 149 ? 7.714   -3.145  9.333   1.00 30.65 ?  141 PHE D CE2   1 
ATOM   3364 C CZ    . PHE B 1 149 ? 7.633   -4.296  8.576   1.00 29.83 ?  141 PHE D CZ    1 
ATOM   3365 N N     . GLU B 1 150 ? 4.563   -4.832  12.091  1.00 32.23 ?  142 GLU D N     1 
ATOM   3366 C CA    . GLU B 1 150 ? 5.451   -5.301  13.146  1.00 34.76 ?  142 GLU D CA    1 
ATOM   3367 C C     . GLU B 1 150 ? 6.825   -5.574  12.556  1.00 31.68 ?  142 GLU D C     1 
ATOM   3368 O O     . GLU B 1 150 ? 6.971   -6.507  11.750  1.00 33.02 ?  142 GLU D O     1 
ATOM   3369 C CB    . GLU B 1 150 ? 4.895   -6.557  13.820  1.00 32.15 ?  142 GLU D CB    1 
ATOM   3370 C CG    . GLU B 1 150 ? 5.496   -6.816  15.197  1.00 37.08 ?  142 GLU D CG    1 
ATOM   3371 C CD    . GLU B 1 150 ? 5.344   -8.255  15.651  1.00 45.10 ?  142 GLU D CD    1 
ATOM   3372 O OE1   . GLU B 1 150 ? 4.801   -9.071  14.875  1.00 44.31 ?  142 GLU D OE1   1 
ATOM   3373 O OE2   . GLU B 1 150 ? 5.772   -8.570  16.783  1.00 42.76 ?  142 GLU D OE2   1 
ATOM   3374 N N     . PRO B 1 151 ? 7.848   -4.782  12.896  1.00 30.55 ?  143 PRO D N     1 
ATOM   3375 C CA    . PRO B 1 151 ? 9.188   -5.045  12.343  1.00 30.00 ?  143 PRO D CA    1 
ATOM   3376 C C     . PRO B 1 151 ? 9.715   -6.437  12.649  1.00 30.70 ?  143 PRO D C     1 
ATOM   3377 O O     . PRO B 1 151 ? 10.344  -7.054  11.779  1.00 30.66 ?  143 PRO D O     1 
ATOM   3378 C CB    . PRO B 1 151 ? 10.050  -3.953  12.993  1.00 30.24 ?  143 PRO D CB    1 
ATOM   3379 C CG    . PRO B 1 151 ? 9.096   -2.848  13.303  1.00 31.58 ?  143 PRO D CG    1 
ATOM   3380 C CD    . PRO B 1 151 ? 7.775   -3.495  13.609  1.00 30.74 ?  143 PRO D CD    1 
ATOM   3381 N N     . GLN B 1 152 ? 9.468   -6.951  13.857  1.00 29.07 ?  144 GLN D N     1 
ATOM   3382 C CA    . GLN B 1 152 ? 9.970   -8.253  14.288  1.00 32.91 ?  144 GLN D CA    1 
ATOM   3383 C C     . GLN B 1 152 ? 11.490  -8.305  14.192  1.00 30.79 ?  144 GLN D C     1 
ATOM   3384 O O     . GLN B 1 152 ? 12.041  -8.875  13.245  1.00 32.25 ?  144 GLN D O     1 
ATOM   3385 C CB    . GLN B 1 152 ? 9.342   -9.382  13.463  1.00 37.42 ?  144 GLN D CB    1 
ATOM   3386 C CG    . GLN B 1 152 ? 7.830   -9.481  13.589  1.00 37.02 ?  144 GLN D CG    1 
ATOM   3387 C CD    . GLN B 1 152 ? 7.237   -10.558 12.701  1.00 41.09 ?  144 GLN D CD    1 
ATOM   3388 O OE1   . GLN B 1 152 ? 7.958   -11.277 12.010  1.00 45.44 ?  144 GLN D OE1   1 
ATOM   3389 N NE2   . GLN B 1 152 ? 5.913   -10.673 12.715  1.00 44.09 ?  144 GLN D NE2   1 
ATOM   3390 N N     . GLN B 1 153 ? 12.175  -7.719  15.177  1.00 28.27 ?  145 GLN D N     1 
ATOM   3391 C CA    . GLN B 1 153 ? 13.629  -7.614  15.129  1.00 30.91 ?  145 GLN D CA    1 
ATOM   3392 C C     . GLN B 1 153 ? 14.328  -8.968  15.201  1.00 30.38 ?  145 GLN D C     1 
ATOM   3393 O O     . GLN B 1 153 ? 15.491  -9.070  14.795  1.00 29.18 ?  145 GLN D O     1 
ATOM   3394 C CB    . GLN B 1 153 ? 14.120  -6.721  16.268  1.00 31.08 ?  145 GLN D CB    1 
ATOM   3395 C CG    . GLN B 1 153 ? 13.627  -7.146  17.643  1.00 27.62 ?  145 GLN D CG    1 
ATOM   3396 C CD    . GLN B 1 153 ? 14.382  -6.460  18.761  1.00 33.41 ?  145 GLN D CD    1 
ATOM   3397 O OE1   . GLN B 1 153 ? 15.522  -6.033  18.581  1.00 30.16 ?  145 GLN D OE1   1 
ATOM   3398 N NE2   . GLN B 1 153 ? 13.748  -6.346  19.924  1.00 28.36 ?  145 GLN D NE2   1 
ATOM   3399 N N     . PHE B 1 154 ? 13.657  -10.004 15.702  1.00 31.25 ?  146 PHE D N     1 
ATOM   3400 C CA    . PHE B 1 154 ? 14.273  -11.316 15.843  1.00 32.91 ?  146 PHE D CA    1 
ATOM   3401 C C     . PHE B 1 154 ? 14.046  -12.221 14.639  1.00 33.87 ?  146 PHE D C     1 
ATOM   3402 O O     . PHE B 1 154 ? 14.615  -13.317 14.594  1.00 32.31 ?  146 PHE D O     1 
ATOM   3403 C CB    . PHE B 1 154 ? 13.756  -12.008 17.108  1.00 34.87 ?  146 PHE D CB    1 
ATOM   3404 C CG    . PHE B 1 154 ? 14.170  -11.328 18.383  1.00 32.61 ?  146 PHE D CG    1 
ATOM   3405 C CD1   . PHE B 1 154 ? 15.464  -11.457 18.861  1.00 32.32 ?  146 PHE D CD1   1 
ATOM   3406 C CD2   . PHE B 1 154 ? 13.268  -10.560 19.102  1.00 28.98 ?  146 PHE D CD2   1 
ATOM   3407 C CE1   . PHE B 1 154 ? 15.852  -10.832 20.033  1.00 32.07 ?  146 PHE D CE1   1 
ATOM   3408 C CE2   . PHE B 1 154 ? 13.649  -9.933  20.275  1.00 29.52 ?  146 PHE D CE2   1 
ATOM   3409 C CZ    . PHE B 1 154 ? 14.942  -10.070 20.741  1.00 32.07 ?  146 PHE D CZ    1 
ATOM   3410 N N     . GLU B 1 155 ? 13.232  -11.796 13.670  1.00 33.96 ?  147 GLU D N     1 
ATOM   3411 C CA    . GLU B 1 155 ? 12.999  -12.569 12.458  1.00 31.34 ?  147 GLU D CA    1 
ATOM   3412 C C     . GLU B 1 155 ? 13.236  -11.789 11.174  1.00 34.60 ?  147 GLU D C     1 
ATOM   3413 O O     . GLU B 1 155 ? 13.323  -12.410 10.109  1.00 40.47 ?  147 GLU D O     1 
ATOM   3414 C CB    . GLU B 1 155 ? 11.565  -13.124 12.432  1.00 31.10 ?  147 GLU D CB    1 
ATOM   3415 C CG    . GLU B 1 155 ? 10.900  -13.247 13.795  1.00 39.49 ?  147 GLU D CG    1 
ATOM   3416 C CD    . GLU B 1 155 ? 11.477  -14.372 14.630  1.00 49.66 ?  147 GLU D CD    1 
ATOM   3417 O OE1   . GLU B 1 155 ? 12.066  -15.308 14.046  1.00 50.02 ?  147 GLU D OE1   1 
ATOM   3418 O OE2   . GLU B 1 155 ? 11.340  -14.321 15.871  1.00 51.63 ?  147 GLU D OE2   1 
ATOM   3419 N N     . ASN B 1 156 ? 13.345  -10.467 11.231  1.00 32.99 ?  148 ASN D N     1 
ATOM   3420 C CA    . ASN B 1 156 ? 13.464  -9.665  10.020  1.00 31.97 ?  148 ASN D CA    1 
ATOM   3421 C C     . ASN B 1 156 ? 14.857  -9.827  9.424   1.00 29.60 ?  148 ASN D C     1 
ATOM   3422 O O     . ASN B 1 156 ? 15.843  -9.477  10.082  1.00 31.84 ?  148 ASN D O     1 
ATOM   3423 C CB    . ASN B 1 156 ? 13.189  -8.198  10.327  1.00 28.71 ?  148 ASN D CB    1 
ATOM   3424 C CG    . ASN B 1 156 ? 12.794  -7.410  9.096   1.00 29.68 ?  148 ASN D CG    1 
ATOM   3425 O OD1   . ASN B 1 156 ? 13.323  -7.627  8.006   1.00 26.53 ?  148 ASN D OD1   1 
ATOM   3426 N ND2   . ASN B 1 156 ? 11.849  -6.493  9.262   1.00 25.61 ?  148 ASN D ND2   1 
ATOM   3427 N N     . PRO B 1 157 ? 14.987  -10.342 8.197   1.00 34.59 ?  149 PRO D N     1 
ATOM   3428 C CA    . PRO B 1 157 ? 16.327  -10.471 7.600   1.00 30.53 ?  149 PRO D CA    1 
ATOM   3429 C C     . PRO B 1 157 ? 16.987  -9.138  7.302   1.00 29.03 ?  149 PRO D C     1 
ATOM   3430 O O     . PRO B 1 157 ? 18.200  -9.110  7.063   1.00 30.93 ?  149 PRO D O     1 
ATOM   3431 C CB    . PRO B 1 157 ? 16.074  -11.269 6.310   1.00 29.88 ?  149 PRO D CB    1 
ATOM   3432 C CG    . PRO B 1 157 ? 14.653  -11.744 6.380   1.00 34.16 ?  149 PRO D CG    1 
ATOM   3433 C CD    . PRO B 1 157 ? 13.924  -10.820 7.300   1.00 33.89 ?  149 PRO D CD    1 
ATOM   3434 N N     . ALA B 1 158 ? 16.236  -8.036  7.300   1.00 29.63 ?  150 ALA D N     1 
ATOM   3435 C CA    . ALA B 1 158 ? 16.854  -6.723  7.166   1.00 32.22 ?  150 ALA D CA    1 
ATOM   3436 C C     . ALA B 1 158 ? 17.748  -6.390  8.353   1.00 30.09 ?  150 ALA D C     1 
ATOM   3437 O O     . ALA B 1 158 ? 18.630  -5.529  8.230   1.00 28.61 ?  150 ALA D O     1 
ATOM   3438 C CB    . ALA B 1 158 ? 15.775  -5.653  6.993   1.00 25.55 ?  150 ALA D CB    1 
ATOM   3439 N N     . ASN B 1 159 ? 17.535  -7.053  9.498   1.00 30.25 ?  151 ASN D N     1 
ATOM   3440 C CA    . ASN B 1 159 ? 18.394  -6.823  10.658  1.00 26.60 ?  151 ASN D CA    1 
ATOM   3441 C C     . ASN B 1 159 ? 19.824  -7.283  10.380  1.00 29.66 ?  151 ASN D C     1 
ATOM   3442 O O     . ASN B 1 159 ? 20.740  -6.443  10.414  1.00 27.69 ?  151 ASN D O     1 
ATOM   3443 C CB    . ASN B 1 159 ? 17.752  -7.480  11.887  1.00 29.35 ?  151 ASN D CB    1 
ATOM   3444 C CG    . ASN B 1 159 ? 18.633  -7.435  13.137  1.00 28.37 ?  151 ASN D CG    1 
ATOM   3445 O OD1   . ASN B 1 159 ? 19.796  -7.048  13.107  1.00 24.77 ?  151 ASN D OD1   1 
ATOM   3446 N ND2   . ASN B 1 159 ? 18.057  -7.861  14.258  1.00 22.93 ?  151 ASN D ND2   1 
ATOM   3447 N N     . PRO B 1 160 ? 20.095  -8.564  10.078  1.00 29.15 ?  152 PRO D N     1 
ATOM   3448 C CA    . PRO B 1 160 ? 21.492  -8.933  9.797   1.00 27.09 ?  152 PRO D CA    1 
ATOM   3449 C C     . PRO B 1 160 ? 21.994  -8.370  8.484   1.00 32.44 ?  152 PRO D C     1 
ATOM   3450 O O     . PRO B 1 160 ? 23.206  -8.197  8.328   1.00 28.85 ?  152 PRO D O     1 
ATOM   3451 C CB    . PRO B 1 160 ? 21.454  -10.464 9.779   1.00 29.63 ?  152 PRO D CB    1 
ATOM   3452 C CG    . PRO B 1 160 ? 20.074  -10.809 9.408   1.00 31.33 ?  152 PRO D CG    1 
ATOM   3453 C CD    . PRO B 1 160 ? 19.194  -9.736  9.986   1.00 28.23 ?  152 PRO D CD    1 
ATOM   3454 N N     . GLU B 1 161 ? 21.099  -8.078  7.536   1.00 32.45 ?  153 GLU D N     1 
ATOM   3455 C CA    . GLU B 1 161 ? 21.538  -7.589  6.234   1.00 35.34 ?  153 GLU D CA    1 
ATOM   3456 C C     . GLU B 1 161 ? 22.142  -6.193  6.339   1.00 34.11 ?  153 GLU D C     1 
ATOM   3457 O O     . GLU B 1 161 ? 23.126  -5.886  5.655   1.00 31.62 ?  153 GLU D O     1 
ATOM   3458 C CB    . GLU B 1 161 ? 20.370  -7.604  5.246   1.00 37.85 ?  153 GLU D CB    1 
ATOM   3459 C CG    . GLU B 1 161 ? 20.482  -6.580  4.127   1.00 40.52 ?  153 GLU D CG    1 
ATOM   3460 C CD    . GLU B 1 161 ? 19.447  -6.784  3.037   1.00 46.96 ?  153 GLU D CD    1 
ATOM   3461 O OE1   . GLU B 1 161 ? 19.677  -7.638  2.153   1.00 51.19 ?  153 GLU D OE1   1 
ATOM   3462 O OE2   . GLU B 1 161 ? 18.406  -6.093  3.060   1.00 50.75 ?  153 GLU D OE2   1 
ATOM   3463 N N     . VAL B 1 162 ? 21.575  -5.335  7.193   1.00 34.11 ?  154 VAL D N     1 
ATOM   3464 C CA    . VAL B 1 162 ? 22.101  -3.978  7.319   1.00 30.91 ?  154 VAL D CA    1 
ATOM   3465 C C     . VAL B 1 162 ? 23.510  -3.999  7.894   1.00 31.72 ?  154 VAL D C     1 
ATOM   3466 O O     . VAL B 1 162 ? 24.327  -3.122  7.590   1.00 32.40 ?  154 VAL D O     1 
ATOM   3467 C CB    . VAL B 1 162 ? 21.150  -3.099  8.157   1.00 28.56 ?  154 VAL D CB    1 
ATOM   3468 C CG1   . VAL B 1 162 ? 21.305  -3.371  9.645   1.00 25.90 ?  154 VAL D CG1   1 
ATOM   3469 C CG2   . VAL B 1 162 ? 21.388  -1.625  7.855   1.00 29.39 ?  154 VAL D CG2   1 
ATOM   3470 N N     . HIS B 1 163 ? 23.828  -5.000  8.717   1.00 29.90 ?  155 HIS D N     1 
ATOM   3471 C CA    . HIS B 1 163 ? 25.199  -5.170  9.176   1.00 29.78 ?  155 HIS D CA    1 
ATOM   3472 C C     . HIS B 1 163 ? 26.080  -5.751  8.081   1.00 34.30 ?  155 HIS D C     1 
ATOM   3473 O O     . HIS B 1 163 ? 27.291  -5.500  8.062   1.00 36.53 ?  155 HIS D O     1 
ATOM   3474 C CB    . HIS B 1 163 ? 25.228  -6.060  10.419  1.00 33.26 ?  155 HIS D CB    1 
ATOM   3475 C CG    . HIS B 1 163 ? 24.636  -5.414  11.631  1.00 31.58 ?  155 HIS D CG    1 
ATOM   3476 N ND1   . HIS B 1 163 ? 25.203  -4.316  12.242  1.00 29.16 ?  155 HIS D ND1   1 
ATOM   3477 C CD2   . HIS B 1 163 ? 23.519  -5.703  12.340  1.00 28.71 ?  155 HIS D CD2   1 
ATOM   3478 C CE1   . HIS B 1 163 ? 24.465  -3.961  13.278  1.00 30.70 ?  155 HIS D CE1   1 
ATOM   3479 N NE2   . HIS B 1 163 ? 23.437  -4.787  13.360  1.00 27.16 ?  155 HIS D NE2   1 
ATOM   3480 N N     . GLU B 1 164 ? 25.490  -6.523  7.165   1.00 36.95 ?  156 GLU D N     1 
ATOM   3481 C CA    . GLU B 1 164 ? 26.232  -7.031  6.016   1.00 36.47 ?  156 GLU D CA    1 
ATOM   3482 C C     . GLU B 1 164 ? 26.553  -5.924  5.022   1.00 35.44 ?  156 GLU D C     1 
ATOM   3483 O O     . GLU B 1 164 ? 27.556  -6.007  4.304   1.00 35.22 ?  156 GLU D O     1 
ATOM   3484 C CB    . GLU B 1 164 ? 25.429  -8.134  5.325   1.00 35.91 ?  156 GLU D CB    1 
ATOM   3485 C CG    . GLU B 1 164 ? 26.199  -8.924  4.280   1.00 41.56 ?  156 GLU D CG    1 
ATOM   3486 C CD    . GLU B 1 164 ? 25.302  -9.860  3.491   1.00 50.94 ?  156 GLU D CD    1 
ATOM   3487 O OE1   . GLU B 1 164 ? 24.217  -10.214 3.998   1.00 48.96 ?  156 GLU D OE1   1 
ATOM   3488 O OE2   . GLU B 1 164 ? 25.676  -10.231 2.358   1.00 54.71 ?  156 GLU D OE2   1 
ATOM   3489 N N     . LEU B 1 165 ? 25.720  -4.886  4.965   1.00 33.16 ?  157 LEU D N     1 
ATOM   3490 C CA    . LEU B 1 165 ? 25.882  -3.812  3.993   1.00 32.41 ?  157 LEU D CA    1 
ATOM   3491 C C     . LEU B 1 165 ? 26.637  -2.607  4.531   1.00 32.67 ?  157 LEU D C     1 
ATOM   3492 O O     . LEU B 1 165 ? 27.285  -1.903  3.749   1.00 34.57 ?  157 LEU D O     1 
ATOM   3493 C CB    . LEU B 1 165 ? 24.515  -3.337  3.490   1.00 34.91 ?  157 LEU D CB    1 
ATOM   3494 C CG    . LEU B 1 165 ? 23.680  -4.341  2.698   1.00 33.76 ?  157 LEU D CG    1 
ATOM   3495 C CD1   . LEU B 1 165 ? 22.241  -3.863  2.619   1.00 38.04 ?  157 LEU D CD1   1 
ATOM   3496 C CD2   . LEU B 1 165 ? 24.268  -4.554  1.314   1.00 34.71 ?  157 LEU D CD2   1 
ATOM   3497 N N     . THR B 1 166 ? 26.570  -2.335  5.834   1.00 33.06 ?  158 THR D N     1 
ATOM   3498 C CA    . THR B 1 166 ? 27.155  -1.113  6.378   1.00 32.53 ?  158 THR D CA    1 
ATOM   3499 C C     . THR B 1 166 ? 28.206  -1.390  7.443   1.00 31.63 ?  158 THR D C     1 
ATOM   3500 O O     . THR B 1 166 ? 29.371  -1.029  7.253   1.00 32.46 ?  158 THR D O     1 
ATOM   3501 C CB    . THR B 1 166 ? 26.056  -0.203  6.941   1.00 29.02 ?  158 THR D CB    1 
ATOM   3502 O OG1   . THR B 1 166 ? 25.348  -0.889  7.980   1.00 33.80 ?  158 THR D OG1   1 
ATOM   3503 C CG2   . THR B 1 166 ? 25.084  0.203   5.849   1.00 29.46 ?  158 THR D CG2   1 
ATOM   3504 N N     . THR B 1 167 ? 27.829  -2.009  8.564   1.00 31.26 ?  159 THR D N     1 
ATOM   3505 C CA    . THR B 1 167 ? 28.773  -2.206  9.661   1.00 32.34 ?  159 THR D CA    1 
ATOM   3506 C C     . THR B 1 167 ? 29.979  -3.022  9.211   1.00 31.66 ?  159 THR D C     1 
ATOM   3507 O O     . THR B 1 167 ? 31.127  -2.669  9.505   1.00 30.34 ?  159 THR D O     1 
ATOM   3508 C CB    . THR B 1 167 ? 28.079  -2.891  10.838  1.00 29.53 ?  159 THR D CB    1 
ATOM   3509 O OG1   . THR B 1 167 ? 26.753  -2.371  10.981  1.00 29.70 ?  159 THR D OG1   1 
ATOM   3510 C CG2   . THR B 1 167 ? 28.855  -2.647  12.124  1.00 26.66 ?  159 THR D CG2   1 
ATOM   3511 N N     . GLY B 1 168 ? 29.733  -4.117  8.497   1.00 32.28 ?  160 GLY D N     1 
ATOM   3512 C CA    . GLY B 1 168 ? 30.787  -4.978  8.013   1.00 32.44 ?  160 GLY D CA    1 
ATOM   3513 C C     . GLY B 1 168 ? 31.743  -4.271  7.073   1.00 34.57 ?  160 GLY D C     1 
ATOM   3514 O O     . GLY B 1 168 ? 32.945  -4.171  7.341   1.00 33.13 ?  160 GLY D O     1 
ATOM   3515 N N     . PRO B 1 169 ? 31.229  -3.778  5.941   1.00 31.21 ?  161 PRO D N     1 
ATOM   3516 C CA    . PRO B 1 169 ? 32.085  -3.018  5.015   1.00 34.45 ?  161 PRO D CA    1 
ATOM   3517 C C     . PRO B 1 169 ? 32.790  -1.839  5.660   1.00 36.25 ?  161 PRO D C     1 
ATOM   3518 O O     . PRO B 1 169 ? 33.897  -1.482  5.235   1.00 32.95 ?  161 PRO D O     1 
ATOM   3519 C CB    . PRO B 1 169 ? 31.098  -2.561  3.934   1.00 31.67 ?  161 PRO D CB    1 
ATOM   3520 C CG    . PRO B 1 169 ? 30.047  -3.615  3.931   1.00 31.37 ?  161 PRO D CG    1 
ATOM   3521 C CD    . PRO B 1 169 ? 29.900  -4.053  5.363   1.00 31.67 ?  161 PRO D CD    1 
ATOM   3522 N N     . GLU B 1 170 ? 32.177  -1.212  6.669   1.00 32.34 ?  162 GLU D N     1 
ATOM   3523 C CA    . GLU B 1 170 ? 32.860  -0.160  7.415   1.00 31.04 ?  162 GLU D CA    1 
ATOM   3524 C C     . GLU B 1 170 ? 34.152  -0.683  8.026   1.00 33.84 ?  162 GLU D C     1 
ATOM   3525 O O     . GLU B 1 170 ? 35.213  -0.061  7.898   1.00 34.87 ?  162 GLU D O     1 
ATOM   3526 C CB    . GLU B 1 170 ? 31.941  0.391   8.506   1.00 30.04 ?  162 GLU D CB    1 
ATOM   3527 C CG    . GLU B 1 170 ? 31.061  1.542   8.064   1.00 37.34 ?  162 GLU D CG    1 
ATOM   3528 C CD    . GLU B 1 170 ? 29.991  1.868   9.086   1.00 34.82 ?  162 GLU D CD    1 
ATOM   3529 O OE1   . GLU B 1 170 ? 30.288  1.803   10.298  1.00 33.64 ?  162 GLU D OE1   1 
ATOM   3530 O OE2   . GLU B 1 170 ? 28.853  2.187   8.679   1.00 31.63 ?  162 GLU D OE2   1 
ATOM   3531 N N     . LEU B 1 171 ? 34.080  -1.840  8.688   1.00 29.74 ?  163 LEU D N     1 
ATOM   3532 C CA    . LEU B 1 171 ? 35.265  -2.419  9.308   1.00 33.54 ?  163 LEU D CA    1 
ATOM   3533 C C     . LEU B 1 171 ? 36.280  -2.870  8.266   1.00 34.75 ?  163 LEU D C     1 
ATOM   3534 O O     . LEU B 1 171 ? 37.490  -2.802  8.514   1.00 37.68 ?  163 LEU D O     1 
ATOM   3535 C CB    . LEU B 1 171 ? 34.865  -3.589  10.207  1.00 35.56 ?  163 LEU D CB    1 
ATOM   3536 C CG    . LEU B 1 171 ? 34.400  -3.209  11.615  1.00 33.55 ?  163 LEU D CG    1 
ATOM   3537 C CD1   . LEU B 1 171 ? 33.668  -4.367  12.279  1.00 32.53 ?  163 LEU D CD1   1 
ATOM   3538 C CD2   . LEU B 1 171 ? 35.575  -2.750  12.463  1.00 26.05 ?  163 LEU D CD2   1 
ATOM   3539 N N     . LEU B 1 172 ? 35.812  -3.332  7.103   1.00 37.12 ?  164 LEU D N     1 
ATOM   3540 C CA    . LEU B 1 172 ? 36.726  -3.679  6.018   1.00 38.38 ?  164 LEU D CA    1 
ATOM   3541 C C     . LEU B 1 172 ? 37.554  -2.472  5.598   1.00 38.99 ?  164 LEU D C     1 
ATOM   3542 O O     . LEU B 1 172 ? 38.779  -2.560  5.452   1.00 43.51 ?  164 LEU D O     1 
ATOM   3543 C CB    . LEU B 1 172 ? 35.941  -4.227  4.825   1.00 39.01 ?  164 LEU D CB    1 
ATOM   3544 C CG    . LEU B 1 172 ? 35.512  -5.695  4.857   1.00 37.67 ?  164 LEU D CG    1 
ATOM   3545 C CD1   . LEU B 1 172 ? 35.195  -6.192  3.452   1.00 41.41 ?  164 LEU D CD1   1 
ATOM   3546 C CD2   . LEU B 1 172 ? 36.588  -6.550  5.497   1.00 37.68 ?  164 LEU D CD2   1 
ATOM   3547 N N     . GLN B 1 173 ? 36.896  -1.329  5.402   1.00 39.04 ?  165 GLN D N     1 
ATOM   3548 C CA    . GLN B 1 173 ? 37.606  -0.116  5.014   1.00 41.25 ?  165 GLN D CA    1 
ATOM   3549 C C     . GLN B 1 173 ? 38.450  0.424   6.161   1.00 40.63 ?  165 GLN D C     1 
ATOM   3550 O O     . GLN B 1 173 ? 39.546  0.952   5.938   1.00 41.83 ?  165 GLN D O     1 
ATOM   3551 C CB    . GLN B 1 173 ? 36.608  0.939   4.540   1.00 38.32 ?  165 GLN D CB    1 
ATOM   3552 C CG    . GLN B 1 173 ? 37.228  2.273   4.176   1.00 44.47 ?  165 GLN D CG    1 
ATOM   3553 C CD    . GLN B 1 173 ? 36.370  3.441   4.615   1.00 56.84 ?  165 GLN D CD    1 
ATOM   3554 O OE1   . GLN B 1 173 ? 35.757  4.119   3.791   1.00 62.77 ?  165 GLN D OE1   1 
ATOM   3555 N NE2   . GLN B 1 173 ? 36.323  3.683   5.919   1.00 56.68 ?  165 GLN D NE2   1 
ATOM   3556 N N     . GLN B 1 174 ? 37.960  0.306   7.396   1.00 37.84 ?  166 GLN D N     1 
ATOM   3557 C CA    . GLN B 1 174 ? 38.713  0.838   8.525   1.00 39.81 ?  166 GLN D CA    1 
ATOM   3558 C C     . GLN B 1 174 ? 39.989  0.049   8.774   1.00 43.07 ?  166 GLN D C     1 
ATOM   3559 O O     . GLN B 1 174 ? 40.998  0.625   9.196   1.00 41.58 ?  166 GLN D O     1 
ATOM   3560 C CB    . GLN B 1 174 ? 37.840  0.856   9.777   1.00 35.38 ?  166 GLN D CB    1 
ATOM   3561 C CG    . GLN B 1 174 ? 36.853  2.003   9.792   1.00 34.83 ?  166 GLN D CG    1 
ATOM   3562 C CD    . GLN B 1 174 ? 35.834  1.877   10.898  1.00 33.22 ?  166 GLN D CD    1 
ATOM   3563 O OE1   . GLN B 1 174 ? 35.126  0.875   10.995  1.00 31.40 ?  166 GLN D OE1   1 
ATOM   3564 N NE2   . GLN B 1 174 ? 35.747  2.900   11.739  1.00 31.92 ?  166 GLN D NE2   1 
ATOM   3565 N N     . PHE B 1 175 ? 39.976  -1.254  8.515   1.00 40.64 ?  167 PHE D N     1 
ATOM   3566 C CA    . PHE B 1 175 ? 41.157  -2.096  8.666   1.00 40.63 ?  167 PHE D CA    1 
ATOM   3567 C C     . PHE B 1 175 ? 41.734  -2.482  7.308   1.00 46.15 ?  167 PHE D C     1 
ATOM   3568 O O     . PHE B 1 175 ? 42.177  -3.611  7.100   1.00 43.55 ?  167 PHE D O     1 
ATOM   3569 C CB    . PHE B 1 175 ? 40.835  -3.330  9.504   1.00 39.56 ?  167 PHE D CB    1 
ATOM   3570 C CG    . PHE B 1 175 ? 40.673  -3.034  10.968  1.00 41.03 ?  167 PHE D CG    1 
ATOM   3571 C CD1   . PHE B 1 175 ? 39.466  -2.570  11.467  1.00 37.33 ?  167 PHE D CD1   1 
ATOM   3572 C CD2   . PHE B 1 175 ? 41.734  -3.199  11.842  1.00 38.89 ?  167 PHE D CD2   1 
ATOM   3573 C CE1   . PHE B 1 175 ? 39.318  -2.286  12.816  1.00 35.84 ?  167 PHE D CE1   1 
ATOM   3574 C CE2   . PHE B 1 175 ? 41.593  -2.918  13.192  1.00 44.45 ?  167 PHE D CE2   1 
ATOM   3575 C CZ    . PHE B 1 175 ? 40.383  -2.460  13.679  1.00 40.73 ?  167 PHE D CZ    1 
ATOM   3576 N N     . GLU B 1 176 ? 41.715  -1.532  6.373   1.00 46.93 ?  168 GLU D N     1 
ATOM   3577 C CA    . GLU B 1 176 ? 42.342  -1.698  5.068   1.00 48.35 ?  168 GLU D CA    1 
ATOM   3578 C C     . GLU B 1 176 ? 43.808  -2.073  5.220   1.00 50.20 ?  168 GLU D C     1 
ATOM   3579 O O     . GLU B 1 176 ? 44.564  -1.397  5.925   1.00 43.71 ?  168 GLU D O     1 
ATOM   3580 C CB    . GLU B 1 176 ? 42.203  -0.399  4.270   1.00 50.30 ?  168 GLU D CB    1 
ATOM   3581 C CG    . GLU B 1 176 ? 40.976  -0.315  3.378   1.00 52.09 ?  168 GLU D CG    1 
ATOM   3582 C CD    . GLU B 1 176 ? 41.328  -0.443  1.914   1.00 61.48 ?  168 GLU D CD    1 
ATOM   3583 O OE1   . GLU B 1 176 ? 41.932  0.511   1.384   1.00 64.81 ?  168 GLU D OE1   1 
ATOM   3584 O OE2   . GLU B 1 176 ? 41.001  -1.475  1.291   1.00 67.30 ?  168 GLU D OE2   1 
ATOM   3585 N N     . GLY B 1 177 ? 44.204  -3.166  4.571   1.00 51.82 ?  169 GLY D N     1 
ATOM   3586 C CA    . GLY B 1 177 ? 45.586  -3.593  4.577   1.00 54.81 ?  169 GLY D CA    1 
ATOM   3587 C C     . GLY B 1 177 ? 46.065  -4.247  5.854   1.00 46.62 ?  169 GLY D C     1 
ATOM   3588 O O     . GLY B 1 177 ? 47.200  -4.741  5.886   1.00 51.79 ?  169 GLY D O     1 
ATOM   3589 N N     . LYS B 1 178 ? 45.254  -4.263  6.909   1.00 46.26 ?  170 LYS D N     1 
ATOM   3590 C CA    . LYS B 1 178 ? 45.577  -4.956  8.146   1.00 39.37 ?  170 LYS D CA    1 
ATOM   3591 C C     . LYS B 1 178 ? 44.749  -6.230  8.251   1.00 39.72 ?  170 LYS D C     1 
ATOM   3592 O O     . LYS B 1 178 ? 43.712  -6.381  7.601   1.00 45.38 ?  170 LYS D O     1 
ATOM   3593 C CB    . LYS B 1 178 ? 45.324  -4.065  9.366   1.00 44.63 ?  170 LYS D CB    1 
ATOM   3594 C CG    . LYS B 1 178 ? 46.219  -2.841  9.434   1.00 47.44 ?  170 LYS D CG    1 
ATOM   3595 C CD    . LYS B 1 178 ? 46.741  -2.592  10.845  1.00 58.09 ?  170 LYS D CD    1 
ATOM   3596 C CE    . LYS B 1 178 ? 45.717  -2.957  11.910  1.00 51.23 ?  170 LYS D CE    1 
ATOM   3597 N NZ    . LYS B 1 178 ? 45.823  -2.063  13.097  1.00 45.44 ?  170 LYS D NZ    1 
ATOM   3598 N N     . THR B 1 179 ? 45.216  -7.149  9.088   1.00 43.20 ?  171 THR D N     1 
ATOM   3599 C CA    . THR B 1 179 ? 44.585  -8.452  9.255   1.00 44.42 ?  171 THR D CA    1 
ATOM   3600 C C     . THR B 1 179 ? 43.848  -8.492  10.587  1.00 44.20 ?  171 THR D C     1 
ATOM   3601 O O     . THR B 1 179 ? 44.472  -8.405  11.650  1.00 43.75 ?  171 THR D O     1 
ATOM   3602 C CB    . THR B 1 179 ? 45.620  -9.575  9.185   1.00 49.95 ?  171 THR D CB    1 
ATOM   3603 O OG1   . THR B 1 179 ? 46.216  -9.596  7.882   1.00 50.21 ?  171 THR D OG1   1 
ATOM   3604 C CG2   . THR B 1 179 ? 44.964  -10.920 9.462   1.00 47.06 ?  171 THR D CG2   1 
ATOM   3605 N N     . ILE B 1 180 ? 42.525  -8.619  10.526  1.00 43.00 ?  172 ILE D N     1 
ATOM   3606 C CA    . ILE B 1 180 ? 41.723  -8.863  11.720  1.00 42.99 ?  172 ILE D CA    1 
ATOM   3607 C C     . ILE B 1 180 ? 41.764  -10.356 12.015  1.00 41.96 ?  172 ILE D C     1 
ATOM   3608 O O     . ILE B 1 180 ? 41.332  -11.174 11.196  1.00 42.13 ?  172 ILE D O     1 
ATOM   3609 C CB    . ILE B 1 180 ? 40.280  -8.375  11.536  1.00 35.83 ?  172 ILE D CB    1 
ATOM   3610 C CG1   . ILE B 1 180 ? 40.251  -6.876  11.238  1.00 37.63 ?  172 ILE D CG1   1 
ATOM   3611 C CG2   . ILE B 1 180 ? 39.454  -8.681  12.776  1.00 32.42 ?  172 ILE D CG2   1 
ATOM   3612 C CD1   . ILE B 1 180 ? 38.856  -6.328  11.048  1.00 42.69 ?  172 ILE D CD1   1 
ATOM   3613 N N     . ASP B 1 181 ? 42.294  -10.715 13.181  1.00 40.97 ?  173 ASP D N     1 
ATOM   3614 C CA    . ASP B 1 181 ? 42.428  -12.117 13.551  1.00 43.41 ?  173 ASP D CA    1 
ATOM   3615 C C     . ASP B 1 181 ? 41.206  -12.651 14.285  1.00 44.55 ?  173 ASP D C     1 
ATOM   3616 O O     . ASP B 1 181 ? 40.922  -13.852 14.208  1.00 45.40 ?  173 ASP D O     1 
ATOM   3617 C CB    . ASP B 1 181 ? 43.680  -12.315 14.411  1.00 40.54 ?  173 ASP D CB    1 
ATOM   3618 C CG    . ASP B 1 181 ? 44.930  -11.735 13.765  1.00 45.07 ?  173 ASP D CG    1 
ATOM   3619 O OD1   . ASP B 1 181 ? 45.378  -12.275 12.731  1.00 49.79 ?  173 ASP D OD1   1 
ATOM   3620 O OD2   . ASP B 1 181 ? 45.460  -10.731 14.285  1.00 42.22 ?  173 ASP D OD2   1 
ATOM   3621 N N     . ALA B 1 182 ? 40.473  -11.788 14.985  1.00 39.12 ?  174 ALA D N     1 
ATOM   3622 C CA    . ALA B 1 182 ? 39.301  -12.217 15.736  1.00 40.01 ?  174 ALA D CA    1 
ATOM   3623 C C     . ALA B 1 182 ? 38.303  -11.073 15.814  1.00 39.03 ?  174 ALA D C     1 
ATOM   3624 O O     . ALA B 1 182 ? 38.676  -9.942  16.137  1.00 37.33 ?  174 ALA D O     1 
ATOM   3625 C CB    . ALA B 1 182 ? 39.684  -12.679 17.146  1.00 37.78 ?  174 ALA D CB    1 
ATOM   3626 N N     . PHE B 1 183 ? 37.044  -11.373 15.510  1.00 37.44 ?  175 PHE D N     1 
ATOM   3627 C CA    . PHE B 1 183 ? 35.935  -10.458 15.732  1.00 34.51 ?  175 PHE D CA    1 
ATOM   3628 C C     . PHE B 1 183 ? 35.002  -11.078 16.760  1.00 34.42 ?  175 PHE D C     1 
ATOM   3629 O O     . PHE B 1 183 ? 34.663  -12.261 16.659  1.00 38.99 ?  175 PHE D O     1 
ATOM   3630 C CB    . PHE B 1 183 ? 35.178  -10.158 14.433  1.00 35.64 ?  175 PHE D CB    1 
ATOM   3631 C CG    . PHE B 1 183 ? 33.936  -9.335  14.636  1.00 33.76 ?  175 PHE D CG    1 
ATOM   3632 C CD1   . PHE B 1 183 ? 34.007  -7.953  14.660  1.00 35.73 ?  175 PHE D CD1   1 
ATOM   3633 C CD2   . PHE B 1 183 ? 32.700  -9.941  14.799  1.00 35.99 ?  175 PHE D CD2   1 
ATOM   3634 C CE1   . PHE B 1 183 ? 32.871  -7.190  14.850  1.00 32.58 ?  175 PHE D CE1   1 
ATOM   3635 C CE2   . PHE B 1 183 ? 31.562  -9.183  14.989  1.00 35.26 ?  175 PHE D CE2   1 
ATOM   3636 C CZ    . PHE B 1 183 ? 31.648  -7.806  15.015  1.00 34.82 ?  175 PHE D CZ    1 
ATOM   3637 N N     . LEU B 1 184 ? 34.596  -10.283 17.745  1.00 32.42 ?  176 LEU D N     1 
ATOM   3638 C CA    . LEU B 1 184 ? 33.691  -10.733 18.790  1.00 33.08 ?  176 LEU D CA    1 
ATOM   3639 C C     . LEU B 1 184 ? 32.538  -9.750  18.917  1.00 32.20 ?  176 LEU D C     1 
ATOM   3640 O O     . LEU B 1 184 ? 32.701  -8.547  18.702  1.00 31.06 ?  176 LEU D O     1 
ATOM   3641 C CB    . LEU B 1 184 ? 34.404  -10.876 20.147  1.00 34.91 ?  176 LEU D CB    1 
ATOM   3642 C CG    . LEU B 1 184 ? 35.718  -11.657 20.223  1.00 35.12 ?  176 LEU D CG    1 
ATOM   3643 C CD1   . LEU B 1 184 ? 36.905  -10.787 19.861  1.00 31.98 ?  176 LEU D CD1   1 
ATOM   3644 C CD2   . LEU B 1 184 ? 35.900  -12.247 21.613  1.00 35.20 ?  176 LEU D CD2   1 
ATOM   3645 N N     . ALA B 1 185 ? 31.368  -10.275 19.267  1.00 29.18 ?  177 ALA D N     1 
ATOM   3646 C CA    . ALA B 1 185 ? 30.186  -9.445  19.434  1.00 30.43 ?  177 ALA D CA    1 
ATOM   3647 C C     . ALA B 1 185 ? 29.207  -10.152 20.355  1.00 30.95 ?  177 ALA D C     1 
ATOM   3648 O O     . ALA B 1 185 ? 29.030  -11.371 20.267  1.00 33.32 ?  177 ALA D O     1 
ATOM   3649 C CB    . ALA B 1 185 ? 29.520  -9.141  18.087  1.00 28.14 ?  177 ALA D CB    1 
ATOM   3650 N N     . GLY B 1 186 ? 28.590  -9.384  21.248  1.00 27.04 ?  178 GLY D N     1 
ATOM   3651 C CA    . GLY B 1 186 ? 27.505  -9.922  22.046  1.00 27.87 ?  178 GLY D CA    1 
ATOM   3652 C C     . GLY B 1 186 ? 26.287  -10.204 21.186  1.00 27.45 ?  178 GLY D C     1 
ATOM   3653 O O     . GLY B 1 186 ? 25.991  -9.482  20.235  1.00 28.29 ?  178 GLY D O     1 
ATOM   3654 N N     . VAL B 1 187 ? 25.576  -11.271 21.526  1.00 28.62 ?  179 VAL D N     1 
ATOM   3655 C CA    . VAL B 1 187 ? 24.448  -11.743 20.733  1.00 31.19 ?  179 VAL D CA    1 
ATOM   3656 C C     . VAL B 1 187 ? 23.163  -11.290 21.415  1.00 33.05 ?  179 VAL D C     1 
ATOM   3657 O O     . VAL B 1 187 ? 22.820  -11.765 22.503  1.00 27.07 ?  179 VAL D O     1 
ATOM   3658 C CB    . VAL B 1 187 ? 24.485  -13.267 20.550  1.00 35.32 ?  179 VAL D CB    1 
ATOM   3659 C CG1   . VAL B 1 187 ? 23.170  -13.767 19.962  1.00 32.41 ?  179 VAL D CG1   1 
ATOM   3660 C CG2   . VAL B 1 187 ? 25.657  -13.661 19.661  1.00 30.06 ?  179 VAL D CG2   1 
ATOM   3661 N N     . GLY B 1 188 ? 22.463  -10.353 20.783  1.00 32.18 ?  180 GLY D N     1 
ATOM   3662 C CA    . GLY B 1 188 ? 21.125  -9.991  21.197  1.00 32.27 ?  180 GLY D CA    1 
ATOM   3663 C C     . GLY B 1 188 ? 20.123  -10.560 20.217  1.00 32.52 ?  180 GLY D C     1 
ATOM   3664 O O     . GLY B 1 188 ? 19.520  -11.606 20.468  1.00 25.89 ?  180 GLY D O     1 
ATOM   3665 N N     . THR B 1 189 ? 19.941  -9.877  19.087  1.00 29.13 ?  181 THR D N     1 
ATOM   3666 C CA    . THR B 1 189 ? 19.264  -10.491 17.955  1.00 28.42 ?  181 THR D CA    1 
ATOM   3667 C C     . THR B 1 189 ? 20.210  -11.343 17.124  1.00 33.62 ?  181 THR D C     1 
ATOM   3668 O O     . THR B 1 189 ? 19.747  -12.145 16.305  1.00 28.35 ?  181 THR D O     1 
ATOM   3669 C CB    . THR B 1 189 ? 18.634  -9.426  17.057  1.00 31.70 ?  181 THR D CB    1 
ATOM   3670 O OG1   . THR B 1 189 ? 19.663  -8.585  16.522  1.00 27.19 ?  181 THR D OG1   1 
ATOM   3671 C CG2   . THR B 1 189 ? 17.647  -8.577  17.841  1.00 28.15 ?  181 THR D CG2   1 
ATOM   3672 N N     . GLY B 1 190 ? 21.519  -11.188 17.322  1.00 31.03 ?  182 GLY D N     1 
ATOM   3673 C CA    . GLY B 1 190 ? 22.510  -11.862 16.515  1.00 30.46 ?  182 GLY D CA    1 
ATOM   3674 C C     . GLY B 1 190 ? 22.808  -11.202 15.188  1.00 32.11 ?  182 GLY D C     1 
ATOM   3675 O O     . GLY B 1 190 ? 23.685  -11.685 14.460  1.00 33.96 ?  182 GLY D O     1 
ATOM   3676 N N     . GLY B 1 191 ? 22.116  -10.111 14.852  1.00 31.99 ?  183 GLY D N     1 
ATOM   3677 C CA    . GLY B 1 191 ? 22.323  -9.483  13.556  1.00 30.77 ?  183 GLY D CA    1 
ATOM   3678 C C     . GLY B 1 191 ? 23.708  -8.885  13.400  1.00 34.07 ?  183 GLY D C     1 
ATOM   3679 O O     . GLY B 1 191 ? 24.312  -8.969  12.327  1.00 31.27 ?  183 GLY D O     1 
ATOM   3680 N N     . THR B 1 192 ? 24.228  -8.265  14.463  1.00 32.88 ?  184 THR D N     1 
ATOM   3681 C CA    . THR B 1 192 ? 25.565  -7.681  14.400  1.00 32.70 ?  184 THR D CA    1 
ATOM   3682 C C     . THR B 1 192 ? 26.611  -8.745  14.097  1.00 33.76 ?  184 THR D C     1 
ATOM   3683 O O     . THR B 1 192 ? 27.422  -8.592  13.178  1.00 28.55 ?  184 THR D O     1 
ATOM   3684 C CB    . THR B 1 192 ? 25.898  -6.967  15.711  1.00 33.17 ?  184 THR D CB    1 
ATOM   3685 O OG1   . THR B 1 192 ? 25.047  -5.825  15.872  1.00 27.71 ?  184 THR D OG1   1 
ATOM   3686 C CG2   . THR B 1 192 ? 27.354  -6.521  15.721  1.00 30.33 ?  184 THR D CG2   1 
ATOM   3687 N N     . LEU B 1 193 ? 26.599  -9.839  14.861  1.00 34.62 ?  185 LEU D N     1 
ATOM   3688 C CA    . LEU B 1 193 ? 27.566  -10.909 14.639  1.00 31.28 ?  185 LEU D CA    1 
ATOM   3689 C C     . LEU B 1 193 ? 27.366  -11.556 13.274  1.00 33.55 ?  185 LEU D C     1 
ATOM   3690 O O     . LEU B 1 193 ? 28.332  -11.798 12.541  1.00 33.29 ?  185 LEU D O     1 
ATOM   3691 C CB    . LEU B 1 193 ? 27.452  -11.955 15.749  1.00 32.13 ?  185 LEU D CB    1 
ATOM   3692 C CG    . LEU B 1 193 ? 28.556  -13.013 15.766  1.00 31.69 ?  185 LEU D CG    1 
ATOM   3693 C CD1   . LEU B 1 193 ? 29.843  -12.445 16.352  1.00 30.67 ?  185 LEU D CD1   1 
ATOM   3694 C CD2   . LEU B 1 193 ? 28.109  -14.254 16.520  1.00 32.53 ?  185 LEU D CD2   1 
ATOM   3695 N N     . SER B 1 194 ? 26.113  -11.845 12.916  1.00 32.47 ?  186 SER D N     1 
ATOM   3696 C CA    . SER B 1 194 ? 25.840  -12.512 11.647  1.00 28.49 ?  186 SER D CA    1 
ATOM   3697 C C     . SER B 1 194 ? 26.246  -11.637 10.468  1.00 36.09 ?  186 SER D C     1 
ATOM   3698 O O     . SER B 1 194 ? 26.970  -12.081 9.570   1.00 37.58 ?  186 SER D O     1 
ATOM   3699 C CB    . SER B 1 194 ? 24.359  -12.884 11.558  1.00 30.39 ?  186 SER D CB    1 
ATOM   3700 O OG    . SER B 1 194 ? 24.019  -13.859 12.529  1.00 30.21 ?  186 SER D OG    1 
ATOM   3701 N N     . GLY B 1 195 ? 25.799  -10.380 10.462  1.00 36.29 ?  187 GLY D N     1 
ATOM   3702 C CA    . GLY B 1 195 ? 26.082  -9.512  9.330   1.00 32.40 ?  187 GLY D CA    1 
ATOM   3703 C C     . GLY B 1 195 ? 27.557  -9.195  9.189   1.00 34.34 ?  187 GLY D C     1 
ATOM   3704 O O     . GLY B 1 195 ? 28.140  -9.349  8.113   1.00 35.57 ?  187 GLY D O     1 
ATOM   3705 N N     . VAL B 1 196 ? 28.185  -8.752  10.280  1.00 34.48 ?  188 VAL D N     1 
ATOM   3706 C CA    . VAL B 1 196 ? 29.596  -8.388  10.218  1.00 35.79 ?  188 VAL D CA    1 
ATOM   3707 C C     . VAL B 1 196 ? 30.460  -9.628  10.027  1.00 34.30 ?  188 VAL D C     1 
ATOM   3708 O O     . VAL B 1 196 ? 31.405  -9.624  9.229   1.00 40.92 ?  188 VAL D O     1 
ATOM   3709 C CB    . VAL B 1 196 ? 30.000  -7.600  11.478  1.00 33.56 ?  188 VAL D CB    1 
ATOM   3710 C CG1   . VAL B 1 196 ? 31.513  -7.448  11.550  1.00 29.94 ?  188 VAL D CG1   1 
ATOM   3711 C CG2   . VAL B 1 196 ? 29.320  -6.243  11.490  1.00 25.49 ?  188 VAL D CG2   1 
ATOM   3712 N N     . GLY B 1 197 ? 30.146  -10.708 10.746  1.00 36.42 ?  189 GLY D N     1 
ATOM   3713 C CA    . GLY B 1 197 ? 30.927  -11.928 10.615  1.00 40.54 ?  189 GLY D CA    1 
ATOM   3714 C C     . GLY B 1 197 ? 30.929  -12.475 9.200   1.00 37.76 ?  189 GLY D C     1 
ATOM   3715 O O     . GLY B 1 197 ? 31.955  -12.951 8.711   1.00 41.04 ?  189 GLY D O     1 
ATOM   3716 N N     . LYS B 1 198 ? 29.781  -12.409 8.523   1.00 40.58 ?  190 LYS D N     1 
ATOM   3717 C CA    . LYS B 1 198 ? 29.712  -12.840 7.130   1.00 39.29 ?  190 LYS D CA    1 
ATOM   3718 C C     . LYS B 1 198 ? 30.677  -12.044 6.261   1.00 44.65 ?  190 LYS D C     1 
ATOM   3719 O O     . LYS B 1 198 ? 31.419  -12.613 5.452   1.00 41.24 ?  190 LYS D O     1 
ATOM   3720 C CB    . LYS B 1 198 ? 28.280  -12.698 6.614   1.00 33.34 ?  190 LYS D CB    1 
ATOM   3721 C CG    . LYS B 1 198 ? 28.068  -13.195 5.197   1.00 37.11 ?  190 LYS D CG    1 
ATOM   3722 C CD    . LYS B 1 198 ? 26.711  -12.752 4.676   1.00 43.84 ?  190 LYS D CD    1 
ATOM   3723 C CE    . LYS B 1 198 ? 26.068  -13.809 3.798   1.00 45.60 ?  190 LYS D CE    1 
ATOM   3724 N NZ    . LYS B 1 198 ? 24.670  -13.440 3.438   1.00 54.29 ?  190 LYS D NZ    1 
ATOM   3725 N N     . VAL B 1 199 ? 30.686  -10.720 6.424   1.00 41.95 ?  191 VAL D N     1 
ATOM   3726 C CA    . VAL B 1 199 ? 31.535  -9.870  5.596   1.00 44.72 ?  191 VAL D CA    1 
ATOM   3727 C C     . VAL B 1 199 ? 33.007  -10.097 5.922   1.00 40.76 ?  191 VAL D C     1 
ATOM   3728 O O     . VAL B 1 199 ? 33.858  -10.129 5.023   1.00 40.70 ?  191 VAL D O     1 
ATOM   3729 C CB    . VAL B 1 199 ? 31.132  -8.394  5.772   1.00 40.08 ?  191 VAL D CB    1 
ATOM   3730 C CG1   . VAL B 1 199 ? 32.125  -7.474  5.076   1.00 38.91 ?  191 VAL D CG1   1 
ATOM   3731 C CG2   . VAL B 1 199 ? 29.727  -8.167  5.244   1.00 38.39 ?  191 VAL D CG2   1 
ATOM   3732 N N     . LEU B 1 200 ? 33.333  -10.270 7.206   1.00 42.02 ?  192 LEU D N     1 
ATOM   3733 C CA    . LEU B 1 200 ? 34.732  -10.397 7.601   1.00 40.31 ?  192 LEU D CA    1 
ATOM   3734 C C     . LEU B 1 200 ? 35.319  -11.747 7.210   1.00 42.74 ?  192 LEU D C     1 
ATOM   3735 O O     . LEU B 1 200 ? 36.526  -11.843 6.959   1.00 46.70 ?  192 LEU D O     1 
ATOM   3736 C CB    . LEU B 1 200 ? 34.878  -10.177 9.106   1.00 35.79 ?  192 LEU D CB    1 
ATOM   3737 C CG    . LEU B 1 200 ? 34.659  -8.746  9.598   1.00 47.84 ?  192 LEU D CG    1 
ATOM   3738 C CD1   . LEU B 1 200 ? 34.994  -8.622  11.076  1.00 37.89 ?  192 LEU D CD1   1 
ATOM   3739 C CD2   . LEU B 1 200 ? 35.480  -7.770  8.773   1.00 40.30 ?  192 LEU D CD2   1 
ATOM   3740 N N     . LYS B 1 201 ? 34.496  -12.798 7.162   1.00 45.49 ?  193 LYS D N     1 
ATOM   3741 C CA    . LYS B 1 201 ? 35.009  -14.117 6.801   1.00 43.33 ?  193 LYS D CA    1 
ATOM   3742 C C     . LYS B 1 201 ? 35.404  -14.192 5.331   1.00 44.64 ?  193 LYS D C     1 
ATOM   3743 O O     . LYS B 1 201 ? 36.314  -14.950 4.976   1.00 49.19 ?  193 LYS D O     1 
ATOM   3744 C CB    . LYS B 1 201 ? 33.977  -15.198 7.125   1.00 46.78 ?  193 LYS D CB    1 
ATOM   3745 C CG    . LYS B 1 201 ? 33.810  -15.487 8.609   1.00 49.61 ?  193 LYS D CG    1 
ATOM   3746 C CD    . LYS B 1 201 ? 33.283  -16.897 8.848   1.00 49.04 ?  193 LYS D CD    1 
ATOM   3747 C CE    . LYS B 1 201 ? 34.389  -17.935 8.708   1.00 54.37 ?  193 LYS D CE    1 
ATOM   3748 N NZ    . LYS B 1 201 ? 35.305  -17.922 9.882   1.00 53.37 ?  193 LYS D NZ    1 
ATOM   3749 N N     . LYS B 1 202 ? 34.736  -13.426 4.465   1.00 42.78 ?  194 LYS D N     1 
ATOM   3750 C CA    . LYS B 1 202 ? 35.103  -13.426 3.051   1.00 43.24 ?  194 LYS D CA    1 
ATOM   3751 C C     . LYS B 1 202 ? 36.450  -12.754 2.826   1.00 47.89 ?  194 LYS D C     1 
ATOM   3752 O O     . LYS B 1 202 ? 37.233  -13.192 1.973   1.00 50.63 ?  194 LYS D O     1 
ATOM   3753 C CB    . LYS B 1 202 ? 34.017  -12.739 2.223   1.00 45.09 ?  194 LYS D CB    1 
ATOM   3754 C CG    . LYS B 1 202 ? 32.603  -13.142 2.595   1.00 50.30 ?  194 LYS D CG    1 
ATOM   3755 C CD    . LYS B 1 202 ? 31.911  -13.896 1.468   1.00 53.86 ?  194 LYS D CD    1 
ATOM   3756 C CE    . LYS B 1 202 ? 30.398  -13.886 1.650   1.00 50.22 ?  194 LYS D CE    1 
ATOM   3757 N NZ    . LYS B 1 202 ? 29.758  -12.746 0.936   1.00 50.41 ?  194 LYS D NZ    1 
ATOM   3758 N N     . GLU B 1 203 ? 36.738  -11.689 3.576   1.00 43.15 ?  195 GLU D N     1 
ATOM   3759 C CA    . GLU B 1 203 ? 37.998  -10.979 3.382   1.00 45.06 ?  195 GLU D CA    1 
ATOM   3760 C C     . GLU B 1 203 ? 39.131  -11.612 4.180   1.00 45.99 ?  195 GLU D C     1 
ATOM   3761 O O     . GLU B 1 203 ? 40.278  -11.645 3.720   1.00 45.46 ?  195 GLU D O     1 
ATOM   3762 C CB    . GLU B 1 203 ? 37.833  -9.509  3.764   1.00 43.59 ?  195 GLU D CB    1 
ATOM   3763 C CG    . GLU B 1 203 ? 38.968  -8.613  3.287   1.00 48.58 ?  195 GLU D CG    1 
ATOM   3764 C CD    . GLU B 1 203 ? 38.907  -8.312  1.801   1.00 52.65 ?  195 GLU D CD    1 
ATOM   3765 O OE1   . GLU B 1 203 ? 37.850  -8.547  1.177   1.00 56.61 ?  195 GLU D OE1   1 
ATOM   3766 O OE2   . GLU B 1 203 ? 39.925  -7.837  1.256   1.00 60.40 ?  195 GLU D OE2   1 
ATOM   3767 N N     . TYR B 1 204 ? 38.825  -12.123 5.372   1.00 45.75 ?  196 TYR D N     1 
ATOM   3768 C CA    . TYR B 1 204 ? 39.800  -12.727 6.274   1.00 45.12 ?  196 TYR D CA    1 
ATOM   3769 C C     . TYR B 1 204 ? 39.399  -14.187 6.457   1.00 46.47 ?  196 TYR D C     1 
ATOM   3770 O O     . TYR B 1 204 ? 38.690  -14.534 7.413   1.00 42.83 ?  196 TYR D O     1 
ATOM   3771 C CB    . TYR B 1 204 ? 39.854  -11.976 7.602   1.00 43.78 ?  196 TYR D CB    1 
ATOM   3772 C CG    . TYR B 1 204 ? 40.173  -10.507 7.437   1.00 46.17 ?  196 TYR D CG    1 
ATOM   3773 C CD1   . TYR B 1 204 ? 41.443  -10.094 7.059   1.00 47.57 ?  196 TYR D CD1   1 
ATOM   3774 C CD2   . TYR B 1 204 ? 39.203  -9.534  7.649   1.00 44.36 ?  196 TYR D CD2   1 
ATOM   3775 C CE1   . TYR B 1 204 ? 41.744  -8.757  6.904   1.00 44.36 ?  196 TYR D CE1   1 
ATOM   3776 C CE2   . TYR B 1 204 ? 39.496  -8.190  7.496   1.00 45.05 ?  196 TYR D CE2   1 
ATOM   3777 C CZ    . TYR B 1 204 ? 40.768  -7.809  7.123   1.00 43.79 ?  196 TYR D CZ    1 
ATOM   3778 O OH    . TYR B 1 204 ? 41.072  -6.476  6.966   1.00 39.81 ?  196 TYR D OH    1 
ATOM   3779 N N     . PRO B 1 205 ? 39.825  -15.069 5.550   1.00 44.83 ?  197 PRO D N     1 
ATOM   3780 C CA    . PRO B 1 205 ? 39.332  -16.457 5.587   1.00 44.39 ?  197 PRO D CA    1 
ATOM   3781 C C     . PRO B 1 205 ? 39.672  -17.197 6.869   1.00 45.50 ?  197 PRO D C     1 
ATOM   3782 O O     . PRO B 1 205 ? 38.914  -18.086 7.273   1.00 48.62 ?  197 PRO D O     1 
ATOM   3783 C CB    . PRO B 1 205 ? 40.010  -17.094 4.366   1.00 48.74 ?  197 PRO D CB    1 
ATOM   3784 C CG    . PRO B 1 205 ? 40.327  -15.938 3.459   1.00 46.61 ?  197 PRO D CG    1 
ATOM   3785 C CD    . PRO B 1 205 ? 40.686  -14.816 4.383   1.00 42.30 ?  197 PRO D CD    1 
ATOM   3786 N N     . ASN B 1 206 ? 40.781  -16.858 7.527   1.00 42.50 ?  198 ASN D N     1 
ATOM   3787 C CA    . ASN B 1 206 ? 41.199  -17.530 8.750   1.00 46.62 ?  198 ASN D CA    1 
ATOM   3788 C C     . ASN B 1 206 ? 40.760  -16.789 10.007  1.00 45.86 ?  198 ASN D C     1 
ATOM   3789 O O     . ASN B 1 206 ? 41.289  -17.052 11.091  1.00 39.35 ?  198 ASN D O     1 
ATOM   3790 C CB    . ASN B 1 206 ? 42.717  -17.722 8.758   1.00 49.79 ?  198 ASN D CB    1 
ATOM   3791 C CG    . ASN B 1 206 ? 43.249  -18.218 7.429   1.00 53.09 ?  198 ASN D CG    1 
ATOM   3792 O OD1   . ASN B 1 206 ? 42.491  -18.689 6.583   1.00 49.82 ?  198 ASN D OD1   1 
ATOM   3793 N ND2   . ASN B 1 206 ? 44.559  -18.117 7.241   1.00 48.24 ?  198 ASN D ND2   1 
ATOM   3794 N N     . ILE B 1 207 ? 39.803  -15.868 9.885   1.00 43.95 ?  199 ILE D N     1 
ATOM   3795 C CA    . ILE B 1 207 ? 39.357  -15.108 11.044  1.00 41.08 ?  199 ILE D CA    1 
ATOM   3796 C C     . ILE B 1 207 ? 38.538  -16.009 11.962  1.00 43.55 ?  199 ILE D C     1 
ATOM   3797 O O     . ILE B 1 207 ? 37.858  -16.946 11.517  1.00 47.96 ?  199 ILE D O     1 
ATOM   3798 C CB    . ILE B 1 207 ? 38.544  -13.872 10.615  1.00 44.87 ?  199 ILE D CB    1 
ATOM   3799 C CG1   . ILE B 1 207 ? 38.422  -12.884 11.775  1.00 42.34 ?  199 ILE D CG1   1 
ATOM   3800 C CG2   . ILE B 1 207 ? 37.152  -14.272 10.141  1.00 41.72 ?  199 ILE D CG2   1 
ATOM   3801 C CD1   . ILE B 1 207 ? 37.703  -11.611 11.411  1.00 40.12 ?  199 ILE D CD1   1 
ATOM   3802 N N     . GLU B 1 208 ? 38.615  -15.736 13.260  1.00 42.93 ?  200 GLU D N     1 
ATOM   3803 C CA    . GLU B 1 208 ? 37.745  -16.365 14.243  1.00 43.52 ?  200 GLU D CA    1 
ATOM   3804 C C     . GLU B 1 208 ? 36.593  -15.425 14.567  1.00 44.54 ?  200 GLU D C     1 
ATOM   3805 O O     . GLU B 1 208 ? 36.811  -14.252 14.889  1.00 39.63 ?  200 GLU D O     1 
ATOM   3806 C CB    . GLU B 1 208 ? 38.498  -16.720 15.525  1.00 41.60 ?  200 GLU D CB    1 
ATOM   3807 C CG    . GLU B 1 208 ? 37.679  -17.583 16.479  1.00 46.01 ?  200 GLU D CG    1 
ATOM   3808 C CD    . GLU B 1 208 ? 38.474  -18.080 17.673  1.00 48.43 ?  200 GLU D CD    1 
ATOM   3809 O OE1   . GLU B 1 208 ? 39.682  -17.772 17.761  1.00 40.42 ?  200 GLU D OE1   1 
ATOM   3810 O OE2   . GLU B 1 208 ? 37.886  -18.778 18.527  1.00 46.42 ?  200 GLU D OE2   1 
ATOM   3811 N N     . ILE B 1 209 ? 35.373  -15.942 14.473  1.00 40.81 ?  201 ILE D N     1 
ATOM   3812 C CA    . ILE B 1 209 ? 34.168  -15.217 14.853  1.00 37.39 ?  201 ILE D CA    1 
ATOM   3813 C C     . ILE B 1 209 ? 33.702  -15.793 16.182  1.00 37.62 ?  201 ILE D C     1 
ATOM   3814 O O     . ILE B 1 209 ? 33.430  -16.996 16.282  1.00 39.95 ?  201 ILE D O     1 
ATOM   3815 C CB    . ILE B 1 209 ? 33.078  -15.329 13.777  1.00 41.37 ?  201 ILE D CB    1 
ATOM   3816 C CG1   . ILE B 1 209 ? 33.612  -14.847 12.426  1.00 39.57 ?  201 ILE D CG1   1 
ATOM   3817 C CG2   . ILE B 1 209 ? 31.844  -14.539 14.175  1.00 36.91 ?  201 ILE D CG2   1 
ATOM   3818 C CD1   . ILE B 1 209 ? 34.010  -13.388 12.411  1.00 35.32 ?  201 ILE D CD1   1 
ATOM   3819 N N     . VAL B 1 210 ? 33.631  -14.947 17.205  1.00 36.70 ?  202 VAL D N     1 
ATOM   3820 C CA    . VAL B 1 210 ? 33.287  -15.369 18.557  1.00 35.90 ?  202 VAL D CA    1 
ATOM   3821 C C     . VAL B 1 210 ? 31.992  -14.687 18.970  1.00 40.47 ?  202 VAL D C     1 
ATOM   3822 O O     . VAL B 1 210 ? 31.859  -13.465 18.841  1.00 36.19 ?  202 VAL D O     1 
ATOM   3823 C CB    . VAL B 1 210 ? 34.413  -15.048 19.556  1.00 36.79 ?  202 VAL D CB    1 
ATOM   3824 C CG1   . VAL B 1 210 ? 34.057  -15.573 20.934  1.00 34.52 ?  202 VAL D CG1   1 
ATOM   3825 C CG2   . VAL B 1 210 ? 35.731  -15.639 19.080  1.00 39.11 ?  202 VAL D CG2   1 
ATOM   3826 N N     . ALA B 1 211 ? 31.041  -15.479 19.460  1.00 32.21 ?  203 ALA D N     1 
ATOM   3827 C CA    . ALA B 1 211 ? 29.805  -14.955 20.018  1.00 29.37 ?  203 ALA D CA    1 
ATOM   3828 C C     . ALA B 1 211 ? 29.955  -14.789 21.522  1.00 34.37 ?  203 ALA D C     1 
ATOM   3829 O O     . ALA B 1 211 ? 30.615  -15.594 22.184  1.00 33.02 ?  203 ALA D O     1 
ATOM   3830 C CB    . ALA B 1 211 ? 28.629  -15.884 19.709  1.00 37.39 ?  203 ALA D CB    1 
ATOM   3831 N N     . ILE B 1 212 ? 29.345  -13.735 22.058  1.00 36.51 ?  204 ILE D N     1 
ATOM   3832 C CA    . ILE B 1 212 ? 29.377  -13.444 23.485  1.00 31.09 ?  204 ILE D CA    1 
ATOM   3833 C C     . ILE B 1 212 ? 27.952  -13.505 24.013  1.00 31.72 ?  204 ILE D C     1 
ATOM   3834 O O     . ILE B 1 212 ? 27.040  -12.916 23.423  1.00 30.90 ?  204 ILE D O     1 
ATOM   3835 C CB    . ILE B 1 212 ? 30.014  -12.072 23.773  1.00 33.67 ?  204 ILE D CB    1 
ATOM   3836 C CG1   . ILE B 1 212 ? 31.462  -12.049 23.281  1.00 33.91 ?  204 ILE D CG1   1 
ATOM   3837 C CG2   . ILE B 1 212 ? 29.957  -11.756 25.261  1.00 36.44 ?  204 ILE D CG2   1 
ATOM   3838 C CD1   . ILE B 1 212 ? 31.946  -10.679 22.862  1.00 33.30 ?  204 ILE D CD1   1 
ATOM   3839 N N     . GLU B 1 213 ? 27.766  -14.221 25.117  1.00 30.68 ?  205 GLU D N     1 
ATOM   3840 C CA    . GLU B 1 213 ? 26.459  -14.388 25.734  1.00 34.57 ?  205 GLU D CA    1 
ATOM   3841 C C     . GLU B 1 213 ? 26.641  -14.440 27.241  1.00 35.38 ?  205 GLU D C     1 
ATOM   3842 O O     . GLU B 1 213 ? 27.740  -14.735 27.726  1.00 34.39 ?  205 GLU D O     1 
ATOM   3843 C CB    . GLU B 1 213 ? 25.762  -15.658 25.231  1.00 32.67 ?  205 GLU D CB    1 
ATOM   3844 C CG    . GLU B 1 213 ? 26.401  -16.949 25.686  1.00 37.04 ?  205 GLU D CG    1 
ATOM   3845 C CD    . GLU B 1 213 ? 25.636  -18.149 25.181  1.00 42.63 ?  205 GLU D CD    1 
ATOM   3846 O OE1   . GLU B 1 213 ? 26.200  -19.262 25.177  1.00 41.24 ?  205 GLU D OE1   1 
ATOM   3847 O OE2   . GLU B 1 213 ? 24.454  -17.977 24.814  1.00 34.00 ?  205 GLU D OE2   1 
ATOM   3848 N N     . PRO B 1 214 ? 25.587  -14.162 28.013  1.00 38.87 ?  206 PRO D N     1 
ATOM   3849 C CA    . PRO B 1 214 ? 25.732  -14.185 29.475  1.00 36.83 ?  206 PRO D CA    1 
ATOM   3850 C C     . PRO B 1 214 ? 25.967  -15.597 29.989  1.00 40.46 ?  206 PRO D C     1 
ATOM   3851 O O     . PRO B 1 214 ? 25.265  -16.539 29.615  1.00 39.16 ?  206 PRO D O     1 
ATOM   3852 C CB    . PRO B 1 214 ? 24.401  -13.615 29.984  1.00 35.11 ?  206 PRO D CB    1 
ATOM   3853 C CG    . PRO B 1 214 ? 23.712  -13.054 28.789  1.00 35.44 ?  206 PRO D CG    1 
ATOM   3854 C CD    . PRO B 1 214 ? 24.215  -13.813 27.613  1.00 33.18 ?  206 PRO D CD    1 
ATOM   3855 N N     . GLU B 1 215 ? 26.966  -15.731 30.859  1.00 35.34 ?  207 GLU D N     1 
ATOM   3856 C CA    . GLU B 1 215 ? 27.221  -17.000 31.526  1.00 36.86 ?  207 GLU D CA    1 
ATOM   3857 C C     . GLU B 1 215 ? 26.018  -17.461 32.344  1.00 42.64 ?  207 GLU D C     1 
ATOM   3858 O O     . GLU B 1 215 ? 25.846  -18.669 32.551  1.00 43.21 ?  207 GLU D O     1 
ATOM   3859 C CB    . GLU B 1 215 ? 28.483  -16.864 32.388  1.00 43.09 ?  207 GLU D CB    1 
ATOM   3860 C CG    . GLU B 1 215 ? 28.593  -17.816 33.563  1.00 45.62 ?  207 GLU D CG    1 
ATOM   3861 C CD    . GLU B 1 215 ? 29.490  -17.275 34.658  1.00 55.77 ?  207 GLU D CD    1 
ATOM   3862 O OE1   . GLU B 1 215 ? 30.720  -17.465 34.562  1.00 58.34 ?  207 GLU D OE1   1 
ATOM   3863 O OE2   . GLU B 1 215 ? 28.969  -16.660 35.615  1.00 56.31 ?  207 GLU D OE2   1 
ATOM   3864 N N     . ALA B 1 216 ? 25.160  -16.533 32.775  1.00 42.21 ?  208 ALA D N     1 
ATOM   3865 C CA    . ALA B 1 216 ? 23.935  -16.876 33.486  1.00 34.94 ?  208 ALA D CA    1 
ATOM   3866 C C     . ALA B 1 216 ? 22.783  -17.241 32.556  1.00 40.47 ?  208 ALA D C     1 
ATOM   3867 O O     . ALA B 1 216 ? 21.725  -17.656 33.042  1.00 42.33 ?  208 ALA D O     1 
ATOM   3868 C CB    . ALA B 1 216 ? 23.509  -15.718 34.393  1.00 39.68 ?  208 ALA D CB    1 
ATOM   3869 N N     . SER B 1 217 ? 22.958  -17.092 31.241  1.00 38.31 ?  209 SER D N     1 
ATOM   3870 C CA    . SER B 1 217 ? 21.949  -17.488 30.255  1.00 39.02 ?  209 SER D CA    1 
ATOM   3871 C C     . SER B 1 217 ? 22.648  -18.044 29.016  1.00 38.86 ?  209 SER D C     1 
ATOM   3872 O O     . SER B 1 217 ? 22.519  -17.503 27.913  1.00 36.62 ?  209 SER D O     1 
ATOM   3873 C CB    . SER B 1 217 ? 21.048  -16.303 29.903  1.00 38.70 ?  209 SER D CB    1 
ATOM   3874 O OG    . SER B 1 217 ? 19.774  -16.729 29.446  1.00 35.79 ?  209 SER D OG    1 
ATOM   3875 N N     . PRO B 1 218 ? 23.396  -19.161 29.165  1.00 35.84 ?  210 PRO D N     1 
ATOM   3876 C CA    . PRO B 1 218 ? 24.251  -19.665 28.073  1.00 41.10 ?  210 PRO D CA    1 
ATOM   3877 C C     . PRO B 1 218 ? 23.482  -20.513 27.063  1.00 40.27 ?  210 PRO D C     1 
ATOM   3878 O O     . PRO B 1 218 ? 23.775  -21.693 26.849  1.00 40.83 ?  210 PRO D O     1 
ATOM   3879 C CB    . PRO B 1 218 ? 25.296  -20.487 28.836  1.00 37.63 ?  210 PRO D CB    1 
ATOM   3880 C CG    . PRO B 1 218 ? 24.542  -21.033 30.008  1.00 36.16 ?  210 PRO D CG    1 
ATOM   3881 C CD    . PRO B 1 218 ? 23.413  -20.069 30.326  1.00 39.26 ?  210 PRO D CD    1 
ATOM   3882 N N     . VAL B 1 219 ? 22.490  -19.900 26.414  1.00 35.35 ?  211 VAL D N     1 
ATOM   3883 C CA    . VAL B 1 219 ? 21.612  -20.652 25.522  1.00 40.14 ?  211 VAL D CA    1 
ATOM   3884 C C     . VAL B 1 219 ? 22.363  -21.096 24.271  1.00 39.15 ?  211 VAL D C     1 
ATOM   3885 O O     . VAL B 1 219 ? 22.188  -22.224 23.796  1.00 39.55 ?  211 VAL D O     1 
ATOM   3886 C CB    . VAL B 1 219 ? 20.363  -19.818 25.181  1.00 38.82 ?  211 VAL D CB    1 
ATOM   3887 C CG1   . VAL B 1 219 ? 19.810  -20.202 23.814  1.00 36.12 ?  211 VAL D CG1   1 
ATOM   3888 C CG2   . VAL B 1 219 ? 19.303  -19.995 26.258  1.00 39.33 ?  211 VAL D CG2   1 
ATOM   3889 N N     . LEU B 1 220 ? 23.213  -20.224 23.720  1.00 35.42 ?  212 LEU D N     1 
ATOM   3890 C CA    . LEU B 1 220 ? 24.003  -20.604 22.553  1.00 34.78 ?  212 LEU D CA    1 
ATOM   3891 C C     . LEU B 1 220 ? 24.989  -21.717 22.883  1.00 36.42 ?  212 LEU D C     1 
ATOM   3892 O O     . LEU B 1 220 ? 25.366  -22.496 22.001  1.00 39.93 ?  212 LEU D O     1 
ATOM   3893 C CB    . LEU B 1 220 ? 24.749  -19.390 21.997  1.00 37.39 ?  212 LEU D CB    1 
ATOM   3894 C CG    . LEU B 1 220 ? 23.920  -18.215 21.470  1.00 35.42 ?  212 LEU D CG    1 
ATOM   3895 C CD1   . LEU B 1 220 ? 24.800  -17.241 20.699  1.00 34.20 ?  212 LEU D CD1   1 
ATOM   3896 C CD2   . LEU B 1 220 ? 22.765  -18.699 20.606  1.00 32.79 ?  212 LEU D CD2   1 
ATOM   3897 N N     . SER B 1 221 ? 25.417  -21.808 24.142  1.00 37.04 ?  213 SER D N     1 
ATOM   3898 C CA    . SER B 1 221 ? 26.352  -22.844 24.556  1.00 40.28 ?  213 SER D CA    1 
ATOM   3899 C C     . SER B 1 221 ? 25.677  -24.182 24.823  1.00 42.85 ?  213 SER D C     1 
ATOM   3900 O O     . SER B 1 221 ? 26.377  -25.181 25.018  1.00 41.46 ?  213 SER D O     1 
ATOM   3901 C CB    . SER B 1 221 ? 27.111  -22.393 25.806  1.00 39.00 ?  213 SER D CB    1 
ATOM   3902 O OG    . SER B 1 221 ? 27.952  -21.288 25.521  1.00 42.17 ?  213 SER D OG    1 
ATOM   3903 N N     . GLY B 1 222 ? 24.350  -24.229 24.830  1.00 43.77 ?  214 GLY D N     1 
ATOM   3904 C CA    . GLY B 1 222 ? 23.627  -25.443 25.134  1.00 42.19 ?  214 GLY D CA    1 
ATOM   3905 C C     . GLY B 1 222 ? 23.068  -25.528 26.535  1.00 42.10 ?  214 GLY D C     1 
ATOM   3906 O O     . GLY B 1 222 ? 22.604  -26.602 26.933  1.00 45.01 ?  214 GLY D O     1 
ATOM   3907 N N     . GLY B 1 223 ? 23.101  -24.435 27.299  1.00 39.34 ?  215 GLY D N     1 
ATOM   3908 C CA    . GLY B 1 223 ? 22.573  -24.416 28.643  1.00 41.04 ?  215 GLY D CA    1 
ATOM   3909 C C     . GLY B 1 223 ? 21.140  -23.907 28.695  1.00 44.30 ?  215 GLY D C     1 
ATOM   3910 O O     . GLY B 1 223 ? 20.505  -23.614 27.685  1.00 44.17 ?  215 GLY D O     1 
ATOM   3911 N N     . GLU B 1 224 ? 20.633  -23.806 29.924  1.00 45.81 ?  216 GLU D N     1 
ATOM   3912 C CA    . GLU B 1 224 ? 19.268  -23.348 30.127  1.00 45.01 ?  216 GLU D CA    1 
ATOM   3913 C C     . GLU B 1 224 ? 19.222  -21.828 30.249  1.00 43.96 ?  216 GLU D C     1 
ATOM   3914 O O     . GLU B 1 224 ? 20.173  -21.208 30.736  1.00 46.33 ?  216 GLU D O     1 
ATOM   3915 C CB    . GLU B 1 224 ? 18.676  -23.978 31.384  1.00 45.78 ?  216 GLU D CB    1 
ATOM   3916 C CG    . GLU B 1 224 ? 18.678  -25.496 31.376  1.00 50.91 ?  216 GLU D CG    1 
ATOM   3917 C CD    . GLU B 1 224 ? 17.364  -26.074 30.893  1.00 53.85 ?  216 GLU D CD    1 
ATOM   3918 O OE1   . GLU B 1 224 ? 16.443  -26.237 31.722  1.00 51.59 ?  216 GLU D OE1   1 
ATOM   3919 O OE2   . GLU B 1 224 ? 17.250  -26.366 29.683  1.00 51.29 ?  216 GLU D OE2   1 
ATOM   3920 N N     . PRO B 1 225 ? 18.132  -21.206 29.810  1.00 42.51 ?  217 PRO D N     1 
ATOM   3921 C CA    . PRO B 1 225 ? 17.991  -19.760 30.006  1.00 41.27 ?  217 PRO D CA    1 
ATOM   3922 C C     . PRO B 1 225 ? 17.816  -19.429 31.478  1.00 39.83 ?  217 PRO D C     1 
ATOM   3923 O O     . PRO B 1 225 ? 17.242  -20.200 32.251  1.00 44.66 ?  217 PRO D O     1 
ATOM   3924 C CB    . PRO B 1 225 ? 16.736  -19.399 29.199  1.00 44.67 ?  217 PRO D CB    1 
ATOM   3925 C CG    . PRO B 1 225 ? 16.329  -20.642 28.466  1.00 40.77 ?  217 PRO D CG    1 
ATOM   3926 C CD    . PRO B 1 225 ? 16.967  -21.804 29.140  1.00 39.09 ?  217 PRO D CD    1 
ATOM   3927 N N     . GLY B 1 226 ? 18.332  -18.267 31.863  1.00 41.46 ?  218 GLY D N     1 
ATOM   3928 C CA    . GLY B 1 226 ? 18.264  -17.831 33.234  1.00 35.54 ?  218 GLY D CA    1 
ATOM   3929 C C     . GLY B 1 226 ? 18.245  -16.323 33.352  1.00 39.86 ?  218 GLY D C     1 
ATOM   3930 O O     . GLY B 1 226 ? 18.421  -15.595 32.370  1.00 38.32 ?  218 GLY D O     1 
ATOM   3931 N N     . PRO B 1 227 ? 18.023  -15.823 34.565  1.00 46.05 ?  219 PRO D N     1 
ATOM   3932 C CA    . PRO B 1 227 ? 18.037  -14.372 34.771  1.00 41.56 ?  219 PRO D CA    1 
ATOM   3933 C C     . PRO B 1 227 ? 19.457  -13.833 34.729  1.00 37.95 ?  219 PRO D C     1 
ATOM   3934 O O     . PRO B 1 227 ? 20.391  -14.452 35.243  1.00 40.21 ?  219 PRO D O     1 
ATOM   3935 C CB    . PRO B 1 227 ? 17.408  -14.210 36.158  1.00 39.04 ?  219 PRO D CB    1 
ATOM   3936 C CG    . PRO B 1 227 ? 17.803  -15.469 36.868  1.00 46.21 ?  219 PRO D CG    1 
ATOM   3937 C CD    . PRO B 1 227 ? 17.760  -16.555 35.817  1.00 38.43 ?  219 PRO D CD    1 
ATOM   3938 N N     . HIS B 1 228 ? 19.615  -12.670 34.103  1.00 42.05 ?  220 HIS D N     1 
ATOM   3939 C CA    . HIS B 1 228 ? 20.929  -12.067 33.943  1.00 44.12 ?  220 HIS D CA    1 
ATOM   3940 C C     . HIS B 1 228 ? 20.775  -10.555 33.847  1.00 46.73 ?  220 HIS D C     1 
ATOM   3941 O O     . HIS B 1 228 ? 19.664  -10.022 33.790  1.00 41.14 ?  220 HIS D O     1 
ATOM   3942 C CB    . HIS B 1 228 ? 21.655  -12.630 32.715  1.00 41.23 ?  220 HIS D CB    1 
ATOM   3943 C CG    . HIS B 1 228 ? 21.128  -12.116 31.412  1.00 38.72 ?  220 HIS D CG    1 
ATOM   3944 N ND1   . HIS B 1 228 ? 21.747  -11.109 30.703  1.00 38.28 ?  220 HIS D ND1   1 
ATOM   3945 C CD2   . HIS B 1 228 ? 20.039  -12.470 30.690  1.00 39.94 ?  220 HIS D CD2   1 
ATOM   3946 C CE1   . HIS B 1 228 ? 21.061  -10.865 29.601  1.00 43.09 ?  220 HIS D CE1   1 
ATOM   3947 N NE2   . HIS B 1 228 ? 20.020  -11.677 29.568  1.00 41.14 ?  220 HIS D NE2   1 
ATOM   3948 N N     . LYS B 1 229 ? 21.917  -9.866  33.827  1.00 43.33 ?  221 LYS D N     1 
ATOM   3949 C CA    . LYS B 1 229 ? 21.952  -8.409  33.869  1.00 42.20 ?  221 LYS D CA    1 
ATOM   3950 C C     . LYS B 1 229 ? 22.660  -7.800  32.666  1.00 42.64 ?  221 LYS D C     1 
ATOM   3951 O O     . LYS B 1 229 ? 22.846  -6.579  32.624  1.00 41.33 ?  221 LYS D O     1 
ATOM   3952 C CB    . LYS B 1 229 ? 22.631  -7.939  35.159  1.00 50.39 ?  221 LYS D CB    1 
ATOM   3953 C CG    . LYS B 1 229 ? 22.032  -8.520  36.428  1.00 50.39 ?  221 LYS D CG    1 
ATOM   3954 C CD    . LYS B 1 229 ? 23.041  -8.495  37.566  1.00 55.81 ?  221 LYS D CD    1 
ATOM   3955 C CE    . LYS B 1 229 ? 22.417  -7.990  38.859  1.00 66.49 ?  221 LYS D CE    1 
ATOM   3956 N NZ    . LYS B 1 229 ? 23.440  -7.445  39.799  1.00 63.63 ?  221 LYS D NZ    1 
ATOM   3957 N N     . LEU B 1 230 ? 23.066  -8.613  31.692  1.00 37.74 ?  222 LEU D N     1 
ATOM   3958 C CA    . LEU B 1 230 ? 23.777  -8.120  30.513  1.00 37.77 ?  222 LEU D CA    1 
ATOM   3959 C C     . LEU B 1 230 ? 22.747  -7.571  29.530  1.00 32.81 ?  222 LEU D C     1 
ATOM   3960 O O     . LEU B 1 230 ? 22.316  -8.237  28.584  1.00 33.18 ?  222 LEU D O     1 
ATOM   3961 C CB    . LEU B 1 230 ? 24.623  -9.224  29.890  1.00 34.75 ?  222 LEU D CB    1 
ATOM   3962 C CG    . LEU B 1 230 ? 25.657  -9.890  30.805  1.00 34.72 ?  222 LEU D CG    1 
ATOM   3963 C CD1   . LEU B 1 230 ? 26.696  -10.630 29.981  1.00 26.54 ?  222 LEU D CD1   1 
ATOM   3964 C CD2   . LEU B 1 230 ? 26.323  -8.876  31.725  1.00 35.55 ?  222 LEU D CD2   1 
ATOM   3965 N N     . GLN B 1 231 ? 22.348  -6.323  29.771  1.00 34.76 ?  223 GLN D N     1 
ATOM   3966 C CA    . GLN B 1 231 ? 21.305  -5.694  28.970  1.00 34.69 ?  223 GLN D CA    1 
ATOM   3967 C C     . GLN B 1 231 ? 21.709  -5.640  27.503  1.00 33.44 ?  223 GLN D C     1 
ATOM   3968 O O     . GLN B 1 231 ? 22.832  -5.250  27.166  1.00 29.45 ?  223 GLN D O     1 
ATOM   3969 C CB    . GLN B 1 231 ? 21.014  -4.288  29.493  1.00 35.34 ?  223 GLN D CB    1 
ATOM   3970 C CG    . GLN B 1 231 ? 20.089  -4.256  30.699  1.00 36.25 ?  223 GLN D CG    1 
ATOM   3971 C CD    . GLN B 1 231 ? 19.510  -2.878  30.950  1.00 49.21 ?  223 GLN D CD    1 
ATOM   3972 O OE1   . GLN B 1 231 ? 19.116  -2.178  30.017  1.00 48.88 ?  223 GLN D OE1   1 
ATOM   3973 N NE2   . GLN B 1 231 ? 19.454  -2.482  32.217  1.00 52.86 ?  223 GLN D NE2   1 
ATOM   3974 N N     . GLY B 1 232 ? 20.783  -6.035  26.630  1.00 30.77 ?  224 GLY D N     1 
ATOM   3975 C CA    . GLY B 1 232 ? 21.052  -6.161  25.219  1.00 34.87 ?  224 GLY D CA    1 
ATOM   3976 C C     . GLY B 1 232 ? 21.434  -7.557  24.772  1.00 30.46 ?  224 GLY D C     1 
ATOM   3977 O O     . GLY B 1 232 ? 21.386  -7.842  23.571  1.00 32.31 ?  224 GLY D O     1 
ATOM   3978 N N     . LEU B 1 233 ? 21.805  -8.433  25.701  1.00 30.36 ?  225 LEU D N     1 
ATOM   3979 C CA    . LEU B 1 233 ? 22.208  -9.803  25.412  1.00 30.20 ?  225 LEU D CA    1 
ATOM   3980 C C     . LEU B 1 233 ? 21.233  -10.778 26.066  1.00 31.53 ?  225 LEU D C     1 
ATOM   3981 O O     . LEU B 1 233 ? 20.284  -10.385 26.748  1.00 34.62 ?  225 LEU D O     1 
ATOM   3982 C CB    . LEU B 1 233 ? 23.634  -10.064 25.900  1.00 32.40 ?  225 LEU D CB    1 
ATOM   3983 C CG    . LEU B 1 233 ? 24.695  -9.030  25.536  1.00 29.94 ?  225 LEU D CG    1 
ATOM   3984 C CD1   . LEU B 1 233 ? 26.057  -9.471  26.038  1.00 31.74 ?  225 LEU D CD1   1 
ATOM   3985 C CD2   . LEU B 1 233 ? 24.726  -8.815  24.038  1.00 31.67 ?  225 LEU D CD2   1 
ATOM   3986 N N     . GLY B 1 234 ? 21.486  -12.067 25.849  1.00 35.36 ?  226 GLY D N     1 
ATOM   3987 C CA    . GLY B 1 234 ? 20.748  -13.126 26.513  1.00 31.99 ?  226 GLY D CA    1 
ATOM   3988 C C     . GLY B 1 234 ? 19.248  -13.107 26.301  1.00 36.48 ?  226 GLY D C     1 
ATOM   3989 O O     . GLY B 1 234 ? 18.486  -12.958 27.261  1.00 35.60 ?  226 GLY D O     1 
ATOM   3990 N N     . ALA B 1 235 ? 18.806  -13.276 25.054  1.00 33.89 ?  227 ALA D N     1 
ATOM   3991 C CA    . ALA B 1 235 ? 17.376  -13.272 24.774  1.00 31.11 ?  227 ALA D CA    1 
ATOM   3992 C C     . ALA B 1 235 ? 16.667  -14.488 25.356  1.00 32.37 ?  227 ALA D C     1 
ATOM   3993 O O     . ALA B 1 235 ? 15.434  -14.488 25.440  1.00 31.39 ?  227 ALA D O     1 
ATOM   3994 C CB    . ALA B 1 235 ? 17.134  -13.198 23.265  1.00 29.65 ?  227 ALA D CB    1 
ATOM   3995 N N     . GLY B 1 236 ? 17.410  -15.511 25.774  1.00 31.99 ?  228 GLY D N     1 
ATOM   3996 C CA    . GLY B 1 236 ? 16.813  -16.729 26.273  1.00 33.21 ?  228 GLY D CA    1 
ATOM   3997 C C     . GLY B 1 236 ? 16.395  -17.713 25.205  1.00 38.29 ?  228 GLY D C     1 
ATOM   3998 O O     . GLY B 1 236 ? 15.868  -18.781 25.541  1.00 40.09 ?  228 GLY D O     1 
ATOM   3999 N N     . PHE B 1 237 ? 16.609  -17.389 23.933  1.00 33.98 ?  229 PHE D N     1 
ATOM   4000 C CA    . PHE B 1 237 ? 16.283  -18.279 22.830  1.00 37.50 ?  229 PHE D CA    1 
ATOM   4001 C C     . PHE B 1 237 ? 17.281  -18.023 21.710  1.00 38.85 ?  229 PHE D C     1 
ATOM   4002 O O     . PHE B 1 237 ? 18.139  -17.141 21.807  1.00 41.29 ?  229 PHE D O     1 
ATOM   4003 C CB    . PHE B 1 237 ? 14.838  -18.071 22.359  1.00 38.31 ?  229 PHE D CB    1 
ATOM   4004 C CG    . PHE B 1 237 ? 14.520  -16.651 21.981  1.00 34.89 ?  229 PHE D CG    1 
ATOM   4005 C CD1   . PHE B 1 237 ? 14.038  -15.763 22.925  1.00 28.00 ?  229 PHE D CD1   1 
ATOM   4006 C CD2   . PHE B 1 237 ? 14.697  -16.208 20.680  1.00 37.36 ?  229 PHE D CD2   1 
ATOM   4007 C CE1   . PHE B 1 237 ? 13.745  -14.456 22.585  1.00 37.26 ?  229 PHE D CE1   1 
ATOM   4008 C CE2   . PHE B 1 237 ? 14.404  -14.901 20.332  1.00 34.35 ?  229 PHE D CE2   1 
ATOM   4009 C CZ    . PHE B 1 237 ? 13.928  -14.025 21.286  1.00 32.32 ?  229 PHE D CZ    1 
ATOM   4010 N N     . ILE B 1 238 ? 17.165  -18.802 20.639  1.00 35.77 ?  230 ILE D N     1 
ATOM   4011 C CA    . ILE B 1 238 ? 18.005  -18.641 19.457  1.00 39.13 ?  230 ILE D CA    1 
ATOM   4012 C C     . ILE B 1 238 ? 17.199  -17.862 18.420  1.00 39.91 ?  230 ILE D C     1 
ATOM   4013 O O     . ILE B 1 238 ? 16.223  -18.404 17.876  1.00 41.76 ?  230 ILE D O     1 
ATOM   4014 C CB    . ILE B 1 238 ? 18.470  -19.991 18.899  1.00 37.10 ?  230 ILE D CB    1 
ATOM   4015 C CG1   . ILE B 1 238 ? 19.410  -20.677 19.890  1.00 33.62 ?  230 ILE D CG1   1 
ATOM   4016 C CG2   . ILE B 1 238 ? 19.161  -19.795 17.560  1.00 42.90 ?  230 ILE D CG2   1 
ATOM   4017 C CD1   . ILE B 1 238 ? 19.005  -22.086 20.235  1.00 37.33 ?  230 ILE D CD1   1 
ATOM   4018 N N     . PRO B 1 239 ? 17.554  -16.618 18.123  1.00 33.51 ?  231 PRO D N     1 
ATOM   4019 C CA    . PRO B 1 239 ? 16.758  -15.826 17.183  1.00 34.16 ?  231 PRO D CA    1 
ATOM   4020 C C     . PRO B 1 239 ? 16.967  -16.271 15.745  1.00 35.30 ?  231 PRO D C     1 
ATOM   4021 O O     . PRO B 1 239 ? 18.051  -16.707 15.350  1.00 34.47 ?  231 PRO D O     1 
ATOM   4022 C CB    . PRO B 1 239 ? 17.275  -14.395 17.394  1.00 37.35 ?  231 PRO D CB    1 
ATOM   4023 C CG    . PRO B 1 239 ? 18.151  -14.449 18.621  1.00 33.11 ?  231 PRO D CG    1 
ATOM   4024 C CD    . PRO B 1 239 ? 18.669  -15.844 18.686  1.00 33.40 ?  231 PRO D CD    1 
ATOM   4025 N N     . GLY B 1 240 ? 15.897  -16.150 14.956  1.00 36.59 ?  232 GLY D N     1 
ATOM   4026 C CA    . GLY B 1 240 ? 15.997  -16.401 13.530  1.00 34.28 ?  232 GLY D CA    1 
ATOM   4027 C C     . GLY B 1 240 ? 16.951  -15.469 12.816  1.00 36.59 ?  232 GLY D C     1 
ATOM   4028 O O     . GLY B 1 240 ? 17.412  -15.790 11.715  1.00 36.73 ?  232 GLY D O     1 
ATOM   4029 N N     . THR B 1 241 ? 17.261  -14.321 13.419  1.00 38.65 ?  233 THR D N     1 
ATOM   4030 C CA    . THR B 1 241 ? 18.217  -13.375 12.861  1.00 29.81 ?  233 THR D CA    1 
ATOM   4031 C C     . THR B 1 241 ? 19.664  -13.738 13.169  1.00 35.12 ?  233 THR D C     1 
ATOM   4032 O O     . THR B 1 241 ? 20.574  -13.084 12.647  1.00 31.30 ?  233 THR D O     1 
ATOM   4033 C CB    . THR B 1 241 ? 17.924  -11.963 13.379  1.00 32.00 ?  233 THR D CB    1 
ATOM   4034 O OG1   . THR B 1 241 ? 17.587  -12.024 14.770  1.00 28.49 ?  233 THR D OG1   1 
ATOM   4035 C CG2   . THR B 1 241 ? 16.768  -11.344 12.604  1.00 29.92 ?  233 THR D CG2   1 
ATOM   4036 N N     . LEU B 1 242 ? 19.900  -14.750 13.999  1.00 30.34 ?  234 LEU D N     1 
ATOM   4037 C CA    . LEU B 1 242 ? 21.250  -15.217 14.283  1.00 33.24 ?  234 LEU D CA    1 
ATOM   4038 C C     . LEU B 1 242 ? 21.602  -16.378 13.364  1.00 34.85 ?  234 LEU D C     1 
ATOM   4039 O O     . LEU B 1 242 ? 20.843  -17.348 13.260  1.00 36.00 ?  234 LEU D O     1 
ATOM   4040 C CB    . LEU B 1 242 ? 21.389  -15.654 15.741  1.00 33.24 ?  234 LEU D CB    1 
ATOM   4041 C CG    . LEU B 1 242 ? 22.722  -16.343 16.046  1.00 31.16 ?  234 LEU D CG    1 
ATOM   4042 C CD1   . LEU B 1 242 ? 23.866  -15.340 16.006  1.00 28.61 ?  234 LEU D CD1   1 
ATOM   4043 C CD2   . LEU B 1 242 ? 22.683  -17.070 17.380  1.00 30.46 ?  234 LEU D CD2   1 
ATOM   4044 N N     . ASN B 1 243 ? 22.752  -16.276 12.703  1.00 32.57 ?  235 ASN D N     1 
ATOM   4045 C CA    . ASN B 1 243 ? 23.295  -17.374 11.907  1.00 37.37 ?  235 ASN D CA    1 
ATOM   4046 C C     . ASN B 1 243 ? 24.170  -18.207 12.836  1.00 34.32 ?  235 ASN D C     1 
ATOM   4047 O O     . ASN B 1 243 ? 25.300  -17.828 13.150  1.00 36.45 ?  235 ASN D O     1 
ATOM   4048 C CB    . ASN B 1 243 ? 24.076  -16.841 10.710  1.00 29.36 ?  235 ASN D CB    1 
ATOM   4049 C CG    . ASN B 1 243 ? 24.680  -17.948 9.861   1.00 38.01 ?  235 ASN D CG    1 
ATOM   4050 O OD1   . ASN B 1 243 ? 24.341  -19.122 10.013  1.00 39.32 ?  235 ASN D OD1   1 
ATOM   4051 N ND2   . ASN B 1 243 ? 25.583  -17.575 8.960   1.00 37.21 ?  235 ASN D ND2   1 
ATOM   4052 N N     . THR B 1 244 ? 23.643  -19.346 13.286  1.00 37.20 ?  236 THR D N     1 
ATOM   4053 C CA    . THR B 1 244 ? 24.370  -20.196 14.223  1.00 36.14 ?  236 THR D CA    1 
ATOM   4054 C C     . THR B 1 244 ? 25.586  -20.868 13.602  1.00 39.63 ?  236 THR D C     1 
ATOM   4055 O O     . THR B 1 244 ? 26.278  -21.617 14.300  1.00 40.64 ?  236 THR D O     1 
ATOM   4056 C CB    . THR B 1 244 ? 23.432  -21.256 14.801  1.00 39.55 ?  236 THR D CB    1 
ATOM   4057 O OG1   . THR B 1 244 ? 22.815  -21.981 13.733  1.00 42.11 ?  236 THR D OG1   1 
ATOM   4058 C CG2   . THR B 1 244 ? 22.355  -20.602 15.647  1.00 40.34 ?  236 THR D CG2   1 
ATOM   4059 N N     . GLU B 1 245 ? 25.860  -20.629 12.323  1.00 36.35 ?  237 GLU D N     1 
ATOM   4060 C CA    . GLU B 1 245 ? 27.045  -21.153 11.663  1.00 41.21 ?  237 GLU D CA    1 
ATOM   4061 C C     . GLU B 1 245 ? 28.139  -20.109 11.499  1.00 40.55 ?  237 GLU D C     1 
ATOM   4062 O O     . GLU B 1 245 ? 29.197  -20.423 10.946  1.00 39.91 ?  237 GLU D O     1 
ATOM   4063 C CB    . GLU B 1 245 ? 26.673  -21.724 10.290  1.00 48.66 ?  237 GLU D CB    1 
ATOM   4064 C CG    . GLU B 1 245 ? 25.636  -22.833 10.328  1.00 45.35 ?  237 GLU D CG    1 
ATOM   4065 C CD    . GLU B 1 245 ? 25.776  -23.797 9.167   1.00 62.77 ?  237 GLU D CD    1 
ATOM   4066 O OE1   . GLU B 1 245 ? 26.020  -24.998 9.411   1.00 71.62 ?  237 GLU D OE1   1 
ATOM   4067 O OE2   . GLU B 1 245 ? 25.644  -23.353 8.007   1.00 76.68 ?  237 GLU D OE2   1 
ATOM   4068 N N     . ILE B 1 246 ? 27.916  -18.881 11.969  1.00 42.72 ?  238 ILE D N     1 
ATOM   4069 C CA    . ILE B 1 246 ? 28.877  -17.819 11.687  1.00 38.62 ?  238 ILE D CA    1 
ATOM   4070 C C     . ILE B 1 246 ? 30.006  -17.791 12.711  1.00 40.28 ?  238 ILE D C     1 
ATOM   4071 O O     . ILE B 1 246 ? 31.139  -17.431 12.373  1.00 43.69 ?  238 ILE D O     1 
ATOM   4072 C CB    . ILE B 1 246 ? 28.164  -16.458 11.590  1.00 33.50 ?  238 ILE D CB    1 
ATOM   4073 C CG1   . ILE B 1 246 ? 29.023  -15.467 10.809  1.00 35.07 ?  238 ILE D CG1   1 
ATOM   4074 C CG2   . ILE B 1 246 ? 27.836  -15.898 12.968  1.00 36.56 ?  238 ILE D CG2   1 
ATOM   4075 C CD1   . ILE B 1 246 ? 28.922  -15.626 9.311   1.00 41.70 ?  238 ILE D CD1   1 
ATOM   4076 N N     . TYR B 1 247 ? 29.742  -18.183 13.954  1.00 37.54 ?  239 TYR D N     1 
ATOM   4077 C CA    . TYR B 1 247 ? 30.733  -18.088 15.016  1.00 41.44 ?  239 TYR D CA    1 
ATOM   4078 C C     . TYR B 1 247 ? 31.431  -19.427 15.218  1.00 45.89 ?  239 TYR D C     1 
ATOM   4079 O O     . TYR B 1 247 ? 30.801  -20.487 15.157  1.00 47.42 ?  239 TYR D O     1 
ATOM   4080 C CB    . TYR B 1 247 ? 30.101  -17.615 16.329  1.00 37.10 ?  239 TYR D CB    1 
ATOM   4081 C CG    . TYR B 1 247 ? 28.860  -18.366 16.763  1.00 39.30 ?  239 TYR D CG    1 
ATOM   4082 C CD1   . TYR B 1 247 ? 28.957  -19.528 17.517  1.00 40.42 ?  239 TYR D CD1   1 
ATOM   4083 C CD2   . TYR B 1 247 ? 27.592  -17.898 16.441  1.00 38.90 ?  239 TYR D CD2   1 
ATOM   4084 C CE1   . TYR B 1 247 ? 27.828  -20.213 17.925  1.00 41.87 ?  239 TYR D CE1   1 
ATOM   4085 C CE2   . TYR B 1 247 ? 26.455  -18.577 16.846  1.00 39.27 ?  239 TYR D CE2   1 
ATOM   4086 C CZ    . TYR B 1 247 ? 26.580  -19.733 17.588  1.00 39.72 ?  239 TYR D CZ    1 
ATOM   4087 O OH    . TYR B 1 247 ? 25.456  -20.412 17.994  1.00 45.35 ?  239 TYR D OH    1 
ATOM   4088 N N     . ASP B 1 248 ? 32.741  -19.365 15.452  1.00 38.85 ?  240 ASP D N     1 
ATOM   4089 C CA    . ASP B 1 248 ? 33.551  -20.557 15.657  1.00 41.49 ?  240 ASP D CA    1 
ATOM   4090 C C     . ASP B 1 248 ? 33.695  -20.932 17.127  1.00 44.66 ?  240 ASP D C     1 
ATOM   4091 O O     . ASP B 1 248 ? 34.045  -22.079 17.428  1.00 47.31 ?  240 ASP D O     1 
ATOM   4092 C CB    . ASP B 1 248 ? 34.940  -20.354 15.039  1.00 45.52 ?  240 ASP D CB    1 
ATOM   4093 C CG    . ASP B 1 248 ? 34.875  -19.794 13.625  1.00 49.97 ?  240 ASP D CG    1 
ATOM   4094 O OD1   . ASP B 1 248 ? 34.355  -20.491 12.728  1.00 56.82 ?  240 ASP D OD1   1 
ATOM   4095 O OD2   . ASP B 1 248 ? 35.340  -18.653 13.410  1.00 45.53 ?  240 ASP D OD2   1 
ATOM   4096 N N     . SER B 1 249 ? 33.436  -20.000 18.042  1.00 43.47 ?  241 SER D N     1 
ATOM   4097 C CA    . SER B 1 249 ? 33.490  -20.279 19.470  1.00 37.02 ?  241 SER D CA    1 
ATOM   4098 C C     . SER B 1 249 ? 32.585  -19.294 20.195  1.00 36.64 ?  241 SER D C     1 
ATOM   4099 O O     . SER B 1 249 ? 32.089  -18.326 19.613  1.00 38.19 ?  241 SER D O     1 
ATOM   4100 C CB    . SER B 1 249 ? 34.923  -20.200 20.009  1.00 35.74 ?  241 SER D CB    1 
ATOM   4101 O OG    . SER B 1 249 ? 35.467  -18.905 19.828  1.00 43.67 ?  241 SER D OG    1 
ATOM   4102 N N     . ILE B 1 250 ? 32.372  -19.554 21.481  1.00 33.95 ?  242 ILE D N     1 
ATOM   4103 C CA    . ILE B 1 250 ? 31.523  -18.727 22.329  1.00 39.23 ?  242 ILE D CA    1 
ATOM   4104 C C     . ILE B 1 250 ? 32.285  -18.406 23.606  1.00 39.38 ?  242 ILE D C     1 
ATOM   4105 O O     . ILE B 1 250 ? 32.952  -19.277 24.176  1.00 39.68 ?  242 ILE D O     1 
ATOM   4106 C CB    . ILE B 1 250 ? 30.184  -19.426 22.654  1.00 36.74 ?  242 ILE D CB    1 
ATOM   4107 C CG1   . ILE B 1 250 ? 29.390  -19.691 21.373  1.00 36.39 ?  242 ILE D CG1   1 
ATOM   4108 C CG2   . ILE B 1 250 ? 29.353  -18.592 23.619  1.00 40.80 ?  242 ILE D CG2   1 
ATOM   4109 C CD1   . ILE B 1 250 ? 28.344  -20.775 21.520  1.00 42.96 ?  242 ILE D CD1   1 
ATOM   4110 N N     . ILE B 1 251 ? 32.197  -17.154 24.047  1.00 37.56 ?  243 ILE D N     1 
ATOM   4111 C CA    . ILE B 1 251 ? 32.756  -16.726 25.324  1.00 28.74 ?  243 ILE D CA    1 
ATOM   4112 C C     . ILE B 1 251 ? 31.607  -16.268 26.209  1.00 35.91 ?  243 ILE D C     1 
ATOM   4113 O O     . ILE B 1 251 ? 30.895  -15.313 25.870  1.00 34.48 ?  243 ILE D O     1 
ATOM   4114 C CB    . ILE B 1 251 ? 33.795  -15.607 25.159  1.00 34.73 ?  243 ILE D CB    1 
ATOM   4115 C CG1   . ILE B 1 251 ? 35.017  -16.121 24.396  1.00 34.31 ?  243 ILE D CG1   1 
ATOM   4116 C CG2   . ILE B 1 251 ? 34.205  -15.061 26.519  1.00 35.49 ?  243 ILE D CG2   1 
ATOM   4117 C CD1   . ILE B 1 251 ? 35.992  -15.033 24.019  1.00 37.90 ?  243 ILE D CD1   1 
ATOM   4118 N N     . LYS B 1 252 ? 31.422  -16.952 27.334  1.00 36.97 ?  244 LYS D N     1 
ATOM   4119 C CA    . LYS B 1 252 ? 30.433  -16.558 28.325  1.00 37.44 ?  244 LYS D CA    1 
ATOM   4120 C C     . LYS B 1 252 ? 31.061  -15.581 29.308  1.00 32.93 ?  244 LYS D C     1 
ATOM   4121 O O     . LYS B 1 252 ? 32.227  -15.726 29.686  1.00 37.88 ?  244 LYS D O     1 
ATOM   4122 C CB    . LYS B 1 252 ? 29.890  -17.782 29.065  1.00 35.41 ?  244 LYS D CB    1 
ATOM   4123 C CG    . LYS B 1 252 ? 29.418  -18.897 28.145  1.00 39.77 ?  244 LYS D CG    1 
ATOM   4124 C CD    . LYS B 1 252 ? 28.914  -20.097 28.932  1.00 38.74 ?  244 LYS D CD    1 
ATOM   4125 C CE    . LYS B 1 252 ? 30.065  -20.940 29.459  1.00 42.98 ?  244 LYS D CE    1 
ATOM   4126 N NZ    . LYS B 1 252 ? 29.652  -21.797 30.607  1.00 52.14 ?  244 LYS D NZ    1 
ATOM   4127 N N     . VAL B 1 253 ? 30.287  -14.574 29.708  1.00 37.15 ?  245 VAL D N     1 
ATOM   4128 C CA    . VAL B 1 253 ? 30.761  -13.530 30.609  1.00 34.82 ?  245 VAL D CA    1 
ATOM   4129 C C     . VAL B 1 253 ? 29.804  -13.421 31.788  1.00 34.11 ?  245 VAL D C     1 
ATOM   4130 O O     . VAL B 1 253 ? 28.581  -13.467 31.615  1.00 36.00 ?  245 VAL D O     1 
ATOM   4131 C CB    . VAL B 1 253 ? 30.894  -12.170 29.890  1.00 32.54 ?  245 VAL D CB    1 
ATOM   4132 C CG1   . VAL B 1 253 ? 31.622  -11.170 30.774  1.00 28.05 ?  245 VAL D CG1   1 
ATOM   4133 C CG2   . VAL B 1 253 ? 31.619  -12.332 28.561  1.00 34.15 ?  245 VAL D CG2   1 
ATOM   4134 N N     . GLY B 1 254 ? 30.366  -13.275 32.991  1.00 37.76 ?  246 GLY D N     1 
ATOM   4135 C CA    . GLY B 1 254 ? 29.549  -13.107 34.172  1.00 38.78 ?  246 GLY D CA    1 
ATOM   4136 C C     . GLY B 1 254 ? 28.999  -11.699 34.307  1.00 38.97 ?  246 GLY D C     1 
ATOM   4137 O O     . GLY B 1 254 ? 29.444  -10.759 33.649  1.00 35.17 ?  246 GLY D O     1 
ATOM   4138 N N     . ASN B 1 255 ? 28.004  -11.560 35.187  1.00 41.87 ?  247 ASN D N     1 
ATOM   4139 C CA    . ASN B 1 255 ? 27.369  -10.260 35.384  1.00 38.20 ?  247 ASN D CA    1 
ATOM   4140 C C     . ASN B 1 255 ? 28.352  -9.239  35.941  1.00 41.68 ?  247 ASN D C     1 
ATOM   4141 O O     . ASN B 1 255 ? 28.375  -8.082  35.504  1.00 37.75 ?  247 ASN D O     1 
ATOM   4142 C CB    . ASN B 1 255 ? 26.167  -10.397 36.316  1.00 38.96 ?  247 ASN D CB    1 
ATOM   4143 C CG    . ASN B 1 255 ? 25.066  -11.248 35.725  1.00 42.37 ?  247 ASN D CG    1 
ATOM   4144 O OD1   . ASN B 1 255 ? 24.959  -11.387 34.508  1.00 42.80 ?  247 ASN D OD1   1 
ATOM   4145 N ND2   . ASN B 1 255 ? 24.237  -11.824 36.588  1.00 42.61 ?  247 ASN D ND2   1 
ATOM   4146 N N     . ASP B 1 256 ? 29.177  -9.650  36.905  1.00 44.53 ?  248 ASP D N     1 
ATOM   4147 C CA    . ASP B 1 256 ? 30.059  -8.708  37.582  1.00 43.36 ?  248 ASP D CA    1 
ATOM   4148 C C     . ASP B 1 256 ? 31.329  -8.430  36.790  1.00 41.87 ?  248 ASP D C     1 
ATOM   4149 O O     . ASP B 1 256 ? 31.879  -7.327  36.882  1.00 39.35 ?  248 ASP D O     1 
ATOM   4150 C CB    . ASP B 1 256 ? 30.412  -9.231  38.973  1.00 46.65 ?  248 ASP D CB    1 
ATOM   4151 C CG    . ASP B 1 256 ? 29.269  -9.080  39.957  1.00 54.46 ?  248 ASP D CG    1 
ATOM   4152 O OD1   . ASP B 1 256 ? 28.120  -8.879  39.510  1.00 54.16 ?  248 ASP D OD1   1 
ATOM   4153 O OD2   . ASP B 1 256 ? 29.520  -9.164  41.177  1.00 55.72 ?  248 ASP D OD2   1 
ATOM   4154 N N     . THR B 1 257 ? 31.815  -9.407  36.020  1.00 38.11 ?  249 THR D N     1 
ATOM   4155 C CA    . THR B 1 257 ? 33.010  -9.173  35.216  1.00 39.21 ?  249 THR D CA    1 
ATOM   4156 C C     . THR B 1 257 ? 32.738  -8.165  34.107  1.00 41.76 ?  249 THR D C     1 
ATOM   4157 O O     . THR B 1 257 ? 33.572  -7.294  33.834  1.00 38.00 ?  249 THR D O     1 
ATOM   4158 C CB    . THR B 1 257 ? 33.524  -10.488 34.631  1.00 38.28 ?  249 THR D CB    1 
ATOM   4159 O OG1   . THR B 1 257 ? 32.466  -11.141 33.919  1.00 49.99 ?  249 THR D OG1   1 
ATOM   4160 C CG2   . THR B 1 257 ? 34.023  -11.403 35.735  1.00 40.25 ?  249 THR D CG2   1 
ATOM   4161 N N     . ALA B 1 258 ? 31.577  -8.269  33.457  1.00 35.92 ?  250 ALA D N     1 
ATOM   4162 C CA    . ALA B 1 258 ? 31.193  -7.274  32.461  1.00 37.48 ?  250 ALA D CA    1 
ATOM   4163 C C     . ALA B 1 258 ? 31.031  -5.902  33.101  1.00 34.62 ?  250 ALA D C     1 
ATOM   4164 O O     . ALA B 1 258 ? 31.476  -4.887  32.550  1.00 36.15 ?  250 ALA D O     1 
ATOM   4165 C CB    . ALA B 1 258 ? 29.900  -7.701  31.766  1.00 32.01 ?  250 ALA D CB    1 
ATOM   4166 N N     . MET B 1 259 ? 30.387  -5.856  34.270  1.00 33.97 ?  251 MET D N     1 
ATOM   4167 C CA    . MET B 1 259 ? 30.248  -4.606  35.010  1.00 37.61 ?  251 MET D CA    1 
ATOM   4168 C C     . MET B 1 259 ? 31.608  -4.009  35.350  1.00 39.08 ?  251 MET D C     1 
ATOM   4169 O O     . MET B 1 259 ? 31.864  -2.830  35.082  1.00 34.41 ?  251 MET D O     1 
ATOM   4170 C CB    . MET B 1 259 ? 29.426  -4.847  36.277  1.00 38.97 ?  251 MET D CB    1 
ATOM   4171 C CG    . MET B 1 259 ? 29.153  -3.605  37.107  1.00 49.82 ?  251 MET D CG    1 
ATOM   4172 S SD    . MET B 1 259 ? 28.397  -4.010  38.696  1.00 79.57 ?  251 MET D SD    1 
ATOM   4173 C CE    . MET B 1 259 ? 29.844  -4.338  39.700  1.00 58.26 ?  251 MET D CE    1 
ATOM   4174 N N     . GLU B 1 260 ? 32.496  -4.814  35.939  1.00 39.59 ?  252 GLU D N     1 
ATOM   4175 C CA    . GLU B 1 260 ? 33.819  -4.317  36.304  1.00 32.74 ?  252 GLU D CA    1 
ATOM   4176 C C     . GLU B 1 260 ? 34.613  -3.869  35.082  1.00 32.56 ?  252 GLU D C     1 
ATOM   4177 O O     . GLU B 1 260 ? 35.417  -2.934  35.174  1.00 37.80 ?  252 GLU D O     1 
ATOM   4178 C CB    . GLU B 1 260 ? 34.588  -5.392  37.072  1.00 30.72 ?  252 GLU D CB    1 
ATOM   4179 N N     . MET B 1 261 ? 34.402  -4.514  33.933  1.00 31.35 ?  253 MET D N     1 
ATOM   4180 C CA    . MET B 1 261 ? 35.129  -4.122  32.730  1.00 31.13 ?  253 MET D CA    1 
ATOM   4181 C C     . MET B 1 261 ? 34.652  -2.771  32.213  1.00 33.33 ?  253 MET D C     1 
ATOM   4182 O O     . MET B 1 261 ? 35.462  -1.953  31.762  1.00 31.46 ?  253 MET D O     1 
ATOM   4183 C CB    . MET B 1 261 ? 34.984  -5.194  31.650  1.00 33.26 ?  253 MET D CB    1 
ATOM   4184 C CG    . MET B 1 261 ? 35.932  -5.023  30.467  1.00 39.54 ?  253 MET D CG    1 
ATOM   4185 S SD    . MET B 1 261 ? 37.511  -4.249  30.886  1.00 45.01 ?  253 MET D SD    1 
ATOM   4186 C CE    . MET B 1 261 ? 38.470  -5.676  31.386  1.00 44.96 ?  253 MET D CE    1 
ATOM   4187 N N     . SER B 1 262 ? 33.344  -2.514  32.274  1.00 32.24 ?  254 SER D N     1 
ATOM   4188 C CA    . SER B 1 262 ? 32.828  -1.219  31.840  1.00 32.60 ?  254 SER D CA    1 
ATOM   4189 C C     . SER B 1 262 ? 33.369  -0.089  32.707  1.00 33.62 ?  254 SER D C     1 
ATOM   4190 O O     . SER B 1 262 ? 33.686  0.994   32.201  1.00 30.89 ?  254 SER D O     1 
ATOM   4191 C CB    . SER B 1 262 ? 31.300  -1.228  31.860  1.00 33.29 ?  254 SER D CB    1 
ATOM   4192 O OG    . SER B 1 262 ? 30.779  -1.939  30.752  1.00 36.06 ?  254 SER D OG    1 
ATOM   4193 N N     . ARG B 1 263 ? 33.482  -0.321  34.017  1.00 31.34 ?  255 ARG D N     1 
ATOM   4194 C CA    . ARG B 1 263 ? 34.004  0.710   34.909  1.00 34.93 ?  255 ARG D CA    1 
ATOM   4195 C C     . ARG B 1 263 ? 35.484  0.967   34.659  1.00 34.00 ?  255 ARG D C     1 
ATOM   4196 O O     . ARG B 1 263 ? 35.932  2.120   34.678  1.00 34.95 ?  255 ARG D O     1 
ATOM   4197 C CB    . ARG B 1 263 ? 33.765  0.310   36.364  1.00 32.67 ?  255 ARG D CB    1 
ATOM   4198 C CG    . ARG B 1 263 ? 32.379  -0.244  36.625  1.00 36.63 ?  255 ARG D CG    1 
ATOM   4199 C CD    . ARG B 1 263 ? 31.653  0.568   37.678  1.00 40.67 ?  255 ARG D CD    1 
ATOM   4200 N NE    . ARG B 1 263 ? 31.880  0.039   39.017  1.00 49.45 ?  255 ARG D NE    1 
ATOM   4201 C CZ    . ARG B 1 263 ? 31.018  -0.727  39.673  1.00 56.51 ?  255 ARG D CZ    1 
ATOM   4202 N NH1   . ARG B 1 263 ? 29.852  -1.063  39.145  1.00 50.48 ?  255 ARG D NH1   1 
ATOM   4203 N NH2   . ARG B 1 263 ? 31.332  -1.164  40.890  1.00 60.00 ?  255 ARG D NH2   1 
ATOM   4204 N N     . ARG B 1 264 ? 36.258  -0.095  34.426  1.00 28.24 ?  256 ARG D N     1 
ATOM   4205 C CA    . ARG B 1 264 ? 37.675  0.073   34.123  1.00 37.96 ?  256 ARG D CA    1 
ATOM   4206 C C     . ARG B 1 264 ? 37.877  0.810   32.805  1.00 37.28 ?  256 ARG D C     1 
ATOM   4207 O O     . ARG B 1 264 ? 38.781  1.646   32.688  1.00 41.27 ?  256 ARG D O     1 
ATOM   4208 C CB    . ARG B 1 264 ? 38.368  -1.290  34.083  1.00 41.09 ?  256 ARG D CB    1 
ATOM   4209 C CG    . ARG B 1 264 ? 38.502  -1.975  35.433  1.00 39.42 ?  256 ARG D CG    1 
ATOM   4210 C CD    . ARG B 1 264 ? 39.944  -2.358  35.706  1.00 45.79 ?  256 ARG D CD    1 
ATOM   4211 N NE    . ARG B 1 264 ? 40.567  -2.990  34.549  1.00 46.15 ?  256 ARG D NE    1 
ATOM   4212 C CZ    . ARG B 1 264 ? 41.850  -2.878  34.235  1.00 43.57 ?  256 ARG D CZ    1 
ATOM   4213 N NH1   . ARG B 1 264 ? 42.681  -2.158  34.970  1.00 49.46 ?  256 ARG D NH1   1 
ATOM   4214 N NH2   . ARG B 1 264 ? 42.311  -3.502  33.155  1.00 46.34 ?  256 ARG D NH2   1 
ATOM   4215 N N     . VAL B 1 265 ? 37.045  0.519   31.803  1.00 29.51 ?  257 VAL D N     1 
ATOM   4216 C CA    . VAL B 1 265 ? 37.209  1.151   30.497  1.00 32.57 ?  257 VAL D CA    1 
ATOM   4217 C C     . VAL B 1 265 ? 36.831  2.626   30.564  1.00 33.89 ?  257 VAL D C     1 
ATOM   4218 O O     . VAL B 1 265 ? 37.480  3.476   29.940  1.00 34.87 ?  257 VAL D O     1 
ATOM   4219 C CB    . VAL B 1 265 ? 36.391  0.397   29.431  1.00 35.01 ?  257 VAL D CB    1 
ATOM   4220 C CG1   . VAL B 1 265 ? 36.251  1.230   28.163  1.00 26.45 ?  257 VAL D CG1   1 
ATOM   4221 C CG2   . VAL B 1 265 ? 37.042  -0.942  29.118  1.00 32.62 ?  257 VAL D CG2   1 
ATOM   4222 N N     . ALA B 1 266 ? 35.786  2.956   31.326  1.00 32.02 ?  258 ALA D N     1 
ATOM   4223 C CA    . ALA B 1 266 ? 35.390  4.354   31.461  1.00 33.75 ?  258 ALA D CA    1 
ATOM   4224 C C     . ALA B 1 266 ? 36.461  5.163   32.183  1.00 36.56 ?  258 ALA D C     1 
ATOM   4225 O O     . ALA B 1 266 ? 36.759  6.299   31.794  1.00 33.63 ?  258 ALA D O     1 
ATOM   4226 C CB    . ALA B 1 266 ? 34.053  4.452   32.197  1.00 30.10 ?  258 ALA D CB    1 
ATOM   4227 N N     . LYS B 1 267 ? 37.060  4.590   33.228  1.00 38.56 ?  259 LYS D N     1 
ATOM   4228 C CA    . LYS B 1 267 ? 38.037  5.330   34.019  1.00 34.67 ?  259 LYS D CA    1 
ATOM   4229 C C     . LYS B 1 267 ? 39.401  5.389   33.340  1.00 36.30 ?  259 LYS D C     1 
ATOM   4230 O O     . LYS B 1 267 ? 40.064  6.432   33.371  1.00 38.33 ?  259 LYS D O     1 
ATOM   4231 C CB    . LYS B 1 267 ? 38.174  4.704   35.406  1.00 36.74 ?  259 LYS D CB    1 
ATOM   4232 C CG    . LYS B 1 267 ? 36.993  4.945   36.324  1.00 37.36 ?  259 LYS D CG    1 
ATOM   4233 C CD    . LYS B 1 267 ? 37.245  4.326   37.691  1.00 39.56 ?  259 LYS D CD    1 
ATOM   4234 C CE    . LYS B 1 267 ? 36.052  4.501   38.615  1.00 38.96 ?  259 LYS D CE    1 
ATOM   4235 N NZ    . LYS B 1 267 ? 34.840  3.793   38.118  1.00 43.99 ?  259 LYS D NZ    1 
ATOM   4236 N N     . GLU B 1 268 ? 39.838  4.288   32.728  1.00 35.91 ?  260 GLU D N     1 
ATOM   4237 C CA    . GLU B 1 268 ? 41.196  4.195   32.206  1.00 41.26 ?  260 GLU D CA    1 
ATOM   4238 C C     . GLU B 1 268 ? 41.318  4.530   30.727  1.00 41.18 ?  260 GLU D C     1 
ATOM   4239 O O     . GLU B 1 268 ? 42.426  4.835   30.272  1.00 36.88 ?  260 GLU D O     1 
ATOM   4240 C CB    . GLU B 1 268 ? 41.760  2.789   32.445  1.00 32.92 ?  260 GLU D CB    1 
ATOM   4241 C CG    . GLU B 1 268 ? 41.772  2.380   33.903  1.00 36.00 ?  260 GLU D CG    1 
ATOM   4242 C CD    . GLU B 1 268 ? 42.198  0.943   34.101  1.00 42.14 ?  260 GLU D CD    1 
ATOM   4243 O OE1   . GLU B 1 268 ? 43.228  0.536   33.521  1.00 40.08 ?  260 GLU D OE1   1 
ATOM   4244 O OE2   . GLU B 1 268 ? 41.505  0.220   34.845  1.00 49.25 ?  260 GLU D OE2   1 
ATOM   4245 N N     . GLU B 1 269 ? 40.226  4.477   29.964  1.00 37.04 ?  261 GLU D N     1 
ATOM   4246 C CA    . GLU B 1 269 ? 40.268  4.814   28.549  1.00 39.09 ?  261 GLU D CA    1 
ATOM   4247 C C     . GLU B 1 269 ? 39.380  5.989   28.170  1.00 34.24 ?  261 GLU D C     1 
ATOM   4248 O O     . GLU B 1 269 ? 39.492  6.483   27.041  1.00 29.90 ?  261 GLU D O     1 
ATOM   4249 C CB    . GLU B 1 269 ? 39.873  3.600   27.691  1.00 32.49 ?  261 GLU D CB    1 
ATOM   4250 C CG    . GLU B 1 269 ? 40.424  2.275   28.190  1.00 33.64 ?  261 GLU D CG    1 
ATOM   4251 C CD    . GLU B 1 269 ? 41.736  1.904   27.525  1.00 33.45 ?  261 GLU D CD    1 
ATOM   4252 O OE1   . GLU B 1 269 ? 42.110  2.559   26.529  1.00 36.61 ?  261 GLU D OE1   1 
ATOM   4253 O OE2   . GLU B 1 269 ? 42.395  0.954   27.997  1.00 34.95 ?  261 GLU D OE2   1 
ATOM   4254 N N     . GLY B 1 270 ? 38.513  6.453   29.067  1.00 32.08 ?  262 GLY D N     1 
ATOM   4255 C CA    . GLY B 1 270 ? 37.601  7.524   28.722  1.00 32.55 ?  262 GLY D CA    1 
ATOM   4256 C C     . GLY B 1 270 ? 36.461  7.111   27.823  1.00 31.51 ?  262 GLY D C     1 
ATOM   4257 O O     . GLY B 1 270 ? 35.812  7.974   27.227  1.00 34.17 ?  262 GLY D O     1 
ATOM   4258 N N     . ILE B 1 271 ? 36.196  5.814   27.707  1.00 32.65 ?  263 ILE D N     1 
ATOM   4259 C CA    . ILE B 1 271 ? 35.127  5.289   26.865  1.00 29.85 ?  263 ILE D CA    1 
ATOM   4260 C C     . ILE B 1 271 ? 34.019  4.798   27.786  1.00 30.13 ?  263 ILE D C     1 
ATOM   4261 O O     . ILE B 1 271 ? 34.146  3.743   28.420  1.00 32.10 ?  263 ILE D O     1 
ATOM   4262 C CB    . ILE B 1 271 ? 35.627  4.167   25.945  1.00 27.53 ?  263 ILE D CB    1 
ATOM   4263 C CG1   . ILE B 1 271 ? 36.730  4.691   25.024  1.00 24.00 ?  263 ILE D CG1   1 
ATOM   4264 C CG2   . ILE B 1 271 ? 34.480  3.589   25.132  1.00 28.05 ?  263 ILE D CG2   1 
ATOM   4265 C CD1   . ILE B 1 271 ? 37.413  3.609   24.226  1.00 26.76 ?  263 ILE D CD1   1 
ATOM   4266 N N     . LEU B 1 272 ? 32.932  5.563   27.862  1.00 27.41 ?  264 LEU D N     1 
ATOM   4267 C CA    . LEU B 1 272 ? 31.810  5.261   28.742  1.00 30.17 ?  264 LEU D CA    1 
ATOM   4268 C C     . LEU B 1 272 ? 30.749  4.519   27.937  1.00 30.95 ?  264 LEU D C     1 
ATOM   4269 O O     . LEU B 1 272 ? 30.049  5.122   27.115  1.00 28.24 ?  264 LEU D O     1 
ATOM   4270 C CB    . LEU B 1 272 ? 31.242  6.541   29.347  1.00 30.61 ?  264 LEU D CB    1 
ATOM   4271 C CG    . LEU B 1 272 ? 30.012  6.366   30.233  1.00 35.83 ?  264 LEU D CG    1 
ATOM   4272 C CD1   . LEU B 1 272 ? 30.410  5.829   31.599  1.00 25.47 ?  264 LEU D CD1   1 
ATOM   4273 C CD2   . LEU B 1 272 ? 29.269  7.678   30.353  1.00 30.24 ?  264 LEU D CD2   1 
ATOM   4274 N N     . ALA B 1 273 ? 30.620  3.219   28.181  1.00 31.69 ?  265 ALA D N     1 
ATOM   4275 C CA    . ALA B 1 273 ? 29.737  2.370   27.399  1.00 30.27 ?  265 ALA D CA    1 
ATOM   4276 C C     . ALA B 1 273 ? 28.906  1.487   28.323  1.00 30.83 ?  265 ALA D C     1 
ATOM   4277 O O     . ALA B 1 273 ? 29.149  1.402   29.530  1.00 30.46 ?  265 ALA D O     1 
ATOM   4278 C CB    . ALA B 1 273 ? 30.533  1.521   26.403  1.00 26.29 ?  265 ALA D CB    1 
ATOM   4279 N N     . GLY B 1 274 ? 27.915  0.825   27.735  1.00 32.72 ?  266 GLY D N     1 
ATOM   4280 C CA    . GLY B 1 274 ? 26.994  0.001   28.487  1.00 26.53 ?  266 GLY D CA    1 
ATOM   4281 C C     . GLY B 1 274 ? 27.640  -1.261  29.034  1.00 34.82 ?  266 GLY D C     1 
ATOM   4282 O O     . GLY B 1 274 ? 28.836  -1.516  28.886  1.00 32.06 ?  266 GLY D O     1 
ATOM   4283 N N     . ILE B 1 275 ? 26.805  -2.075  29.686  1.00 31.83 ?  267 ILE D N     1 
ATOM   4284 C CA    . ILE B 1 275 ? 27.305  -3.289  30.322  1.00 35.42 ?  267 ILE D CA    1 
ATOM   4285 C C     . ILE B 1 275 ? 27.661  -4.338  29.275  1.00 33.27 ?  267 ILE D C     1 
ATOM   4286 O O     . ILE B 1 275 ? 28.657  -5.059  29.415  1.00 30.23 ?  267 ILE D O     1 
ATOM   4287 C CB    . ILE B 1 275 ? 26.281  -3.820  31.344  1.00 34.80 ?  267 ILE D CB    1 
ATOM   4288 C CG1   . ILE B 1 275 ? 26.755  -5.149  31.937  1.00 43.09 ?  267 ILE D CG1   1 
ATOM   4289 C CG2   . ILE B 1 275 ? 24.903  -3.964  30.712  1.00 40.50 ?  267 ILE D CG2   1 
ATOM   4290 C CD1   . ILE B 1 275 ? 26.449  -5.310  33.412  1.00 43.59 ?  267 ILE D CD1   1 
ATOM   4291 N N     . SER B 1 276 ? 26.868  -4.434  28.203  1.00 31.92 ?  268 SER D N     1 
ATOM   4292 C CA    . SER B 1 276 ? 27.182  -5.382  27.139  1.00 27.79 ?  268 SER D CA    1 
ATOM   4293 C C     . SER B 1 276 ? 28.497  -5.033  26.453  1.00 31.00 ?  268 SER D C     1 
ATOM   4294 O O     . SER B 1 276 ? 29.177  -5.921  25.928  1.00 30.09 ?  268 SER D O     1 
ATOM   4295 C CB    . SER B 1 276 ? 26.044  -5.427  26.118  1.00 32.04 ?  268 SER D CB    1 
ATOM   4296 O OG    . SER B 1 276 ? 26.017  -4.248  25.333  1.00 32.78 ?  268 SER D OG    1 
ATOM   4297 N N     . SER B 1 277 ? 28.868  -3.750  26.444  1.00 28.87 ?  269 SER D N     1 
ATOM   4298 C CA    . SER B 1 277 ? 30.176  -3.366  25.926  1.00 28.41 ?  269 SER D CA    1 
ATOM   4299 C C     . SER B 1 277 ? 31.285  -3.826  26.861  1.00 29.36 ?  269 SER D C     1 
ATOM   4300 O O     . SER B 1 277 ? 32.374  -4.202  26.409  1.00 26.18 ?  269 SER D O     1 
ATOM   4301 C CB    . SER B 1 277 ? 30.242  -1.854  25.727  1.00 27.16 ?  269 SER D CB    1 
ATOM   4302 O OG    . SER B 1 277 ? 29.138  -1.379  24.979  1.00 27.77 ?  269 SER D OG    1 
ATOM   4303 N N     . GLY B 1 278 ? 31.030  -3.790  28.170  1.00 25.53 ?  270 GLY D N     1 
ATOM   4304 C CA    . GLY B 1 278 ? 31.979  -4.357  29.112  1.00 33.60 ?  270 GLY D CA    1 
ATOM   4305 C C     . GLY B 1 278 ? 32.117  -5.857  28.949  1.00 34.07 ?  270 GLY D C     1 
ATOM   4306 O O     . GLY B 1 278 ? 33.213  -6.407  29.084  1.00 34.96 ?  270 GLY D O     1 
ATOM   4307 N N     . ALA B 1 279 ? 31.009  -6.540  28.656  1.00 30.46 ?  271 ALA D N     1 
ATOM   4308 C CA    . ALA B 1 279 ? 31.082  -7.961  28.336  1.00 32.51 ?  271 ALA D CA    1 
ATOM   4309 C C     . ALA B 1 279 ? 31.868  -8.184  27.052  1.00 33.62 ?  271 ALA D C     1 
ATOM   4310 O O     . ALA B 1 279 ? 32.689  -9.104  26.962  1.00 34.10 ?  271 ALA D O     1 
ATOM   4311 C CB    . ALA B 1 279 ? 29.674  -8.546  28.220  1.00 31.29 ?  271 ALA D CB    1 
ATOM   4312 N N     . ALA B 1 280 ? 31.635  -7.338  26.047  1.00 33.22 ?  272 ALA D N     1 
ATOM   4313 C CA    . ALA B 1 280 ? 32.346  -7.476  24.780  1.00 30.29 ?  272 ALA D CA    1 
ATOM   4314 C C     . ALA B 1 280 ? 33.835  -7.209  24.957  1.00 33.46 ?  272 ALA D C     1 
ATOM   4315 O O     . ALA B 1 280 ? 34.677  -7.945  24.430  1.00 31.00 ?  272 ALA D O     1 
ATOM   4316 C CB    . ALA B 1 280 ? 31.744  -6.534  23.737  1.00 28.29 ?  272 ALA D CB    1 
ATOM   4317 N N     . ILE B 1 281 ? 34.179  -6.159  25.706  1.00 31.08 ?  273 ILE D N     1 
ATOM   4318 C CA    . ILE B 1 281 ? 35.584  -5.811  25.891  1.00 30.08 ?  273 ILE D CA    1 
ATOM   4319 C C     . ILE B 1 281 ? 36.293  -6.864  26.735  1.00 34.29 ?  273 ILE D C     1 
ATOM   4320 O O     . ILE B 1 281 ? 37.440  -7.233  26.455  1.00 30.73 ?  273 ILE D O     1 
ATOM   4321 C CB    . ILE B 1 281 ? 35.708  -4.403  26.502  1.00 28.80 ?  273 ILE D CB    1 
ATOM   4322 C CG1   . ILE B 1 281 ? 35.427  -3.343  25.435  1.00 27.49 ?  273 ILE D CG1   1 
ATOM   4323 C CG2   . ILE B 1 281 ? 37.091  -4.189  27.104  1.00 34.69 ?  273 ILE D CG2   1 
ATOM   4324 C CD1   . ILE B 1 281 ? 35.587  -1.921  25.918  1.00 28.28 ?  273 ILE D CD1   1 
ATOM   4325 N N     . TYR B 1 282 ? 35.621  -7.375  27.771  1.00 37.42 ?  274 TYR D N     1 
ATOM   4326 C CA    . TYR B 1 282 ? 36.217  -8.424  28.595  1.00 32.18 ?  274 TYR D CA    1 
ATOM   4327 C C     . TYR B 1 282 ? 36.513  -9.670  27.772  1.00 38.28 ?  274 TYR D C     1 
ATOM   4328 O O     . TYR B 1 282 ? 37.574  -10.288 27.925  1.00 40.61 ?  274 TYR D O     1 
ATOM   4329 C CB    . TYR B 1 282 ? 35.294  -8.767  29.764  1.00 36.15 ?  274 TYR D CB    1 
ATOM   4330 C CG    . TYR B 1 282 ? 35.824  -9.868  30.655  1.00 38.82 ?  274 TYR D CG    1 
ATOM   4331 C CD1   . TYR B 1 282 ? 36.712  -9.586  31.684  1.00 37.99 ?  274 TYR D CD1   1 
ATOM   4332 C CD2   . TYR B 1 282 ? 35.436  -11.191 30.470  1.00 40.86 ?  274 TYR D CD2   1 
ATOM   4333 C CE1   . TYR B 1 282 ? 37.201  -10.585 32.501  1.00 40.38 ?  274 TYR D CE1   1 
ATOM   4334 C CE2   . TYR B 1 282 ? 35.922  -12.199 31.283  1.00 45.92 ?  274 TYR D CE2   1 
ATOM   4335 C CZ    . TYR B 1 282 ? 36.804  -11.889 32.297  1.00 41.29 ?  274 TYR D CZ    1 
ATOM   4336 O OH    . TYR B 1 282 ? 37.292  -12.883 33.112  1.00 55.12 ?  274 TYR D OH    1 
ATOM   4337 N N     . ALA B 1 283 ? 35.582  -10.059 26.899  1.00 33.35 ?  275 ALA D N     1 
ATOM   4338 C CA    . ALA B 1 283 ? 35.807  -11.223 26.049  1.00 39.22 ?  275 ALA D CA    1 
ATOM   4339 C C     . ALA B 1 283 ? 36.899  -10.953 25.023  1.00 32.74 ?  275 ALA D C     1 
ATOM   4340 O O     . ALA B 1 283 ? 37.692  -11.846 24.703  1.00 36.59 ?  275 ALA D O     1 
ATOM   4341 C CB    . ALA B 1 283 ? 34.507  -11.625 25.356  1.00 33.09 ?  275 ALA D CB    1 
ATOM   4342 N N     . ALA B 1 284 ? 36.956  -9.727  24.495  1.00 33.52 ?  276 ALA D N     1 
ATOM   4343 C CA    . ALA B 1 284 ? 37.977  -9.395  23.508  1.00 36.48 ?  276 ALA D CA    1 
ATOM   4344 C C     . ALA B 1 284 ? 39.373  -9.402  24.117  1.00 34.02 ?  276 ALA D C     1 
ATOM   4345 O O     . ALA B 1 284 ? 40.343  -9.739  23.430  1.00 35.26 ?  276 ALA D O     1 
ATOM   4346 C CB    . ALA B 1 284 ? 37.680  -8.034  22.878  1.00 32.64 ?  276 ALA D CB    1 
ATOM   4347 N N     . ILE B 1 285 ? 39.498  -9.034  25.394  1.00 33.33 ?  277 ILE D N     1 
ATOM   4348 C CA    . ILE B 1 285 ? 40.803  -9.058  26.046  1.00 35.66 ?  277 ILE D CA    1 
ATOM   4349 C C     . ILE B 1 285 ? 41.232  -10.492 26.326  1.00 36.67 ?  277 ILE D C     1 
ATOM   4350 O O     . ILE B 1 285 ? 42.402  -10.850 26.147  1.00 34.68 ?  277 ILE D O     1 
ATOM   4351 C CB    . ILE B 1 285 ? 40.772  -8.207  27.330  1.00 35.92 ?  277 ILE D CB    1 
ATOM   4352 C CG1   . ILE B 1 285 ? 40.658  -6.723  26.978  1.00 35.06 ?  277 ILE D CG1   1 
ATOM   4353 C CG2   . ILE B 1 285 ? 42.010  -8.462  28.179  1.00 36.09 ?  277 ILE D CG2   1 
ATOM   4354 C CD1   . ILE B 1 285 ? 40.271  -5.849  28.146  1.00 28.66 ?  277 ILE D CD1   1 
ATOM   4355 N N     . GLN B 1 286 ? 40.293  -11.333 26.768  1.00 38.84 ?  278 GLN D N     1 
ATOM   4356 C CA    . GLN B 1 286 ? 40.581  -12.754 26.940  1.00 40.69 ?  278 GLN D CA    1 
ATOM   4357 C C     . GLN B 1 286 ? 41.080  -13.369 25.639  1.00 47.15 ?  278 GLN D C     1 
ATOM   4358 O O     . GLN B 1 286 ? 42.061  -14.124 25.629  1.00 44.33 ?  278 GLN D O     1 
ATOM   4359 C CB    . GLN B 1 286 ? 39.332  -13.483 27.435  1.00 42.31 ?  278 GLN D CB    1 
ATOM   4360 C CG    . GLN B 1 286 ? 39.577  -14.912 27.891  1.00 48.53 ?  278 GLN D CG    1 
ATOM   4361 C CD    . GLN B 1 286 ? 38.295  -15.714 28.009  1.00 48.26 ?  278 GLN D CD    1 
ATOM   4362 O OE1   . GLN B 1 286 ? 38.022  -16.592 27.191  1.00 47.90 ?  278 GLN D OE1   1 
ATOM   4363 N NE2   . GLN B 1 286 ? 37.501  -15.417 29.032  1.00 45.15 ?  278 GLN D NE2   1 
ATOM   4364 N N     . LYS B 1 287 ? 40.413  -13.052 24.526  1.00 41.28 ?  279 LYS D N     1 
ATOM   4365 C CA    . LYS B 1 287 ? 40.868  -13.528 23.225  1.00 32.12 ?  279 LYS D CA    1 
ATOM   4366 C C     . LYS B 1 287 ? 42.184  -12.877 22.820  1.00 40.27 ?  279 LYS D C     1 
ATOM   4367 O O     . LYS B 1 287 ? 43.019  -13.518 22.172  1.00 37.22 ?  279 LYS D O     1 
ATOM   4368 C CB    . LYS B 1 287 ? 39.793  -13.269 22.167  1.00 37.09 ?  279 LYS D CB    1 
ATOM   4369 C CG    . LYS B 1 287 ? 40.214  -13.596 20.740  1.00 34.73 ?  279 LYS D CG    1 
ATOM   4370 C CD    . LYS B 1 287 ? 40.486  -15.082 20.560  1.00 34.24 ?  279 LYS D CD    1 
ATOM   4371 C CE    . LYS B 1 287 ? 39.316  -15.930 21.037  1.00 40.96 ?  279 LYS D CE    1 
ATOM   4372 N NZ    . LYS B 1 287 ? 39.459  -17.351 20.617  1.00 46.39 ?  279 LYS D NZ    1 
ATOM   4373 N N     . ALA B 1 288 ? 42.391  -11.613 23.195  1.00 36.90 ?  280 ALA D N     1 
ATOM   4374 C CA    . ALA B 1 288 ? 43.646  -10.940 22.875  1.00 41.13 ?  280 ALA D CA    1 
ATOM   4375 C C     . ALA B 1 288 ? 44.816  -11.579 23.612  1.00 43.63 ?  280 ALA D C     1 
ATOM   4376 O O     . ALA B 1 288 ? 45.882  -11.803 23.027  1.00 46.17 ?  280 ALA D O     1 
ATOM   4377 C CB    . ALA B 1 288 ? 43.547  -9.453  23.208  1.00 39.27 ?  280 ALA D CB    1 
ATOM   4378 N N     . LYS B 1 289 ? 44.637  -11.870 24.905  1.00 41.03 ?  281 LYS D N     1 
ATOM   4379 C CA    . LYS B 1 289 ? 45.666  -12.581 25.658  1.00 39.98 ?  281 LYS D CA    1 
ATOM   4380 C C     . LYS B 1 289 ? 45.976  -13.928 25.019  1.00 44.49 ?  281 LYS D C     1 
ATOM   4381 O O     . LYS B 1 289 ? 47.126  -14.382 25.025  1.00 44.62 ?  281 LYS D O     1 
ATOM   4382 C CB    . LYS B 1 289 ? 45.219  -12.777 27.108  1.00 35.24 ?  281 LYS D CB    1 
ATOM   4383 C CG    . LYS B 1 289 ? 45.064  -11.497 27.912  1.00 41.19 ?  281 LYS D CG    1 
ATOM   4384 C CD    . LYS B 1 289 ? 44.711  -11.814 29.358  1.00 34.99 ?  281 LYS D CD    1 
ATOM   4385 C CE    . LYS B 1 289 ? 44.858  -10.595 30.253  1.00 44.09 ?  281 LYS D CE    1 
ATOM   4386 N NZ    . LYS B 1 289 ? 43.923  -10.647 31.414  1.00 43.33 ?  281 LYS D NZ    1 
ATOM   4387 N N     . GLU B 1 290 ? 44.956  -14.578 24.456  1.00 43.59 ?  282 GLU D N     1 
ATOM   4388 C CA    . GLU B 1 290 ? 45.147  -15.881 23.831  1.00 43.40 ?  282 GLU D CA    1 
ATOM   4389 C C     . GLU B 1 290 ? 46.003  -15.776 22.574  1.00 45.38 ?  282 GLU D C     1 
ATOM   4390 O O     . GLU B 1 290 ? 46.826  -16.658 22.302  1.00 49.68 ?  282 GLU D O     1 
ATOM   4391 C CB    . GLU B 1 290 ? 43.785  -16.497 23.511  1.00 44.41 ?  282 GLU D CB    1 
ATOM   4392 C CG    . GLU B 1 290 ? 43.834  -17.768 22.689  1.00 44.52 ?  282 GLU D CG    1 
ATOM   4393 C CD    . GLU B 1 290 ? 42.466  -18.401 22.532  1.00 53.32 ?  282 GLU D CD    1 
ATOM   4394 O OE1   . GLU B 1 290 ? 41.652  -18.302 23.475  1.00 49.13 ?  282 GLU D OE1   1 
ATOM   4395 O OE2   . GLU B 1 290 ? 42.202  -18.993 21.465  1.00 51.82 ?  282 GLU D OE2   1 
ATOM   4396 N N     . LEU B 1 291 ? 45.829  -14.704 21.800  1.00 45.49 ?  283 LEU D N     1 
ATOM   4397 C CA    . LEU B 1 291 ? 46.547  -14.548 20.540  1.00 47.47 ?  283 LEU D CA    1 
ATOM   4398 C C     . LEU B 1 291 ? 47.922  -13.918 20.711  1.00 47.47 ?  283 LEU D C     1 
ATOM   4399 O O     . LEU B 1 291 ? 48.836  -14.231 19.939  1.00 50.31 ?  283 LEU D O     1 
ATOM   4400 C CB    . LEU B 1 291 ? 45.718  -13.711 19.562  1.00 42.53 ?  283 LEU D CB    1 
ATOM   4401 C CG    . LEU B 1 291 ? 44.348  -14.292 19.206  1.00 47.07 ?  283 LEU D CG    1 
ATOM   4402 C CD1   . LEU B 1 291 ? 43.652  -13.446 18.149  1.00 42.20 ?  283 LEU D CD1   1 
ATOM   4403 C CD2   . LEU B 1 291 ? 44.483  -15.735 18.744  1.00 38.53 ?  283 LEU D CD2   1 
ATOM   4404 N N     . GLY B 1 292 ? 48.090  -13.034 21.691  1.00 48.39 ?  284 GLY D N     1 
ATOM   4405 C CA    . GLY B 1 292 ? 49.384  -12.456 21.985  1.00 41.95 ?  284 GLY D CA    1 
ATOM   4406 C C     . GLY B 1 292 ? 49.715  -11.251 21.122  1.00 48.66 ?  284 GLY D C     1 
ATOM   4407 O O     . GLY B 1 292 ? 49.022  -10.910 20.162  1.00 47.00 ?  284 GLY D O     1 
ATOM   4408 N N     . LYS B 1 293 ? 50.821  -10.599 21.488  1.00 47.64 ?  285 LYS D N     1 
ATOM   4409 C CA    . LYS B 1 293 ? 51.299  -9.410  20.792  1.00 47.77 ?  285 LYS D CA    1 
ATOM   4410 C C     . LYS B 1 293 ? 51.437  -9.663  19.296  1.00 51.13 ?  285 LYS D C     1 
ATOM   4411 O O     . LYS B 1 293 ? 51.838  -10.747 18.865  1.00 50.44 ?  285 LYS D O     1 
ATOM   4412 C CB    . LYS B 1 293 ? 52.648  -8.984  21.378  1.00 51.50 ?  285 LYS D CB    1 
ATOM   4413 C CG    . LYS B 1 293 ? 53.109  -7.580  21.026  1.00 54.61 ?  285 LYS D CG    1 
ATOM   4414 C CD    . LYS B 1 293 ? 54.603  -7.582  20.730  1.00 59.91 ?  285 LYS D CD    1 
ATOM   4415 C CE    . LYS B 1 293 ? 55.331  -6.488  21.496  1.00 61.55 ?  285 LYS D CE    1 
ATOM   4416 N NZ    . LYS B 1 293 ? 54.730  -5.140  21.292  1.00 60.07 ?  285 LYS D NZ    1 
ATOM   4417 N N     . GLY B 1 294 ? 51.096  -8.647  18.505  1.00 50.57 ?  286 GLY D N     1 
ATOM   4418 C CA    . GLY B 1 294 ? 51.188  -8.723  17.064  1.00 47.94 ?  286 GLY D CA    1 
ATOM   4419 C C     . GLY B 1 294 ? 49.887  -9.035  16.355  1.00 46.07 ?  286 GLY D C     1 
ATOM   4420 O O     . GLY B 1 294 ? 49.810  -8.849  15.135  1.00 41.56 ?  286 GLY D O     1 
ATOM   4421 N N     . LYS B 1 295 ? 48.870  -9.504  17.071  1.00 43.65 ?  287 LYS D N     1 
ATOM   4422 C CA    . LYS B 1 295 ? 47.585  -9.837  16.476  1.00 43.50 ?  287 LYS D CA    1 
ATOM   4423 C C     . LYS B 1 295 ? 46.595  -8.689  16.662  1.00 42.49 ?  287 LYS D C     1 
ATOM   4424 O O     . LYS B 1 295 ? 46.848  -7.727  17.391  1.00 43.19 ?  287 LYS D O     1 
ATOM   4425 C CB    . LYS B 1 295 ? 47.036  -11.135 17.077  1.00 49.50 ?  287 LYS D CB    1 
ATOM   4426 N N     . THR B 1 296 ? 45.452  -8.800  15.986  1.00 40.07 ?  288 THR D N     1 
ATOM   4427 C CA    . THR B 1 296 ? 44.454  -7.737  15.957  1.00 40.92 ?  288 THR D CA    1 
ATOM   4428 C C     . THR B 1 296 ? 43.083  -8.303  16.300  1.00 42.88 ?  288 THR D C     1 
ATOM   4429 O O     . THR B 1 296 ? 42.628  -9.263  15.671  1.00 39.18 ?  288 THR D O     1 
ATOM   4430 C CB    . THR B 1 296 ? 44.414  -7.055  14.585  1.00 39.97 ?  288 THR D CB    1 
ATOM   4431 O OG1   . THR B 1 296 ? 45.646  -6.354  14.362  1.00 39.09 ?  288 THR D OG1   1 
ATOM   4432 C CG2   . THR B 1 296 ? 43.259  -6.068  14.510  1.00 37.77 ?  288 THR D CG2   1 
ATOM   4433 N N     . VAL B 1 297 ? 42.426  -7.694  17.287  1.00 35.16 ?  289 VAL D N     1 
ATOM   4434 C CA    . VAL B 1 297 ? 41.128  -8.137  17.785  1.00 38.31 ?  289 VAL D CA    1 
ATOM   4435 C C     . VAL B 1 297 ? 40.157  -6.963  17.743  1.00 36.02 ?  289 VAL D C     1 
ATOM   4436 O O     . VAL B 1 297 ? 40.504  -5.846  18.141  1.00 34.96 ?  289 VAL D O     1 
ATOM   4437 C CB    . VAL B 1 297 ? 41.247  -8.704  19.216  1.00 44.14 ?  289 VAL D CB    1 
ATOM   4438 C CG1   . VAL B 1 297 ? 39.880  -8.932  19.819  1.00 38.25 ?  289 VAL D CG1   1 
ATOM   4439 C CG2   . VAL B 1 297 ? 42.047  -9.998  19.208  1.00 39.25 ?  289 VAL D CG2   1 
ATOM   4440 N N     . VAL B 1 298 ? 38.941  -7.214  17.257  1.00 30.52 ?  290 VAL D N     1 
ATOM   4441 C CA    . VAL B 1 298 ? 37.936  -6.174  17.064  1.00 32.87 ?  290 VAL D CA    1 
ATOM   4442 C C     . VAL B 1 298 ? 36.621  -6.618  17.693  1.00 36.17 ?  290 VAL D C     1 
ATOM   4443 O O     . VAL B 1 298 ? 36.221  -7.781  17.566  1.00 32.68 ?  290 VAL D O     1 
ATOM   4444 C CB    . VAL B 1 298 ? 37.732  -5.851  15.567  1.00 33.69 ?  290 VAL D CB    1 
ATOM   4445 C CG1   . VAL B 1 298 ? 36.694  -4.752  15.389  1.00 35.87 ?  290 VAL D CG1   1 
ATOM   4446 C CG2   . VAL B 1 298 ? 39.050  -5.458  14.918  1.00 33.66 ?  290 VAL D CG2   1 
ATOM   4447 N N     . THR B 1 299 ? 35.945  -5.687  18.367  1.00 33.81 ?  291 THR D N     1 
ATOM   4448 C CA    . THR B 1 299 ? 34.616  -5.930  18.911  1.00 32.78 ?  291 THR D CA    1 
ATOM   4449 C C     . THR B 1 299 ? 33.787  -4.656  18.782  1.00 30.89 ?  291 THR D C     1 
ATOM   4450 O O     . THR B 1 299 ? 34.258  -3.629  18.283  1.00 31.14 ?  291 THR D O     1 
ATOM   4451 C CB    . THR B 1 299 ? 34.681  -6.413  20.365  1.00 31.33 ?  291 THR D CB    1 
ATOM   4452 O OG1   . THR B 1 299 ? 33.419  -6.985  20.731  1.00 32.79 ?  291 THR D OG1   1 
ATOM   4453 C CG2   . THR B 1 299 ? 35.008  -5.261  21.305  1.00 24.50 ?  291 THR D CG2   1 
ATOM   4454 N N     . VAL B 1 300 ? 32.538  -4.727  19.237  1.00 32.33 ?  292 VAL D N     1 
ATOM   4455 C CA    . VAL B 1 300 ? 31.564  -3.658  19.050  1.00 32.72 ?  292 VAL D CA    1 
ATOM   4456 C C     . VAL B 1 300 ? 31.000  -3.258  20.406  1.00 31.46 ?  292 VAL D C     1 
ATOM   4457 O O     . VAL B 1 300 ? 30.637  -4.122  21.212  1.00 29.51 ?  292 VAL D O     1 
ATOM   4458 C CB    . VAL B 1 300 ? 30.431  -4.091  18.098  1.00 36.52 ?  292 VAL D CB    1 
ATOM   4459 C CG1   . VAL B 1 300 ? 29.275  -3.110  18.160  1.00 31.33 ?  292 VAL D CG1   1 
ATOM   4460 C CG2   . VAL B 1 300 ? 30.955  -4.215  16.676  1.00 31.79 ?  292 VAL D CG2   1 
ATOM   4461 N N     . LEU B 1 301 ? 30.928  -1.946  20.657  1.00 29.60 ?  293 LEU D N     1 
ATOM   4462 C CA    . LEU B 1 301 ? 30.299  -1.419  21.860  1.00 28.70 ?  293 LEU D CA    1 
ATOM   4463 C C     . LEU B 1 301 ? 28.923  -0.877  21.493  1.00 27.49 ?  293 LEU D C     1 
ATOM   4464 O O     . LEU B 1 301 ? 28.827  0.209   20.899  1.00 25.44 ?  293 LEU D O     1 
ATOM   4465 C CB    . LEU B 1 301 ? 31.162  -0.327  22.496  1.00 27.58 ?  293 LEU D CB    1 
ATOM   4466 C CG    . LEU B 1 301 ? 32.673  -0.566  22.525  1.00 30.86 ?  293 LEU D CG    1 
ATOM   4467 C CD1   . LEU B 1 301 ? 33.379  0.561   23.261  1.00 28.46 ?  293 LEU D CD1   1 
ATOM   4468 C CD2   . LEU B 1 301 ? 32.997  -1.906  23.167  1.00 26.29 ?  293 LEU D CD2   1 
ATOM   4469 N N     . PRO B 1 302 ? 27.834  -1.580  21.821  1.00 26.94 ?  294 PRO D N     1 
ATOM   4470 C CA    . PRO B 1 302 ? 26.532  -1.223  21.235  1.00 28.24 ?  294 PRO D CA    1 
ATOM   4471 C C     . PRO B 1 302 ? 25.912  0.047   21.793  1.00 25.22 ?  294 PRO D C     1 
ATOM   4472 O O     . PRO B 1 302 ? 25.195  0.730   21.053  1.00 27.24 ?  294 PRO D O     1 
ATOM   4473 C CB    . PRO B 1 302 ? 25.663  -2.450  21.545  1.00 27.70 ?  294 PRO D CB    1 
ATOM   4474 C CG    . PRO B 1 302 ? 26.641  -3.555  21.802  1.00 27.50 ?  294 PRO D CG    1 
ATOM   4475 C CD    . PRO B 1 302 ? 27.786  -2.888  22.492  1.00 25.63 ?  294 PRO D CD    1 
ATOM   4476 N N     . SER B 1 303 ? 26.141  0.390   23.059  1.00 29.46 ?  295 SER D N     1 
ATOM   4477 C CA    . SER B 1 303 ? 25.432  1.514   23.654  1.00 28.52 ?  295 SER D CA    1 
ATOM   4478 C C     . SER B 1 303 ? 26.349  2.297   24.581  1.00 30.88 ?  295 SER D C     1 
ATOM   4479 O O     . SER B 1 303 ? 27.416  1.827   24.985  1.00 28.98 ?  295 SER D O     1 
ATOM   4480 C CB    . SER B 1 303 ? 24.188  1.047   24.420  1.00 28.43 ?  295 SER D CB    1 
ATOM   4481 O OG    . SER B 1 303 ? 24.515  0.022   25.341  1.00 26.60 ?  295 SER D OG    1 
ATOM   4482 N N     . ASN B 1 304 ? 25.907  3.506   24.918  1.00 30.34 ?  296 ASN D N     1 
ATOM   4483 C CA    . ASN B 1 304 ? 26.642  4.397   25.801  1.00 30.92 ?  296 ASN D CA    1 
ATOM   4484 C C     . ASN B 1 304 ? 26.245  4.163   27.254  1.00 31.07 ?  296 ASN D C     1 
ATOM   4485 O O     . ASN B 1 304 ? 25.095  3.837   27.560  1.00 30.88 ?  296 ASN D O     1 
ATOM   4486 C CB    . ASN B 1 304 ? 26.389  5.859   25.429  1.00 31.27 ?  296 ASN D CB    1 
ATOM   4487 C CG    . ASN B 1 304 ? 27.360  6.806   26.102  1.00 29.86 ?  296 ASN D CG    1 
ATOM   4488 O OD1   . ASN B 1 304 ? 27.201  7.145   27.275  1.00 29.82 ?  296 ASN D OD1   1 
ATOM   4489 N ND2   . ASN B 1 304 ? 28.373  7.242   25.362  1.00 28.91 ?  296 ASN D ND2   1 
ATOM   4490 N N     . GLY B 1 305 ? 27.216  4.346   28.152  1.00 31.53 ?  297 GLY D N     1 
ATOM   4491 C CA    . GLY B 1 305 ? 26.977  4.140   29.570  1.00 29.61 ?  297 GLY D CA    1 
ATOM   4492 C C     . GLY B 1 305 ? 26.043  5.155   30.194  1.00 29.76 ?  297 GLY D C     1 
ATOM   4493 O O     . GLY B 1 305 ? 25.509  4.903   31.279  1.00 31.19 ?  297 GLY D O     1 
ATOM   4494 N N     . GLU B 1 306 ? 25.835  6.296   29.535  1.00 27.38 ?  298 GLU D N     1 
ATOM   4495 C CA    . GLU B 1 306 ? 24.891  7.287   30.040  1.00 31.22 ?  298 GLU D CA    1 
ATOM   4496 C C     . GLU B 1 306 ? 23.461  6.760   30.025  1.00 34.03 ?  298 GLU D C     1 
ATOM   4497 O O     . GLU B 1 306 ? 22.626  7.212   30.817  1.00 34.65 ?  298 GLU D O     1 
ATOM   4498 C CB    . GLU B 1 306 ? 24.999  8.573   29.220  1.00 32.36 ?  298 GLU D CB    1 
ATOM   4499 C CG    . GLU B 1 306 ? 24.234  9.748   29.800  1.00 33.22 ?  298 GLU D CG    1 
ATOM   4500 C CD    . GLU B 1 306 ? 24.589  11.063  29.135  1.00 34.47 ?  298 GLU D CD    1 
ATOM   4501 O OE1   . GLU B 1 306 ? 25.622  11.118  28.432  1.00 34.59 ?  298 GLU D OE1   1 
ATOM   4502 O OE2   . GLU B 1 306 ? 23.834  12.041  29.316  1.00 25.85 ?  298 GLU D OE2   1 
ATOM   4503 N N     . ARG B 1 307 ? 23.161  5.806   29.141  1.00 28.96 ?  299 ARG D N     1 
ATOM   4504 C CA    . ARG B 1 307 ? 21.839  5.191   29.099  1.00 32.85 ?  299 ARG D CA    1 
ATOM   4505 C C     . ARG B 1 307 ? 21.572  4.291   30.301  1.00 35.60 ?  299 ARG D C     1 
ATOM   4506 O O     . ARG B 1 307 ? 20.433  3.848   30.486  1.00 36.17 ?  299 ARG D O     1 
ATOM   4507 C CB    . ARG B 1 307 ? 21.687  4.399   27.792  1.00 31.48 ?  299 ARG D CB    1 
ATOM   4508 C CG    . ARG B 1 307 ? 20.273  3.916   27.481  1.00 30.70 ?  299 ARG D CG    1 
ATOM   4509 C CD    . ARG B 1 307 ? 20.064  3.675   25.993  1.00 24.47 ?  299 ARG D CD    1 
ATOM   4510 N NE    . ARG B 1 307 ? 20.090  4.907   25.214  1.00 31.56 ?  299 ARG D NE    1 
ATOM   4511 C CZ    . ARG B 1 307 ? 20.099  4.957   23.888  1.00 29.71 ?  299 ARG D CZ    1 
ATOM   4512 N NH1   . ARG B 1 307 ? 20.088  3.856   23.154  1.00 23.59 ?  299 ARG D NH1   1 
ATOM   4513 N NH2   . ARG B 1 307 ? 20.113  6.142   23.284  1.00 27.32 ?  299 ARG D NH2   1 
ATOM   4514 N N     . TYR B 1 308 ? 22.576  4.030   31.129  1.00 39.41 ?  300 TYR D N     1 
ATOM   4515 C CA    . TYR B 1 308 ? 22.463  3.071   32.220  1.00 39.48 ?  300 TYR D CA    1 
ATOM   4516 C C     . TYR B 1 308 ? 22.907  3.691   33.535  1.00 38.77 ?  300 TYR D C     1 
ATOM   4517 O O     . TYR B 1 308 ? 23.521  3.032   34.377  1.00 45.82 ?  300 TYR D O     1 
ATOM   4518 C CB    . TYR B 1 308 ? 23.269  1.813   31.907  1.00 37.20 ?  300 TYR D CB    1 
ATOM   4519 C CG    . TYR B 1 308 ? 23.012  1.274   30.517  1.00 39.41 ?  300 TYR D CG    1 
ATOM   4520 C CD1   . TYR B 1 308 ? 21.892  0.499   30.248  1.00 45.66 ?  300 TYR D CD1   1 
ATOM   4521 C CD2   . TYR B 1 308 ? 23.876  1.561   29.468  1.00 38.40 ?  300 TYR D CD2   1 
ATOM   4522 C CE1   . TYR B 1 308 ? 21.646  0.011   28.975  1.00 45.90 ?  300 TYR D CE1   1 
ATOM   4523 C CE2   . TYR B 1 308 ? 23.638  1.078   28.189  1.00 37.85 ?  300 TYR D CE2   1 
ATOM   4524 C CZ    . TYR B 1 308 ? 22.521  0.303   27.949  1.00 37.27 ?  300 TYR D CZ    1 
ATOM   4525 O OH    . TYR B 1 308 ? 22.277  -0.182  26.683  1.00 35.68 ?  300 TYR D OH    1 
ATOM   4526 N N     . LEU B 1 309 ? 22.601  4.976   33.735  1.00 37.71 ?  301 LEU D N     1 
ATOM   4527 C CA    . LEU B 1 309 ? 23.004  5.648   34.966  1.00 43.83 ?  301 LEU D CA    1 
ATOM   4528 C C     . LEU B 1 309 ? 22.167  5.222   36.165  1.00 48.72 ?  301 LEU D C     1 
ATOM   4529 O O     . LEU B 1 309 ? 22.592  5.438   37.304  1.00 48.57 ?  301 LEU D O     1 
ATOM   4530 C CB    . LEU B 1 309 ? 22.929  7.166   34.791  1.00 37.24 ?  301 LEU D CB    1 
ATOM   4531 C CG    . LEU B 1 309 ? 23.879  7.765   33.755  1.00 38.49 ?  301 LEU D CG    1 
ATOM   4532 C CD1   . LEU B 1 309 ? 23.831  9.277   33.825  1.00 33.40 ?  301 LEU D CD1   1 
ATOM   4533 C CD2   . LEU B 1 309 ? 25.300  7.256   33.963  1.00 42.90 ?  301 LEU D CD2   1 
ATOM   4534 N N     . SER B 1 310 ? 21.001  4.620   35.940  1.00 45.26 ?  302 SER D N     1 
ATOM   4535 C CA    . SER B 1 310 ? 20.149  4.138   37.019  1.00 45.63 ?  302 SER D CA    1 
ATOM   4536 C C     . SER B 1 310 ? 20.238  2.631   37.228  1.00 48.37 ?  302 SER D C     1 
ATOM   4537 O O     . SER B 1 310 ? 19.554  2.102   38.110  1.00 53.91 ?  302 SER D O     1 
ATOM   4538 C CB    . SER B 1 310 ? 18.692  4.545   36.759  1.00 48.96 ?  302 SER D CB    1 
ATOM   4539 O OG    . SER B 1 310 ? 18.500  5.927   36.996  1.00 52.73 ?  302 SER D OG    1 
ATOM   4540 N N     . THR B 1 311 ? 21.048  1.936   36.440  1.00 47.92 ?  303 THR D N     1 
ATOM   4541 C CA    . THR B 1 311 ? 21.346  0.531   36.663  1.00 46.13 ?  303 THR D CA    1 
ATOM   4542 C C     . THR B 1 311 ? 22.440  0.412   37.721  1.00 47.41 ?  303 THR D C     1 
ATOM   4543 O O     . THR B 1 311 ? 23.067  1.406   38.097  1.00 45.10 ?  303 THR D O     1 
ATOM   4544 C CB    . THR B 1 311 ? 21.773  -0.120  35.347  1.00 47.08 ?  303 THR D CB    1 
ATOM   4545 O OG1   . THR B 1 311 ? 23.036  0.418   34.932  1.00 40.64 ?  303 THR D OG1   1 
ATOM   4546 C CG2   . THR B 1 311 ? 20.736  0.146   34.259  1.00 37.99 ?  303 THR D CG2   1 
ATOM   4547 N N     . PRO B 1 312 ? 22.697  -0.798  38.245  1.00 55.82 ?  304 PRO D N     1 
ATOM   4548 C CA    . PRO B 1 312 ? 23.804  -0.949  39.202  1.00 50.87 ?  304 PRO D CA    1 
ATOM   4549 C C     . PRO B 1 312 ? 25.174  -0.795  38.553  1.00 49.72 ?  304 PRO D C     1 
ATOM   4550 O O     . PRO B 1 312 ? 26.204  -0.894  39.229  1.00 55.77 ?  304 PRO D O     1 
ATOM   4551 C CB    . PRO B 1 312 ? 23.609  -2.361  39.778  1.00 43.83 ?  304 PRO D CB    1 
ATOM   4552 C CG    . PRO B 1 312 ? 22.326  -2.865  39.250  1.00 48.98 ?  304 PRO D CG    1 
ATOM   4553 C CD    . PRO B 1 312 ? 21.866  -2.003  38.135  1.00 53.41 ?  304 PRO D CD    1 
ATOM   4554 N N     . LEU B 1 313 ? 25.198  -0.535  37.244  1.00 47.86 ?  305 LEU D N     1 
ATOM   4555 C CA    . LEU B 1 313 ? 26.464  -0.391  36.533  1.00 51.84 ?  305 LEU D CA    1 
ATOM   4556 C C     . LEU B 1 313 ? 27.234  0.843   36.998  1.00 48.36 ?  305 LEU D C     1 
ATOM   4557 O O     . LEU B 1 313 ? 28.444  0.767   37.242  1.00 42.56 ?  305 LEU D O     1 
ATOM   4558 C CB    . LEU B 1 313 ? 26.210  -0.342  35.024  1.00 43.24 ?  305 LEU D CB    1 
ATOM   4559 C CG    . LEU B 1 313 ? 27.428  -0.100  34.136  1.00 41.79 ?  305 LEU D CG    1 
ATOM   4560 C CD1   . LEU B 1 313 ? 28.547  -1.090  34.444  1.00 46.37 ?  305 LEU D CD1   1 
ATOM   4561 C CD2   . LEU B 1 313 ? 27.043  -0.165  32.669  1.00 41.99 ?  305 LEU D CD2   1 
ATOM   4562 N N     . TYR B 1 314 ? 26.557  1.985   37.137  1.00 48.87 ?  306 TYR D N     1 
ATOM   4563 C CA    . TYR B 1 314 ? 27.226  3.230   37.501  1.00 48.89 ?  306 TYR D CA    1 
ATOM   4564 C C     . TYR B 1 314 ? 26.642  3.887   38.747  1.00 52.94 ?  306 TYR D C     1 
ATOM   4565 O O     . TYR B 1 314 ? 26.987  5.038   39.043  1.00 50.21 ?  306 TYR D O     1 
ATOM   4566 C CB    . TYR B 1 314 ? 27.195  4.212   36.326  1.00 44.74 ?  306 TYR D CB    1 
ATOM   4567 C CG    . TYR B 1 314 ? 27.987  3.727   35.135  1.00 42.72 ?  306 TYR D CG    1 
ATOM   4568 C CD1   . TYR B 1 314 ? 29.312  3.337   35.275  1.00 39.96 ?  306 TYR D CD1   1 
ATOM   4569 C CD2   . TYR B 1 314 ? 27.408  3.643   33.877  1.00 39.52 ?  306 TYR D CD2   1 
ATOM   4570 C CE1   . TYR B 1 314 ? 30.041  2.883   34.192  1.00 41.41 ?  306 TYR D CE1   1 
ATOM   4571 C CE2   . TYR B 1 314 ? 28.129  3.191   32.788  1.00 34.80 ?  306 TYR D CE2   1 
ATOM   4572 C CZ    . TYR B 1 314 ? 29.445  2.811   32.952  1.00 40.34 ?  306 TYR D CZ    1 
ATOM   4573 O OH    . TYR B 1 314 ? 30.170  2.361   31.873  1.00 35.93 ?  306 TYR D OH    1 
ATOM   4574 N N     . SER B 1 315 ? 25.779  3.193   39.482  1.00 52.50 ?  307 SER D N     1 
ATOM   4575 C CA    . SER B 1 315 ? 25.245  3.703   40.743  1.00 55.95 ?  307 SER D CA    1 
ATOM   4576 C C     . SER B 1 315 ? 26.259  3.534   41.870  1.00 53.13 ?  307 SER D C     1 
ATOM   4577 O O     . SER B 1 315 ? 26.892  2.485   41.994  1.00 58.91 ?  307 SER D O     1 
ATOM   4578 C CB    . SER B 1 315 ? 23.939  2.992   41.105  1.00 48.27 ?  307 SER D CB    1 
ATOM   4579 O OG    . SER B 1 315 ? 22.819  3.665   40.559  1.00 55.63 ?  307 SER D OG    1 
ATOM   4580 N N     . MET C 1 9   ? 17.269  6.017   -6.204  1.00 61.72 ?  1   MET B N     1 
ATOM   4581 C CA    . MET C 1 9   ? 18.383  5.098   -6.408  1.00 65.14 ?  1   MET B CA    1 
ATOM   4582 C C     . MET C 1 9   ? 18.400  4.584   -7.843  1.00 65.02 ?  1   MET B C     1 
ATOM   4583 O O     . MET C 1 9   ? 18.139  3.407   -8.096  1.00 67.52 ?  1   MET B O     1 
ATOM   4584 C CB    . MET C 1 9   ? 18.306  3.927   -5.427  1.00 67.27 ?  1   MET B CB    1 
ATOM   4585 C CG    . MET C 1 9   ? 19.661  3.442   -4.935  1.00 72.66 ?  1   MET B CG    1 
ATOM   4586 S SD    . MET C 1 9   ? 20.709  4.790   -4.354  1.00 91.15 ?  1   MET B SD    1 
ATOM   4587 C CE    . MET C 1 9   ? 19.800  5.322   -2.906  1.00 73.27 ?  1   MET B CE    1 
ATOM   4588 N N     . ALA C 1 10  ? 18.715  5.474   -8.776  1.00 60.54 ?  2   ALA B N     1 
ATOM   4589 C CA    . ALA C 1 10  ? 18.702  5.151   -10.193 1.00 50.16 ?  2   ALA B CA    1 
ATOM   4590 C C     . ALA C 1 10  ? 20.038  4.562   -10.640 1.00 52.53 ?  2   ALA B C     1 
ATOM   4591 O O     . ALA C 1 10  ? 21.082  4.763   -10.014 1.00 48.71 ?  2   ALA B O     1 
ATOM   4592 C CB    . ALA C 1 10  ? 18.377  6.394   -11.023 1.00 43.63 ?  2   ALA B CB    1 
ATOM   4593 N N     . GLN C 1 11  ? 19.984  3.828   -11.748 1.00 46.37 ?  3   GLN B N     1 
ATOM   4594 C CA    . GLN C 1 11  ? 21.177  3.237   -12.332 1.00 44.08 ?  3   GLN B CA    1 
ATOM   4595 C C     . GLN C 1 11  ? 22.060  4.312   -12.958 1.00 45.37 ?  3   GLN B C     1 
ATOM   4596 O O     . GLN C 1 11  ? 21.577  5.334   -13.453 1.00 38.80 ?  3   GLN B O     1 
ATOM   4597 C CB    . GLN C 1 11  ? 20.783  2.198   -13.381 1.00 40.16 ?  3   GLN B CB    1 
ATOM   4598 C CG    . GLN C 1 11  ? 21.832  1.137   -13.659 1.00 47.43 ?  3   GLN B CG    1 
ATOM   4599 C CD    . GLN C 1 11  ? 21.564  0.385   -14.950 1.00 51.40 ?  3   GLN B CD    1 
ATOM   4600 O OE1   . GLN C 1 11  ? 20.424  0.023   -15.244 1.00 54.14 ?  3   GLN B OE1   1 
ATOM   4601 N NE2   . GLN C 1 11  ? 22.616  0.140   -15.723 1.00 46.05 ?  3   GLN B NE2   1 
ATOM   4602 N N     . LYS C 1 12  ? 23.370  4.072   -12.931 1.00 39.43 ?  4   LYS B N     1 
ATOM   4603 C CA    . LYS C 1 12  ? 24.306  5.015   -13.521 1.00 37.57 ?  4   LYS B CA    1 
ATOM   4604 C C     . LYS C 1 12  ? 24.225  4.960   -15.047 1.00 35.63 ?  4   LYS B C     1 
ATOM   4605 O O     . LYS C 1 12  ? 23.899  3.917   -15.621 1.00 34.53 ?  4   LYS B O     1 
ATOM   4606 C CB    . LYS C 1 12  ? 25.729  4.717   -13.056 1.00 40.75 ?  4   LYS B CB    1 
ATOM   4607 C CG    . LYS C 1 12  ? 25.968  5.041   -11.590 1.00 48.73 ?  4   LYS B CG    1 
ATOM   4608 C CD    . LYS C 1 12  ? 26.583  6.422   -11.415 1.00 46.93 ?  4   LYS B CD    1 
ATOM   4609 C CE    . LYS C 1 12  ? 27.246  6.565   -10.052 1.00 54.04 ?  4   LYS B CE    1 
ATOM   4610 N NZ    . LYS C 1 12  ? 26.451  7.415   -9.122  1.00 51.50 ?  4   LYS B NZ    1 
ATOM   4611 N N     . PRO C 1 13  ? 24.511  6.075   -15.725 1.00 36.61 ?  5   PRO B N     1 
ATOM   4612 C CA    . PRO C 1 13  ? 24.341  6.123   -17.184 1.00 33.95 ?  5   PRO B CA    1 
ATOM   4613 C C     . PRO C 1 13  ? 25.168  5.063   -17.898 1.00 33.43 ?  5   PRO B C     1 
ATOM   4614 O O     . PRO C 1 13  ? 26.216  4.627   -17.416 1.00 35.32 ?  5   PRO B O     1 
ATOM   4615 C CB    . PRO C 1 13  ? 24.812  7.535   -17.548 1.00 36.80 ?  5   PRO B CB    1 
ATOM   4616 C CG    . PRO C 1 13  ? 24.614  8.330   -16.301 1.00 32.86 ?  5   PRO B CG    1 
ATOM   4617 C CD    . PRO C 1 13  ? 24.890  7.385   -15.169 1.00 33.64 ?  5   PRO B CD    1 
ATOM   4618 N N     . VAL C 1 14  ? 24.680  4.653   -19.068 1.00 30.23 ?  6   VAL B N     1 
ATOM   4619 C CA    . VAL C 1 14  ? 25.276  3.566   -19.832 1.00 31.61 ?  6   VAL B CA    1 
ATOM   4620 C C     . VAL C 1 14  ? 25.538  4.032   -21.257 1.00 32.22 ?  6   VAL B C     1 
ATOM   4621 O O     . VAL C 1 14  ? 24.874  4.940   -21.768 1.00 29.58 ?  6   VAL B O     1 
ATOM   4622 C CB    . VAL C 1 14  ? 24.378  2.310   -19.832 1.00 35.11 ?  6   VAL B CB    1 
ATOM   4623 C CG1   . VAL C 1 14  ? 24.331  1.692   -18.444 1.00 29.71 ?  6   VAL B CG1   1 
ATOM   4624 C CG2   . VAL C 1 14  ? 22.977  2.659   -20.315 1.00 30.89 ?  6   VAL B CG2   1 
ATOM   4625 N N     . ASP C 1 15  ? 26.516  3.393   -21.902 1.00 32.83 ?  7   ASP B N     1 
ATOM   4626 C CA    . ASP C 1 15  ? 26.863  3.740   -23.276 1.00 34.28 ?  7   ASP B CA    1 
ATOM   4627 C C     . ASP C 1 15  ? 25.872  3.168   -24.279 1.00 31.11 ?  7   ASP B C     1 
ATOM   4628 O O     . ASP C 1 15  ? 25.648  3.772   -25.334 1.00 33.13 ?  7   ASP B O     1 
ATOM   4629 C CB    . ASP C 1 15  ? 28.273  3.246   -23.606 1.00 36.28 ?  7   ASP B CB    1 
ATOM   4630 C CG    . ASP C 1 15  ? 29.355  4.100   -22.977 1.00 48.40 ?  7   ASP B CG    1 
ATOM   4631 O OD1   . ASP C 1 15  ? 30.345  3.527   -22.475 1.00 46.80 ?  7   ASP B OD1   1 
ATOM   4632 O OD2   . ASP C 1 15  ? 29.222  5.342   -22.991 1.00 46.64 ?  7   ASP B OD2   1 
ATOM   4633 N N     . ASN C 1 16  ? 25.272  2.020   -23.974 1.00 28.34 ?  8   ASN B N     1 
ATOM   4634 C CA    . ASN C 1 16  ? 24.391  1.338   -24.908 1.00 29.75 ?  8   ASN B CA    1 
ATOM   4635 C C     . ASN C 1 16  ? 23.154  0.839   -24.176 1.00 28.42 ?  8   ASN B C     1 
ATOM   4636 O O     . ASN C 1 16  ? 23.230  0.442   -23.009 1.00 29.32 ?  8   ASN B O     1 
ATOM   4637 C CB    . ASN C 1 16  ? 25.118  0.174   -25.595 1.00 29.19 ?  8   ASN B CB    1 
ATOM   4638 C CG    . ASN C 1 16  ? 24.325  -0.411  -26.745 1.00 32.34 ?  8   ASN B CG    1 
ATOM   4639 O OD1   . ASN C 1 16  ? 23.325  -1.096  -26.542 1.00 32.91 ?  8   ASN B OD1   1 
ATOM   4640 N ND2   . ASN C 1 16  ? 24.772  -0.141  -27.966 1.00 32.17 ?  8   ASN B ND2   1 
ATOM   4641 N N     . ILE C 1 17  ? 22.020  0.852   -24.887 1.00 29.10 ?  9   ILE B N     1 
ATOM   4642 C CA    . ILE C 1 17  ? 20.720  0.496   -24.318 1.00 28.75 ?  9   ILE B CA    1 
ATOM   4643 C C     . ILE C 1 17  ? 20.704  -0.953  -23.842 1.00 30.24 ?  9   ILE B C     1 
ATOM   4644 O O     . ILE C 1 17  ? 19.952  -1.304  -22.924 1.00 33.28 ?  9   ILE B O     1 
ATOM   4645 C CB    . ILE C 1 17  ? 19.618  0.772   -25.368 1.00 30.19 ?  9   ILE B CB    1 
ATOM   4646 C CG1   . ILE C 1 17  ? 18.203  0.588   -24.799 1.00 29.96 ?  9   ILE B CG1   1 
ATOM   4647 C CG2   . ILE C 1 17  ? 19.821  -0.107  -26.588 1.00 26.92 ?  9   ILE B CG2   1 
ATOM   4648 C CD1   . ILE C 1 17  ? 17.724  1.723   -23.907 1.00 33.94 ?  9   ILE B CD1   1 
ATOM   4649 N N     . THR C 1 18  ? 21.534  -1.816  -24.439 1.00 26.32 ?  10  THR B N     1 
ATOM   4650 C CA    . THR C 1 18  ? 21.566  -3.219  -24.036 1.00 27.63 ?  10  THR B CA    1 
ATOM   4651 C C     . THR C 1 18  ? 22.040  -3.395  -22.602 1.00 29.66 ?  10  THR B C     1 
ATOM   4652 O O     . THR C 1 18  ? 21.771  -4.437  -21.995 1.00 24.39 ?  10  THR B O     1 
ATOM   4653 C CB    . THR C 1 18  ? 22.473  -4.028  -24.967 1.00 26.94 ?  10  THR B CB    1 
ATOM   4654 O OG1   . THR C 1 18  ? 23.783  -3.448  -24.983 1.00 30.87 ?  10  THR B OG1   1 
ATOM   4655 C CG2   . THR C 1 18  ? 21.909  -4.059  -26.377 1.00 32.48 ?  10  THR B CG2   1 
ATOM   4656 N N     . GLN C 1 19  ? 22.730  -2.401  -22.048 1.00 30.26 ?  11  GLN B N     1 
ATOM   4657 C CA    . GLN C 1 19  ? 23.298  -2.504  -20.712 1.00 27.81 ?  11  GLN B CA    1 
ATOM   4658 C C     . GLN C 1 19  ? 22.271  -2.352  -19.597 1.00 29.22 ?  11  GLN B C     1 
ATOM   4659 O O     . GLN C 1 19  ? 22.650  -2.453  -18.426 1.00 33.62 ?  11  GLN B O     1 
ATOM   4660 C CB    . GLN C 1 19  ? 24.409  -1.466  -20.530 1.00 33.22 ?  11  GLN B CB    1 
ATOM   4661 C CG    . GLN C 1 19  ? 25.638  -1.727  -21.386 1.00 33.68 ?  11  GLN B CG    1 
ATOM   4662 C CD    . GLN C 1 19  ? 26.640  -0.592  -21.330 1.00 36.58 ?  11  GLN B CD    1 
ATOM   4663 O OE1   . GLN C 1 19  ? 27.188  -0.180  -22.351 1.00 41.27 ?  11  GLN B OE1   1 
ATOM   4664 N NE2   . GLN C 1 19  ? 26.885  -0.079  -20.130 1.00 44.40 ?  11  GLN B NE2   1 
ATOM   4665 N N     . ILE C 1 20  ? 20.997  -2.106  -19.902 1.00 32.70 ?  12  ILE B N     1 
ATOM   4666 C CA    . ILE C 1 20  ? 19.958  -2.147  -18.878 1.00 31.60 ?  12  ILE B CA    1 
ATOM   4667 C C     . ILE C 1 20  ? 19.039  -3.342  -19.042 1.00 27.99 ?  12  ILE B C     1 
ATOM   4668 O O     . ILE C 1 20  ? 18.017  -3.425  -18.344 1.00 33.19 ?  12  ILE B O     1 
ATOM   4669 C CB    . ILE C 1 20  ? 19.138  -0.842  -18.827 1.00 39.60 ?  12  ILE B CB    1 
ATOM   4670 C CG1   . ILE C 1 20  ? 18.507  -0.528  -20.184 1.00 35.87 ?  12  ILE B CG1   1 
ATOM   4671 C CG2   . ILE C 1 20  ? 20.025  0.316   -18.406 1.00 42.02 ?  12  ILE B CG2   1 
ATOM   4672 C CD1   . ILE C 1 20  ? 18.031  0.924   -20.348 1.00 44.40 ?  12  ILE B CD1   1 
ATOM   4673 N N     . ILE C 1 21  ? 19.359  -4.269  -19.947 1.00 29.31 ?  13  ILE B N     1 
ATOM   4674 C CA    . ILE C 1 21  ? 18.626  -5.525  -20.003 1.00 30.17 ?  13  ILE B CA    1 
ATOM   4675 C C     . ILE C 1 21  ? 18.878  -6.300  -18.717 1.00 33.19 ?  13  ILE B C     1 
ATOM   4676 O O     . ILE C 1 21  ? 20.017  -6.399  -18.241 1.00 30.76 ?  13  ILE B O     1 
ATOM   4677 C CB    . ILE C 1 21  ? 19.042  -6.336  -21.241 1.00 24.25 ?  13  ILE B CB    1 
ATOM   4678 C CG1   . ILE C 1 21  ? 18.666  -5.587  -22.519 1.00 26.56 ?  13  ILE B CG1   1 
ATOM   4679 C CG2   . ILE C 1 21  ? 18.403  -7.716  -21.226 1.00 26.65 ?  13  ILE B CG2   1 
ATOM   4680 C CD1   . ILE C 1 21  ? 19.236  -6.210  -23.769 1.00 26.90 ?  13  ILE B CD1   1 
ATOM   4681 N N     . GLY C 1 22  ? 17.809  -6.836  -18.136 1.00 30.13 ?  14  GLY B N     1 
ATOM   4682 C CA    . GLY C 1 22  ? 17.919  -7.585  -16.901 1.00 29.36 ?  14  GLY B CA    1 
ATOM   4683 C C     . GLY C 1 22  ? 17.679  -6.727  -15.676 1.00 29.01 ?  14  GLY B C     1 
ATOM   4684 O O     . GLY C 1 22  ? 17.364  -5.536  -15.749 1.00 30.88 ?  14  GLY B O     1 
ATOM   4685 N N     . GLY C 1 23  ? 17.843  -7.356  -14.517 1.00 26.75 ?  15  GLY B N     1 
ATOM   4686 C CA    . GLY C 1 23  ? 17.596  -6.681  -13.253 1.00 32.11 ?  15  GLY B CA    1 
ATOM   4687 C C     . GLY C 1 23  ? 16.143  -6.312  -13.053 1.00 31.17 ?  15  GLY B C     1 
ATOM   4688 O O     . GLY C 1 23  ? 15.845  -5.218  -12.556 1.00 33.34 ?  15  GLY B O     1 
ATOM   4689 N N     . THR C 1 24  ? 15.234  -7.198  -13.426 1.00 29.15 ?  16  THR B N     1 
ATOM   4690 C CA    . THR C 1 24  ? 13.812  -6.905  -13.433 1.00 30.65 ?  16  THR B CA    1 
ATOM   4691 C C     . THR C 1 24  ? 13.221  -7.033  -12.028 1.00 28.88 ?  16  THR B C     1 
ATOM   4692 O O     . THR C 1 24  ? 13.688  -7.840  -11.220 1.00 26.24 ?  16  THR B O     1 
ATOM   4693 C CB    . THR C 1 24  ? 13.088  -7.844  -14.392 1.00 26.65 ?  16  THR B CB    1 
ATOM   4694 O OG1   . THR C 1 24  ? 13.511  -9.192  -14.159 1.00 27.09 ?  16  THR B OG1   1 
ATOM   4695 C CG2   . THR C 1 24  ? 13.406  -7.469  -15.831 1.00 24.90 ?  16  THR B CG2   1 
ATOM   4696 N N     . PRO C 1 25  ? 12.198  -6.243  -11.716 1.00 26.59 ?  17  PRO B N     1 
ATOM   4697 C CA    . PRO C 1 25  ? 11.640  -6.243  -10.361 1.00 31.64 ?  17  PRO B CA    1 
ATOM   4698 C C     . PRO C 1 25  ? 10.667  -7.396  -10.142 1.00 32.17 ?  17  PRO B C     1 
ATOM   4699 O O     . PRO C 1 25  ? 10.257  -8.097  -11.068 1.00 30.09 ?  17  PRO B O     1 
ATOM   4700 C CB    . PRO C 1 25  ? 10.925  -4.892  -10.289 1.00 32.68 ?  17  PRO B CB    1 
ATOM   4701 C CG    . PRO C 1 25  ? 10.465  -4.668  -11.688 1.00 30.44 ?  17  PRO B CG    1 
ATOM   4702 C CD    . PRO C 1 25  ? 11.554  -5.230  -12.572 1.00 30.80 ?  17  PRO B CD    1 
ATOM   4703 N N     . VAL C 1 26  ? 10.301  -7.574  -8.874  1.00 29.36 ?  18  VAL B N     1 
ATOM   4704 C CA    . VAL C 1 26  ? 9.385   -8.622  -8.439  1.00 29.86 ?  18  VAL B CA    1 
ATOM   4705 C C     . VAL C 1 26  ? 8.297   -7.974  -7.592  1.00 31.83 ?  18  VAL B C     1 
ATOM   4706 O O     . VAL C 1 26  ? 8.592   -7.138  -6.732  1.00 33.02 ?  18  VAL B O     1 
ATOM   4707 C CB    . VAL C 1 26  ? 10.115  -9.724  -7.645  1.00 31.61 ?  18  VAL B CB    1 
ATOM   4708 C CG1   . VAL C 1 26  ? 9.124   -10.612 -6.907  1.00 27.57 ?  18  VAL B CG1   1 
ATOM   4709 C CG2   . VAL C 1 26  ? 10.994  -10.554 -8.571  1.00 29.37 ?  18  VAL B CG2   1 
ATOM   4710 N N     . VAL C 1 27  ? 7.044   -8.349  -7.841  1.00 28.87 ?  19  VAL B N     1 
ATOM   4711 C CA    . VAL C 1 27  ? 5.896   -7.772  -7.151  1.00 28.97 ?  19  VAL B CA    1 
ATOM   4712 C C     . VAL C 1 27  ? 5.078   -8.892  -6.522  1.00 33.08 ?  19  VAL B C     1 
ATOM   4713 O O     . VAL C 1 27  ? 4.843   -9.932  -7.149  1.00 32.91 ?  19  VAL B O     1 
ATOM   4714 C CB    . VAL C 1 27  ? 5.026   -6.926  -8.108  1.00 28.37 ?  19  VAL B CB    1 
ATOM   4715 C CG1   . VAL C 1 27  ? 3.774   -6.418  -7.400  1.00 34.97 ?  19  VAL B CG1   1 
ATOM   4716 C CG2   . VAL C 1 27  ? 5.830   -5.761  -8.667  1.00 20.92 ?  19  VAL B CG2   1 
ATOM   4717 N N     . LYS C 1 28  ? 4.652   -8.679  -5.278  1.00 29.62 ?  20  LYS B N     1 
ATOM   4718 C CA    . LYS C 1 28  ? 3.786   -9.624  -4.584  1.00 29.66 ?  20  LYS B CA    1 
ATOM   4719 C C     . LYS C 1 28  ? 2.330   -9.383  -4.967  1.00 30.53 ?  20  LYS B C     1 
ATOM   4720 O O     . LYS C 1 28  ? 1.867   -8.238  -4.990  1.00 35.36 ?  20  LYS B O     1 
ATOM   4721 C CB    . LYS C 1 28  ? 3.970   -9.490  -3.072  1.00 29.62 ?  20  LYS B CB    1 
ATOM   4722 C CG    . LYS C 1 28  ? 3.151   -10.462 -2.233  1.00 35.68 ?  20  LYS B CG    1 
ATOM   4723 C CD    . LYS C 1 28  ? 3.301   -10.161 -0.745  1.00 35.41 ?  20  LYS B CD    1 
ATOM   4724 C CE    . LYS C 1 28  ? 2.206   -10.822 0.081   1.00 42.28 ?  20  LYS B CE    1 
ATOM   4725 N NZ    . LYS C 1 28  ? 0.853   -10.565 -0.489  1.00 52.18 ?  20  LYS B NZ    1 
ATOM   4726 N N     . LEU C 1 29  ? 1.609   -10.461 -5.271  1.00 31.33 ?  21  LEU B N     1 
ATOM   4727 C CA    . LEU C 1 29  ? 0.196   -10.345 -5.601  1.00 33.41 ?  21  LEU B CA    1 
ATOM   4728 C C     . LEU C 1 29  ? -0.625  -10.139 -4.336  1.00 36.49 ?  21  LEU B C     1 
ATOM   4729 O O     . LEU C 1 29  ? -0.345  -10.733 -3.292  1.00 36.65 ?  21  LEU B O     1 
ATOM   4730 C CB    . LEU C 1 29  ? -0.287  -11.586 -6.350  1.00 32.22 ?  21  LEU B CB    1 
ATOM   4731 C CG    . LEU C 1 29  ? 0.266   -11.760 -7.766  1.00 32.63 ?  21  LEU B CG    1 
ATOM   4732 C CD1   . LEU C 1 29  ? -0.489  -12.854 -8.504  1.00 30.81 ?  21  LEU B CD1   1 
ATOM   4733 C CD2   . LEU C 1 29  ? 0.207   -10.446 -8.535  1.00 31.23 ?  21  LEU B CD2   1 
ATOM   4734 N N     . ARG C 1 30  ? -1.648  -9.293  -4.436  1.00 37.05 ?  22  ARG B N     1 
ATOM   4735 C CA    . ARG C 1 30  ? -2.422  -8.857  -3.279  1.00 36.90 ?  22  ARG B CA    1 
ATOM   4736 C C     . ARG C 1 30  ? -3.872  -9.309  -3.293  1.00 36.66 ?  22  ARG B C     1 
ATOM   4737 O O     . ARG C 1 30  ? -4.392  -9.717  -2.252  1.00 36.18 ?  22  ARG B O     1 
ATOM   4738 C CB    . ARG C 1 30  ? -2.388  -7.328  -3.171  1.00 35.95 ?  22  ARG B CB    1 
ATOM   4739 C CG    . ARG C 1 30  ? -1.164  -6.773  -2.466  1.00 35.31 ?  22  ARG B CG    1 
ATOM   4740 C CD    . ARG C 1 30  ? -1.114  -5.260  -2.583  1.00 35.85 ?  22  ARG B CD    1 
ATOM   4741 N NE    . ARG C 1 30  ? -1.074  -4.826  -3.974  1.00 33.53 ?  22  ARG B NE    1 
ATOM   4742 C CZ    . ARG C 1 30  ? -2.069  -4.204  -4.593  1.00 35.40 ?  22  ARG B CZ    1 
ATOM   4743 N NH1   . ARG C 1 30  ? -3.200  -3.917  -3.968  1.00 32.53 ?  22  ARG B NH1   1 
ATOM   4744 N NH2   . ARG C 1 30  ? -1.926  -3.863  -5.870  1.00 31.15 ?  22  ARG B NH2   1 
ATOM   4745 N N     . ASN C 1 31  ? -4.548  -9.243  -4.441  1.00 33.29 ?  23  ASN B N     1 
ATOM   4746 C CA    . ASN C 1 31  ? -5.997  -9.396  -4.486  1.00 33.80 ?  23  ASN B CA    1 
ATOM   4747 C C     . ASN C 1 31  ? -6.479  -10.644 -5.211  1.00 35.54 ?  23  ASN B C     1 
ATOM   4748 O O     . ASN C 1 31  ? -7.514  -11.195 -4.829  1.00 35.29 ?  23  ASN B O     1 
ATOM   4749 C CB    . ASN C 1 31  ? -6.634  -8.164  -5.146  1.00 30.49 ?  23  ASN B CB    1 
ATOM   4750 C CG    . ASN C 1 31  ? -6.455  -6.900  -4.321  1.00 37.73 ?  23  ASN B CG    1 
ATOM   4751 O OD1   . ASN C 1 31  ? -6.683  -6.896  -3.111  1.00 40.26 ?  23  ASN B OD1   1 
ATOM   4752 N ND2   . ASN C 1 31  ? -6.042  -5.819  -4.974  1.00 40.68 ?  23  ASN B ND2   1 
ATOM   4753 N N     . VAL C 1 32  ? -5.768  -11.107 -6.244  1.00 37.43 ?  24  VAL B N     1 
ATOM   4754 C CA    . VAL C 1 32  ? -6.250  -12.248 -7.022  1.00 40.15 ?  24  VAL B CA    1 
ATOM   4755 C C     . VAL C 1 32  ? -5.954  -13.587 -6.367  1.00 40.30 ?  24  VAL B C     1 
ATOM   4756 O O     . VAL C 1 32  ? -6.484  -14.612 -6.815  1.00 38.47 ?  24  VAL B O     1 
ATOM   4757 C CB    . VAL C 1 32  ? -5.654  -12.250 -8.443  1.00 38.73 ?  24  VAL B CB    1 
ATOM   4758 C CG1   . VAL C 1 32  ? -6.061  -10.988 -9.192  1.00 32.73 ?  24  VAL B CG1   1 
ATOM   4759 C CG2   . VAL C 1 32  ? -4.140  -12.389 -8.387  1.00 31.63 ?  24  VAL B CG2   1 
ATOM   4760 N N     . VAL C 1 33  ? -5.129  -13.614 -5.323  1.00 34.19 ?  25  VAL B N     1 
ATOM   4761 C CA    . VAL C 1 33  ? -4.796  -14.840 -4.609  1.00 39.28 ?  25  VAL B CA    1 
ATOM   4762 C C     . VAL C 1 33  ? -5.337  -14.729 -3.190  1.00 46.51 ?  25  VAL B C     1 
ATOM   4763 O O     . VAL C 1 33  ? -5.145  -13.706 -2.523  1.00 49.79 ?  25  VAL B O     1 
ATOM   4764 C CB    . VAL C 1 33  ? -3.279  -15.110 -4.611  1.00 45.05 ?  25  VAL B CB    1 
ATOM   4765 C CG1   . VAL C 1 33  ? -2.505  -13.847 -4.266  1.00 39.35 ?  25  VAL B CG1   1 
ATOM   4766 C CG2   . VAL C 1 33  ? -2.929  -16.244 -3.653  1.00 38.58 ?  25  VAL B CG2   1 
ATOM   4767 N N     . ASP C 1 34  ? -6.017  -15.780 -2.738  1.00 48.59 ?  26  ASP B N     1 
ATOM   4768 C CA    . ASP C 1 34  ? -6.646  -15.775 -1.426  1.00 57.36 ?  26  ASP B CA    1 
ATOM   4769 C C     . ASP C 1 34  ? -5.596  -15.757 -0.317  1.00 59.45 ?  26  ASP B C     1 
ATOM   4770 O O     . ASP C 1 34  ? -4.474  -16.244 -0.482  1.00 56.74 ?  26  ASP B O     1 
ATOM   4771 C CB    . ASP C 1 34  ? -7.566  -16.990 -1.289  1.00 58.47 ?  26  ASP B CB    1 
ATOM   4772 C CG    . ASP C 1 34  ? -7.793  -17.394 0.148   1.00 69.47 ?  26  ASP B CG    1 
ATOM   4773 O OD1   . ASP C 1 34  ? -7.159  -18.372 0.592   1.00 71.15 ?  26  ASP B OD1   1 
ATOM   4774 O OD2   . ASP C 1 34  ? -8.595  -16.728 0.836   1.00 69.50 ?  26  ASP B OD2   1 
ATOM   4775 N N     . ASP C 1 35  ? -5.973  -15.173 0.828   1.00 64.65 ?  27  ASP B N     1 
ATOM   4776 C CA    . ASP C 1 35  ? -5.036  -14.994 1.933   1.00 65.23 ?  27  ASP B CA    1 
ATOM   4777 C C     . ASP C 1 35  ? -4.620  -16.309 2.582   1.00 62.59 ?  27  ASP B C     1 
ATOM   4778 O O     . ASP C 1 35  ? -3.547  -16.367 3.192   1.00 60.37 ?  27  ASP B O     1 
ATOM   4779 C CB    . ASP C 1 35  ? -5.638  -14.068 2.990   1.00 67.14 ?  27  ASP B CB    1 
ATOM   4780 C CG    . ASP C 1 35  ? -4.823  -12.804 3.189   1.00 68.41 ?  27  ASP B CG    1 
ATOM   4781 O OD1   . ASP C 1 35  ? -3.586  -12.907 3.337   1.00 60.72 ?  27  ASP B OD1   1 
ATOM   4782 O OD2   . ASP C 1 35  ? -5.420  -11.707 3.191   1.00 65.21 ?  27  ASP B OD2   1 
ATOM   4783 N N     . ASN C 1 36  ? -5.434  -17.356 2.476   1.00 60.93 ?  28  ASN B N     1 
ATOM   4784 C CA    . ASN C 1 36  ? -5.093  -18.656 3.038   1.00 62.83 ?  28  ASN B CA    1 
ATOM   4785 C C     . ASN C 1 36  ? -4.257  -19.507 2.090   1.00 55.98 ?  28  ASN B C     1 
ATOM   4786 O O     . ASN C 1 36  ? -3.972  -20.667 2.404   1.00 57.16 ?  28  ASN B O     1 
ATOM   4787 C CB    . ASN C 1 36  ? -6.364  -19.408 3.443   1.00 68.69 ?  28  ASN B CB    1 
ATOM   4788 C CG    . ASN C 1 36  ? -6.967  -18.879 4.730   1.00 73.75 ?  28  ASN B CG    1 
ATOM   4789 O OD1   . ASN C 1 36  ? -6.249  -18.558 5.678   1.00 75.86 ?  28  ASN B OD1   1 
ATOM   4790 N ND2   . ASN C 1 36  ? -8.291  -18.786 4.770   1.00 73.50 ?  28  ASN B ND2   1 
ATOM   4791 N N     . ALA C 1 37  ? -3.864  -18.961 0.945   1.00 51.41 ?  29  ALA B N     1 
ATOM   4792 C CA    . ALA C 1 37  ? -2.939  -19.613 0.033   1.00 44.06 ?  29  ALA B CA    1 
ATOM   4793 C C     . ALA C 1 37  ? -1.546  -19.012 0.194   1.00 39.99 ?  29  ALA B C     1 
ATOM   4794 O O     . ALA C 1 37  ? -1.348  -18.008 0.883   1.00 42.01 ?  29  ALA B O     1 
ATOM   4795 C CB    . ALA C 1 37  ? -3.421  -19.480 -1.414  1.00 42.10 ?  29  ALA B CB    1 
ATOM   4796 N N     . ALA C 1 38  ? -0.573  -19.644 -0.454  1.00 38.93 ?  30  ALA B N     1 
ATOM   4797 C CA    . ALA C 1 38  ? 0.799   -19.171 -0.376  1.00 34.30 ?  30  ALA B CA    1 
ATOM   4798 C C     . ALA C 1 38  ? 0.943   -17.817 -1.064  1.00 34.79 ?  30  ALA B C     1 
ATOM   4799 O O     . ALA C 1 38  ? 0.135   -17.428 -1.913  1.00 38.77 ?  30  ALA B O     1 
ATOM   4800 C CB    . ALA C 1 38  ? 1.753   -20.185 -1.008  1.00 35.55 ?  30  ALA B CB    1 
ATOM   4801 N N     . ASP C 1 39  ? 1.986   -17.089 -0.674  1.00 30.44 ?  31  ASP B N     1 
ATOM   4802 C CA    . ASP C 1 39  ? 2.308   -15.837 -1.343  1.00 30.40 ?  31  ASP B CA    1 
ATOM   4803 C C     . ASP C 1 39  ? 2.716   -16.104 -2.785  1.00 33.21 ?  31  ASP B C     1 
ATOM   4804 O O     . ASP C 1 39  ? 3.406   -17.083 -3.082  1.00 34.50 ?  31  ASP B O     1 
ATOM   4805 C CB    . ASP C 1 39  ? 3.437   -15.115 -0.607  1.00 36.93 ?  31  ASP B CB    1 
ATOM   4806 C CG    . ASP C 1 39  ? 3.018   -14.619 0.759   1.00 38.40 ?  31  ASP B CG    1 
ATOM   4807 O OD1   . ASP C 1 39  ? 1.818   -14.333 0.949   1.00 40.47 ?  31  ASP B OD1   1 
ATOM   4808 O OD2   . ASP C 1 39  ? 3.893   -14.512 1.643   1.00 34.48 ?  31  ASP B OD2   1 
ATOM   4809 N N     . VAL C 1 40  ? 2.283   -15.227 -3.686  1.00 28.47 ?  32  VAL B N     1 
ATOM   4810 C CA    . VAL C 1 40  ? 2.603   -15.336 -5.104  1.00 28.90 ?  32  VAL B CA    1 
ATOM   4811 C C     . VAL C 1 40  ? 3.376   -14.091 -5.510  1.00 33.47 ?  32  VAL B C     1 
ATOM   4812 O O     . VAL C 1 40  ? 2.869   -12.969 -5.380  1.00 31.36 ?  32  VAL B O     1 
ATOM   4813 C CB    . VAL C 1 40  ? 1.346   -15.504 -5.969  1.00 26.71 ?  32  VAL B CB    1 
ATOM   4814 C CG1   . VAL C 1 40  ? 1.723   -15.515 -7.441  1.00 25.76 ?  32  VAL B CG1   1 
ATOM   4815 C CG2   . VAL C 1 40  ? 0.611   -16.776 -5.593  1.00 28.75 ?  32  VAL B CG2   1 
ATOM   4816 N N     . TYR C 1 41  ? 4.597   -14.290 -5.996  1.00 29.35 ?  33  TYR B N     1 
ATOM   4817 C CA    . TYR C 1 41  ? 5.449   -13.218 -6.486  1.00 29.90 ?  33  TYR B CA    1 
ATOM   4818 C C     . TYR C 1 41  ? 5.630   -13.368 -7.990  1.00 28.99 ?  33  TYR B C     1 
ATOM   4819 O O     . TYR C 1 41  ? 5.801   -14.484 -8.492  1.00 30.14 ?  33  TYR B O     1 
ATOM   4820 C CB    . TYR C 1 41  ? 6.814   -13.243 -5.792  1.00 27.30 ?  33  TYR B CB    1 
ATOM   4821 C CG    . TYR C 1 41  ? 6.768   -12.930 -4.313  1.00 31.38 ?  33  TYR B CG    1 
ATOM   4822 C CD1   . TYR C 1 41  ? 6.559   -13.935 -3.378  1.00 35.76 ?  33  TYR B CD1   1 
ATOM   4823 C CD2   . TYR C 1 41  ? 6.952   -11.633 -3.851  1.00 32.96 ?  33  TYR B CD2   1 
ATOM   4824 C CE1   . TYR C 1 41  ? 6.523   -13.656 -2.025  1.00 31.13 ?  33  TYR B CE1   1 
ATOM   4825 C CE2   . TYR C 1 41  ? 6.920   -11.345 -2.499  1.00 34.96 ?  33  TYR B CE2   1 
ATOM   4826 C CZ    . TYR C 1 41  ? 6.704   -12.359 -1.591  1.00 31.90 ?  33  TYR B CZ    1 
ATOM   4827 O OH    . TYR C 1 41  ? 6.670   -12.073 -0.246  1.00 43.50 ?  33  TYR B OH    1 
ATOM   4828 N N     . VAL C 1 42  ? 5.592   -12.246 -8.707  1.00 24.41 ?  34  VAL B N     1 
ATOM   4829 C CA    . VAL C 1 42  ? 5.746   -12.232 -10.157 1.00 26.08 ?  34  VAL B CA    1 
ATOM   4830 C C     . VAL C 1 42  ? 6.935   -11.351 -10.518 1.00 30.00 ?  34  VAL B C     1 
ATOM   4831 O O     . VAL C 1 42  ? 7.072   -10.236 -10.003 1.00 30.09 ?  34  VAL B O     1 
ATOM   4832 C CB    . VAL C 1 42  ? 4.464   -11.752 -10.866 1.00 28.20 ?  34  VAL B CB    1 
ATOM   4833 C CG1   . VAL C 1 42  ? 3.348   -12.766 -10.679 1.00 27.03 ?  34  VAL B CG1   1 
ATOM   4834 C CG2   . VAL C 1 42  ? 4.027   -10.391 -10.342 1.00 27.02 ?  34  VAL B CG2   1 
ATOM   4835 N N     . LYS C 1 43  ? 7.795   -11.859 -11.396 1.00 26.06 ?  35  LYS B N     1 
ATOM   4836 C CA    . LYS C 1 43  ? 8.953   -11.125 -11.889 1.00 29.63 ?  35  LYS B CA    1 
ATOM   4837 C C     . LYS C 1 43  ? 8.585   -10.491 -13.225 1.00 28.14 ?  35  LYS B C     1 
ATOM   4838 O O     . LYS C 1 43  ? 8.163   -11.191 -14.151 1.00 29.18 ?  35  LYS B O     1 
ATOM   4839 C CB    . LYS C 1 43  ? 10.157  -12.056 -12.027 1.00 26.35 ?  35  LYS B CB    1 
ATOM   4840 C CG    . LYS C 1 43  ? 11.490  -11.370 -12.280 1.00 22.55 ?  35  LYS B CG    1 
ATOM   4841 C CD    . LYS C 1 43  ? 12.636  -12.358 -12.091 1.00 27.38 ?  35  LYS B CD    1 
ATOM   4842 C CE    . LYS C 1 43  ? 13.994  -11.733 -12.385 1.00 23.24 ?  35  LYS B CE    1 
ATOM   4843 N NZ    . LYS C 1 43  ? 14.247  -10.502 -11.583 1.00 25.08 ?  35  LYS B NZ    1 
ATOM   4844 N N     . LEU C 1 44  ? 8.736   -9.170  -13.319 1.00 27.85 ?  36  LEU B N     1 
ATOM   4845 C CA    . LEU C 1 44  ? 8.233   -8.401  -14.459 1.00 33.33 ?  36  LEU B CA    1 
ATOM   4846 C C     . LEU C 1 44  ? 9.305   -8.336  -15.537 1.00 29.82 ?  36  LEU B C     1 
ATOM   4847 O O     . LEU C 1 44  ? 10.138  -7.429  -15.562 1.00 31.90 ?  36  LEU B O     1 
ATOM   4848 C CB    . LEU C 1 44  ? 7.814   -7.006  -14.018 1.00 33.33 ?  36  LEU B CB    1 
ATOM   4849 C CG    . LEU C 1 44  ? 6.887   -6.928  -12.808 1.00 29.42 ?  36  LEU B CG    1 
ATOM   4850 C CD1   . LEU C 1 44  ? 6.398   -5.513  -12.654 1.00 25.11 ?  36  LEU B CD1   1 
ATOM   4851 C CD2   . LEU C 1 44  ? 5.717   -7.888  -12.950 1.00 27.18 ?  36  LEU B CD2   1 
ATOM   4852 N N     . GLU C 1 45  ? 9.273   -9.302  -16.455 1.00 28.12 ?  37  GLU B N     1 
ATOM   4853 C CA    . GLU C 1 45  ? 10.229  -9.315  -17.554 1.00 28.63 ?  37  GLU B CA    1 
ATOM   4854 C C     . GLU C 1 45  ? 9.892   -8.314  -18.652 1.00 26.58 ?  37  GLU B C     1 
ATOM   4855 O O     . GLU C 1 45  ? 10.740  -8.063  -19.514 1.00 26.24 ?  37  GLU B O     1 
ATOM   4856 C CB    . GLU C 1 45  ? 10.330  -10.720 -18.145 1.00 26.07 ?  37  GLU B CB    1 
ATOM   4857 C CG    . GLU C 1 45  ? 11.067  -11.700 -17.249 1.00 22.85 ?  37  GLU B CG    1 
ATOM   4858 C CD    . GLU C 1 45  ? 12.507  -11.288 -17.006 1.00 25.73 ?  37  GLU B CD    1 
ATOM   4859 O OE1   . GLU C 1 45  ? 13.235  -11.053 -17.993 1.00 22.50 ?  37  GLU B OE1   1 
ATOM   4860 O OE2   . GLU C 1 45  ? 12.911  -11.194 -15.827 1.00 26.71 ?  37  GLU B OE2   1 
ATOM   4861 N N     . TYR C 1 46  ? 8.687   -7.737  -18.648 1.00 27.07 ?  38  TYR B N     1 
ATOM   4862 C CA    . TYR C 1 46  ? 8.398   -6.665  -19.592 1.00 27.61 ?  38  TYR B CA    1 
ATOM   4863 C C     . TYR C 1 46  ? 9.067   -5.353  -19.202 1.00 28.19 ?  38  TYR B C     1 
ATOM   4864 O O     . TYR C 1 46  ? 9.031   -4.401  -19.989 1.00 26.69 ?  38  TYR B O     1 
ATOM   4865 C CB    . TYR C 1 46  ? 6.884   -6.469  -19.740 1.00 27.73 ?  38  TYR B CB    1 
ATOM   4866 C CG    . TYR C 1 46  ? 6.129   -6.129  -18.468 1.00 28.33 ?  38  TYR B CG    1 
ATOM   4867 C CD1   . TYR C 1 46  ? 6.203   -4.860  -17.902 1.00 25.85 ?  38  TYR B CD1   1 
ATOM   4868 C CD2   . TYR C 1 46  ? 5.319   -7.072  -17.850 1.00 27.15 ?  38  TYR B CD2   1 
ATOM   4869 C CE1   . TYR C 1 46  ? 5.506   -4.548  -16.749 1.00 27.68 ?  38  TYR B CE1   1 
ATOM   4870 C CE2   . TYR C 1 46  ? 4.618   -6.769  -16.698 1.00 28.63 ?  38  TYR B CE2   1 
ATOM   4871 C CZ    . TYR C 1 46  ? 4.715   -5.506  -16.152 1.00 27.02 ?  38  TYR B CZ    1 
ATOM   4872 O OH    . TYR C 1 46  ? 4.016   -5.205  -15.005 1.00 24.96 ?  38  TYR B OH    1 
ATOM   4873 N N     . GLN C 1 47  ? 9.669   -5.282  -18.012 1.00 27.68 ?  39  GLN B N     1 
ATOM   4874 C CA    . GLN C 1 47  ? 10.455  -4.119  -17.622 1.00 27.71 ?  39  GLN B CA    1 
ATOM   4875 C C     . GLN C 1 47  ? 11.776  -4.031  -18.369 1.00 27.53 ?  39  GLN B C     1 
ATOM   4876 O O     . GLN C 1 47  ? 12.452  -3.001  -18.276 1.00 31.61 ?  39  GLN B O     1 
ATOM   4877 C CB    . GLN C 1 47  ? 10.713  -4.140  -16.114 1.00 30.41 ?  39  GLN B CB    1 
ATOM   4878 C CG    . GLN C 1 47  ? 9.533   -3.683  -15.269 1.00 30.20 ?  39  GLN B CG    1 
ATOM   4879 C CD    . GLN C 1 47  ? 9.048   -2.296  -15.646 1.00 31.33 ?  39  GLN B CD    1 
ATOM   4880 O OE1   . GLN C 1 47  ? 8.204   -2.137  -16.530 1.00 29.03 ?  39  GLN B OE1   1 
ATOM   4881 N NE2   . GLN C 1 47  ? 9.585   -1.281  -14.977 1.00 31.47 ?  39  GLN B NE2   1 
ATOM   4882 N N     . ASN C 1 48  ? 12.161  -5.082  -19.088 1.00 28.75 ?  40  ASN B N     1 
ATOM   4883 C CA    . ASN C 1 48  ? 13.319  -5.009  -19.961 1.00 25.09 ?  40  ASN B CA    1 
ATOM   4884 C C     . ASN C 1 48  ? 13.116  -3.892  -20.984 1.00 28.09 ?  40  ASN B C     1 
ATOM   4885 O O     . ASN C 1 48  ? 11.986  -3.630  -21.408 1.00 29.18 ?  40  ASN B O     1 
ATOM   4886 C CB    . ASN C 1 48  ? 13.536  -6.343  -20.670 1.00 24.50 ?  40  ASN B CB    1 
ATOM   4887 C CG    . ASN C 1 48  ? 14.096  -7.401  -19.750 1.00 28.49 ?  40  ASN B CG    1 
ATOM   4888 O OD1   . ASN C 1 48  ? 15.109  -7.186  -19.087 1.00 24.15 ?  40  ASN B OD1   1 
ATOM   4889 N ND2   . ASN C 1 48  ? 13.436  -8.551  -19.696 1.00 26.95 ?  40  ASN B ND2   1 
ATOM   4890 N N     . PRO C 1 49  ? 14.192  -3.217  -21.396 1.00 27.13 ?  41  PRO B N     1 
ATOM   4891 C CA    . PRO C 1 49  ? 14.027  -2.048  -22.275 1.00 26.06 ?  41  PRO B CA    1 
ATOM   4892 C C     . PRO C 1 49  ? 13.323  -2.359  -23.587 1.00 24.13 ?  41  PRO B C     1 
ATOM   4893 O O     . PRO C 1 49  ? 12.634  -1.486  -24.129 1.00 26.42 ?  41  PRO B O     1 
ATOM   4894 C CB    . PRO C 1 49  ? 15.470  -1.581  -22.505 1.00 23.74 ?  41  PRO B CB    1 
ATOM   4895 C CG    . PRO C 1 49  ? 16.306  -2.796  -22.246 1.00 25.07 ?  41  PRO B CG    1 
ATOM   4896 C CD    . PRO C 1 49  ? 15.609  -3.507  -21.128 1.00 23.40 ?  41  PRO B CD    1 
ATOM   4897 N N     . GLY C 1 50  ? 13.473  -3.571  -24.122 1.00 24.26 ?  42  GLY B N     1 
ATOM   4898 C CA    . GLY C 1 50  ? 12.722  -3.940  -25.307 1.00 26.64 ?  42  GLY B CA    1 
ATOM   4899 C C     . GLY C 1 50  ? 11.310  -4.403  -25.038 1.00 26.48 ?  42  GLY B C     1 
ATOM   4900 O O     . GLY C 1 50  ? 10.548  -4.620  -25.986 1.00 21.55 ?  42  GLY B O     1 
ATOM   4901 N N     . GLY C 1 51  ? 10.953  -4.579  -23.770 1.00 26.71 ?  43  GLY B N     1 
ATOM   4902 C CA    . GLY C 1 51  ? 9.584   -4.849  -23.385 1.00 24.91 ?  43  GLY B CA    1 
ATOM   4903 C C     . GLY C 1 51  ? 9.215   -6.295  -23.135 1.00 27.33 ?  43  GLY B C     1 
ATOM   4904 O O     . GLY C 1 51  ? 8.028   -6.578  -22.946 1.00 22.33 ?  43  GLY B O     1 
ATOM   4905 N N     . SER C 1 52  ? 10.177  -7.216  -23.120 1.00 27.05 ?  44  SER B N     1 
ATOM   4906 C CA    . SER C 1 52  ? 9.854   -8.619  -22.893 1.00 27.40 ?  44  SER B CA    1 
ATOM   4907 C C     . SER C 1 52  ? 11.107  -9.365  -22.456 1.00 28.72 ?  44  SER B C     1 
ATOM   4908 O O     . SER C 1 52  ? 12.221  -8.839  -22.505 1.00 26.26 ?  44  SER B O     1 
ATOM   4909 C CB    . SER C 1 52  ? 9.256   -9.272  -24.143 1.00 25.43 ?  44  SER B CB    1 
ATOM   4910 O OG    . SER C 1 52  ? 10.262  -9.915  -24.904 1.00 28.75 ?  44  SER B OG    1 
ATOM   4911 N N     . VAL C 1 53  ? 10.904  -10.615 -22.047 1.00 25.18 ?  45  VAL B N     1 
ATOM   4912 C CA    . VAL C 1 53  ? 11.976  -11.474 -21.555 1.00 24.04 ?  45  VAL B CA    1 
ATOM   4913 C C     . VAL C 1 53  ? 12.962  -11.808 -22.674 1.00 27.00 ?  45  VAL B C     1 
ATOM   4914 O O     . VAL C 1 53  ? 14.122  -12.140 -22.417 1.00 24.53 ?  45  VAL B O     1 
ATOM   4915 C CB    . VAL C 1 53  ? 11.393  -12.762 -20.927 1.00 23.70 ?  45  VAL B CB    1 
ATOM   4916 C CG1   . VAL C 1 53  ? 10.658  -13.586 -21.977 1.00 24.13 ?  45  VAL B CG1   1 
ATOM   4917 C CG2   . VAL C 1 53  ? 12.482  -13.583 -20.245 1.00 24.37 ?  45  VAL B CG2   1 
HETATM 4918 N N1    . LLP C 1 54  ? 5.610   -15.601 -22.947 0.97 25.97 ?  46  LLP B N1    1 
HETATM 4919 C C2    . LLP C 1 54  ? 5.991   -14.785 -23.931 0.97 26.44 ?  46  LLP B C2    1 
HETATM 4920 C "C2'" . LLP C 1 54  ? 5.163   -13.504 -24.237 0.97 28.93 ?  46  LLP B "C2'" 1 
HETATM 4921 C C3    . LLP C 1 54  ? 7.149   -15.085 -24.700 0.97 27.48 ?  46  LLP B C3    1 
HETATM 4922 O O3    . LLP C 1 54  ? 7.530   -14.214 -25.728 0.97 28.75 ?  46  LLP B O3    1 
HETATM 4923 C C4    . LLP C 1 54  ? 7.886   -16.219 -24.429 0.97 29.66 ?  46  LLP B C4    1 
HETATM 4924 C "C4'" . LLP C 1 54  ? 9.197   -16.556 -25.312 0.97 31.02 ?  46  LLP B "C4'" 1 
HETATM 4925 C C5    . LLP C 1 54  ? 7.498   -17.054 -23.422 0.97 26.64 ?  46  LLP B C5    1 
HETATM 4926 C C6    . LLP C 1 54  ? 6.354   -16.754 -22.668 0.97 25.79 ?  46  LLP B C6    1 
HETATM 4927 C "C5'" . LLP C 1 54  ? 8.299   -18.351 -23.086 0.97 27.17 ?  46  LLP B "C5'" 1 
HETATM 4928 O OP4   . LLP C 1 54  ? 9.584   -18.052 -22.585 0.97 27.46 ?  46  LLP B OP4   1 
HETATM 4929 P P     . LLP C 1 54  ? 10.694  -19.096 -22.837 0.97 29.22 ?  46  LLP B P     1 
HETATM 4930 O OP1   . LLP C 1 54  ? 11.074  -19.075 -24.323 0.97 21.37 ?  46  LLP B OP1   1 
HETATM 4931 O OP2   . LLP C 1 54  ? 10.192  -20.439 -22.474 0.97 24.72 ?  46  LLP B OP2   1 
HETATM 4932 O OP3   . LLP C 1 54  ? 11.894  -18.780 -22.010 0.97 24.19 ?  46  LLP B OP3   1 
HETATM 4933 N N     . LLP C 1 54  ? 12.499  -11.695 -23.916 0.97 24.32 ?  46  LLP B N     1 
HETATM 4934 C CA    . LLP C 1 54  ? 13.310  -12.047 -25.094 0.97 23.84 ?  46  LLP B CA    1 
HETATM 4935 C CB    . LLP C 1 54  ? 12.454  -11.987 -26.335 0.97 26.09 ?  46  LLP B CB    1 
HETATM 4936 C CG    . LLP C 1 54  ? 11.437  -13.132 -26.331 0.97 22.53 ?  46  LLP B CG    1 
HETATM 4937 C CD    . LLP C 1 54  ? 12.109  -14.442 -25.884 0.97 22.90 ?  46  LLP B CD    1 
HETATM 4938 C CE    . LLP C 1 54  ? 11.187  -15.638 -26.201 0.97 31.80 ?  46  LLP B CE    1 
HETATM 4939 N NZ    . LLP C 1 54  ? 9.817   -15.344 -25.752 0.97 26.16 ?  46  LLP B NZ    1 
HETATM 4940 C C     . LLP C 1 54  ? 14.498  -11.156 -25.249 0.97 26.31 ?  46  LLP B C     1 
HETATM 4941 O O     . LLP C 1 54  ? 15.411  -11.490 -25.989 0.97 25.25 ?  46  LLP B O     1 
ATOM   4942 N N     . ASP C 1 55  ? 14.490  -10.015 -24.564 1.00 26.51 ?  47  ASP B N     1 
ATOM   4943 C CA    . ASP C 1 55  ? 15.644  -9.120  -24.536 1.00 23.50 ?  47  ASP B CA    1 
ATOM   4944 C C     . ASP C 1 55  ? 16.901  -9.857  -24.090 1.00 26.17 ?  47  ASP B C     1 
ATOM   4945 O O     . ASP C 1 55  ? 17.976  -9.677  -24.661 1.00 25.91 ?  47  ASP B O     1 
ATOM   4946 C CB    . ASP C 1 55  ? 15.396  -7.941  -23.594 1.00 24.42 ?  47  ASP B CB    1 
ATOM   4947 C CG    . ASP C 1 55  ? 14.631  -6.814  -24.250 1.00 27.70 ?  47  ASP B CG    1 
ATOM   4948 O OD1   . ASP C 1 55  ? 13.996  -7.042  -25.300 1.00 30.90 ?  47  ASP B OD1   1 
ATOM   4949 O OD2   . ASP C 1 55  ? 14.677  -5.688  -23.711 1.00 25.49 ?  47  ASP B OD2   1 
ATOM   4950 N N     . ARG C 1 56  ? 16.751  -10.686 -23.056 1.00 28.10 ?  48  ARG B N     1 
ATOM   4951 C CA    . ARG C 1 56  ? 17.899  -11.384 -22.487 1.00 26.41 ?  48  ARG B CA    1 
ATOM   4952 C C     . ARG C 1 56  ? 18.523  -12.338 -23.497 1.00 27.94 ?  48  ARG B C     1 
ATOM   4953 O O     . ARG C 1 56  ? 19.747  -12.363 -23.671 1.00 22.45 ?  48  ARG B O     1 
ATOM   4954 C CB    . ARG C 1 56  ? 17.477  -12.141 -21.229 1.00 22.88 ?  48  ARG B CB    1 
ATOM   4955 C CG    . ARG C 1 56  ? 16.781  -11.294 -20.182 1.00 25.95 ?  48  ARG B CG    1 
ATOM   4956 C CD    . ARG C 1 56  ? 16.499  -12.125 -18.941 1.00 26.99 ?  48  ARG B CD    1 
ATOM   4957 N NE    . ARG C 1 56  ? 15.832  -11.366 -17.890 1.00 28.82 ?  48  ARG B NE    1 
ATOM   4958 C CZ    . ARG C 1 56  ? 16.431  -10.919 -16.796 1.00 26.86 ?  48  ARG B CZ    1 
ATOM   4959 N NH1   . ARG C 1 56  ? 17.719  -11.128 -16.580 1.00 27.27 ?  48  ARG B NH1   1 
ATOM   4960 N NH2   . ARG C 1 56  ? 15.721  -10.246 -15.895 1.00 22.39 ?  48  ARG B NH2   1 
ATOM   4961 N N     . ILE C 1 57  ? 17.695  -13.138 -24.171 1.00 22.93 ?  49  ILE B N     1 
ATOM   4962 C CA    . ILE C 1 57  ? 18.237  -14.140 -25.081 1.00 24.33 ?  49  ILE B CA    1 
ATOM   4963 C C     . ILE C 1 57  ? 18.656  -13.516 -26.409 1.00 26.06 ?  49  ILE B C     1 
ATOM   4964 O O     . ILE C 1 57  ? 19.549  -14.038 -27.086 1.00 24.32 ?  49  ILE B O     1 
ATOM   4965 C CB    . ILE C 1 57  ? 17.227  -15.284 -25.282 1.00 25.97 ?  49  ILE B CB    1 
ATOM   4966 C CG1   . ILE C 1 57  ? 16.115  -14.873 -26.249 1.00 25.87 ?  49  ILE B CG1   1 
ATOM   4967 C CG2   . ILE C 1 57  ? 16.637  -15.701 -23.944 1.00 17.80 ?  49  ILE B CG2   1 
ATOM   4968 C CD1   . ILE C 1 57  ? 15.290  -16.036 -26.746 1.00 24.11 ?  49  ILE B CD1   1 
ATOM   4969 N N     . ALA C 1 58  ? 18.041  -12.397 -26.802 1.00 23.45 ?  50  ALA B N     1 
ATOM   4970 C CA    . ALA C 1 58  ? 18.468  -11.721 -28.022 1.00 23.74 ?  50  ALA B CA    1 
ATOM   4971 C C     . ALA C 1 58  ? 19.885  -11.180 -27.882 1.00 26.32 ?  50  ALA B C     1 
ATOM   4972 O O     . ALA C 1 58  ? 20.696  -11.292 -28.809 1.00 28.20 ?  50  ALA B O     1 
ATOM   4973 C CB    . ALA C 1 58  ? 17.494  -10.595 -28.369 1.00 22.95 ?  50  ALA B CB    1 
ATOM   4974 N N     . LEU C 1 59  ? 20.202  -10.593 -26.726 1.00 24.06 ?  51  LEU B N     1 
ATOM   4975 C CA    . LEU C 1 59  ? 21.550  -10.082 -26.500 1.00 24.58 ?  51  LEU B CA    1 
ATOM   4976 C C     . LEU C 1 59  ? 22.544  -11.219 -26.298 1.00 25.22 ?  51  LEU B C     1 
ATOM   4977 O O     . LEU C 1 59  ? 23.654  -11.191 -26.844 1.00 28.93 ?  51  LEU B O     1 
ATOM   4978 C CB    . LEU C 1 59  ? 21.560  -9.141  -25.295 1.00 26.19 ?  51  LEU B CB    1 
ATOM   4979 C CG    . LEU C 1 59  ? 22.938  -8.638  -24.851 1.00 29.53 ?  51  LEU B CG    1 
ATOM   4980 C CD1   . LEU C 1 59  ? 23.513  -7.659  -25.865 1.00 25.36 ?  51  LEU B CD1   1 
ATOM   4981 C CD2   . LEU C 1 59  ? 22.867  -8.006  -23.468 1.00 26.11 ?  51  LEU B CD2   1 
ATOM   4982 N N     . ALA C 1 60  ? 22.162  -12.230 -25.515 1.00 25.17 ?  52  ALA B N     1 
ATOM   4983 C CA    . ALA C 1 60  ? 23.074  -13.332 -25.228 1.00 27.27 ?  52  ALA B CA    1 
ATOM   4984 C C     . ALA C 1 60  ? 23.423  -14.108 -26.491 1.00 29.35 ?  52  ALA B C     1 
ATOM   4985 O O     . ALA C 1 60  ? 24.577  -14.506 -26.684 1.00 30.80 ?  52  ALA B O     1 
ATOM   4986 C CB    . ALA C 1 60  ? 22.463  -14.261 -24.182 1.00 22.89 ?  52  ALA B CB    1 
ATOM   4987 N N     . MET C 1 61  ? 22.442  -14.330 -27.366 1.00 27.64 ?  53  MET B N     1 
ATOM   4988 C CA    . MET C 1 61  ? 22.710  -15.092 -28.580 1.00 29.49 ?  53  MET B CA    1 
ATOM   4989 C C     . MET C 1 61  ? 23.635  -14.321 -29.515 1.00 27.55 ?  53  MET B C     1 
ATOM   4990 O O     . MET C 1 61  ? 24.513  -14.914 -30.153 1.00 25.89 ?  53  MET B O     1 
ATOM   4991 C CB    . MET C 1 61  ? 21.395  -15.449 -29.275 1.00 23.90 ?  53  MET B CB    1 
ATOM   4992 C CG    . MET C 1 61  ? 20.770  -16.737 -28.751 1.00 30.42 ?  53  MET B CG    1 
ATOM   4993 S SD    . MET C 1 61  ? 19.315  -17.263 -29.676 1.00 29.73 ?  53  MET B SD    1 
ATOM   4994 C CE    . MET C 1 61  ? 18.182  -15.928 -29.307 1.00 24.61 ?  53  MET B CE    1 
ATOM   4995 N N     . ILE C 1 62  ? 23.463  -12.999 -29.599 1.00 26.28 ?  54  ILE B N     1 
ATOM   4996 C CA    . ILE C 1 62  ? 24.357  -12.180 -30.412 1.00 27.88 ?  54  ILE B CA    1 
ATOM   4997 C C     . ILE C 1 62  ? 25.746  -12.130 -29.786 1.00 27.98 ?  54  ILE B C     1 
ATOM   4998 O O     . ILE C 1 62  ? 26.762  -12.239 -30.484 1.00 26.18 ?  54  ILE B O     1 
ATOM   4999 C CB    . ILE C 1 62  ? 23.768  -10.769 -30.597 1.00 25.91 ?  54  ILE B CB    1 
ATOM   5000 C CG1   . ILE C 1 62  ? 22.567  -10.801 -31.545 1.00 29.85 ?  54  ILE B CG1   1 
ATOM   5001 C CG2   . ILE C 1 62  ? 24.823  -9.813  -31.126 1.00 26.86 ?  54  ILE B CG2   1 
ATOM   5002 C CD1   . ILE C 1 62  ? 22.917  -11.155 -32.979 1.00 27.04 ?  54  ILE B CD1   1 
ATOM   5003 N N     . GLU C 1 63  ? 25.812  -11.978 -28.461 1.00 29.27 ?  55  GLU B N     1 
ATOM   5004 C CA    . GLU C 1 63  ? 27.101  -11.907 -27.781 1.00 25.43 ?  55  GLU B CA    1 
ATOM   5005 C C     . GLU C 1 63  ? 27.872  -13.215 -27.909 1.00 30.42 ?  55  GLU B C     1 
ATOM   5006 O O     . GLU C 1 63  ? 29.099  -13.204 -28.057 1.00 32.21 ?  55  GLU B O     1 
ATOM   5007 C CB    . GLU C 1 63  ? 26.897  -11.551 -26.310 1.00 27.91 ?  55  GLU B CB    1 
ATOM   5008 C CG    . GLU C 1 63  ? 26.693  -10.072 -26.059 1.00 26.79 ?  55  GLU B CG    1 
ATOM   5009 C CD    . GLU C 1 63  ? 26.410  -9.768  -24.604 1.00 33.49 ?  55  GLU B CD    1 
ATOM   5010 O OE1   . GLU C 1 63  ? 26.152  -10.717 -23.833 1.00 33.81 ?  55  GLU B OE1   1 
ATOM   5011 O OE2   . GLU C 1 63  ? 26.442  -8.576  -24.232 1.00 36.18 ?  55  GLU B OE2   1 
ATOM   5012 N N     . LYS C 1 64  ? 27.172  -14.351 -27.852 1.00 28.66 ?  56  LYS B N     1 
ATOM   5013 C CA    . LYS C 1 64  ? 27.847  -15.638 -27.991 1.00 28.62 ?  56  LYS B CA    1 
ATOM   5014 C C     . LYS C 1 64  ? 28.475  -15.782 -29.372 1.00 32.83 ?  56  LYS B C     1 
ATOM   5015 O O     . LYS C 1 64  ? 29.611  -16.253 -29.501 1.00 32.91 ?  56  LYS B O     1 
ATOM   5016 C CB    . LYS C 1 64  ? 26.866  -16.780 -27.729 1.00 25.74 ?  56  LYS B CB    1 
ATOM   5017 C CG    . LYS C 1 64  ? 27.470  -18.170 -27.885 1.00 32.75 ?  56  LYS B CG    1 
ATOM   5018 C CD    . LYS C 1 64  ? 26.501  -19.252 -27.432 1.00 39.22 ?  56  LYS B CD    1 
ATOM   5019 C CE    . LYS C 1 64  ? 26.945  -20.635 -27.885 1.00 36.82 ?  56  LYS B CE    1 
ATOM   5020 N NZ    . LYS C 1 64  ? 26.245  -21.057 -29.132 1.00 41.02 ?  56  LYS B NZ    1 
ATOM   5021 N N     . ALA C 1 65  ? 27.749  -15.383 -30.418 1.00 30.10 ?  57  ALA B N     1 
ATOM   5022 C CA    . ALA C 1 65  ? 28.311  -15.442 -31.762 1.00 34.64 ?  57  ALA B CA    1 
ATOM   5023 C C     . ALA C 1 65  ? 29.458  -14.455 -31.929 1.00 34.45 ?  57  ALA B C     1 
ATOM   5024 O O     . ALA C 1 65  ? 30.398  -14.723 -32.685 1.00 33.80 ?  57  ALA B O     1 
ATOM   5025 C CB    . ALA C 1 65  ? 27.222  -15.183 -32.802 1.00 29.30 ?  57  ALA B CB    1 
ATOM   5026 N N     . GLU C 1 66  ? 29.404  -13.318 -31.233 1.00 31.13 ?  58  GLU B N     1 
ATOM   5027 C CA    . GLU C 1 66  ? 30.514  -12.372 -31.281 1.00 36.09 ?  58  GLU B CA    1 
ATOM   5028 C C     . GLU C 1 66  ? 31.750  -12.946 -30.602 1.00 34.73 ?  58  GLU B C     1 
ATOM   5029 O O     . GLU C 1 66  ? 32.861  -12.864 -31.138 1.00 34.99 ?  58  GLU B O     1 
ATOM   5030 C CB    . GLU C 1 66  ? 30.109  -11.051 -30.629 1.00 34.61 ?  58  GLU B CB    1 
ATOM   5031 C CG    . GLU C 1 66  ? 29.172  -10.206 -31.462 1.00 33.66 ?  58  GLU B CG    1 
ATOM   5032 C CD    . GLU C 1 66  ? 28.803  -8.909  -30.773 1.00 34.24 ?  58  GLU B CD    1 
ATOM   5033 O OE1   . GLU C 1 66  ? 28.746  -8.897  -29.525 1.00 32.22 ?  58  GLU B OE1   1 
ATOM   5034 O OE2   . GLU C 1 66  ? 28.575  -7.901  -31.476 1.00 36.83 ?  58  GLU B OE2   1 
ATOM   5035 N N     . ARG C 1 67  ? 31.572  -13.539 -29.417 1.00 33.76 ?  59  ARG B N     1 
ATOM   5036 C CA    . ARG C 1 67  ? 32.702  -14.108 -28.690 1.00 33.61 ?  59  ARG B CA    1 
ATOM   5037 C C     . ARG C 1 67  ? 33.337  -15.264 -29.450 1.00 38.95 ?  59  ARG B C     1 
ATOM   5038 O O     . ARG C 1 67  ? 34.529  -15.541 -29.276 1.00 35.54 ?  59  ARG B O     1 
ATOM   5039 C CB    . ARG C 1 67  ? 32.249  -14.568 -27.306 1.00 35.20 ?  59  ARG B CB    1 
ATOM   5040 C CG    . ARG C 1 67  ? 32.468  -13.538 -26.216 1.00 38.78 ?  59  ARG B CG    1 
ATOM   5041 C CD    . ARG C 1 67  ? 32.222  -14.123 -24.833 1.00 48.21 ?  59  ARG B CD    1 
ATOM   5042 N NE    . ARG C 1 67  ? 30.812  -14.403 -24.590 1.00 44.82 ?  59  ARG B NE    1 
ATOM   5043 C CZ    . ARG C 1 67  ? 30.276  -15.617 -24.587 1.00 50.01 ?  59  ARG B CZ    1 
ATOM   5044 N NH1   . ARG C 1 67  ? 31.008  -16.698 -24.806 1.00 48.23 ?  59  ARG B NH1   1 
ATOM   5045 N NH2   . ARG C 1 67  ? 28.974  -15.751 -24.350 1.00 47.06 ?  59  ARG B NH2   1 
ATOM   5046 N N     . GLU C 1 68  ? 32.562  -15.949 -30.290 1.00 34.58 ?  60  GLU B N     1 
ATOM   5047 C CA    . GLU C 1 68  ? 33.064  -17.057 -31.088 1.00 31.76 ?  60  GLU B CA    1 
ATOM   5048 C C     . GLU C 1 68  ? 33.556  -16.628 -32.463 1.00 33.73 ?  60  GLU B C     1 
ATOM   5049 O O     . GLU C 1 68  ? 34.093  -17.463 -33.199 1.00 39.61 ?  60  GLU B O     1 
ATOM   5050 C CB    . GLU C 1 68  ? 31.975  -18.123 -31.247 1.00 36.20 ?  60  GLU B CB    1 
ATOM   5051 C CG    . GLU C 1 68  ? 31.652  -18.863 -29.961 1.00 33.24 ?  60  GLU B CG    1 
ATOM   5052 C CD    . GLU C 1 68  ? 30.271  -19.485 -29.974 1.00 34.36 ?  60  GLU B CD    1 
ATOM   5053 O OE1   . GLU C 1 68  ? 29.604  -19.447 -31.031 1.00 31.84 ?  60  GLU B OE1   1 
ATOM   5054 O OE2   . GLU C 1 68  ? 29.848  -20.005 -28.922 1.00 32.07 ?  60  GLU B OE2   1 
ATOM   5055 N N     . GLY C 1 69  ? 33.390  -15.359 -32.827 1.00 33.62 ?  61  GLY B N     1 
ATOM   5056 C CA    . GLY C 1 69  ? 33.832  -14.885 -34.121 1.00 34.47 ?  61  GLY B CA    1 
ATOM   5057 C C     . GLY C 1 69  ? 32.948  -15.267 -35.284 1.00 35.29 ?  61  GLY B C     1 
ATOM   5058 O O     . GLY C 1 69  ? 33.372  -15.123 -36.436 1.00 34.23 ?  61  GLY B O     1 
ATOM   5059 N N     . LYS C 1 70  ? 31.732  -15.755 -35.026 1.00 34.92 ?  62  LYS B N     1 
ATOM   5060 C CA    . LYS C 1 70  ? 30.850  -16.121 -36.128 1.00 30.48 ?  62  LYS B CA    1 
ATOM   5061 C C     . LYS C 1 70  ? 30.269  -14.892 -36.813 1.00 32.36 ?  62  LYS B C     1 
ATOM   5062 O O     . LYS C 1 70  ? 29.984  -14.932 -38.015 1.00 33.73 ?  62  LYS B O     1 
ATOM   5063 C CB    . LYS C 1 70  ? 29.732  -17.032 -35.625 1.00 28.83 ?  62  LYS B CB    1 
ATOM   5064 C CG    . LYS C 1 70  ? 30.226  -18.312 -34.976 1.00 30.73 ?  62  LYS B CG    1 
ATOM   5065 C CD    . LYS C 1 70  ? 29.065  -19.150 -34.476 1.00 28.26 ?  62  LYS B CD    1 
ATOM   5066 C CE    . LYS C 1 70  ? 29.406  -20.630 -34.480 1.00 30.34 ?  62  LYS B CE    1 
ATOM   5067 N NZ    . LYS C 1 70  ? 30.165  -21.032 -33.264 1.00 35.85 ?  62  LYS B NZ    1 
ATOM   5068 N N     . ILE C 1 71  ? 30.084  -13.799 -36.075 1.00 28.59 ?  63  ILE B N     1 
ATOM   5069 C CA    . ILE C 1 71  ? 29.537  -12.570 -36.632 1.00 30.96 ?  63  ILE B CA    1 
ATOM   5070 C C     . ILE C 1 71  ? 30.314  -11.381 -36.089 1.00 31.32 ?  63  ILE B C     1 
ATOM   5071 O O     . ILE C 1 71  ? 30.906  -11.436 -35.008 1.00 25.48 ?  63  ILE B O     1 
ATOM   5072 C CB    . ILE C 1 71  ? 28.032  -12.399 -36.322 1.00 31.66 ?  63  ILE B CB    1 
ATOM   5073 C CG1   . ILE C 1 71  ? 27.811  -12.216 -34.818 1.00 25.75 ?  63  ILE B CG1   1 
ATOM   5074 C CG2   . ILE C 1 71  ? 27.231  -13.566 -36.860 1.00 25.23 ?  63  ILE B CG2   1 
ATOM   5075 C CD1   . ILE C 1 71  ? 26.371  -11.952 -34.443 1.00 31.09 ?  63  ILE B CD1   1 
ATOM   5076 N N     . LYS C 1 72  ? 30.301  -10.302 -36.859 1.00 31.59 ?  64  LYS B N     1 
ATOM   5077 C CA    . LYS C 1 72  ? 30.832  -9.008  -36.474 1.00 32.84 ?  64  LYS B CA    1 
ATOM   5078 C C     . LYS C 1 72  ? 29.808  -7.947  -36.846 1.00 35.13 ?  64  LYS B C     1 
ATOM   5079 O O     . LYS C 1 72  ? 28.993  -8.165  -37.748 1.00 33.11 ?  64  LYS B O     1 
ATOM   5080 C CB    . LYS C 1 72  ? 32.167  -8.717  -37.174 1.00 28.66 ?  64  LYS B CB    1 
ATOM   5081 N N     . PRO C 1 73  ? 29.802  -6.809  -36.150 1.00 31.91 ?  65  PRO B N     1 
ATOM   5082 C CA    . PRO C 1 73  ? 28.838  -5.750  -36.476 1.00 30.86 ?  65  PRO B CA    1 
ATOM   5083 C C     . PRO C 1 73  ? 28.834  -5.432  -37.965 1.00 35.09 ?  65  PRO B C     1 
ATOM   5084 O O     . PRO C 1 73  ? 29.883  -5.356  -38.606 1.00 33.47 ?  65  PRO B O     1 
ATOM   5085 C CB    . PRO C 1 73  ? 29.328  -4.563  -35.642 1.00 32.02 ?  65  PRO B CB    1 
ATOM   5086 C CG    . PRO C 1 73  ? 29.952  -5.197  -34.449 1.00 30.86 ?  65  PRO B CG    1 
ATOM   5087 C CD    . PRO C 1 73  ? 30.556  -6.505  -34.918 1.00 27.85 ?  65  PRO B CD    1 
ATOM   5088 N N     . GLY C 1 74  ? 27.632  -5.270  -38.514 1.00 32.09 ?  66  GLY B N     1 
ATOM   5089 C CA    . GLY C 1 74  ? 27.447  -5.115  -39.937 1.00 29.20 ?  66  GLY B CA    1 
ATOM   5090 C C     . GLY C 1 74  ? 26.968  -6.364  -40.645 1.00 31.57 ?  66  GLY B C     1 
ATOM   5091 O O     . GLY C 1 74  ? 26.535  -6.274  -41.801 1.00 36.75 ?  66  GLY B O     1 
ATOM   5092 N N     . ASP C 1 75  ? 27.028  -7.519  -39.989 1.00 30.31 ?  67  ASP B N     1 
ATOM   5093 C CA    . ASP C 1 75  ? 26.557  -8.760  -40.579 1.00 27.01 ?  67  ASP B CA    1 
ATOM   5094 C C     . ASP C 1 75  ? 25.036  -8.846  -40.506 1.00 30.13 ?  67  ASP B C     1 
ATOM   5095 O O     . ASP C 1 75  ? 24.371  -8.087  -39.796 1.00 30.86 ?  67  ASP B O     1 
ATOM   5096 C CB    . ASP C 1 75  ? 27.184  -9.965  -39.876 1.00 27.81 ?  67  ASP B CB    1 
ATOM   5097 C CG    . ASP C 1 75  ? 28.676  -10.063 -40.111 1.00 33.02 ?  67  ASP B CG    1 
ATOM   5098 O OD1   . ASP C 1 75  ? 29.180  -9.357  -41.008 1.00 32.64 ?  67  ASP B OD1   1 
ATOM   5099 O OD2   . ASP C 1 75  ? 29.345  -10.843 -39.401 1.00 32.24 ?  67  ASP B OD2   1 
ATOM   5100 N N     . THR C 1 76  ? 24.487  -9.800  -41.250 1.00 28.49 ?  68  THR B N     1 
ATOM   5101 C CA    . THR C 1 76  ? 23.051  -10.035 -41.294 1.00 32.27 ?  68  THR B CA    1 
ATOM   5102 C C     . THR C 1 76  ? 22.709  -11.265 -40.466 1.00 27.41 ?  68  THR B C     1 
ATOM   5103 O O     . THR C 1 76  ? 23.367  -12.304 -40.584 1.00 27.07 ?  68  THR B O     1 
ATOM   5104 C CB    . THR C 1 76  ? 22.568  -10.223 -42.733 1.00 33.61 ?  68  THR B CB    1 
ATOM   5105 O OG1   . THR C 1 76  ? 22.787  -9.018  -43.477 1.00 33.15 ?  68  THR B OG1   1 
ATOM   5106 C CG2   . THR C 1 76  ? 21.082  -10.569 -42.759 1.00 31.93 ?  68  THR B CG2   1 
ATOM   5107 N N     . ILE C 1 77  ? 21.686  -11.144 -39.627 1.00 31.20 ?  69  ILE B N     1 
ATOM   5108 C CA    . ILE C 1 77  ? 21.146  -12.272 -38.884 1.00 28.38 ?  69  ILE B CA    1 
ATOM   5109 C C     . ILE C 1 77  ? 19.718  -12.510 -39.356 1.00 28.27 ?  69  ILE B C     1 
ATOM   5110 O O     . ILE C 1 77  ? 18.986  -11.562 -39.661 1.00 33.41 ?  69  ILE B O     1 
ATOM   5111 C CB    . ILE C 1 77  ? 21.215  -12.047 -37.355 1.00 34.50 ?  69  ILE B CB    1 
ATOM   5112 C CG1   . ILE C 1 77  ? 20.153  -11.056 -36.878 1.00 38.92 ?  69  ILE B CG1   1 
ATOM   5113 C CG2   . ILE C 1 77  ? 22.603  -11.568 -36.948 1.00 29.74 ?  69  ILE B CG2   1 
ATOM   5114 C CD1   . ILE C 1 77  ? 18.983  -11.711 -36.178 1.00 40.19 ?  69  ILE B CD1   1 
ATOM   5115 N N     . VAL C 1 78  ? 19.339  -13.781 -39.455 1.00 27.65 ?  70  VAL B N     1 
ATOM   5116 C CA    . VAL C 1 78  ? 18.016  -14.170 -39.923 1.00 29.21 ?  70  VAL B CA    1 
ATOM   5117 C C     . VAL C 1 78  ? 17.421  -15.163 -38.934 1.00 27.86 ?  70  VAL B C     1 
ATOM   5118 O O     . VAL C 1 78  ? 18.122  -16.043 -38.422 1.00 26.83 ?  70  VAL B O     1 
ATOM   5119 C CB    . VAL C 1 78  ? 18.062  -14.757 -41.354 1.00 30.49 ?  70  VAL B CB    1 
ATOM   5120 C CG1   . VAL C 1 78  ? 18.871  -16.048 -41.396 1.00 26.12 ?  70  VAL B CG1   1 
ATOM   5121 C CG2   . VAL C 1 78  ? 16.653  -14.974 -41.891 1.00 26.86 ?  70  VAL B CG2   1 
ATOM   5122 N N     . GLU C 1 79  ? 16.128  -15.006 -38.648 1.00 26.84 ?  71  GLU B N     1 
ATOM   5123 C CA    . GLU C 1 79  ? 15.449  -15.867 -37.702 1.00 26.52 ?  71  GLU B CA    1 
ATOM   5124 C C     . GLU C 1 79  ? 13.962  -15.928 -38.019 1.00 27.44 ?  71  GLU B C     1 
ATOM   5125 O O     . GLU C 1 79  ? 13.334  -14.870 -38.191 1.00 27.13 ?  71  GLU B O     1 
ATOM   5126 C CB    . GLU C 1 79  ? 15.647  -15.383 -36.265 1.00 27.85 ?  71  GLU B CB    1 
ATOM   5127 C CG    . GLU C 1 79  ? 14.993  -16.267 -35.218 1.00 25.58 ?  71  GLU B CG    1 
ATOM   5128 C CD    . GLU C 1 79  ? 15.858  -17.448 -34.827 1.00 30.41 ?  71  GLU B CD    1 
ATOM   5129 O OE1   . GLU C 1 79  ? 16.925  -17.640 -35.448 1.00 27.18 ?  71  GLU B OE1   1 
ATOM   5130 O OE2   . GLU C 1 79  ? 15.473  -18.183 -33.893 1.00 31.32 ?  71  GLU B OE2   1 
ATOM   5131 N N     . PRO C 1 80  ? 13.375  -17.124 -38.101 1.00 29.27 ?  72  PRO B N     1 
ATOM   5132 C CA    . PRO C 1 80  ? 11.916  -17.231 -38.251 1.00 26.21 ?  72  PRO B CA    1 
ATOM   5133 C C     . PRO C 1 80  ? 11.244  -17.056 -36.897 1.00 28.93 ?  72  PRO B C     1 
ATOM   5134 O O     . PRO C 1 80  ? 11.465  -17.843 -35.975 1.00 29.63 ?  72  PRO B O     1 
ATOM   5135 C CB    . PRO C 1 80  ? 11.720  -18.647 -38.804 1.00 25.55 ?  72  PRO B CB    1 
ATOM   5136 C CG    . PRO C 1 80  ? 12.900  -19.420 -38.286 1.00 30.40 ?  72  PRO B CG    1 
ATOM   5137 C CD    . PRO C 1 80  ? 14.028  -18.444 -38.029 1.00 28.51 ?  72  PRO B CD    1 
ATOM   5138 N N     . THR C 1 81  ? 10.425  -16.015 -36.774 1.00 29.41 ?  73  THR B N     1 
ATOM   5139 C CA    . THR C 1 81  ? 9.825   -15.690 -35.488 1.00 29.67 ?  73  THR B CA    1 
ATOM   5140 C C     . THR C 1 81  ? 8.526   -14.931 -35.704 1.00 30.63 ?  73  THR B C     1 
ATOM   5141 O O     . THR C 1 81  ? 8.448   -14.048 -36.560 1.00 31.22 ?  73  THR B O     1 
ATOM   5142 C CB    . THR C 1 81  ? 10.782  -14.860 -34.626 1.00 28.97 ?  73  THR B CB    1 
ATOM   5143 O OG1   . THR C 1 81  ? 10.063  -14.286 -33.528 1.00 26.87 ?  73  THR B OG1   1 
ATOM   5144 C CG2   . THR C 1 81  ? 11.425  -13.755 -35.453 1.00 25.54 ?  73  THR B CG2   1 
ATOM   5145 N N     . SER C 1 82  ? 7.513   -15.279 -34.912 1.00 34.29 ?  74  SER B N     1 
ATOM   5146 C CA    . SER C 1 82  ? 6.212   -14.624 -34.967 1.00 37.44 ?  74  SER B CA    1 
ATOM   5147 C C     . SER C 1 82  ? 5.865   -13.943 -33.648 1.00 35.38 ?  74  SER B C     1 
ATOM   5148 O O     . SER C 1 82  ? 4.694   -13.632 -33.408 1.00 35.15 ?  74  SER B O     1 
ATOM   5149 C CB    . SER C 1 82  ? 5.124   -15.632 -35.350 1.00 38.69 ?  74  SER B CB    1 
ATOM   5150 O OG    . SER C 1 82  ? 5.335   -16.876 -34.703 1.00 40.60 ?  74  SER B OG    1 
ATOM   5151 N N     . GLY C 1 83  ? 6.855   -13.699 -32.794 1.00 31.76 ?  75  GLY B N     1 
ATOM   5152 C CA    . GLY C 1 83  ? 6.607   -13.216 -31.441 1.00 28.85 ?  75  GLY B CA    1 
ATOM   5153 C C     . GLY C 1 83  ? 7.692   -12.296 -30.945 1.00 30.13 ?  75  GLY B C     1 
ATOM   5154 O O     . GLY C 1 83  ? 8.270   -11.522 -31.721 1.00 28.86 ?  75  GLY B O     1 
ATOM   5155 N N     . ASN C 1 84  ? 7.984   -12.378 -29.645 1.00 31.68 ?  76  ASN B N     1 
ATOM   5156 C CA    . ASN C 1 84  ? 8.823   -11.378 -28.993 1.00 29.79 ?  76  ASN B CA    1 
ATOM   5157 C C     . ASN C 1 84  ? 10.305  -11.550 -29.302 1.00 28.03 ?  76  ASN B C     1 
ATOM   5158 O O     . ASN C 1 84  ? 11.078  -10.611 -29.085 1.00 28.03 ?  76  ASN B O     1 
ATOM   5159 C CB    . ASN C 1 84  ? 8.597   -11.417 -27.483 1.00 24.75 ?  76  ASN B CB    1 
ATOM   5160 C CG    . ASN C 1 84  ? 7.303   -10.749 -27.073 1.00 29.94 ?  76  ASN B CG    1 
ATOM   5161 O OD1   . ASN C 1 84  ? 6.987   -9.651  -27.522 1.00 33.04 ?  76  ASN B OD1   1 
ATOM   5162 N ND2   . ASN C 1 84  ? 6.535   -11.424 -26.231 1.00 27.35 ?  76  ASN B ND2   1 
ATOM   5163 N N     . THR C 1 85  ? 10.724  -12.721 -29.790 1.00 28.28 ?  77  THR B N     1 
ATOM   5164 C CA    . THR C 1 85  ? 12.117  -12.887 -30.193 1.00 29.31 ?  77  THR B CA    1 
ATOM   5165 C C     . THR C 1 85  ? 12.454  -11.977 -31.368 1.00 31.31 ?  77  THR B C     1 
ATOM   5166 O O     . THR C 1 85  ? 13.560  -11.427 -31.442 1.00 29.23 ?  77  THR B O     1 
ATOM   5167 C CB    . THR C 1 85  ? 12.394  -14.352 -30.538 1.00 31.18 ?  77  THR B CB    1 
ATOM   5168 O OG1   . THR C 1 85  ? 12.273  -15.150 -29.355 1.00 27.90 ?  77  THR B OG1   1 
ATOM   5169 C CG2   . THR C 1 85  ? 13.798  -14.522 -31.101 1.00 29.02 ?  77  THR B CG2   1 
ATOM   5170 N N     . GLY C 1 86  ? 11.504  -11.793 -32.287 1.00 25.92 ?  78  GLY B N     1 
ATOM   5171 C CA    . GLY C 1 86  ? 11.716  -10.852 -33.374 1.00 25.51 ?  78  GLY B CA    1 
ATOM   5172 C C     . GLY C 1 86  ? 11.849  -9.424  -32.885 1.00 28.47 ?  78  GLY B C     1 
ATOM   5173 O O     . GLY C 1 86  ? 12.705  -8.673  -33.359 1.00 27.00 ?  78  GLY B O     1 
ATOM   5174 N N     . ILE C 1 87  ? 11.002  -9.027  -31.933 1.00 26.57 ?  79  ILE B N     1 
ATOM   5175 C CA    . ILE C 1 87  ? 11.118  -7.694  -31.348 1.00 30.65 ?  79  ILE B CA    1 
ATOM   5176 C C     . ILE C 1 87  ? 12.437  -7.559  -30.601 1.00 27.55 ?  79  ILE B C     1 
ATOM   5177 O O     . ILE C 1 87  ? 13.132  -6.542  -30.713 1.00 25.87 ?  79  ILE B O     1 
ATOM   5178 C CB    . ILE C 1 87  ? 9.920   -7.403  -30.425 1.00 31.13 ?  79  ILE B CB    1 
ATOM   5179 C CG1   . ILE C 1 87  ? 8.600   -7.646  -31.163 1.00 30.56 ?  79  ILE B CG1   1 
ATOM   5180 C CG2   . ILE C 1 87  ? 9.986   -5.976  -29.902 1.00 28.02 ?  79  ILE B CG2   1 
ATOM   5181 C CD1   . ILE C 1 87  ? 7.405   -7.788  -30.243 1.00 28.33 ?  79  ILE B CD1   1 
ATOM   5182 N N     . GLY C 1 88  ? 12.805  -8.584  -29.830 1.00 27.92 ?  80  GLY B N     1 
ATOM   5183 C CA    . GLY C 1 88  ? 14.053  -8.525  -29.087 1.00 30.50 ?  80  GLY B CA    1 
ATOM   5184 C C     . GLY C 1 88  ? 15.272  -8.499  -29.988 1.00 25.16 ?  80  GLY B C     1 
ATOM   5185 O O     . GLY C 1 88  ? 16.227  -7.762  -29.733 1.00 24.43 ?  80  GLY B O     1 
ATOM   5186 N N     . LEU C 1 89  ? 15.259  -9.302  -31.054 1.00 24.75 ?  81  LEU B N     1 
ATOM   5187 C CA    . LEU C 1 89  ? 16.400  -9.315  -31.964 1.00 24.83 ?  81  LEU B CA    1 
ATOM   5188 C C     . LEU C 1 89  ? 16.483  -8.023  -32.767 1.00 27.33 ?  81  LEU B C     1 
ATOM   5189 O O     . LEU C 1 89  ? 17.577  -7.489  -32.975 1.00 28.17 ?  81  LEU B O     1 
ATOM   5190 C CB    . LEU C 1 89  ? 16.330  -10.524 -32.895 1.00 23.44 ?  81  LEU B CB    1 
ATOM   5191 C CG    . LEU C 1 89  ? 16.877  -11.830 -32.312 1.00 26.41 ?  81  LEU B CG    1 
ATOM   5192 C CD1   . LEU C 1 89  ? 16.476  -13.015 -33.179 1.00 19.98 ?  81  LEU B CD1   1 
ATOM   5193 C CD2   . LEU C 1 89  ? 18.389  -11.758 -32.149 1.00 16.85 ?  81  LEU B CD2   1 
ATOM   5194 N N     . ALA C 1 90  ? 15.342  -7.505  -33.228 1.00 22.33 ?  82  ALA B N     1 
ATOM   5195 C CA    . ALA C 1 90  ? 15.351  -6.221  -33.923 1.00 25.19 ?  82  ALA B CA    1 
ATOM   5196 C C     . ALA C 1 90  ? 15.858  -5.111  -33.012 1.00 24.76 ?  82  ALA B C     1 
ATOM   5197 O O     . ALA C 1 90  ? 16.594  -4.220  -33.453 1.00 25.58 ?  82  ALA B O     1 
ATOM   5198 C CB    . ALA C 1 90  ? 13.952  -5.889  -34.442 1.00 26.04 ?  82  ALA B CB    1 
ATOM   5199 N N     . PHE C 1 91  ? 15.475  -5.152  -31.737 1.00 25.95 ?  83  PHE B N     1 
ATOM   5200 C CA    . PHE C 1 91  ? 15.940  -4.156  -30.778 1.00 23.64 ?  83  PHE B CA    1 
ATOM   5201 C C     . PHE C 1 91  ? 17.438  -4.297  -30.526 1.00 26.39 ?  83  PHE B C     1 
ATOM   5202 O O     . PHE C 1 91  ? 18.177  -3.305  -30.540 1.00 28.51 ?  83  PHE B O     1 
ATOM   5203 C CB    . PHE C 1 91  ? 15.131  -4.294  -29.485 1.00 25.35 ?  83  PHE B CB    1 
ATOM   5204 C CG    . PHE C 1 91  ? 15.849  -3.839  -28.248 1.00 27.41 ?  83  PHE B CG    1 
ATOM   5205 C CD1   . PHE C 1 91  ? 16.311  -2.538  -28.125 1.00 26.95 ?  83  PHE B CD1   1 
ATOM   5206 C CD2   . PHE C 1 91  ? 16.045  -4.718  -27.195 1.00 26.71 ?  83  PHE B CD2   1 
ATOM   5207 C CE1   . PHE C 1 91  ? 16.964  -2.128  -26.981 1.00 26.87 ?  83  PHE B CE1   1 
ATOM   5208 C CE2   . PHE C 1 91  ? 16.697  -4.314  -26.046 1.00 27.56 ?  83  PHE B CE2   1 
ATOM   5209 C CZ    . PHE C 1 91  ? 17.158  -3.016  -25.939 1.00 32.04 ?  83  PHE B CZ    1 
ATOM   5210 N N     . VAL C 1 92  ? 17.911  -5.527  -30.312 1.00 24.77 ?  84  VAL B N     1 
ATOM   5211 C CA    . VAL C 1 92  ? 19.327  -5.731  -30.019 1.00 28.02 ?  84  VAL B CA    1 
ATOM   5212 C C     . VAL C 1 92  ? 20.180  -5.455  -31.253 1.00 27.03 ?  84  VAL B C     1 
ATOM   5213 O O     . VAL C 1 92  ? 21.244  -4.829  -31.158 1.00 26.86 ?  84  VAL B O     1 
ATOM   5214 C CB    . VAL C 1 92  ? 19.556  -7.152  -29.467 1.00 25.93 ?  84  VAL B CB    1 
ATOM   5215 C CG1   . VAL C 1 92  ? 21.004  -7.586  -29.668 1.00 23.70 ?  84  VAL B CG1   1 
ATOM   5216 C CG2   . VAL C 1 92  ? 19.177  -7.213  -27.994 1.00 23.72 ?  84  VAL B CG2   1 
ATOM   5217 N N     . CYS C 1 93  ? 19.726  -5.900  -32.429 1.00 24.38 ?  85  CYS B N     1 
ATOM   5218 C CA    . CYS C 1 93  ? 20.502  -5.695  -33.650 1.00 26.39 ?  85  CYS B CA    1 
ATOM   5219 C C     . CYS C 1 93  ? 20.679  -4.213  -33.955 1.00 28.90 ?  85  CYS B C     1 
ATOM   5220 O O     . CYS C 1 93  ? 21.750  -3.788  -34.403 1.00 27.02 ?  85  CYS B O     1 
ATOM   5221 C CB    . CYS C 1 93  ? 19.834  -6.401  -34.827 1.00 28.41 ?  85  CYS B CB    1 
ATOM   5222 S SG    . CYS C 1 93  ? 20.086  -8.184  -34.844 1.00 29.59 ?  85  CYS B SG    1 
ATOM   5223 N N     . ALA C 1 94  ? 19.635  -3.413  -33.731 1.00 27.83 ?  86  ALA B N     1 
ATOM   5224 C CA    . ALA C 1 94  ? 19.768  -1.971  -33.900 1.00 27.58 ?  86  ALA B CA    1 
ATOM   5225 C C     . ALA C 1 94  ? 20.743  -1.390  -32.885 1.00 27.39 ?  86  ALA B C     1 
ATOM   5226 O O     . ALA C 1 94  ? 21.524  -0.486  -33.206 1.00 27.94 ?  86  ALA B O     1 
ATOM   5227 C CB    . ALA C 1 94  ? 18.401  -1.298  -33.778 1.00 26.52 ?  86  ALA B CB    1 
ATOM   5228 N N     . ALA C 1 95  ? 20.719  -1.908  -31.654 1.00 25.30 ?  87  ALA B N     1 
ATOM   5229 C CA    . ALA C 1 95  ? 21.588  -1.384  -30.608 1.00 28.81 ?  87  ALA B CA    1 
ATOM   5230 C C     . ALA C 1 95  ? 23.049  -1.747  -30.843 1.00 27.91 ?  87  ALA B C     1 
ATOM   5231 O O     . ALA C 1 95  ? 23.943  -0.970  -30.490 1.00 29.51 ?  87  ALA B O     1 
ATOM   5232 C CB    . ALA C 1 95  ? 21.134  -1.903  -29.248 1.00 28.55 ?  87  ALA B CB    1 
ATOM   5233 N N     . LYS C 1 96  ? 23.312  -2.913  -31.432 1.00 27.01 ?  88  LYS B N     1 
ATOM   5234 C CA    . LYS C 1 96  ? 24.670  -3.406  -31.606 1.00 29.49 ?  88  LYS B CA    1 
ATOM   5235 C C     . LYS C 1 96  ? 25.154  -3.347  -33.048 1.00 27.99 ?  88  LYS B C     1 
ATOM   5236 O O     . LYS C 1 96  ? 26.277  -3.781  -33.328 1.00 24.82 ?  88  LYS B O     1 
ATOM   5237 C CB    . LYS C 1 96  ? 24.779  -4.841  -31.079 1.00 24.95 ?  88  LYS B CB    1 
ATOM   5238 C CG    . LYS C 1 96  ? 24.624  -4.952  -29.570 1.00 28.08 ?  88  LYS B CG    1 
ATOM   5239 C CD    . LYS C 1 96  ? 24.624  -6.402  -29.117 1.00 34.21 ?  88  LYS B CD    1 
ATOM   5240 C CE    . LYS C 1 96  ? 26.018  -7.004  -29.202 1.00 28.47 ?  88  LYS B CE    1 
ATOM   5241 N NZ    . LYS C 1 96  ? 26.978  -6.294  -28.314 1.00 34.02 ?  88  LYS B NZ    1 
ATOM   5242 N N     . GLY C 1 97  ? 24.345  -2.831  -33.969 1.00 27.47 ?  89  GLY B N     1 
ATOM   5243 C CA    . GLY C 1 97  ? 24.796  -2.617  -35.329 1.00 27.89 ?  89  GLY B CA    1 
ATOM   5244 C C     . GLY C 1 97  ? 24.773  -3.855  -36.200 1.00 32.48 ?  89  GLY B C     1 
ATOM   5245 O O     . GLY C 1 97  ? 25.785  -4.216  -36.808 1.00 30.23 ?  89  GLY B O     1 
ATOM   5246 N N     . TYR C 1 98  ? 23.620  -4.513  -36.273 1.00 29.73 ?  90  TYR B N     1 
ATOM   5247 C CA    . TYR C 1 98  ? 23.444  -5.678  -37.125 1.00 29.48 ?  90  TYR B CA    1 
ATOM   5248 C C     . TYR C 1 98  ? 22.206  -5.503  -37.989 1.00 28.56 ?  90  TYR B C     1 
ATOM   5249 O O     . TYR C 1 98  ? 21.260  -4.803  -37.617 1.00 34.21 ?  90  TYR B O     1 
ATOM   5250 C CB    . TYR C 1 98  ? 23.325  -6.970  -36.307 1.00 27.06 ?  90  TYR B CB    1 
ATOM   5251 C CG    . TYR C 1 98  ? 24.624  -7.425  -35.689 1.00 28.33 ?  90  TYR B CG    1 
ATOM   5252 C CD1   . TYR C 1 98  ? 25.011  -6.984  -34.430 1.00 26.34 ?  90  TYR B CD1   1 
ATOM   5253 C CD2   . TYR C 1 98  ? 25.470  -8.289  -36.370 1.00 31.17 ?  90  TYR B CD2   1 
ATOM   5254 C CE1   . TYR C 1 98  ? 26.201  -7.398  -33.865 1.00 34.46 ?  90  TYR B CE1   1 
ATOM   5255 C CE2   . TYR C 1 98  ? 26.659  -8.706  -35.814 1.00 31.62 ?  90  TYR B CE2   1 
ATOM   5256 C CZ    . TYR C 1 98  ? 27.020  -8.259  -34.563 1.00 30.43 ?  90  TYR B CZ    1 
ATOM   5257 O OH    . TYR C 1 98  ? 28.207  -8.674  -34.009 1.00 29.06 ?  90  TYR B OH    1 
ATOM   5258 N N     . LYS C 1 99  ? 22.227  -6.144  -39.152 1.00 33.46 ?  91  LYS B N     1 
ATOM   5259 C CA    . LYS C 1 99  ? 21.076  -6.176  -40.039 1.00 31.13 ?  91  LYS B CA    1 
ATOM   5260 C C     . LYS C 1 99  ? 20.192  -7.356  -39.663 1.00 32.25 ?  91  LYS B C     1 
ATOM   5261 O O     . LYS C 1 99  ? 20.655  -8.501  -39.624 1.00 39.06 ?  91  LYS B O     1 
ATOM   5262 C CB    . LYS C 1 99  ? 21.517  -6.281  -41.498 1.00 33.22 ?  91  LYS B CB    1 
ATOM   5263 C CG    . LYS C 1 99  ? 22.480  -5.189  -41.933 1.00 38.74 ?  91  LYS B CG    1 
ATOM   5264 C CD    . LYS C 1 99  ? 22.129  -4.664  -43.316 1.00 47.21 ?  91  LYS B CD    1 
ATOM   5265 C CE    . LYS C 1 99  ? 23.010  -5.294  -44.384 1.00 44.03 ?  91  LYS B CE    1 
ATOM   5266 N NZ    . LYS C 1 99  ? 24.270  -4.529  -44.595 1.00 47.28 ?  91  LYS B NZ    1 
ATOM   5267 N N     . ALA C 1 100 ? 18.924  -7.074  -39.380 1.00 26.05 ?  92  ALA B N     1 
ATOM   5268 C CA    . ALA C 1 100 ? 17.976  -8.079  -38.923 1.00 28.59 ?  92  ALA B CA    1 
ATOM   5269 C C     . ALA C 1 100 ? 17.009  -8.429  -40.044 1.00 31.59 ?  92  ALA B C     1 
ATOM   5270 O O     . ALA C 1 100 ? 16.392  -7.540  -40.640 1.00 28.06 ?  92  ALA B O     1 
ATOM   5271 C CB    . ALA C 1 100 ? 17.204  -7.587  -37.696 1.00 31.09 ?  92  ALA B CB    1 
ATOM   5272 N N     . VAL C 1 101 ? 16.887  -9.722  -40.328 1.00 30.17 ?  93  VAL B N     1 
ATOM   5273 C CA    . VAL C 1 101 ? 15.913  -10.248 -41.274 1.00 30.07 ?  93  VAL B CA    1 
ATOM   5274 C C     . VAL C 1 101 ? 15.081  -11.290 -40.546 1.00 29.91 ?  93  VAL B C     1 
ATOM   5275 O O     . VAL C 1 101 ? 15.632  -12.206 -39.926 1.00 25.83 ?  93  VAL B O     1 
ATOM   5276 C CB    . VAL C 1 101 ? 16.589  -10.860 -42.514 1.00 32.26 ?  93  VAL B CB    1 
ATOM   5277 C CG1   . VAL C 1 101 ? 15.539  -11.372 -43.489 1.00 27.59 ?  93  VAL B CG1   1 
ATOM   5278 C CG2   . VAL C 1 101 ? 17.489  -9.839  -43.187 1.00 26.66 ?  93  VAL B CG2   1 
ATOM   5279 N N     . PHE C 1 102 ? 13.761  -11.146 -40.609 1.00 27.94 ?  94  PHE B N     1 
ATOM   5280 C CA    . PHE C 1 102 ? 12.854  -12.084 -39.965 1.00 31.65 ?  94  PHE B CA    1 
ATOM   5281 C C     . PHE C 1 102 ? 11.855  -12.607 -40.982 1.00 29.83 ?  94  PHE B C     1 
ATOM   5282 O O     . PHE C 1 102 ? 11.225  -11.825 -41.700 1.00 29.25 ?  94  PHE B O     1 
ATOM   5283 C CB    . PHE C 1 102 ? 12.112  -11.438 -38.793 1.00 26.23 ?  94  PHE B CB    1 
ATOM   5284 C CG    . PHE C 1 102 ? 13.010  -10.765 -37.799 1.00 28.62 ?  94  PHE B CG    1 
ATOM   5285 C CD1   . PHE C 1 102 ? 14.001  -11.476 -37.142 1.00 27.39 ?  94  PHE B CD1   1 
ATOM   5286 C CD2   . PHE C 1 102 ? 12.850  -9.421  -37.509 1.00 26.47 ?  94  PHE B CD2   1 
ATOM   5287 C CE1   . PHE C 1 102 ? 14.826  -10.853 -36.221 1.00 28.44 ?  94  PHE B CE1   1 
ATOM   5288 C CE2   . PHE C 1 102 ? 13.669  -8.795  -36.590 1.00 26.20 ?  94  PHE B CE2   1 
ATOM   5289 C CZ    . PHE C 1 102 ? 14.659  -9.511  -35.946 1.00 24.48 ?  94  PHE B CZ    1 
ATOM   5290 N N     . THR C 1 103 ? 11.714  -13.927 -41.040 1.00 26.87 ?  95  THR B N     1 
ATOM   5291 C CA    . THR C 1 103 ? 10.671  -14.550 -41.837 1.00 28.34 ?  95  THR B CA    1 
ATOM   5292 C C     . THR C 1 103 ? 9.469   -14.842 -40.951 1.00 32.84 ?  95  THR B C     1 
ATOM   5293 O O     . THR C 1 103 ? 9.618   -15.239 -39.792 1.00 30.43 ?  95  THR B O     1 
ATOM   5294 C CB    . THR C 1 103 ? 11.171  -15.840 -42.489 1.00 25.69 ?  95  THR B CB    1 
ATOM   5295 O OG1   . THR C 1 103 ? 11.495  -16.796 -41.473 1.00 25.97 ?  95  THR B OG1   1 
ATOM   5296 C CG2   . THR C 1 103 ? 12.406  -15.566 -43.337 1.00 24.41 ?  95  THR B CG2   1 
ATOM   5297 N N     . MET C 1 104 ? 8.278   -14.631 -41.500 1.00 33.07 ?  96  MET B N     1 
ATOM   5298 C CA    . MET C 1 104 ? 7.043   -14.841 -40.759 1.00 32.74 ?  96  MET B CA    1 
ATOM   5299 C C     . MET C 1 104 ? 5.925   -15.082 -41.757 1.00 34.07 ?  96  MET B C     1 
ATOM   5300 O O     . MET C 1 104 ? 6.025   -14.663 -42.918 1.00 32.00 ?  96  MET B O     1 
ATOM   5301 C CB    . MET C 1 104 ? 6.703   -13.628 -39.882 1.00 31.86 ?  96  MET B CB    1 
ATOM   5302 C CG    . MET C 1 104 ? 6.683   -12.314 -40.642 1.00 28.36 ?  96  MET B CG    1 
ATOM   5303 S SD    . MET C 1 104 ? 6.955   -10.903 -39.563 1.00 37.94 ?  96  MET B SD    1 
ATOM   5304 C CE    . MET C 1 104 ? 8.688   -11.113 -39.194 1.00 32.51 ?  96  MET B CE    1 
ATOM   5305 N N     . PRO C 1 105 ? 4.841   -15.733 -41.339 1.00 35.41 ?  97  PRO B N     1 
ATOM   5306 C CA    . PRO C 1 105 ? 3.683   -15.854 -42.229 1.00 37.91 ?  97  PRO B CA    1 
ATOM   5307 C C     . PRO C 1 105 ? 3.110   -14.484 -42.557 1.00 37.58 ?  97  PRO B C     1 
ATOM   5308 O O     . PRO C 1 105 ? 3.151   -13.559 -41.742 1.00 33.45 ?  97  PRO B O     1 
ATOM   5309 C CB    . PRO C 1 105 ? 2.695   -16.704 -41.423 1.00 35.65 ?  97  PRO B CB    1 
ATOM   5310 C CG    . PRO C 1 105 ? 3.508   -17.357 -40.358 1.00 40.40 ?  97  PRO B CG    1 
ATOM   5311 C CD    . PRO C 1 105 ? 4.632   -16.424 -40.056 1.00 33.62 ?  97  PRO B CD    1 
ATOM   5312 N N     . GLU C 1 106 ? 2.560   -14.364 -43.764 1.00 38.96 ?  98  GLU B N     1 
ATOM   5313 C CA    . GLU C 1 106 ? 1.972   -13.113 -44.229 1.00 37.64 ?  98  GLU B CA    1 
ATOM   5314 C C     . GLU C 1 106 ? 0.770   -12.713 -43.382 1.00 40.90 ?  98  GLU B C     1 
ATOM   5315 O O     . GLU C 1 106 ? 0.179   -11.649 -43.594 1.00 40.28 ?  98  GLU B O     1 
ATOM   5316 C CB    . GLU C 1 106 ? 1.563   -13.242 -45.696 1.00 42.42 ?  98  GLU B CB    1 
ATOM   5317 C CG    . GLU C 1 106 ? 0.578   -14.367 -45.948 1.00 46.33 ?  98  GLU B CG    1 
ATOM   5318 C CD    . GLU C 1 106 ? 0.415   -14.678 -47.419 1.00 42.13 ?  98  GLU B CD    1 
ATOM   5319 O OE1   . GLU C 1 106 ? 0.379   -13.727 -48.228 1.00 42.23 ?  98  GLU B OE1   1 
ATOM   5320 O OE2   . GLU C 1 106 ? 0.329   -15.874 -47.768 1.00 48.27 ?  98  GLU B OE2   1 
ATOM   5321 N N     . THR C 1 107 ? 0.405   -13.558 -42.422 1.00 33.89 ?  99  THR B N     1 
ATOM   5322 C CA    . THR C 1 107 ? -0.745  -13.326 -41.562 1.00 38.99 ?  99  THR B CA    1 
ATOM   5323 C C     . THR C 1 107 ? -0.437  -12.423 -40.376 1.00 41.71 ?  99  THR B C     1 
ATOM   5324 O O     . THR C 1 107 ? -1.340  -12.158 -39.577 1.00 45.74 ?  99  THR B O     1 
ATOM   5325 C CB    . THR C 1 107 ? -1.282  -14.662 -41.047 1.00 49.12 ?  99  THR B CB    1 
ATOM   5326 O OG1   . THR C 1 107 ? -0.188  -15.461 -40.576 1.00 62.55 ?  99  THR B OG1   1 
ATOM   5327 C CG2   . THR C 1 107 ? -1.995  -15.405 -42.170 1.00 49.90 ?  99  THR B CG2   1 
ATOM   5328 N N     . MET C 1 108 ? 0.798   -11.953 -40.230 1.00 36.92 ?  100 MET B N     1 
ATOM   5329 C CA    . MET C 1 108 ? 1.137   -11.121 -39.085 1.00 39.46 ?  100 MET B CA    1 
ATOM   5330 C C     . MET C 1 108 ? 0.462   -9.758  -39.189 1.00 43.62 ?  100 MET B C     1 
ATOM   5331 O O     . MET C 1 108 ? 0.178   -9.260  -40.281 1.00 41.70 ?  100 MET B O     1 
ATOM   5332 C CB    . MET C 1 108 ? 2.653   -10.953 -38.970 1.00 37.13 ?  100 MET B CB    1 
ATOM   5333 C CG    . MET C 1 108 ? 3.411   -12.257 -38.769 1.00 37.71 ?  100 MET B CG    1 
ATOM   5334 S SD    . MET C 1 108 ? 3.035   -13.049 -37.192 1.00 46.75 ?  100 MET B SD    1 
ATOM   5335 C CE    . MET C 1 108 ? 3.380   -11.717 -36.045 1.00 38.38 ?  100 MET B CE    1 
ATOM   5336 N N     . SER C 1 109 ? 0.208   -9.155  -38.030 1.00 36.91 ?  101 SER B N     1 
ATOM   5337 C CA    . SER C 1 109 ? -0.502  -7.885  -37.979 1.00 41.65 ?  101 SER B CA    1 
ATOM   5338 C C     . SER C 1 109 ? 0.377   -6.744  -38.478 1.00 41.68 ?  101 SER B C     1 
ATOM   5339 O O     . SER C 1 109 ? 1.608   -6.791  -38.390 1.00 41.08 ?  101 SER B O     1 
ATOM   5340 C CB    . SER C 1 109 ? -0.968  -7.591  -36.553 1.00 44.63 ?  101 SER B CB    1 
ATOM   5341 O OG    . SER C 1 109 ? 0.135   -7.447  -35.675 1.00 49.72 ?  101 SER B OG    1 
ATOM   5342 N N     . GLN C 1 110 ? -0.277  -5.703  -39.003 1.00 47.61 ?  102 GLN B N     1 
ATOM   5343 C CA    . GLN C 1 110 ? 0.451   -4.520  -39.451 1.00 48.65 ?  102 GLN B CA    1 
ATOM   5344 C C     . GLN C 1 110 ? 1.111   -3.798  -38.286 1.00 45.83 ?  102 GLN B C     1 
ATOM   5345 O O     . GLN C 1 110 ? 2.175   -3.190  -38.456 1.00 46.59 ?  102 GLN B O     1 
ATOM   5346 C CB    . GLN C 1 110 ? -0.489  -3.575  -40.199 1.00 46.83 ?  102 GLN B CB    1 
ATOM   5347 C CG    . GLN C 1 110 ? 0.205   -2.377  -40.831 1.00 49.60 ?  102 GLN B CG    1 
ATOM   5348 C CD    . GLN C 1 110 ? 1.043   -2.758  -42.037 1.00 50.33 ?  102 GLN B CD    1 
ATOM   5349 O OE1   . GLN C 1 110 ? 2.050   -2.116  -42.338 1.00 56.54 ?  102 GLN B OE1   1 
ATOM   5350 N NE2   . GLN C 1 110 ? 0.627   -3.808  -42.737 1.00 53.05 ?  102 GLN B NE2   1 
ATOM   5351 N N     . GLU C 1 111 ? 0.502   -3.856  -37.100 1.00 44.77 ?  103 GLU B N     1 
ATOM   5352 C CA    . GLU C 1 111 ? 1.101   -3.227  -35.929 1.00 50.61 ?  103 GLU B CA    1 
ATOM   5353 C C     . GLU C 1 111 ? 2.421   -3.893  -35.563 1.00 49.16 ?  103 GLU B C     1 
ATOM   5354 O O     . GLU C 1 111 ? 3.362   -3.226  -35.113 1.00 45.13 ?  103 GLU B O     1 
ATOM   5355 C CB    . GLU C 1 111 ? 0.125   -3.282  -34.755 1.00 50.77 ?  103 GLU B CB    1 
ATOM   5356 C CG    . GLU C 1 111 ? -0.780  -2.060  -34.625 1.00 63.28 ?  103 GLU B CG    1 
ATOM   5357 C CD    . GLU C 1 111 ? -1.554  -1.730  -35.896 1.00 70.57 ?  103 GLU B CD    1 
ATOM   5358 O OE1   . GLU C 1 111 ? -1.844  -0.535  -36.119 1.00 63.56 ?  103 GLU B OE1   1 
ATOM   5359 O OE2   . GLU C 1 111 ? -1.900  -2.660  -36.657 1.00 66.27 ?  103 GLU B OE2   1 
ATOM   5360 N N     . ARG C 1 112 ? 2.507   -5.213  -35.746 1.00 42.79 ?  104 ARG B N     1 
ATOM   5361 C CA    . ARG C 1 112 ? 3.757   -5.916  -35.483 1.00 45.39 ?  104 ARG B CA    1 
ATOM   5362 C C     . ARG C 1 112 ? 4.807   -5.571  -36.531 1.00 38.69 ?  104 ARG B C     1 
ATOM   5363 O O     . ARG C 1 112 ? 5.977   -5.353  -36.196 1.00 38.66 ?  104 ARG B O     1 
ATOM   5364 C CB    . ARG C 1 112 ? 3.507   -7.424  -35.434 1.00 40.67 ?  104 ARG B CB    1 
ATOM   5365 C CG    . ARG C 1 112 ? 4.764   -8.285  -35.483 1.00 41.70 ?  104 ARG B CG    1 
ATOM   5366 C CD    . ARG C 1 112 ? 5.738   -7.947  -34.348 1.00 41.59 ?  104 ARG B CD    1 
ATOM   5367 N NE    . ARG C 1 112 ? 5.095   -7.631  -33.074 1.00 36.04 ?  104 ARG B NE    1 
ATOM   5368 C CZ    . ARG C 1 112 ? 4.350   -8.466  -32.358 1.00 35.51 ?  104 ARG B CZ    1 
ATOM   5369 N NH1   . ARG C 1 112 ? 4.158   -9.722  -32.730 1.00 42.72 ?  104 ARG B NH1   1 
ATOM   5370 N NH2   . ARG C 1 112 ? 3.795   -8.032  -31.230 1.00 43.63 ?  104 ARG B NH2   1 
ATOM   5371 N N     . ARG C 1 113 ? 4.408   -5.506  -37.804 1.00 42.80 ?  105 ARG B N     1 
ATOM   5372 C CA    . ARG C 1 113 ? 5.356   -5.129  -38.847 1.00 39.04 ?  105 ARG B CA    1 
ATOM   5373 C C     . ARG C 1 113 ? 5.938   -3.745  -38.588 1.00 39.44 ?  105 ARG B C     1 
ATOM   5374 O O     . ARG C 1 113 ? 7.140   -3.526  -38.772 1.00 36.22 ?  105 ARG B O     1 
ATOM   5375 C CB    . ARG C 1 113 ? 4.685   -5.179  -40.220 1.00 38.32 ?  105 ARG B CB    1 
ATOM   5376 C CG    . ARG C 1 113 ? 4.051   -6.515  -40.564 1.00 43.20 ?  105 ARG B CG    1 
ATOM   5377 C CD    . ARG C 1 113 ? 2.793   -6.309  -41.388 1.00 48.72 ?  105 ARG B CD    1 
ATOM   5378 N NE    . ARG C 1 113 ? 2.234   -7.561  -41.882 1.00 42.98 ?  105 ARG B NE    1 
ATOM   5379 C CZ    . ARG C 1 113 ? 2.072   -7.855  -43.165 1.00 45.59 ?  105 ARG B CZ    1 
ATOM   5380 N NH1   . ARG C 1 113 ? 2.435   -7.013  -44.120 1.00 49.07 ?  105 ARG B NH1   1 
ATOM   5381 N NH2   . ARG C 1 113 ? 1.528   -9.021  -43.500 1.00 43.34 ?  105 ARG B NH2   1 
ATOM   5382 N N     . ASN C 1 114 ? 5.102   -2.805  -38.143 1.00 36.71 ?  106 ASN B N     1 
ATOM   5383 C CA    . ASN C 1 114 ? 5.582   -1.456  -37.859 1.00 41.39 ?  106 ASN B CA    1 
ATOM   5384 C C     . ASN C 1 114 ? 6.597   -1.454  -36.722 1.00 38.92 ?  106 ASN B C     1 
ATOM   5385 O O     . ASN C 1 114 ? 7.594   -0.722  -36.771 1.00 38.46 ?  106 ASN B O     1 
ATOM   5386 C CB    . ASN C 1 114 ? 4.403   -0.544  -37.525 1.00 41.09 ?  106 ASN B CB    1 
ATOM   5387 C CG    . ASN C 1 114 ? 3.436   -0.396  -38.682 1.00 49.64 ?  106 ASN B CG    1 
ATOM   5388 O OD1   . ASN C 1 114 ? 3.659   -0.934  -39.766 1.00 47.29 ?  106 ASN B OD1   1 
ATOM   5389 N ND2   . ASN C 1 114 ? 2.353   0.338   -38.455 1.00 50.31 ?  106 ASN B ND2   1 
ATOM   5390 N N     . LEU C 1 115 ? 6.358   -2.261  -35.686 1.00 35.20 ?  107 LEU B N     1 
ATOM   5391 C CA    . LEU C 1 115 ? 7.291   -2.338  -34.566 1.00 36.68 ?  107 LEU B CA    1 
ATOM   5392 C C     . LEU C 1 115 ? 8.650   -2.859  -35.018 1.00 28.41 ?  107 LEU B C     1 
ATOM   5393 O O     . LEU C 1 115 ? 9.692   -2.278  -34.691 1.00 28.42 ?  107 LEU B O     1 
ATOM   5394 C CB    . LEU C 1 115 ? 6.709   -3.227  -33.465 1.00 35.22 ?  107 LEU B CB    1 
ATOM   5395 C CG    . LEU C 1 115 ? 7.604   -3.510  -32.256 1.00 30.70 ?  107 LEU B CG    1 
ATOM   5396 C CD1   . LEU C 1 115 ? 8.141   -2.217  -31.673 1.00 30.09 ?  107 LEU B CD1   1 
ATOM   5397 C CD2   . LEU C 1 115 ? 6.853   -4.304  -31.195 1.00 34.55 ?  107 LEU B CD2   1 
ATOM   5398 N N     . LEU C 1 116 ? 8.657   -3.956  -35.778 1.00 29.17 ?  108 LEU B N     1 
ATOM   5399 C CA    . LEU C 1 116 ? 9.916   -4.530  -36.243 1.00 30.50 ?  108 LEU B CA    1 
ATOM   5400 C C     . LEU C 1 116 ? 10.631  -3.590  -37.203 1.00 33.95 ?  108 LEU B C     1 
ATOM   5401 O O     . LEU C 1 116 ? 11.859  -3.451  -37.151 1.00 31.37 ?  108 LEU B O     1 
ATOM   5402 C CB    . LEU C 1 116 ? 9.658   -5.879  -36.913 1.00 25.79 ?  108 LEU B CB    1 
ATOM   5403 C CG    . LEU C 1 116 ? 9.014   -6.946  -36.029 1.00 27.16 ?  108 LEU B CG    1 
ATOM   5404 C CD1   . LEU C 1 116 ? 8.483   -8.093  -36.872 1.00 28.06 ?  108 LEU B CD1   1 
ATOM   5405 C CD2   . LEU C 1 116 ? 10.008  -7.445  -34.998 1.00 25.48 ?  108 LEU B CD2   1 
ATOM   5406 N N     . LYS C 1 117 ? 9.879   -2.935  -38.088 1.00 34.07 ?  109 LYS B N     1 
ATOM   5407 C CA    . LYS C 1 117 ? 10.493  -2.030  -39.051 1.00 31.77 ?  109 LYS B CA    1 
ATOM   5408 C C     . LYS C 1 117 ? 10.997  -0.756  -38.386 1.00 33.99 ?  109 LYS B C     1 
ATOM   5409 O O     . LYS C 1 117 ? 11.935  -0.128  -38.890 1.00 36.65 ?  109 LYS B O     1 
ATOM   5410 C CB    . LYS C 1 117 ? 9.499   -1.696  -40.162 1.00 33.18 ?  109 LYS B CB    1 
ATOM   5411 C CG    . LYS C 1 117 ? 9.169   -2.871  -41.071 1.00 37.57 ?  109 LYS B CG    1 
ATOM   5412 C CD    . LYS C 1 117 ? 8.539   -2.404  -42.373 1.00 40.58 ?  109 LYS B CD    1 
ATOM   5413 C CE    . LYS C 1 117 ? 7.446   -3.359  -42.823 1.00 50.72 ?  109 LYS B CE    1 
ATOM   5414 N NZ    . LYS C 1 117 ? 6.144   -2.666  -43.029 1.00 56.36 ?  109 LYS B NZ    1 
ATOM   5415 N N     . ALA C 1 118 ? 10.394  -0.358  -37.261 1.00 29.06 ?  110 ALA B N     1 
ATOM   5416 C CA    . ALA C 1 118 ? 10.859  0.841   -36.570 1.00 32.66 ?  110 ALA B CA    1 
ATOM   5417 C C     . ALA C 1 118 ? 12.282  0.668   -36.057 1.00 32.85 ?  110 ALA B C     1 
ATOM   5418 O O     . ALA C 1 118 ? 13.007  1.654   -35.888 1.00 32.95 ?  110 ALA B O     1 
ATOM   5419 C CB    . ALA C 1 118 ? 9.915   1.190   -35.422 1.00 31.68 ?  110 ALA B CB    1 
ATOM   5420 N N     . TYR C 1 119 ? 12.696  -0.569  -35.803 1.00 30.31 ?  111 TYR B N     1 
ATOM   5421 C CA    . TYR C 1 119 ? 14.076  -0.876  -35.458 1.00 29.18 ?  111 TYR B CA    1 
ATOM   5422 C C     . TYR C 1 119 ? 14.963  -1.048  -36.685 1.00 33.11 ?  111 TYR B C     1 
ATOM   5423 O O     . TYR C 1 119 ? 16.172  -1.251  -36.534 1.00 28.74 ?  111 TYR B O     1 
ATOM   5424 C CB    . TYR C 1 119 ? 14.131  -2.144  -34.600 1.00 30.89 ?  111 TYR B CB    1 
ATOM   5425 C CG    . TYR C 1 119 ? 13.764  -1.931  -33.149 1.00 28.03 ?  111 TYR B CG    1 
ATOM   5426 C CD1   . TYR C 1 119 ? 14.463  -1.025  -32.362 1.00 26.70 ?  111 TYR B CD1   1 
ATOM   5427 C CD2   . TYR C 1 119 ? 12.727  -2.645  -32.562 1.00 29.71 ?  111 TYR B CD2   1 
ATOM   5428 C CE1   . TYR C 1 119 ? 14.135  -0.833  -31.033 1.00 27.11 ?  111 TYR B CE1   1 
ATOM   5429 C CE2   . TYR C 1 119 ? 12.393  -2.461  -31.235 1.00 24.88 ?  111 TYR B CE2   1 
ATOM   5430 C CZ    . TYR C 1 119 ? 13.099  -1.555  -30.475 1.00 29.44 ?  111 TYR B CZ    1 
ATOM   5431 O OH    . TYR C 1 119 ? 12.765  -1.375  -29.153 1.00 25.58 ?  111 TYR B OH    1 
ATOM   5432 N N     . GLY C 1 120 ? 14.397  -0.974  -37.890 1.00 28.84 ?  112 GLY B N     1 
ATOM   5433 C CA    . GLY C 1 120 ? 15.154  -1.146  -39.111 1.00 34.77 ?  112 GLY B CA    1 
ATOM   5434 C C     . GLY C 1 120 ? 15.186  -2.556  -39.658 1.00 35.00 ?  112 GLY B C     1 
ATOM   5435 O O     . GLY C 1 120 ? 15.848  -2.792  -40.677 1.00 33.79 ?  112 GLY B O     1 
ATOM   5436 N N     . ALA C 1 121 ? 14.490  -3.495  -39.022 1.00 31.47 ?  113 ALA B N     1 
ATOM   5437 C CA    . ALA C 1 121 ? 14.516  -4.886  -39.449 1.00 29.93 ?  113 ALA B CA    1 
ATOM   5438 C C     . ALA C 1 121 ? 13.801  -5.067  -40.783 1.00 29.00 ?  113 ALA B C     1 
ATOM   5439 O O     . ALA C 1 121 ? 12.835  -4.368  -41.099 1.00 30.11 ?  113 ALA B O     1 
ATOM   5440 C CB    . ALA C 1 121 ? 13.864  -5.778  -38.392 1.00 28.60 ?  113 ALA B CB    1 
ATOM   5441 N N     . GLU C 1 122 ? 14.289  -6.023  -41.568 1.00 27.15 ?  114 GLU B N     1 
ATOM   5442 C CA    . GLU C 1 122 ? 13.642  -6.402  -42.814 1.00 32.50 ?  114 GLU B CA    1 
ATOM   5443 C C     . GLU C 1 122 ? 12.695  -7.566  -42.564 1.00 27.50 ?  114 GLU B C     1 
ATOM   5444 O O     . GLU C 1 122 ? 13.015  -8.495  -41.817 1.00 29.97 ?  114 GLU B O     1 
ATOM   5445 C CB    . GLU C 1 122 ? 14.674  -6.790  -43.873 1.00 29.57 ?  114 GLU B CB    1 
ATOM   5446 C CG    . GLU C 1 122 ? 14.070  -7.104  -45.234 1.00 29.07 ?  114 GLU B CG    1 
ATOM   5447 C CD    . GLU C 1 122 ? 14.924  -8.058  -46.044 1.00 34.57 ?  114 GLU B CD    1 
ATOM   5448 O OE1   . GLU C 1 122 ? 16.134  -8.161  -45.756 1.00 34.69 ?  114 GLU B OE1   1 
ATOM   5449 O OE2   . GLU C 1 122 ? 14.385  -8.706  -46.966 1.00 32.37 ?  114 GLU B OE2   1 
ATOM   5450 N N     . LEU C 1 123 ? 11.528  -7.515  -43.197 1.00 30.38 ?  115 LEU B N     1 
ATOM   5451 C CA    . LEU C 1 123 ? 10.498  -8.527  -43.022 1.00 28.00 ?  115 LEU B CA    1 
ATOM   5452 C C     . LEU C 1 123 ? 10.325  -9.335  -44.300 1.00 31.45 ?  115 LEU B C     1 
ATOM   5453 O O     . LEU C 1 123 ? 10.272  -8.776  -45.400 1.00 29.77 ?  115 LEU B O     1 
ATOM   5454 C CB    . LEU C 1 123 ? 9.168   -7.888  -42.619 1.00 28.35 ?  115 LEU B CB    1 
ATOM   5455 C CG    . LEU C 1 123 ? 9.238   -6.901  -41.455 1.00 33.51 ?  115 LEU B CG    1 
ATOM   5456 C CD1   . LEU C 1 123 ? 7.843   -6.528  -41.028 1.00 35.39 ?  115 LEU B CD1   1 
ATOM   5457 C CD2   . LEU C 1 123 ? 10.014  -7.489  -40.285 1.00 29.77 ?  115 LEU B CD2   1 
ATOM   5458 N N     . VAL C 1 124 ? 10.244  -10.653 -44.145 1.00 32.00 ?  116 VAL B N     1 
ATOM   5459 C CA    . VAL C 1 124 ? 10.068  -11.580 -45.255 1.00 32.03 ?  116 VAL B CA    1 
ATOM   5460 C C     . VAL C 1 124 ? 8.801   -12.373 -44.977 1.00 31.00 ?  116 VAL B C     1 
ATOM   5461 O O     . VAL C 1 124 ? 8.777   -13.217 -44.072 1.00 28.87 ?  116 VAL B O     1 
ATOM   5462 C CB    . VAL C 1 124 ? 11.274  -12.512 -45.427 1.00 29.77 ?  116 VAL B CB    1 
ATOM   5463 C CG1   . VAL C 1 124 ? 11.011  -13.514 -46.540 1.00 31.72 ?  116 VAL B CG1   1 
ATOM   5464 C CG2   . VAL C 1 124 ? 12.532  -11.707 -45.709 1.00 28.26 ?  116 VAL B CG2   1 
ATOM   5465 N N     . LEU C 1 125 ? 7.750   -12.103 -45.746 1.00 32.57 ?  117 LEU B N     1 
ATOM   5466 C CA    . LEU C 1 125 ? 6.457   -12.736 -45.531 1.00 31.97 ?  117 LEU B CA    1 
ATOM   5467 C C     . LEU C 1 125 ? 6.371   -14.037 -46.317 1.00 32.29 ?  117 LEU B C     1 
ATOM   5468 O O     . LEU C 1 125 ? 6.638   -14.064 -47.522 1.00 37.83 ?  117 LEU B O     1 
ATOM   5469 C CB    . LEU C 1 125 ? 5.325   -11.791 -45.931 1.00 33.74 ?  117 LEU B CB    1 
ATOM   5470 C CG    . LEU C 1 125 ? 5.437   -10.366 -45.380 1.00 39.44 ?  117 LEU B CG    1 
ATOM   5471 C CD1   . LEU C 1 125 ? 4.320   -9.484  -45.918 1.00 38.36 ?  117 LEU B CD1   1 
ATOM   5472 C CD2   . LEU C 1 125 ? 5.435   -10.373 -43.857 1.00 33.67 ?  117 LEU B CD2   1 
ATOM   5473 N N     . THR C 1 126 ? 6.002   -15.109 -45.629 1.00 32.89 ?  118 THR B N     1 
ATOM   5474 C CA    . THR C 1 126 ? 5.863   -16.435 -46.206 1.00 36.81 ?  118 THR B CA    1 
ATOM   5475 C C     . THR C 1 126 ? 4.387   -16.803 -46.346 1.00 38.46 ?  118 THR B C     1 
ATOM   5476 O O     . THR C 1 126 ? 3.525   -16.185 -45.711 1.00 33.09 ?  118 THR B O     1 
ATOM   5477 C CB    . THR C 1 126 ? 6.591   -17.470 -45.333 1.00 35.23 ?  118 THR B CB    1 
ATOM   5478 O OG1   . THR C 1 126 ? 6.297   -17.233 -43.951 1.00 33.21 ?  118 THR B OG1   1 
ATOM   5479 C CG2   . THR C 1 126 ? 8.092   -17.375 -45.546 1.00 30.67 ?  118 THR B CG2   1 
ATOM   5480 N N     . PRO C 1 127 ? 4.058   -17.782 -47.194 1.00 38.38 ?  119 PRO B N     1 
ATOM   5481 C CA    . PRO C 1 127 ? 2.649   -18.160 -47.386 1.00 40.22 ?  119 PRO B CA    1 
ATOM   5482 C C     . PRO C 1 127 ? 1.924   -18.402 -46.069 1.00 40.37 ?  119 PRO B C     1 
ATOM   5483 O O     . PRO C 1 127 ? 2.374   -19.176 -45.221 1.00 38.96 ?  119 PRO B O     1 
ATOM   5484 C CB    . PRO C 1 127 ? 2.733   -19.444 -48.224 1.00 42.75 ?  119 PRO B CB    1 
ATOM   5485 C CG    . PRO C 1 127 ? 4.198   -19.700 -48.480 1.00 45.12 ?  119 PRO B CG    1 
ATOM   5486 C CD    . PRO C 1 127 ? 4.934   -18.443 -48.174 1.00 47.39 ?  119 PRO B CD    1 
ATOM   5487 N N     . GLY C 1 128 ? 0.783   -17.726 -45.907 1.00 40.05 ?  120 GLY B N     1 
ATOM   5488 C CA    . GLY C 1 128 ? 0.043   -17.812 -44.659 1.00 43.11 ?  120 GLY B CA    1 
ATOM   5489 C C     . GLY C 1 128 ? -0.469  -19.205 -44.352 1.00 38.68 ?  120 GLY B C     1 
ATOM   5490 O O     . GLY C 1 128 ? -0.609  -19.574 -43.183 1.00 41.89 ?  120 GLY B O     1 
ATOM   5491 N N     . SER C 1 129 ? -0.759  -19.996 -45.385 1.00 36.63 ?  121 SER B N     1 
ATOM   5492 C CA    . SER C 1 129 ? -1.191  -21.369 -45.156 1.00 41.62 ?  121 SER B CA    1 
ATOM   5493 C C     . SER C 1 129 ? -0.066  -22.244 -44.621 1.00 46.20 ?  121 SER B C     1 
ATOM   5494 O O     . SER C 1 129 ? -0.341  -23.300 -44.042 1.00 40.64 ?  121 SER B O     1 
ATOM   5495 C CB    . SER C 1 129 ? -1.749  -21.971 -46.447 1.00 47.64 ?  121 SER B CB    1 
ATOM   5496 O OG    . SER C 1 129 ? -0.729  -22.125 -47.418 1.00 41.76 ?  121 SER B OG    1 
ATOM   5497 N N     . GLU C 1 130 ? 1.189   -21.826 -44.797 1.00 44.84 ?  122 GLU B N     1 
ATOM   5498 C CA    . GLU C 1 130 ? 2.332   -22.603 -44.341 1.00 38.65 ?  122 GLU B CA    1 
ATOM   5499 C C     . GLU C 1 130 ? 2.671   -22.356 -42.877 1.00 35.81 ?  122 GLU B C     1 
ATOM   5500 O O     . GLU C 1 130 ? 3.453   -23.124 -42.306 1.00 37.10 ?  122 GLU B O     1 
ATOM   5501 C CB    . GLU C 1 130 ? 3.553   -22.287 -45.209 1.00 41.74 ?  122 GLU B CB    1 
ATOM   5502 C CG    . GLU C 1 130 ? 3.452   -22.798 -46.641 1.00 49.91 ?  122 GLU B CG    1 
ATOM   5503 C CD    . GLU C 1 130 ? 2.924   -24.219 -46.729 1.00 62.82 ?  122 GLU B CD    1 
ATOM   5504 O OE1   . GLU C 1 130 ? 2.042   -24.472 -47.577 1.00 63.55 ?  122 GLU B OE1   1 
ATOM   5505 O OE2   . GLU C 1 130 ? 3.400   -25.085 -45.962 1.00 63.13 ?  122 GLU B OE2   1 
ATOM   5506 N N     . ALA C 1 131 ? 2.099   -21.316 -42.266 1.00 37.20 ?  123 ALA B N     1 
ATOM   5507 C CA    . ALA C 1 131 ? 2.332   -20.988 -40.863 1.00 37.91 ?  123 ALA B CA    1 
ATOM   5508 C C     . ALA C 1 131 ? 3.828   -20.861 -40.588 1.00 39.51 ?  123 ALA B C     1 
ATOM   5509 O O     . ALA C 1 131 ? 4.548   -20.225 -41.365 1.00 32.77 ?  123 ALA B O     1 
ATOM   5510 C CB    . ALA C 1 131 ? 1.678   -22.032 -39.957 1.00 38.29 ?  123 ALA B CB    1 
ATOM   5511 N N     . MET C 1 132 ? 4.316   -21.459 -39.499 1.00 37.57 ?  124 MET B N     1 
ATOM   5512 C CA    . MET C 1 132 ? 5.728   -21.313 -39.154 1.00 37.77 ?  124 MET B CA    1 
ATOM   5513 C C     . MET C 1 132 ? 6.628   -22.268 -39.922 1.00 34.08 ?  124 MET B C     1 
ATOM   5514 O O     . MET C 1 132 ? 7.840   -22.035 -39.989 1.00 39.60 ?  124 MET B O     1 
ATOM   5515 C CB    . MET C 1 132 ? 5.938   -21.520 -37.654 1.00 36.93 ?  124 MET B CB    1 
ATOM   5516 C CG    . MET C 1 132 ? 5.189   -20.536 -36.783 1.00 39.54 ?  124 MET B CG    1 
ATOM   5517 S SD    . MET C 1 132 ? 5.671   -18.830 -37.115 1.00 41.89 ?  124 MET B SD    1 
ATOM   5518 C CE    . MET C 1 132 ? 7.458   -18.966 -37.163 1.00 35.47 ?  124 MET B CE    1 
ATOM   5519 N N     . LYS C 1 133 ? 6.067   -23.345 -40.476 1.00 32.07 ?  125 LYS B N     1 
ATOM   5520 C CA    . LYS C 1 133 ? 6.850   -24.241 -41.320 1.00 31.83 ?  125 LYS B CA    1 
ATOM   5521 C C     . LYS C 1 133 ? 7.400   -23.505 -42.534 1.00 36.37 ?  125 LYS B C     1 
ATOM   5522 O O     . LYS C 1 133 ? 8.543   -23.738 -42.947 1.00 33.04 ?  125 LYS B O     1 
ATOM   5523 C CB    . LYS C 1 133 ? 5.993   -25.429 -41.756 1.00 40.36 ?  125 LYS B CB    1 
ATOM   5524 N N     . GLY C 1 134 ? 6.599   -22.613 -43.120 1.00 34.04 ?  126 GLY B N     1 
ATOM   5525 C CA    . GLY C 1 134 ? 7.075   -21.843 -44.256 1.00 39.94 ?  126 GLY B CA    1 
ATOM   5526 C C     . GLY C 1 134 ? 8.125   -20.820 -43.871 1.00 35.62 ?  126 GLY B C     1 
ATOM   5527 O O     . GLY C 1 134 ? 9.089   -20.599 -44.609 1.00 34.43 ?  126 GLY B O     1 
ATOM   5528 N N     . ALA C 1 135 ? 7.955   -20.179 -42.711 1.00 31.00 ?  127 ALA B N     1 
ATOM   5529 C CA    . ALA C 1 135 ? 8.942   -19.207 -42.254 1.00 34.79 ?  127 ALA B CA    1 
ATOM   5530 C C     . ALA C 1 135 ? 10.264  -19.882 -41.911 1.00 28.29 ?  127 ALA B C     1 
ATOM   5531 O O     . ALA C 1 135 ? 11.337  -19.322 -42.162 1.00 28.56 ?  127 ALA B O     1 
ATOM   5532 C CB    . ALA C 1 135 ? 8.403   -18.435 -41.050 1.00 30.99 ?  127 ALA B CB    1 
ATOM   5533 N N     . ILE C 1 136 ? 10.206  -21.084 -41.332 1.00 29.83 ?  128 ILE B N     1 
ATOM   5534 C CA    . ILE C 1 136 ? 11.428  -21.835 -41.057 1.00 31.18 ?  128 ILE B CA    1 
ATOM   5535 C C     . ILE C 1 136 ? 12.113  -22.223 -42.360 1.00 35.28 ?  128 ILE B C     1 
ATOM   5536 O O     . ILE C 1 136 ? 13.341  -22.142 -42.485 1.00 38.37 ?  128 ILE B O     1 
ATOM   5537 C CB    . ILE C 1 136 ? 11.107  -23.070 -40.195 1.00 27.86 ?  128 ILE B CB    1 
ATOM   5538 C CG1   . ILE C 1 136 ? 10.734  -22.646 -38.776 1.00 35.94 ?  128 ILE B CG1   1 
ATOM   5539 C CG2   . ILE C 1 136 ? 12.286  -24.036 -40.173 1.00 31.91 ?  128 ILE B CG2   1 
ATOM   5540 C CD1   . ILE C 1 136 ? 10.009  -23.716 -37.997 1.00 30.77 ?  128 ILE B CD1   1 
ATOM   5541 N N     . LYS C 1 137 ? 11.325  -22.638 -43.354 1.00 36.32 ?  129 LYS B N     1 
ATOM   5542 C CA    . LYS C 1 137 ? 11.880  -23.034 -44.644 1.00 34.87 ?  129 LYS B CA    1 
ATOM   5543 C C     . LYS C 1 137 ? 12.572  -21.862 -45.330 1.00 36.06 ?  129 LYS B C     1 
ATOM   5544 O O     . LYS C 1 137 ? 13.691  -21.998 -45.839 1.00 35.58 ?  129 LYS B O     1 
ATOM   5545 C CB    . LYS C 1 137 ? 10.765  -23.601 -45.522 1.00 39.69 ?  129 LYS B CB    1 
ATOM   5546 C CG    . LYS C 1 137 ? 11.193  -24.035 -46.910 1.00 41.41 ?  129 LYS B CG    1 
ATOM   5547 C CD    . LYS C 1 137 ? 9.966   -24.344 -47.759 1.00 48.68 ?  129 LYS B CD    1 
ATOM   5548 C CE    . LYS C 1 137 ? 10.145  -23.943 -49.216 1.00 52.28 ?  129 LYS B CE    1 
ATOM   5549 N NZ    . LYS C 1 137 ? 11.535  -24.162 -49.696 1.00 53.33 ?  129 LYS B NZ    1 
ATOM   5550 N N     . LYS C 1 138 ? 11.919  -20.698 -45.351 1.00 31.85 ?  130 LYS B N     1 
ATOM   5551 C CA    . LYS C 1 138 ? 12.516  -19.525 -45.982 1.00 31.39 ?  130 LYS B CA    1 
ATOM   5552 C C     . LYS C 1 138 ? 13.784  -19.091 -45.258 1.00 29.67 ?  130 LYS B C     1 
ATOM   5553 O O     . LYS C 1 138 ? 14.779  -18.731 -45.898 1.00 36.16 ?  130 LYS B O     1 
ATOM   5554 C CB    . LYS C 1 138 ? 11.506  -18.379 -46.021 1.00 25.89 ?  130 LYS B CB    1 
ATOM   5555 C CG    . LYS C 1 138 ? 12.012  -17.120 -46.711 1.00 28.45 ?  130 LYS B CG    1 
ATOM   5556 C CD    . LYS C 1 138 ? 12.445  -17.397 -48.143 1.00 33.73 ?  130 LYS B CD    1 
ATOM   5557 N N     . ALA C 1 139 ? 13.768  -19.113 -43.924 1.00 29.46 ?  131 ALA B N     1 
ATOM   5558 C CA    . ALA C 1 139 ? 14.944  -18.696 -43.167 1.00 34.58 ?  131 ALA B CA    1 
ATOM   5559 C C     . ALA C 1 139 ? 16.134  -19.599 -43.465 1.00 35.38 ?  131 ALA B C     1 
ATOM   5560 O O     . ALA C 1 139 ? 17.262  -19.123 -43.640 1.00 34.79 ?  131 ALA B O     1 
ATOM   5561 C CB    . ALA C 1 139 ? 14.630  -18.685 -41.670 1.00 26.99 ?  131 ALA B CB    1 
ATOM   5562 N N     . LYS C 1 140 ? 15.899  -20.911 -43.534 1.00 35.58 ?  132 LYS B N     1 
ATOM   5563 C CA    . LYS C 1 140 ? 16.973  -21.833 -43.886 1.00 34.42 ?  132 LYS B CA    1 
ATOM   5564 C C     . LYS C 1 140 ? 17.489  -21.559 -45.294 1.00 36.74 ?  132 LYS B C     1 
ATOM   5565 O O     . LYS C 1 140 ? 18.701  -21.604 -45.537 1.00 33.13 ?  132 LYS B O     1 
ATOM   5566 C CB    . LYS C 1 140 ? 16.487  -23.279 -43.749 1.00 37.79 ?  132 LYS B CB    1 
ATOM   5567 C CG    . LYS C 1 140 ? 17.345  -24.318 -44.467 1.00 41.17 ?  132 LYS B CG    1 
ATOM   5568 C CD    . LYS C 1 140 ? 16.756  -24.724 -45.818 1.00 53.76 ?  132 LYS B CD    1 
ATOM   5569 C CE    . LYS C 1 140 ? 17.622  -25.767 -46.508 1.00 56.20 ?  132 LYS B CE    1 
ATOM   5570 N NZ    . LYS C 1 140 ? 18.696  -25.140 -47.326 1.00 57.53 ?  132 LYS B NZ    1 
ATOM   5571 N N     . GLU C 1 141 ? 16.584  -21.260 -46.229 1.00 34.87 ?  133 GLU B N     1 
ATOM   5572 C CA    . GLU C 1 141 ? 16.989  -20.974 -47.602 1.00 34.21 ?  133 GLU B CA    1 
ATOM   5573 C C     . GLU C 1 141 ? 17.940  -19.784 -47.660 1.00 32.63 ?  133 GLU B C     1 
ATOM   5574 O O     . GLU C 1 141 ? 19.022  -19.867 -48.252 1.00 33.07 ?  133 GLU B O     1 
ATOM   5575 C CB    . GLU C 1 141 ? 15.756  -20.708 -48.465 1.00 40.18 ?  133 GLU B CB    1 
ATOM   5576 C CG    . GLU C 1 141 ? 15.274  -21.900 -49.267 1.00 48.55 ?  133 GLU B CG    1 
ATOM   5577 C CD    . GLU C 1 141 ? 13.860  -21.710 -49.778 1.00 52.21 ?  133 GLU B CD    1 
ATOM   5578 O OE1   . GLU C 1 141 ? 13.638  -20.790 -50.594 1.00 55.72 ?  133 GLU B OE1   1 
ATOM   5579 O OE2   . GLU C 1 141 ? 12.971  -22.474 -49.355 1.00 52.07 ?  133 GLU B OE2   1 
ATOM   5580 N N     . LEU C 1 142 ? 17.546  -18.664 -47.047 1.00 32.36 ?  134 LEU B N     1 
ATOM   5581 C CA    . LEU C 1 142 ? 18.386  -17.471 -47.059 1.00 33.04 ?  134 LEU B CA    1 
ATOM   5582 C C     . LEU C 1 142 ? 19.701  -17.713 -46.329 1.00 29.99 ?  134 LEU B C     1 
ATOM   5583 O O     . LEU C 1 142 ? 20.750  -17.199 -46.734 1.00 36.14 ?  134 LEU B O     1 
ATOM   5584 C CB    . LEU C 1 142 ? 17.633  -16.300 -46.430 1.00 30.79 ?  134 LEU B CB    1 
ATOM   5585 C CG    . LEU C 1 142 ? 16.361  -15.863 -47.161 1.00 29.28 ?  134 LEU B CG    1 
ATOM   5586 C CD1   . LEU C 1 142 ? 15.531  -14.930 -46.290 1.00 25.62 ?  134 LEU B CD1   1 
ATOM   5587 C CD2   . LEU C 1 142 ? 16.705  -15.203 -48.486 1.00 31.08 ?  134 LEU B CD2   1 
ATOM   5588 N N     . LYS C 1 143 ? 19.661  -18.491 -45.244 1.00 32.48 ?  135 LYS B N     1 
ATOM   5589 C CA    . LYS C 1 143 ? 20.884  -18.830 -44.524 1.00 35.37 ?  135 LYS B CA    1 
ATOM   5590 C C     . LYS C 1 143 ? 21.850  -19.606 -45.411 1.00 36.99 ?  135 LYS B C     1 
ATOM   5591 O O     . LYS C 1 143 ? 23.059  -19.344 -45.404 1.00 38.37 ?  135 LYS B O     1 
ATOM   5592 C CB    . LYS C 1 143 ? 20.541  -19.637 -43.272 1.00 29.09 ?  135 LYS B CB    1 
ATOM   5593 C CG    . LYS C 1 143 ? 21.746  -20.138 -42.492 1.00 40.16 ?  135 LYS B CG    1 
ATOM   5594 C CD    . LYS C 1 143 ? 21.418  -21.432 -41.759 1.00 43.21 ?  135 LYS B CD    1 
ATOM   5595 C CE    . LYS C 1 143 ? 21.952  -21.426 -40.334 1.00 44.48 ?  135 LYS B CE    1 
ATOM   5596 N NZ    . LYS C 1 143 ? 23.414  -21.717 -40.280 1.00 47.34 ?  135 LYS B NZ    1 
ATOM   5597 N N     . GLU C 1 144 ? 21.334  -20.562 -46.186 1.00 32.72 ?  136 GLU B N     1 
ATOM   5598 C CA    . GLU C 1 144 ? 22.207  -21.394 -47.006 1.00 39.00 ?  136 GLU B CA    1 
ATOM   5599 C C     . GLU C 1 144 ? 22.755  -20.622 -48.200 1.00 37.67 ?  136 GLU B C     1 
ATOM   5600 O O     . GLU C 1 144 ? 23.942  -20.735 -48.528 1.00 39.83 ?  136 GLU B O     1 
ATOM   5601 C CB    . GLU C 1 144 ? 21.456  -22.638 -47.481 1.00 34.53 ?  136 GLU B CB    1 
ATOM   5602 C CG    . GLU C 1 144 ? 21.816  -23.916 -46.735 1.00 46.42 ?  136 GLU B CG    1 
ATOM   5603 C CD    . GLU C 1 144 ? 21.701  -23.771 -45.231 1.00 52.74 ?  136 GLU B CD    1 
ATOM   5604 O OE1   . GLU C 1 144 ? 20.597  -23.448 -44.745 1.00 57.24 ?  136 GLU B OE1   1 
ATOM   5605 O OE2   . GLU C 1 144 ? 22.714  -23.983 -44.532 1.00 54.07 ?  136 GLU B OE2   1 
ATOM   5606 N N     . GLU C 1 145 ? 21.910  -19.827 -48.856 1.00 36.03 ?  137 GLU B N     1 
ATOM   5607 C CA    . GLU C 1 145 ? 22.300  -19.204 -50.115 1.00 36.73 ?  137 GLU B CA    1 
ATOM   5608 C C     . GLU C 1 145 ? 23.187  -17.980 -49.912 1.00 41.51 ?  137 GLU B C     1 
ATOM   5609 O O     . GLU C 1 145 ? 24.037  -17.691 -50.763 1.00 39.09 ?  137 GLU B O     1 
ATOM   5610 C CB    . GLU C 1 145 ? 21.043  -18.844 -50.912 1.00 37.79 ?  137 GLU B CB    1 
ATOM   5611 C CG    . GLU C 1 145 ? 21.157  -17.617 -51.792 1.00 47.83 ?  137 GLU B CG    1 
ATOM   5612 C CD    . GLU C 1 145 ? 20.097  -17.586 -52.875 1.00 57.33 ?  137 GLU B CD    1 
ATOM   5613 O OE1   . GLU C 1 145 ? 20.381  -17.057 -53.971 1.00 57.30 ?  137 GLU B OE1   1 
ATOM   5614 O OE2   . GLU C 1 145 ? 18.979  -18.090 -52.628 1.00 61.43 ?  137 GLU B OE2   1 
ATOM   5615 N N     . HIS C 1 146 ? 23.037  -17.269 -48.791 1.00 39.98 ?  138 HIS B N     1 
ATOM   5616 C CA    . HIS C 1 146 ? 23.767  -16.028 -48.567 1.00 38.65 ?  138 HIS B CA    1 
ATOM   5617 C C     . HIS C 1 146 ? 24.655  -16.027 -47.331 1.00 36.03 ?  138 HIS B C     1 
ATOM   5618 O O     . HIS C 1 146 ? 25.447  -15.090 -47.170 1.00 37.37 ?  138 HIS B O     1 
ATOM   5619 C CB    . HIS C 1 146 ? 22.790  -14.847 -48.473 1.00 38.96 ?  138 HIS B CB    1 
ATOM   5620 C CG    . HIS C 1 146 ? 21.999  -14.624 -49.722 1.00 37.69 ?  138 HIS B CG    1 
ATOM   5621 N ND1   . HIS C 1 146 ? 20.624  -14.711 -49.758 1.00 39.26 ?  138 HIS B ND1   1 
ATOM   5622 C CD2   . HIS C 1 146 ? 22.390  -14.330 -50.983 1.00 39.11 ?  138 HIS B CD2   1 
ATOM   5623 C CE1   . HIS C 1 146 ? 20.203  -14.472 -50.987 1.00 41.82 ?  138 HIS B CE1   1 
ATOM   5624 N NE2   . HIS C 1 146 ? 21.255  -14.241 -51.751 1.00 40.08 ?  138 HIS B NE2   1 
ATOM   5625 N N     . GLY C 1 147 ? 24.549  -17.025 -46.457 1.00 36.22 ?  139 GLY B N     1 
ATOM   5626 C CA    . GLY C 1 147 ? 25.450  -17.109 -45.325 1.00 30.09 ?  139 GLY B CA    1 
ATOM   5627 C C     . GLY C 1 147 ? 25.056  -16.289 -44.121 1.00 32.37 ?  139 GLY B C     1 
ATOM   5628 O O     . GLY C 1 147 ? 25.913  -15.993 -43.280 1.00 30.09 ?  139 GLY B O     1 
ATOM   5629 N N     . TYR C 1 148 ? 23.788  -15.906 -44.011 1.00 28.63 ?  140 TYR B N     1 
ATOM   5630 C CA    . TYR C 1 148 ? 23.328  -15.175 -42.841 1.00 30.27 ?  140 TYR B CA    1 
ATOM   5631 C C     . TYR C 1 148 ? 23.375  -16.066 -41.604 1.00 27.96 ?  140 TYR B C     1 
ATOM   5632 O O     . TYR C 1 148 ? 23.216  -17.288 -41.683 1.00 32.05 ?  140 TYR B O     1 
ATOM   5633 C CB    . TYR C 1 148 ? 21.907  -14.656 -43.058 1.00 29.70 ?  140 TYR B CB    1 
ATOM   5634 C CG    . TYR C 1 148 ? 21.717  -13.853 -44.328 1.00 30.93 ?  140 TYR B CG    1 
ATOM   5635 C CD1   . TYR C 1 148 ? 22.734  -13.046 -44.826 1.00 29.86 ?  140 TYR B CD1   1 
ATOM   5636 C CD2   . TYR C 1 148 ? 20.515  -13.892 -45.020 1.00 34.44 ?  140 TYR B CD2   1 
ATOM   5637 C CE1   . TYR C 1 148 ? 22.557  -12.307 -45.983 1.00 37.63 ?  140 TYR B CE1   1 
ATOM   5638 C CE2   . TYR C 1 148 ? 20.329  -13.158 -46.176 1.00 36.14 ?  140 TYR B CE2   1 
ATOM   5639 C CZ    . TYR C 1 148 ? 21.352  -12.367 -46.652 1.00 37.91 ?  140 TYR B CZ    1 
ATOM   5640 O OH    . TYR C 1 148 ? 21.165  -11.637 -47.804 1.00 37.03 ?  140 TYR B OH    1 
ATOM   5641 N N     . PHE C 1 149 ? 23.599  -15.442 -40.451 1.00 29.31 ?  141 PHE B N     1 
ATOM   5642 C CA    . PHE C 1 149 ? 23.670  -16.161 -39.187 1.00 27.86 ?  141 PHE B CA    1 
ATOM   5643 C C     . PHE C 1 149 ? 22.272  -16.348 -38.613 1.00 27.62 ?  141 PHE B C     1 
ATOM   5644 O O     . PHE C 1 149 ? 21.523  -15.381 -38.456 1.00 25.78 ?  141 PHE B O     1 
ATOM   5645 C CB    . PHE C 1 149 ? 24.555  -15.413 -38.191 1.00 30.57 ?  141 PHE B CB    1 
ATOM   5646 C CG    . PHE C 1 149 ? 24.548  -16.004 -36.807 1.00 27.77 ?  141 PHE B CG    1 
ATOM   5647 C CD1   . PHE C 1 149 ? 25.271  -17.152 -36.524 1.00 28.35 ?  141 PHE B CD1   1 
ATOM   5648 C CD2   . PHE C 1 149 ? 23.822  -15.408 -35.788 1.00 31.73 ?  141 PHE B CD2   1 
ATOM   5649 C CE1   . PHE C 1 149 ? 25.267  -17.698 -35.249 1.00 29.02 ?  141 PHE B CE1   1 
ATOM   5650 C CE2   . PHE C 1 149 ? 23.813  -15.948 -34.512 1.00 29.96 ?  141 PHE B CE2   1 
ATOM   5651 C CZ    . PHE C 1 149 ? 24.536  -17.095 -34.242 1.00 29.67 ?  141 PHE B CZ    1 
ATOM   5652 N N     . GLU C 1 150 ? 21.929  -17.590 -38.297 1.00 28.07 ?  142 GLU B N     1 
ATOM   5653 C CA    . GLU C 1 150 ? 20.629  -17.907 -37.719 1.00 27.49 ?  142 GLU B CA    1 
ATOM   5654 C C     . GLU C 1 150 ? 20.792  -18.216 -36.238 1.00 28.49 ?  142 GLU B C     1 
ATOM   5655 O O     . GLU C 1 150 ? 21.415  -19.231 -35.888 1.00 29.74 ?  142 GLU B O     1 
ATOM   5656 C CB    . GLU C 1 150 ? 19.988  -19.090 -38.446 1.00 28.89 ?  142 GLU B CB    1 
ATOM   5657 C CG    . GLU C 1 150 ? 18.554  -19.370 -38.037 1.00 35.37 ?  142 GLU B CG    1 
ATOM   5658 C CD    . GLU C 1 150 ? 17.967  -20.560 -38.769 1.00 39.32 ?  142 GLU B CD    1 
ATOM   5659 O OE1   . GLU C 1 150 ? 18.746  -21.436 -39.199 1.00 44.76 ?  142 GLU B OE1   1 
ATOM   5660 O OE2   . GLU C 1 150 ? 16.729  -20.615 -38.924 1.00 42.24 ?  142 GLU B OE2   1 
ATOM   5661 N N     . PRO C 1 151 ? 20.270  -17.376 -35.341 1.00 27.35 ?  143 PRO B N     1 
ATOM   5662 C CA    . PRO C 1 151 ? 20.411  -17.655 -33.901 1.00 26.94 ?  143 PRO B CA    1 
ATOM   5663 C C     . PRO C 1 151 ? 19.788  -18.970 -33.462 1.00 30.77 ?  143 PRO B C     1 
ATOM   5664 O O     . PRO C 1 151 ? 20.319  -19.611 -32.546 1.00 29.24 ?  143 PRO B O     1 
ATOM   5665 C CB    . PRO C 1 151 ? 19.706  -16.460 -33.242 1.00 29.92 ?  143 PRO B CB    1 
ATOM   5666 C CG    . PRO C 1 151 ? 19.744  -15.378 -34.265 1.00 29.37 ?  143 PRO B CG    1 
ATOM   5667 C CD    . PRO C 1 151 ? 19.688  -16.049 -35.603 1.00 29.68 ?  143 PRO B CD    1 
ATOM   5668 N N     . GLN C 1 152 ? 18.679  -19.385 -34.081 1.00 26.83 ?  144 GLN B N     1 
ATOM   5669 C CA    . GLN C 1 152 ? 17.964  -20.602 -33.703 1.00 30.29 ?  144 GLN B CA    1 
ATOM   5670 C C     . GLN C 1 152 ? 17.580  -20.571 -32.228 1.00 27.51 ?  144 GLN B C     1 
ATOM   5671 O O     . GLN C 1 152 ? 18.252  -21.185 -31.393 1.00 31.17 ?  144 GLN B O     1 
ATOM   5672 C CB    . GLN C 1 152 ? 18.807  -21.844 -34.005 1.00 29.03 ?  144 GLN B CB    1 
ATOM   5673 C CG    . GLN C 1 152 ? 19.339  -21.907 -35.425 1.00 33.70 ?  144 GLN B CG    1 
ATOM   5674 C CD    . GLN C 1 152 ? 20.228  -23.113 -35.658 1.00 37.66 ?  144 GLN B CD    1 
ATOM   5675 O OE1   . GLN C 1 152 ? 19.820  -24.252 -35.432 1.00 37.55 ?  144 GLN B OE1   1 
ATOM   5676 N NE2   . GLN C 1 152 ? 21.453  -22.867 -36.107 1.00 42.81 ?  144 GLN B NE2   1 
ATOM   5677 N N     . GLN C 1 153 ? 16.490  -19.872 -31.902 1.00 26.96 ?  145 GLN B N     1 
ATOM   5678 C CA    . GLN C 1 153 ? 16.125  -19.649 -30.507 1.00 26.95 ?  145 GLN B CA    1 
ATOM   5679 C C     . GLN C 1 153 ? 15.744  -20.932 -29.776 1.00 29.90 ?  145 GLN B C     1 
ATOM   5680 O O     . GLN C 1 153 ? 15.786  -20.958 -28.541 1.00 31.29 ?  145 GLN B O     1 
ATOM   5681 C CB    . GLN C 1 153 ? 14.973  -18.647 -30.424 1.00 30.56 ?  145 GLN B CB    1 
ATOM   5682 C CG    . GLN C 1 153 ? 13.668  -19.148 -31.018 1.00 26.35 ?  145 GLN B CG    1 
ATOM   5683 C CD    . GLN C 1 153 ? 12.534  -18.159 -30.838 1.00 31.91 ?  145 GLN B CD    1 
ATOM   5684 O OE1   . GLN C 1 153 ? 12.352  -17.601 -29.756 1.00 36.15 ?  145 GLN B OE1   1 
ATOM   5685 N NE2   . GLN C 1 153 ? 11.768  -17.931 -31.900 1.00 26.88 ?  145 GLN B NE2   1 
ATOM   5686 N N     . PHE C 1 154 ? 15.378  -21.987 -30.497 1.00 26.63 ?  146 PHE B N     1 
ATOM   5687 C CA    . PHE C 1 154 ? 14.961  -23.238 -29.876 1.00 27.12 ?  146 PHE B CA    1 
ATOM   5688 C C     . PHE C 1 154 ? 16.100  -24.235 -29.714 1.00 29.98 ?  146 PHE B C     1 
ATOM   5689 O O     . PHE C 1 154 ? 15.870  -25.331 -29.194 1.00 28.08 ?  146 PHE B O     1 
ATOM   5690 C CB    . PHE C 1 154 ? 13.833  -23.883 -30.687 1.00 24.96 ?  146 PHE B CB    1 
ATOM   5691 C CG    . PHE C 1 154 ? 12.567  -23.077 -30.715 1.00 28.14 ?  146 PHE B CG    1 
ATOM   5692 C CD1   . PHE C 1 154 ? 11.694  -23.096 -29.640 1.00 22.19 ?  146 PHE B CD1   1 
ATOM   5693 C CD2   . PHE C 1 154 ? 12.248  -22.303 -31.818 1.00 25.82 ?  146 PHE B CD2   1 
ATOM   5694 C CE1   . PHE C 1 154 ? 10.525  -22.356 -29.665 1.00 25.43 ?  146 PHE B CE1   1 
ATOM   5695 C CE2   . PHE C 1 154 ? 11.081  -21.561 -31.849 1.00 27.63 ?  146 PHE B CE2   1 
ATOM   5696 C CZ    . PHE C 1 154 ? 10.218  -21.587 -30.771 1.00 24.97 ?  146 PHE B CZ    1 
ATOM   5697 N N     . GLU C 1 155 ? 17.313  -23.888 -30.143 1.00 28.66 ?  147 GLU B N     1 
ATOM   5698 C CA    . GLU C 1 155 ? 18.447  -24.801 -30.049 1.00 30.24 ?  147 GLU B CA    1 
ATOM   5699 C C     . GLU C 1 155 ? 19.658  -24.127 -29.415 1.00 30.77 ?  147 GLU B C     1 
ATOM   5700 O O     . GLU C 1 155 ? 20.484  -24.794 -28.785 1.00 24.57 ?  147 GLU B O     1 
ATOM   5701 C CB    . GLU C 1 155 ? 18.819  -25.341 -31.434 1.00 31.33 ?  147 GLU B CB    1 
ATOM   5702 C CG    . GLU C 1 155 ? 17.693  -26.057 -32.162 1.00 27.13 ?  147 GLU B CG    1 
ATOM   5703 C CD    . GLU C 1 155 ? 17.458  -27.460 -31.639 1.00 35.32 ?  147 GLU B CD    1 
ATOM   5704 O OE1   . GLU C 1 155 ? 18.406  -28.062 -31.090 1.00 36.06 ?  147 GLU B OE1   1 
ATOM   5705 O OE2   . GLU C 1 155 ? 16.325  -27.964 -31.780 1.00 42.13 ?  147 GLU B OE2   1 
ATOM   5706 N N     . ASN C 1 156 ? 19.769  -22.815 -29.575 1.00 27.91 ?  148 ASN B N     1 
ATOM   5707 C CA    . ASN C 1 156 ? 20.945  -22.081 -29.124 1.00 27.79 ?  148 ASN B CA    1 
ATOM   5708 C C     . ASN C 1 156 ? 21.072  -22.158 -27.607 1.00 28.45 ?  148 ASN B C     1 
ATOM   5709 O O     . ASN C 1 156 ? 20.197  -21.648 -26.893 1.00 29.34 ?  148 ASN B O     1 
ATOM   5710 C CB    . ASN C 1 156 ? 20.866  -20.627 -29.579 1.00 28.00 ?  148 ASN B CB    1 
ATOM   5711 C CG    . ASN C 1 156 ? 22.197  -19.904 -29.479 1.00 25.95 ?  148 ASN B CG    1 
ATOM   5712 O OD1   . ASN C 1 156 ? 22.951  -20.087 -28.523 1.00 24.64 ?  148 ASN B OD1   1 
ATOM   5713 N ND2   . ASN C 1 156 ? 22.495  -19.082 -30.477 1.00 30.03 ?  148 ASN B ND2   1 
ATOM   5714 N N     . PRO C 1 157 ? 22.140  -22.760 -27.074 1.00 26.59 ?  149 PRO B N     1 
ATOM   5715 C CA    . PRO C 1 157 ? 22.269  -22.883 -25.611 1.00 29.08 ?  149 PRO B CA    1 
ATOM   5716 C C     . PRO C 1 157 ? 22.464  -21.557 -24.893 1.00 29.19 ?  149 PRO B C     1 
ATOM   5717 O O     . PRO C 1 157 ? 22.316  -21.518 -23.665 1.00 27.94 ?  149 PRO B O     1 
ATOM   5718 C CB    . PRO C 1 157 ? 23.493  -23.789 -25.432 1.00 32.41 ?  149 PRO B CB    1 
ATOM   5719 C CG    . PRO C 1 157 ? 24.215  -23.780 -26.729 1.00 34.45 ?  149 PRO B CG    1 
ATOM   5720 C CD    . PRO C 1 157 ? 23.294  -23.309 -27.806 1.00 32.35 ?  149 PRO B CD    1 
ATOM   5721 N N     . ALA C 1 158 ? 22.791  -20.477 -25.608 1.00 26.96 ?  150 ALA B N     1 
ATOM   5722 C CA    . ALA C 1 158 ? 22.868  -19.162 -24.985 1.00 29.82 ?  150 ALA B CA    1 
ATOM   5723 C C     . ALA C 1 158 ? 21.518  -18.706 -24.449 1.00 28.11 ?  150 ALA B C     1 
ATOM   5724 O O     . ALA C 1 158 ? 21.469  -17.872 -23.540 1.00 28.32 ?  150 ALA B O     1 
ATOM   5725 C CB    . ALA C 1 158 ? 23.407  -18.138 -25.983 1.00 29.68 ?  150 ALA B CB    1 
ATOM   5726 N N     . ASN C 1 159 ? 20.422  -19.243 -24.990 1.00 25.54 ?  151 ASN B N     1 
ATOM   5727 C CA    . ASN C 1 159 ? 19.089  -18.895 -24.499 1.00 25.65 ?  151 ASN B CA    1 
ATOM   5728 C C     . ASN C 1 159 ? 18.897  -19.380 -23.067 1.00 22.73 ?  151 ASN B C     1 
ATOM   5729 O O     . ASN C 1 159 ? 18.694  -18.538 -22.177 1.00 23.76 ?  151 ASN B O     1 
ATOM   5730 C CB    . ASN C 1 159 ? 18.043  -19.421 -25.496 1.00 22.22 ?  151 ASN B CB    1 
ATOM   5731 C CG    . ASN C 1 159 ? 16.602  -19.344 -24.981 1.00 23.48 ?  151 ASN B CG    1 
ATOM   5732 O OD1   . ASN C 1 159 ? 16.320  -18.844 -23.893 1.00 23.77 ?  151 ASN B OD1   1 
ATOM   5733 N ND2   . ASN C 1 159 ? 15.678  -19.863 -25.785 1.00 19.68 ?  151 ASN B ND2   1 
ATOM   5734 N N     . PRO C 1 160 ? 18.975  -20.682 -22.757 1.00 26.09 ?  152 PRO B N     1 
ATOM   5735 C CA    . PRO C 1 160 ? 18.836  -21.088 -21.349 1.00 24.38 ?  152 PRO B CA    1 
ATOM   5736 C C     . PRO C 1 160 ? 20.009  -20.668 -20.485 1.00 28.27 ?  152 PRO B C     1 
ATOM   5737 O O     . PRO C 1 160 ? 19.857  -20.599 -19.258 1.00 26.39 ?  152 PRO B O     1 
ATOM   5738 C CB    . PRO C 1 160 ? 18.722  -22.614 -21.429 1.00 27.06 ?  152 PRO B CB    1 
ATOM   5739 C CG    . PRO C 1 160 ? 19.419  -22.980 -22.677 1.00 24.64 ?  152 PRO B CG    1 
ATOM   5740 C CD    . PRO C 1 160 ? 19.193  -21.849 -23.634 1.00 23.14 ?  152 PRO B CD    1 
ATOM   5741 N N     . GLU C 1 161 ? 21.169  -20.378 -21.082 1.00 25.05 ?  153 GLU B N     1 
ATOM   5742 C CA    . GLU C 1 161 ? 22.333  -19.995 -20.291 1.00 27.80 ?  153 GLU B CA    1 
ATOM   5743 C C     . GLU C 1 161 ? 22.171  -18.602 -19.698 1.00 25.34 ?  153 GLU B C     1 
ATOM   5744 O O     . GLU C 1 161 ? 22.576  -18.361 -18.555 1.00 27.38 ?  153 GLU B O     1 
ATOM   5745 C CB    . GLU C 1 161 ? 23.600  -20.063 -21.143 1.00 28.18 ?  153 GLU B CB    1 
ATOM   5746 C CG    . GLU C 1 161 ? 24.888  -19.990 -20.335 1.00 32.80 ?  153 GLU B CG    1 
ATOM   5747 C CD    . GLU C 1 161 ? 26.055  -19.448 -21.139 1.00 38.71 ?  153 GLU B CD    1 
ATOM   5748 O OE1   . GLU C 1 161 ? 25.835  -18.541 -21.970 1.00 44.31 ?  153 GLU B OE1   1 
ATOM   5749 O OE2   . GLU C 1 161 ? 27.193  -19.926 -20.942 1.00 43.57 ?  153 GLU B OE2   1 
ATOM   5750 N N     . VAL C 1 162 ? 21.588  -17.668 -20.455 1.00 21.07 ?  154 VAL B N     1 
ATOM   5751 C CA    . VAL C 1 162 ? 21.445  -16.309 -19.943 1.00 24.18 ?  154 VAL B CA    1 
ATOM   5752 C C     . VAL C 1 162 ? 20.481  -16.269 -18.762 1.00 24.36 ?  154 VAL B C     1 
ATOM   5753 O O     . VAL C 1 162 ? 20.640  -15.446 -17.854 1.00 25.21 ?  154 VAL B O     1 
ATOM   5754 C CB    . VAL C 1 162 ? 21.026  -15.344 -21.069 1.00 22.53 ?  154 VAL B CB    1 
ATOM   5755 C CG1   . VAL C 1 162 ? 19.530  -15.415 -21.335 1.00 21.09 ?  154 VAL B CG1   1 
ATOM   5756 C CG2   . VAL C 1 162 ? 21.442  -13.920 -20.723 1.00 19.85 ?  154 VAL B CG2   1 
ATOM   5757 N N     . HIS C 1 163 ? 19.482  -17.154 -18.735 1.00 22.24 ?  155 HIS B N     1 
ATOM   5758 C CA    . HIS C 1 163 ? 18.631  -17.247 -17.555 1.00 24.97 ?  155 HIS B CA    1 
ATOM   5759 C C     . HIS C 1 163 ? 19.379  -17.886 -16.396 1.00 26.89 ?  155 HIS B C     1 
ATOM   5760 O O     . HIS C 1 163 ? 19.130  -17.552 -15.231 1.00 27.71 ?  155 HIS B O     1 
ATOM   5761 C CB    . HIS C 1 163 ? 17.364  -18.035 -17.881 1.00 25.25 ?  155 HIS B CB    1 
ATOM   5762 C CG    . HIS C 1 163 ? 16.492  -17.370 -18.899 1.00 24.07 ?  155 HIS B CG    1 
ATOM   5763 N ND1   . HIS C 1 163 ? 15.793  -16.212 -18.637 1.00 22.59 ?  155 HIS B ND1   1 
ATOM   5764 C CD2   . HIS C 1 163 ? 16.222  -17.690 -20.187 1.00 20.38 ?  155 HIS B CD2   1 
ATOM   5765 C CE1   . HIS C 1 163 ? 15.120  -15.854 -19.717 1.00 23.17 ?  155 HIS B CE1   1 
ATOM   5766 N NE2   . HIS C 1 163 ? 15.364  -16.734 -20.671 1.00 21.36 ?  155 HIS B NE2   1 
ATOM   5767 N N     . GLU C 1 164 ? 20.300  -18.799 -16.702 1.00 27.87 ?  156 GLU B N     1 
ATOM   5768 C CA    . GLU C 1 164 ? 21.164  -19.375 -15.679 1.00 28.98 ?  156 GLU B CA    1 
ATOM   5769 C C     . GLU C 1 164 ? 22.137  -18.342 -15.124 1.00 28.00 ?  156 GLU B C     1 
ATOM   5770 O O     . GLU C 1 164 ? 22.524  -18.423 -13.953 1.00 26.67 ?  156 GLU B O     1 
ATOM   5771 C CB    . GLU C 1 164 ? 21.919  -20.568 -16.268 1.00 30.42 ?  156 GLU B CB    1 
ATOM   5772 C CG    . GLU C 1 164 ? 22.854  -21.280 -15.311 1.00 35.72 ?  156 GLU B CG    1 
ATOM   5773 C CD    . GLU C 1 164 ? 23.561  -22.456 -15.961 1.00 33.61 ?  156 GLU B CD    1 
ATOM   5774 O OE1   . GLU C 1 164 ? 23.153  -22.863 -17.071 1.00 37.99 ?  156 GLU B OE1   1 
ATOM   5775 O OE2   . GLU C 1 164 ? 24.527  -22.973 -15.363 1.00 37.68 ?  156 GLU B OE2   1 
ATOM   5776 N N     . LEU C 1 165 ? 22.534  -17.361 -15.934 1.00 23.73 ?  157 LEU B N     1 
ATOM   5777 C CA    . LEU C 1 165 ? 23.526  -16.384 -15.504 1.00 25.89 ?  157 LEU B CA    1 
ATOM   5778 C C     . LEU C 1 165 ? 22.916  -15.112 -14.935 1.00 27.24 ?  157 LEU B C     1 
ATOM   5779 O O     . LEU C 1 165 ? 23.555  -14.450 -14.109 1.00 24.29 ?  157 LEU B O     1 
ATOM   5780 C CB    . LEU C 1 165 ? 24.447  -16.015 -16.671 1.00 30.12 ?  157 LEU B CB    1 
ATOM   5781 C CG    . LEU C 1 165 ? 25.383  -17.105 -17.196 1.00 30.32 ?  157 LEU B CG    1 
ATOM   5782 C CD1   . LEU C 1 165 ? 26.116  -16.620 -18.436 1.00 36.18 ?  157 LEU B CD1   1 
ATOM   5783 C CD2   . LEU C 1 165 ? 26.370  -17.528 -16.120 1.00 25.11 ?  157 LEU B CD2   1 
ATOM   5784 N N     . THR C 1 166 ? 21.701  -14.745 -15.354 1.00 27.12 ?  158 THR B N     1 
ATOM   5785 C CA    . THR C 1 166 ? 21.102  -13.474 -14.951 1.00 26.39 ?  158 THR B CA    1 
ATOM   5786 C C     . THR C 1 166 ? 19.756  -13.677 -14.267 1.00 30.49 ?  158 THR B C     1 
ATOM   5787 O O     . THR C 1 166 ? 19.631  -13.367 -13.080 1.00 30.03 ?  158 THR B O     1 
ATOM   5788 C CB    . THR C 1 166 ? 20.968  -12.547 -16.160 1.00 30.92 ?  158 THR B CB    1 
ATOM   5789 O OG1   . THR C 1 166 ? 20.204  -13.200 -17.182 1.00 28.07 ?  158 THR B OG1   1 
ATOM   5790 C CG2   . THR C 1 166 ? 22.338  -12.182 -16.708 1.00 28.01 ?  158 THR B CG2   1 
ATOM   5791 N N     . THR C 1 167 ? 18.740  -14.177 -14.978 1.00 28.55 ?  159 THR B N     1 
ATOM   5792 C CA    . THR C 1 167 ? 17.396  -14.251 -14.410 1.00 28.54 ?  159 THR B CA    1 
ATOM   5793 C C     . THR C 1 167 ? 17.382  -15.058 -13.118 1.00 27.60 ?  159 THR B C     1 
ATOM   5794 O O     . THR C 1 167 ? 16.799  -14.634 -12.114 1.00 24.74 ?  159 THR B O     1 
ATOM   5795 C CB    . THR C 1 167 ? 16.422  -14.852 -15.424 1.00 28.67 ?  159 THR B CB    1 
ATOM   5796 O OG1   . THR C 1 167 ? 16.733  -14.369 -16.737 1.00 25.01 ?  159 THR B OG1   1 
ATOM   5797 C CG2   . THR C 1 167 ? 14.995  -14.462 -15.075 1.00 26.51 ?  159 THR B CG2   1 
ATOM   5798 N N     . GLY C 1 168 ? 18.028  -16.221 -13.123 1.00 34.24 ?  160 GLY B N     1 
ATOM   5799 C CA    . GLY C 1 168 ? 18.119  -17.057 -11.950 1.00 28.42 ?  160 GLY B CA    1 
ATOM   5800 C C     . GLY C 1 168 ? 18.790  -16.368 -10.777 1.00 28.70 ?  160 GLY B C     1 
ATOM   5801 O O     . GLY C 1 168 ? 18.197  -16.201 -9.707  1.00 26.99 ?  160 GLY B O     1 
ATOM   5802 N N     . PRO C 1 169 ? 20.053  -15.967 -10.953 1.00 34.03 ?  161 PRO B N     1 
ATOM   5803 C CA    . PRO C 1 169 ? 20.753  -15.262 -9.865  1.00 27.18 ?  161 PRO B CA    1 
ATOM   5804 C C     . PRO C 1 169 ? 20.037  -14.013 -9.384  1.00 25.66 ?  161 PRO B C     1 
ATOM   5805 O O     . PRO C 1 169 ? 20.151  -13.667 -8.201  1.00 28.26 ?  161 PRO B O     1 
ATOM   5806 C CB    . PRO C 1 169 ? 22.116  -14.927 -10.486 1.00 26.61 ?  161 PRO B CB    1 
ATOM   5807 C CG    . PRO C 1 169 ? 22.315  -15.958 -11.538 1.00 30.66 ?  161 PRO B CG    1 
ATOM   5808 C CD    . PRO C 1 169 ? 20.957  -16.316 -12.064 1.00 31.88 ?  161 PRO B CD    1 
ATOM   5809 N N     . GLU C 1 170 ? 19.309  -13.319 -10.265 1.00 30.81 ?  162 GLU B N     1 
ATOM   5810 C CA    . GLU C 1 170 ? 18.493  -12.193 -9.819  1.00 28.62 ?  162 GLU B CA    1 
ATOM   5811 C C     . GLU C 1 170 ? 17.465  -12.639 -8.789  1.00 27.75 ?  162 GLU B C     1 
ATOM   5812 O O     . GLU C 1 170 ? 17.264  -11.969 -7.770  1.00 25.90 ?  162 GLU B O     1 
ATOM   5813 C CB    . GLU C 1 170 ? 17.796  -11.537 -11.012 1.00 26.26 ?  162 GLU B CB    1 
ATOM   5814 C CG    . GLU C 1 170 ? 18.681  -10.614 -11.834 1.00 30.47 ?  162 GLU B CG    1 
ATOM   5815 C CD    . GLU C 1 170 ? 18.014  -10.162 -13.118 1.00 31.32 ?  162 GLU B CD    1 
ATOM   5816 O OE1   . GLU C 1 170 ? 16.767  -10.199 -13.185 1.00 30.19 ?  162 GLU B OE1   1 
ATOM   5817 O OE2   . GLU C 1 170 ? 18.734  -9.771  -14.062 1.00 26.15 ?  162 GLU B OE2   1 
ATOM   5818 N N     . LEU C 1 171 ? 16.810  -13.775 -9.034  1.00 23.92 ?  163 LEU B N     1 
ATOM   5819 C CA    . LEU C 1 171 ? 15.792  -14.257 -8.107  1.00 30.05 ?  163 LEU B CA    1 
ATOM   5820 C C     . LEU C 1 171 ? 16.411  -14.711 -6.791  1.00 29.71 ?  163 LEU B C     1 
ATOM   5821 O O     . LEU C 1 171 ? 15.798  -14.555 -5.728  1.00 30.40 ?  163 LEU B O     1 
ATOM   5822 C CB    . LEU C 1 171 ? 14.995  -15.391 -8.748  1.00 26.34 ?  163 LEU B CB    1 
ATOM   5823 C CG    . LEU C 1 171 ? 13.889  -14.960 -9.711  1.00 30.39 ?  163 LEU B CG    1 
ATOM   5824 C CD1   . LEU C 1 171 ? 13.340  -16.162 -10.458 1.00 25.74 ?  163 LEU B CD1   1 
ATOM   5825 C CD2   . LEU C 1 171 ? 12.780  -14.238 -8.962  1.00 23.20 ?  163 LEU B CD2   1 
ATOM   5826 N N     . LEU C 1 172 ? 17.619  -15.280 -6.842  1.00 31.84 ?  164 LEU B N     1 
ATOM   5827 C CA    . LEU C 1 172 ? 18.309  -15.663 -5.613  1.00 30.93 ?  164 LEU B CA    1 
ATOM   5828 C C     . LEU C 1 172 ? 18.568  -14.448 -4.733  1.00 31.01 ?  164 LEU B C     1 
ATOM   5829 O O     . LEU C 1 172 ? 18.268  -14.458 -3.533  1.00 34.33 ?  164 LEU B O     1 
ATOM   5830 C CB    . LEU C 1 172 ? 19.624  -16.374 -5.938  1.00 27.37 ?  164 LEU B CB    1 
ATOM   5831 C CG    . LEU C 1 172 ? 19.556  -17.812 -6.453  1.00 35.35 ?  164 LEU B CG    1 
ATOM   5832 C CD1   . LEU C 1 172 ? 20.945  -18.443 -6.481  1.00 36.33 ?  164 LEU B CD1   1 
ATOM   5833 C CD2   . LEU C 1 172 ? 18.599  -18.634 -5.608  1.00 35.38 ?  164 LEU B CD2   1 
ATOM   5834 N N     . GLN C 1 173 ? 19.133  -13.390 -5.314  1.00 30.28 ?  165 GLN B N     1 
ATOM   5835 C CA    . GLN C 1 173 ? 19.340  -12.161 -4.558  1.00 32.11 ?  165 GLN B CA    1 
ATOM   5836 C C     . GLN C 1 173 ? 18.014  -11.548 -4.128  1.00 36.65 ?  165 GLN B C     1 
ATOM   5837 O O     . GLN C 1 173 ? 17.892  -11.036 -3.008  1.00 37.17 ?  165 GLN B O     1 
ATOM   5838 C CB    . GLN C 1 173 ? 20.141  -11.163 -5.391  1.00 34.68 ?  165 GLN B CB    1 
ATOM   5839 C CG    . GLN C 1 173 ? 20.820  -10.081 -4.576  1.00 50.88 ?  165 GLN B CG    1 
ATOM   5840 C CD    . GLN C 1 173 ? 20.695  -8.720  -5.222  1.00 58.92 ?  165 GLN B CD    1 
ATOM   5841 O OE1   . GLN C 1 173 ? 21.054  -8.539  -6.384  1.00 59.87 ?  165 GLN B OE1   1 
ATOM   5842 N NE2   . GLN C 1 173 ? 20.174  -7.755  -4.474  1.00 65.03 ?  165 GLN B NE2   1 
ATOM   5843 N N     . GLN C 1 174 ? 17.007  -11.594 -5.005  1.00 34.00 ?  166 GLN B N     1 
ATOM   5844 C CA    . GLN C 1 174 ? 15.718  -10.991 -4.686  1.00 35.76 ?  166 GLN B CA    1 
ATOM   5845 C C     . GLN C 1 174 ? 15.017  -11.725 -3.550  1.00 32.58 ?  166 GLN B C     1 
ATOM   5846 O O     . GLN C 1 174 ? 14.240  -11.116 -2.808  1.00 32.41 ?  166 GLN B O     1 
ATOM   5847 C CB    . GLN C 1 174 ? 14.833  -10.956 -5.933  1.00 32.93 ?  166 GLN B CB    1 
ATOM   5848 C CG    . GLN C 1 174 ? 15.099  -9.758  -6.841  1.00 32.70 ?  166 GLN B CG    1 
ATOM   5849 C CD    . GLN C 1 174 ? 14.449  -9.884  -8.209  1.00 28.58 ?  166 GLN B CD    1 
ATOM   5850 O OE1   . GLN C 1 174 ? 14.488  -10.943 -8.835  1.00 25.18 ?  166 GLN B OE1   1 
ATOM   5851 N NE2   . GLN C 1 174 ? 13.851  -8.795  -8.681  1.00 30.37 ?  166 GLN B NE2   1 
ATOM   5852 N N     . PHE C 1 175 ? 15.282  -13.020 -3.385  1.00 31.66 ?  167 PHE B N     1 
ATOM   5853 C CA    . PHE C 1 175 ? 14.663  -13.804 -2.324  1.00 37.12 ?  167 PHE B CA    1 
ATOM   5854 C C     . PHE C 1 175 ? 15.677  -14.239 -1.270  1.00 36.03 ?  167 PHE B C     1 
ATOM   5855 O O     . PHE C 1 175 ? 15.555  -15.319 -0.687  1.00 35.07 ?  167 PHE B O     1 
ATOM   5856 C CB    . PHE C 1 175 ? 13.927  -15.006 -2.913  1.00 30.30 ?  167 PHE B CB    1 
ATOM   5857 C CG    . PHE C 1 175 ? 12.597  -14.651 -3.512  1.00 27.93 ?  167 PHE B CG    1 
ATOM   5858 C CD1   . PHE C 1 175 ? 12.504  -14.234 -4.828  1.00 25.95 ?  167 PHE B CD1   1 
ATOM   5859 C CD2   . PHE C 1 175 ? 11.443  -14.703 -2.746  1.00 29.40 ?  167 PHE B CD2   1 
ATOM   5860 C CE1   . PHE C 1 175 ? 11.281  -13.893 -5.378  1.00 31.69 ?  167 PHE B CE1   1 
ATOM   5861 C CE2   . PHE C 1 175 ? 10.218  -14.364 -3.289  1.00 33.07 ?  167 PHE B CE2   1 
ATOM   5862 C CZ    . PHE C 1 175 ? 10.137  -13.957 -4.606  1.00 30.16 ?  167 PHE B CZ    1 
ATOM   5863 N N     . GLU C 1 176 ? 16.682  -13.403 -1.021  1.00 39.52 ?  168 GLU B N     1 
ATOM   5864 C CA    . GLU C 1 176 ? 17.570  -13.618 0.113   1.00 44.83 ?  168 GLU B CA    1 
ATOM   5865 C C     . GLU C 1 176 ? 16.780  -13.504 1.411   1.00 44.37 ?  168 GLU B C     1 
ATOM   5866 O O     . GLU C 1 176 ? 15.991  -12.571 1.591   1.00 43.01 ?  168 GLU B O     1 
ATOM   5867 C CB    . GLU C 1 176 ? 18.710  -12.600 0.098   1.00 41.30 ?  168 GLU B CB    1 
ATOM   5868 C CG    . GLU C 1 176 ? 19.968  -13.069 -0.614  1.00 41.61 ?  168 GLU B CG    1 
ATOM   5869 C CD    . GLU C 1 176 ? 20.926  -11.928 -0.905  1.00 50.18 ?  168 GLU B CD    1 
ATOM   5870 O OE1   . GLU C 1 176 ? 20.944  -10.953 -0.124  1.00 54.45 ?  168 GLU B OE1   1 
ATOM   5871 O OE2   . GLU C 1 176 ? 21.663  -12.006 -1.912  1.00 49.27 ?  168 GLU B OE2   1 
ATOM   5872 N N     . GLY C 1 177 ? 16.990  -14.457 2.315   1.00 42.84 ?  169 GLY B N     1 
ATOM   5873 C CA    . GLY C 1 177 ? 16.258  -14.485 3.562   1.00 39.40 ?  169 GLY B CA    1 
ATOM   5874 C C     . GLY C 1 177 ? 14.904  -15.152 3.492   1.00 47.76 ?  169 GLY B C     1 
ATOM   5875 O O     . GLY C 1 177 ? 14.183  -15.162 4.500   1.00 39.26 ?  169 GLY B O     1 
ATOM   5876 N N     . LYS C 1 178 ? 14.530  -15.705 2.341   1.00 44.62 ?  170 LYS B N     1 
ATOM   5877 C CA    . LYS C 1 178 ? 13.273  -16.419 2.187   1.00 40.35 ?  170 LYS B CA    1 
ATOM   5878 C C     . LYS C 1 178 ? 13.532  -17.712 1.429   1.00 37.66 ?  170 LYS B C     1 
ATOM   5879 O O     . LYS C 1 178 ? 14.543  -17.859 0.738   1.00 48.37 ?  170 LYS B O     1 
ATOM   5880 C CB    . LYS C 1 178 ? 12.226  -15.568 1.454   1.00 40.58 ?  170 LYS B CB    1 
ATOM   5881 C CG    . LYS C 1 178 ? 10.794  -16.055 1.622   1.00 48.68 ?  170 LYS B CG    1 
ATOM   5882 C CD    . LYS C 1 178 ? 9.803   -15.116 0.953   1.00 48.14 ?  170 LYS B CD    1 
ATOM   5883 C CE    . LYS C 1 178 ? 9.980   -13.685 1.424   1.00 40.98 ?  170 LYS B CE    1 
ATOM   5884 N NZ    . LYS C 1 178 ? 8.754   -13.201 2.113   1.00 41.41 ?  170 LYS B NZ    1 
ATOM   5885 N N     . THR C 1 179 ? 12.609  -18.657 1.574   1.00 41.64 ?  171 THR B N     1 
ATOM   5886 C CA    . THR C 1 179 ? 12.662  -19.925 0.862   1.00 41.69 ?  171 THR B CA    1 
ATOM   5887 C C     . THR C 1 179 ? 11.599  -19.932 -0.227  1.00 39.19 ?  171 THR B C     1 
ATOM   5888 O O     . THR C 1 179 ? 10.428  -19.645 0.043   1.00 43.42 ?  171 THR B O     1 
ATOM   5889 C CB    . THR C 1 179 ? 12.446  -21.105 1.812   1.00 42.82 ?  171 THR B CB    1 
ATOM   5890 O OG1   . THR C 1 179 ? 11.373  -20.804 2.714   1.00 53.69 ?  171 THR B OG1   1 
ATOM   5891 C CG2   . THR C 1 179 ? 13.708  -21.391 2.610   1.00 37.16 ?  171 THR B CG2   1 
ATOM   5892 N N     . ILE C 1 180 ? 12.007  -20.254 -1.450  1.00 36.61 ?  172 ILE B N     1 
ATOM   5893 C CA    . ILE C 1 180 ? 11.077  -20.395 -2.565  1.00 34.83 ?  172 ILE B CA    1 
ATOM   5894 C C     . ILE C 1 180 ? 10.615  -21.846 -2.613  1.00 30.49 ?  172 ILE B C     1 
ATOM   5895 O O     . ILE C 1 180 ? 11.419  -22.755 -2.847  1.00 34.52 ?  172 ILE B O     1 
ATOM   5896 C CB    . ILE C 1 180 ? 11.724  -19.976 -3.894  1.00 33.39 ?  172 ILE B CB    1 
ATOM   5897 C CG1   . ILE C 1 180 ? 12.255  -18.544 -3.807  1.00 29.36 ?  172 ILE B CG1   1 
ATOM   5898 C CG2   . ILE C 1 180 ? 10.719  -20.097 -5.029  1.00 28.49 ?  172 ILE B CG2   1 
ATOM   5899 C CD1   . ILE C 1 180 ? 13.107  -18.136 -4.992  1.00 24.95 ?  172 ILE B CD1   1 
ATOM   5900 N N     . ASP C 1 181 ? 9.320   -22.064 -2.387  1.00 29.61 ?  173 ASP B N     1 
ATOM   5901 C CA    . ASP C 1 181 ? 8.774   -23.413 -2.336  1.00 31.62 ?  173 ASP B CA    1 
ATOM   5902 C C     . ASP C 1 181 ? 8.398   -23.961 -3.706  1.00 32.43 ?  173 ASP B C     1 
ATOM   5903 O O     . ASP C 1 181 ? 8.318   -25.184 -3.866  1.00 36.14 ?  173 ASP B O     1 
ATOM   5904 C CB    . ASP C 1 181 ? 7.548   -23.447 -1.415  1.00 32.72 ?  173 ASP B CB    1 
ATOM   5905 C CG    . ASP C 1 181 ? 7.892   -23.110 0.027   1.00 35.92 ?  173 ASP B CG    1 
ATOM   5906 O OD1   . ASP C 1 181 ? 8.394   -24.001 0.745   1.00 35.32 ?  173 ASP B OD1   1 
ATOM   5907 O OD2   . ASP C 1 181 ? 7.665   -21.954 0.442   1.00 36.81 ?  173 ASP B OD2   1 
ATOM   5908 N N     . ALA C 1 182 ? 8.173   -23.096 -4.693  1.00 32.80 ?  174 ALA B N     1 
ATOM   5909 C CA    . ALA C 1 182 ? 7.826   -23.545 -6.033  1.00 31.76 ?  174 ALA B CA    1 
ATOM   5910 C C     . ALA C 1 182 ? 8.077   -22.417 -7.020  1.00 32.15 ?  174 ALA B C     1 
ATOM   5911 O O     . ALA C 1 182 ? 7.781   -21.255 -6.730  1.00 33.86 ?  174 ALA B O     1 
ATOM   5912 C CB    . ALA C 1 182 ? 6.363   -24.000 -6.112  1.00 30.88 ?  174 ALA B CB    1 
ATOM   5913 N N     . PHE C 1 183 ? 8.623   -22.769 -8.181  1.00 30.74 ?  175 PHE B N     1 
ATOM   5914 C CA    . PHE C 1 183 ? 8.789   -21.837 -9.287  1.00 27.99 ?  175 PHE B CA    1 
ATOM   5915 C C     . PHE C 1 183 ? 8.064   -22.387 -10.507 1.00 30.47 ?  175 PHE B C     1 
ATOM   5916 O O     . PHE C 1 183 ? 8.187   -23.575 -10.824 1.00 29.66 ?  175 PHE B O     1 
ATOM   5917 C CB    . PHE C 1 183 ? 10.267  -21.599 -9.607  1.00 28.57 ?  175 PHE B CB    1 
ATOM   5918 C CG    . PHE C 1 183 ? 10.488  -20.786 -10.850 1.00 25.88 ?  175 PHE B CG    1 
ATOM   5919 C CD1   . PHE C 1 183 ? 10.404  -19.405 -10.810 1.00 25.86 ?  175 PHE B CD1   1 
ATOM   5920 C CD2   . PHE C 1 183 ? 10.772  -21.402 -12.058 1.00 26.91 ?  175 PHE B CD2   1 
ATOM   5921 C CE1   . PHE C 1 183 ? 10.600  -18.651 -11.949 1.00 27.80 ?  175 PHE B CE1   1 
ATOM   5922 C CE2   . PHE C 1 183 ? 10.969  -20.653 -13.202 1.00 27.25 ?  175 PHE B CE2   1 
ATOM   5923 C CZ    . PHE C 1 183 ? 10.882  -19.276 -13.148 1.00 28.12 ?  175 PHE B CZ    1 
ATOM   5924 N N     . LEU C 1 184 ? 7.314   -21.522 -11.184 1.00 25.41 ?  176 LEU B N     1 
ATOM   5925 C CA    . LEU C 1 184 ? 6.553   -21.889 -12.368 1.00 27.37 ?  176 LEU B CA    1 
ATOM   5926 C C     . LEU C 1 184 ? 6.874   -20.915 -13.491 1.00 31.98 ?  176 LEU B C     1 
ATOM   5927 O O     . LEU C 1 184 ? 7.164   -19.740 -13.248 1.00 28.43 ?  176 LEU B O     1 
ATOM   5928 C CB    . LEU C 1 184 ? 5.040   -21.889 -12.095 1.00 29.27 ?  176 LEU B CB    1 
ATOM   5929 C CG    . LEU C 1 184 ? 4.533   -22.643 -10.863 1.00 30.15 ?  176 LEU B CG    1 
ATOM   5930 C CD1   . LEU C 1 184 ? 4.547   -21.760 -9.629  1.00 31.37 ?  176 LEU B CD1   1 
ATOM   5931 C CD2   . LEU C 1 184 ? 3.136   -23.180 -11.112 1.00 23.84 ?  176 LEU B CD2   1 
ATOM   5932 N N     . ALA C 1 185 ? 6.820   -21.414 -14.726 1.00 26.28 ?  177 ALA B N     1 
ATOM   5933 C CA    . ALA C 1 185 ? 7.094   -20.582 -15.891 1.00 25.25 ?  177 ALA B CA    1 
ATOM   5934 C C     . ALA C 1 185 ? 6.498   -21.239 -17.125 1.00 25.39 ?  177 ALA B C     1 
ATOM   5935 O O     . ALA C 1 185 ? 6.658   -22.447 -17.325 1.00 26.29 ?  177 ALA B O     1 
ATOM   5936 C CB    . ALA C 1 185 ? 8.600   -20.371 -16.081 1.00 22.89 ?  177 ALA B CB    1 
ATOM   5937 N N     . GLY C 1 186 ? 5.812   -20.445 -17.942 1.00 21.46 ?  178 GLY B N     1 
ATOM   5938 C CA    . GLY C 1 186 ? 5.350   -20.949 -19.223 1.00 22.76 ?  178 GLY B CA    1 
ATOM   5939 C C     . GLY C 1 186 ? 6.524   -21.307 -20.116 1.00 27.53 ?  178 GLY B C     1 
ATOM   5940 O O     . GLY C 1 186 ? 7.576   -20.664 -20.083 1.00 23.21 ?  178 GLY B O     1 
ATOM   5941 N N     . VAL C 1 187 ? 6.344   -22.351 -20.918 1.00 24.71 ?  179 VAL B N     1 
ATOM   5942 C CA    . VAL C 1 187 ? 7.410   -22.884 -21.758 1.00 26.97 ?  179 VAL B CA    1 
ATOM   5943 C C     . VAL C 1 187 ? 7.136   -22.470 -23.198 1.00 24.48 ?  179 VAL B C     1 
ATOM   5944 O O     . VAL C 1 187 ? 6.175   -22.939 -23.821 1.00 24.38 ?  179 VAL B O     1 
ATOM   5945 C CB    . VAL C 1 187 ? 7.532   -24.408 -21.626 1.00 24.98 ?  179 VAL B CB    1 
ATOM   5946 C CG1   . VAL C 1 187 ? 8.465   -24.966 -22.692 1.00 24.85 ?  179 VAL B CG1   1 
ATOM   5947 C CG2   . VAL C 1 187 ? 8.028   -24.776 -20.236 1.00 21.35 ?  179 VAL B CG2   1 
ATOM   5948 N N     . GLY C 1 188 ? 7.971   -21.579 -23.722 1.00 25.05 ?  180 GLY B N     1 
ATOM   5949 C CA    . GLY C 1 188 ? 7.985   -21.286 -25.141 1.00 20.83 ?  180 GLY B CA    1 
ATOM   5950 C C     . GLY C 1 188 ? 9.163   -21.995 -25.770 1.00 22.88 ?  180 GLY B C     1 
ATOM   5951 O O     . GLY C 1 188 ? 9.009   -23.063 -26.370 1.00 21.39 ?  180 GLY B O     1 
ATOM   5952 N N     . THR C 1 189 ? 10.353  -21.416 -25.621 1.00 21.11 ?  181 THR B N     1 
ATOM   5953 C CA    . THR C 1 189 ? 11.578  -22.143 -25.916 1.00 21.01 ?  181 THR B CA    1 
ATOM   5954 C C     . THR C 1 189 ? 12.035  -23.000 -24.745 1.00 21.29 ?  181 THR B C     1 
ATOM   5955 O O     . THR C 1 189 ? 12.893  -23.870 -24.929 1.00 25.71 ?  181 THR B O     1 
ATOM   5956 C CB    . THR C 1 189 ? 12.704  -21.178 -26.297 1.00 24.83 ?  181 THR B CB    1 
ATOM   5957 O OG1   . THR C 1 189 ? 13.081  -20.406 -25.150 1.00 16.94 ?  181 THR B OG1   1 
ATOM   5958 C CG2   . THR C 1 189 ? 12.253  -20.239 -27.408 1.00 26.43 ?  181 THR B CG2   1 
ATOM   5959 N N     . GLY C 1 190 ? 11.483  -22.780 -23.554 1.00 22.26 ?  182 GLY B N     1 
ATOM   5960 C CA    . GLY C 1 190 ? 11.932  -23.468 -22.365 1.00 28.10 ?  182 GLY B CA    1 
ATOM   5961 C C     . GLY C 1 190 ? 13.178  -22.893 -21.732 1.00 25.10 ?  182 GLY B C     1 
ATOM   5962 O O     . GLY C 1 190 ? 13.660  -23.453 -20.739 1.00 28.25 ?  182 GLY B O     1 
ATOM   5963 N N     . GLY C 1 191 ? 13.714  -21.794 -22.267 1.00 25.10 ?  183 GLY B N     1 
ATOM   5964 C CA    . GLY C 1 191 ? 14.937  -21.234 -21.716 1.00 27.64 ?  183 GLY B CA    1 
ATOM   5965 C C     . GLY C 1 191 ? 14.753  -20.658 -20.325 1.00 25.32 ?  183 GLY B C     1 
ATOM   5966 O O     . GLY C 1 191 ? 15.622  -20.814 -19.462 1.00 25.82 ?  183 GLY B O     1 
ATOM   5967 N N     . THR C 1 192 ? 13.624  -19.985 -20.086 1.00 26.55 ?  184 THR B N     1 
ATOM   5968 C CA    . THR C 1 192 ? 13.380  -19.392 -18.774 1.00 23.55 ?  184 THR B CA    1 
ATOM   5969 C C     . THR C 1 192 ? 13.269  -20.465 -17.698 1.00 29.58 ?  184 THR B C     1 
ATOM   5970 O O     . THR C 1 192 ? 13.931  -20.389 -16.657 1.00 27.42 ?  184 THR B O     1 
ATOM   5971 C CB    . THR C 1 192 ? 12.111  -18.538 -18.803 1.00 29.21 ?  184 THR B CB    1 
ATOM   5972 O OG1   . THR C 1 192 ? 12.173  -17.612 -19.897 1.00 22.86 ?  184 THR B OG1   1 
ATOM   5973 C CG2   . THR C 1 192 ? 11.959  -17.772 -17.494 1.00 25.61 ?  184 THR B CG2   1 
ATOM   5974 N N     . LEU C 1 193 ? 12.430  -21.477 -17.933 1.00 25.90 ?  185 LEU B N     1 
ATOM   5975 C CA    . LEU C 1 193 ? 12.262  -22.542 -16.950 1.00 28.62 ?  185 LEU B CA    1 
ATOM   5976 C C     . LEU C 1 193 ? 13.561  -23.308 -16.733 1.00 27.60 ?  185 LEU B C     1 
ATOM   5977 O O     . LEU C 1 193 ? 13.914  -23.635 -15.595 1.00 26.70 ?  185 LEU B O     1 
ATOM   5978 C CB    . LEU C 1 193 ? 11.151  -23.492 -17.391 1.00 26.93 ?  185 LEU B CB    1 
ATOM   5979 C CG    . LEU C 1 193 ? 10.719  -24.515 -16.340 1.00 32.90 ?  185 LEU B CG    1 
ATOM   5980 C CD1   . LEU C 1 193 ? 9.738   -23.902 -15.348 1.00 30.61 ?  185 LEU B CD1   1 
ATOM   5981 C CD2   . LEU C 1 193 ? 10.129  -25.747 -17.004 1.00 32.26 ?  185 LEU B CD2   1 
ATOM   5982 N N     . SER C 1 194 ? 14.288  -23.597 -17.815 1.00 26.15 ?  186 SER B N     1 
ATOM   5983 C CA    . SER C 1 194 ? 15.518  -24.374 -17.697 1.00 30.81 ?  186 SER B CA    1 
ATOM   5984 C C     . SER C 1 194 ? 16.596  -23.590 -16.958 1.00 29.42 ?  186 SER B C     1 
ATOM   5985 O O     . SER C 1 194 ? 17.211  -24.100 -16.015 1.00 28.53 ?  186 SER B O     1 
ATOM   5986 C CB    . SER C 1 194 ? 16.014  -24.787 -19.083 1.00 27.81 ?  186 SER B CB    1 
ATOM   5987 O OG    . SER C 1 194 ? 15.070  -25.612 -19.743 1.00 26.43 ?  186 SER B OG    1 
ATOM   5988 N N     . GLY C 1 195 ? 16.837  -22.345 -17.375 1.00 30.02 ?  187 GLY B N     1 
ATOM   5989 C CA    . GLY C 1 195 ? 17.914  -21.571 -16.779 1.00 28.36 ?  187 GLY B CA    1 
ATOM   5990 C C     . GLY C 1 195 ? 17.627  -21.151 -15.350 1.00 33.03 ?  187 GLY B C     1 
ATOM   5991 O O     . GLY C 1 195 ? 18.526  -21.149 -14.504 1.00 28.96 ?  187 GLY B O     1 
ATOM   5992 N N     . VAL C 1 196 ? 16.378  -20.786 -15.059 1.00 26.11 ?  188 VAL B N     1 
ATOM   5993 C CA    . VAL C 1 196 ? 16.031  -20.360 -13.708 1.00 29.24 ?  188 VAL B CA    1 
ATOM   5994 C C     . VAL C 1 196 ? 15.864  -21.563 -12.789 1.00 28.19 ?  188 VAL B C     1 
ATOM   5995 O O     . VAL C 1 196 ? 16.325  -21.555 -11.641 1.00 31.72 ?  188 VAL B O     1 
ATOM   5996 C CB    . VAL C 1 196 ? 14.761  -19.489 -13.726 1.00 26.38 ?  188 VAL B CB    1 
ATOM   5997 C CG1   . VAL C 1 196 ? 14.294  -19.209 -12.306 1.00 24.85 ?  188 VAL B CG1   1 
ATOM   5998 C CG2   . VAL C 1 196 ? 15.015  -18.196 -14.479 1.00 23.80 ?  188 VAL B CG2   1 
ATOM   5999 N N     . GLY C 1 197 ? 15.199  -22.614 -13.279 1.00 29.13 ?  189 GLY B N     1 
ATOM   6000 C CA    . GLY C 1 197 ? 14.978  -23.787 -12.448 1.00 27.90 ?  189 GLY B CA    1 
ATOM   6001 C C     . GLY C 1 197 ? 16.267  -24.471 -12.036 1.00 30.57 ?  189 GLY B C     1 
ATOM   6002 O O     . GLY C 1 197 ? 16.366  -25.022 -10.938 1.00 33.54 ?  189 GLY B O     1 
ATOM   6003 N N     . LYS C 1 198 ? 17.271  -24.445 -12.913 1.00 33.28 ?  190 LYS B N     1 
ATOM   6004 C CA    . LYS C 1 198 ? 18.576  -24.996 -12.565 1.00 34.33 ?  190 LYS B CA    1 
ATOM   6005 C C     . LYS C 1 198 ? 19.203  -24.227 -11.407 1.00 35.17 ?  190 LYS B C     1 
ATOM   6006 O O     . LYS C 1 198 ? 19.720  -24.821 -10.454 1.00 40.50 ?  190 LYS B O     1 
ATOM   6007 C CB    . LYS C 1 198 ? 19.495  -24.970 -13.784 1.00 32.08 ?  190 LYS B CB    1 
ATOM   6008 C CG    . LYS C 1 198 ? 20.900  -25.437 -13.483 1.00 35.24 ?  190 LYS B CG    1 
ATOM   6009 C CD    . LYS C 1 198 ? 21.840  -25.163 -14.640 1.00 36.03 ?  190 LYS B CD    1 
ATOM   6010 C CE    . LYS C 1 198 ? 21.660  -26.166 -15.764 1.00 34.98 ?  190 LYS B CE    1 
ATOM   6011 N NZ    . LYS C 1 198 ? 22.710  -25.989 -16.805 1.00 33.88 ?  190 LYS B NZ    1 
ATOM   6012 N N     . VAL C 1 199 ? 19.161  -22.895 -11.475 1.00 31.36 ?  191 VAL B N     1 
ATOM   6013 C CA    . VAL C 1 199 ? 19.751  -22.069 -10.426 1.00 27.62 ?  191 VAL B CA    1 
ATOM   6014 C C     . VAL C 1 199 ? 18.981  -22.231 -9.120  1.00 38.03 ?  191 VAL B C     1 
ATOM   6015 O O     . VAL C 1 199 ? 19.575  -22.325 -8.038  1.00 37.12 ?  191 VAL B O     1 
ATOM   6016 C CB    . VAL C 1 199 ? 19.799  -20.599 -10.885 1.00 35.28 ?  191 VAL B CB    1 
ATOM   6017 C CG1   . VAL C 1 199 ? 19.955  -19.662 -9.702  1.00 33.35 ?  191 VAL B CG1   1 
ATOM   6018 C CG2   . VAL C 1 199 ? 20.922  -20.396 -11.889 1.00 40.94 ?  191 VAL B CG2   1 
ATOM   6019 N N     . LEU C 1 200 ? 17.650  -22.290 -9.200  1.00 32.24 ?  192 LEU B N     1 
ATOM   6020 C CA    . LEU C 1 200 ? 16.836  -22.309 -7.988  1.00 30.29 ?  192 LEU B CA    1 
ATOM   6021 C C     . LEU C 1 200 ? 16.951  -23.639 -7.252  1.00 34.22 ?  192 LEU B C     1 
ATOM   6022 O O     . LEU C 1 200 ? 16.980  -23.667 -6.016  1.00 34.16 ?  192 LEU B O     1 
ATOM   6023 C CB    . LEU C 1 200 ? 15.378  -22.012 -8.334  1.00 27.65 ?  192 LEU B CB    1 
ATOM   6024 C CG    . LEU C 1 200 ? 15.050  -20.566 -8.714  1.00 32.93 ?  192 LEU B CG    1 
ATOM   6025 C CD1   . LEU C 1 200 ? 13.576  -20.272 -8.483  1.00 29.61 ?  192 LEU B CD1   1 
ATOM   6026 C CD2   . LEU C 1 200 ? 15.922  -19.580 -7.949  1.00 29.47 ?  192 LEU B CD2   1 
ATOM   6027 N N     . LYS C 1 201 ? 17.010  -24.751 -7.989  1.00 33.30 ?  193 LYS B N     1 
ATOM   6028 C CA    . LYS C 1 201 ? 17.086  -26.058 -7.344  1.00 36.56 ?  193 LYS B CA    1 
ATOM   6029 C C     . LYS C 1 201 ? 18.397  -26.241 -6.591  1.00 40.47 ?  193 LYS B C     1 
ATOM   6030 O O     . LYS C 1 201 ? 18.450  -26.993 -5.612  1.00 42.95 ?  193 LYS B O     1 
ATOM   6031 C CB    . LYS C 1 201 ? 16.909  -27.169 -8.380  1.00 32.02 ?  193 LYS B CB    1 
ATOM   6032 C CG    . LYS C 1 201 ? 15.458  -27.437 -8.752  1.00 40.54 ?  193 LYS B CG    1 
ATOM   6033 C CD    . LYS C 1 201 ? 15.320  -28.525 -9.810  1.00 46.23 ?  193 LYS B CD    1 
ATOM   6034 C CE    . LYS C 1 201 ? 16.314  -29.655 -9.597  1.00 52.06 ?  193 LYS B CE    1 
ATOM   6035 N NZ    . LYS C 1 201 ? 16.217  -30.686 -10.669 1.00 48.23 ?  193 LYS B NZ    1 
ATOM   6036 N N     . LYS C 1 202 ? 19.460  -25.564 -7.027  1.00 37.84 ?  194 LYS B N     1 
ATOM   6037 C CA    . LYS C 1 202 ? 20.743  -25.694 -6.346  1.00 39.54 ?  194 LYS B CA    1 
ATOM   6038 C C     . LYS C 1 202 ? 20.740  -24.967 -5.005  1.00 39.47 ?  194 LYS B C     1 
ATOM   6039 O O     . LYS C 1 202 ? 21.365  -25.437 -4.047  1.00 40.13 ?  194 LYS B O     1 
ATOM   6040 C CB    . LYS C 1 202 ? 21.865  -25.180 -7.251  1.00 37.99 ?  194 LYS B CB    1 
ATOM   6041 C CG    . LYS C 1 202 ? 22.959  -24.397 -6.546  1.00 42.40 ?  194 LYS B CG    1 
ATOM   6042 C CD    . LYS C 1 202 ? 23.907  -23.757 -7.551  1.00 54.12 ?  194 LYS B CD    1 
ATOM   6043 C CE    . LYS C 1 202 ? 23.258  -22.571 -8.260  1.00 47.65 ?  194 LYS B CE    1 
ATOM   6044 N NZ    . LYS C 1 202 ? 22.707  -21.567 -7.307  1.00 47.43 ?  194 LYS B NZ    1 
ATOM   6045 N N     . GLU C 1 203 ? 20.034  -23.840 -4.908  1.00 37.97 ?  195 GLU B N     1 
ATOM   6046 C CA    . GLU C 1 203 ? 19.951  -23.099 -3.654  1.00 37.26 ?  195 GLU B CA    1 
ATOM   6047 C C     . GLU C 1 203 ? 18.790  -23.554 -2.780  1.00 38.60 ?  195 GLU B C     1 
ATOM   6048 O O     . GLU C 1 203 ? 18.896  -23.511 -1.548  1.00 35.47 ?  195 GLU B O     1 
ATOM   6049 C CB    . GLU C 1 203 ? 19.824  -21.599 -3.939  1.00 31.51 ?  195 GLU B CB    1 
ATOM   6050 C CG    . GLU C 1 203 ? 19.805  -20.709 -2.702  1.00 37.11 ?  195 GLU B CG    1 
ATOM   6051 C CD    . GLU C 1 203 ? 21.184  -20.486 -2.110  1.00 41.90 ?  195 GLU B CD    1 
ATOM   6052 O OE1   . GLU C 1 203 ? 22.178  -20.968 -2.697  1.00 41.21 ?  195 GLU B OE1   1 
ATOM   6053 O OE2   . GLU C 1 203 ? 21.276  -19.826 -1.053  1.00 38.78 ?  195 GLU B OE2   1 
ATOM   6054 N N     . TYR C 1 204 ? 17.685  -23.985 -3.393  1.00 32.90 ?  196 TYR B N     1 
ATOM   6055 C CA    . TYR C 1 204 ? 16.508  -24.489 -2.689  1.00 40.10 ?  196 TYR B CA    1 
ATOM   6056 C C     . TYR C 1 204 ? 16.279  -25.922 -3.156  1.00 38.80 ?  196 TYR B C     1 
ATOM   6057 O O     . TYR C 1 204 ? 15.506  -26.163 -4.093  1.00 35.93 ?  196 TYR B O     1 
ATOM   6058 C CB    . TYR C 1 204 ? 15.278  -23.623 -2.954  1.00 38.93 ?  196 TYR B CB    1 
ATOM   6059 C CG    . TYR C 1 204 ? 15.451  -22.161 -2.602  1.00 35.31 ?  196 TYR B CG    1 
ATOM   6060 C CD1   . TYR C 1 204 ? 15.481  -21.741 -1.278  1.00 30.08 ?  196 TYR B CD1   1 
ATOM   6061 C CD2   . TYR C 1 204 ? 15.573  -21.200 -3.597  1.00 33.14 ?  196 TYR B CD2   1 
ATOM   6062 C CE1   . TYR C 1 204 ? 15.636  -20.409 -0.956  1.00 32.77 ?  196 TYR B CE1   1 
ATOM   6063 C CE2   . TYR C 1 204 ? 15.727  -19.866 -3.283  1.00 38.97 ?  196 TYR B CE2   1 
ATOM   6064 C CZ    . TYR C 1 204 ? 15.757  -19.476 -1.961  1.00 33.35 ?  196 TYR B CZ    1 
ATOM   6065 O OH    . TYR C 1 204 ? 15.911  -18.148 -1.639  1.00 38.15 ?  196 TYR B OH    1 
ATOM   6066 N N     . PRO C 1 205 ? 16.927  -26.904 -2.520  1.00 45.04 ?  197 PRO B N     1 
ATOM   6067 C CA    . PRO C 1 205 ? 16.849  -28.286 -3.026  1.00 38.46 ?  197 PRO B CA    1 
ATOM   6068 C C     . PRO C 1 205 ? 15.483  -28.937 -2.860  1.00 42.26 ?  197 PRO B C     1 
ATOM   6069 O O     . PRO C 1 205 ? 15.278  -30.034 -3.391  1.00 38.29 ?  197 PRO B O     1 
ATOM   6070 C CB    . PRO C 1 205 ? 17.920  -29.022 -2.205  1.00 43.49 ?  197 PRO B CB    1 
ATOM   6071 C CG    . PRO C 1 205 ? 18.091  -28.223 -0.960  1.00 48.70 ?  197 PRO B CG    1 
ATOM   6072 C CD    . PRO C 1 205 ? 17.618  -26.815 -1.217  1.00 45.23 ?  197 PRO B CD    1 
ATOM   6073 N N     . ASN C 1 206 ? 14.546  -28.304 -2.162  1.00 43.56 ?  198 ASN B N     1 
ATOM   6074 C CA    . ASN C 1 206 ? 13.201  -28.840 -2.017  1.00 41.13 ?  198 ASN B CA    1 
ATOM   6075 C C     . ASN C 1 206 ? 12.186  -28.132 -2.902  1.00 40.27 ?  198 ASN B C     1 
ATOM   6076 O O     . ASN C 1 206 ? 10.991  -28.433 -2.817  1.00 41.49 ?  198 ASN B O     1 
ATOM   6077 C CB    . ASN C 1 206 ? 12.757  -28.761 -0.554  1.00 42.12 ?  198 ASN B CB    1 
ATOM   6078 C CG    . ASN C 1 206 ? 13.612  -29.616 0.357   1.00 44.43 ?  198 ASN B CG    1 
ATOM   6079 O OD1   . ASN C 1 206 ? 13.863  -30.787 0.069   1.00 38.60 ?  198 ASN B OD1   1 
ATOM   6080 N ND2   . ASN C 1 206 ? 14.069  -29.036 1.461   1.00 44.91 ?  198 ASN B ND2   1 
ATOM   6081 N N     . ILE C 1 207 ? 12.632  -27.204 -3.749  1.00 38.18 ?  199 ILE B N     1 
ATOM   6082 C CA    . ILE C 1 207 ? 11.710  -26.436 -4.575  1.00 37.89 ?  199 ILE B CA    1 
ATOM   6083 C C     . ILE C 1 207 ? 11.068  -27.341 -5.619  1.00 37.80 ?  199 ILE B C     1 
ATOM   6084 O O     . ILE C 1 207 ? 11.657  -28.333 -6.070  1.00 38.81 ?  199 ILE B O     1 
ATOM   6085 C CB    . ILE C 1 207 ? 12.440  -25.251 -5.236  1.00 40.40 ?  199 ILE B CB    1 
ATOM   6086 C CG1   . ILE C 1 207 ? 11.441  -24.209 -5.740  1.00 32.29 ?  199 ILE B CG1   1 
ATOM   6087 C CG2   . ILE C 1 207 ? 13.327  -25.723 -6.379  1.00 38.76 ?  199 ILE B CG2   1 
ATOM   6088 C CD1   . ILE C 1 207 ? 12.089  -23.085 -6.511  1.00 32.00 ?  199 ILE B CD1   1 
ATOM   6089 N N     . GLU C 1 208 ? 9.837   -27.008 -5.995  1.00 35.18 ?  200 GLU B N     1 
ATOM   6090 C CA    . GLU C 1 208 ? 9.151   -27.669 -7.096  1.00 35.32 ?  200 GLU B CA    1 
ATOM   6091 C C     . GLU C 1 208 ? 9.237   -26.793 -8.338  1.00 34.62 ?  200 GLU B C     1 
ATOM   6092 O O     . GLU C 1 208 ? 8.882   -25.610 -8.296  1.00 31.12 ?  200 GLU B O     1 
ATOM   6093 C CB    . GLU C 1 208 ? 7.687   -27.955 -6.754  1.00 36.25 ?  200 GLU B CB    1 
ATOM   6094 C CG    . GLU C 1 208 ? 7.018   -28.920 -7.729  1.00 39.56 ?  200 GLU B CG    1 
ATOM   6095 C CD    . GLU C 1 208 ? 5.529   -29.068 -7.489  1.00 44.23 ?  200 GLU B CD    1 
ATOM   6096 O OE1   . GLU C 1 208 ? 5.013   -28.444 -6.538  1.00 39.56 ?  200 GLU B OE1   1 
ATOM   6097 O OE2   . GLU C 1 208 ? 4.872   -29.802 -8.258  1.00 41.31 ?  200 GLU B OE2   1 
ATOM   6098 N N     . ILE C 1 209 ? 9.712   -27.373 -9.435  1.00 33.93 ?  201 ILE B N     1 
ATOM   6099 C CA    . ILE C 1 209 ? 9.801   -26.684 -10.716 1.00 32.16 ?  201 ILE B CA    1 
ATOM   6100 C C     . ILE C 1 209 ? 8.634   -27.152 -11.573 1.00 32.81 ?  201 ILE B C     1 
ATOM   6101 O O     . ILE C 1 209 ? 8.492   -28.351 -11.842 1.00 33.42 ?  201 ILE B O     1 
ATOM   6102 C CB    . ILE C 1 209 ? 11.146  -26.951 -11.407 1.00 36.88 ?  201 ILE B CB    1 
ATOM   6103 C CG1   . ILE C 1 209 ? 12.301  -26.592 -10.471 1.00 25.94 ?  201 ILE B CG1   1 
ATOM   6104 C CG2   . ILE C 1 209 ? 11.245  -26.160 -12.703 1.00 31.95 ?  201 ILE B CG2   1 
ATOM   6105 C CD1   . ILE C 1 209 ? 12.277  -25.158 -9.989  1.00 30.39 ?  201 ILE B CD1   1 
ATOM   6106 N N     . VAL C 1 210 ? 7.793   -26.211 -11.993 1.00 35.56 ?  202 VAL B N     1 
ATOM   6107 C CA    . VAL C 1 210 ? 6.552   -26.516 -12.696 1.00 29.53 ?  202 VAL B CA    1 
ATOM   6108 C C     . VAL C 1 210 ? 6.604   -25.873 -14.075 1.00 27.04 ?  202 VAL B C     1 
ATOM   6109 O O     . VAL C 1 210 ? 6.760   -24.651 -14.193 1.00 26.84 ?  202 VAL B O     1 
ATOM   6110 C CB    . VAL C 1 210 ? 5.321   -26.029 -11.916 1.00 31.27 ?  202 VAL B CB    1 
ATOM   6111 C CG1   . VAL C 1 210 ? 4.054   -26.665 -12.468 1.00 27.47 ?  202 VAL B CG1   1 
ATOM   6112 C CG2   . VAL C 1 210 ? 5.475   -26.325 -10.430 1.00 31.82 ?  202 VAL B CG2   1 
ATOM   6113 N N     . ALA C 1 211 ? 6.468   -26.694 -15.111 1.00 30.66 ?  203 ALA B N     1 
ATOM   6114 C CA    . ALA C 1 211 ? 6.309   -26.213 -16.475 1.00 29.41 ?  203 ALA B CA    1 
ATOM   6115 C C     . ALA C 1 211 ? 4.842   -25.911 -16.751 1.00 33.69 ?  203 ALA B C     1 
ATOM   6116 O O     . ALA C 1 211 ? 3.950   -26.650 -16.322 1.00 32.09 ?  203 ALA B O     1 
ATOM   6117 C CB    . ALA C 1 211 ? 6.824   -27.248 -17.477 1.00 24.83 ?  203 ALA B CB    1 
ATOM   6118 N N     . ILE C 1 212 ? 4.595   -24.821 -17.473 1.00 29.63 ?  204 ILE B N     1 
ATOM   6119 C CA    . ILE C 1 212 ? 3.249   -24.415 -17.857 1.00 35.28 ?  204 ILE B CA    1 
ATOM   6120 C C     . ILE C 1 212 ? 3.147   -24.469 -19.375 1.00 32.85 ?  204 ILE B C     1 
ATOM   6121 O O     . ILE C 1 212 ? 4.006   -23.926 -20.079 1.00 29.08 ?  204 ILE B O     1 
ATOM   6122 C CB    . ILE C 1 212 ? 2.908   -23.007 -17.336 1.00 32.22 ?  204 ILE B CB    1 
ATOM   6123 C CG1   . ILE C 1 212 ? 3.034   -22.958 -15.814 1.00 29.53 ?  204 ILE B CG1   1 
ATOM   6124 C CG2   . ILE C 1 212 ? 1.513   -22.599 -17.780 1.00 28.18 ?  204 ILE B CG2   1 
ATOM   6125 C CD1   . ILE C 1 212 ? 3.161   -21.556 -15.268 1.00 28.88 ?  204 ILE B CD1   1 
ATOM   6126 N N     . GLU C 1 213 ? 2.105   -25.126 -19.873 1.00 33.75 ?  205 GLU B N     1 
ATOM   6127 C CA    . GLU C 1 213 ? 1.884   -25.217 -21.310 1.00 32.80 ?  205 GLU B CA    1 
ATOM   6128 C C     . GLU C 1 213 ? 0.394   -25.070 -21.600 1.00 33.77 ?  205 GLU B C     1 
ATOM   6129 O O     . GLU C 1 213 ? -0.426  -25.190 -20.681 1.00 33.51 ?  205 GLU B O     1 
ATOM   6130 C CB    . GLU C 1 213 ? 2.423   -26.542 -21.858 1.00 31.73 ?  205 GLU B CB    1 
ATOM   6131 C CG    . GLU C 1 213 ? 1.913   -27.784 -21.158 1.00 33.13 ?  205 GLU B CG    1 
ATOM   6132 C CD    . GLU C 1 213 ? 2.284   -29.048 -21.910 1.00 37.15 ?  205 GLU B CD    1 
ATOM   6133 O OE1   . GLU C 1 213 ? 2.900   -28.936 -22.993 1.00 31.28 ?  205 GLU B OE1   1 
ATOM   6134 O OE2   . GLU C 1 213 ? 1.961   -30.152 -21.423 1.00 35.66 ?  205 GLU B OE2   1 
ATOM   6135 N N     . PRO C 1 214 ? 0.001   -24.799 -22.845 1.00 36.36 ?  206 PRO B N     1 
ATOM   6136 C CA    . PRO C 1 214 ? -1.429  -24.659 -23.139 1.00 32.42 ?  206 PRO B CA    1 
ATOM   6137 C C     . PRO C 1 214 ? -2.159  -25.990 -23.063 1.00 34.82 ?  206 PRO B C     1 
ATOM   6138 O O     . PRO C 1 214 ? -1.624  -27.039 -23.431 1.00 32.62 ?  206 PRO B O     1 
ATOM   6139 C CB    . PRO C 1 214 ? -1.451  -24.094 -24.567 1.00 30.77 ?  206 PRO B CB    1 
ATOM   6140 C CG    . PRO C 1 214 ? -0.063  -23.614 -24.831 1.00 33.54 ?  206 PRO B CG    1 
ATOM   6141 C CD    . PRO C 1 214 ? 0.831   -24.487 -24.021 1.00 36.34 ?  206 PRO B CD    1 
ATOM   6142 N N     . GLU C 1 215 ? -3.399  -25.932 -22.575 1.00 35.55 ?  207 GLU B N     1 
ATOM   6143 C CA    . GLU C 1 215 ? -4.268  -27.102 -22.612 1.00 34.92 ?  207 GLU B CA    1 
ATOM   6144 C C     . GLU C 1 215 ? -4.535  -27.549 -24.044 1.00 35.81 ?  207 GLU B C     1 
ATOM   6145 O O     . GLU C 1 215 ? -4.655  -28.751 -24.309 1.00 34.18 ?  207 GLU B O     1 
ATOM   6146 C CB    . GLU C 1 215 ? -5.580  -26.792 -21.887 1.00 37.18 ?  207 GLU B CB    1 
ATOM   6147 C CG    . GLU C 1 215 ? -6.700  -27.789 -22.134 1.00 42.68 ?  207 GLU B CG    1 
ATOM   6148 C CD    . GLU C 1 215 ? -6.435  -29.141 -21.502 1.00 41.63 ?  207 GLU B CD    1 
ATOM   6149 O OE1   . GLU C 1 215 ? -6.214  -29.193 -20.273 1.00 40.28 ?  207 GLU B OE1   1 
ATOM   6150 O OE2   . GLU C 1 215 ? -6.442  -30.152 -22.236 1.00 42.72 ?  207 GLU B OE2   1 
ATOM   6151 N N     . ALA C 1 216 ? -4.610  -26.600 -24.979 1.00 32.17 ?  208 ALA B N     1 
ATOM   6152 C CA    . ALA C 1 216 ? -4.885  -26.902 -26.378 1.00 34.58 ?  208 ALA B CA    1 
ATOM   6153 C C     . ALA C 1 216 ? -3.667  -27.417 -27.135 1.00 40.06 ?  208 ALA B C     1 
ATOM   6154 O O     . ALA C 1 216 ? -3.814  -27.868 -28.275 1.00 39.68 ?  208 ALA B O     1 
ATOM   6155 C CB    . ALA C 1 216 ? -5.437  -25.661 -27.080 1.00 35.06 ?  208 ALA B CB    1 
ATOM   6156 N N     . SER C 1 217 ? -2.477  -27.355 -26.546 1.00 36.71 ?  209 SER B N     1 
ATOM   6157 C CA    . SER C 1 217 ? -1.298  -27.937 -27.172 1.00 36.85 ?  209 SER B CA    1 
ATOM   6158 C C     . SER C 1 217 ? -0.392  -28.558 -26.114 1.00 36.55 ?  209 SER B C     1 
ATOM   6159 O O     . SER C 1 217 ? 0.753   -28.117 -25.947 1.00 37.57 ?  209 SER B O     1 
ATOM   6160 C CB    . SER C 1 217 ? -0.545  -26.890 -27.991 1.00 33.83 ?  209 SER B CB    1 
ATOM   6161 O OG    . SER C 1 217 ? 0.455   -27.499 -28.787 1.00 34.55 ?  209 SER B OG    1 
ATOM   6162 N N     . PRO C 1 218 ? -0.856  -29.594 -25.390 1.00 37.38 ?  210 PRO B N     1 
ATOM   6163 C CA    . PRO C 1 218 ? -0.075  -30.123 -24.252 1.00 33.49 ?  210 PRO B CA    1 
ATOM   6164 C C     . PRO C 1 218 ? 0.970   -31.148 -24.678 1.00 35.18 ?  210 PRO B C     1 
ATOM   6165 O O     . PRO C 1 218 ? 0.888   -32.345 -24.381 1.00 34.11 ?  210 PRO B O     1 
ATOM   6166 C CB    . PRO C 1 218 ? -1.166  -30.735 -23.369 1.00 34.01 ?  210 PRO B CB    1 
ATOM   6167 C CG    . PRO C 1 218 ? -2.222  -31.197 -24.342 1.00 35.81 ?  210 PRO B CG    1 
ATOM   6168 C CD    . PRO C 1 218 ? -2.086  -30.378 -25.615 1.00 31.62 ?  210 PRO B CD    1 
ATOM   6169 N N     . VAL C 1 219 ? 1.997   -30.665 -25.377 1.00 37.19 ?  211 VAL B N     1 
ATOM   6170 C CA    . VAL C 1 219 ? 3.028   -31.558 -25.895 1.00 37.40 ?  211 VAL B CA    1 
ATOM   6171 C C     . VAL C 1 219 ? 3.909   -32.077 -24.765 1.00 34.62 ?  211 VAL B C     1 
ATOM   6172 O O     . VAL C 1 219 ? 4.311   -33.248 -24.761 1.00 35.37 ?  211 VAL B O     1 
ATOM   6173 C CB    . VAL C 1 219 ? 3.849   -30.836 -26.978 1.00 35.80 ?  211 VAL B CB    1 
ATOM   6174 C CG1   . VAL C 1 219 ? 5.149   -31.576 -27.256 1.00 36.18 ?  211 VAL B CG1   1 
ATOM   6175 C CG2   . VAL C 1 219 ? 3.027   -30.686 -28.249 1.00 31.85 ?  211 VAL B CG2   1 
ATOM   6176 N N     . LEU C 1 220 ? 4.218   -31.224 -23.786 1.00 35.82 ?  212 LEU B N     1 
ATOM   6177 C CA    . LEU C 1 220 ? 5.038   -31.665 -22.661 1.00 34.24 ?  212 LEU B CA    1 
ATOM   6178 C C     . LEU C 1 220 ? 4.332   -32.749 -21.857 1.00 34.30 ?  212 LEU B C     1 
ATOM   6179 O O     . LEU C 1 220 ? 4.974   -33.686 -21.367 1.00 36.65 ?  212 LEU B O     1 
ATOM   6180 C CB    . LEU C 1 220 ? 5.387   -30.479 -21.762 1.00 30.23 ?  212 LEU B CB    1 
ATOM   6181 C CG    . LEU C 1 220 ? 6.338   -29.428 -22.334 1.00 32.01 ?  212 LEU B CG    1 
ATOM   6182 C CD1   . LEU C 1 220 ? 6.731   -28.424 -21.262 1.00 29.50 ?  212 LEU B CD1   1 
ATOM   6183 C CD2   . LEU C 1 220 ? 7.563   -30.097 -22.923 1.00 28.25 ?  212 LEU B CD2   1 
ATOM   6184 N N     . SER C 1 221 ? 3.012   -32.640 -21.710 1.00 35.79 ?  213 SER B N     1 
ATOM   6185 C CA    . SER C 1 221 ? 2.241   -33.632 -20.971 1.00 38.56 ?  213 SER B CA    1 
ATOM   6186 C C     . SER C 1 221 ? 2.025   -34.921 -21.752 1.00 39.99 ?  213 SER B C     1 
ATOM   6187 O O     . SER C 1 221 ? 1.479   -35.879 -21.192 1.00 44.90 ?  213 SER B O     1 
ATOM   6188 C CB    . SER C 1 221 ? 0.884   -33.046 -20.567 1.00 37.18 ?  213 SER B CB    1 
ATOM   6189 O OG    . SER C 1 221 ? 1.050   -31.864 -19.804 1.00 38.95 ?  213 SER B OG    1 
ATOM   6190 N N     . GLY C 1 222 ? 2.435   -34.973 -23.018 1.00 39.38 ?  214 GLY B N     1 
ATOM   6191 C CA    . GLY C 1 222 ? 2.289   -36.160 -23.836 1.00 39.09 ?  214 GLY B CA    1 
ATOM   6192 C C     . GLY C 1 222 ? 1.216   -36.076 -24.898 1.00 42.14 ?  214 GLY B C     1 
ATOM   6193 O O     . GLY C 1 222 ? 1.025   -37.049 -25.636 1.00 45.90 ?  214 GLY B O     1 
ATOM   6194 N N     . GLY C 1 223 ? 0.510   -34.949 -25.007 1.00 39.75 ?  215 GLY B N     1 
ATOM   6195 C CA    . GLY C 1 223 ? -0.565  -34.808 -25.963 1.00 40.29 ?  215 GLY B CA    1 
ATOM   6196 C C     . GLY C 1 223 ? -0.080  -34.369 -27.333 1.00 43.06 ?  215 GLY B C     1 
ATOM   6197 O O     . GLY C 1 223 ? 1.114   -34.230 -27.596 1.00 47.38 ?  215 GLY B O     1 
ATOM   6198 N N     . GLU C 1 224 ? -1.049  -34.149 -28.224 1.00 40.53 ?  216 GLU B N     1 
ATOM   6199 C CA    . GLU C 1 224 ? -0.822  -33.753 -29.604 1.00 45.73 ?  216 GLU B CA    1 
ATOM   6200 C C     . GLU C 1 224 ? -0.689  -32.238 -29.717 1.00 37.83 ?  216 GLU B C     1 
ATOM   6201 O O     . GLU C 1 224 ? -1.311  -31.493 -28.953 1.00 36.72 ?  216 GLU B O     1 
ATOM   6202 C CB    . GLU C 1 224 ? -1.975  -34.224 -30.489 1.00 46.01 ?  216 GLU B CB    1 
ATOM   6203 C CG    . GLU C 1 224 ? -1.961  -35.710 -30.831 1.00 55.46 ?  216 GLU B CG    1 
ATOM   6204 C CD    . GLU C 1 224 ? -0.572  -36.319 -30.775 1.00 62.57 ?  216 GLU B CD    1 
ATOM   6205 O OE1   . GLU C 1 224 ? -0.198  -36.863 -29.713 1.00 69.18 ?  216 GLU B OE1   1 
ATOM   6206 O OE2   . GLU C 1 224 ? 0.150   -36.249 -31.792 1.00 66.60 ?  216 GLU B OE2   1 
ATOM   6207 N N     . PRO C 1 225 ? 0.125   -31.759 -30.654 1.00 42.36 ?  217 PRO B N     1 
ATOM   6208 C CA    . PRO C 1 225 ? 0.138   -30.323 -30.943 1.00 36.58 ?  217 PRO B CA    1 
ATOM   6209 C C     . PRO C 1 225 ? -1.184  -29.884 -31.551 1.00 37.45 ?  217 PRO B C     1 
ATOM   6210 O O     . PRO C 1 225 ? -1.828  -30.623 -32.300 1.00 42.87 ?  217 PRO B O     1 
ATOM   6211 C CB    . PRO C 1 225 ? 1.291   -30.165 -31.942 1.00 29.88 ?  217 PRO B CB    1 
ATOM   6212 C CG    . PRO C 1 225 ? 2.112   -31.408 -31.795 1.00 32.26 ?  217 PRO B CG    1 
ATOM   6213 C CD    . PRO C 1 225 ? 1.152   -32.488 -31.415 1.00 37.93 ?  217 PRO B CD    1 
ATOM   6214 N N     . GLY C 1 226 ? -1.591  -28.666 -31.210 1.00 40.65 ?  218 GLY B N     1 
ATOM   6215 C CA    . GLY C 1 226 ? -2.833  -28.120 -31.697 1.00 35.23 ?  218 GLY B CA    1 
ATOM   6216 C C     . GLY C 1 226 ? -2.851  -26.608 -31.623 1.00 41.64 ?  218 GLY B C     1 
ATOM   6217 O O     . GLY C 1 226 ? -1.987  -25.985 -30.998 1.00 45.67 ?  218 GLY B O     1 
ATOM   6218 N N     . PRO C 1 227 ? -3.840  -25.986 -32.259 1.00 44.93 ?  219 PRO B N     1 
ATOM   6219 C CA    . PRO C 1 227 ? -3.935  -24.526 -32.207 1.00 40.15 ?  219 PRO B CA    1 
ATOM   6220 C C     . PRO C 1 227 ? -4.318  -24.050 -30.816 1.00 36.35 ?  219 PRO B C     1 
ATOM   6221 O O     . PRO C 1 227 ? -5.068  -24.707 -30.092 1.00 40.81 ?  219 PRO B O     1 
ATOM   6222 C CB    . PRO C 1 227 ? -5.028  -24.206 -33.231 1.00 41.25 ?  219 PRO B CB    1 
ATOM   6223 C CG    . PRO C 1 227 ? -5.905  -25.416 -33.213 1.00 41.98 ?  219 PRO B CG    1 
ATOM   6224 C CD    . PRO C 1 227 ? -5.001  -26.596 -32.933 1.00 43.44 ?  219 PRO B CD    1 
ATOM   6225 N N     . HIS C 1 228 ? -3.783  -22.892 -30.446 1.00 35.94 ?  220 HIS B N     1 
ATOM   6226 C CA    . HIS C 1 228 ? -4.026  -22.329 -29.125 1.00 33.60 ?  220 HIS B CA    1 
ATOM   6227 C C     . HIS C 1 228 ? -3.790  -20.826 -29.191 1.00 34.03 ?  220 HIS B C     1 
ATOM   6228 O O     . HIS C 1 228 ? -3.363  -20.287 -30.216 1.00 31.22 ?  220 HIS B O     1 
ATOM   6229 C CB    . HIS C 1 228 ? -3.142  -23.000 -28.071 1.00 35.48 ?  220 HIS B CB    1 
ATOM   6230 C CG    . HIS C 1 228 ? -1.686  -22.691 -28.221 1.00 32.04 ?  220 HIS B CG    1 
ATOM   6231 N ND1   . HIS C 1 228 ? -1.100  -21.579 -27.657 1.00 33.09 ?  220 HIS B ND1   1 
ATOM   6232 C CD2   . HIS C 1 228 ? -0.700  -23.345 -28.878 1.00 37.46 ?  220 HIS B CD2   1 
ATOM   6233 C CE1   . HIS C 1 228 ? 0.186   -21.562 -27.958 1.00 33.65 ?  220 HIS B CE1   1 
ATOM   6234 N NE2   . HIS C 1 228 ? 0.455   -22.623 -28.698 1.00 32.72 ?  220 HIS B NE2   1 
ATOM   6235 N N     . LYS C 1 229 ? -4.074  -20.151 -28.080 1.00 29.40 ?  221 LYS B N     1 
ATOM   6236 C CA    . LYS C 1 229 ? -3.995  -18.701 -28.010 1.00 32.22 ?  221 LYS B CA    1 
ATOM   6237 C C     . LYS C 1 229 ? -3.023  -18.197 -26.955 1.00 32.75 ?  221 LYS B C     1 
ATOM   6238 O O     . LYS C 1 229 ? -2.910  -16.979 -26.774 1.00 30.64 ?  221 LYS B O     1 
ATOM   6239 C CB    . LYS C 1 229 ? -5.386  -18.113 -27.746 1.00 39.13 ?  221 LYS B CB    1 
ATOM   6240 C CG    . LYS C 1 229 ? -6.502  -18.888 -28.422 1.00 43.72 ?  221 LYS B CG    1 
ATOM   6241 C CD    . LYS C 1 229 ? -7.455  -17.975 -29.168 1.00 40.84 ?  221 LYS B CD    1 
ATOM   6242 C CE    . LYS C 1 229 ? -8.864  -18.545 -29.154 1.00 49.41 ?  221 LYS B CE    1 
ATOM   6243 N NZ    . LYS C 1 229 ? -9.857  -17.577 -29.691 1.00 61.55 ?  221 LYS B NZ    1 
ATOM   6244 N N     . LEU C 1 230 ? -2.320  -19.086 -26.252 1.00 29.43 ?  222 LEU B N     1 
ATOM   6245 C CA    . LEU C 1 230 ? -1.342  -18.668 -25.247 1.00 28.96 ?  222 LEU B CA    1 
ATOM   6246 C C     . LEU C 1 230 ? -0.087  -18.203 -25.979 1.00 31.91 ?  222 LEU B C     1 
ATOM   6247 O O     . LEU C 1 230 ? 0.889   -18.939 -26.147 1.00 28.59 ?  222 LEU B O     1 
ATOM   6248 C CB    . LEU C 1 230 ? -1.048  -19.796 -24.266 1.00 27.77 ?  222 LEU B CB    1 
ATOM   6249 C CG    . LEU C 1 230 ? -2.248  -20.384 -23.517 1.00 30.27 ?  222 LEU B CG    1 
ATOM   6250 C CD1   . LEU C 1 230 ? -1.802  -21.167 -22.290 1.00 29.16 ?  222 LEU B CD1   1 
ATOM   6251 C CD2   . LEU C 1 230 ? -3.236  -19.295 -23.128 1.00 26.06 ?  222 LEU B CD2   1 
ATOM   6252 N N     . GLN C 1 231 ? -0.130  -16.947 -26.426 1.00 30.06 ?  223 GLN B N     1 
ATOM   6253 C CA    . GLN C 1 231 ? 0.961   -16.383 -27.211 1.00 35.24 ?  223 GLN B CA    1 
ATOM   6254 C C     . GLN C 1 231 ? 2.262   -16.426 -26.422 1.00 28.53 ?  223 GLN B C     1 
ATOM   6255 O O     . GLN C 1 231 ? 2.324   -15.975 -25.274 1.00 26.99 ?  223 GLN B O     1 
ATOM   6256 C CB    . GLN C 1 231 ? 0.630   -14.945 -27.610 1.00 35.42 ?  223 GLN B CB    1 
ATOM   6257 C CG    . GLN C 1 231 ? 0.206   -14.781 -29.060 1.00 45.96 ?  223 GLN B CG    1 
ATOM   6258 C CD    . GLN C 1 231 ? -0.420  -13.428 -29.333 1.00 52.46 ?  223 GLN B CD    1 
ATOM   6259 O OE1   . GLN C 1 231 ? -1.610  -13.222 -29.094 1.00 52.66 ?  223 GLN B OE1   1 
ATOM   6260 N NE2   . GLN C 1 231 ? 0.382   -12.493 -29.831 1.00 49.26 ?  223 GLN B NE2   1 
ATOM   6261 N N     . GLY C 1 232 ? 3.300   -16.981 -27.041 1.00 31.56 ?  224 GLY B N     1 
ATOM   6262 C CA    . GLY C 1 232 ? 4.577   -17.176 -26.393 1.00 29.42 ?  224 GLY B CA    1 
ATOM   6263 C C     . GLY C 1 232 ? 4.815   -18.577 -25.875 1.00 29.48 ?  224 GLY B C     1 
ATOM   6264 O O     . GLY C 1 232 ? 5.965   -18.922 -25.580 1.00 27.98 ?  224 GLY B O     1 
ATOM   6265 N N     . LEU C 1 233 ? 3.772   -19.389 -25.754 1.00 28.54 ?  225 LEU B N     1 
ATOM   6266 C CA    . LEU C 1 233 ? 3.880   -20.773 -25.310 1.00 28.39 ?  225 LEU B CA    1 
ATOM   6267 C C     . LEU C 1 233 ? 3.458   -21.708 -26.440 1.00 29.17 ?  225 LEU B C     1 
ATOM   6268 O O     . LEU C 1 233 ? 3.136   -21.276 -27.549 1.00 27.32 ?  225 LEU B O     1 
ATOM   6269 C CB    . LEU C 1 233 ? 3.027   -21.017 -24.061 1.00 29.39 ?  225 LEU B CB    1 
ATOM   6270 C CG    . LEU C 1 233 ? 2.998   -19.935 -22.981 1.00 30.19 ?  225 LEU B CG    1 
ATOM   6271 C CD1   . LEU C 1 233 ? 2.149   -20.385 -21.804 1.00 28.80 ?  225 LEU B CD1   1 
ATOM   6272 C CD2   . LEU C 1 233 ? 4.405   -19.610 -22.519 1.00 29.57 ?  225 LEU B CD2   1 
ATOM   6273 N N     . GLY C 1 234 ? 3.468   -23.006 -26.140 1.00 31.32 ?  226 GLY B N     1 
ATOM   6274 C CA    . GLY C 1 234 ? 2.963   -24.016 -27.050 1.00 32.53 ?  226 GLY B CA    1 
ATOM   6275 C C     . GLY C 1 234 ? 3.613   -24.024 -28.418 1.00 34.04 ?  226 GLY B C     1 
ATOM   6276 O O     . GLY C 1 234 ? 2.948   -23.774 -29.429 1.00 33.23 ?  226 GLY B O     1 
ATOM   6277 N N     . ALA C 1 235 ? 4.916   -24.310 -28.465 1.00 26.90 ?  227 ALA B N     1 
ATOM   6278 C CA    . ALA C 1 235 ? 5.614   -24.378 -29.743 1.00 27.99 ?  227 ALA B CA    1 
ATOM   6279 C C     . ALA C 1 235 ? 5.230   -25.614 -30.545 1.00 32.59 ?  227 ALA B C     1 
ATOM   6280 O O     . ALA C 1 235 ? 5.443   -25.638 -31.762 1.00 29.36 ?  227 ALA B O     1 
ATOM   6281 C CB    . ALA C 1 235 ? 7.128   -24.350 -29.521 1.00 27.78 ?  227 ALA B CB    1 
ATOM   6282 N N     . GLY C 1 236 ? 4.669   -26.631 -29.898 1.00 31.03 ?  228 GLY B N     1 
ATOM   6283 C CA    . GLY C 1 236 ? 4.272   -27.847 -30.576 1.00 35.12 ?  228 GLY B CA    1 
ATOM   6284 C C     . GLY C 1 236 ? 5.341   -28.910 -30.686 1.00 35.42 ?  228 GLY B C     1 
ATOM   6285 O O     . GLY C 1 236 ? 5.159   -29.866 -31.449 1.00 32.69 ?  228 GLY B O     1 
ATOM   6286 N N     . PHE C 1 237 ? 6.445   -28.778 -29.958 1.00 34.78 ?  229 PHE B N     1 
ATOM   6287 C CA    . PHE C 1 237 ? 7.520   -29.763 -29.991 1.00 34.23 ?  229 PHE B CA    1 
ATOM   6288 C C     . PHE C 1 237 ? 8.362   -29.588 -28.733 1.00 30.48 ?  229 PHE B C     1 
ATOM   6289 O O     . PHE C 1 237 ? 8.122   -28.689 -27.923 1.00 29.05 ?  229 PHE B O     1 
ATOM   6290 C CB    . PHE C 1 237 ? 8.366   -29.622 -31.263 1.00 34.20 ?  229 PHE B CB    1 
ATOM   6291 C CG    . PHE C 1 237 ? 8.966   -28.254 -31.450 1.00 35.55 ?  229 PHE B CG    1 
ATOM   6292 C CD1   . PHE C 1 237 ? 10.216  -27.956 -30.932 1.00 33.11 ?  229 PHE B CD1   1 
ATOM   6293 C CD2   . PHE C 1 237 ? 8.283   -27.270 -32.146 1.00 27.68 ?  229 PHE B CD2   1 
ATOM   6294 C CE1   . PHE C 1 237 ? 10.771  -26.700 -31.098 1.00 28.83 ?  229 PHE B CE1   1 
ATOM   6295 C CE2   . PHE C 1 237 ? 8.833   -26.013 -32.317 1.00 26.53 ?  229 PHE B CE2   1 
ATOM   6296 C CZ    . PHE C 1 237 ? 10.079  -25.728 -31.792 1.00 30.85 ?  229 PHE B CZ    1 
ATOM   6297 N N     . ILE C 1 238 ? 9.350   -30.463 -28.569 1.00 28.55 ?  230 ILE B N     1 
ATOM   6298 C CA    . ILE C 1 238 ? 10.298  -30.383 -27.464 1.00 27.38 ?  230 ILE B CA    1 
ATOM   6299 C C     . ILE C 1 238 ? 11.478  -29.522 -27.928 1.00 29.79 ?  230 ILE B C     1 
ATOM   6300 O O     . ILE C 1 238 ? 12.267  -29.989 -28.765 1.00 27.97 ?  230 ILE B O     1 
ATOM   6301 C CB    . ILE C 1 238 ? 10.770  -31.772 -27.017 1.00 28.45 ?  230 ILE B CB    1 
ATOM   6302 C CG1   . ILE C 1 238 ? 9.575   -32.694 -26.752 1.00 27.90 ?  230 ILE B CG1   1 
ATOM   6303 C CG2   . ILE C 1 238 ? 11.651  -31.667 -25.779 1.00 27.46 ?  230 ILE B CG2   1 
ATOM   6304 C CD1   . ILE C 1 238 ? 8.649   -32.206 -25.659 1.00 33.16 ?  230 ILE B CD1   1 
ATOM   6305 N N     . PRO C 1 239 ? 11.616  -28.291 -27.440 1.00 31.26 ?  231 PRO B N     1 
ATOM   6306 C CA    . PRO C 1 239 ? 12.742  -27.457 -27.877 1.00 29.38 ?  231 PRO B CA    1 
ATOM   6307 C C     . PRO C 1 239 ? 14.064  -27.999 -27.359 1.00 29.00 ?  231 PRO B C     1 
ATOM   6308 O O     . PRO C 1 239 ? 14.150  -28.524 -26.246 1.00 28.62 ?  231 PRO B O     1 
ATOM   6309 C CB    . PRO C 1 239 ? 12.428  -26.088 -27.260 1.00 27.56 ?  231 PRO B CB    1 
ATOM   6310 C CG    . PRO C 1 239 ? 10.954  -26.122 -26.986 1.00 26.04 ?  231 PRO B CG    1 
ATOM   6311 C CD    . PRO C 1 239 ? 10.697  -27.540 -26.571 1.00 27.51 ?  231 PRO B CD    1 
ATOM   6312 N N     . GLY C 1 240 ? 15.105  -27.867 -28.183 1.00 32.44 ?  232 GLY B N     1 
ATOM   6313 C CA    . GLY C 1 240 ? 16.445  -28.208 -27.744 1.00 28.30 ?  232 GLY B CA    1 
ATOM   6314 C C     . GLY C 1 240 ? 16.977  -27.332 -26.630 1.00 29.19 ?  232 GLY B C     1 
ATOM   6315 O O     . GLY C 1 240 ? 17.973  -27.699 -25.996 1.00 28.96 ?  232 GLY B O     1 
ATOM   6316 N N     . THR C 1 241 ? 16.342  -26.188 -26.383 1.00 30.65 ?  233 THR B N     1 
ATOM   6317 C CA    . THR C 1 241 ? 16.703  -25.295 -25.292 1.00 24.54 ?  233 THR B CA    1 
ATOM   6318 C C     . THR C 1 241 ? 15.948  -25.605 -24.008 1.00 28.59 ?  233 THR B C     1 
ATOM   6319 O O     . THR C 1 241 ? 16.127  -24.896 -23.013 1.00 25.98 ?  233 THR B O     1 
ATOM   6320 C CB    . THR C 1 241 ? 16.441  -23.840 -25.694 1.00 26.63 ?  233 THR B CB    1 
ATOM   6321 O OG1   . THR C 1 241 ? 15.167  -23.743 -26.343 1.00 23.99 ?  233 THR B OG1   1 
ATOM   6322 C CG2   . THR C 1 241 ? 17.517  -23.350 -26.643 1.00 25.61 ?  233 THR B CG2   1 
ATOM   6323 N N     . LEU C 1 242 ? 15.109  -26.637 -24.008 1.00 29.16 ?  234 LEU B N     1 
ATOM   6324 C CA    . LEU C 1 242 ? 14.306  -26.999 -22.848 1.00 28.54 ?  234 LEU B CA    1 
ATOM   6325 C C     . LEU C 1 242 ? 14.900  -28.236 -22.187 1.00 29.74 ?  234 LEU B C     1 
ATOM   6326 O O     . LEU C 1 242 ? 14.974  -29.303 -22.808 1.00 28.62 ?  234 LEU B O     1 
ATOM   6327 C CB    . LEU C 1 242 ? 12.852  -27.253 -23.244 1.00 28.28 ?  234 LEU B CB    1 
ATOM   6328 C CG    . LEU C 1 242 ? 11.990  -27.877 -22.146 1.00 25.88 ?  234 LEU B CG    1 
ATOM   6329 C CD1   . LEU C 1 242 ? 11.721  -26.874 -21.038 1.00 25.80 ?  234 LEU B CD1   1 
ATOM   6330 C CD2   . LEU C 1 242 ? 10.691  -28.406 -22.717 1.00 26.01 ?  234 LEU B CD2   1 
ATOM   6331 N N     . ASN C 1 243 ? 15.320  -28.089 -20.935 1.00 28.78 ?  235 ASN B N     1 
ATOM   6332 C CA    . ASN C 1 243 ? 15.764  -29.217 -20.122 1.00 32.64 ?  235 ASN B CA    1 
ATOM   6333 C C     . ASN C 1 243 ? 14.524  -29.964 -19.651 1.00 31.04 ?  235 ASN B C     1 
ATOM   6334 O O     . ASN C 1 243 ? 13.837  -29.530 -18.725 1.00 27.75 ?  235 ASN B O     1 
ATOM   6335 C CB    . ASN C 1 243 ? 16.606  -28.730 -18.948 1.00 34.24 ?  235 ASN B CB    1 
ATOM   6336 C CG    . ASN C 1 243 ? 17.195  -29.867 -18.135 1.00 30.47 ?  235 ASN B CG    1 
ATOM   6337 O OD1   . ASN C 1 243 ? 17.155  -31.028 -18.544 1.00 36.57 ?  235 ASN B OD1   1 
ATOM   6338 N ND2   . ASN C 1 243 ? 17.752  -29.535 -16.975 1.00 36.82 ?  235 ASN B ND2   1 
ATOM   6339 N N     . THR C 1 244 ? 14.224  -31.092 -20.297 1.00 31.66 ?  236 THR B N     1 
ATOM   6340 C CA    . THR C 1 244 ? 13.036  -31.861 -19.945 1.00 33.33 ?  236 THR B CA    1 
ATOM   6341 C C     . THR C 1 244 ? 13.111  -32.465 -18.549 1.00 33.38 ?  236 THR B C     1 
ATOM   6342 O O     . THR C 1 244 ? 12.087  -32.932 -18.041 1.00 39.17 ?  236 THR B O     1 
ATOM   6343 C CB    . THR C 1 244 ? 12.807  -32.974 -20.969 1.00 29.87 ?  236 THR B CB    1 
ATOM   6344 O OG1   . THR C 1 244 ? 14.012  -33.730 -21.133 1.00 34.72 ?  236 THR B OG1   1 
ATOM   6345 C CG2   . THR C 1 244 ? 12.401  -32.385 -22.308 1.00 31.75 ?  236 THR B CG2   1 
ATOM   6346 N N     . GLU C 1 245 ? 14.283  -32.465 -17.919 1.00 36.83 ?  237 GLU B N     1 
ATOM   6347 C CA    . GLU C 1 245 ? 14.458  -33.038 -16.592 1.00 38.35 ?  237 GLU B CA    1 
ATOM   6348 C C     . GLU C 1 245 ? 14.318  -32.013 -15.474 1.00 33.90 ?  237 GLU B C     1 
ATOM   6349 O O     . GLU C 1 245 ? 14.391  -32.389 -14.300 1.00 35.31 ?  237 GLU B O     1 
ATOM   6350 C CB    . GLU C 1 245 ? 15.830  -33.713 -16.487 1.00 35.10 ?  237 GLU B CB    1 
ATOM   6351 C CG    . GLU C 1 245 ? 16.097  -34.766 -17.546 1.00 46.01 ?  237 GLU B CG    1 
ATOM   6352 C CD    . GLU C 1 245 ? 15.322  -36.044 -17.304 1.00 51.51 ?  237 GLU B CD    1 
ATOM   6353 O OE1   . GLU C 1 245 ? 15.123  -36.406 -16.123 1.00 56.76 ?  237 GLU B OE1   1 
ATOM   6354 O OE2   . GLU C 1 245 ? 14.912  -36.687 -18.292 1.00 57.61 ?  237 GLU B OE2   1 
ATOM   6355 N N     . ILE C 1 246 ? 14.110  -30.736 -15.801 1.00 30.54 ?  238 ILE B N     1 
ATOM   6356 C CA    . ILE C 1 246 ? 14.174  -29.708 -14.767 1.00 31.87 ?  238 ILE B CA    1 
ATOM   6357 C C     . ILE C 1 246 ? 12.854  -29.578 -14.015 1.00 31.77 ?  238 ILE B C     1 
ATOM   6358 O O     . ILE C 1 246 ? 12.853  -29.277 -12.815 1.00 31.49 ?  238 ILE B O     1 
ATOM   6359 C CB    . ILE C 1 246 ? 14.616  -28.361 -15.369 1.00 35.08 ?  238 ILE B CB    1 
ATOM   6360 C CG1   . ILE C 1 246 ? 15.095  -27.419 -14.260 1.00 34.37 ?  238 ILE B CG1   1 
ATOM   6361 C CG2   . ILE C 1 246 ? 13.492  -27.708 -16.163 1.00 30.56 ?  238 ILE B CG2   1 
ATOM   6362 C CD1   . ILE C 1 246 ? 16.424  -27.817 -13.659 1.00 30.77 ?  238 ILE B CD1   1 
ATOM   6363 N N     . TYR C 1 247 ? 11.720  -29.808 -14.674 1.00 34.46 ?  239 TYR B N     1 
ATOM   6364 C CA    . TYR C 1 247 ? 10.428  -29.606 -14.035 1.00 32.67 ?  239 TYR B CA    1 
ATOM   6365 C C     . TYR C 1 247 ? 9.958   -30.883 -13.353 1.00 34.85 ?  239 TYR B C     1 
ATOM   6366 O O     . TYR C 1 247 ? 10.135  -31.988 -13.876 1.00 34.92 ?  239 TYR B O     1 
ATOM   6367 C CB    . TYR C 1 247 ? 9.370   -29.132 -15.038 1.00 32.27 ?  239 TYR B CB    1 
ATOM   6368 C CG    . TYR C 1 247 ? 9.379   -29.818 -16.388 1.00 33.28 ?  239 TYR B CG    1 
ATOM   6369 C CD1   . TYR C 1 247 ? 10.192  -29.365 -17.419 1.00 32.21 ?  239 TYR B CD1   1 
ATOM   6370 C CD2   . TYR C 1 247 ? 8.553   -30.906 -16.637 1.00 36.48 ?  239 TYR B CD2   1 
ATOM   6371 C CE1   . TYR C 1 247 ? 10.191  -29.984 -18.656 1.00 29.88 ?  239 TYR B CE1   1 
ATOM   6372 C CE2   . TYR C 1 247 ? 8.545   -31.532 -17.869 1.00 33.26 ?  239 TYR B CE2   1 
ATOM   6373 C CZ    . TYR C 1 247 ? 9.365   -31.067 -18.875 1.00 33.13 ?  239 TYR B CZ    1 
ATOM   6374 O OH    . TYR C 1 247 ? 9.361   -31.688 -20.104 1.00 35.89 ?  239 TYR B OH    1 
ATOM   6375 N N     . ASP C 1 248 ? 9.360   -30.720 -12.172 1.00 34.67 ?  240 ASP B N     1 
ATOM   6376 C CA    . ASP C 1 248 ? 8.810   -31.837 -11.420 1.00 39.68 ?  240 ASP B CA    1 
ATOM   6377 C C     . ASP C 1 248 ? 7.358   -32.133 -11.771 1.00 37.29 ?  240 ASP B C     1 
ATOM   6378 O O     . ASP C 1 248 ? 6.866   -33.218 -11.441 1.00 41.33 ?  240 ASP B O     1 
ATOM   6379 C CB    . ASP C 1 248 ? 8.917   -31.566 -9.915  1.00 33.30 ?  240 ASP B CB    1 
ATOM   6380 C CG    . ASP C 1 248 ? 10.291  -31.073 -9.504  1.00 37.68 ?  240 ASP B CG    1 
ATOM   6381 O OD1   . ASP C 1 248 ? 11.212  -31.908 -9.378  1.00 43.24 ?  240 ASP B OD1   1 
ATOM   6382 O OD2   . ASP C 1 248 ? 10.449  -29.850 -9.305  1.00 36.26 ?  240 ASP B OD2   1 
ATOM   6383 N N     . SER C 1 249 ? 6.667   -31.202 -12.428 1.00 36.63 ?  241 SER B N     1 
ATOM   6384 C CA    . SER C 1 249 ? 5.266   -31.384 -12.782 1.00 35.12 ?  241 SER B CA    1 
ATOM   6385 C C     . SER C 1 249 ? 4.912   -30.393 -13.882 1.00 36.35 ?  241 SER B C     1 
ATOM   6386 O O     . SER C 1 249 ? 5.693   -29.499 -14.219 1.00 35.75 ?  241 SER B O     1 
ATOM   6387 C CB    . SER C 1 249 ? 4.354   -31.207 -11.566 1.00 30.78 ?  241 SER B CB    1 
ATOM   6388 O OG    . SER C 1 249 ? 4.358   -29.862 -11.120 1.00 35.87 ?  241 SER B OG    1 
ATOM   6389 N N     . ILE C 1 250 ? 3.714   -30.566 -14.441 1.00 31.84 ?  242 ILE B N     1 
ATOM   6390 C CA    . ILE C 1 250 ? 3.222   -29.747 -15.542 1.00 32.79 ?  242 ILE B CA    1 
ATOM   6391 C C     . ILE C 1 250 ? 1.813   -29.280 -15.206 1.00 31.97 ?  242 ILE B C     1 
ATOM   6392 O O     . ILE C 1 250 ? 0.998   -30.058 -14.699 1.00 37.14 ?  242 ILE B O     1 
ATOM   6393 C CB    . ILE C 1 250 ? 3.229   -30.523 -16.877 1.00 30.51 ?  242 ILE B CB    1 
ATOM   6394 C CG1   . ILE C 1 250 ? 4.636   -31.023 -17.206 1.00 29.74 ?  242 ILE B CG1   1 
ATOM   6395 C CG2   . ILE C 1 250 ? 2.705   -29.655 -18.012 1.00 27.83 ?  242 ILE B CG2   1 
ATOM   6396 C CD1   . ILE C 1 250 ? 4.682   -31.992 -18.363 1.00 24.51 ?  242 ILE B CD1   1 
ATOM   6397 N N     . ILE C 1 251 ? 1.528   -28.011 -15.486 1.00 32.15 ?  243 ILE B N     1 
ATOM   6398 C CA    . ILE C 1 251 ? 0.186   -27.453 -15.360 1.00 30.20 ?  243 ILE B CA    1 
ATOM   6399 C C     . ILE C 1 251 ? -0.256  -26.973 -16.735 1.00 34.55 ?  243 ILE B C     1 
ATOM   6400 O O     . ILE C 1 251 ? 0.420   -26.142 -17.356 1.00 31.54 ?  243 ILE B O     1 
ATOM   6401 C CB    . ILE C 1 251 ? 0.125   -26.308 -14.336 1.00 30.12 ?  243 ILE B CB    1 
ATOM   6402 C CG1   . ILE C 1 251 ? 0.438   -26.824 -12.932 1.00 26.66 ?  243 ILE B CG1   1 
ATOM   6403 C CG2   . ILE C 1 251 ? -1.244  -25.641 -14.359 1.00 31.36 ?  243 ILE B CG2   1 
ATOM   6404 C CD1   . ILE C 1 251 ? 0.540   -25.729 -11.893 1.00 24.53 ?  243 ILE B CD1   1 
ATOM   6405 N N     . LYS C 1 252 ? -1.383  -27.496 -17.209 1.00 33.11 ?  244 LYS B N     1 
ATOM   6406 C CA    . LYS C 1 252 ? -1.972  -27.058 -18.465 1.00 34.02 ?  244 LYS B CA    1 
ATOM   6407 C C     . LYS C 1 252 ? -2.977  -25.946 -18.197 1.00 34.43 ?  244 LYS B C     1 
ATOM   6408 O O     . LYS C 1 252 ? -3.717  -25.987 -17.210 1.00 37.91 ?  244 LYS B O     1 
ATOM   6409 C CB    . LYS C 1 252 ? -2.654  -28.225 -19.179 1.00 36.73 ?  244 LYS B CB    1 
ATOM   6410 C CG    . LYS C 1 252 ? -1.724  -29.381 -19.491 1.00 36.41 ?  244 LYS B CG    1 
ATOM   6411 C CD    . LYS C 1 252 ? -2.482  -30.544 -20.102 1.00 38.19 ?  244 LYS B CD    1 
ATOM   6412 C CE    . LYS C 1 252 ? -3.305  -31.279 -19.061 1.00 43.72 ?  244 LYS B CE    1 
ATOM   6413 N NZ    . LYS C 1 252 ? -4.464  -31.981 -19.681 1.00 53.05 ?  244 LYS B NZ    1 
ATOM   6414 N N     . VAL C 1 253 ? -2.993  -24.946 -19.076 1.00 30.92 ?  245 VAL B N     1 
ATOM   6415 C CA    . VAL C 1 253 ? -3.858  -23.782 -18.928 1.00 32.10 ?  245 VAL B CA    1 
ATOM   6416 C C     . VAL C 1 253 ? -4.664  -23.599 -20.206 1.00 33.05 ?  245 VAL B C     1 
ATOM   6417 O O     . VAL C 1 253 ? -4.102  -23.606 -21.307 1.00 32.42 ?  245 VAL B O     1 
ATOM   6418 C CB    . VAL C 1 253 ? -3.057  -22.503 -18.616 1.00 33.46 ?  245 VAL B CB    1 
ATOM   6419 C CG1   . VAL C 1 253 ? -4.002  -21.347 -18.327 1.00 28.52 ?  245 VAL B CG1   1 
ATOM   6420 C CG2   . VAL C 1 253 ? -2.114  -22.732 -17.443 1.00 26.92 ?  245 VAL B CG2   1 
ATOM   6421 N N     . GLY C 1 254 ? -5.979  -23.428 -20.058 1.00 28.94 ?  246 GLY B N     1 
ATOM   6422 C CA    . GLY C 1 254 ? -6.825  -23.141 -21.194 1.00 26.09 ?  246 GLY B CA    1 
ATOM   6423 C C     . GLY C 1 254 ? -6.679  -21.710 -21.683 1.00 29.40 ?  246 GLY B C     1 
ATOM   6424 O O     . GLY C 1 254 ? -6.137  -20.838 -21.005 1.00 27.79 ?  246 GLY B O     1 
ATOM   6425 N N     . ASN C 1 255 ? -7.184  -21.474 -22.897 1.00 32.11 ?  247 ASN B N     1 
ATOM   6426 C CA    . ASN C 1 255 ? -7.077  -20.147 -23.498 1.00 27.45 ?  247 ASN B CA    1 
ATOM   6427 C C     . ASN C 1 255 ? -7.907  -19.125 -22.730 1.00 32.75 ?  247 ASN B C     1 
ATOM   6428 O O     . ASN C 1 255 ? -7.410  -18.051 -22.372 1.00 32.67 ?  247 ASN B O     1 
ATOM   6429 C CB    . ASN C 1 255 ? -7.508  -20.198 -24.965 1.00 29.78 ?  247 ASN B CB    1 
ATOM   6430 C CG    . ASN C 1 255 ? -6.754  -21.247 -25.758 1.00 35.87 ?  247 ASN B CG    1 
ATOM   6431 O OD1   . ASN C 1 255 ? -5.572  -21.492 -25.519 1.00 31.52 ?  247 ASN B OD1   1 
ATOM   6432 N ND2   . ASN C 1 255 ? -7.437  -21.871 -26.712 1.00 32.21 ?  247 ASN B ND2   1 
ATOM   6433 N N     . ASP C 1 256 ? -9.177  -19.443 -22.466 1.00 32.59 ?  248 ASP B N     1 
ATOM   6434 C CA    . ASP C 1 256 ? -10.046 -18.510 -21.755 1.00 29.61 ?  248 ASP B CA    1 
ATOM   6435 C C     . ASP C 1 256 ? -9.564  -18.279 -20.329 1.00 28.27 ?  248 ASP B C     1 
ATOM   6436 O O     . ASP C 1 256 ? -9.682  -17.168 -19.799 1.00 29.08 ?  248 ASP B O     1 
ATOM   6437 C CB    . ASP C 1 256 ? -11.481 -19.034 -21.748 1.00 33.76 ?  248 ASP B CB    1 
ATOM   6438 C CG    . ASP C 1 256 ? -12.140 -18.955 -23.108 1.00 43.51 ?  248 ASP B CG    1 
ATOM   6439 O OD1   . ASP C 1 256 ? -11.686 -18.158 -23.956 1.00 35.03 ?  248 ASP B OD1   1 
ATOM   6440 O OD2   . ASP C 1 256 ? -13.116 -19.701 -23.327 1.00 42.41 ?  248 ASP B OD2   1 
ATOM   6441 N N     . THR C 1 257 ? -9.025  -19.321 -19.692 1.00 28.87 ?  249 THR B N     1 
ATOM   6442 C CA    . THR C 1 257 ? -8.579  -19.207 -18.307 1.00 31.79 ?  249 THR B CA    1 
ATOM   6443 C C     . THR C 1 257 ? -7.442  -18.200 -18.169 1.00 34.48 ?  249 THR B C     1 
ATOM   6444 O O     . THR C 1 257 ? -7.426  -17.393 -17.232 1.00 29.13 ?  249 THR B O     1 
ATOM   6445 C CB    . THR C 1 257 ? -8.144  -20.578 -17.792 1.00 29.63 ?  249 THR B CB    1 
ATOM   6446 O OG1   . THR C 1 257 ? -9.291  -21.420 -17.632 1.00 38.39 ?  249 THR B OG1   1 
ATOM   6447 C CG2   . THR C 1 257 ? -7.431  -20.447 -16.468 1.00 33.05 ?  249 THR B CG2   1 
ATOM   6448 N N     . ALA C 1 258 ? -6.481  -18.236 -19.095 1.00 30.43 ?  250 ALA B N     1 
ATOM   6449 C CA    . ALA C 1 258 ? -5.355  -17.309 -19.039 1.00 31.76 ?  250 ALA B CA    1 
ATOM   6450 C C     . ALA C 1 258 ? -5.801  -15.882 -19.326 1.00 31.46 ?  250 ALA B C     1 
ATOM   6451 O O     . ALA C 1 258 ? -5.378  -14.940 -18.646 1.00 31.29 ?  250 ALA B O     1 
ATOM   6452 C CB    . ALA C 1 258 ? -4.273  -17.738 -20.030 1.00 26.62 ?  250 ALA B CB    1 
ATOM   6453 N N     . MET C 1 259 ? -6.655  -15.703 -20.335 1.00 29.26 ?  251 MET B N     1 
ATOM   6454 C CA    . MET C 1 259 ? -7.061  -14.359 -20.732 1.00 33.71 ?  251 MET B CA    1 
ATOM   6455 C C     . MET C 1 259 ? -7.828  -13.658 -19.617 1.00 34.36 ?  251 MET B C     1 
ATOM   6456 O O     . MET C 1 259 ? -7.593  -12.477 -19.334 1.00 36.00 ?  251 MET B O     1 
ATOM   6457 C CB    . MET C 1 259 ? -7.898  -14.416 -22.009 1.00 36.87 ?  251 MET B CB    1 
ATOM   6458 C CG    . MET C 1 259 ? -7.193  -14.972 -23.226 1.00 39.86 ?  251 MET B CG    1 
ATOM   6459 S SD    . MET C 1 259 ? -8.009  -14.405 -24.733 1.00 58.09 ?  251 MET B SD    1 
ATOM   6460 C CE    . MET C 1 259 ? -9.089  -15.791 -25.075 1.00 48.60 ?  251 MET B CE    1 
ATOM   6461 N N     . GLU C 1 260 ? -8.751  -14.371 -18.967 1.00 34.23 ?  252 GLU B N     1 
ATOM   6462 C CA    . GLU C 1 260 ? -9.520  -13.760 -17.888 1.00 29.72 ?  252 GLU B CA    1 
ATOM   6463 C C     . GLU C 1 260 ? -8.642  -13.434 -16.688 1.00 28.34 ?  252 GLU B C     1 
ATOM   6464 O O     . GLU C 1 260 ? -8.890  -12.446 -15.987 1.00 29.35 ?  252 GLU B O     1 
ATOM   6465 C CB    . GLU C 1 260 ? -10.670 -14.678 -17.472 1.00 33.90 ?  252 GLU B CB    1 
ATOM   6466 N N     . MET C 1 261 ? -7.613  -14.247 -16.436 1.00 29.37 ?  253 MET B N     1 
ATOM   6467 C CA    . MET C 1 261 ? -6.701  -13.961 -15.334 1.00 33.72 ?  253 MET B CA    1 
ATOM   6468 C C     . MET C 1 261 ? -5.869  -12.715 -15.616 1.00 27.96 ?  253 MET B C     1 
ATOM   6469 O O     . MET C 1 261 ? -5.609  -11.918 -14.707 1.00 29.61 ?  253 MET B O     1 
ATOM   6470 C CB    . MET C 1 261 ? -5.800  -15.167 -15.072 1.00 31.57 ?  253 MET B CB    1 
ATOM   6471 C CG    . MET C 1 261 ? -4.765  -14.936 -13.985 1.00 33.03 ?  253 MET B CG    1 
ATOM   6472 S SD    . MET C 1 261 ? -5.503  -14.382 -12.432 1.00 36.60 ?  253 MET B SD    1 
ATOM   6473 C CE    . MET C 1 261 ? -6.585  -15.756 -12.049 1.00 31.97 ?  253 MET B CE    1 
ATOM   6474 N N     . SER C 1 262 ? -5.440  -12.530 -16.869 1.00 31.10 ?  254 SER B N     1 
ATOM   6475 C CA    . SER C 1 262 ? -4.741  -11.301 -17.234 1.00 27.34 ?  254 SER B CA    1 
ATOM   6476 C C     . SER C 1 262 ? -5.620  -10.082 -16.997 1.00 33.30 ?  254 SER B C     1 
ATOM   6477 O O     . SER C 1 262 ? -5.144  -9.045  -16.517 1.00 30.94 ?  254 SER B O     1 
ATOM   6478 C CB    . SER C 1 262 ? -4.296  -11.355 -18.696 1.00 30.15 ?  254 SER B CB    1 
ATOM   6479 O OG    . SER C 1 262 ? -3.148  -12.168 -18.860 1.00 32.45 ?  254 SER B OG    1 
ATOM   6480 N N     . ARG C 1 263 ? -6.910  -10.189 -17.326 1.00 29.81 ?  255 ARG B N     1 
ATOM   6481 C CA    . ARG C 1 263 ? -7.830  -9.082  -17.089 1.00 30.61 ?  255 ARG B CA    1 
ATOM   6482 C C     . ARG C 1 263 ? -7.998  -8.821  -15.598 1.00 31.16 ?  255 ARG B C     1 
ATOM   6483 O O     . ARG C 1 263 ? -8.005  -7.667  -15.155 1.00 34.70 ?  255 ARG B O     1 
ATOM   6484 C CB    . ARG C 1 263 ? -9.184  -9.370  -17.737 1.00 35.42 ?  255 ARG B CB    1 
ATOM   6485 C CG    . ARG C 1 263 ? -9.139  -9.528  -19.242 1.00 37.53 ?  255 ARG B CG    1 
ATOM   6486 C CD    . ARG C 1 263 ? -10.298 -10.374 -19.734 1.00 44.39 ?  255 ARG B CD    1 
ATOM   6487 N NE    . ARG C 1 263 ? -10.635 -10.066 -21.118 1.00 47.05 ?  255 ARG B NE    1 
ATOM   6488 C CZ    . ARG C 1 263 ? -10.453 -10.893 -22.137 1.00 56.48 ?  255 ARG B CZ    1 
ATOM   6489 N NH1   . ARG C 1 263 ? -9.969  -12.109 -21.960 1.00 50.50 ?  255 ARG B NH1   1 
ATOM   6490 N NH2   . ARG C 1 263 ? -10.775 -10.491 -23.362 1.00 58.69 ?  255 ARG B NH2   1 
ATOM   6491 N N     . ARG C 1 264 ? -8.139  -9.888  -14.806 1.00 30.95 ?  256 ARG B N     1 
ATOM   6492 C CA    . ARG C 1 264 ? -8.265  -9.724  -13.360 1.00 33.03 ?  256 ARG B CA    1 
ATOM   6493 C C     . ARG C 1 264 ? -7.020  -9.080  -12.766 1.00 32.19 ?  256 ARG B C     1 
ATOM   6494 O O     . ARG C 1 264 ? -7.118  -8.171  -11.934 1.00 29.83 ?  256 ARG B O     1 
ATOM   6495 C CB    . ARG C 1 264 ? -8.528  -11.076 -12.698 1.00 34.66 ?  256 ARG B CB    1 
ATOM   6496 C CG    . ARG C 1 264 ? -9.994  -11.437 -12.572 1.00 40.82 ?  256 ARG B CG    1 
ATOM   6497 C CD    . ARG C 1 264 ? -10.193 -12.539 -11.542 1.00 42.94 ?  256 ARG B CD    1 
ATOM   6498 N NE    . ARG C 1 264 ? -10.021 -12.056 -10.177 1.00 44.34 ?  256 ARG B NE    1 
ATOM   6499 C CZ    . ARG C 1 264 ? -9.776  -12.837 -9.133  1.00 40.48 ?  256 ARG B CZ    1 
ATOM   6500 N NH1   . ARG C 1 264 ? -9.652  -14.147 -9.265  1.00 44.03 ?  256 ARG B NH1   1 
ATOM   6501 N NH2   . ARG C 1 264 ? -9.653  -12.289 -7.927  1.00 35.55 ?  256 ARG B NH2   1 
ATOM   6502 N N     . VAL C 1 265 ? -5.838  -9.536  -13.185 1.00 27.95 ?  257 VAL B N     1 
ATOM   6503 C CA    . VAL C 1 265 ? -4.596  -9.006  -12.633 1.00 30.69 ?  257 VAL B CA    1 
ATOM   6504 C C     . VAL C 1 265 ? -4.430  -7.537  -13.001 1.00 28.04 ?  257 VAL B C     1 
ATOM   6505 O O     . VAL C 1 265 ? -4.006  -6.718  -12.175 1.00 26.32 ?  257 VAL B O     1 
ATOM   6506 C CB    . VAL C 1 265 ? -3.402  -9.854  -13.108 1.00 27.85 ?  257 VAL B CB    1 
ATOM   6507 C CG1   . VAL C 1 265 ? -2.090  -9.161  -12.786 1.00 27.02 ?  257 VAL B CG1   1 
ATOM   6508 C CG2   . VAL C 1 265 ? -3.451  -11.230 -12.463 1.00 27.19 ?  257 VAL B CG2   1 
ATOM   6509 N N     . ALA C 1 266 ? -4.772  -7.175  -14.238 1.00 28.48 ?  258 ALA B N     1 
ATOM   6510 C CA    . ALA C 1 266 ? -4.683  -5.777  -14.645 1.00 27.66 ?  258 ALA B CA    1 
ATOM   6511 C C     . ALA C 1 266 ? -5.650  -4.912  -13.845 1.00 31.47 ?  258 ALA B C     1 
ATOM   6512 O O     . ALA C 1 266 ? -5.294  -3.820  -13.389 1.00 30.30 ?  258 ALA B O     1 
ATOM   6513 C CB    . ALA C 1 266 ? -4.950  -5.647  -16.144 1.00 21.89 ?  258 ALA B CB    1 
ATOM   6514 N N     . LYS C 1 267 ? -6.877  -5.395  -13.643 1.00 29.97 ?  259 LYS B N     1 
ATOM   6515 C CA    . LYS C 1 267 ? -7.875  -4.580  -12.959 1.00 29.45 ?  259 LYS B CA    1 
ATOM   6516 C C     . LYS C 1 267 ? -7.657  -4.575  -11.448 1.00 31.12 ?  259 LYS B C     1 
ATOM   6517 O O     . LYS C 1 267 ? -7.831  -3.538  -10.798 1.00 29.63 ?  259 LYS B O     1 
ATOM   6518 C CB    . LYS C 1 267 ? -9.281  -5.075  -13.301 1.00 34.35 ?  259 LYS B CB    1 
ATOM   6519 N N     . GLU C 1 268 ? -7.261  -5.714  -10.873 1.00 31.56 ?  260 GLU B N     1 
ATOM   6520 C CA    . GLU C 1 268 ? -7.205  -5.859  -9.423  1.00 27.95 ?  260 GLU B CA    1 
ATOM   6521 C C     . GLU C 1 268 ? -5.813  -5.672  -8.832  1.00 34.97 ?  260 GLU B C     1 
ATOM   6522 O O     . GLU C 1 268 ? -5.701  -5.463  -7.619  1.00 31.67 ?  260 GLU B O     1 
ATOM   6523 C CB    . GLU C 1 268 ? -7.742  -7.235  -9.008  1.00 34.60 ?  260 GLU B CB    1 
ATOM   6524 C CG    . GLU C 1 268 ? -9.223  -7.420  -9.297  1.00 33.45 ?  260 GLU B CG    1 
ATOM   6525 C CD    . GLU C 1 268 ? -9.746  -8.780  -8.874  1.00 40.54 ?  260 GLU B CD    1 
ATOM   6526 O OE1   . GLU C 1 268 ? -9.383  -9.250  -7.775  1.00 46.18 ?  260 GLU B OE1   1 
ATOM   6527 O OE2   . GLU C 1 268 ? -10.527 -9.380  -9.643  1.00 46.71 ?  260 GLU B OE2   1 
ATOM   6528 N N     . GLU C 1 269 ? -4.756  -5.751  -9.643  1.00 29.45 ?  261 GLU B N     1 
ATOM   6529 C CA    . GLU C 1 269 ? -3.400  -5.508  -9.172  1.00 28.32 ?  261 GLU B CA    1 
ATOM   6530 C C     . GLU C 1 269 ? -2.714  -4.338  -9.861  1.00 29.14 ?  261 GLU B C     1 
ATOM   6531 O O     . GLU C 1 269 ? -1.646  -3.917  -9.403  1.00 26.56 ?  261 GLU B O     1 
ATOM   6532 C CB    . GLU C 1 269 ? -2.525  -6.759  -9.356  1.00 24.94 ?  261 GLU B CB    1 
ATOM   6533 C CG    . GLU C 1 269 ? -3.216  -8.066  -9.031  1.00 26.68 ?  261 GLU B CG    1 
ATOM   6534 C CD    . GLU C 1 269 ? -3.094  -8.440  -7.569  1.00 32.66 ?  261 GLU B CD    1 
ATOM   6535 O OE1   . GLU C 1 269 ? -2.294  -7.799  -6.853  1.00 31.91 ?  261 GLU B OE1   1 
ATOM   6536 O OE2   . GLU C 1 269 ? -3.793  -9.380  -7.136  1.00 29.80 ?  261 GLU B OE2   1 
ATOM   6537 N N     . GLY C 1 270 ? -3.288  -3.803  -10.936 1.00 29.61 ?  262 GLY B N     1 
ATOM   6538 C CA    . GLY C 1 270 ? -2.611  -2.768  -11.688 1.00 24.80 ?  262 GLY B CA    1 
ATOM   6539 C C     . GLY C 1 270 ? -1.431  -3.264  -12.487 1.00 27.52 ?  262 GLY B C     1 
ATOM   6540 O O     . GLY C 1 270 ? -0.529  -2.483  -12.801 1.00 27.59 ?  262 GLY B O     1 
ATOM   6541 N N     . ILE C 1 271 ? -1.411  -4.552  -12.820 1.00 26.92 ?  263 ILE B N     1 
ATOM   6542 C CA    . ILE C 1 271 ? -0.318  -5.176  -13.554 1.00 26.66 ?  263 ILE B CA    1 
ATOM   6543 C C     . ILE C 1 271 ? -0.882  -5.638  -14.891 1.00 31.31 ?  263 ILE B C     1 
ATOM   6544 O O     . ILE C 1 271 ? -1.613  -6.636  -14.955 1.00 31.11 ?  263 ILE B O     1 
ATOM   6545 C CB    . ILE C 1 271 ? 0.301   -6.345  -12.777 1.00 24.12 ?  263 ILE B CB    1 
ATOM   6546 C CG1   . ILE C 1 271 ? 0.915   -5.842  -11.467 1.00 26.79 ?  263 ILE B CG1   1 
ATOM   6547 C CG2   . ILE C 1 271 ? 1.349   -7.054  -13.619 1.00 24.01 ?  263 ILE B CG2   1 
ATOM   6548 C CD1   . ILE C 1 271 ? 1.500   -6.939  -10.602 1.00 23.65 ?  263 ILE B CD1   1 
ATOM   6549 N N     . LEU C 1 272 ? -0.546  -4.912  -15.955 1.00 26.62 ?  264 LEU B N     1 
ATOM   6550 C CA    . LEU C 1 272 ? -1.068  -5.163  -17.297 1.00 24.89 ?  264 LEU B CA    1 
ATOM   6551 C C     . LEU C 1 272 ? -0.060  -6.022  -18.053 1.00 24.78 ?  264 LEU B C     1 
ATOM   6552 O O     . LEU C 1 272 ? 0.971   -5.526  -18.513 1.00 23.88 ?  264 LEU B O     1 
ATOM   6553 C CB    . LEU C 1 272 ? -1.328  -3.846  -18.017 1.00 24.95 ?  264 LEU B CB    1 
ATOM   6554 C CG    . LEU C 1 272 ? -1.736  -3.932  -19.484 1.00 32.27 ?  264 LEU B CG    1 
ATOM   6555 C CD1   . LEU C 1 272 ? -3.218  -4.238  -19.599 1.00 31.90 ?  264 LEU B CD1   1 
ATOM   6556 C CD2   . LEU C 1 272 ? -1.388  -2.639  -20.195 1.00 28.91 ?  264 LEU B CD2   1 
ATOM   6557 N N     . ALA C 1 273 ? -0.366  -7.309  -18.194 1.00 23.05 ?  265 ALA B N     1 
ATOM   6558 C CA    . ALA C 1 273 ? 0.557   -8.269  -18.776 1.00 24.90 ?  265 ALA B CA    1 
ATOM   6559 C C     . ALA C 1 273 ? -0.140  -9.072  -19.868 1.00 29.79 ?  265 ALA B C     1 
ATOM   6560 O O     . ALA C 1 273 ? -1.355  -8.983  -20.062 1.00 29.37 ?  265 ALA B O     1 
ATOM   6561 C CB    . ALA C 1 273 ? 1.129   -9.199  -17.701 1.00 25.18 ?  265 ALA B CB    1 
ATOM   6562 N N     . GLY C 1 274 ? 0.653   -9.871  -20.584 1.00 28.14 ?  266 GLY B N     1 
ATOM   6563 C CA    . GLY C 1 274 ? 0.167   -10.601 -21.735 1.00 28.34 ?  266 GLY B CA    1 
ATOM   6564 C C     . GLY C 1 274 ? -0.616  -11.848 -21.370 1.00 26.47 ?  266 GLY B C     1 
ATOM   6565 O O     . GLY C 1 274 ? -0.856  -12.160 -20.203 1.00 27.82 ?  266 GLY B O     1 
ATOM   6566 N N     . ILE C 1 275 ? -1.023  -12.575 -22.416 1.00 31.59 ?  267 ILE B N     1 
ATOM   6567 C CA    . ILE C 1 275 ? -1.823  -13.784 -22.233 1.00 28.19 ?  267 ILE B CA    1 
ATOM   6568 C C     . ILE C 1 275 ? -1.045  -14.825 -21.441 1.00 27.45 ?  267 ILE B C     1 
ATOM   6569 O O     . ILE C 1 275 ? -1.586  -15.468 -20.532 1.00 28.63 ?  267 ILE B O     1 
ATOM   6570 C CB    . ILE C 1 275 ? -2.272  -14.346 -23.596 1.00 34.80 ?  267 ILE B CB    1 
ATOM   6571 C CG1   . ILE C 1 275 ? -3.110  -13.322 -24.360 1.00 40.71 ?  267 ILE B CG1   1 
ATOM   6572 C CG2   . ILE C 1 275 ? -3.065  -15.627 -23.405 1.00 34.71 ?  267 ILE B CG2   1 
ATOM   6573 C CD1   . ILE C 1 275 ? -2.875  -13.328 -25.859 1.00 47.15 ?  267 ILE B CD1   1 
ATOM   6574 N N     . SER C 1 276 ? 0.233   -15.014 -21.778 1.00 25.43 ?  268 SER B N     1 
ATOM   6575 C CA    . SER C 1 276 ? 1.025   -16.043 -21.115 1.00 24.71 ?  268 SER B CA    1 
ATOM   6576 C C     . SER C 1 276 ? 1.251   -15.724 -19.644 1.00 27.17 ?  268 SER B C     1 
ATOM   6577 O O     . SER C 1 276 ? 1.455   -16.639 -18.840 1.00 25.01 ?  268 SER B O     1 
ATOM   6578 C CB    . SER C 1 276 ? 2.362   -16.218 -21.831 1.00 26.44 ?  268 SER B CB    1 
ATOM   6579 O OG    . SER C 1 276 ? 3.137   -15.036 -21.744 1.00 23.97 ?  268 SER B OG    1 
ATOM   6580 N N     . SER C 1 277 ? 1.231   -14.442 -19.278 1.00 24.64 ?  269 SER B N     1 
ATOM   6581 C CA    . SER C 1 277 ? 1.346   -14.071 -17.872 1.00 25.99 ?  269 SER B CA    1 
ATOM   6582 C C     . SER C 1 277 ? 0.076   -14.425 -17.108 1.00 26.03 ?  269 SER B C     1 
ATOM   6583 O O     . SER C 1 277 ? 0.140   -14.839 -15.944 1.00 27.40 ?  269 SER B O     1 
ATOM   6584 C CB    . SER C 1 277 ? 1.655   -12.581 -17.749 1.00 21.98 ?  269 SER B CB    1 
ATOM   6585 O OG    . SER C 1 277 ? 2.818   -12.243 -18.488 1.00 24.86 ?  269 SER B OG    1 
ATOM   6586 N N     . GLY C 1 278 ? -1.088  -14.268 -17.743 1.00 25.45 ?  270 GLY B N     1 
ATOM   6587 C CA    . GLY C 1 278 ? -2.315  -14.750 -17.131 1.00 27.94 ?  270 GLY B CA    1 
ATOM   6588 C C     . GLY C 1 278 ? -2.281  -16.246 -16.892 1.00 27.35 ?  270 GLY B C     1 
ATOM   6589 O O     . GLY C 1 278 ? -2.761  -16.734 -15.866 1.00 28.64 ?  270 GLY B O     1 
ATOM   6590 N N     . ALA C 1 279 ? -1.701  -16.993 -17.835 1.00 25.12 ?  271 ALA B N     1 
ATOM   6591 C CA    . ALA C 1 279 ? -1.506  -18.425 -17.642 1.00 26.31 ?  271 ALA B CA    1 
ATOM   6592 C C     . ALA C 1 279 ? -0.519  -18.696 -16.515 1.00 28.55 ?  271 ALA B C     1 
ATOM   6593 O O     . ALA C 1 279 ? -0.713  -19.621 -15.717 1.00 24.79 ?  271 ALA B O     1 
ATOM   6594 C CB    . ALA C 1 279 ? -1.022  -19.065 -18.943 1.00 23.85 ?  271 ALA B CB    1 
ATOM   6595 N N     . ALA C 1 280 ? 0.549   -17.898 -16.437 1.00 27.35 ?  272 ALA B N     1 
ATOM   6596 C CA    . ALA C 1 280 ? 1.542   -18.083 -15.385 1.00 25.46 ?  272 ALA B CA    1 
ATOM   6597 C C     . ALA C 1 280 ? 0.958   -17.781 -14.013 1.00 26.14 ?  272 ALA B C     1 
ATOM   6598 O O     . ALA C 1 280 ? 1.256   -18.479 -13.037 1.00 24.46 ?  272 ALA B O     1 
ATOM   6599 C CB    . ALA C 1 280 ? 2.761   -17.200 -15.656 1.00 25.15 ?  272 ALA B CB    1 
ATOM   6600 N N     . ILE C 1 281 ? 0.118   -16.751 -13.918 1.00 26.05 ?  273 ILE B N     1 
ATOM   6601 C CA    . ILE C 1 281 ? -0.440  -16.379 -12.624 1.00 24.34 ?  273 ILE B CA    1 
ATOM   6602 C C     . ILE C 1 281 ? -1.547  -17.343 -12.211 1.00 28.01 ?  273 ILE B C     1 
ATOM   6603 O O     . ILE C 1 281 ? -1.677  -17.682 -11.029 1.00 28.64 ?  273 ILE B O     1 
ATOM   6604 C CB    . ILE C 1 281 ? -0.921  -14.917 -12.661 1.00 26.54 ?  273 ILE B CB    1 
ATOM   6605 C CG1   . ILE C 1 281 ? 0.285   -13.976 -12.624 1.00 23.61 ?  273 ILE B CG1   1 
ATOM   6606 C CG2   . ILE C 1 281 ? -1.861  -14.618 -11.504 1.00 29.15 ?  273 ILE B CG2   1 
ATOM   6607 C CD1   . ILE C 1 281 ? -0.052  -12.534 -12.907 1.00 27.16 ?  273 ILE B CD1   1 
ATOM   6608 N N     . TYR C 1 282 ? -2.347  -17.816 -13.171 1.00 26.28 ?  274 TYR B N     1 
ATOM   6609 C CA    . TYR C 1 282 ? -3.383  -18.793 -12.849 1.00 29.29 ?  274 TYR B CA    1 
ATOM   6610 C C     . TYR C 1 282 ? -2.776  -20.079 -12.302 1.00 30.04 ?  274 TYR B C     1 
ATOM   6611 O O     . TYR C 1 282 ? -3.262  -20.637 -11.311 1.00 30.99 ?  274 TYR B O     1 
ATOM   6612 C CB    . TYR C 1 282 ? -4.236  -19.094 -14.081 1.00 28.78 ?  274 TYR B CB    1 
ATOM   6613 C CG    . TYR C 1 282 ? -5.147  -20.288 -13.891 1.00 33.39 ?  274 TYR B CG    1 
ATOM   6614 C CD1   . TYR C 1 282 ? -6.352  -20.162 -13.213 1.00 34.47 ?  274 TYR B CD1   1 
ATOM   6615 C CD2   . TYR C 1 282 ? -4.802  -21.541 -14.388 1.00 33.91 ?  274 TYR B CD2   1 
ATOM   6616 C CE1   . TYR C 1 282 ? -7.189  -21.248 -13.034 1.00 37.43 ?  274 TYR B CE1   1 
ATOM   6617 C CE2   . TYR C 1 282 ? -5.633  -22.633 -14.212 1.00 35.70 ?  274 TYR B CE2   1 
ATOM   6618 C CZ    . TYR C 1 282 ? -6.826  -22.480 -13.536 1.00 40.09 ?  274 TYR B CZ    1 
ATOM   6619 O OH    . TYR C 1 282 ? -7.660  -23.560 -13.358 1.00 43.33 ?  274 TYR B OH    1 
ATOM   6620 N N     . ALA C 1 283 ? -1.719  -20.573 -12.950 1.00 28.18 ?  275 ALA B N     1 
ATOM   6621 C CA    . ALA C 1 283 ? -1.060  -21.785 -12.479 1.00 27.65 ?  275 ALA B CA    1 
ATOM   6622 C C     . ALA C 1 283 ? -0.400  -21.561 -11.127 1.00 29.62 ?  275 ALA B C     1 
ATOM   6623 O O     . ALA C 1 283 ? -0.450  -22.433 -10.251 1.00 31.02 ?  275 ALA B O     1 
ATOM   6624 C CB    . ALA C 1 283 ? -0.033  -22.258 -13.507 1.00 20.75 ?  275 ALA B CB    1 
ATOM   6625 N N     . ALA C 1 284 ? 0.221   -20.394 -10.937 1.00 28.69 ?  276 ALA B N     1 
ATOM   6626 C CA    . ALA C 1 284 ? 0.858   -20.096 -9.660  1.00 29.27 ?  276 ALA B CA    1 
ATOM   6627 C C     . ALA C 1 284 ? -0.170  -19.993 -8.542  1.00 32.11 ?  276 ALA B C     1 
ATOM   6628 O O     . ALA C 1 284 ? 0.102   -20.386 -7.402  1.00 32.88 ?  276 ALA B O     1 
ATOM   6629 C CB    . ALA C 1 284 ? 1.668   -18.804 -9.768  1.00 26.46 ?  276 ALA B CB    1 
ATOM   6630 N N     . ILE C 1 285 ? -1.357  -19.462 -8.847  1.00 32.31 ?  277 ILE B N     1 
ATOM   6631 C CA    . ILE C 1 285 ? -2.412  -19.379 -7.840  1.00 33.90 ?  277 ILE B CA    1 
ATOM   6632 C C     . ILE C 1 285 ? -2.868  -20.774 -7.436  1.00 34.96 ?  277 ILE B C     1 
ATOM   6633 O O     . ILE C 1 285 ? -3.047  -21.066 -6.247  1.00 35.97 ?  277 ILE B O     1 
ATOM   6634 C CB    . ILE C 1 285 ? -3.584  -18.526 -8.358  1.00 35.74 ?  277 ILE B CB    1 
ATOM   6635 C CG1   . ILE C 1 285 ? -3.270  -17.040 -8.199  1.00 37.10 ?  277 ILE B CG1   1 
ATOM   6636 C CG2   . ILE C 1 285 ? -4.872  -18.879 -7.626  1.00 33.85 ?  277 ILE B CG2   1 
ATOM   6637 C CD1   . ILE C 1 285 ? -4.119  -16.147 -9.069  1.00 35.74 ?  277 ILE B CD1   1 
ATOM   6638 N N     . GLN C 1 286 ? -3.059  -21.658 -8.418  1.00 32.57 ?  278 GLN B N     1 
ATOM   6639 C CA    . GLN C 1 286 ? -3.444  -23.030 -8.108  1.00 34.84 ?  278 GLN B CA    1 
ATOM   6640 C C     . GLN C 1 286 ? -2.370  -23.727 -7.281  1.00 36.55 ?  278 GLN B C     1 
ATOM   6641 O O     . GLN C 1 286 ? -2.681  -24.451 -6.329  1.00 37.19 ?  278 GLN B O     1 
ATOM   6642 C CB    . GLN C 1 286 ? -3.723  -23.796 -9.402  1.00 38.44 ?  278 GLN B CB    1 
ATOM   6643 C CG    . GLN C 1 286 ? -3.342  -25.262 -9.353  1.00 44.59 ?  278 GLN B CG    1 
ATOM   6644 C CD    . GLN C 1 286 ? -3.789  -26.020 -10.584 1.00 48.62 ?  278 GLN B CD    1 
ATOM   6645 O OE1   . GLN C 1 286 ? -4.712  -25.603 -11.284 1.00 52.12 ?  278 GLN B OE1   1 
ATOM   6646 N NE2   . GLN C 1 286 ? -3.132  -27.141 -10.857 1.00 41.99 ?  278 GLN B NE2   1 
ATOM   6647 N N     . LYS C 1 287 ? -1.098  -23.510 -7.623  1.00 33.92 ?  279 LYS B N     1 
ATOM   6648 C CA    . LYS C 1 287 ? -0.013  -24.052 -6.812  1.00 33.16 ?  279 LYS B CA    1 
ATOM   6649 C C     . LYS C 1 287 ? 0.003   -23.421 -5.424  1.00 33.95 ?  279 LYS B C     1 
ATOM   6650 O O     . LYS C 1 287 ? 0.289   -24.097 -4.430  1.00 34.48 ?  279 LYS B O     1 
ATOM   6651 C CB    . LYS C 1 287 ? 1.328   -23.839 -7.518  1.00 33.60 ?  279 LYS B CB    1 
ATOM   6652 C CG    . LYS C 1 287 ? 2.549   -24.292 -6.723  1.00 35.07 ?  279 LYS B CG    1 
ATOM   6653 C CD    . LYS C 1 287 ? 2.524   -25.786 -6.433  1.00 36.04 ?  279 LYS B CD    1 
ATOM   6654 C CE    . LYS C 1 287 ? 2.382   -26.596 -7.706  1.00 34.17 ?  279 LYS B CE    1 
ATOM   6655 N NZ    . LYS C 1 287 ? 2.397   -28.055 -7.426  1.00 39.12 ?  279 LYS B NZ    1 
ATOM   6656 N N     . ALA C 1 288 ? -0.310  -22.126 -5.337  1.00 32.61 ?  280 ALA B N     1 
ATOM   6657 C CA    . ALA C 1 288 ? -0.318  -21.450 -4.042  1.00 31.96 ?  280 ALA B CA    1 
ATOM   6658 C C     . ALA C 1 288 ? -1.464  -21.940 -3.166  1.00 38.21 ?  280 ALA B C     1 
ATOM   6659 O O     . ALA C 1 288 ? -1.306  -22.070 -1.946  1.00 34.91 ?  280 ALA B O     1 
ATOM   6660 C CB    . ALA C 1 288 ? -0.404  -19.938 -4.238  1.00 36.12 ?  280 ALA B CB    1 
ATOM   6661 N N     . LYS C 1 289 ? -2.630  -22.200 -3.765  1.00 34.76 ?  281 LYS B N     1 
ATOM   6662 C CA    . LYS C 1 289 ? -3.722  -22.816 -3.020  1.00 37.84 ?  281 LYS B CA    1 
ATOM   6663 C C     . LYS C 1 289 ? -3.319  -24.183 -2.485  1.00 44.27 ?  281 LYS B C     1 
ATOM   6664 O O     . LYS C 1 289 ? -3.769  -24.589 -1.406  1.00 39.72 ?  281 LYS B O     1 
ATOM   6665 C CB    . LYS C 1 289 ? -4.959  -22.949 -3.909  1.00 36.21 ?  281 LYS B CB    1 
ATOM   6666 C CG    . LYS C 1 289 ? -5.630  -21.640 -4.277  1.00 33.54 ?  281 LYS B CG    1 
ATOM   6667 C CD    . LYS C 1 289 ? -7.055  -21.887 -4.748  1.00 36.87 ?  281 LYS B CD    1 
ATOM   6668 C CE    . LYS C 1 289 ? -7.128  -21.978 -6.261  1.00 43.69 ?  281 LYS B CE    1 
ATOM   6669 N NZ    . LYS C 1 289 ? -8.508  -21.738 -6.769  1.00 42.53 ?  281 LYS B NZ    1 
ATOM   6670 N N     . GLU C 1 290 ? -2.468  -24.898 -3.223  1.00 39.65 ?  282 GLU B N     1 
ATOM   6671 C CA    . GLU C 1 290 ? -2.054  -26.235 -2.813  1.00 37.32 ?  282 GLU B CA    1 
ATOM   6672 C C     . GLU C 1 290 ? -1.105  -26.185 -1.622  1.00 41.62 ?  282 GLU B C     1 
ATOM   6673 O O     . GLU C 1 290 ? -1.157  -27.055 -0.744  1.00 44.32 ?  282 GLU B O     1 
ATOM   6674 C CB    . GLU C 1 290 ? -1.398  -26.948 -3.995  1.00 37.78 ?  282 GLU B CB    1 
ATOM   6675 C CG    . GLU C 1 290 ? -1.071  -28.416 -3.776  1.00 44.79 ?  282 GLU B CG    1 
ATOM   6676 C CD    . GLU C 1 290 ? -0.324  -29.015 -4.957  1.00 46.05 ?  282 GLU B CD    1 
ATOM   6677 O OE1   . GLU C 1 290 ? -0.365  -28.413 -6.051  1.00 43.98 ?  282 GLU B OE1   1 
ATOM   6678 O OE2   . GLU C 1 290 ? 0.301   -30.085 -4.795  1.00 50.60 ?  282 GLU B OE2   1 
ATOM   6679 N N     . LEU C 1 291 ? -0.239  -25.175 -1.567  1.00 37.79 ?  283 LEU B N     1 
ATOM   6680 C CA    . LEU C 1 291 ? 0.806   -25.133 -0.552  1.00 37.05 ?  283 LEU B CA    1 
ATOM   6681 C C     . LEU C 1 291 ? 0.366   -24.443 0.732   1.00 39.01 ?  283 LEU B C     1 
ATOM   6682 O O     . LEU C 1 291 ? 0.918   -24.732 1.799   1.00 42.64 ?  283 LEU B O     1 
ATOM   6683 C CB    . LEU C 1 291 ? 2.050   -24.440 -1.113  1.00 38.77 ?  283 LEU B CB    1 
ATOM   6684 C CG    . LEU C 1 291 ? 2.607   -25.082 -2.387  1.00 37.85 ?  283 LEU B CG    1 
ATOM   6685 C CD1   . LEU C 1 291 ? 3.927   -24.447 -2.786  1.00 36.64 ?  283 LEU B CD1   1 
ATOM   6686 C CD2   . LEU C 1 291 ? 2.761   -26.587 -2.208  1.00 39.23 ?  283 LEU B CD2   1 
ATOM   6687 N N     . GLY C 1 292 ? -0.606  -23.536 0.658   1.00 35.64 ?  284 GLY B N     1 
ATOM   6688 C CA    . GLY C 1 292 ? -1.161  -22.931 1.850   1.00 38.12 ?  284 GLY B CA    1 
ATOM   6689 C C     . GLY C 1 292 ? -0.340  -21.768 2.376   1.00 41.76 ?  284 GLY B C     1 
ATOM   6690 O O     . GLY C 1 292 ? 0.729   -21.422 1.869   1.00 36.97 ?  284 GLY B O     1 
ATOM   6691 N N     . LYS C 1 293 ? -0.870  -21.160 3.436   1.00 42.33 ?  285 LYS B N     1 
ATOM   6692 C CA    . LYS C 1 293 ? -0.267  -19.969 4.018   1.00 43.92 ?  285 LYS B CA    1 
ATOM   6693 C C     . LYS C 1 293 ? 1.148   -20.252 4.506   1.00 39.44 ?  285 LYS B C     1 
ATOM   6694 O O     . LYS C 1 293 ? 1.457   -21.345 4.987   1.00 38.24 ?  285 LYS B O     1 
ATOM   6695 C CB    . LYS C 1 293 ? -1.124  -19.462 5.179   1.00 43.86 ?  285 LYS B CB    1 
ATOM   6696 C CG    . LYS C 1 293 ? -1.376  -17.966 5.178   1.00 51.55 ?  285 LYS B CG    1 
ATOM   6697 C CD    . LYS C 1 293 ? -1.479  -17.430 6.600   1.00 48.58 ?  285 LYS B CD    1 
ATOM   6698 C CE    . LYS C 1 293 ? -2.673  -16.501 6.760   1.00 53.28 ?  285 LYS B CE    1 
ATOM   6699 N NZ    . LYS C 1 293 ? -3.959  -17.189 6.455   1.00 59.68 ?  285 LYS B NZ    1 
ATOM   6700 N N     . GLY C 1 294 ? 2.014   -19.245 4.379   1.00 39.38 ?  286 GLY B N     1 
ATOM   6701 C CA    . GLY C 1 294 ? 3.385   -19.312 4.828   1.00 40.62 ?  286 GLY B CA    1 
ATOM   6702 C C     . GLY C 1 294 ? 4.383   -19.671 3.744   1.00 42.51 ?  286 GLY B C     1 
ATOM   6703 O O     . GLY C 1 294 ? 5.552   -19.279 3.837   1.00 40.53 ?  286 GLY B O     1 
ATOM   6704 N N     . LYS C 1 295 ? 3.952   -20.408 2.725   1.00 42.00 ?  287 LYS B N     1 
ATOM   6705 C CA    . LYS C 1 295 ? 4.845   -20.809 1.652   1.00 39.60 ?  287 LYS B CA    1 
ATOM   6706 C C     . LYS C 1 295 ? 4.953   -19.694 0.612   1.00 40.51 ?  287 LYS B C     1 
ATOM   6707 O O     . LYS C 1 295 ? 4.194   -18.721 0.621   1.00 35.73 ?  287 LYS B O     1 
ATOM   6708 C CB    . LYS C 1 295 ? 4.362   -22.116 1.021   1.00 38.71 ?  287 LYS B CB    1 
ATOM   6709 C CG    . LYS C 1 295 ? 4.208   -23.273 2.013   1.00 35.85 ?  287 LYS B CG    1 
ATOM   6710 C CD    . LYS C 1 295 ? 5.309   -23.263 3.071   1.00 45.60 ?  287 LYS B CD    1 
ATOM   6711 C CE    . LYS C 1 295 ? 5.201   -24.454 4.012   1.00 45.03 ?  287 LYS B CE    1 
ATOM   6712 N NZ    . LYS C 1 295 ? 5.197   -25.751 3.279   1.00 54.96 ?  287 LYS B NZ    1 
ATOM   6713 N N     . THR C 1 296 ? 5.922   -19.837 -0.292  1.00 36.95 ?  288 THR B N     1 
ATOM   6714 C CA    . THR C 1 296 ? 6.257   -18.789 -1.248  1.00 35.12 ?  288 THR B CA    1 
ATOM   6715 C C     . THR C 1 296 ? 6.338   -19.377 -2.649  1.00 36.27 ?  288 THR B C     1 
ATOM   6716 O O     . THR C 1 296 ? 7.046   -20.365 -2.871  1.00 40.00 ?  288 THR B O     1 
ATOM   6717 C CB    . THR C 1 296 ? 7.580   -18.111 -0.871  1.00 36.57 ?  288 THR B CB    1 
ATOM   6718 O OG1   . THR C 1 296 ? 7.403   -17.371 0.343   1.00 37.73 ?  288 THR B OG1   1 
ATOM   6719 C CG2   . THR C 1 296 ? 8.031   -17.161 -1.968  1.00 34.94 ?  288 THR B CG2   1 
ATOM   6720 N N     . VAL C 1 297 ? 5.617   -18.765 -3.588  1.00 29.06 ?  289 VAL B N     1 
ATOM   6721 C CA    . VAL C 1 297 ? 5.512   -19.243 -4.962  1.00 29.37 ?  289 VAL B CA    1 
ATOM   6722 C C     . VAL C 1 297 ? 5.922   -18.113 -5.899  1.00 31.22 ?  289 VAL B C     1 
ATOM   6723 O O     . VAL C 1 297 ? 5.464   -16.976 -5.744  1.00 33.09 ?  289 VAL B O     1 
ATOM   6724 C CB    . VAL C 1 297 ? 4.085   -19.734 -5.275  1.00 35.41 ?  289 VAL B CB    1 
ATOM   6725 C CG1   . VAL C 1 297 ? 3.853   -19.811 -6.773  1.00 27.98 ?  289 VAL B CG1   1 
ATOM   6726 C CG2   . VAL C 1 297 ? 3.838   -21.087 -4.624  1.00 32.61 ?  289 VAL B CG2   1 
ATOM   6727 N N     . VAL C 1 298 ? 6.782   -18.428 -6.870  1.00 32.31 ?  290 VAL B N     1 
ATOM   6728 C CA    . VAL C 1 298 ? 7.364   -17.440 -7.772  1.00 28.12 ?  290 VAL B CA    1 
ATOM   6729 C C     . VAL C 1 298 ? 7.071   -17.841 -9.213  1.00 27.36 ?  290 VAL B C     1 
ATOM   6730 O O     . VAL C 1 298 ? 7.103   -19.028 -9.556  1.00 30.39 ?  290 VAL B O     1 
ATOM   6731 C CB    . VAL C 1 298 ? 8.885   -17.304 -7.540  1.00 28.75 ?  290 VAL B CB    1 
ATOM   6732 C CG1   . VAL C 1 298 ? 9.489   -16.254 -8.465  1.00 27.30 ?  290 VAL B CG1   1 
ATOM   6733 C CG2   . VAL C 1 298 ? 9.172   -16.971 -6.086  1.00 28.42 ?  290 VAL B CG2   1 
ATOM   6734 N N     . THR C 1 299 ? 6.783   -16.849 -10.056 1.00 28.30 ?  291 THR B N     1 
ATOM   6735 C CA    . THR C 1 299 ? 6.596   -17.072 -11.484 1.00 29.70 ?  291 THR B CA    1 
ATOM   6736 C C     . THR C 1 299 ? 7.059   -15.830 -12.238 1.00 25.26 ?  291 THR B C     1 
ATOM   6737 O O     . THR C 1 299 ? 7.497   -14.844 -11.640 1.00 28.38 ?  291 THR B O     1 
ATOM   6738 C CB    . THR C 1 299 ? 5.140   -17.423 -11.813 1.00 29.25 ?  291 THR B CB    1 
ATOM   6739 O OG1   . THR C 1 299 ? 5.057   -17.892 -13.165 1.00 26.92 ?  291 THR B OG1   1 
ATOM   6740 C CG2   . THR C 1 299 ? 4.240   -16.210 -11.642 1.00 24.95 ?  291 THR B CG2   1 
ATOM   6741 N N     . VAL C 1 300 ? 6.955   -15.883 -13.565 1.00 29.71 ?  292 VAL B N     1 
ATOM   6742 C CA    . VAL C 1 300 ? 7.507   -14.861 -14.447 1.00 24.98 ?  292 VAL B CA    1 
ATOM   6743 C C     . VAL C 1 300 ? 6.409   -14.338 -15.363 1.00 27.06 ?  292 VAL B C     1 
ATOM   6744 O O     . VAL C 1 300 ? 5.612   -15.115 -15.899 1.00 30.07 ?  292 VAL B O     1 
ATOM   6745 C CB    . VAL C 1 300 ? 8.691   -15.419 -15.269 1.00 28.62 ?  292 VAL B CB    1 
ATOM   6746 C CG1   . VAL C 1 300 ? 8.878   -14.642 -16.567 1.00 25.11 ?  292 VAL B CG1   1 
ATOM   6747 C CG2   . VAL C 1 300 ? 9.967   -15.399 -14.444 1.00 26.02 ?  292 VAL B CG2   1 
ATOM   6748 N N     . LEU C 1 301 ? 6.369   -13.015 -15.537 1.00 29.12 ?  293 LEU B N     1 
ATOM   6749 C CA    . LEU C 1 301 ? 5.493   -12.376 -16.516 1.00 27.59 ?  293 LEU B CA    1 
ATOM   6750 C C     . LEU C 1 301 ? 6.328   -11.934 -17.712 1.00 27.35 ?  293 LEU B C     1 
ATOM   6751 O O     . LEU C 1 301 ? 7.034   -10.916 -17.634 1.00 27.48 ?  293 LEU B O     1 
ATOM   6752 C CB    . LEU C 1 301 ? 4.758   -11.181 -15.900 1.00 25.00 ?  293 LEU B CB    1 
ATOM   6753 C CG    . LEU C 1 301 ? 4.082   -11.380 -14.540 1.00 28.71 ?  293 LEU B CG    1 
ATOM   6754 C CD1   . LEU C 1 301 ? 3.140   -10.223 -14.249 1.00 23.47 ?  293 LEU B CD1   1 
ATOM   6755 C CD2   . LEU C 1 301 ? 3.334   -12.704 -14.476 1.00 25.58 ?  293 LEU B CD2   1 
ATOM   6756 N N     . PRO C 1 302 ? 6.283   -12.655 -18.837 1.00 25.91 ?  294 PRO B N     1 
ATOM   6757 C CA    . PRO C 1 302 ? 7.251   -12.398 -19.915 1.00 29.21 ?  294 PRO B CA    1 
ATOM   6758 C C     . PRO C 1 302 ? 7.009   -11.135 -20.729 1.00 27.31 ?  294 PRO B C     1 
ATOM   6759 O O     . PRO C 1 302 ? 7.971   -10.624 -21.317 1.00 26.40 ?  294 PRO B O     1 
ATOM   6760 C CB    . PRO C 1 302 ? 7.119   -13.646 -20.804 1.00 28.31 ?  294 PRO B CB    1 
ATOM   6761 C CG    . PRO C 1 302 ? 6.529   -14.690 -19.895 1.00 27.04 ?  294 PRO B CG    1 
ATOM   6762 C CD    . PRO C 1 302 ? 5.563   -13.919 -19.053 1.00 27.96 ?  294 PRO B CD    1 
ATOM   6763 N N     . SER C 1 303 ? 5.785   -10.615 -20.802 1.00 23.29 ?  295 SER B N     1 
ATOM   6764 C CA    . SER C 1 303 ? 5.523   -9.481  -21.678 1.00 26.66 ?  295 SER B CA    1 
ATOM   6765 C C     . SER C 1 303 ? 4.405   -8.620  -21.105 1.00 26.07 ?  295 SER B C     1 
ATOM   6766 O O     . SER C 1 303 ? 3.698   -9.011  -20.171 1.00 26.38 ?  295 SER B O     1 
ATOM   6767 C CB    . SER C 1 303 ? 5.177   -9.940  -23.099 1.00 26.89 ?  295 SER B CB    1 
ATOM   6768 O OG    . SER C 1 303 ? 3.968   -10.680 -23.121 1.00 27.91 ?  295 SER B OG    1 
ATOM   6769 N N     . ASN C 1 304 ? 4.250   -7.435  -21.693 1.00 21.73 ?  296 ASN B N     1 
ATOM   6770 C CA    . ASN C 1 304 ? 3.305   -6.425  -21.239 1.00 24.06 ?  296 ASN B CA    1 
ATOM   6771 C C     . ASN C 1 304 ? 2.004   -6.502  -22.029 1.00 29.10 ?  296 ASN B C     1 
ATOM   6772 O O     . ASN C 1 304 ? 1.989   -6.871  -23.207 1.00 27.52 ?  296 ASN B O     1 
ATOM   6773 C CB    . ASN C 1 304 ? 3.911   -5.026  -21.369 1.00 24.76 ?  296 ASN B CB    1 
ATOM   6774 C CG    . ASN C 1 304 ? 3.096   -3.970  -20.652 1.00 33.16 ?  296 ASN B CG    1 
ATOM   6775 O OD1   . ASN C 1 304 ? 2.145   -3.424  -21.211 1.00 29.22 ?  296 ASN B OD1   1 
ATOM   6776 N ND2   . ASN C 1 304 ? 3.459   -3.682  -19.408 1.00 29.54 ?  296 ASN B ND2   1 
ATOM   6777 N N     . GLY C 1 305 ? 0.904   -6.138  -21.364 1.00 29.53 ?  297 GLY B N     1 
ATOM   6778 C CA    . GLY C 1 305 ? -0.402  -6.230  -21.995 1.00 30.67 ?  297 GLY B CA    1 
ATOM   6779 C C     . GLY C 1 305 ? -0.613  -5.215  -23.101 1.00 31.90 ?  297 GLY B C     1 
ATOM   6780 O O     . GLY C 1 305 ? -1.457  -5.419  -23.979 1.00 36.49 ?  297 GLY B O     1 
ATOM   6781 N N     . GLU C 1 306 ? 0.143   -4.114  -23.079 1.00 29.23 ?  298 GLU B N     1 
ATOM   6782 C CA    . GLU C 1 306 ? 0.015   -3.095  -24.115 1.00 36.55 ?  298 GLU B CA    1 
ATOM   6783 C C     . GLU C 1 306 ? 0.387   -3.634  -25.488 1.00 33.37 ?  298 GLU B C     1 
ATOM   6784 O O     . GLU C 1 306 ? -0.093  -3.114  -26.500 1.00 31.18 ?  298 GLU B O     1 
ATOM   6785 C CB    . GLU C 1 306 ? 0.884   -1.884  -23.759 1.00 31.96 ?  298 GLU B CB    1 
ATOM   6786 C CG    . GLU C 1 306 ? 0.663   -0.672  -24.651 1.00 36.28 ?  298 GLU B CG    1 
ATOM   6787 C CD    . GLU C 1 306 ? 1.319   0.585   -24.109 1.00 34.27 ?  298 GLU B CD    1 
ATOM   6788 O OE1   . GLU C 1 306 ? 1.602   0.639   -22.893 1.00 32.44 ?  298 GLU B OE1   1 
ATOM   6789 O OE2   . GLU C 1 306 ? 1.553   1.520   -24.903 1.00 29.29 ?  298 GLU B OE2   1 
ATOM   6790 N N     . ARG C 1 307 ? 1.216   -4.674  -25.541 1.00 32.58 ?  299 ARG B N     1 
ATOM   6791 C CA    . ARG C 1 307 ? 1.575   -5.327  -26.791 1.00 31.74 ?  299 ARG B CA    1 
ATOM   6792 C C     . ARG C 1 307 ? 0.439   -6.173  -27.360 1.00 33.70 ?  299 ARG B C     1 
ATOM   6793 O O     . ARG C 1 307 ? 0.577   -6.712  -28.463 1.00 34.97 ?  299 ARG B O     1 
ATOM   6794 C CB    . ARG C 1 307 ? 2.827   -6.181  -26.558 1.00 27.27 ?  299 ARG B CB    1 
ATOM   6795 C CG    . ARG C 1 307 ? 3.524   -6.674  -27.811 1.00 29.89 ?  299 ARG B CG    1 
ATOM   6796 C CD    . ARG C 1 307 ? 4.935   -7.127  -27.497 1.00 30.13 ?  299 ARG B CD    1 
ATOM   6797 N NE    . ARG C 1 307 ? 5.818   -6.006  -27.197 1.00 31.18 ?  299 ARG B NE    1 
ATOM   6798 C CZ    . ARG C 1 307 ? 7.092   -6.129  -26.853 1.00 31.21 ?  299 ARG B CZ    1 
ATOM   6799 N NH1   . ARG C 1 307 ? 7.664   -7.317  -26.739 1.00 25.96 ?  299 ARG B NH1   1 
ATOM   6800 N NH2   . ARG C 1 307 ? 7.810   -5.035  -26.619 1.00 24.93 ?  299 ARG B NH2   1 
ATOM   6801 N N     . TYR C 1 308 ? -0.691  -6.278  -26.653 1.00 39.18 ?  300 TYR B N     1 
ATOM   6802 C CA    . TYR C 1 308 ? -1.767  -7.181  -27.045 1.00 38.02 ?  300 TYR B CA    1 
ATOM   6803 C C     . TYR C 1 308 ? -3.117  -6.472  -27.134 1.00 46.47 ?  300 TYR B C     1 
ATOM   6804 O O     . TYR C 1 308 ? -4.159  -7.119  -26.983 1.00 45.65 ?  300 TYR B O     1 
ATOM   6805 C CB    . TYR C 1 308 ? -1.862  -8.363  -26.071 1.00 40.14 ?  300 TYR B CB    1 
ATOM   6806 C CG    . TYR C 1 308 ? -0.575  -9.153  -25.909 1.00 42.66 ?  300 TYR B CG    1 
ATOM   6807 C CD1   . TYR C 1 308 ? 0.506   -8.633  -25.205 1.00 33.58 ?  300 TYR B CD1   1 
ATOM   6808 C CD2   . TYR C 1 308 ? -0.441  -10.416 -26.468 1.00 46.39 ?  300 TYR B CD2   1 
ATOM   6809 C CE1   . TYR C 1 308 ? 1.681   -9.350  -25.061 1.00 35.93 ?  300 TYR B CE1   1 
ATOM   6810 C CE2   . TYR C 1 308 ? 0.731   -11.141 -26.328 1.00 46.91 ?  300 TYR B CE2   1 
ATOM   6811 C CZ    . TYR C 1 308 ? 1.788   -10.604 -25.624 1.00 35.10 ?  300 TYR B CZ    1 
ATOM   6812 O OH    . TYR C 1 308 ? 2.955   -11.322 -25.485 1.00 40.36 ?  300 TYR B OH    1 
ATOM   6813 N N     . LEU C 1 309 ? -3.124  -5.159  -27.380 1.00 40.27 ?  301 LEU B N     1 
ATOM   6814 C CA    . LEU C 1 309 ? -4.373  -4.403  -27.412 1.00 45.59 ?  301 LEU B CA    1 
ATOM   6815 C C     . LEU C 1 309 ? -5.217  -4.690  -28.647 1.00 47.41 ?  301 LEU B C     1 
ATOM   6816 O O     . LEU C 1 309 ? -6.394  -4.312  -28.670 1.00 43.50 ?  301 LEU B O     1 
ATOM   6817 C CB    . LEU C 1 309 ? -4.085  -2.902  -27.327 1.00 41.23 ?  301 LEU B CB    1 
ATOM   6818 C CG    . LEU C 1 309 ? -3.310  -2.413  -26.103 1.00 44.84 ?  301 LEU B CG    1 
ATOM   6819 C CD1   . LEU C 1 309 ? -2.957  -0.943  -26.251 1.00 41.09 ?  301 LEU B CD1   1 
ATOM   6820 C CD2   . LEU C 1 309 ? -4.111  -2.651  -24.830 1.00 37.13 ?  301 LEU B CD2   1 
ATOM   6821 N N     . SER C 1 310 ? -4.656  -5.338  -29.665 1.00 48.86 ?  302 SER B N     1 
ATOM   6822 C CA    . SER C 1 310 ? -5.396  -5.691  -30.868 1.00 51.87 ?  302 SER B CA    1 
ATOM   6823 C C     . SER C 1 310 ? -5.820  -7.154  -30.889 1.00 52.31 ?  302 SER B C     1 
ATOM   6824 O O     . SER C 1 310 ? -6.516  -7.571  -31.820 1.00 57.17 ?  302 SER B O     1 
ATOM   6825 C CB    . SER C 1 310 ? -4.561  -5.371  -32.112 1.00 50.55 ?  302 SER B CB    1 
ATOM   6826 O OG    . SER C 1 310 ? -4.492  -3.971  -32.328 1.00 57.48 ?  302 SER B OG    1 
ATOM   6827 N N     . THR C 1 311 ? -5.420  -7.934  -29.893 1.00 47.48 ?  303 THR B N     1 
ATOM   6828 C CA    . THR C 1 311 ? -5.830  -9.324  -29.749 1.00 46.57 ?  303 THR B CA    1 
ATOM   6829 C C     . THR C 1 311 ? -7.071  -9.408  -28.870 1.00 53.08 ?  303 THR B C     1 
ATOM   6830 O O     . THR C 1 311 ? -7.462  -8.428  -28.231 1.00 49.33 ?  303 THR B O     1 
ATOM   6831 C CB    . THR C 1 311 ? -4.672  -10.138 -29.169 1.00 49.31 ?  303 THR B CB    1 
ATOM   6832 O OG1   . THR C 1 311 ? -4.658  -10.012 -27.740 1.00 47.72 ?  303 THR B OG1   1 
ATOM   6833 C CG2   . THR C 1 311 ? -3.342  -9.657  -29.740 1.00 45.54 ?  303 THR B CG2   1 
ATOM   6834 N N     . PRO C 1 312 ? -7.743  -10.566 -28.827 1.00 51.17 ?  304 PRO B N     1 
ATOM   6835 C CA    . PRO C 1 312 ? -8.925  -10.692 -27.952 1.00 53.61 ?  304 PRO B CA    1 
ATOM   6836 C C     . PRO C 1 312 ? -8.632  -10.511 -26.467 1.00 51.48 ?  304 PRO B C     1 
ATOM   6837 O O     . PRO C 1 312 ? -9.584  -10.468 -25.676 1.00 50.30 ?  304 PRO B O     1 
ATOM   6838 C CB    . PRO C 1 312 ? -9.443  -12.110 -28.234 1.00 48.87 ?  304 PRO B CB    1 
ATOM   6839 C CG    . PRO C 1 312 ? -8.793  -12.554 -29.479 1.00 50.76 ?  304 PRO B CG    1 
ATOM   6840 C CD    . PRO C 1 312 ? -7.586  -11.717 -29.736 1.00 47.33 ?  304 PRO B CD    1 
ATOM   6841 N N     . LEU C 1 313 ? -7.361  -10.397 -26.069 1.00 49.80 ?  305 LEU B N     1 
ATOM   6842 C CA    . LEU C 1 313 ? -7.021  -10.307 -24.651 1.00 48.26 ?  305 LEU B CA    1 
ATOM   6843 C C     . LEU C 1 313 ? -7.633  -9.074  -23.997 1.00 45.59 ?  305 LEU B C     1 
ATOM   6844 O O     . LEU C 1 313 ? -8.117  -9.144  -22.861 1.00 46.03 ?  305 LEU B O     1 
ATOM   6845 C CB    . LEU C 1 313 ? -5.501  -10.297 -24.476 1.00 49.12 ?  305 LEU B CB    1 
ATOM   6846 C CG    . LEU C 1 313 ? -5.020  -10.191 -23.028 1.00 40.90 ?  305 LEU B CG    1 
ATOM   6847 C CD1   . LEU C 1 313 ? -5.602  -11.319 -22.186 1.00 45.07 ?  305 LEU B CD1   1 
ATOM   6848 C CD2   . LEU C 1 313 ? -3.499  -10.168 -22.938 1.00 37.34 ?  305 LEU B CD2   1 
ATOM   6849 N N     . TYR C 1 314 ? -7.620  -7.932  -24.690 1.00 44.97 ?  306 TYR B N     1 
ATOM   6850 C CA    . TYR C 1 314 ? -8.083  -6.687  -24.088 1.00 48.00 ?  306 TYR B CA    1 
ATOM   6851 C C     . TYR C 1 314 ? -9.098  -5.956  -24.960 1.00 49.88 ?  306 TYR B C     1 
ATOM   6852 O O     . TYR C 1 314 ? -9.240  -4.735  -24.842 1.00 47.10 ?  306 TYR B O     1 
ATOM   6853 C CB    . TYR C 1 314 ? -6.896  -5.777  -23.768 1.00 40.98 ?  306 TYR B CB    1 
ATOM   6854 C CG    . TYR C 1 314 ? -6.019  -6.329  -22.670 1.00 41.25 ?  306 TYR B CG    1 
ATOM   6855 C CD1   . TYR C 1 314 ? -6.567  -6.748  -21.463 1.00 42.85 ?  306 TYR B CD1   1 
ATOM   6856 C CD2   . TYR C 1 314 ? -4.648  -6.448  -22.843 1.00 40.11 ?  306 TYR B CD2   1 
ATOM   6857 C CE1   . TYR C 1 314 ? -5.771  -7.262  -20.456 1.00 37.33 ?  306 TYR B CE1   1 
ATOM   6858 C CE2   . TYR C 1 314 ? -3.844  -6.957  -21.841 1.00 36.01 ?  306 TYR B CE2   1 
ATOM   6859 C CZ    . TYR C 1 314 ? -4.410  -7.366  -20.651 1.00 37.57 ?  306 TYR B CZ    1 
ATOM   6860 O OH    . TYR C 1 314 ? -3.610  -7.875  -19.653 1.00 37.24 ?  306 TYR B OH    1 
ATOM   6861 N N     . SER C 1 315 ? -9.816  -6.673  -25.818 1.00 52.75 ?  307 SER B N     1 
ATOM   6862 C CA    . SER C 1 315 ? -10.882 -6.069  -26.610 1.00 58.01 ?  307 SER B CA    1 
ATOM   6863 C C     . SER C 1 315 ? -12.115 -5.805  -25.751 1.00 56.02 ?  307 SER B C     1 
ATOM   6864 O O     . SER C 1 315 ? -12.637 -6.712  -25.101 1.00 61.00 ?  307 SER B O     1 
ATOM   6865 C CB    . SER C 1 315 ? -11.249 -6.966  -27.791 1.00 53.62 ?  307 SER B CB    1 
ATOM   6866 O OG    . SER C 1 315 ? -12.633 -6.873  -28.086 1.00 68.96 ?  307 SER B OG    1 
ATOM   6867 N N     . MET D 1 9   ? 21.893  -8.353  -10.425 1.00 49.73 ?  1   MET C N     1 
ATOM   6868 C CA    . MET D 1 9   ? 21.452  -7.491  -9.336  1.00 56.61 ?  1   MET C CA    1 
ATOM   6869 C C     . MET D 1 9   ? 20.102  -6.861  -9.668  1.00 49.50 ?  1   MET C C     1 
ATOM   6870 O O     . MET D 1 9   ? 19.922  -6.291  -10.744 1.00 50.78 ?  1   MET C O     1 
ATOM   6871 C CB    . MET D 1 9   ? 22.495  -6.407  -9.051  1.00 54.86 ?  1   MET C CB    1 
ATOM   6872 C CG    . MET D 1 9   ? 22.089  -5.413  -7.976  1.00 57.97 ?  1   MET C CG    1 
ATOM   6873 S SD    . MET D 1 9   ? 22.961  -5.695  -6.422  1.00 78.06 ?  1   MET C SD    1 
ATOM   6874 C CE    . MET D 1 9   ? 24.148  -4.354  -6.444  1.00 70.30 ?  1   MET C CE    1 
ATOM   6875 N N     . ALA D 1 10  ? 19.156  -6.972  -8.739  1.00 47.02 ?  2   ALA C N     1 
ATOM   6876 C CA    . ALA D 1 10  ? 17.812  -6.456  -8.951  1.00 44.31 ?  2   ALA C CA    1 
ATOM   6877 C C     . ALA D 1 10  ? 17.198  -6.086  -7.610  1.00 42.78 ?  2   ALA C C     1 
ATOM   6878 O O     . ALA D 1 10  ? 17.599  -6.590  -6.558  1.00 48.01 ?  2   ALA C O     1 
ATOM   6879 C CB    . ALA D 1 10  ? 16.927  -7.473  -9.683  1.00 37.74 ?  2   ALA C CB    1 
ATOM   6880 N N     . GLN D 1 11  ? 16.205  -5.201  -7.666  1.00 43.17 ?  3   GLN C N     1 
ATOM   6881 C CA    . GLN D 1 11  ? 15.556  -4.714  -6.458  1.00 42.85 ?  3   GLN C CA    1 
ATOM   6882 C C     . GLN D 1 11  ? 14.773  -5.827  -5.770  1.00 38.46 ?  3   GLN C C     1 
ATOM   6883 O O     . GLN D 1 11  ? 14.234  -6.731  -6.414  1.00 36.65 ?  3   GLN C O     1 
ATOM   6884 C CB    . GLN D 1 11  ? 14.620  -3.550  -6.787  1.00 40.00 ?  3   GLN C CB    1 
ATOM   6885 C CG    . GLN D 1 11  ? 14.011  -3.607  -8.181  1.00 52.65 ?  3   GLN C CG    1 
ATOM   6886 C CD    . GLN D 1 11  ? 13.434  -2.272  -8.620  1.00 53.01 ?  3   GLN C CD    1 
ATOM   6887 O OE1   . GLN D 1 11  ? 12.779  -1.582  -7.838  1.00 53.67 ?  3   GLN C OE1   1 
ATOM   6888 N NE2   . GLN D 1 11  ? 13.672  -1.903  -9.875  1.00 40.04 ?  3   GLN C NE2   1 
ATOM   6889 N N     . LYS D 1 12  ? 14.713  -5.744  -4.439  1.00 33.78 ?  4   LYS C N     1 
ATOM   6890 C CA    . LYS D 1 12  ? 13.962  -6.701  -3.645  1.00 38.89 ?  4   LYS C CA    1 
ATOM   6891 C C     . LYS D 1 12  ? 12.472  -6.610  -3.979  1.00 37.22 ?  4   LYS C C     1 
ATOM   6892 O O     . LYS D 1 12  ? 12.005  -5.598  -4.507  1.00 38.55 ?  4   LYS C O     1 
ATOM   6893 C CB    . LYS D 1 12  ? 14.197  -6.446  -2.155  1.00 43.73 ?  4   LYS C CB    1 
ATOM   6894 C CG    . LYS D 1 12  ? 15.622  -6.724  -1.692  1.00 43.66 ?  4   LYS C CG    1 
ATOM   6895 C CD    . LYS D 1 12  ? 15.859  -8.210  -1.478  1.00 43.18 ?  4   LYS C CD    1 
ATOM   6896 C CE    . LYS D 1 12  ? 16.600  -8.470  -0.177  1.00 46.29 ?  4   LYS C CE    1 
ATOM   6897 N NZ    . LYS D 1 12  ? 18.073  -8.555  -0.380  1.00 51.03 ?  4   LYS C NZ    1 
ATOM   6898 N N     . PRO D 1 13  ? 11.706  -7.664  -3.689  1.00 33.15 ?  5   PRO C N     1 
ATOM   6899 C CA    . PRO D 1 13  ? 10.285  -7.661  -4.055  1.00 34.68 ?  5   PRO C CA    1 
ATOM   6900 C C     . PRO D 1 13  ? 9.518   -6.556  -3.345  1.00 32.48 ?  5   PRO C C     1 
ATOM   6901 O O     . PRO D 1 13  ? 9.745   -6.267  -2.168  1.00 37.21 ?  5   PRO C O     1 
ATOM   6902 C CB    . PRO D 1 13  ? 9.802   -9.048  -3.614  1.00 32.79 ?  5   PRO C CB    1 
ATOM   6903 C CG    . PRO D 1 13  ? 11.033  -9.885  -3.586  1.00 34.84 ?  5   PRO C CG    1 
ATOM   6904 C CD    . PRO D 1 13  ? 12.120  -8.963  -3.134  1.00 35.16 ?  5   PRO C CD    1 
ATOM   6905 N N     . VAL D 1 14  ? 8.605   -5.934  -4.082  1.00 33.47 ?  6   VAL C N     1 
ATOM   6906 C CA    . VAL D 1 14  ? 7.702   -4.935  -3.532  1.00 32.45 ?  6   VAL C CA    1 
ATOM   6907 C C     . VAL D 1 14  ? 6.303   -5.533  -3.470  1.00 33.05 ?  6   VAL C C     1 
ATOM   6908 O O     . VAL D 1 14  ? 5.987   -6.527  -4.132  1.00 32.30 ?  6   VAL C O     1 
ATOM   6909 C CB    . VAL D 1 14  ? 7.709   -3.629  -4.353  1.00 32.88 ?  6   VAL C CB    1 
ATOM   6910 C CG1   . VAL D 1 14  ? 9.091   -2.993  -4.325  1.00 26.36 ?  6   VAL C CG1   1 
ATOM   6911 C CG2   . VAL D 1 14  ? 7.267   -3.898  -5.782  1.00 28.16 ?  6   VAL C CG2   1 
ATOM   6912 N N     . ASP D 1 15  ? 5.454   -4.916  -2.655  1.00 32.75 ?  7   ASP C N     1 
ATOM   6913 C CA    . ASP D 1 15  ? 4.096   -5.405  -2.474  1.00 33.53 ?  7   ASP C CA    1 
ATOM   6914 C C     . ASP D 1 15  ? 3.091   -4.744  -3.409  1.00 32.36 ?  7   ASP C C     1 
ATOM   6915 O O     . ASP D 1 15  ? 1.948   -5.204  -3.486  1.00 31.34 ?  7   ASP C O     1 
ATOM   6916 C CB    . ASP D 1 15  ? 3.650   -5.207  -1.022  1.00 31.21 ?  7   ASP C CB    1 
ATOM   6917 C CG    . ASP D 1 15  ? 4.387   -6.114  -0.051  1.00 34.16 ?  7   ASP C CG    1 
ATOM   6918 O OD1   . ASP D 1 15  ? 5.478   -6.617  -0.397  1.00 44.01 ?  7   ASP C OD1   1 
ATOM   6919 O OD2   . ASP D 1 15  ? 3.867   -6.328  1.062   1.00 41.46 ?  7   ASP C OD2   1 
ATOM   6920 N N     . ASN D 1 16  ? 3.480   -3.689  -4.120  1.00 32.67 ?  8   ASN C N     1 
ATOM   6921 C CA    . ASN D 1 16  ? 2.566   -3.002  -5.019  1.00 30.01 ?  8   ASN C CA    1 
ATOM   6922 C C     . ASN D 1 16  ? 3.352   -2.496  -6.219  1.00 31.02 ?  8   ASN C C     1 
ATOM   6923 O O     . ASN D 1 16  ? 4.505   -2.076  -6.080  1.00 32.88 ?  8   ASN C O     1 
ATOM   6924 C CB    . ASN D 1 16  ? 1.854   -1.844  -4.310  1.00 36.01 ?  8   ASN C CB    1 
ATOM   6925 C CG    . ASN D 1 16  ? 0.683   -1.299  -5.107  1.00 33.03 ?  8   ASN C CG    1 
ATOM   6926 O OD1   . ASN D 1 16  ? 0.855   -0.755  -6.197  1.00 37.77 ?  8   ASN C OD1   1 
ATOM   6927 N ND2   . ASN D 1 16  ? -0.518  -1.441  -4.561  1.00 38.23 ?  8   ASN C ND2   1 
ATOM   6928 N N     . ILE D 1 17  ? 2.715   -2.536  -7.393  1.00 30.39 ?  9   ILE C N     1 
ATOM   6929 C CA    . ILE D 1 17  ? 3.392   -2.158  -8.632  1.00 32.72 ?  9   ILE C CA    1 
ATOM   6930 C C     . ILE D 1 17  ? 3.824   -0.697  -8.604  1.00 32.75 ?  9   ILE C C     1 
ATOM   6931 O O     . ILE D 1 17  ? 4.811   -0.321  -9.250  1.00 36.63 ?  9   ILE C O     1 
ATOM   6932 C CB    . ILE D 1 17  ? 2.483   -2.468  -9.840  1.00 32.09 ?  9   ILE C CB    1 
ATOM   6933 C CG1   . ILE D 1 17  ? 3.166   -2.097  -11.155 1.00 32.31 ?  9   ILE C CG1   1 
ATOM   6934 C CG2   . ILE D 1 17  ? 1.161   -1.747  -9.715  1.00 31.30 ?  9   ILE C CG2   1 
ATOM   6935 C CD1   . ILE D 1 17  ? 4.306   -2.993  -11.512 1.00 26.49 ?  9   ILE C CD1   1 
ATOM   6936 N N     . THR D 1 18  ? 3.120   0.145   -7.843  1.00 30.93 ?  10  THR C N     1 
ATOM   6937 C CA    . THR D 1 18  ? 3.474   1.558   -7.774  1.00 29.24 ?  10  THR C CA    1 
ATOM   6938 C C     . THR D 1 18  ? 4.847   1.790   -7.157  1.00 31.65 ?  10  THR C C     1 
ATOM   6939 O O     . THR D 1 18  ? 5.435   2.856   -7.368  1.00 28.66 ?  10  THR C O     1 
ATOM   6940 C CB    . THR D 1 18  ? 2.420   2.333   -6.978  1.00 34.13 ?  10  THR C CB    1 
ATOM   6941 O OG1   . THR D 1 18  ? 2.404   1.870   -5.619  1.00 40.21 ?  10  THR C OG1   1 
ATOM   6942 C CG2   . THR D 1 18  ? 1.045   2.147   -7.591  1.00 33.55 ?  10  THR C CG2   1 
ATOM   6943 N N     . GLN D 1 19  ? 5.378   0.819   -6.414  1.00 35.47 ?  11  GLN C N     1 
ATOM   6944 C CA    . GLN D 1 19  ? 6.635   1.012   -5.704  1.00 36.44 ?  11  GLN C CA    1 
ATOM   6945 C C     . GLN D 1 19  ? 7.859   0.954   -6.611  1.00 35.46 ?  11  GLN C C     1 
ATOM   6946 O O     . GLN D 1 19  ? 8.957   1.296   -6.160  1.00 39.22 ?  11  GLN C O     1 
ATOM   6947 C CB    . GLN D 1 19  ? 6.771   -0.026  -4.588  1.00 35.20 ?  11  GLN C CB    1 
ATOM   6948 C CG    . GLN D 1 19  ? 5.764   0.153   -3.461  1.00 29.40 ?  11  GLN C CG    1 
ATOM   6949 C CD    . GLN D 1 19  ? 5.769   1.560   -2.893  1.00 32.59 ?  11  GLN C CD    1 
ATOM   6950 O OE1   . GLN D 1 19  ? 4.847   2.341   -3.130  1.00 38.75 ?  11  GLN C OE1   1 
ATOM   6951 N NE2   . GLN D 1 19  ? 6.809   1.890   -2.138  1.00 32.20 ?  11  GLN C NE2   1 
ATOM   6952 N N     . ILE D 1 20  ? 7.710   0.537   -7.866  1.00 34.56 ?  12  ILE C N     1 
ATOM   6953 C CA    . ILE D 1 20  ? 8.818   0.539   -8.811  1.00 35.81 ?  12  ILE C CA    1 
ATOM   6954 C C     . ILE D 1 20  ? 8.690   1.669   -9.825  1.00 32.81 ?  12  ILE C C     1 
ATOM   6955 O O     . ILE D 1 20  ? 9.415   1.689   -10.825 1.00 29.96 ?  12  ILE C O     1 
ATOM   6956 C CB    . ILE D 1 20  ? 8.964   -0.824  -9.508  1.00 38.94 ?  12  ILE C CB    1 
ATOM   6957 C CG1   . ILE D 1 20  ? 7.761   -1.107  -10.402 1.00 33.48 ?  12  ILE C CG1   1 
ATOM   6958 C CG2   . ILE D 1 20  ? 9.134   -1.932  -8.477  1.00 36.34 ?  12  ILE C CG2   1 
ATOM   6959 C CD1   . ILE D 1 20  ? 8.125   -1.822  -11.678 1.00 41.32 ?  12  ILE C CD1   1 
ATOM   6960 N N     . ILE D 1 21  ? 7.784   2.617   -9.586  1.00 29.06 ?  13  ILE C N     1 
ATOM   6961 C CA    . ILE D 1 21  ? 7.738   3.835   -10.382 1.00 31.91 ?  13  ILE C CA    1 
ATOM   6962 C C     . ILE D 1 21  ? 8.985   4.662   -10.105 1.00 33.72 ?  13  ILE C C     1 
ATOM   6963 O O     . ILE D 1 21  ? 9.399   4.830   -8.950  1.00 33.25 ?  13  ILE C O     1 
ATOM   6964 C CB    . ILE D 1 21  ? 6.461   4.635   -10.069 1.00 30.24 ?  13  ILE C CB    1 
ATOM   6965 C CG1   . ILE D 1 21  ? 5.223   3.901   -10.587 1.00 29.25 ?  13  ILE C CG1   1 
ATOM   6966 C CG2   . ILE D 1 21  ? 6.532   6.034   -10.664 1.00 32.80 ?  13  ILE C CG2   1 
ATOM   6967 C CD1   . ILE D 1 21  ? 3.924   4.596   -10.245 1.00 28.06 ?  13  ILE C CD1   1 
ATOM   6968 N N     . GLY D 1 22  ? 9.598   5.174   -11.165 1.00 27.86 ?  14  GLY C N     1 
ATOM   6969 C CA    . GLY D 1 22  ? 10.776  6.002   -11.019 1.00 32.87 ?  14  GLY C CA    1 
ATOM   6970 C C     . GLY D 1 22  ? 12.062  5.208   -11.096 1.00 32.95 ?  14  GLY C C     1 
ATOM   6971 O O     . GLY D 1 22  ? 12.097  4.030   -11.467 1.00 28.74 ?  14  GLY C O     1 
ATOM   6972 N N     . GLY D 1 23  ? 13.148  5.884   -10.725 1.00 31.51 ?  15  GLY C N     1 
ATOM   6973 C CA    . GLY D 1 23  ? 14.472  5.296   -10.781 1.00 32.35 ?  15  GLY C CA    1 
ATOM   6974 C C     . GLY D 1 23  ? 14.851  4.877   -12.185 1.00 30.90 ?  15  GLY C C     1 
ATOM   6975 O O     . GLY D 1 23  ? 15.360  3.773   -12.394 1.00 32.12 ?  15  GLY C O     1 
ATOM   6976 N N     . THR D 1 24  ? 14.608  5.762   -13.159 1.00 26.11 ?  16  THR C N     1 
ATOM   6977 C CA    . THR D 1 24  ? 14.742  5.418   -14.566 1.00 26.19 ?  16  THR C CA    1 
ATOM   6978 C C     . THR D 1 24  ? 16.192  5.558   -15.033 1.00 33.72 ?  16  THR C C     1 
ATOM   6979 O O     . THR D 1 24  ? 16.930  6.419   -14.546 1.00 27.40 ?  16  THR C O     1 
ATOM   6980 C CB    . THR D 1 24  ? 13.831  6.302   -15.415 1.00 30.15 ?  16  THR C CB    1 
ATOM   6981 O OG1   . THR D 1 24  ? 13.991  7.673   -15.031 1.00 27.00 ?  16  THR C OG1   1 
ATOM   6982 C CG2   . THR D 1 24  ? 12.371  5.894   -15.225 1.00 27.22 ?  16  THR C CG2   1 
ATOM   6983 N N     . PRO D 1 25  ? 16.623  4.718   -15.971 1.00 29.66 ?  17  PRO C N     1 
ATOM   6984 C CA    . PRO D 1 25  ? 18.024  4.731   -16.401 1.00 26.82 ?  17  PRO C CA    1 
ATOM   6985 C C     . PRO D 1 25  ? 18.315  5.862   -17.380 1.00 28.95 ?  17  PRO C C     1 
ATOM   6986 O O     . PRO D 1 25  ? 17.420  6.516   -17.915 1.00 30.30 ?  17  PRO C O     1 
ATOM   6987 C CB    . PRO D 1 25  ? 18.192  3.367   -17.076 1.00 31.09 ?  17  PRO C CB    1 
ATOM   6988 C CG    . PRO D 1 25  ? 16.835  3.081   -17.630 1.00 33.69 ?  17  PRO C CG    1 
ATOM   6989 C CD    . PRO D 1 25  ? 15.862  3.629   -16.614 1.00 27.00 ?  17  PRO C CD    1 
ATOM   6990 N N     . VAL D 1 26  ? 19.610  6.071   -17.612 1.00 27.01 ?  18  VAL C N     1 
ATOM   6991 C CA    . VAL D 1 26  ? 20.108  7.090   -18.526 1.00 29.69 ?  18  VAL C CA    1 
ATOM   6992 C C     . VAL D 1 26  ? 21.040  6.429   -19.532 1.00 30.25 ?  18  VAL C C     1 
ATOM   6993 O O     . VAL D 1 26  ? 21.877  5.596   -19.165 1.00 28.20 ?  18  VAL C O     1 
ATOM   6994 C CB    . VAL D 1 26  ? 20.832  8.227   -17.772 1.00 30.00 ?  18  VAL C CB    1 
ATOM   6995 C CG1   . VAL D 1 26  ? 21.524  9.161   -18.747 1.00 29.47 ?  18  VAL C CG1   1 
ATOM   6996 C CG2   . VAL D 1 26  ? 19.845  9.001   -16.920 1.00 28.84 ?  18  VAL C CG2   1 
ATOM   6997 N N     . VAL D 1 27  ? 20.883  6.789   -20.804 1.00 26.41 ?  19  VAL C N     1 
ATOM   6998 C CA    . VAL D 1 27  ? 21.688  6.243   -21.889 1.00 24.90 ?  19  VAL C CA    1 
ATOM   6999 C C     . VAL D 1 27  ? 22.362  7.391   -22.624 1.00 30.34 ?  19  VAL C C     1 
ATOM   7000 O O     . VAL D 1 27  ? 21.739  8.427   -22.884 1.00 32.99 ?  19  VAL C O     1 
ATOM   7001 C CB    . VAL D 1 27  ? 20.837  5.396   -22.859 1.00 31.28 ?  19  VAL C CB    1 
ATOM   7002 C CG1   . VAL D 1 27  ? 21.714  4.772   -23.940 1.00 26.57 ?  19  VAL C CG1   1 
ATOM   7003 C CG2   . VAL D 1 27  ? 20.082  4.319   -22.100 1.00 29.82 ?  19  VAL C CG2   1 
ATOM   7004 N N     . LYS D 1 28  ? 23.640  7.207   -22.948 1.00 32.33 ?  20  LYS C N     1 
ATOM   7005 C CA    . LYS D 1 28  ? 24.378  8.150   -23.778 1.00 29.95 ?  20  LYS C CA    1 
ATOM   7006 C C     . LYS D 1 28  ? 24.190  7.786   -25.245 1.00 30.44 ?  20  LYS C C     1 
ATOM   7007 O O     . LYS D 1 28  ? 24.292  6.612   -25.616 1.00 28.69 ?  20  LYS C O     1 
ATOM   7008 C CB    . LYS D 1 28  ? 25.861  8.138   -23.410 1.00 31.28 ?  20  LYS C CB    1 
ATOM   7009 C CG    . LYS D 1 28  ? 26.712  9.146   -24.167 1.00 40.38 ?  20  LYS C CG    1 
ATOM   7010 C CD    . LYS D 1 28  ? 28.192  8.801   -24.067 1.00 38.56 ?  20  LYS C CD    1 
ATOM   7011 C CE    . LYS D 1 28  ? 29.030  9.691   -24.969 1.00 39.84 ?  20  LYS C CE    1 
ATOM   7012 N NZ    . LYS D 1 28  ? 30.450  9.740   -24.529 1.00 45.07 ?  20  LYS C NZ    1 
ATOM   7013 N N     . LEU D 1 29  ? 23.907  8.788   -26.073 1.00 28.95 ?  21  LEU C N     1 
ATOM   7014 C CA    . LEU D 1 29  ? 23.745  8.555   -27.499 1.00 28.71 ?  21  LEU C CA    1 
ATOM   7015 C C     . LEU D 1 29  ? 25.105  8.440   -28.177 1.00 32.72 ?  21  LEU C C     1 
ATOM   7016 O O     . LEU D 1 29  ? 26.073  9.100   -27.791 1.00 35.53 ?  21  LEU C O     1 
ATOM   7017 C CB    . LEU D 1 29  ? 22.929  9.676   -28.140 1.00 30.49 ?  21  LEU C CB    1 
ATOM   7018 C CG    . LEU D 1 29  ? 21.576  9.947   -27.483 1.00 30.91 ?  21  LEU C CG    1 
ATOM   7019 C CD1   . LEU D 1 29  ? 20.890  11.144  -28.125 1.00 25.05 ?  21  LEU C CD1   1 
ATOM   7020 C CD2   . LEU D 1 29  ? 20.694  8.710   -27.556 1.00 28.18 ?  21  LEU C CD2   1 
ATOM   7021 N N     . ARG D 1 30  ? 25.169  7.596   -29.204 1.00 35.09 ?  22  ARG C N     1 
ATOM   7022 C CA    . ARG D 1 30  ? 26.437  7.246   -29.830 1.00 38.07 ?  22  ARG C CA    1 
ATOM   7023 C C     . ARG D 1 30  ? 26.538  7.692   -31.279 1.00 37.75 ?  22  ARG C C     1 
ATOM   7024 O O     . ARG D 1 30  ? 27.555  8.277   -31.670 1.00 46.13 ?  22  ARG C O     1 
ATOM   7025 C CB    . ARG D 1 30  ? 26.658  5.727   -29.749 1.00 34.70 ?  22  ARG C CB    1 
ATOM   7026 C CG    . ARG D 1 30  ? 26.931  5.194   -28.354 1.00 35.52 ?  22  ARG C CG    1 
ATOM   7027 C CD    . ARG D 1 30  ? 26.908  3.668   -28.339 1.00 39.27 ?  22  ARG C CD    1 
ATOM   7028 N NE    . ARG D 1 30  ? 25.551  3.135   -28.406 1.00 30.53 ?  22  ARG C NE    1 
ATOM   7029 C CZ    . ARG D 1 30  ? 24.968  2.694   -29.513 1.00 37.32 ?  22  ARG C CZ    1 
ATOM   7030 N NH1   . ARG D 1 30  ? 25.603  2.689   -30.674 1.00 42.55 ?  22  ARG C NH1   1 
ATOM   7031 N NH2   . ARG D 1 30  ? 23.717  2.248   -29.454 1.00 36.95 ?  22  ARG C NH2   1 
ATOM   7032 N N     . ASN D 1 31  ? 25.512  7.430   -32.094 1.00 39.54 ?  23  ASN C N     1 
ATOM   7033 C CA    . ASN D 1 31  ? 25.640  7.534   -33.541 1.00 36.42 ?  23  ASN C CA    1 
ATOM   7034 C C     . ASN D 1 31  ? 24.936  8.732   -34.162 1.00 37.10 ?  23  ASN C C     1 
ATOM   7035 O O     . ASN D 1 31  ? 25.314  9.138   -35.265 1.00 36.93 ?  23  ASN C O     1 
ATOM   7036 C CB    . ASN D 1 31  ? 25.109  6.256   -34.210 1.00 40.59 ?  23  ASN C CB    1 
ATOM   7037 C CG    . ASN D 1 31  ? 25.825  5.009   -33.731 1.00 39.49 ?  23  ASN C CG    1 
ATOM   7038 O OD1   . ASN D 1 31  ? 25.215  4.121   -33.135 1.00 41.57 ?  23  ASN C OD1   1 
ATOM   7039 N ND2   . ASN D 1 31  ? 27.126  4.938   -33.982 1.00 39.86 ?  23  ASN C ND2   1 
ATOM   7040 N N     . VAL D 1 32  ? 23.928  9.303   -33.502 1.00 39.07 ?  24  VAL C N     1 
ATOM   7041 C CA    . VAL D 1 32  ? 23.187  10.431  -34.058 1.00 34.23 ?  24  VAL C CA    1 
ATOM   7042 C C     . VAL D 1 32  ? 23.718  11.770  -33.557 1.00 40.91 ?  24  VAL C C     1 
ATOM   7043 O O     . VAL D 1 32  ? 23.146  12.817  -33.876 1.00 35.68 ?  24  VAL C O     1 
ATOM   7044 C CB    . VAL D 1 32  ? 21.682  10.300  -33.774 1.00 34.23 ?  24  VAL C CB    1 
ATOM   7045 C CG1   . VAL D 1 32  ? 21.183  8.927   -34.196 1.00 37.99 ?  24  VAL C CG1   1 
ATOM   7046 C CG2   . VAL D 1 32  ? 21.400  10.543  -32.301 1.00 34.92 ?  24  VAL C CG2   1 
ATOM   7047 N N     . VAL D 1 33  ? 24.802  11.764  -32.784 1.00 40.22 ?  25  VAL C N     1 
ATOM   7048 C CA    . VAL D 1 33  ? 25.414  12.981  -32.259 1.00 47.67 ?  25  VAL C CA    1 
ATOM   7049 C C     . VAL D 1 33  ? 26.764  13.166  -32.937 1.00 46.34 ?  25  VAL C C     1 
ATOM   7050 O O     . VAL D 1 33  ? 27.610  12.263  -32.909 1.00 48.89 ?  25  VAL C O     1 
ATOM   7051 C CB    . VAL D 1 33  ? 25.570  12.930  -30.732 1.00 45.14 ?  25  VAL C CB    1 
ATOM   7052 C CG1   . VAL D 1 33  ? 26.050  14.276  -30.210 1.00 44.70 ?  25  VAL C CG1   1 
ATOM   7053 C CG2   . VAL D 1 33  ? 24.256  12.539  -30.077 1.00 42.10 ?  25  VAL C CG2   1 
ATOM   7054 N N     . ASP D 1 34  ? 26.963  14.337  -33.538 1.00 51.42 ?  26  ASP C N     1 
ATOM   7055 C CA    . ASP D 1 34  ? 28.216  14.639  -34.215 1.00 53.07 ?  26  ASP C CA    1 
ATOM   7056 C C     . ASP D 1 34  ? 29.376  14.600  -33.223 1.00 53.09 ?  26  ASP C C     1 
ATOM   7057 O O     . ASP D 1 34  ? 29.222  14.916  -32.040 1.00 57.20 ?  26  ASP C O     1 
ATOM   7058 C CB    . ASP D 1 34  ? 28.114  16.007  -34.898 1.00 52.52 ?  26  ASP C CB    1 
ATOM   7059 C CG    . ASP D 1 34  ? 29.449  16.524  -35.391 1.00 60.15 ?  26  ASP C CG    1 
ATOM   7060 O OD1   . ASP D 1 34  ? 30.227  17.047  -34.570 1.00 58.21 ?  26  ASP C OD1   1 
ATOM   7061 O OD2   . ASP D 1 34  ? 29.721  16.406  -36.604 1.00 65.98 ?  26  ASP C OD2   1 
ATOM   7062 N N     . ASP D 1 35  ? 30.550  14.196  -33.718 1.00 55.16 ?  27  ASP C N     1 
ATOM   7063 C CA    . ASP D 1 35  ? 31.707  13.995  -32.850 1.00 54.19 ?  27  ASP C CA    1 
ATOM   7064 C C     . ASP D 1 35  ? 32.228  15.293  -32.242 1.00 50.17 ?  27  ASP C C     1 
ATOM   7065 O O     . ASP D 1 35  ? 32.944  15.244  -31.236 1.00 51.11 ?  27  ASP C O     1 
ATOM   7066 C CB    . ASP D 1 35  ? 32.828  13.301  -33.625 1.00 54.20 ?  27  ASP C CB    1 
ATOM   7067 N N     . ASN D 1 36  ? 31.896  16.445  -32.819 1.00 48.40 ?  28  ASN C N     1 
ATOM   7068 C CA    . ASN D 1 36  ? 32.316  17.728  -32.270 1.00 49.66 ?  28  ASN C CA    1 
ATOM   7069 C C     . ASN D 1 36  ? 31.301  18.316  -31.301 1.00 51.32 ?  28  ASN C C     1 
ATOM   7070 O O     . ASN D 1 36  ? 31.556  19.381  -30.729 1.00 49.46 ?  28  ASN C O     1 
ATOM   7071 C CB    . ASN D 1 36  ? 32.579  18.730  -33.398 1.00 47.67 ?  28  ASN C CB    1 
ATOM   7072 C CG    . ASN D 1 36  ? 33.282  18.101  -34.580 1.00 49.17 ?  28  ASN C CG    1 
ATOM   7073 O OD1   . ASN D 1 36  ? 34.371  17.543  -34.444 1.00 53.73 ?  28  ASN C OD1   1 
ATOM   7074 N ND2   . ASN D 1 36  ? 32.661  18.185  -35.750 1.00 58.58 ?  28  ASN C ND2   1 
ATOM   7075 N N     . ALA D 1 37  ? 30.164  17.657  -31.109 1.00 45.83 ?  29  ALA C N     1 
ATOM   7076 C CA    . ALA D 1 37  ? 29.133  18.139  -30.206 1.00 42.91 ?  29  ALA C CA    1 
ATOM   7077 C C     . ALA D 1 37  ? 29.332  17.564  -28.808 1.00 40.94 ?  29  ALA C C     1 
ATOM   7078 O O     . ALA D 1 37  ? 30.061  16.590  -28.605 1.00 39.22 ?  29  ALA C O     1 
ATOM   7079 C CB    . ALA D 1 37  ? 27.743  17.773  -30.730 1.00 43.05 ?  29  ALA C CB    1 
ATOM   7080 N N     . ALA D 1 38  ? 28.670  18.187  -27.838 1.00 39.57 ?  30  ALA C N     1 
ATOM   7081 C CA    . ALA D 1 38  ? 28.718  17.703  -26.469 1.00 41.96 ?  30  ALA C CA    1 
ATOM   7082 C C     . ALA D 1 38  ? 28.034  16.345  -26.359 1.00 37.79 ?  30  ALA C C     1 
ATOM   7083 O O     . ALA D 1 38  ? 27.244  15.943  -27.218 1.00 38.82 ?  30  ALA C O     1 
ATOM   7084 C CB    . ALA D 1 38  ? 28.051  18.703  -25.523 1.00 39.11 ?  30  ALA C CB    1 
ATOM   7085 N N     . ASP D 1 39  ? 28.355  15.628  -25.286 1.00 32.45 ?  31  ASP C N     1 
ATOM   7086 C CA    . ASP D 1 39  ? 27.669  14.375  -25.011 1.00 34.21 ?  31  ASP C CA    1 
ATOM   7087 C C     . ASP D 1 39  ? 26.193  14.640  -24.745 1.00 37.94 ?  31  ASP C C     1 
ATOM   7088 O O     . ASP D 1 39  ? 25.828  15.628  -24.102 1.00 38.03 ?  31  ASP C O     1 
ATOM   7089 C CB    . ASP D 1 39  ? 28.305  13.666  -23.813 1.00 33.67 ?  31  ASP C CB    1 
ATOM   7090 C CG    . ASP D 1 39  ? 29.733  13.229  -24.083 1.00 41.57 ?  31  ASP C CG    1 
ATOM   7091 O OD1   . ASP D 1 39  ? 30.076  13.006  -25.264 1.00 40.53 ?  31  ASP C OD1   1 
ATOM   7092 O OD2   . ASP D 1 39  ? 30.511  13.103  -23.114 1.00 35.02 ?  31  ASP C OD2   1 
ATOM   7093 N N     . VAL D 1 40  ? 25.339  13.760  -25.260 1.00 34.49 ?  32  VAL C N     1 
ATOM   7094 C CA    . VAL D 1 40  ? 23.899  13.846  -25.048 1.00 33.05 ?  32  VAL C CA    1 
ATOM   7095 C C     . VAL D 1 40  ? 23.457  12.590  -24.312 1.00 31.24 ?  32  VAL C C     1 
ATOM   7096 O O     . VAL D 1 40  ? 23.668  11.471  -24.797 1.00 33.46 ?  32  VAL C O     1 
ATOM   7097 C CB    . VAL D 1 40  ? 23.128  14.007  -26.367 1.00 37.33 ?  32  VAL C CB    1 
ATOM   7098 C CG1   . VAL D 1 40  ? 21.636  14.104  -26.091 1.00 36.76 ?  32  VAL C CG1   1 
ATOM   7099 C CG2   . VAL D 1 40  ? 23.614  15.233  -27.120 1.00 36.61 ?  32  VAL C CG2   1 
ATOM   7100 N N     . TYR D 1 41  ? 22.851  12.775  -23.145 1.00 33.21 ?  33  TYR C N     1 
ATOM   7101 C CA    . TYR D 1 41  ? 22.314  11.689  -22.344 1.00 34.65 ?  33  TYR C CA    1 
ATOM   7102 C C     . TYR D 1 41  ? 20.794  11.783  -22.320 1.00 33.08 ?  33  TYR C C     1 
ATOM   7103 O O     . TYR D 1 41  ? 20.225  12.877  -22.305 1.00 31.82 ?  33  TYR C O     1 
ATOM   7104 C CB    . TYR D 1 41  ? 22.864  11.737  -20.916 1.00 30.55 ?  33  TYR C CB    1 
ATOM   7105 C CG    . TYR D 1 41  ? 24.357  11.519  -20.826 1.00 35.44 ?  33  TYR C CG    1 
ATOM   7106 C CD1   . TYR D 1 41  ? 25.243  12.576  -20.989 1.00 35.06 ?  33  TYR C CD1   1 
ATOM   7107 C CD2   . TYR D 1 41  ? 24.881  10.259  -20.568 1.00 32.69 ?  33  TYR C CD2   1 
ATOM   7108 C CE1   . TYR D 1 41  ? 26.609  12.384  -20.905 1.00 39.38 ?  33  TYR C CE1   1 
ATOM   7109 C CE2   . TYR D 1 41  ? 26.247  10.057  -20.481 1.00 33.47 ?  33  TYR C CE2   1 
ATOM   7110 C CZ    . TYR D 1 41  ? 27.106  11.123  -20.651 1.00 37.72 ?  33  TYR C CZ    1 
ATOM   7111 O OH    . TYR D 1 41  ? 28.466  10.930  -20.566 1.00 46.10 ?  33  TYR C OH    1 
ATOM   7112 N N     . VAL D 1 42  ? 20.136  10.626  -22.322 1.00 32.25 ?  34  VAL C N     1 
ATOM   7113 C CA    . VAL D 1 42  ? 18.679  10.554  -22.348 1.00 30.97 ?  34  VAL C CA    1 
ATOM   7114 C C     . VAL D 1 42  ? 18.200  9.713   -21.170 1.00 27.80 ?  34  VAL C C     1 
ATOM   7115 O O     . VAL D 1 42  ? 18.709  8.611   -20.935 1.00 30.37 ?  34  VAL C O     1 
ATOM   7116 C CB    . VAL D 1 42  ? 18.150  9.988   -23.683 1.00 30.54 ?  34  VAL C CB    1 
ATOM   7117 C CG1   . VAL D 1 42  ? 18.460  10.949  -24.817 1.00 32.21 ?  34  VAL C CG1   1 
ATOM   7118 C CG2   . VAL D 1 42  ? 18.750  8.620   -23.982 1.00 28.84 ?  34  VAL C CG2   1 
ATOM   7119 N N     . LYS D 1 43  ? 17.238  10.246  -20.420 1.00 30.58 ?  35  LYS C N     1 
ATOM   7120 C CA    . LYS D 1 43  ? 16.613  9.533   -19.313 1.00 31.24 ?  35  LYS C CA    1 
ATOM   7121 C C     . LYS D 1 43  ? 15.336  8.876   -19.821 1.00 29.79 ?  35  LYS C C     1 
ATOM   7122 O O     . LYS D 1 43  ? 14.426  9.564   -20.298 1.00 30.13 ?  35  LYS C O     1 
ATOM   7123 C CB    . LYS D 1 43  ? 16.317  10.489  -18.157 1.00 28.37 ?  35  LYS C CB    1 
ATOM   7124 C CG    . LYS D 1 43  ? 15.928  9.819   -16.847 1.00 30.09 ?  35  LYS C CG    1 
ATOM   7125 C CD    . LYS D 1 43  ? 16.249  10.730  -15.670 1.00 28.03 ?  35  LYS C CD    1 
ATOM   7126 C CE    . LYS D 1 43  ? 15.724  10.177  -14.355 1.00 27.63 ?  35  LYS C CE    1 
ATOM   7127 N NZ    . LYS D 1 43  ? 16.315  8.848   -14.032 1.00 32.73 ?  35  LYS C NZ    1 
ATOM   7128 N N     . LEU D 1 44  ? 15.272  7.549   -19.726 1.00 28.14 ?  36  LEU C N     1 
ATOM   7129 C CA    . LEU D 1 44  ? 14.179  6.771   -20.309 1.00 33.76 ?  36  LEU C CA    1 
ATOM   7130 C C     . LEU D 1 44  ? 13.035  6.699   -19.309 1.00 33.15 ?  36  LEU C C     1 
ATOM   7131 O O     . LEU D 1 44  ? 12.989  5.823   -18.445 1.00 32.36 ?  36  LEU C O     1 
ATOM   7132 C CB    . LEU D 1 44  ? 14.663  5.382   -20.700 1.00 31.50 ?  36  LEU C CB    1 
ATOM   7133 C CG    . LEU D 1 44  ? 16.030  5.327   -21.379 1.00 31.23 ?  36  LEU C CG    1 
ATOM   7134 C CD1   . LEU D 1 44  ? 16.533  3.907   -21.402 1.00 26.04 ?  36  LEU C CD1   1 
ATOM   7135 C CD2   . LEU D 1 44  ? 15.955  5.896   -22.788 1.00 32.53 ?  36  LEU C CD2   1 
ATOM   7136 N N     . GLU D 1 45  ? 12.089  7.628   -19.437 1.00 26.99 ?  37  GLU C N     1 
ATOM   7137 C CA    . GLU D 1 45  ? 10.927  7.629   -18.560 1.00 30.30 ?  37  GLU C CA    1 
ATOM   7138 C C     . GLU D 1 45  ? 9.913   6.555   -18.930 1.00 29.58 ?  37  GLU C C     1 
ATOM   7139 O O     . GLU D 1 45  ? 9.055   6.224   -18.105 1.00 26.93 ?  37  GLU C O     1 
ATOM   7140 C CB    . GLU D 1 45  ? 10.261  9.003   -18.575 1.00 27.01 ?  37  GLU C CB    1 
ATOM   7141 C CG    . GLU D 1 45  ? 11.016  10.047  -17.770 1.00 31.53 ?  37  GLU C CG    1 
ATOM   7142 C CD    . GLU D 1 45  ? 11.073  9.711   -16.294 1.00 30.01 ?  37  GLU C CD    1 
ATOM   7143 O OE1   . GLU D 1 45  ? 9.999   9.535   -15.683 1.00 27.99 ?  37  GLU C OE1   1 
ATOM   7144 O OE2   . GLU D 1 45  ? 12.190  9.624   -15.740 1.00 30.00 ?  37  GLU C OE2   1 
ATOM   7145 N N     . TYR D 1 46  ? 9.990   6.000   -20.140 1.00 28.62 ?  38  TYR C N     1 
ATOM   7146 C CA    . TYR D 1 46  ? 9.104   4.893   -20.475 1.00 25.91 ?  38  TYR C CA    1 
ATOM   7147 C C     . TYR D 1 46  ? 9.469   3.609   -19.743 1.00 27.91 ?  38  TYR C C     1 
ATOM   7148 O O     . TYR D 1 46  ? 8.748   2.615   -19.885 1.00 21.79 ?  38  TYR C O     1 
ATOM   7149 C CB    . TYR D 1 46  ? 9.088   4.654   -21.989 1.00 24.81 ?  38  TYR C CB    1 
ATOM   7150 C CG    . TYR D 1 46  ? 10.428  4.333   -22.616 1.00 26.06 ?  38  TYR C CG    1 
ATOM   7151 C CD1   . TYR D 1 46  ? 10.974  3.056   -22.535 1.00 27.61 ?  38  TYR C CD1   1 
ATOM   7152 C CD2   . TYR D 1 46  ? 11.135  5.303   -23.313 1.00 29.55 ?  38  TYR C CD2   1 
ATOM   7153 C CE1   . TYR D 1 46  ? 12.194  2.762   -23.118 1.00 29.40 ?  38  TYR C CE1   1 
ATOM   7154 C CE2   . TYR D 1 46  ? 12.353  5.019   -23.898 1.00 29.20 ?  38  TYR C CE2   1 
ATOM   7155 C CZ    . TYR D 1 46  ? 12.878  3.748   -23.799 1.00 31.36 ?  38  TYR C CZ    1 
ATOM   7156 O OH    . TYR D 1 46  ? 14.091  3.471   -24.384 1.00 29.09 ?  38  TYR C OH    1 
ATOM   7157 N N     . GLN D 1 47  ? 10.562  3.604   -18.978 1.00 26.30 ?  39  GLN C N     1 
ATOM   7158 C CA    . GLN D 1 47  ? 10.899  2.473   -18.125 1.00 24.46 ?  39  GLN C CA    1 
ATOM   7159 C C     . GLN D 1 47  ? 10.076  2.437   -16.846 1.00 27.03 ?  39  GLN C C     1 
ATOM   7160 O O     . GLN D 1 47  ? 10.173  1.462   -16.094 1.00 24.89 ?  39  GLN C O     1 
ATOM   7161 C CB    . GLN D 1 47  ? 12.390  2.495   -17.778 1.00 30.34 ?  39  GLN C CB    1 
ATOM   7162 C CG    . GLN D 1 47  ? 13.292  2.089   -18.929 1.00 22.71 ?  39  GLN C CG    1 
ATOM   7163 C CD    . GLN D 1 47  ? 13.000  0.688   -19.427 1.00 31.95 ?  39  GLN C CD    1 
ATOM   7164 O OE1   . GLN D 1 47  ? 12.183  0.493   -20.328 1.00 31.37 ?  39  GLN C OE1   1 
ATOM   7165 N NE2   . GLN D 1 47  ? 13.666  -0.300  -18.840 1.00 26.04 ?  39  GLN C NE2   1 
ATOM   7166 N N     . ASN D 1 48  ? 9.289   3.474   -16.578 1.00 25.40 ?  40  ASN C N     1 
ATOM   7167 C CA    . ASN D 1 48  ? 8.307   3.395   -15.511 1.00 28.00 ?  40  ASN C CA    1 
ATOM   7168 C C     . ASN D 1 48  ? 7.341   2.250   -15.802 1.00 30.70 ?  40  ASN C C     1 
ATOM   7169 O O     . ASN D 1 48  ? 7.024   1.990   -16.969 1.00 25.99 ?  40  ASN C O     1 
ATOM   7170 C CB    . ASN D 1 48  ? 7.542   4.713   -15.385 1.00 29.63 ?  40  ASN C CB    1 
ATOM   7171 C CG    . ASN D 1 48  ? 8.320   5.766   -14.627 1.00 30.20 ?  40  ASN C CG    1 
ATOM   7172 O OD1   . ASN D 1 48  ? 8.732   5.548   -13.489 1.00 32.37 ?  40  ASN C OD1   1 
ATOM   7173 N ND2   . ASN D 1 48  ? 8.526   6.917   -15.256 1.00 30.31 ?  40  ASN C ND2   1 
ATOM   7174 N N     . PRO D 1 49  ? 6.861   1.545   -14.776 1.00 31.97 ?  41  PRO C N     1 
ATOM   7175 C CA    . PRO D 1 49  ? 6.031   0.352   -15.023 1.00 30.64 ?  41  PRO C CA    1 
ATOM   7176 C C     . PRO D 1 49  ? 4.810   0.611   -15.889 1.00 29.40 ?  41  PRO C C     1 
ATOM   7177 O O     . PRO D 1 49  ? 4.397   -0.281  -16.641 1.00 29.86 ?  41  PRO C O     1 
ATOM   7178 C CB    . PRO D 1 49  ? 5.638   -0.098  -13.607 1.00 27.90 ?  41  PRO C CB    1 
ATOM   7179 C CG    . PRO D 1 49  ? 5.928   1.074   -12.719 1.00 28.11 ?  41  PRO C CG    1 
ATOM   7180 C CD    . PRO D 1 49  ? 7.083   1.778   -13.341 1.00 25.77 ?  41  PRO C CD    1 
ATOM   7181 N N     . GLY D 1 50  ? 4.220   1.804   -15.816 1.00 29.74 ?  42  GLY C N     1 
ATOM   7182 C CA    . GLY D 1 50  ? 3.110   2.132   -16.691 1.00 28.78 ?  42  GLY C CA    1 
ATOM   7183 C C     . GLY D 1 50  ? 3.495   2.516   -18.104 1.00 33.39 ?  42  GLY C C     1 
ATOM   7184 O O     . GLY D 1 50  ? 2.622   2.565   -18.976 1.00 29.77 ?  42  GLY C O     1 
ATOM   7185 N N     . GLY D 1 51  ? 4.771   2.803   -18.349 1.00 26.97 ?  43  GLY C N     1 
ATOM   7186 C CA    . GLY D 1 51  ? 5.260   3.047   -19.689 1.00 27.03 ?  43  GLY C CA    1 
ATOM   7187 C C     . GLY D 1 51  ? 5.500   4.491   -20.073 1.00 26.49 ?  43  GLY C C     1 
ATOM   7188 O O     . GLY D 1 51  ? 5.754   4.759   -21.253 1.00 27.09 ?  43  GLY C O     1 
ATOM   7189 N N     . SER D 1 52  ? 5.435   5.427   -19.130 1.00 28.01 ?  44  SER C N     1 
ATOM   7190 C CA    . SER D 1 52  ? 5.640   6.832   -19.457 1.00 25.94 ?  44  SER C CA    1 
ATOM   7191 C C     . SER D 1 52  ? 6.002   7.595   -18.191 1.00 33.76 ?  44  SER C C     1 
ATOM   7192 O O     . SER D 1 52  ? 5.964   7.060   -17.081 1.00 26.89 ?  44  SER C O     1 
ATOM   7193 C CB    . SER D 1 52  ? 4.400   7.443   -20.118 1.00 27.69 ?  44  SER C CB    1 
ATOM   7194 O OG    . SER D 1 52  ? 3.588   8.112   -19.168 1.00 27.86 ?  44  SER C OG    1 
ATOM   7195 N N     . VAL D 1 53  ? 6.341   8.867   -18.381 1.00 34.02 ?  45  VAL C N     1 
ATOM   7196 C CA    . VAL D 1 53  ? 6.717   9.754   -17.289 1.00 31.94 ?  45  VAL C CA    1 
ATOM   7197 C C     . VAL D 1 53  ? 5.509   10.071  -16.407 1.00 30.55 ?  45  VAL C C     1 
ATOM   7198 O O     . VAL D 1 53  ? 5.658   10.427  -15.237 1.00 27.98 ?  45  VAL C O     1 
ATOM   7199 C CB    . VAL D 1 53  ? 7.359   11.048  -17.844 1.00 29.50 ?  45  VAL C CB    1 
ATOM   7200 C CG1   . VAL D 1 53  ? 6.341   11.852  -18.642 1.00 28.25 ?  45  VAL C CG1   1 
ATOM   7201 C CG2   . VAL D 1 53  ? 7.967   11.886  -16.726 1.00 28.87 ?  45  VAL C CG2   1 
HETATM 7202 N N1    . LLP D 1 54  ? 5.830   13.835  -23.883 1.00 33.44 ?  46  LLP C N1    1 
HETATM 7203 C C2    . LLP D 1 54  ? 4.856   12.975  -23.577 1.00 32.75 ?  46  LLP C C2    1 
HETATM 7204 C "C2'" . LLP D 1 54  ? 4.658   11.680  -24.419 1.00 34.07 ?  46  LLP C "C2'" 1 
HETATM 7205 C C3    . LLP D 1 54  ? 3.993   13.237  -22.481 1.00 34.14 ?  46  LLP C C3    1 
HETATM 7206 O O3    . LLP D 1 54  ? 2.978   12.321  -22.179 1.00 34.59 ?  46  LLP C O3    1 
HETATM 7207 C C4    . LLP D 1 54  ? 4.159   14.377  -21.724 1.00 33.12 ?  46  LLP C C4    1 
HETATM 7208 C "C4'" . LLP D 1 54  ? 3.165   14.664  -20.484 1.00 30.23 ?  46  LLP C "C4'" 1 
HETATM 7209 C C5    . LLP D 1 54  ? 5.155   15.257  -22.035 1.00 30.58 ?  46  LLP C C5    1 
HETATM 7210 C C6    . LLP D 1 54  ? 6.004   14.997  -23.119 1.00 31.81 ?  46  LLP C C6    1 
HETATM 7211 C "C5'" . LLP D 1 54  ? 5.372   16.564  -21.208 1.00 29.91 ?  46  LLP C "C5'" 1 
HETATM 7212 O OP4   . LLP D 1 54  ? 5.758   16.282  -19.881 1.00 30.75 ?  46  LLP C OP4   1 
HETATM 7213 P P     . LLP D 1 54  ? 5.391   17.320  -18.798 1.00 31.41 ?  46  LLP C P     1 
HETATM 7214 O OP1   . LLP D 1 54  ? 3.871   17.322  -18.590 1.00 32.95 ?  46  LLP C OP1   1 
HETATM 7215 O OP2   . LLP D 1 54  ? 5.833   18.662  -19.236 1.00 29.85 ?  46  LLP C OP2   1 
HETATM 7216 O OP3   . LLP D 1 54  ? 6.057   16.965  -17.514 1.00 30.39 ?  46  LLP C OP3   1 
HETATM 7217 N N     . LLP D 1 54  ? 4.313   9.918   -16.967 1.00 29.84 ?  46  LLP C N     1 
HETATM 7218 C CA    . LLP D 1 54  ? 3.071   10.265  -16.258 1.00 31.42 ?  46  LLP C CA    1 
HETATM 7219 C CB    . LLP D 1 54  ? 1.904   10.179  -17.208 1.00 35.44 ?  46  LLP C CB    1 
HETATM 7220 C CG    . LLP D 1 54  ? 2.030   11.274  -18.268 1.00 31.64 ?  46  LLP C CG    1 
HETATM 7221 C CD    . LLP D 1 54  ? 2.138   12.652  -17.596 1.00 33.53 ?  46  LLP C CD    1 
HETATM 7222 C CE    . LLP D 1 54  ? 1.981   13.754  -18.662 1.00 33.28 ?  46  LLP C CE    1 
HETATM 7223 N NZ    . LLP D 1 54  ? 2.824   13.441  -19.826 1.00 32.74 ?  46  LLP C NZ    1 
HETATM 7224 C C     . LLP D 1 54  ? 2.841   9.384   -15.077 1.00 34.22 ?  46  LLP C C     1 
HETATM 7225 O O     . LLP D 1 54  ? 2.034   9.718   -14.223 1.00 30.98 ?  46  LLP C O     1 
ATOM   7226 N N     . ASP D 1 55  ? 3.538   8.252   -15.025 1.00 29.47 ?  47  ASP C N     1 
ATOM   7227 C CA    . ASP D 1 55  ? 3.493   7.364   -13.868 1.00 28.53 ?  47  ASP C CA    1 
ATOM   7228 C C     . ASP D 1 55  ? 3.779   8.123   -12.580 1.00 30.63 ?  47  ASP C C     1 
ATOM   7229 O O     . ASP D 1 55  ? 3.087   7.953   -11.576 1.00 31.41 ?  47  ASP C O     1 
ATOM   7230 C CB    . ASP D 1 55  ? 4.507   6.231   -14.017 1.00 30.61 ?  47  ASP C CB    1 
ATOM   7231 C CG    . ASP D 1 55  ? 3.984   5.085   -14.847 1.00 31.76 ?  47  ASP C CG    1 
ATOM   7232 O OD1   . ASP D 1 55  ? 3.142   5.328   -15.737 1.00 27.65 ?  47  ASP C OD1   1 
ATOM   7233 O OD2   . ASP D 1 55  ? 4.418   3.940   -14.604 1.00 30.40 ?  47  ASP C OD2   1 
ATOM   7234 N N     . ARG D 1 56  ? 4.814   8.963   -12.631 1.00 30.47 ?  48  ARG C N     1 
ATOM   7235 C CA    . ARG D 1 56  ? 5.243   9.702   -11.450 1.00 30.02 ?  48  ARG C CA    1 
ATOM   7236 C C     . ARG D 1 56  ? 4.148   10.632  -10.951 1.00 35.35 ?  48  ARG C C     1 
ATOM   7237 O O     . ARG D 1 56  ? 3.780   10.603  -9.771  1.00 33.14 ?  48  ARG C O     1 
ATOM   7238 C CB    . ARG D 1 56  ? 6.508   10.496  -11.769 1.00 29.89 ?  48  ARG C CB    1 
ATOM   7239 C CG    . ARG D 1 56  ? 7.740   9.648   -12.001 1.00 28.92 ?  48  ARG C CG    1 
ATOM   7240 C CD    . ARG D 1 56  ? 8.901   10.531  -12.402 1.00 27.83 ?  48  ARG C CD    1 
ATOM   7241 N NE    . ARG D 1 56  ? 10.034  9.779   -12.924 1.00 28.96 ?  48  ARG C NE    1 
ATOM   7242 C CZ    . ARG D 1 56  ? 11.060  9.370   -12.191 1.00 36.31 ?  48  ARG C CZ    1 
ATOM   7243 N NH1   . ARG D 1 56  ? 11.118  9.609   -10.891 1.00 30.68 ?  48  ARG C NH1   1 
ATOM   7244 N NH2   . ARG D 1 56  ? 12.053  8.708   -12.777 1.00 32.78 ?  48  ARG C NH2   1 
ATOM   7245 N N     . ILE D 1 57  ? 3.615   11.473  -11.836 1.00 30.50 ?  49  ILE C N     1 
ATOM   7246 C CA    . ILE D 1 57  ? 2.637   12.450  -11.381 1.00 35.51 ?  49  ILE C CA    1 
ATOM   7247 C C     . ILE D 1 57  ? 1.314   11.774  -11.036 1.00 37.33 ?  49  ILE C C     1 
ATOM   7248 O O     . ILE D 1 57  ? 0.618   12.209  -10.113 1.00 35.53 ?  49  ILE C O     1 
ATOM   7249 C CB    . ILE D 1 57  ? 2.479   13.568  -12.429 1.00 34.36 ?  49  ILE C CB    1 
ATOM   7250 C CG1   . ILE D 1 57  ? 1.619   13.112  -13.608 1.00 36.07 ?  49  ILE C CG1   1 
ATOM   7251 C CG2   . ILE D 1 57  ? 3.850   14.011  -12.924 1.00 27.12 ?  49  ILE C CG2   1 
ATOM   7252 C CD1   . ILE D 1 57  ? 0.881   14.247  -14.283 1.00 29.52 ?  49  ILE C CD1   1 
ATOM   7253 N N     . ALA D 1 58  ? 0.959   10.688  -11.730 1.00 34.32 ?  50  ALA C N     1 
ATOM   7254 C CA    . ALA D 1 58  ? -0.270  9.975   -11.396 1.00 36.24 ?  50  ALA C CA    1 
ATOM   7255 C C     . ALA D 1 58  ? -0.231  9.466   -9.961  1.00 38.18 ?  50  ALA C C     1 
ATOM   7256 O O     . ALA D 1 58  ? -1.218  9.579   -9.226  1.00 34.91 ?  50  ALA C O     1 
ATOM   7257 C CB    . ALA D 1 58  ? -0.499  8.821   -12.373 1.00 28.47 ?  50  ALA C CB    1 
ATOM   7258 N N     . LEU D 1 59  ? 0.910   8.920   -9.539  1.00 33.53 ?  51  LEU C N     1 
ATOM   7259 C CA    . LEU D 1 59  ? 1.053   8.483   -8.155  1.00 38.30 ?  51  LEU C CA    1 
ATOM   7260 C C     . LEU D 1 59  ? 1.048   9.667   -7.197  1.00 38.62 ?  51  LEU C C     1 
ATOM   7261 O O     . LEU D 1 59  ? 0.490   9.580   -6.097  1.00 40.95 ?  51  LEU C O     1 
ATOM   7262 C CB    . LEU D 1 59  ? 2.339   7.673   -7.992  1.00 39.34 ?  51  LEU C CB    1 
ATOM   7263 C CG    . LEU D 1 59  ? 2.585   7.065   -6.610  1.00 34.73 ?  51  LEU C CG    1 
ATOM   7264 C CD1   . LEU D 1 59  ? 1.435   6.150   -6.218  1.00 31.55 ?  51  LEU C CD1   1 
ATOM   7265 C CD2   . LEU D 1 59  ? 3.910   6.320   -6.574  1.00 33.19 ?  51  LEU C CD2   1 
ATOM   7266 N N     . ALA D 1 60  ? 1.655   10.785  -7.601  1.00 35.67 ?  52  ALA C N     1 
ATOM   7267 C CA    . ALA D 1 60  ? 1.800   11.925  -6.699  1.00 38.10 ?  52  ALA C CA    1 
ATOM   7268 C C     . ALA D 1 60  ? 0.451   12.559  -6.376  1.00 35.98 ?  52  ALA C C     1 
ATOM   7269 O O     . ALA D 1 60  ? 0.113   12.755  -5.203  1.00 41.68 ?  52  ALA C O     1 
ATOM   7270 C CB    . ALA D 1 60  ? 2.748   12.956  -7.312  1.00 34.45 ?  52  ALA C CB    1 
ATOM   7271 N N     . MET D 1 61  ? -0.331  12.901  -7.407  1.00 35.24 ?  53  MET C N     1 
ATOM   7272 C CA    . MET D 1 61  ? -1.628  13.533  -7.171  1.00 40.20 ?  53  MET C CA    1 
ATOM   7273 C C     . MET D 1 61  ? -2.552  12.636  -6.356  1.00 36.77 ?  53  MET C C     1 
ATOM   7274 O O     . MET D 1 61  ? -3.278  13.117  -5.477  1.00 41.52 ?  53  MET C O     1 
ATOM   7275 C CB    . MET D 1 61  ? -2.291  13.913  -8.499  1.00 35.69 ?  53  MET C CB    1 
ATOM   7276 C CG    . MET D 1 61  ? -1.348  14.409  -9.582  1.00 36.23 ?  53  MET C CG    1 
ATOM   7277 S SD    . MET D 1 61  ? -2.185  15.473  -10.771 1.00 39.53 ?  53  MET C SD    1 
ATOM   7278 C CE    . MET D 1 61  ? -2.334  14.343  -12.152 1.00 30.54 ?  53  MET C CE    1 
ATOM   7279 N N     . ILE D 1 62  ? -2.543  11.331  -6.629  1.00 33.22 ?  54  ILE C N     1 
ATOM   7280 C CA    . ILE D 1 62  ? -3.396  10.416  -5.876  1.00 35.30 ?  54  ILE C CA    1 
ATOM   7281 C C     . ILE D 1 62  ? -2.934  10.328  -4.426  1.00 41.18 ?  54  ILE C C     1 
ATOM   7282 O O     . ILE D 1 62  ? -3.748  10.367  -3.495  1.00 35.55 ?  54  ILE C O     1 
ATOM   7283 C CB    . ILE D 1 62  ? -3.426  9.030   -6.545  1.00 35.23 ?  54  ILE C CB    1 
ATOM   7284 C CG1   . ILE D 1 62  ? -4.037  9.127   -7.946  1.00 33.42 ?  54  ILE C CG1   1 
ATOM   7285 C CG2   . ILE D 1 62  ? -4.193  8.037   -5.683  1.00 40.14 ?  54  ILE C CG2   1 
ATOM   7286 C CD1   . ILE D 1 62  ? -5.533  9.336   -7.953  1.00 41.44 ?  54  ILE C CD1   1 
ATOM   7287 N N     . GLU D 1 63  ? -1.621  10.214  -4.213  1.00 35.87 ?  55  GLU C N     1 
ATOM   7288 C CA    . GLU D 1 63  ? -1.103  10.130  -2.852  1.00 37.01 ?  55  GLU C CA    1 
ATOM   7289 C C     . GLU D 1 63  ? -1.285  11.441  -2.097  1.00 39.25 ?  55  GLU C C     1 
ATOM   7290 O O     . GLU D 1 63  ? -1.480  11.427  -0.876  1.00 45.43 ?  55  GLU C O     1 
ATOM   7291 C CB    . GLU D 1 63  ? 0.373   9.728   -2.871  1.00 39.73 ?  55  GLU C CB    1 
ATOM   7292 C CG    . GLU D 1 63  ? 0.608   8.235   -3.048  1.00 37.48 ?  55  GLU C CG    1 
ATOM   7293 C CD    . GLU D 1 63  ? 2.078   7.870   -2.993  1.00 46.50 ?  55  GLU C CD    1 
ATOM   7294 O OE1   . GLU D 1 63  ? 2.920   8.787   -3.093  1.00 45.62 ?  55  GLU C OE1   1 
ATOM   7295 O OE2   . GLU D 1 63  ? 2.390   6.670   -2.846  1.00 49.54 ?  55  GLU C OE2   1 
ATOM   7296 N N     . LYS D 1 64  ? -1.235  12.577  -2.797  1.00 36.76 ?  56  LYS C N     1 
ATOM   7297 C CA    . LYS D 1 64  ? -1.437  13.860  -2.131  1.00 42.07 ?  56  LYS C CA    1 
ATOM   7298 C C     . LYS D 1 64  ? -2.873  14.002  -1.641  1.00 43.91 ?  56  LYS C C     1 
ATOM   7299 O O     . LYS D 1 64  ? -3.110  14.377  -0.487  1.00 47.46 ?  56  LYS C O     1 
ATOM   7300 C CB    . LYS D 1 64  ? -1.075  15.011  -3.069  1.00 42.14 ?  56  LYS C CB    1 
ATOM   7301 C CG    . LYS D 1 64  ? -1.136  16.375  -2.397  1.00 53.40 ?  56  LYS C CG    1 
ATOM   7302 C CD    . LYS D 1 64  ? -0.506  17.456  -3.255  1.00 51.96 ?  56  LYS C CD    1 
ATOM   7303 C CE    . LYS D 1 64  ? -1.275  18.763  -3.145  1.00 54.63 ?  56  LYS C CE    1 
ATOM   7304 N NZ    . LYS D 1 64  ? -2.305  18.902  -4.213  1.00 48.64 ?  56  LYS C NZ    1 
ATOM   7305 N N     . ALA D 1 65  ? -3.846  13.710  -2.506  1.00 43.65 ?  57  ALA C N     1 
ATOM   7306 C CA    . ALA D 1 65  ? -5.244  13.780  -2.093  1.00 45.77 ?  57  ALA C CA    1 
ATOM   7307 C C     . ALA D 1 65  ? -5.568  12.742  -1.028  1.00 44.59 ?  57  ALA C C     1 
ATOM   7308 O O     . ALA D 1 65  ? -6.446  12.972  -0.189  1.00 42.99 ?  57  ALA C O     1 
ATOM   7309 C CB    . ALA D 1 65  ? -6.160  13.600  -3.303  1.00 42.46 ?  57  ALA C CB    1 
ATOM   7310 N N     . GLU D 1 66  ? -4.876  11.601  -1.046  1.00 44.07 ?  58  GLU C N     1 
ATOM   7311 C CA    . GLU D 1 66  ? -5.099  10.578  -0.030  1.00 40.04 ?  58  GLU C CA    1 
ATOM   7312 C C     . GLU D 1 66  ? -4.646  11.061  1.342   1.00 44.07 ?  58  GLU C C     1 
ATOM   7313 O O     . GLU D 1 66  ? -5.403  10.991  2.317   1.00 39.53 ?  58  GLU C O     1 
ATOM   7314 C CB    . GLU D 1 66  ? -4.370  9.290   -0.416  1.00 45.74 ?  58  GLU C CB    1 
ATOM   7315 C CG    . GLU D 1 66  ? -4.780  8.073   0.399   1.00 46.00 ?  58  GLU C CG    1 
ATOM   7316 C CD    . GLU D 1 66  ? -4.481  6.768   -0.313  1.00 56.09 ?  58  GLU C CD    1 
ATOM   7317 O OE1   . GLU D 1 66  ? -4.255  5.751   0.377   1.00 63.12 ?  58  GLU C OE1   1 
ATOM   7318 O OE2   . GLU D 1 66  ? -4.475  6.758   -1.562  1.00 56.90 ?  58  GLU C OE2   1 
ATOM   7319 N N     . ARG D 1 67  ? -3.409  11.558  1.435   1.00 44.93 ?  59  ARG C N     1 
ATOM   7320 C CA    . ARG D 1 67  ? -2.906  12.041  2.716   1.00 49.84 ?  59  ARG C CA    1 
ATOM   7321 C C     . ARG D 1 67  ? -3.636  13.300  3.170   1.00 44.64 ?  59  ARG C C     1 
ATOM   7322 O O     . ARG D 1 67  ? -3.731  13.556  4.376   1.00 42.50 ?  59  ARG C O     1 
ATOM   7323 C CB    . ARG D 1 67  ? -1.398  12.287  2.631   1.00 40.84 ?  59  ARG C CB    1 
ATOM   7324 C CG    . ARG D 1 67  ? -1.004  13.577  1.931   1.00 50.32 ?  59  ARG C CG    1 
ATOM   7325 C CD    . ARG D 1 67  ? 0.475   13.869  2.102   1.00 49.19 ?  59  ARG C CD    1 
ATOM   7326 N NE    . ARG D 1 67  ? 1.267   13.315  1.011   1.00 57.02 ?  59  ARG C NE    1 
ATOM   7327 C CZ    . ARG D 1 67  ? 1.566   13.968  -0.104  1.00 53.14 ?  59  ARG C CZ    1 
ATOM   7328 N NH1   . ARG D 1 67  ? 1.163   15.212  -0.305  1.00 53.48 ?  59  ARG C NH1   1 
ATOM   7329 N NH2   . ARG D 1 67  ? 2.289   13.359  -1.039  1.00 49.30 ?  59  ARG C NH2   1 
ATOM   7330 N N     . GLU D 1 68  ? -4.160  14.091  2.234   1.00 45.96 ?  60  GLU C N     1 
ATOM   7331 C CA    . GLU D 1 68  ? -4.973  15.252  2.575   1.00 39.89 ?  60  GLU C CA    1 
ATOM   7332 C C     . GLU D 1 68  ? -6.434  14.896  2.810   1.00 45.44 ?  60  GLU C C     1 
ATOM   7333 O O     . GLU D 1 68  ? -7.256  15.800  2.994   1.00 47.12 ?  60  GLU C O     1 
ATOM   7334 C CB    . GLU D 1 68  ? -4.868  16.319  1.480   1.00 40.41 ?  60  GLU C CB    1 
ATOM   7335 C CG    . GLU D 1 68  ? -3.487  16.944  1.348   1.00 49.75 ?  60  GLU C CG    1 
ATOM   7336 C CD    . GLU D 1 68  ? -3.361  17.832  0.124   1.00 51.33 ?  60  GLU C CD    1 
ATOM   7337 O OE1   . GLU D 1 68  ? -4.281  17.816  -0.721  1.00 48.96 ?  60  GLU C OE1   1 
ATOM   7338 O OE2   . GLU D 1 68  ? -2.341  18.545  0.008   1.00 50.29 ?  60  GLU C OE2   1 
ATOM   7339 N N     . GLY D 1 69  ? -6.773  13.608  2.801   1.00 42.54 ?  61  GLY C N     1 
ATOM   7340 C CA    . GLY D 1 69  ? -8.124  13.171  3.083   1.00 38.87 ?  61  GLY C CA    1 
ATOM   7341 C C     . GLY D 1 69  ? -9.156  13.507  2.032   1.00 48.56 ?  61  GLY C C     1 
ATOM   7342 O O     . GLY D 1 69  ? -10.347 13.283  2.267   1.00 53.07 ?  61  GLY C O     1 
ATOM   7343 N N     . LYS D 1 70  ? -8.744  14.041  0.879   1.00 41.64 ?  62  LYS C N     1 
ATOM   7344 C CA    . LYS D 1 70  ? -9.716  14.372  -0.158  1.00 47.03 ?  62  LYS C CA    1 
ATOM   7345 C C     . LYS D 1 70  ? -10.297 13.121  -0.798  1.00 47.84 ?  62  LYS C C     1 
ATOM   7346 O O     . LYS D 1 70  ? -11.450 13.133  -1.244  1.00 48.35 ?  62  LYS C O     1 
ATOM   7347 C CB    . LYS D 1 70  ? -9.076  15.271  -1.216  1.00 48.02 ?  62  LYS C CB    1 
ATOM   7348 C CG    . LYS D 1 70  ? -8.610  16.613  -0.677  1.00 49.35 ?  62  LYS C CG    1 
ATOM   7349 C CD    . LYS D 1 70  ? -8.839  17.733  -1.679  1.00 44.06 ?  62  LYS C CD    1 
ATOM   7350 C CE    . LYS D 1 70  ? -8.291  19.055  -1.160  1.00 53.87 ?  62  LYS C CE    1 
ATOM   7351 N NZ    . LYS D 1 70  ? -6.805  19.112  -1.227  1.00 52.86 ?  62  LYS C NZ    1 
ATOM   7352 N N     . ILE D 1 71  ? -9.524  12.039  -0.855  1.00 45.86 ?  63  ILE C N     1 
ATOM   7353 C CA    . ILE D 1 71  ? -10.010 10.764  -1.361  1.00 42.52 ?  63  ILE C CA    1 
ATOM   7354 C C     . ILE D 1 71  ? -9.535  9.649   -0.443  1.00 42.96 ?  63  ILE C C     1 
ATOM   7355 O O     . ILE D 1 71  ? -8.485  9.746   0.201   1.00 42.63 ?  63  ILE C O     1 
ATOM   7356 C CB    . ILE D 1 71  ? -9.550  10.480  -2.810  1.00 40.09 ?  63  ILE C CB    1 
ATOM   7357 C CG1   . ILE D 1 71  ? -8.025  10.376  -2.882  1.00 40.43 ?  63  ILE C CG1   1 
ATOM   7358 C CG2   . ILE D 1 71  ? -10.077 11.538  -3.757  1.00 43.10 ?  63  ILE C CG2   1 
ATOM   7359 C CD1   . ILE D 1 71  ? -7.484  10.325  -4.292  1.00 43.94 ?  63  ILE C CD1   1 
ATOM   7360 N N     . LYS D 1 72  ? -10.330 8.587   -0.383  1.00 43.69 ?  64  LYS C N     1 
ATOM   7361 C CA    . LYS D 1 72  ? -9.985  7.330   0.250   1.00 43.40 ?  64  LYS C CA    1 
ATOM   7362 C C     . LYS D 1 72  ? -10.163 6.205   -0.760  1.00 41.89 ?  64  LYS C C     1 
ATOM   7363 O O     . LYS D 1 72  ? -10.970 6.330   -1.687  1.00 44.71 ?  64  LYS C O     1 
ATOM   7364 C CB    . LYS D 1 72  ? -10.858 7.059   1.483   1.00 40.01 ?  64  LYS C CB    1 
ATOM   7365 N N     . PRO D 1 73  ? -9.404  5.118   -0.632  1.00 39.17 ?  65  PRO C N     1 
ATOM   7366 C CA    . PRO D 1 73  ? -9.557  3.994   -1.564  1.00 41.54 ?  65  PRO C CA    1 
ATOM   7367 C C     . PRO D 1 73  ? -11.014 3.580   -1.705  1.00 40.13 ?  65  PRO C C     1 
ATOM   7368 O O     . PRO D 1 73  ? -11.742 3.453   -0.719  1.00 35.18 ?  65  PRO C O     1 
ATOM   7369 C CB    . PRO D 1 73  ? -8.713  2.891   -0.922  1.00 39.44 ?  65  PRO C CB    1 
ATOM   7370 C CG    . PRO D 1 73  ? -7.647  3.625   -0.182  1.00 34.22 ?  65  PRO C CG    1 
ATOM   7371 C CD    . PRO D 1 73  ? -8.217  4.966   0.230   1.00 46.22 ?  65  PRO C CD    1 
ATOM   7372 N N     . GLY D 1 74  ? -11.446 3.393   -2.950  1.00 39.95 ?  66  GLY C N     1 
ATOM   7373 C CA    . GLY D 1 74  ? -12.835 3.195   -3.276  1.00 37.95 ?  66  GLY C CA    1 
ATOM   7374 C C     . GLY D 1 74  ? -13.504 4.402   -3.898  1.00 37.46 ?  66  GLY C C     1 
ATOM   7375 O O     . GLY D 1 74  ? -14.515 4.245   -4.593  1.00 38.69 ?  66  GLY C O     1 
ATOM   7376 N N     . ASP D 1 75  ? -12.965 5.597   -3.673  1.00 36.35 ?  67  ASP C N     1 
ATOM   7377 C CA    . ASP D 1 75  ? -13.506 6.793   -4.296  1.00 38.92 ?  67  ASP C CA    1 
ATOM   7378 C C     . ASP D 1 75  ? -13.223 6.788   -5.795  1.00 41.39 ?  67  ASP C C     1 
ATOM   7379 O O     . ASP D 1 75  ? -12.417 6.005   -6.307  1.00 40.62 ?  67  ASP C O     1 
ATOM   7380 C CB    . ASP D 1 75  ? -12.913 8.048   -3.660  1.00 38.89 ?  67  ASP C CB    1 
ATOM   7381 C CG    . ASP D 1 75  ? -13.351 8.231   -2.228  1.00 40.99 ?  67  ASP C CG    1 
ATOM   7382 O OD1   . ASP D 1 75  ? -14.282 7.517   -1.799  1.00 43.45 ?  67  ASP C OD1   1 
ATOM   7383 O OD2   . ASP D 1 75  ? -12.765 9.084   -1.530  1.00 42.03 ?  67  ASP C OD2   1 
ATOM   7384 N N     . THR D 1 76  ? -13.892 7.693   -6.499  1.00 37.77 ?  68  THR C N     1 
ATOM   7385 C CA    . THR D 1 76  ? -13.767 7.814   -7.944  1.00 37.29 ?  68  THR C CA    1 
ATOM   7386 C C     . THR D 1 76  ? -13.031 9.100   -8.290  1.00 40.47 ?  68  THR C C     1 
ATOM   7387 O O     . THR D 1 76  ? -13.343 10.164  -7.744  1.00 38.85 ?  68  THR C O     1 
ATOM   7388 C CB    . THR D 1 76  ? -15.139 7.803   -8.618  1.00 38.66 ?  68  THR C CB    1 
ATOM   7389 O OG1   . THR D 1 76  ? -15.787 6.552   -8.361  1.00 42.27 ?  68  THR C OG1   1 
ATOM   7390 C CG2   . THR D 1 76  ? -14.989 7.989   -10.121 1.00 37.21 ?  68  THR C CG2   1 
ATOM   7391 N N     . ILE D 1 77  ? -12.064 9.002   -9.196  1.00 37.19 ?  69  ILE C N     1 
ATOM   7392 C CA    . ILE D 1 77  ? -11.376 10.176  -9.713  1.00 39.25 ?  69  ILE C CA    1 
ATOM   7393 C C     . ILE D 1 77  ? -11.793 10.380  -11.162 1.00 40.02 ?  69  ILE C C     1 
ATOM   7394 O O     . ILE D 1 77  ? -12.095 9.424   -11.888 1.00 37.49 ?  69  ILE C O     1 
ATOM   7395 C CB    . ILE D 1 77  ? -9.842  10.068  -9.587  1.00 38.01 ?  69  ILE C CB    1 
ATOM   7396 C CG1   . ILE D 1 77  ? -9.234  9.378   -10.809 1.00 40.34 ?  69  ILE C CG1   1 
ATOM   7397 C CG2   . ILE D 1 77  ? -9.461  9.336   -8.312  1.00 38.17 ?  69  ILE C CG2   1 
ATOM   7398 C CD1   . ILE D 1 77  ? -7.749  9.592   -10.944 1.00 47.06 ?  69  ILE C CD1   1 
ATOM   7399 N N     . VAL D 1 78  ? -11.828 11.645  -11.579 1.00 39.95 ?  70  VAL C N     1 
ATOM   7400 C CA    . VAL D 1 78  ? -12.197 12.014  -12.941 1.00 38.69 ?  70  VAL C CA    1 
ATOM   7401 C C     . VAL D 1 78  ? -11.142 12.960  -13.498 1.00 35.71 ?  70  VAL C C     1 
ATOM   7402 O O     . VAL D 1 78  ? -10.580 13.779  -12.763 1.00 36.25 ?  70  VAL C O     1 
ATOM   7403 C CB    . VAL D 1 78  ? -13.603 12.654  -13.007 1.00 41.53 ?  70  VAL C CB    1 
ATOM   7404 C CG1   . VAL D 1 78  ? -13.603 14.053  -12.390 1.00 36.86 ?  70  VAL C CG1   1 
ATOM   7405 C CG2   . VAL D 1 78  ? -14.103 12.692  -14.440 1.00 38.98 ?  70  VAL C CG2   1 
ATOM   7406 N N     . GLU D 1 79  ? -10.861 12.837  -14.795 1.00 33.70 ?  71  GLU C N     1 
ATOM   7407 C CA    . GLU D 1 79  ? -9.869  13.707  -15.414 1.00 32.19 ?  71  GLU C CA    1 
ATOM   7408 C C     . GLU D 1 79  ? -10.062 13.757  -16.924 1.00 34.91 ?  71  GLU C C     1 
ATOM   7409 O O     . GLU D 1 79  ? -10.228 12.711  -17.566 1.00 35.11 ?  71  GLU C O     1 
ATOM   7410 C CB    . GLU D 1 79  ? -8.451  13.233  -15.076 1.00 33.82 ?  71  GLU C CB    1 
ATOM   7411 C CG    . GLU D 1 79  ? -7.352  14.093  -15.684 1.00 32.30 ?  71  GLU C CG    1 
ATOM   7412 C CD    . GLU D 1 79  ? -7.024  15.316  -14.844 1.00 34.92 ?  71  GLU C CD    1 
ATOM   7413 O OE1   . GLU D 1 79  ? -7.680  15.531  -13.802 1.00 31.28 ?  71  GLU C OE1   1 
ATOM   7414 O OE2   . GLU D 1 79  ? -6.109  16.070  -15.237 1.00 35.00 ?  71  GLU C OE2   1 
ATOM   7415 N N     . PRO D 1 80  ? -10.057 14.951  -17.525 1.00 38.36 ?  72  PRO C N     1 
ATOM   7416 C CA    . PRO D 1 80  ? -10.060 15.058  -18.991 1.00 37.01 ?  72  PRO C CA    1 
ATOM   7417 C C     . PRO D 1 80  ? -8.643  14.902  -19.524 1.00 39.44 ?  72  PRO C C     1 
ATOM   7418 O O     . PRO D 1 80  ? -7.764  15.718  -19.237 1.00 38.21 ?  72  PRO C O     1 
ATOM   7419 C CB    . PRO D 1 80  ? -10.609 16.467  -19.242 1.00 36.76 ?  72  PRO C CB    1 
ATOM   7420 C CG    . PRO D 1 80  ? -10.224 17.248  -18.013 1.00 33.42 ?  72  PRO C CG    1 
ATOM   7421 C CD    . PRO D 1 80  ? -10.033 16.270  -16.868 1.00 32.38 ?  72  PRO C CD    1 
ATOM   7422 N N     . THR D 1 81  ? -8.417  13.835  -20.284 1.00 40.35 ?  73  THR C N     1 
ATOM   7423 C CA    . THR D 1 81  ? -7.082  13.535  -20.777 1.00 41.54 ?  73  THR C CA    1 
ATOM   7424 C C     . THR D 1 81  ? -7.190  12.667  -22.019 1.00 43.15 ?  73  THR C C     1 
ATOM   7425 O O     . THR D 1 81  ? -8.056  11.793  -22.102 1.00 38.11 ?  73  THR C O     1 
ATOM   7426 C CB    . THR D 1 81  ? -6.236  12.828  -19.710 1.00 43.60 ?  73  THR C CB    1 
ATOM   7427 O OG1   . THR D 1 81  ? -5.098  12.213  -20.328 1.00 36.36 ?  73  THR C OG1   1 
ATOM   7428 C CG2   . THR D 1 81  ? -7.062  11.771  -18.985 1.00 38.56 ?  73  THR C CG2   1 
ATOM   7429 N N     . SER D 1 82  ? -6.304  12.919  -22.980 1.00 40.08 ?  74  SER C N     1 
ATOM   7430 C CA    . SER D 1 82  ? -6.232  12.137  -24.205 1.00 41.38 ?  74  SER C CA    1 
ATOM   7431 C C     . SER D 1 82  ? -4.832  11.575  -24.427 1.00 42.94 ?  74  SER C C     1 
ATOM   7432 O O     . SER D 1 82  ? -4.459  11.273  -25.564 1.00 40.70 ?  74  SER C O     1 
ATOM   7433 C CB    . SER D 1 82  ? -6.674  12.984  -25.401 1.00 45.36 ?  74  SER C CB    1 
ATOM   7434 O OG    . SER D 1 82  ? -5.561  13.479  -26.121 1.00 49.63 ?  74  SER C OG    1 
ATOM   7435 N N     . GLY D 1 83  ? -4.058  11.421  -23.363 1.00 36.12 ?  75  GLY C N     1 
ATOM   7436 C CA    . GLY D 1 83  ? -2.667  11.014  -23.464 1.00 38.76 ?  75  GLY C CA    1 
ATOM   7437 C C     . GLY D 1 83  ? -2.240  10.152  -22.298 1.00 40.25 ?  75  GLY C C     1 
ATOM   7438 O O     . GLY D 1 83  ? -3.051  9.432   -21.707 1.00 34.76 ?  75  GLY C O     1 
ATOM   7439 N N     . ASN D 1 84  ? -0.951  10.243  -21.956 1.00 35.37 ?  76  ASN C N     1 
ATOM   7440 C CA    . ASN D 1 84  ? -0.343  9.321   -21.003 1.00 34.35 ?  76  ASN C CA    1 
ATOM   7441 C C     . ASN D 1 84  ? -0.807  9.549   -19.569 1.00 35.00 ?  76  ASN C C     1 
ATOM   7442 O O     . ASN D 1 84  ? -0.673  8.640   -18.740 1.00 31.06 ?  76  ASN C O     1 
ATOM   7443 C CB    . ASN D 1 84  ? 1.180   9.430   -21.085 1.00 31.76 ?  76  ASN C CB    1 
ATOM   7444 C CG    . ASN D 1 84  ? 1.741   8.804   -22.343 1.00 31.72 ?  76  ASN C CG    1 
ATOM   7445 O OD1   . ASN D 1 84  ? 1.386   7.682   -22.702 1.00 31.13 ?  76  ASN C OD1   1 
ATOM   7446 N ND2   . ASN D 1 84  ? 2.620   9.529   -23.025 1.00 30.27 ?  76  ASN C ND2   1 
ATOM   7447 N N     . THR D 1 85  ? -1.333  10.734  -19.249 1.00 36.81 ?  77  THR C N     1 
ATOM   7448 C CA    . THR D 1 85  ? -1.876  10.956  -17.912 1.00 36.30 ?  77  THR C CA    1 
ATOM   7449 C C     . THR D 1 85  ? -3.084  10.059  -17.663 1.00 34.40 ?  77  THR C C     1 
ATOM   7450 O O     . THR D 1 85  ? -3.266  9.542   -16.554 1.00 31.77 ?  77  THR C O     1 
ATOM   7451 C CB    . THR D 1 85  ? -2.239  12.431  -17.727 1.00 37.20 ?  77  THR C CB    1 
ATOM   7452 O OG1   . THR D 1 85  ? -1.042  13.202  -17.575 1.00 35.03 ?  77  THR C OG1   1 
ATOM   7453 C CG2   . THR D 1 85  ? -3.108  12.632  -16.494 1.00 37.61 ?  77  THR C CG2   1 
ATOM   7454 N N     . GLY D 1 86  ? -3.907  9.847   -18.691 1.00 32.09 ?  78  GLY C N     1 
ATOM   7455 C CA    . GLY D 1 86  ? -4.999  8.897   -18.560 1.00 35.64 ?  78  GLY C CA    1 
ATOM   7456 C C     . GLY D 1 86  ? -4.502  7.485   -18.320 1.00 33.19 ?  78  GLY C C     1 
ATOM   7457 O O     . GLY D 1 86  ? -5.009  6.774   -17.450 1.00 28.97 ?  78  GLY C O     1 
ATOM   7458 N N     . ILE D 1 87  ? -3.496  7.064   -19.091 1.00 32.11 ?  79  ILE C N     1 
ATOM   7459 C CA    . ILE D 1 87  ? -2.911  5.740   -18.898 1.00 29.96 ?  79  ILE C CA    1 
ATOM   7460 C C     . ILE D 1 87  ? -2.295  5.630   -17.510 1.00 29.41 ?  79  ILE C C     1 
ATOM   7461 O O     . ILE D 1 87  ? -2.476  4.626   -16.812 1.00 28.35 ?  79  ILE C O     1 
ATOM   7462 C CB    . ILE D 1 87  ? -1.877  5.446   -20.001 1.00 32.55 ?  79  ILE C CB    1 
ATOM   7463 C CG1   . ILE D 1 87  ? -2.566  5.316   -21.360 1.00 28.64 ?  79  ILE C CG1   1 
ATOM   7464 C CG2   . ILE D 1 87  ? -1.091  4.183   -19.681 1.00 31.11 ?  79  ILE C CG2   1 
ATOM   7465 C CD1   . ILE D 1 87  ? -1.657  5.606   -22.530 1.00 37.62 ?  79  ILE C CD1   1 
ATOM   7466 N N     . GLY D 1 88  ? -1.571  6.665   -17.083 1.00 27.12 ?  80  GLY C N     1 
ATOM   7467 C CA    . GLY D 1 88  ? -0.954  6.631   -15.768 1.00 29.43 ?  80  GLY C CA    1 
ATOM   7468 C C     . GLY D 1 88  ? -1.969  6.611   -14.643 1.00 29.88 ?  80  GLY C C     1 
ATOM   7469 O O     . GLY D 1 88  ? -1.821  5.860   -13.676 1.00 29.99 ?  80  GLY C O     1 
ATOM   7470 N N     . LEU D 1 89  ? -3.015  7.434   -14.750 1.00 30.11 ?  81  LEU C N     1 
ATOM   7471 C CA    . LEU D 1 89  ? -4.034  7.460   -13.706 1.00 31.17 ?  81  LEU C CA    1 
ATOM   7472 C C     . LEU D 1 89  ? -4.825  6.158   -13.674 1.00 30.90 ?  81  LEU C C     1 
ATOM   7473 O O     . LEU D 1 89  ? -5.116  5.633   -12.594 1.00 25.35 ?  81  LEU C O     1 
ATOM   7474 C CB    . LEU D 1 89  ? -4.965  8.654   -13.903 1.00 31.76 ?  81  LEU C CB    1 
ATOM   7475 C CG    . LEU D 1 89  ? -4.426  10.001  -13.419 1.00 34.33 ?  81  LEU C CG    1 
ATOM   7476 C CD1   . LEU D 1 89  ? -5.387  11.116  -13.794 1.00 37.02 ?  81  LEU C CD1   1 
ATOM   7477 C CD2   . LEU D 1 89  ? -4.174  9.983   -11.916 1.00 29.38 ?  81  LEU C CD2   1 
ATOM   7478 N N     . ALA D 1 90  ? -5.184  5.623   -14.843 1.00 30.01 ?  82  ALA C N     1 
ATOM   7479 C CA    . ALA D 1 90  ? -5.832  4.315   -14.882 1.00 30.56 ?  82  ALA C CA    1 
ATOM   7480 C C     . ALA D 1 90  ? -4.930  3.243   -14.288 1.00 31.46 ?  82  ALA C C     1 
ATOM   7481 O O     . ALA D 1 90  ? -5.404  2.328   -13.603 1.00 31.31 ?  82  ALA C O     1 
ATOM   7482 C CB    . ALA D 1 90  ? -6.216  3.959   -16.318 1.00 29.83 ?  82  ALA C CB    1 
ATOM   7483 N N     . PHE D 1 91  ? -3.625  3.346   -14.538 1.00 29.48 ?  83  PHE C N     1 
ATOM   7484 C CA    . PHE D 1 91  ? -2.669  2.395   -13.984 1.00 27.44 ?  83  PHE C CA    1 
ATOM   7485 C C     . PHE D 1 91  ? -2.607  2.510   -12.464 1.00 28.04 ?  83  PHE C C     1 
ATOM   7486 O O     . PHE D 1 91  ? -2.765  1.518   -11.743 1.00 27.12 ?  83  PHE C O     1 
ATOM   7487 C CB    . PHE D 1 91  ? -1.297  2.637   -14.624 1.00 27.77 ?  83  PHE C CB    1 
ATOM   7488 C CG    . PHE D 1 91  ? -0.133  2.116   -13.825 1.00 28.11 ?  83  PHE C CG    1 
ATOM   7489 C CD1   . PHE D 1 91  ? -0.091  0.804   -13.378 1.00 27.50 ?  83  PHE C CD1   1 
ATOM   7490 C CD2   . PHE D 1 91  ? 0.931   2.953   -13.531 1.00 26.81 ?  83  PHE C CD2   1 
ATOM   7491 C CE1   . PHE D 1 91  ? 0.990   0.343   -12.647 1.00 26.96 ?  83  PHE C CE1   1 
ATOM   7492 C CE2   . PHE D 1 91  ? 2.013   2.499   -12.804 1.00 29.81 ?  83  PHE C CE2   1 
ATOM   7493 C CZ    . PHE D 1 91  ? 2.043   1.192   -12.360 1.00 29.67 ?  83  PHE C CZ    1 
ATOM   7494 N N     . VAL D 1 92  ? -2.392  3.726   -11.959 1.00 28.62 ?  84  VAL C N     1 
ATOM   7495 C CA    . VAL D 1 92  ? -2.213  3.913   -10.523 1.00 25.41 ?  84  VAL C CA    1 
ATOM   7496 C C     . VAL D 1 92  ? -3.510  3.627   -9.774  1.00 31.90 ?  84  VAL C C     1 
ATOM   7497 O O     . VAL D 1 92  ? -3.496  3.046   -8.683  1.00 29.89 ?  84  VAL C O     1 
ATOM   7498 C CB    . VAL D 1 92  ? -1.679  5.329   -10.241 1.00 24.88 ?  84  VAL C CB    1 
ATOM   7499 C CG1   . VAL D 1 92  ? -1.765  5.657   -8.758  1.00 29.59 ?  84  VAL C CG1   1 
ATOM   7500 C CG2   . VAL D 1 92  ? -0.246  5.456   -10.738 1.00 23.95 ?  84  VAL C CG2   1 
ATOM   7501 N N     . CYS D 1 93  ? -4.653  4.008   -10.353 1.00 31.21 ?  85  CYS C N     1 
ATOM   7502 C CA    . CYS D 1 93  ? -5.930  3.773   -9.683  1.00 30.69 ?  85  CYS C CA    1 
ATOM   7503 C C     . CYS D 1 93  ? -6.203  2.286   -9.509  1.00 33.08 ?  85  CYS C C     1 
ATOM   7504 O O     . CYS D 1 93  ? -6.701  1.858   -8.461  1.00 34.75 ?  85  CYS C O     1 
ATOM   7505 C CB    . CYS D 1 93  ? -7.065  4.433   -10.462 1.00 28.49 ?  85  CYS C CB    1 
ATOM   7506 S SG    . CYS D 1 93  ? -7.226  6.193   -10.140 1.00 34.50 ?  85  CYS C SG    1 
ATOM   7507 N N     . ALA D 1 94  ? -5.892  1.482   -10.528 1.00 29.69 ?  86  ALA C N     1 
ATOM   7508 C CA    . ALA D 1 94  ? -6.087  0.042   -10.413 1.00 30.87 ?  86  ALA C CA    1 
ATOM   7509 C C     . ALA D 1 94  ? -5.212  -0.543  -9.312  1.00 33.12 ?  86  ALA C C     1 
ATOM   7510 O O     . ALA D 1 94  ? -5.626  -1.463  -8.599  1.00 31.98 ?  86  ALA C O     1 
ATOM   7511 C CB    . ALA D 1 94  ? -5.793  -0.634  -11.752 1.00 31.87 ?  86  ALA C CB    1 
ATOM   7512 N N     . ALA D 1 95  ? -4.003  -0.007  -9.146  1.00 30.76 ?  87  ALA C N     1 
ATOM   7513 C CA    . ALA D 1 95  ? -3.077  -0.528  -8.149  1.00 31.82 ?  87  ALA C CA    1 
ATOM   7514 C C     . ALA D 1 95  ? -3.440  -0.101  -6.733  1.00 33.80 ?  87  ALA C C     1 
ATOM   7515 O O     . ALA D 1 95  ? -3.150  -0.832  -5.778  1.00 31.27 ?  87  ALA C O     1 
ATOM   7516 C CB    . ALA D 1 95  ? -1.654  -0.077  -8.473  1.00 28.87 ?  87  ALA C CB    1 
ATOM   7517 N N     . LYS D 1 96  ? -4.063  1.066   -6.572  1.00 29.76 ?  88  LYS C N     1 
ATOM   7518 C CA    . LYS D 1 96  ? -4.383  1.604   -5.257  1.00 34.91 ?  88  LYS C CA    1 
ATOM   7519 C C     . LYS D 1 96  ? -5.859  1.468   -4.904  1.00 35.71 ?  88  LYS C C     1 
ATOM   7520 O O     . LYS D 1 96  ? -6.298  2.028   -3.895  1.00 31.48 ?  88  LYS C O     1 
ATOM   7521 C CB    . LYS D 1 96  ? -3.955  3.070   -5.173  1.00 34.65 ?  88  LYS C CB    1 
ATOM   7522 C CG    . LYS D 1 96  ? -2.448  3.269   -5.187  1.00 35.17 ?  88  LYS C CG    1 
ATOM   7523 C CD    . LYS D 1 96  ? -2.079  4.730   -5.013  1.00 38.18 ?  88  LYS C CD    1 
ATOM   7524 C CE    . LYS D 1 96  ? -2.219  5.163   -3.562  1.00 49.98 ?  88  LYS C CE    1 
ATOM   7525 N NZ    . LYS D 1 96  ? -1.467  4.273   -2.635  1.00 48.82 ?  88  LYS C NZ    1 
ATOM   7526 N N     . GLY D 1 97  ? -6.632  0.742   -5.707  1.00 34.97 ?  89  GLY C N     1 
ATOM   7527 C CA    . GLY D 1 97  ? -8.024  0.497   -5.381  1.00 32.75 ?  89  GLY C CA    1 
ATOM   7528 C C     . GLY D 1 97  ? -8.939  1.688   -5.554  1.00 37.34 ?  89  GLY C C     1 
ATOM   7529 O O     . GLY D 1 97  ? -9.888  1.847   -4.780  1.00 36.56 ?  89  GLY C O     1 
ATOM   7530 N N     . TYR D 1 98  ? -8.682  2.530   -6.550  1.00 36.87 ?  90  TYR C N     1 
ATOM   7531 C CA    . TYR D 1 98  ? -9.521  3.680   -6.850  1.00 31.89 ?  90  TYR C CA    1 
ATOM   7532 C C     . TYR D 1 98  ? -10.267 3.458   -8.159  1.00 35.76 ?  90  TYR C C     1 
ATOM   7533 O O     . TYR D 1 98  ? -9.763  2.807   -9.079  1.00 32.61 ?  90  TYR C O     1 
ATOM   7534 C CB    . TYR D 1 98  ? -8.688  4.962   -6.948  1.00 34.40 ?  90  TYR C CB    1 
ATOM   7535 C CG    . TYR D 1 98  ? -8.247  5.520   -5.616  1.00 41.13 ?  90  TYR C CG    1 
ATOM   7536 C CD1   . TYR D 1 98  ? -9.059  6.395   -4.907  1.00 37.28 ?  90  TYR C CD1   1 
ATOM   7537 C CD2   . TYR D 1 98  ? -7.018  5.178   -5.069  1.00 33.09 ?  90  TYR C CD2   1 
ATOM   7538 C CE1   . TYR D 1 98  ? -8.662  6.911   -3.691  1.00 40.61 ?  90  TYR C CE1   1 
ATOM   7539 C CE2   . TYR D 1 98  ? -6.611  5.688   -3.851  1.00 41.09 ?  90  TYR C CE2   1 
ATOM   7540 C CZ    . TYR D 1 98  ? -7.438  6.555   -3.166  1.00 45.68 ?  90  TYR C CZ    1 
ATOM   7541 O OH    . TYR D 1 98  ? -7.045  7.070   -1.953  1.00 49.84 ?  90  TYR C OH    1 
ATOM   7542 N N     . LYS D 1 99  ? -11.477 4.003   -8.235  1.00 38.16 ?  91  LYS C N     1 
ATOM   7543 C CA    . LYS D 1 99  ? -12.246 3.993   -9.470  1.00 34.94 ?  91  LYS C CA    1 
ATOM   7544 C C     . LYS D 1 99  ? -11.859 5.205   -10.306 1.00 34.77 ?  91  LYS C C     1 
ATOM   7545 O O     . LYS D 1 99  ? -11.654 6.299   -9.773  1.00 39.34 ?  91  LYS C O     1 
ATOM   7546 C CB    . LYS D 1 99  ? -13.748 3.999   -9.181  1.00 34.17 ?  91  LYS C CB    1 
ATOM   7547 C CG    . LYS D 1 99  ? -14.310 2.628   -8.832  1.00 38.46 ?  91  LYS C CG    1 
ATOM   7548 C CD    . LYS D 1 99  ? -15.779 2.700   -8.448  1.00 39.62 ?  91  LYS C CD    1 
ATOM   7549 C CE    . LYS D 1 99  ? -16.618 3.294   -9.567  1.00 50.79 ?  91  LYS C CE    1 
ATOM   7550 N NZ    . LYS D 1 99  ? -18.076 3.125   -9.315  1.00 56.12 ?  91  LYS C NZ    1 
ATOM   7551 N N     . ALA D 1 100 ? -11.748 5.004   -11.616 1.00 37.34 ?  92  ALA C N     1 
ATOM   7552 C CA    . ALA D 1 100 ? -11.261 6.038   -12.517 1.00 34.72 ?  92  ALA C CA    1 
ATOM   7553 C C     . ALA D 1 100 ? -12.266 6.286   -13.630 1.00 34.32 ?  92  ALA C C     1 
ATOM   7554 O O     . ALA D 1 100 ? -12.835 5.344   -14.190 1.00 31.21 ?  92  ALA C O     1 
ATOM   7555 C CB    . ALA D 1 100 ? -9.904  5.657   -13.120 1.00 29.62 ?  92  ALA C CB    1 
ATOM   7556 N N     . VAL D 1 101 ? -12.479 7.562   -13.942 1.00 32.36 ?  93  VAL C N     1 
ATOM   7557 C CA    . VAL D 1 101 ? -13.307 7.987   -15.063 1.00 33.12 ?  93  VAL C CA    1 
ATOM   7558 C C     . VAL D 1 101 ? -12.523 9.027   -15.849 1.00 31.51 ?  93  VAL C C     1 
ATOM   7559 O O     . VAL D 1 101 ? -11.997 9.981   -15.266 1.00 34.58 ?  93  VAL C O     1 
ATOM   7560 C CB    . VAL D 1 101 ? -14.659 8.564   -14.599 1.00 34.90 ?  93  VAL C CB    1 
ATOM   7561 C CG1   . VAL D 1 101 ? -15.489 9.003   -15.795 1.00 31.86 ?  93  VAL C CG1   1 
ATOM   7562 C CG2   . VAL D 1 101 ? -15.424 7.543   -13.770 1.00 33.75 ?  93  VAL C CG2   1 
ATOM   7563 N N     . PHE D 1 102 ? -12.432 8.839   -17.163 1.00 30.36 ?  94  PHE C N     1 
ATOM   7564 C CA    . PHE D 1 102 ? -11.727 9.773   -18.029 1.00 32.39 ?  94  PHE C CA    1 
ATOM   7565 C C     . PHE D 1 102 ? -12.652 10.237  -19.142 1.00 35.43 ?  94  PHE C C     1 
ATOM   7566 O O     . PHE D 1 102 ? -13.296 9.417   -19.805 1.00 35.99 ?  94  PHE C O     1 
ATOM   7567 C CB    . PHE D 1 102 ? -10.465 9.144   -18.625 1.00 30.80 ?  94  PHE C CB    1 
ATOM   7568 C CG    . PHE D 1 102 ? -9.558  8.524   -17.603 1.00 32.53 ?  94  PHE C CG    1 
ATOM   7569 C CD1   . PHE D 1 102 ? -8.786  9.318   -16.771 1.00 33.45 ?  94  PHE C CD1   1 
ATOM   7570 C CD2   . PHE D 1 102 ? -9.470  7.148   -17.479 1.00 28.97 ?  94  PHE C CD2   1 
ATOM   7571 C CE1   . PHE D 1 102 ? -7.946  8.750   -15.832 1.00 35.82 ?  94  PHE C CE1   1 
ATOM   7572 C CE2   . PHE D 1 102 ? -8.632  6.575   -16.543 1.00 29.54 ?  94  PHE C CE2   1 
ATOM   7573 C CZ    . PHE D 1 102 ? -7.869  7.376   -15.718 1.00 32.90 ?  94  PHE C CZ    1 
ATOM   7574 N N     . THR D 1 103 ? -12.718 11.549  -19.336 1.00 36.92 ?  95  THR C N     1 
ATOM   7575 C CA    . THR D 1 103 ? -13.415 12.137  -20.469 1.00 37.72 ?  95  THR C CA    1 
ATOM   7576 C C     . THR D 1 103 ? -12.415 12.404  -21.582 1.00 37.97 ?  95  THR C C     1 
ATOM   7577 O O     . THR D 1 103 ? -11.278 12.815  -21.325 1.00 38.29 ?  95  THR C O     1 
ATOM   7578 C CB    . THR D 1 103 ? -14.131 13.434  -20.082 1.00 34.76 ?  95  THR C CB    1 
ATOM   7579 O OG1   . THR D 1 103 ? -13.180 14.377  -19.570 1.00 33.76 ?  95  THR C OG1   1 
ATOM   7580 C CG2   . THR D 1 103 ? -15.196 13.162  -19.031 1.00 39.78 ?  95  THR C CG2   1 
ATOM   7581 N N     . MET D 1 104 ? -12.848 12.164  -22.819 1.00 35.76 ?  96  MET C N     1 
ATOM   7582 C CA    . MET D 1 104 ? -11.966 12.235  -23.973 1.00 42.63 ?  96  MET C CA    1 
ATOM   7583 C C     . MET D 1 104 ? -12.823 12.367  -25.216 1.00 40.78 ?  96  MET C C     1 
ATOM   7584 O O     . MET D 1 104 ? -13.960 11.884  -25.229 1.00 40.19 ?  96  MET C O     1 
ATOM   7585 C CB    . MET D 1 104 ? -11.085 10.981  -24.065 1.00 37.23 ?  96  MET C CB    1 
ATOM   7586 C CG    . MET D 1 104 ? -11.781 9.719   -23.577 1.00 41.14 ?  96  MET C CG    1 
ATOM   7587 S SD    . MET D 1 104 ? -10.710 8.273   -23.579 1.00 42.71 ?  96  MET C SD    1 
ATOM   7588 C CE    . MET D 1 104 ? -9.169  9.013   -23.054 1.00 53.15 ?  96  MET C CE    1 
ATOM   7589 N N     . PRO D 1 105 ? -12.318 13.006  -26.269 1.00 39.24 ?  97  PRO C N     1 
ATOM   7590 C CA    . PRO D 1 105 ? -13.077 13.055  -27.525 1.00 39.69 ?  97  PRO C CA    1 
ATOM   7591 C C     . PRO D 1 105 ? -13.295 11.654  -28.073 1.00 41.06 ?  97  PRO C C     1 
ATOM   7592 O O     . PRO D 1 105 ? -12.442 10.776  -27.937 1.00 44.07 ?  97  PRO C O     1 
ATOM   7593 C CB    . PRO D 1 105 ? -12.194 13.895  -28.457 1.00 43.00 ?  97  PRO C CB    1 
ATOM   7594 C CG    . PRO D 1 105 ? -11.077 14.429  -27.636 1.00 44.88 ?  97  PRO C CG    1 
ATOM   7595 C CD    . PRO D 1 105 ? -11.025 13.710  -26.337 1.00 34.70 ?  97  PRO C CD    1 
ATOM   7596 N N     . GLU D 1 106 ? -14.456 11.449  -28.699 1.00 42.83 ?  98  GLU C N     1 
ATOM   7597 C CA    . GLU D 1 106 ? -14.739 10.169  -29.339 1.00 41.62 ?  98  GLU C CA    1 
ATOM   7598 C C     . GLU D 1 106 ? -13.728 9.824   -30.425 1.00 44.66 ?  98  GLU C C     1 
ATOM   7599 O O     . GLU D 1 106 ? -13.714 8.683   -30.901 1.00 42.40 ?  98  GLU C O     1 
ATOM   7600 C CB    . GLU D 1 106 ? -16.152 10.181  -29.926 1.00 40.37 ?  98  GLU C CB    1 
ATOM   7601 C CG    . GLU D 1 106 ? -16.303 11.090  -31.134 1.00 45.60 ?  98  GLU C CG    1 
ATOM   7602 C CD    . GLU D 1 106 ? -17.734 11.535  -31.365 1.00 47.90 ?  98  GLU C CD    1 
ATOM   7603 O OE1   . GLU D 1 106 ? -18.646 10.987  -30.710 1.00 46.57 ?  98  GLU C OE1   1 
ATOM   7604 O OE2   . GLU D 1 106 ? -17.948 12.434  -32.205 1.00 51.81 ?  98  GLU C OE2   1 
ATOM   7605 N N     . THR D 1 107 ? -12.880 10.777  -30.816 1.00 44.04 ?  99  THR C N     1 
ATOM   7606 C CA    . THR D 1 107 ? -11.865 10.574  -31.841 1.00 42.25 ?  99  THR C CA    1 
ATOM   7607 C C     . THR D 1 107 ? -10.741 9.641   -31.404 1.00 46.95 ?  99  THR C C     1 
ATOM   7608 O O     . THR D 1 107 ? -9.931  9.246   -32.249 1.00 47.11 ?  99  THR C O     1 
ATOM   7609 C CB    . THR D 1 107 ? -11.284 11.931  -32.252 1.00 37.88 ?  99  THR C CB    1 
ATOM   7610 O OG1   . THR D 1 107 ? -10.731 11.845  -33.570 1.00 54.13 ?  99  THR C OG1   1 
ATOM   7611 C CG2   . THR D 1 107 ? -10.204 12.378  -31.272 1.00 45.23 ?  99  THR C CG2   1 
ATOM   7612 N N     . MET D 1 108 ? -10.669 9.277   -30.126 1.00 47.38 ?  100 MET C N     1 
ATOM   7613 C CA    . MET D 1 108 ? -9.561  8.461   -29.648 1.00 43.60 ?  100 MET C CA    1 
ATOM   7614 C C     . MET D 1 108 ? -9.635  7.049   -30.217 1.00 43.77 ?  100 MET C C     1 
ATOM   7615 O O     . MET D 1 108 ? -10.715 6.486   -30.410 1.00 43.66 ?  100 MET C O     1 
ATOM   7616 C CB    . MET D 1 108 ? -9.551  8.414   -28.121 1.00 45.50 ?  100 MET C CB    1 
ATOM   7617 C CG    . MET D 1 108 ? -9.472  9.785   -27.479 1.00 43.81 ?  100 MET C CG    1 
ATOM   7618 S SD    . MET D 1 108 ? -7.893  10.611  -27.758 1.00 54.96 ?  100 MET C SD    1 
ATOM   7619 C CE    . MET D 1 108 ? -6.736  9.345   -27.239 1.00 51.35 ?  100 MET C CE    1 
ATOM   7620 N N     . SER D 1 109 ? -8.463  6.480   -30.485 1.00 49.58 ?  101 SER C N     1 
ATOM   7621 C CA    . SER D 1 109 ? -8.376  5.179   -31.131 1.00 42.65 ?  101 SER C CA    1 
ATOM   7622 C C     . SER D 1 109 ? -8.908  4.075   -30.224 1.00 45.54 ?  101 SER C C     1 
ATOM   7623 O O     . SER D 1 109 ? -8.826  4.153   -28.996 1.00 40.61 ?  101 SER C O     1 
ATOM   7624 C CB    . SER D 1 109 ? -6.929  4.871   -31.517 1.00 45.48 ?  101 SER C CB    1 
ATOM   7625 O OG    . SER D 1 109 ? -6.120  4.716   -30.364 1.00 38.23 ?  101 SER C OG    1 
ATOM   7626 N N     . GLN D 1 110 ? -9.453  3.029   -30.854 1.00 44.85 ?  102 GLN C N     1 
ATOM   7627 C CA    . GLN D 1 110 ? -9.938  1.873   -30.108 1.00 44.37 ?  102 GLN C CA    1 
ATOM   7628 C C     . GLN D 1 110 ? -8.832  1.237   -29.276 1.00 46.77 ?  102 GLN C C     1 
ATOM   7629 O O     . GLN D 1 110 ? -9.100  0.704   -28.192 1.00 44.51 ?  102 GLN C O     1 
ATOM   7630 C CB    . GLN D 1 110 ? -10.535 0.845   -31.070 1.00 48.34 ?  102 GLN C CB    1 
ATOM   7631 C CG    . GLN D 1 110 ? -11.165 -0.364  -30.396 1.00 48.59 ?  102 GLN C CG    1 
ATOM   7632 C CD    . GLN D 1 110 ? -12.341 0.004   -29.512 1.00 53.75 ?  102 GLN C CD    1 
ATOM   7633 O OE1   . GLN D 1 110 ? -13.226 0.759   -29.919 1.00 53.58 ?  102 GLN C OE1   1 
ATOM   7634 N NE2   . GLN D 1 110 ? -12.359 -0.531  -28.297 1.00 50.21 ?  102 GLN C NE2   1 
ATOM   7635 N N     . GLU D 1 111 ? -7.589  1.279   -29.762 1.00 41.36 ?  103 GLU C N     1 
ATOM   7636 C CA    . GLU D 1 111 ? -6.481  0.721   -28.994 1.00 44.56 ?  103 GLU C CA    1 
ATOM   7637 C C     . GLU D 1 111 ? -6.287  1.471   -27.682 1.00 45.23 ?  103 GLU C C     1 
ATOM   7638 O O     . GLU D 1 111 ? -6.063  0.856   -26.633 1.00 46.93 ?  103 GLU C O     1 
ATOM   7639 C CB    . GLU D 1 111 ? -5.198  0.749   -29.824 1.00 40.51 ?  103 GLU C CB    1 
ATOM   7640 N N     . ARG D 1 112 ? -6.378  2.803   -27.720 1.00 43.65 ?  104 ARG C N     1 
ATOM   7641 C CA    . ARG D 1 112 ? -6.235  3.586   -26.497 1.00 39.36 ?  104 ARG C CA    1 
ATOM   7642 C C     . ARG D 1 112 ? -7.396  3.335   -25.544 1.00 43.75 ?  104 ARG C C     1 
ATOM   7643 O O     . ARG D 1 112 ? -7.205  3.285   -24.323 1.00 39.43 ?  104 ARG C O     1 
ATOM   7644 C CB    . ARG D 1 112 ? -6.123  5.074   -26.831 1.00 38.62 ?  104 ARG C CB    1 
ATOM   7645 C CG    . ARG D 1 112 ? -5.850  5.974   -25.627 1.00 44.97 ?  104 ARG C CG    1 
ATOM   7646 C CD    . ARG D 1 112 ? -4.444  5.778   -25.072 1.00 47.76 ?  104 ARG C CD    1 
ATOM   7647 N NE    . ARG D 1 112 ? -3.504  5.317   -26.086 1.00 47.73 ?  104 ARG C NE    1 
ATOM   7648 C CZ    . ARG D 1 112 ? -2.445  6.002   -26.494 1.00 50.41 ?  104 ARG C CZ    1 
ATOM   7649 N NH1   . ARG D 1 112 ? -2.158  7.192   -25.993 1.00 50.21 ?  104 ARG C NH1   1 
ATOM   7650 N NH2   . ARG D 1 112 ? -1.654  5.480   -27.427 1.00 47.62 ?  104 ARG C NH2   1 
ATOM   7651 N N     . ARG D 1 113 ? -8.607  3.176   -26.082 1.00 40.33 ?  105 ARG C N     1 
ATOM   7652 C CA    . ARG D 1 113 ? -9.755  2.875   -25.233 1.00 41.58 ?  105 ARG C CA    1 
ATOM   7653 C C     . ARG D 1 113 ? -9.612  1.505   -24.583 1.00 38.91 ?  105 ARG C C     1 
ATOM   7654 O O     . ARG D 1 113 ? -9.989  1.321   -23.419 1.00 38.30 ?  105 ARG C O     1 
ATOM   7655 C CB    . ARG D 1 113 ? -11.048 2.953   -26.046 1.00 38.45 ?  105 ARG C CB    1 
ATOM   7656 C CG    . ARG D 1 113 ? -11.586 4.365   -26.238 1.00 45.18 ?  105 ARG C CG    1 
ATOM   7657 C CD    . ARG D 1 113 ? -11.594 4.752   -27.704 1.00 48.04 ?  105 ARG C CD    1 
ATOM   7658 N NE    . ARG D 1 113 ? -12.526 3.940   -28.475 1.00 49.78 ?  105 ARG C NE    1 
ATOM   7659 C CZ    . ARG D 1 113 ? -13.627 4.405   -29.048 1.00 57.04 ?  105 ARG C CZ    1 
ATOM   7660 N NH1   . ARG D 1 113 ? -13.951 5.686   -28.983 1.00 49.35 ?  105 ARG C NH1   1 
ATOM   7661 N NH2   . ARG D 1 113 ? -14.420 3.565   -29.708 1.00 64.78 ?  105 ARG C NH2   1 
ATOM   7662 N N     . ASN D 1 114 ? -9.066  0.532   -25.318 1.00 34.07 ?  106 ASN C N     1 
ATOM   7663 C CA    . ASN D 1 114 ? -8.845  -0.793  -24.748 1.00 39.72 ?  106 ASN C CA    1 
ATOM   7664 C C     . ASN D 1 114 ? -7.786  -0.753  -23.653 1.00 38.32 ?  106 ASN C C     1 
ATOM   7665 O O     . ASN D 1 114 ? -7.941  -1.393  -22.606 1.00 35.05 ?  106 ASN C O     1 
ATOM   7666 C CB    . ASN D 1 114 ? -8.441  -1.774  -25.848 1.00 43.75 ?  106 ASN C CB    1 
ATOM   7667 C CG    . ASN D 1 114 ? -9.580  -2.085  -26.798 1.00 48.58 ?  106 ASN C CG    1 
ATOM   7668 O OD1   . ASN D 1 114 ? -10.751 -1.918  -26.459 1.00 48.57 ?  106 ASN C OD1   1 
ATOM   7669 N ND2   . ASN D 1 114 ? -9.239  -2.539  -28.000 1.00 44.30 ?  106 ASN C ND2   1 
ATOM   7670 N N     . LEU D 1 115 ? -6.701  -0.009  -23.882 1.00 40.47 ?  107 LEU C N     1 
ATOM   7671 C CA    . LEU D 1 115 ? -5.657  0.134   -22.871 1.00 39.87 ?  107 LEU C CA    1 
ATOM   7672 C C     . LEU D 1 115 ? -6.221  0.701   -21.573 1.00 35.58 ?  107 LEU C C     1 
ATOM   7673 O O     . LEU D 1 115 ? -5.905  0.217   -20.479 1.00 35.20 ?  107 LEU C O     1 
ATOM   7674 C CB    . LEU D 1 115 ? -4.539  1.028   -23.410 1.00 36.65 ?  107 LEU C CB    1 
ATOM   7675 C CG    . LEU D 1 115 ? -3.375  1.385   -22.482 1.00 37.25 ?  107 LEU C CG    1 
ATOM   7676 C CD1   . LEU D 1 115 ? -2.870  0.169   -21.724 1.00 34.68 ?  107 LEU C CD1   1 
ATOM   7677 C CD2   . LEU D 1 115 ? -2.247  2.025   -23.278 1.00 35.60 ?  107 LEU C CD2   1 
ATOM   7678 N N     . LEU D 1 116 ? -7.063  1.729   -21.677 1.00 34.26 ?  108 LEU C N     1 
ATOM   7679 C CA    . LEU D 1 116 ? -7.614  2.356   -20.482 1.00 32.55 ?  108 LEU C CA    1 
ATOM   7680 C C     . LEU D 1 116 ? -8.622  1.445   -19.795 1.00 33.45 ?  108 LEU C C     1 
ATOM   7681 O O     . LEU D 1 116 ? -8.637  1.344   -18.563 1.00 31.97 ?  108 LEU C O     1 
ATOM   7682 C CB    . LEU D 1 116 ? -8.253  3.691   -20.850 1.00 35.41 ?  108 LEU C CB    1 
ATOM   7683 C CG    . LEU D 1 116 ? -7.242  4.741   -21.304 1.00 32.06 ?  108 LEU C CG    1 
ATOM   7684 C CD1   . LEU D 1 116 ? -7.937  5.850   -22.059 1.00 35.64 ?  108 LEU C CD1   1 
ATOM   7685 C CD2   . LEU D 1 116 ? -6.484  5.292   -20.110 1.00 34.81 ?  108 LEU C CD2   1 
ATOM   7686 N N     . LYS D 1 117 ? -9.469  0.769   -20.573 1.00 35.87 ?  109 LYS C N     1 
ATOM   7687 C CA    . LYS D 1 117 ? -10.435 -0.151  -19.988 1.00 30.28 ?  109 LYS C CA    1 
ATOM   7688 C C     . LYS D 1 117 ? -9.780  -1.412  -19.447 1.00 30.77 ?  109 LYS C C     1 
ATOM   7689 O O     . LYS D 1 117 ? -10.363 -2.072  -18.580 1.00 30.66 ?  109 LYS C O     1 
ATOM   7690 C CB    . LYS D 1 117 ? -11.504 -0.528  -21.014 1.00 35.41 ?  109 LYS C CB    1 
ATOM   7691 C CG    . LYS D 1 117 ? -12.466 0.594   -21.350 1.00 37.54 ?  109 LYS C CG    1 
ATOM   7692 C CD    . LYS D 1 117 ? -13.434 0.171   -22.444 1.00 37.16 ?  109 LYS C CD    1 
ATOM   7693 C CE    . LYS D 1 117 ? -14.384 1.299   -22.808 1.00 49.74 ?  109 LYS C CE    1 
ATOM   7694 N NZ    . LYS D 1 117 ? -15.799 0.993   -22.456 1.00 50.66 ?  109 LYS C NZ    1 
ATOM   7695 N N     . ALA D 1 118 ? -8.590  -1.768  -19.938 1.00 33.92 ?  110 ALA C N     1 
ATOM   7696 C CA    . ALA D 1 118 ? -7.897  -2.933  -19.401 1.00 29.42 ?  110 ALA C CA    1 
ATOM   7697 C C     . ALA D 1 118 ? -7.557  -2.749  -17.928 1.00 33.25 ?  110 ALA C C     1 
ATOM   7698 O O     . ALA D 1 118 ? -7.501  -3.728  -17.176 1.00 29.32 ?  110 ALA C O     1 
ATOM   7699 C CB    . ALA D 1 118 ? -6.632  -3.213  -20.210 1.00 31.99 ?  110 ALA C CB    1 
ATOM   7700 N N     . TYR D 1 119 ? -7.329  -1.509  -17.499 1.00 28.30 ?  111 TYR C N     1 
ATOM   7701 C CA    . TYR D 1 119 ? -7.109  -1.206  -16.092 1.00 29.68 ?  111 TYR C CA    1 
ATOM   7702 C C     . TYR D 1 119 ? -8.406  -1.062  -15.306 1.00 32.19 ?  111 TYR C C     1 
ATOM   7703 O O     . TYR D 1 119 ? -8.354  -0.741  -14.114 1.00 31.50 ?  111 TYR C O     1 
ATOM   7704 C CB    . TYR D 1 119 ? -6.285  0.076   -15.954 1.00 30.82 ?  111 TYR C CB    1 
ATOM   7705 C CG    . TYR D 1 119 ? -4.809  -0.102  -16.226 1.00 30.37 ?  111 TYR C CG    1 
ATOM   7706 C CD1   . TYR D 1 119 ? -4.042  -0.980  -15.471 1.00 27.46 ?  111 TYR C CD1   1 
ATOM   7707 C CD2   . TYR D 1 119 ? -4.182  0.614   -17.237 1.00 27.00 ?  111 TYR C CD2   1 
ATOM   7708 C CE1   . TYR D 1 119 ? -2.689  -1.141  -15.718 1.00 28.38 ?  111 TYR C CE1   1 
ATOM   7709 C CE2   . TYR D 1 119 ? -2.834  0.460   -17.491 1.00 29.45 ?  111 TYR C CE2   1 
ATOM   7710 C CZ    . TYR D 1 119 ? -2.091  -0.416  -16.730 1.00 29.39 ?  111 TYR C CZ    1 
ATOM   7711 O OH    . TYR D 1 119 ? -0.747  -0.564  -16.988 1.00 28.39 ?  111 TYR C OH    1 
ATOM   7712 N N     . GLY D 1 120 ? -9.556  -1.287  -15.935 1.00 27.75 ?  112 GLY C N     1 
ATOM   7713 C CA    . GLY D 1 120 ? -10.832 -1.126  -15.273 1.00 30.29 ?  112 GLY C CA    1 
ATOM   7714 C C     . GLY D 1 120 ? -11.396 0.276   -15.297 1.00 33.19 ?  112 GLY C C     1 
ATOM   7715 O O     . GLY D 1 120 ? -12.384 0.540   -14.601 1.00 31.58 ?  112 GLY C O     1 
ATOM   7716 N N     . ALA D 1 121 ? -10.808 1.180   -16.073 1.00 31.77 ?  113 ALA C N     1 
ATOM   7717 C CA    . ALA D 1 121 ? -11.295 2.549   -16.118 1.00 34.78 ?  113 ALA C CA    1 
ATOM   7718 C C     . ALA D 1 121 ? -12.590 2.642   -16.917 1.00 36.12 ?  113 ALA C C     1 
ATOM   7719 O O     . ALA D 1 121 ? -12.849 1.847   -17.826 1.00 33.63 ?  113 ALA C O     1 
ATOM   7720 C CB    . ALA D 1 121 ? -10.240 3.470   -16.728 1.00 32.80 ?  113 ALA C CB    1 
ATOM   7721 N N     . GLU D 1 122 ? -13.410 3.625   -16.559 1.00 39.90 ?  114 GLU C N     1 
ATOM   7722 C CA    . GLU D 1 122 ? -14.626 3.949   -17.290 1.00 40.44 ?  114 GLU C CA    1 
ATOM   7723 C C     . GLU D 1 122 ? -14.360 5.133   -18.208 1.00 37.60 ?  114 GLU C C     1 
ATOM   7724 O O     . GLU D 1 122 ? -13.678 6.089   -17.825 1.00 36.63 ?  114 GLU C O     1 
ATOM   7725 C CB    . GLU D 1 122 ? -15.775 4.274   -16.333 1.00 43.20 ?  114 GLU C CB    1 
ATOM   7726 C CG    . GLU D 1 122 ? -17.106 3.649   -16.729 1.00 63.43 ?  114 GLU C CG    1 
ATOM   7727 C CD    . GLU D 1 122 ? -18.292 4.297   -16.034 1.00 72.55 ?  114 GLU C CD    1 
ATOM   7728 O OE1   . GLU D 1 122 ? -19.197 4.795   -16.739 1.00 67.85 ?  114 GLU C OE1   1 
ATOM   7729 O OE2   . GLU D 1 122 ? -18.320 4.309   -14.785 1.00 68.39 ?  114 GLU C OE2   1 
ATOM   7730 N N     . LEU D 1 123 ? -14.899 5.067   -19.421 1.00 36.06 ?  115 LEU C N     1 
ATOM   7731 C CA    . LEU D 1 123 ? -14.645 6.072   -20.443 1.00 36.96 ?  115 LEU C CA    1 
ATOM   7732 C C     . LEU D 1 123 ? -15.939 6.791   -20.794 1.00 41.13 ?  115 LEU C C     1 
ATOM   7733 O O     . LEU D 1 123 ? -16.937 6.152   -21.144 1.00 36.75 ?  115 LEU C O     1 
ATOM   7734 C CB    . LEU D 1 123 ? -14.030 5.437   -21.692 1.00 36.10 ?  115 LEU C CB    1 
ATOM   7735 C CG    . LEU D 1 123 ? -12.768 4.608   -21.445 1.00 41.68 ?  115 LEU C CG    1 
ATOM   7736 C CD1   . LEU D 1 123 ? -12.179 4.139   -22.756 1.00 35.95 ?  115 LEU C CD1   1 
ATOM   7737 C CD2   . LEU D 1 123 ? -11.740 5.402   -20.650 1.00 32.78 ?  115 LEU C CD2   1 
ATOM   7738 N N     . VAL D 1 124 ? -15.915 8.115   -20.691 1.00 39.33 ?  116 VAL C N     1 
ATOM   7739 C CA    . VAL D 1 124 ? -17.030 8.968   -21.080 1.00 38.25 ?  116 VAL C CA    1 
ATOM   7740 C C     . VAL D 1 124 ? -16.567 9.745   -22.304 1.00 42.77 ?  116 VAL C C     1 
ATOM   7741 O O     . VAL D 1 124 ? -15.784 10.696  -22.192 1.00 41.87 ?  116 VAL C O     1 
ATOM   7742 C CB    . VAL D 1 124 ? -17.464 9.905   -19.947 1.00 42.48 ?  116 VAL C CB    1 
ATOM   7743 C CG1   . VAL D 1 124 ? -18.532 10.872  -20.439 1.00 42.89 ?  116 VAL C CG1   1 
ATOM   7744 C CG2   . VAL D 1 124 ? -17.965 9.105   -18.756 1.00 45.66 ?  116 VAL C CG2   1 
ATOM   7745 N N     . LEU D 1 125 ? -17.039 9.336   -23.478 1.00 41.15 ?  117 LEU C N     1 
ATOM   7746 C CA    . LEU D 1 125 ? -16.619 9.958   -24.724 1.00 42.24 ?  117 LEU C CA    1 
ATOM   7747 C C     . LEU D 1 125 ? -17.349 11.277  -24.940 1.00 40.13 ?  117 LEU C C     1 
ATOM   7748 O O     . LEU D 1 125 ? -18.523 11.422  -24.588 1.00 41.90 ?  117 LEU C O     1 
ATOM   7749 C CB    . LEU D 1 125 ? -16.879 9.018   -25.898 1.00 44.30 ?  117 LEU C CB    1 
ATOM   7750 C CG    . LEU D 1 125 ? -16.208 7.645   -25.816 1.00 45.37 ?  117 LEU C CG    1 
ATOM   7751 C CD1   . LEU D 1 125 ? -16.363 6.902   -27.130 1.00 48.18 ?  117 LEU C CD1   1 
ATOM   7752 C CD2   . LEU D 1 125 ? -14.738 7.780   -25.445 1.00 43.95 ?  117 LEU C CD2   1 
ATOM   7753 N N     . THR D 1 126 ? -16.643 12.236  -25.522 1.00 38.78 ?  118 THR C N     1 
ATOM   7754 C CA    . THR D 1 126 ? -17.159 13.557  -25.830 1.00 41.36 ?  118 THR C CA    1 
ATOM   7755 C C     . THR D 1 126 ? -17.093 13.792  -27.334 1.00 42.08 ?  118 THR C C     1 
ATOM   7756 O O     . THR D 1 126 ? -16.351 13.101  -28.044 1.00 41.37 ?  118 THR C O     1 
ATOM   7757 C CB    . THR D 1 126 ? -16.360 14.637  -25.082 1.00 42.35 ?  118 THR C CB    1 
ATOM   7758 O OG1   . THR D 1 126 ? -14.979 14.559  -25.451 1.00 36.80 ?  118 THR C OG1   1 
ATOM   7759 C CG2   . THR D 1 126 ? -16.489 14.444  -23.577 1.00 41.82 ?  118 THR C CG2   1 
ATOM   7760 N N     . PRO D 1 127 ? -17.875 14.738  -27.860 1.00 45.37 ?  119 PRO C N     1 
ATOM   7761 C CA    . PRO D 1 127 ? -17.896 14.956  -29.314 1.00 48.06 ?  119 PRO C CA    1 
ATOM   7762 C C     . PRO D 1 127 ? -16.507 15.242  -29.871 1.00 44.27 ?  119 PRO C C     1 
ATOM   7763 O O     . PRO D 1 127 ? -15.737 16.021  -29.303 1.00 43.94 ?  119 PRO C O     1 
ATOM   7764 C CB    . PRO D 1 127 ? -18.825 16.163  -29.473 1.00 46.97 ?  119 PRO C CB    1 
ATOM   7765 C CG    . PRO D 1 127 ? -19.751 16.060  -28.313 1.00 43.33 ?  119 PRO C CG    1 
ATOM   7766 C CD    . PRO D 1 127 ? -18.908 15.540  -27.177 1.00 46.67 ?  119 PRO C CD    1 
ATOM   7767 N N     . GLY D 1 128 ? -16.191 14.593  -30.995 1.00 43.05 ?  120 GLY C N     1 
ATOM   7768 C CA    . GLY D 1 128 ? -14.889 14.788  -31.612 1.00 42.69 ?  120 GLY C CA    1 
ATOM   7769 C C     . GLY D 1 128 ? -14.688 16.190  -32.150 1.00 47.80 ?  120 GLY C C     1 
ATOM   7770 O O     . GLY D 1 128 ? -13.557 16.682  -32.203 1.00 50.33 ?  120 GLY C O     1 
ATOM   7771 N N     . SER D 1 129 ? -15.774 16.852  -32.558 1.00 47.31 ?  121 SER C N     1 
ATOM   7772 C CA    . SER D 1 129 ? -15.689 18.220  -33.051 1.00 44.39 ?  121 SER C CA    1 
ATOM   7773 C C     . SER D 1 129 ? -15.398 19.223  -31.945 1.00 42.61 ?  121 SER C C     1 
ATOM   7774 O O     . SER D 1 129 ? -15.021 20.360  -32.247 1.00 38.13 ?  121 SER C O     1 
ATOM   7775 C CB    . SER D 1 129 ? -16.986 18.600  -33.760 1.00 41.55 ?  121 SER C CB    1 
ATOM   7776 O OG    . SER D 1 129 ? -18.010 18.870  -32.820 1.00 43.13 ?  121 SER C OG    1 
ATOM   7777 N N     . GLU D 1 130 ? -15.557 18.834  -30.681 1.00 47.17 ?  122 GLU C N     1 
ATOM   7778 C CA    . GLU D 1 130 ? -15.247 19.711  -29.562 1.00 43.63 ?  122 GLU C CA    1 
ATOM   7779 C C     . GLU D 1 130 ? -13.852 19.488  -28.987 1.00 40.79 ?  122 GLU C C     1 
ATOM   7780 O O     . GLU D 1 130 ? -13.409 20.300  -28.168 1.00 41.27 ?  122 GLU C O     1 
ATOM   7781 C CB    . GLU D 1 130 ? -16.286 19.537  -28.449 1.00 39.68 ?  122 GLU C CB    1 
ATOM   7782 C CG    . GLU D 1 130 ? -17.676 20.018  -28.833 1.00 43.03 ?  122 GLU C CG    1 
ATOM   7783 C CD    . GLU D 1 130 ? -17.674 21.437  -29.367 1.00 50.77 ?  122 GLU C CD    1 
ATOM   7784 O OE1   . GLU D 1 130 ? -17.133 22.331  -28.682 1.00 54.73 ?  122 GLU C OE1   1 
ATOM   7785 O OE2   . GLU D 1 130 ? -18.202 21.656  -30.479 1.00 51.58 ?  122 GLU C OE2   1 
ATOM   7786 N N     . ALA D 1 131 ? -13.159 18.416  -29.385 1.00 45.18 ?  123 ALA C N     1 
ATOM   7787 C CA    . ALA D 1 131 ? -11.809 18.128  -28.914 1.00 41.10 ?  123 ALA C CA    1 
ATOM   7788 C C     . ALA D 1 131 ? -11.682 18.127  -27.395 1.00 43.86 ?  123 ALA C C     1 
ATOM   7789 O O     . ALA D 1 131 ? -12.532 17.582  -26.675 1.00 42.74 ?  123 ALA C O     1 
ATOM   7790 C CB    . ALA D 1 131 ? -10.801 19.116  -29.494 1.00 36.87 ?  123 ALA C CB    1 
ATOM   7791 N N     . MET D 1 132 ? -10.604 18.746  -26.909 1.00 37.97 ?  124 MET C N     1 
ATOM   7792 C CA    . MET D 1 132 ? -10.341 18.798  -25.482 1.00 42.98 ?  124 MET C CA    1 
ATOM   7793 C C     . MET D 1 132 ? -11.279 19.750  -24.758 1.00 43.59 ?  124 MET C C     1 
ATOM   7794 O O     . MET D 1 132 ? -11.509 19.570  -23.557 1.00 37.20 ?  124 MET C O     1 
ATOM   7795 C CB    . MET D 1 132 ? -8.883  19.189  -25.241 1.00 42.35 ?  124 MET C CB    1 
ATOM   7796 C CG    . MET D 1 132 ? -7.889  18.087  -25.600 1.00 48.29 ?  124 MET C CG    1 
ATOM   7797 S SD    . MET D 1 132 ? -8.445  16.413  -25.178 1.00 46.58 ?  124 MET C SD    1 
ATOM   7798 C CE    . MET D 1 132 ? -8.498  16.464  -23.383 1.00 39.92 ?  124 MET C CE    1 
ATOM   7799 N N     . LYS D 1 133 ? -11.841 20.740  -25.457 1.00 43.25 ?  125 LYS C N     1 
ATOM   7800 C CA    . LYS D 1 133 ? -12.791 21.635  -24.805 1.00 38.65 ?  125 LYS C CA    1 
ATOM   7801 C C     . LYS D 1 133 ? -14.020 20.874  -24.329 1.00 39.43 ?  125 LYS C C     1 
ATOM   7802 O O     . LYS D 1 133 ? -14.501 21.096  -23.212 1.00 38.62 ?  125 LYS C O     1 
ATOM   7803 C CB    . LYS D 1 133 ? -13.195 22.767  -25.750 1.00 49.83 ?  125 LYS C CB    1 
ATOM   7804 N N     . GLY D 1 134 ? -14.537 19.964  -25.158 1.00 36.89 ?  126 GLY C N     1 
ATOM   7805 C CA    . GLY D 1 134 ? -15.672 19.161  -24.740 1.00 37.08 ?  126 GLY C CA    1 
ATOM   7806 C C     . GLY D 1 134 ? -15.318 18.144  -23.676 1.00 41.05 ?  126 GLY C C     1 
ATOM   7807 O O     . GLY D 1 134 ? -16.151 17.811  -22.827 1.00 37.80 ?  126 GLY C O     1 
ATOM   7808 N N     . ALA D 1 135 ? -14.081 17.640  -23.700 1.00 41.58 ?  127 ALA C N     1 
ATOM   7809 C CA    . ALA D 1 135 ? -13.644 16.692  -22.682 1.00 36.38 ?  127 ALA C CA    1 
ATOM   7810 C C     . ALA D 1 135 ? -13.536 17.357  -21.317 1.00 41.04 ?  127 ALA C C     1 
ATOM   7811 O O     . ALA D 1 135 ? -13.909 16.762  -20.299 1.00 39.66 ?  127 ALA C O     1 
ATOM   7812 C CB    . ALA D 1 135 ? -12.308 16.070  -23.087 1.00 38.32 ?  127 ALA C CB    1 
ATOM   7813 N N     . ILE D 1 136 ? -13.023 18.589  -21.274 1.00 39.29 ?  128 ILE C N     1 
ATOM   7814 C CA    . ILE D 1 136 ? -12.950 19.321  -20.013 1.00 40.55 ?  128 ILE C CA    1 
ATOM   7815 C C     . ILE D 1 136 ? -14.350 19.615  -19.489 1.00 43.40 ?  128 ILE C C     1 
ATOM   7816 O O     . ILE D 1 136 ? -14.621 19.482  -18.289 1.00 41.81 ?  128 ILE C O     1 
ATOM   7817 C CB    . ILE D 1 136 ? -12.130 20.612  -20.192 1.00 40.71 ?  128 ILE C CB    1 
ATOM   7818 C CG1   . ILE D 1 136 ? -10.649 20.285  -20.378 1.00 40.88 ?  128 ILE C CG1   1 
ATOM   7819 C CG2   . ILE D 1 136 ? -12.326 21.547  -19.008 1.00 32.05 ?  128 ILE C CG2   1 
ATOM   7820 C CD1   . ILE D 1 136 ? -9.849  21.425  -20.959 1.00 39.34 ?  128 ILE C CD1   1 
ATOM   7821 N N     . LYS D 1 137 ? -15.262 20.005  -20.385 1.00 43.22 ?  129 LYS C N     1 
ATOM   7822 C CA    . LYS D 1 137 ? -16.613 20.374  -19.973 1.00 39.96 ?  129 LYS C CA    1 
ATOM   7823 C C     . LYS D 1 137 ? -17.332 19.202  -19.316 1.00 43.92 ?  129 LYS C C     1 
ATOM   7824 O O     . LYS D 1 137 ? -17.946 19.353  -18.253 1.00 45.31 ?  129 LYS C O     1 
ATOM   7825 C CB    . LYS D 1 137 ? -17.405 20.882  -21.179 1.00 41.74 ?  129 LYS C CB    1 
ATOM   7826 C CG    . LYS D 1 137 ? -18.908 20.960  -20.953 1.00 49.16 ?  129 LYS C CG    1 
ATOM   7827 C CD    . LYS D 1 137 ? -19.579 21.862  -21.979 1.00 48.99 ?  129 LYS C CD    1 
ATOM   7828 C CE    . LYS D 1 137 ? -21.075 21.967  -21.726 1.00 52.89 ?  129 LYS C CE    1 
ATOM   7829 N NZ    . LYS D 1 137 ? -21.760 20.656  -21.905 1.00 50.44 ?  129 LYS C NZ    1 
ATOM   7830 N N     . LYS D 1 138 ? -17.269 18.023  -19.938 1.00 39.53 ?  130 LYS C N     1 
ATOM   7831 C CA    . LYS D 1 138 ? -17.922 16.853  -19.361 1.00 43.46 ?  130 LYS C CA    1 
ATOM   7832 C C     . LYS D 1 138 ? -17.282 16.450  -18.040 1.00 41.70 ?  130 LYS C C     1 
ATOM   7833 O O     . LYS D 1 138 ? -17.976 15.977  -17.134 1.00 41.57 ?  130 LYS C O     1 
ATOM   7834 C CB    . LYS D 1 138 ? -17.883 15.686  -20.348 1.00 38.84 ?  130 LYS C CB    1 
ATOM   7835 C CG    . LYS D 1 138 ? -18.630 14.450  -19.876 1.00 40.25 ?  130 LYS C CG    1 
ATOM   7836 C CD    . LYS D 1 138 ? -20.102 14.746  -19.645 1.00 43.54 ?  130 LYS C CD    1 
ATOM   7837 N N     . ALA D 1 139 ? -15.966 16.635  -17.909 1.00 37.54 ?  131 ALA C N     1 
ATOM   7838 C CA    . ALA D 1 139 ? -15.290 16.275  -16.668 1.00 38.91 ?  131 ALA C CA    1 
ATOM   7839 C C     . ALA D 1 139 ? -15.776 17.131  -15.506 1.00 41.90 ?  131 ALA C C     1 
ATOM   7840 O O     . ALA D 1 139 ? -16.014 16.620  -14.406 1.00 42.24 ?  131 ALA C O     1 
ATOM   7841 C CB    . ALA D 1 139 ? -13.777 16.406  -16.838 1.00 36.23 ?  131 ALA C CB    1 
ATOM   7842 N N     . LYS D 1 140 ? -15.934 18.437  -15.731 1.00 44.09 ?  132 LYS C N     1 
ATOM   7843 C CA    . LYS D 1 140 ? -16.420 19.306  -14.666 1.00 47.45 ?  132 LYS C CA    1 
ATOM   7844 C C     . LYS D 1 140 ? -17.900 19.081  -14.390 1.00 46.75 ?  132 LYS C C     1 
ATOM   7845 O O     . LYS D 1 140 ? -18.363 19.324  -13.271 1.00 46.15 ?  132 LYS C O     1 
ATOM   7846 C CB    . LYS D 1 140 ? -16.152 20.768  -15.016 1.00 45.83 ?  132 LYS C CB    1 
ATOM   7847 C CG    . LYS D 1 140 ? -14.719 21.035  -15.435 1.00 50.91 ?  132 LYS C CG    1 
ATOM   7848 C CD    . LYS D 1 140 ? -14.177 22.293  -14.782 1.00 53.95 ?  132 LYS C CD    1 
ATOM   7849 C CE    . LYS D 1 140 ? -12.658 22.333  -14.846 1.00 53.76 ?  132 LYS C CE    1 
ATOM   7850 N NZ    . LYS D 1 140 ? -12.028 21.824  -13.595 1.00 51.12 ?  132 LYS C NZ    1 
ATOM   7851 N N     . GLU D 1 141 ? -18.657 18.621  -15.389 1.00 43.11 ?  133 GLU C N     1 
ATOM   7852 C CA    . GLU D 1 141 ? -20.042 18.231  -15.143 1.00 46.30 ?  133 GLU C CA    1 
ATOM   7853 C C     . GLU D 1 141 ? -20.107 17.028  -14.212 1.00 48.87 ?  133 GLU C C     1 
ATOM   7854 O O     . GLU D 1 141 ? -20.882 17.013  -13.249 1.00 51.96 ?  133 GLU C O     1 
ATOM   7855 C CB    . GLU D 1 141 ? -20.749 17.923  -16.464 1.00 46.32 ?  133 GLU C CB    1 
ATOM   7856 C CG    . GLU D 1 141 ? -21.618 19.053  -16.982 1.00 49.41 ?  133 GLU C CG    1 
ATOM   7857 C CD    . GLU D 1 141 ? -21.500 19.238  -18.482 1.00 53.65 ?  133 GLU C CD    1 
ATOM   7858 O OE1   . GLU D 1 141 ? -21.326 18.226  -19.194 1.00 53.34 ?  133 GLU C OE1   1 
ATOM   7859 O OE2   . GLU D 1 141 ? -21.590 20.393  -18.949 1.00 48.72 ?  133 GLU C OE2   1 
ATOM   7860 N N     . LEU D 1 142 ? -19.292 16.006  -14.485 1.00 42.70 ?  134 LEU C N     1 
ATOM   7861 C CA    . LEU D 1 142 ? -19.244 14.842  -13.609 1.00 50.54 ?  134 LEU C CA    1 
ATOM   7862 C C     . LEU D 1 142 ? -18.669 15.195  -12.243 1.00 47.03 ?  134 LEU C C     1 
ATOM   7863 O O     . LEU D 1 142 ? -19.030 14.568  -11.240 1.00 48.08 ?  134 LEU C O     1 
ATOM   7864 C CB    . LEU D 1 142 ? -18.427 13.732  -14.267 1.00 47.25 ?  134 LEU C CB    1 
ATOM   7865 C CG    . LEU D 1 142 ? -18.917 13.292  -15.648 1.00 44.73 ?  134 LEU C CG    1 
ATOM   7866 C CD1   . LEU D 1 142 ? -17.932 12.329  -16.291 1.00 43.49 ?  134 LEU C CD1   1 
ATOM   7867 C CD2   . LEU D 1 142 ? -20.303 12.673  -15.563 1.00 41.69 ?  134 LEU C CD2   1 
ATOM   7868 N N     . LYS D 1 143 ? -17.780 16.188  -12.183 1.00 45.21 ?  135 LYS C N     1 
ATOM   7869 C CA    . LYS D 1 143 ? -17.251 16.644  -10.901 1.00 48.88 ?  135 LYS C CA    1 
ATOM   7870 C C     . LYS D 1 143 ? -18.365 17.186  -10.013 1.00 49.51 ?  135 LYS C C     1 
ATOM   7871 O O     . LYS D 1 143 ? -18.569 16.716  -8.888  1.00 50.71 ?  135 LYS C O     1 
ATOM   7872 C CB    . LYS D 1 143 ? -16.182 17.712  -11.129 1.00 47.83 ?  135 LYS C CB    1 
ATOM   7873 C CG    . LYS D 1 143 ? -15.269 17.948  -9.938  1.00 49.34 ?  135 LYS C CG    1 
ATOM   7874 C CD    . LYS D 1 143 ? -14.747 19.377  -9.940  1.00 46.15 ?  135 LYS C CD    1 
ATOM   7875 C CE    . LYS D 1 143 ? -13.230 19.428  -9.963  1.00 42.65 ?  135 LYS C CE    1 
ATOM   7876 N NZ    . LYS D 1 143 ? -12.646 19.362  -8.595  1.00 51.24 ?  135 LYS C NZ    1 
ATOM   7877 N N     . GLU D 1 144 ? -19.101 18.182  -10.512 1.00 51.50 ?  136 GLU C N     1 
ATOM   7878 C CA    . GLU D 1 144 ? -20.139 18.820  -9.708  1.00 52.30 ?  136 GLU C CA    1 
ATOM   7879 C C     . GLU D 1 144 ? -21.334 17.901  -9.481  1.00 50.30 ?  136 GLU C C     1 
ATOM   7880 O O     . GLU D 1 144 ? -21.966 17.964  -8.421  1.00 51.00 ?  136 GLU C O     1 
ATOM   7881 C CB    . GLU D 1 144 ? -20.596 20.118  -10.376 1.00 55.27 ?  136 GLU C CB    1 
ATOM   7882 C CG    . GLU D 1 144 ? -19.466 21.052  -10.782 1.00 60.34 ?  136 GLU C CG    1 
ATOM   7883 C CD    . GLU D 1 144 ? -19.789 21.860  -12.028 1.00 66.47 ?  136 GLU C CD    1 
ATOM   7884 O OE1   . GLU D 1 144 ? -20.946 21.804  -12.500 1.00 68.46 ?  136 GLU C OE1   1 
ATOM   7885 O OE2   . GLU D 1 144 ? -18.881 22.551  -12.537 1.00 69.18 ?  136 GLU C OE2   1 
ATOM   7886 N N     . GLU D 1 145 ? -21.658 17.046  -10.452 1.00 49.03 ?  137 GLU C N     1 
ATOM   7887 C CA    . GLU D 1 145 ? -22.863 16.230  -10.349 1.00 50.95 ?  137 GLU C CA    1 
ATOM   7888 C C     . GLU D 1 145 ? -22.665 14.999  -9.473  1.00 54.69 ?  137 GLU C C     1 
ATOM   7889 O O     . GLU D 1 145 ? -23.604 14.580  -8.787  1.00 53.41 ?  137 GLU C O     1 
ATOM   7890 C CB    . GLU D 1 145 ? -23.334 15.803  -11.741 1.00 47.93 ?  137 GLU C CB    1 
ATOM   7891 N N     . HIS D 1 146 ? -21.471 14.408  -9.477  1.00 53.10 ?  138 HIS C N     1 
ATOM   7892 C CA    . HIS D 1 146 ? -21.245 13.140  -8.797  1.00 47.45 ?  138 HIS C CA    1 
ATOM   7893 C C     . HIS D 1 146 ? -20.211 13.208  -7.682  1.00 48.31 ?  138 HIS C C     1 
ATOM   7894 O O     . HIS D 1 146 ? -19.993 12.199  -7.002  1.00 41.35 ?  138 HIS C O     1 
ATOM   7895 C CB    . HIS D 1 146 ? -20.827 12.067  -9.812  1.00 48.46 ?  138 HIS C CB    1 
ATOM   7896 C CG    . HIS D 1 146 ? -21.921 11.667  -10.752 1.00 46.90 ?  138 HIS C CG    1 
ATOM   7897 N ND1   . HIS D 1 146 ? -21.827 10.570  -11.580 1.00 53.67 ?  138 HIS C ND1   1 
ATOM   7898 C CD2   . HIS D 1 146 ? -23.135 12.218  -10.993 1.00 59.35 ?  138 HIS C CD2   1 
ATOM   7899 C CE1   . HIS D 1 146 ? -22.934 10.463  -12.293 1.00 64.25 ?  138 HIS C CE1   1 
ATOM   7900 N NE2   . HIS D 1 146 ? -23.744 11.450  -11.956 1.00 64.93 ?  138 HIS C NE2   1 
ATOM   7901 N N     . GLY D 1 147 ? -19.571 14.355  -7.469  1.00 48.15 ?  139 GLY C N     1 
ATOM   7902 C CA    . GLY D 1 147 ? -18.585 14.455  -6.412  1.00 45.15 ?  139 GLY C CA    1 
ATOM   7903 C C     . GLY D 1 147 ? -17.277 13.755  -6.695  1.00 47.52 ?  139 GLY C C     1 
ATOM   7904 O O     . GLY D 1 147 ? -16.558 13.404  -5.755  1.00 48.02 ?  139 GLY C O     1 
ATOM   7905 N N     . TYR D 1 148 ? -16.949 13.534  -7.964  1.00 45.23 ?  140 TYR C N     1 
ATOM   7906 C CA    . TYR D 1 148 ? -15.675 12.926  -8.312  1.00 44.70 ?  140 TYR C CA    1 
ATOM   7907 C C     . TYR D 1 148 ? -14.526 13.880  -8.004  1.00 38.38 ?  140 TYR C C     1 
ATOM   7908 O O     . TYR D 1 148 ? -14.682 15.105  -8.027  1.00 39.53 ?  140 TYR C O     1 
ATOM   7909 C CB    . TYR D 1 148 ? -15.641 12.548  -9.795  1.00 39.63 ?  140 TYR C CB    1 
ATOM   7910 C CG    . TYR D 1 148 ? -16.650 11.501  -10.212 1.00 42.78 ?  140 TYR C CG    1 
ATOM   7911 C CD1   . TYR D 1 148 ? -17.236 10.655  -9.279  1.00 40.27 ?  140 TYR C CD1   1 
ATOM   7912 C CD2   . TYR D 1 148 ? -17.011 11.355  -11.546 1.00 41.37 ?  140 TYR C CD2   1 
ATOM   7913 C CE1   . TYR D 1 148 ? -18.156 9.697   -9.663  1.00 41.51 ?  140 TYR C CE1   1 
ATOM   7914 C CE2   . TYR D 1 148 ? -17.929 10.401  -11.939 1.00 36.99 ?  140 TYR C CE2   1 
ATOM   7915 C CZ    . TYR D 1 148 ? -18.497 9.576   -10.994 1.00 43.57 ?  140 TYR C CZ    1 
ATOM   7916 O OH    . TYR D 1 148 ? -19.411 8.625   -11.384 1.00 53.85 ?  140 TYR C OH    1 
ATOM   7917 N N     . PHE D 1 149 ? -13.361 13.306  -7.716  1.00 38.82 ?  141 PHE C N     1 
ATOM   7918 C CA    . PHE D 1 149 ? -12.151 14.089  -7.508  1.00 37.60 ?  141 PHE C CA    1 
ATOM   7919 C C     . PHE D 1 149 ? -11.423 14.268  -8.833  1.00 40.38 ?  141 PHE C C     1 
ATOM   7920 O O     . PHE D 1 149 ? -11.232 13.303  -9.579  1.00 37.33 ?  141 PHE C O     1 
ATOM   7921 C CB    . PHE D 1 149 ? -11.236 13.410  -6.490  1.00 37.31 ?  141 PHE C CB    1 
ATOM   7922 C CG    . PHE D 1 149 ? -9.871  14.030  -6.392  1.00 37.36 ?  141 PHE C CG    1 
ATOM   7923 C CD1   . PHE D 1 149 ? -9.678  15.209  -5.690  1.00 41.24 ?  141 PHE C CD1   1 
ATOM   7924 C CD2   . PHE D 1 149 ? -8.780  13.435  -7.003  1.00 35.42 ?  141 PHE C CD2   1 
ATOM   7925 C CE1   . PHE D 1 149 ? -8.422  15.783  -5.600  1.00 42.84 ?  141 PHE C CE1   1 
ATOM   7926 C CE2   . PHE D 1 149 ? -7.523  14.003  -6.919  1.00 37.26 ?  141 PHE C CE2   1 
ATOM   7927 C CZ    . PHE D 1 149 ? -7.344  15.179  -6.217  1.00 36.22 ?  141 PHE C CZ    1 
ATOM   7928 N N     . GLU D 1 150 ? -11.018 15.499  -9.125  1.00 41.18 ?  142 GLU C N     1 
ATOM   7929 C CA    . GLU D 1 150 ? -10.283 15.772  -10.354 1.00 41.63 ?  142 GLU C CA    1 
ATOM   7930 C C     . GLU D 1 150 ? -8.845  16.133  -10.014 1.00 41.03 ?  142 GLU C C     1 
ATOM   7931 O O     . GLU D 1 150 ? -8.609  17.169  -9.371  1.00 41.66 ?  142 GLU C O     1 
ATOM   7932 C CB    . GLU D 1 150 ? -10.945 16.894  -11.155 1.00 40.35 ?  142 GLU C CB    1 
ATOM   7933 C CG    . GLU D 1 150 ? -10.417 17.017  -12.578 1.00 40.85 ?  142 GLU C CG    1 
ATOM   7934 C CD    . GLU D 1 150 ? -10.798 18.325  -13.245 1.00 47.51 ?  142 GLU C CD    1 
ATOM   7935 O OE1   . GLU D 1 150 ? -11.536 19.121  -12.628 1.00 46.41 ?  142 GLU C OE1   1 
ATOM   7936 O OE2   . GLU D 1 150 ? -10.358 18.557  -14.393 1.00 48.07 ?  142 GLU C OE2   1 
ATOM   7937 N N     . PRO D 1 151 ? -7.861  15.311  -10.395 1.00 32.81 ?  143 PRO C N     1 
ATOM   7938 C CA    . PRO D 1 151 ? -6.463  15.656  -10.081 1.00 37.04 ?  143 PRO C CA    1 
ATOM   7939 C C     . PRO D 1 151 ? -6.006  16.960  -10.709 1.00 34.80 ?  143 PRO C C     1 
ATOM   7940 O O     . PRO D 1 151 ? -5.220  17.691  -10.094 1.00 35.05 ?  143 PRO C O     1 
ATOM   7941 C CB    . PRO D 1 151 ? -5.678  14.455  -10.629 1.00 35.07 ?  143 PRO C CB    1 
ATOM   7942 C CG    . PRO D 1 151 ? -6.658  13.328  -10.638 1.00 34.23 ?  143 PRO C CG    1 
ATOM   7943 C CD    . PRO D 1 151 ? -7.988  13.953  -10.952 1.00 35.02 ?  143 PRO C CD    1 
ATOM   7944 N N     . GLN D 1 152 ? -6.479  17.270  -11.920 1.00 30.86 ?  144 GLN C N     1 
ATOM   7945 C CA    . GLN D 1 152 ? -6.116  18.494  -12.628 1.00 33.56 ?  144 GLN C CA    1 
ATOM   7946 C C     . GLN D 1 152 ? -4.609  18.584  -12.829 1.00 39.87 ?  144 GLN C C     1 
ATOM   7947 O O     . GLN D 1 152 ? -3.915  19.273  -12.073 1.00 42.71 ?  144 GLN C O     1 
ATOM   7948 C CB    . GLN D 1 152 ? -6.636  19.719  -11.873 1.00 40.24 ?  144 GLN C CB    1 
ATOM   7949 C CG    . GLN D 1 152 ? -8.104  19.613  -11.520 1.00 42.79 ?  144 GLN C CG    1 
ATOM   7950 C CD    . GLN D 1 152 ? -8.616  20.814  -10.762 1.00 44.67 ?  144 GLN C CD    1 
ATOM   7951 O OE1   . GLN D 1 152 ? -7.859  21.726  -10.434 1.00 46.41 ?  144 GLN C OE1   1 
ATOM   7952 N NE2   . GLN D 1 152 ? -9.911  20.818  -10.473 1.00 50.12 ?  144 GLN C NE2   1 
ATOM   7953 N N     . GLN D 1 153 ? -4.100  17.900  -13.857 1.00 37.09 ?  145 GLN C N     1 
ATOM   7954 C CA    . GLN D 1 153 ? -2.659  17.789  -14.059 1.00 35.73 ?  145 GLN C CA    1 
ATOM   7955 C C     . GLN D 1 153 ? -2.005  19.125  -14.386 1.00 35.50 ?  145 GLN C C     1 
ATOM   7956 O O     . GLN D 1 153 ? -0.803  19.286  -14.150 1.00 32.62 ?  145 GLN C O     1 
ATOM   7957 C CB    . GLN D 1 153 ? -2.366  16.785  -15.175 1.00 40.16 ?  145 GLN C CB    1 
ATOM   7958 C CG    . GLN D 1 153 ? -3.064  17.107  -16.492 1.00 34.39 ?  145 GLN C CG    1 
ATOM   7959 C CD    . GLN D 1 153 ? -2.599  16.226  -17.639 1.00 42.01 ?  145 GLN C CD    1 
ATOM   7960 O OE1   . GLN D 1 153 ? -1.427  15.858  -17.718 1.00 38.05 ?  145 GLN C OE1   1 
ATOM   7961 N NE2   . GLN D 1 153 ? -3.520  15.886  -18.535 1.00 38.52 ?  145 GLN C NE2   1 
ATOM   7962 N N     . PHE D 1 154 ? -2.759  20.077  -14.929 1.00 39.13 ?  146 PHE C N     1 
ATOM   7963 C CA    . PHE D 1 154 ? -2.213  21.379  -15.282 1.00 37.99 ?  146 PHE C CA    1 
ATOM   7964 C C     . PHE D 1 154 ? -2.218  22.362  -14.120 1.00 37.79 ?  146 PHE C C     1 
ATOM   7965 O O     . PHE D 1 154 ? -1.669  23.461  -14.255 1.00 38.39 ?  146 PHE C O     1 
ATOM   7966 C CB    . PHE D 1 154 ? -2.991  21.971  -16.463 1.00 38.22 ?  146 PHE C CB    1 
ATOM   7967 C CG    . PHE D 1 154 ? -2.854  21.182  -17.737 1.00 39.94 ?  146 PHE C CG    1 
ATOM   7968 C CD1   . PHE D 1 154 ? -1.704  21.269  -18.506 1.00 35.63 ?  146 PHE C CD1   1 
ATOM   7969 C CD2   . PHE D 1 154 ? -3.876  20.349  -18.165 1.00 32.98 ?  146 PHE C CD2   1 
ATOM   7970 C CE1   . PHE D 1 154 ? -1.577  20.543  -19.677 1.00 35.88 ?  146 PHE C CE1   1 
ATOM   7971 C CE2   . PHE D 1 154 ? -3.755  19.621  -19.334 1.00 35.33 ?  146 PHE C CE2   1 
ATOM   7972 C CZ    . PHE D 1 154 ? -2.604  19.718  -20.091 1.00 35.58 ?  146 PHE C CZ    1 
ATOM   7973 N N     . GLU D 1 155 ? -2.814  21.995  -12.986 1.00 37.76 ?  147 GLU C N     1 
ATOM   7974 C CA    . GLU D 1 155 ? -2.888  22.874  -11.826 1.00 38.18 ?  147 GLU C CA    1 
ATOM   7975 C C     . GLU D 1 155 ? -2.351  22.258  -10.542 1.00 37.59 ?  147 GLU C C     1 
ATOM   7976 O O     . GLU D 1 155 ? -2.053  23.008  -9.606  1.00 42.41 ?  147 GLU C O     1 
ATOM   7977 C CB    . GLU D 1 155 ? -4.339  23.321  -11.584 1.00 41.06 ?  147 GLU C CB    1 
ATOM   7978 C CG    . GLU D 1 155 ? -5.045  23.883  -12.813 1.00 38.75 ?  147 GLU C CG    1 
ATOM   7979 C CD    . GLU D 1 155 ? -4.356  25.110  -13.379 1.00 48.76 ?  147 GLU C CD    1 
ATOM   7980 O OE1   . GLU D 1 155 ? -3.983  26.002  -12.588 1.00 47.16 ?  147 GLU C OE1   1 
ATOM   7981 O OE2   . GLU D 1 155 ? -4.188  25.185  -14.615 1.00 48.14 ?  147 GLU C OE2   1 
ATOM   7982 N N     . ASN D 1 156 ? -2.201  20.942  -10.466 1.00 35.55 ?  148 ASN C N     1 
ATOM   7983 C CA    . ASN D 1 156 ? -1.867  20.291  -9.205  1.00 31.40 ?  148 ASN C CA    1 
ATOM   7984 C C     . ASN D 1 156 ? -0.392  20.492  -8.879  1.00 37.32 ?  148 ASN C C     1 
ATOM   7985 O O     . ASN D 1 156 ? 0.467   20.083  -9.670  1.00 37.19 ?  148 ASN C O     1 
ATOM   7986 C CB    . ASN D 1 156 ? -2.190  18.806  -9.277  1.00 32.59 ?  148 ASN C CB    1 
ATOM   7987 C CG    . ASN D 1 156 ? -2.400  18.192  -7.911  1.00 33.79 ?  148 ASN C CG    1 
ATOM   7988 O OD1   . ASN D 1 156 ? -1.682  18.501  -6.959  1.00 37.97 ?  148 ASN C OD1   1 
ATOM   7989 N ND2   . ASN D 1 156 ? -3.403  17.330  -7.801  1.00 34.27 ?  148 ASN C ND2   1 
ATOM   7990 N N     . PRO D 1 157 ? -0.052  21.103  -7.739  1.00 37.71 ?  149 PRO C N     1 
ATOM   7991 C CA    . PRO D 1 157 ? 1.371   21.281  -7.407  1.00 32.29 ?  149 PRO C CA    1 
ATOM   7992 C C     . PRO D 1 157 ? 2.122   19.973  -7.245  1.00 33.00 ?  149 PRO C C     1 
ATOM   7993 O O     . PRO D 1 157 ? 3.351   19.960  -7.377  1.00 33.30 ?  149 PRO C O     1 
ATOM   7994 C CB    . PRO D 1 157 ? 1.336   22.070  -6.090  1.00 31.29 ?  149 PRO C CB    1 
ATOM   7995 C CG    . PRO D 1 157 ? -0.015  22.682  -6.019  1.00 35.97 ?  149 PRO C CG    1 
ATOM   7996 C CD    . PRO D 1 157 ? -0.945  21.797  -6.796  1.00 37.69 ?  149 PRO C CD    1 
ATOM   7997 N N     . ALA D 1 158 ? 1.425   18.869  -6.960  1.00 32.88 ?  150 ALA C N     1 
ATOM   7998 C CA    . ALA D 1 158 ? 2.100   17.583  -6.824  1.00 37.64 ?  150 ALA C CA    1 
ATOM   7999 C C     . ALA D 1 158 ? 2.739   17.133  -8.132  1.00 36.40 ?  150 ALA C C     1 
ATOM   8000 O O     . ALA D 1 158 ? 3.655   16.305  -8.109  1.00 34.56 ?  150 ALA C O     1 
ATOM   8001 C CB    . ALA D 1 158 ? 1.122   16.519  -6.328  1.00 35.01 ?  150 ALA C CB    1 
ATOM   8002 N N     . ASN D 1 159 ? 2.278   17.671  -9.271  1.00 35.17 ?  151 ASN C N     1 
ATOM   8003 C CA    . ASN D 1 159 ? 2.852   17.285  -10.562 1.00 32.79 ?  151 ASN C CA    1 
ATOM   8004 C C     . ASN D 1 159 ? 4.286   17.790  -10.686 1.00 34.50 ?  151 ASN C C     1 
ATOM   8005 O O     . ASN D 1 159 ? 5.197   16.965  -10.869 1.00 35.50 ?  151 ASN C O     1 
ATOM   8006 C CB    . ASN D 1 159 ? 1.925   17.751  -11.696 1.00 33.02 ?  151 ASN C CB    1 
ATOM   8007 C CG    . ASN D 1 159 ? 2.561   17.683  -13.084 1.00 40.75 ?  151 ASN C CG    1 
ATOM   8008 O OD1   . ASN D 1 159 ? 3.656   17.156  -13.279 1.00 42.04 ?  151 ASN C OD1   1 
ATOM   8009 N ND2   . ASN D 1 159 ? 1.853   18.232  -14.065 1.00 35.96 ?  151 ASN C ND2   1 
ATOM   8010 N N     . PRO D 1 160 ? 4.575   19.096  -10.586 1.00 33.28 ?  152 PRO C N     1 
ATOM   8011 C CA    . PRO D 1 160 ? 5.988   19.513  -10.618 1.00 34.89 ?  152 PRO C CA    1 
ATOM   8012 C C     . PRO D 1 160 ? 6.743   19.168  -9.345  1.00 36.91 ?  152 PRO C C     1 
ATOM   8013 O O     . PRO D 1 160 ? 7.981   19.176  -9.359  1.00 35.90 ?  152 PRO C O     1 
ATOM   8014 C CB    . PRO D 1 160 ? 5.912   21.030  -10.829 1.00 39.04 ?  152 PRO C CB    1 
ATOM   8015 C CG    . PRO D 1 160 ? 4.597   21.425  -10.304 1.00 35.65 ?  152 PRO C CG    1 
ATOM   8016 C CD    . PRO D 1 160 ? 3.672   20.258  -10.485 1.00 31.15 ?  152 PRO C CD    1 
ATOM   8017 N N     . GLU D 1 161 ? 6.041   18.851  -8.253  1.00 34.22 ?  153 GLU C N     1 
ATOM   8018 C CA    . GLU D 1 161 ? 6.717   18.526  -7.001  1.00 35.42 ?  153 GLU C CA    1 
ATOM   8019 C C     . GLU D 1 161 ? 7.355   17.142  -7.051  1.00 37.10 ?  153 GLU C C     1 
ATOM   8020 O O     . GLU D 1 161 ? 8.457   16.944  -6.527  1.00 34.04 ?  153 GLU C O     1 
ATOM   8021 C CB    . GLU D 1 161 ? 5.733   18.617  -5.834  1.00 33.96 ?  153 GLU C CB    1 
ATOM   8022 C CG    . GLU D 1 161 ? 6.281   18.095  -4.515  1.00 40.16 ?  153 GLU C CG    1 
ATOM   8023 C CD    . GLU D 1 161 ? 5.244   18.091  -3.406  1.00 51.95 ?  153 GLU C CD    1 
ATOM   8024 O OE1   . GLU D 1 161 ? 4.135   17.559  -3.627  1.00 45.29 ?  153 GLU C OE1   1 
ATOM   8025 O OE2   . GLU D 1 161 ? 5.542   18.614  -2.312  1.00 51.77 ?  153 GLU C OE2   1 
ATOM   8026 N N     . VAL D 1 162 ? 6.680   16.171  -7.673  1.00 37.20 ?  154 VAL C N     1 
ATOM   8027 C CA    . VAL D 1 162 ? 7.211   14.810  -7.693  1.00 34.03 ?  154 VAL C CA    1 
ATOM   8028 C C     . VAL D 1 162 ? 8.491   14.741  -8.517  1.00 36.08 ?  154 VAL C C     1 
ATOM   8029 O O     . VAL D 1 162 ? 9.394   13.953  -8.209  1.00 34.92 ?  154 VAL C O     1 
ATOM   8030 C CB    . VAL D 1 162 ? 6.150   13.818  -8.208  1.00 30.34 ?  154 VAL C CB    1 
ATOM   8031 C CG1   . VAL D 1 162 ? 5.802   14.092  -9.662  1.00 32.46 ?  154 VAL C CG1   1 
ATOM   8032 C CG2   . VAL D 1 162 ? 6.629   12.383  -8.029  1.00 30.54 ?  154 VAL C CG2   1 
ATOM   8033 N N     . HIS D 1 163 ? 8.601   15.561  -9.566  1.00 29.33 ?  155 HIS C N     1 
ATOM   8034 C CA    . HIS D 1 163 ? 9.863   15.652  -10.292 1.00 35.47 ?  155 HIS C CA    1 
ATOM   8035 C C     . HIS D 1 163 ? 10.936  16.323  -9.446  1.00 36.09 ?  155 HIS C C     1 
ATOM   8036 O O     . HIS D 1 163 ? 12.126  16.033  -9.610  1.00 36.28 ?  155 HIS C O     1 
ATOM   8037 C CB    . HIS D 1 163 ? 9.661   16.412  -11.602 1.00 33.44 ?  155 HIS C CB    1 
ATOM   8038 C CG    . HIS D 1 163 ? 8.681   15.764  -12.529 1.00 33.94 ?  155 HIS C CG    1 
ATOM   8039 N ND1   . HIS D 1 163 ? 8.917   14.547  -13.132 1.00 31.45 ?  155 HIS C ND1   1 
ATOM   8040 C CD2   . HIS D 1 163 ? 7.458   16.162  -12.953 1.00 30.19 ?  155 HIS C CD2   1 
ATOM   8041 C CE1   . HIS D 1 163 ? 7.884   14.225  -13.889 1.00 32.96 ?  155 HIS C CE1   1 
ATOM   8042 N NE2   . HIS D 1 163 ? 6.985   15.188  -13.798 1.00 36.00 ?  155 HIS C NE2   1 
ATOM   8043 N N     . GLU D 1 164 ? 10.531  17.216  -8.540  1.00 37.68 ?  156 GLU C N     1 
ATOM   8044 C CA    . GLU D 1 164 ? 11.478  17.845  -7.626  1.00 39.80 ?  156 GLU C CA    1 
ATOM   8045 C C     . GLU D 1 164 ? 11.989  16.862  -6.581  1.00 35.27 ?  156 GLU C C     1 
ATOM   8046 O O     . GLU D 1 164 ? 13.142  16.965  -6.145  1.00 36.10 ?  156 GLU C O     1 
ATOM   8047 C CB    . GLU D 1 164 ? 10.820  19.047  -6.947  1.00 34.94 ?  156 GLU C CB    1 
ATOM   8048 C CG    . GLU D 1 164 ? 11.742  19.857  -6.060  1.00 45.92 ?  156 GLU C CG    1 
ATOM   8049 C CD    . GLU D 1 164 ? 11.033  21.038  -5.429  1.00 46.74 ?  156 GLU C CD    1 
ATOM   8050 O OE1   . GLU D 1 164 ? 9.987   21.459  -5.968  1.00 43.39 ?  156 GLU C OE1   1 
ATOM   8051 O OE2   . GLU D 1 164 ? 11.513  21.535  -4.387  1.00 54.11 ?  156 GLU C OE2   1 
ATOM   8052 N N     . LEU D 1 165 ? 11.156  15.907  -6.170  1.00 31.73 ?  157 LEU C N     1 
ATOM   8053 C CA    . LEU D 1 165 ? 11.532  14.955  -5.132  1.00 34.54 ?  157 LEU C CA    1 
ATOM   8054 C C     . LEU D 1 165 ? 12.113  13.658  -5.679  1.00 36.38 ?  157 LEU C C     1 
ATOM   8055 O O     . LEU D 1 165 ? 12.812  12.953  -4.942  1.00 31.08 ?  157 LEU C O     1 
ATOM   8056 C CB    . LEU D 1 165 ? 10.321  14.620  -4.254  1.00 36.20 ?  157 LEU C CB    1 
ATOM   8057 C CG    . LEU D 1 165 ? 9.554   15.795  -3.642  1.00 34.81 ?  157 LEU C CG    1 
ATOM   8058 C CD1   . LEU D 1 165 ? 8.236   15.329  -3.037  1.00 40.96 ?  157 LEU C CD1   1 
ATOM   8059 C CD2   . LEU D 1 165 ? 10.405  16.503  -2.601  1.00 34.19 ?  157 LEU C CD2   1 
ATOM   8060 N N     . THR D 1 166 ? 11.842  13.320  -6.940  1.00 33.02 ?  158 THR C N     1 
ATOM   8061 C CA    . THR D 1 166 ? 12.268  12.032  -7.474  1.00 35.37 ?  158 THR C CA    1 
ATOM   8062 C C     . THR D 1 166 ? 13.114  12.186  -8.734  1.00 31.82 ?  158 THR C C     1 
ATOM   8063 O O     . THR D 1 166 ? 14.298  11.837  -8.729  1.00 35.59 ?  158 THR C O     1 
ATOM   8064 C CB    . THR D 1 166 ? 11.052  11.143  -7.759  1.00 32.02 ?  158 THR C CB    1 
ATOM   8065 O OG1   . THR D 1 166 ? 10.173  11.804  -8.679  1.00 28.30 ?  158 THR C OG1   1 
ATOM   8066 C CG2   . THR D 1 166 ? 10.297  10.836  -6.468  1.00 30.94 ?  158 THR C CG2   1 
ATOM   8067 N N     . THR D 1 167 ? 12.519  12.709  -9.810  1.00 31.87 ?  159 THR C N     1 
ATOM   8068 C CA    . THR D 1 167 ? 13.219  12.783  -11.091 1.00 33.12 ?  159 THR C CA    1 
ATOM   8069 C C     . THR D 1 167 ? 14.491  13.613  -10.981 1.00 30.67 ?  159 THR C C     1 
ATOM   8070 O O     . THR D 1 167 ? 15.560  13.198  -11.444 1.00 33.32 ?  159 THR C O     1 
ATOM   8071 C CB    . THR D 1 167 ? 12.302  13.372  -12.162 1.00 30.33 ?  159 THR C CB    1 
ATOM   8072 O OG1   . THR D 1 167 ? 11.017  12.746  -12.092 1.00 30.96 ?  159 THR C OG1   1 
ATOM   8073 C CG2   . THR D 1 167 ? 12.895  13.149  -13.546 1.00 25.30 ?  159 THR C CG2   1 
ATOM   8074 N N     . GLY D 1 168 ? 14.386  14.799  -10.386 1.00 35.27 ?  160 GLY C N     1 
ATOM   8075 C CA    . GLY D 1 168 ? 15.521  15.665  -10.170 1.00 39.21 ?  160 GLY C CA    1 
ATOM   8076 C C     . GLY D 1 168 ? 16.644  15.006  -9.392  1.00 35.72 ?  160 GLY C C     1 
ATOM   8077 O O     . GLY D 1 168 ? 17.777  14.903  -9.872  1.00 35.86 ?  160 GLY C O     1 
ATOM   8078 N N     . PRO D 1 169 ? 16.356  14.555  -8.166  1.00 36.70 ?  161 PRO C N     1 
ATOM   8079 C CA    . PRO D 1 169 ? 17.405  13.887  -7.377  1.00 36.53 ?  161 PRO C CA    1 
ATOM   8080 C C     . PRO D 1 169 ? 17.981  12.652  -8.046  1.00 38.86 ?  161 PRO C C     1 
ATOM   8081 O O     . PRO D 1 169 ? 19.149  12.323  -7.801  1.00 45.22 ?  161 PRO C O     1 
ATOM   8082 C CB    . PRO D 1 169 ? 16.686  13.538  -6.067  1.00 30.00 ?  161 PRO C CB    1 
ATOM   8083 C CG    . PRO D 1 169 ? 15.600  14.545  -5.960  1.00 36.50 ?  161 PRO C CG    1 
ATOM   8084 C CD    . PRO D 1 169 ? 15.139  14.790  -7.369  1.00 33.56 ?  161 PRO C CD    1 
ATOM   8085 N N     . GLU D 1 170 ? 17.205  11.953  -8.880  1.00 36.21 ?  162 GLU C N     1 
ATOM   8086 C CA    . GLU D 1 170 ? 17.752  10.815  -9.614  1.00 38.11 ?  162 GLU C CA    1 
ATOM   8087 C C     . GLU D 1 170 ? 18.866  11.256  -10.554 1.00 37.81 ?  162 GLU C C     1 
ATOM   8088 O O     . GLU D 1 170 ? 19.935  10.636  -10.605 1.00 33.37 ?  162 GLU C O     1 
ATOM   8089 C CB    . GLU D 1 170 ? 16.648  10.105  -10.396 1.00 37.25 ?  162 GLU C CB    1 
ATOM   8090 C CG    . GLU D 1 170 ? 15.761  9.206   -9.558  1.00 35.75 ?  162 GLU C CG    1 
ATOM   8091 C CD    . GLU D 1 170 ? 14.518  8.768   -10.304 1.00 36.30 ?  162 GLU C CD    1 
ATOM   8092 O OE1   . GLU D 1 170 ? 14.615  8.504   -11.522 1.00 35.95 ?  162 GLU C OE1   1 
ATOM   8093 O OE2   . GLU D 1 170 ? 13.442  8.690   -9.674  1.00 35.91 ?  162 GLU C OE2   1 
ATOM   8094 N N     . LEU D 1 171 ? 18.629  12.330  -11.310 1.00 33.76 ?  163 LEU C N     1 
ATOM   8095 C CA    . LEU D 1 171 ? 19.649  12.839  -12.220 1.00 36.23 ?  163 LEU C CA    1 
ATOM   8096 C C     . LEU D 1 171 ? 20.873  13.346  -11.468 1.00 36.81 ?  163 LEU C C     1 
ATOM   8097 O O     . LEU D 1 171 ? 21.998  13.234  -11.971 1.00 33.60 ?  163 LEU C O     1 
ATOM   8098 C CB    . LEU D 1 171 ? 19.063  13.949  -13.093 1.00 31.62 ?  163 LEU C CB    1 
ATOM   8099 C CG    . LEU D 1 171 ? 18.302  13.486  -14.336 1.00 39.09 ?  163 LEU C CG    1 
ATOM   8100 C CD1   . LEU D 1 171 ? 17.579  14.653  -14.995 1.00 35.13 ?  163 LEU C CD1   1 
ATOM   8101 C CD2   . LEU D 1 171 ? 19.245  12.805  -15.316 1.00 27.75 ?  163 LEU C CD2   1 
ATOM   8102 N N     . LEU D 1 172 ? 20.679  13.908  -10.271 1.00 38.41 ?  164 LEU C N     1 
ATOM   8103 C CA    . LEU D 1 172 ? 21.820  14.370  -9.484  1.00 40.13 ?  164 LEU C CA    1 
ATOM   8104 C C     . LEU D 1 172 ? 22.707  13.206  -9.066  1.00 40.58 ?  164 LEU C C     1 
ATOM   8105 O O     . LEU D 1 172 ? 23.939  13.320  -9.065  1.00 43.25 ?  164 LEU C O     1 
ATOM   8106 C CB    . LEU D 1 172 ? 21.342  15.139  -8.254  1.00 35.86 ?  164 LEU C CB    1 
ATOM   8107 C CG    . LEU D 1 172 ? 20.853  16.567  -8.491  1.00 41.29 ?  164 LEU C CG    1 
ATOM   8108 C CD1   . LEU D 1 172 ? 20.573  17.261  -7.166  1.00 36.01 ?  164 LEU C CD1   1 
ATOM   8109 C CD2   . LEU D 1 172 ? 21.875  17.342  -9.303  1.00 42.68 ?  164 LEU C CD2   1 
ATOM   8110 N N     . GLN D 1 173 ? 22.097  12.078  -8.702  1.00 42.85 ?  165 GLN C N     1 
ATOM   8111 C CA    . GLN D 1 173 ? 22.878  10.889  -8.384  1.00 36.99 ?  165 GLN C CA    1 
ATOM   8112 C C     . GLN D 1 173 ? 23.503  10.292  -9.636  1.00 44.81 ?  165 GLN C C     1 
ATOM   8113 O O     . GLN D 1 173 ? 24.659  9.851   -9.611  1.00 42.91 ?  165 GLN C O     1 
ATOM   8114 C CB    . GLN D 1 173 ? 21.998  9.853   -7.687  1.00 37.02 ?  165 GLN C CB    1 
ATOM   8115 C CG    . GLN D 1 173 ? 22.728  8.576   -7.321  1.00 45.60 ?  165 GLN C CG    1 
ATOM   8116 C CD    . GLN D 1 173 ? 21.907  7.340   -7.608  1.00 57.98 ?  165 GLN C CD    1 
ATOM   8117 O OE1   . GLN D 1 173 ? 21.077  6.931   -6.797  1.00 62.33 ?  165 GLN C OE1   1 
ATOM   8118 N NE2   . GLN D 1 173 ? 22.131  6.736   -8.771  1.00 53.30 ?  165 GLN C NE2   1 
ATOM   8119 N N     . GLN D 1 174 ? 22.755  10.264  -10.739 1.00 38.01 ?  166 GLN C N     1 
ATOM   8120 C CA    . GLN D 1 174 ? 23.259  9.654   -11.962 1.00 39.73 ?  166 GLN C CA    1 
ATOM   8121 C C     . GLN D 1 174 ? 24.416  10.438  -12.565 1.00 37.59 ?  166 GLN C C     1 
ATOM   8122 O O     . GLN D 1 174 ? 25.218  9.862   -13.307 1.00 32.75 ?  166 GLN C O     1 
ATOM   8123 C CB    . GLN D 1 174 ? 22.124  9.513   -12.975 1.00 33.12 ?  166 GLN C CB    1 
ATOM   8124 C CG    . GLN D 1 174 ? 21.135  8.417   -12.618 1.00 36.55 ?  166 GLN C CG    1 
ATOM   8125 C CD    . GLN D 1 174 ? 19.901  8.437   -13.492 1.00 36.50 ?  166 GLN C CD    1 
ATOM   8126 O OE1   . GLN D 1 174 ? 19.227  9.461   -13.610 1.00 30.71 ?  166 GLN C OE1   1 
ATOM   8127 N NE2   . GLN D 1 174 ? 19.592  7.301   -14.106 1.00 35.08 ?  166 GLN C NE2   1 
ATOM   8128 N N     . PHE D 1 175 ? 24.530  11.730  -12.263 1.00 39.40 ?  167 PHE C N     1 
ATOM   8129 C CA    . PHE D 1 175 ? 25.657  12.536  -12.716 1.00 37.83 ?  167 PHE C CA    1 
ATOM   8130 C C     . PHE D 1 175 ? 26.479  13.047  -11.538 1.00 42.41 ?  167 PHE C C     1 
ATOM   8131 O O     . PHE D 1 175 ? 26.991  14.168  -11.564 1.00 42.31 ?  167 PHE C O     1 
ATOM   8132 C CB    . PHE D 1 175 ? 25.181  13.689  -13.598 1.00 39.73 ?  167 PHE C CB    1 
ATOM   8133 C CG    . PHE D 1 175 ? 24.645  13.240  -14.926 1.00 33.18 ?  167 PHE C CG    1 
ATOM   8134 C CD1   . PHE D 1 175 ? 23.321  12.855  -15.060 1.00 32.43 ?  167 PHE C CD1   1 
ATOM   8135 C CD2   . PHE D 1 175 ? 25.471  13.181  -16.037 1.00 31.54 ?  167 PHE C CD2   1 
ATOM   8136 C CE1   . PHE D 1 175 ? 22.828  12.433  -16.280 1.00 31.19 ?  167 PHE C CE1   1 
ATOM   8137 C CE2   . PHE D 1 175 ? 24.983  12.760  -17.260 1.00 32.51 ?  167 PHE C CE2   1 
ATOM   8138 C CZ    . PHE D 1 175 ? 23.660  12.384  -17.381 1.00 33.61 ?  167 PHE C CZ    1 
ATOM   8139 N N     . GLU D 1 176 ? 26.597  12.226  -10.496 1.00 38.53 ?  168 GLU C N     1 
ATOM   8140 C CA    . GLU D 1 176 ? 27.484  12.505  -9.375  1.00 42.91 ?  168 GLU C CA    1 
ATOM   8141 C C     . GLU D 1 176 ? 28.907  12.730  -9.864  1.00 45.51 ?  168 GLU C C     1 
ATOM   8142 O O     . GLU D 1 176 ? 29.485  11.870  -10.534 1.00 43.07 ?  168 GLU C O     1 
ATOM   8143 C CB    . GLU D 1 176 ? 27.442  11.335  -8.389  1.00 49.24 ?  168 GLU C CB    1 
ATOM   8144 C CG    . GLU D 1 176 ? 26.525  11.530  -7.199  1.00 56.25 ?  168 GLU C CG    1 
ATOM   8145 C CD    . GLU D 1 176 ? 27.261  12.033  -5.977  1.00 63.08 ?  168 GLU C CD    1 
ATOM   8146 O OE1   . GLU D 1 176 ? 28.332  12.656  -6.137  1.00 59.87 ?  168 GLU C OE1   1 
ATOM   8147 O OE2   . GLU D 1 176 ? 26.773  11.791  -4.853  1.00 70.08 ?  168 GLU C OE2   1 
ATOM   8148 N N     . GLY D 1 177 ? 29.467  13.891  -9.536  1.00 40.29 ?  169 GLY C N     1 
ATOM   8149 C CA    . GLY D 1 177 ? 30.828  14.190  -9.929  1.00 46.01 ?  169 GLY C CA    1 
ATOM   8150 C C     . GLY D 1 177 ? 31.005  14.593  -11.373 1.00 52.02 ?  169 GLY C C     1 
ATOM   8151 O O     . GLY D 1 177 ? 32.137  14.599  -11.867 1.00 52.56 ?  169 GLY C O     1 
ATOM   8152 N N     . LYS D 1 178 ? 29.922  14.927  -12.070 1.00 41.32 ?  170 LYS C N     1 
ATOM   8153 C CA    . LYS D 1 178 ? 29.983  15.390  -13.448 1.00 41.03 ?  170 LYS C CA    1 
ATOM   8154 C C     . LYS D 1 178 ? 29.107  16.626  -13.595 1.00 46.80 ?  170 LYS C C     1 
ATOM   8155 O O     . LYS D 1 178 ? 28.027  16.706  -13.003 1.00 49.08 ?  170 LYS C O     1 
ATOM   8156 C CB    . LYS D 1 178 ? 29.532  14.297  -14.428 1.00 42.72 ?  170 LYS C CB    1 
ATOM   8157 C CG    . LYS D 1 178 ? 29.475  14.741  -15.885 1.00 49.61 ?  170 LYS C CG    1 
ATOM   8158 C CD    . LYS D 1 178 ? 30.816  14.556  -16.589 1.00 54.31 ?  170 LYS C CD    1 
ATOM   8159 C CE    . LYS D 1 178 ? 31.295  15.853  -17.237 1.00 52.98 ?  170 LYS C CE    1 
ATOM   8160 N NZ    . LYS D 1 178 ? 32.738  15.808  -17.613 1.00 53.88 ?  170 LYS C NZ    1 
ATOM   8161 N N     . THR D 1 179 ? 29.579  17.588  -14.384 1.00 44.15 ?  171 THR C N     1 
ATOM   8162 C CA    . THR D 1 179 ? 28.867  18.842  -14.591 1.00 43.80 ?  171 THR C CA    1 
ATOM   8163 C C     . THR D 1 179 ? 27.864  18.685  -15.728 1.00 43.77 ?  171 THR C C     1 
ATOM   8164 O O     . THR D 1 179 ? 28.240  18.324  -16.849 1.00 40.41 ?  171 THR C O     1 
ATOM   8165 C CB    . THR D 1 179 ? 29.842  19.976  -14.904 1.00 43.62 ?  171 THR C CB    1 
ATOM   8166 O OG1   . THR D 1 179 ? 30.641  20.258  -13.748 1.00 50.00 ?  171 THR C OG1   1 
ATOM   8167 C CG2   . THR D 1 179 ? 29.080  21.230  -15.310 1.00 41.41 ?  171 THR C CG2   1 
ATOM   8168 N N     . ILE D 1 180 ? 26.596  18.956  -15.440 1.00 43.95 ?  172 ILE C N     1 
ATOM   8169 C CA    . ILE D 1 180 ? 25.563  19.030  -16.466 1.00 44.33 ?  172 ILE C CA    1 
ATOM   8170 C C     . ILE D 1 180 ? 25.489  20.471  -16.948 1.00 41.44 ?  172 ILE C C     1 
ATOM   8171 O O     . ILE D 1 180 ? 25.150  21.375  -16.177 1.00 44.83 ?  172 ILE C O     1 
ATOM   8172 C CB    . ILE D 1 180 ? 24.202  18.557  -15.933 1.00 41.79 ?  172 ILE C CB    1 
ATOM   8173 C CG1   . ILE D 1 180 ? 24.284  17.106  -15.460 1.00 41.76 ?  172 ILE C CG1   1 
ATOM   8174 C CG2   . ILE D 1 180 ? 23.133  18.701  -17.004 1.00 35.03 ?  172 ILE C CG2   1 
ATOM   8175 C CD1   . ILE D 1 180 ? 23.004  16.608  -14.828 1.00 37.94 ?  172 ILE C CD1   1 
ATOM   8176 N N     . ASP D 1 181 ? 25.816  20.689  -18.220 1.00 36.60 ?  173 ASP C N     1 
ATOM   8177 C CA    . ASP D 1 181 ? 25.855  22.041  -18.762 1.00 39.74 ?  173 ASP C CA    1 
ATOM   8178 C C     . ASP D 1 181 ? 24.496  22.529  -19.239 1.00 41.26 ?  173 ASP C C     1 
ATOM   8179 O O     . ASP D 1 181 ? 24.266  23.742  -19.281 1.00 40.84 ?  173 ASP C O     1 
ATOM   8180 C CB    . ASP D 1 181 ? 26.863  22.116  -19.911 1.00 42.47 ?  173 ASP C CB    1 
ATOM   8181 C CG    . ASP D 1 181 ? 28.289  21.911  -19.445 1.00 42.07 ?  173 ASP C CG    1 
ATOM   8182 O OD1   . ASP D 1 181 ? 28.900  22.884  -18.954 1.00 40.93 ?  173 ASP C OD1   1 
ATOM   8183 O OD2   . ASP D 1 181 ? 28.798  20.778  -19.565 1.00 42.80 ?  173 ASP C OD2   1 
ATOM   8184 N N     . ALA D 1 182 ? 23.591  21.619  -19.591 1.00 42.79 ?  174 ALA C N     1 
ATOM   8185 C CA    . ALA D 1 182 ? 22.278  22.011  -20.086 1.00 39.15 ?  174 ALA C CA    1 
ATOM   8186 C C     . ALA D 1 182 ? 21.315  20.845  -19.933 1.00 36.91 ?  174 ALA C C     1 
ATOM   8187 O O     . ALA D 1 182 ? 21.660  19.706  -20.265 1.00 34.78 ?  174 ALA C O     1 
ATOM   8188 C CB    . ALA D 1 182 ? 22.348  22.456  -21.552 1.00 31.81 ?  174 ALA C CB    1 
ATOM   8189 N N     . PHE D 1 183 ? 20.119  21.131  -19.427 1.00 39.08 ?  175 PHE C N     1 
ATOM   8190 C CA    . PHE D 1 183 ? 19.029  20.169  -19.369 1.00 34.03 ?  175 PHE C CA    1 
ATOM   8191 C C     . PHE D 1 183 ? 17.864  20.704  -20.186 1.00 34.24 ?  175 PHE C C     1 
ATOM   8192 O O     . PHE D 1 183 ? 17.435  21.845  -19.987 1.00 35.69 ?  175 PHE C O     1 
ATOM   8193 C CB    . PHE D 1 183 ? 18.582  19.902  -17.929 1.00 32.52 ?  175 PHE C CB    1 
ATOM   8194 C CG    . PHE D 1 183 ? 17.369  19.017  -17.829 1.00 36.06 ?  175 PHE C CG    1 
ATOM   8195 C CD1   . PHE D 1 183 ? 17.495  17.639  -17.906 1.00 35.03 ?  175 PHE C CD1   1 
ATOM   8196 C CD2   . PHE D 1 183 ? 16.104  19.561  -17.663 1.00 31.67 ?  175 PHE C CD2   1 
ATOM   8197 C CE1   . PHE D 1 183 ? 16.385  16.820  -17.819 1.00 32.78 ?  175 PHE C CE1   1 
ATOM   8198 C CE2   . PHE D 1 183 ? 14.990  18.747  -17.576 1.00 29.11 ?  175 PHE C CE2   1 
ATOM   8199 C CZ    . PHE D 1 183 ? 15.131  17.373  -17.654 1.00 34.86 ?  175 PHE C CZ    1 
ATOM   8200 N N     . LEU D 1 184 ? 17.358  19.881  -21.098 1.00 37.28 ?  176 LEU C N     1 
ATOM   8201 C CA    . LEU D 1 184 ? 16.238  20.244  -21.951 1.00 34.78 ?  176 LEU C CA    1 
ATOM   8202 C C     . LEU D 1 184 ? 15.094  19.265  -21.736 1.00 34.04 ?  176 LEU C C     1 
ATOM   8203 O O     . LEU D 1 184 ? 15.312  18.084  -21.450 1.00 33.28 ?  176 LEU C O     1 
ATOM   8204 C CB    . LEU D 1 184 ? 16.638  20.255  -23.432 1.00 33.50 ?  176 LEU C CB    1 
ATOM   8205 C CG    . LEU D 1 184 ? 17.935  20.960  -23.834 1.00 32.28 ?  176 LEU C CG    1 
ATOM   8206 C CD1   . LEU D 1 184 ? 19.114  20.008  -23.785 1.00 32.85 ?  176 LEU C CD1   1 
ATOM   8207 C CD2   . LEU D 1 184 ? 17.793  21.559  -25.221 1.00 32.76 ?  176 LEU C CD2   1 
ATOM   8208 N N     . ALA D 1 185 ? 13.869  19.765  -21.880 1.00 34.56 ?  177 ALA C N     1 
ATOM   8209 C CA    . ALA D 1 185 ? 12.693  18.925  -21.719 1.00 28.23 ?  177 ALA C CA    1 
ATOM   8210 C C     . ALA D 1 185 ? 11.529  19.550  -22.473 1.00 35.29 ?  177 ALA C C     1 
ATOM   8211 O O     . ALA D 1 185 ? 11.355  20.771  -22.455 1.00 33.48 ?  177 ALA C O     1 
ATOM   8212 C CB    . ALA D 1 185 ? 12.334  18.744  -20.240 1.00 27.72 ?  177 ALA C CB    1 
ATOM   8213 N N     . GLY D 1 186 ? 10.748  18.706  -23.141 1.00 29.20 ?  178 GLY C N     1 
ATOM   8214 C CA    . GLY D 1 186 ? 9.519   19.174  -23.747 1.00 33.37 ?  178 GLY C CA    1 
ATOM   8215 C C     . GLY D 1 186 ? 8.486   19.528  -22.695 1.00 32.78 ?  178 GLY C C     1 
ATOM   8216 O O     . GLY D 1 186 ? 8.445   18.952  -21.608 1.00 27.74 ?  178 GLY C O     1 
ATOM   8217 N N     . VAL D 1 187 ? 7.638   20.498  -23.022 1.00 35.20 ?  179 VAL C N     1 
ATOM   8218 C CA    . VAL D 1 187 ? 6.674   21.041  -22.072 1.00 36.10 ?  179 VAL C CA    1 
ATOM   8219 C C     . VAL D 1 187 ? 5.282   20.558  -22.453 1.00 31.02 ?  179 VAL C C     1 
ATOM   8220 O O     . VAL D 1 187 ? 4.762   20.906  -23.520 1.00 35.51 ?  179 VAL C O     1 
ATOM   8221 C CB    . VAL D 1 187 ? 6.727   22.575  -22.020 1.00 36.20 ?  179 VAL C CB    1 
ATOM   8222 C CG1   . VAL D 1 187 ? 5.569   23.115  -21.192 1.00 31.62 ?  179 VAL C CG1   1 
ATOM   8223 C CG2   . VAL D 1 187 ? 8.057   23.035  -21.444 1.00 34.37 ?  179 VAL C CG2   1 
ATOM   8224 N N     . GLY D 1 188 ? 4.684   19.752  -21.581 1.00 31.17 ?  180 GLY C N     1 
ATOM   8225 C CA    . GLY D 1 188 ? 3.274   19.430  -21.676 1.00 29.13 ?  180 GLY C CA    1 
ATOM   8226 C C     . GLY D 1 188 ? 2.518   20.176  -20.599 1.00 33.63 ?  180 GLY C C     1 
ATOM   8227 O O     . GLY D 1 188 ? 1.895   21.208  -20.865 1.00 37.84 ?  180 GLY C O     1 
ATOM   8228 N N     . THR D 1 189 ? 2.575   19.661  -19.373 1.00 32.34 ?  181 THR C N     1 
ATOM   8229 C CA    . THR D 1 189 ? 2.157   20.405  -18.194 1.00 31.28 ?  181 THR C CA    1 
ATOM   8230 C C     . THR D 1 189 ? 3.275   21.264  -17.623 1.00 33.26 ?  181 THR C C     1 
ATOM   8231 O O     . THR D 1 189 ? 3.024   22.058  -16.710 1.00 32.26 ?  181 THR C O     1 
ATOM   8232 C CB    . THR D 1 189 ? 1.661   19.449  -17.103 1.00 34.11 ?  181 THR C CB    1 
ATOM   8233 O OG1   . THR D 1 189 ? 2.777   18.745  -16.544 1.00 29.57 ?  181 THR C OG1   1 
ATOM   8234 C CG2   . THR D 1 189 ? 0.671   18.450  -17.678 1.00 31.84 ?  181 THR C CG2   1 
ATOM   8235 N N     . GLY D 1 190 ? 4.495   21.123  -18.138 1.00 36.39 ?  182 GLY C N     1 
ATOM   8236 C CA    . GLY D 1 190 ? 5.651   21.782  -17.573 1.00 33.59 ?  182 GLY C CA    1 
ATOM   8237 C C     . GLY D 1 190 ? 6.152   21.190  -16.277 1.00 34.38 ?  182 GLY C C     1 
ATOM   8238 O O     . GLY D 1 190 ? 7.087   21.744  -15.685 1.00 36.53 ?  182 GLY C O     1 
ATOM   8239 N N     . GLY D 1 191 ? 5.569   20.081  -15.816 1.00 31.88 ?  183 GLY C N     1 
ATOM   8240 C CA    . GLY D 1 191 ? 5.980   19.516  -14.541 1.00 33.56 ?  183 GLY C CA    1 
ATOM   8241 C C     . GLY D 1 191 ? 7.399   18.981  -14.562 1.00 34.35 ?  183 GLY C C     1 
ATOM   8242 O O     . GLY D 1 191 ? 8.157   19.171  -13.607 1.00 35.12 ?  183 GLY C O     1 
ATOM   8243 N N     . THR D 1 192 ? 7.778   18.303  -15.648 1.00 30.82 ?  184 THR C N     1 
ATOM   8244 C CA    . THR D 1 192 ? 9.123   17.743  -15.741 1.00 32.32 ?  184 THR C CA    1 
ATOM   8245 C C     . THR D 1 192 ? 10.174  18.845  -15.776 1.00 33.82 ?  184 THR C C     1 
ATOM   8246 O O     . THR D 1 192 ? 11.169  18.795  -15.044 1.00 32.96 ?  184 THR C O     1 
ATOM   8247 C CB    . THR D 1 192 ? 9.240   16.856  -16.982 1.00 30.03 ?  184 THR C CB    1 
ATOM   8248 O OG1   . THR D 1 192 ? 8.284   15.791  -16.904 1.00 27.53 ?  184 THR C OG1   1 
ATOM   8249 C CG2   . THR D 1 192 ? 10.642  16.270  -17.091 1.00 32.17 ?  184 THR C CG2   1 
ATOM   8250 N N     . LEU D 1 193 ? 9.966   19.851  -16.628 1.00 35.00 ?  185 LEU C N     1 
ATOM   8251 C CA    . LEU D 1 193 ? 10.926  20.945  -16.745 1.00 31.05 ?  185 LEU C CA    1 
ATOM   8252 C C     . LEU D 1 193 ? 11.046  21.720  -15.438 1.00 38.29 ?  185 LEU C C     1 
ATOM   8253 O O     . LEU D 1 193 ? 12.155  22.017  -14.978 1.00 37.03 ?  185 LEU C O     1 
ATOM   8254 C CB    . LEU D 1 193 ? 10.512  21.879  -17.880 1.00 31.47 ?  185 LEU C CB    1 
ATOM   8255 C CG    . LEU D 1 193 ? 11.515  22.979  -18.219 1.00 34.17 ?  185 LEU C CG    1 
ATOM   8256 C CD1   . LEU D 1 193 ? 12.726  22.413  -18.959 1.00 30.65 ?  185 LEU C CD1   1 
ATOM   8257 C CD2   . LEU D 1 193 ? 10.840  24.073  -19.022 1.00 31.03 ?  185 LEU C CD2   1 
ATOM   8258 N N     . SER D 1 194 ? 9.909   22.058  -14.826 1.00 37.99 ?  186 SER C N     1 
ATOM   8259 C CA    . SER D 1 194 ? 9.930   22.879  -13.620 1.00 37.36 ?  186 SER C CA    1 
ATOM   8260 C C     . SER D 1 194 ? 10.551  22.132  -12.447 1.00 34.55 ?  186 SER C C     1 
ATOM   8261 O O     . SER D 1 194 ? 11.344  22.704  -11.690 1.00 40.75 ?  186 SER C O     1 
ATOM   8262 C CB    . SER D 1 194 ? 8.513   23.336  -13.273 1.00 35.92 ?  186 SER C CB    1 
ATOM   8263 O OG    . SER D 1 194 ? 7.920   24.036  -14.353 1.00 36.77 ?  186 SER C OG    1 
ATOM   8264 N N     . GLY D 1 195 ? 10.205  20.854  -12.280 1.00 36.72 ?  187 GLY C N     1 
ATOM   8265 C CA    . GLY D 1 195 ? 10.722  20.104  -11.147 1.00 38.58 ?  187 GLY C CA    1 
ATOM   8266 C C     . GLY D 1 195 ? 12.205  19.807  -11.270 1.00 38.44 ?  187 GLY C C     1 
ATOM   8267 O O     . GLY D 1 195 ? 12.975  20.030  -10.330 1.00 39.47 ?  187 GLY C O     1 
ATOM   8268 N N     . VAL D 1 196 ? 12.627  19.302  -12.431 1.00 39.73 ?  188 VAL C N     1 
ATOM   8269 C CA    . VAL D 1 196 ? 14.032  18.953  -12.620 1.00 37.81 ?  188 VAL C CA    1 
ATOM   8270 C C     . VAL D 1 196 ? 14.895  20.207  -12.667 1.00 40.06 ?  188 VAL C C     1 
ATOM   8271 O O     . VAL D 1 196 ? 15.991  20.243  -12.096 1.00 39.18 ?  188 VAL C O     1 
ATOM   8272 C CB    . VAL D 1 196 ? 14.205  18.099  -13.890 1.00 36.06 ?  188 VAL C CB    1 
ATOM   8273 C CG1   . VAL D 1 196 ? 15.681  17.847  -14.167 1.00 30.52 ?  188 VAL C CG1   1 
ATOM   8274 C CG2   . VAL D 1 196 ? 13.450  16.787  -13.755 1.00 29.29 ?  188 VAL C CG2   1 
ATOM   8275 N N     . GLY D 1 197 ? 14.414  21.254  -13.343 1.00 39.06 ?  189 GLY C N     1 
ATOM   8276 C CA    . GLY D 1 197 ? 15.207  22.468  -13.471 1.00 39.67 ?  189 GLY C CA    1 
ATOM   8277 C C     . GLY D 1 197 ? 15.518  23.108  -12.132 1.00 41.05 ?  189 GLY C C     1 
ATOM   8278 O O     . GLY D 1 197 ? 16.649  23.533  -11.881 1.00 40.81 ?  189 GLY C O     1 
ATOM   8279 N N     . LYS D 1 198 ? 14.514  23.188  -11.255 1.00 39.30 ?  190 LYS C N     1 
ATOM   8280 C CA    . LYS D 1 198 ? 14.733  23.737  -9.920  1.00 39.01 ?  190 LYS C CA    1 
ATOM   8281 C C     . LYS D 1 198 ? 15.778  22.933  -9.159  1.00 40.60 ?  190 LYS C C     1 
ATOM   8282 O O     . LYS D 1 198 ? 16.649  23.503  -8.491  1.00 41.78 ?  190 LYS C O     1 
ATOM   8283 C CB    . LYS D 1 198 ? 13.412  23.768  -9.149  1.00 38.95 ?  190 LYS C CB    1 
ATOM   8284 C CG    . LYS D 1 198 ? 13.560  23.965  -7.648  1.00 36.78 ?  190 LYS C CG    1 
ATOM   8285 C CD    . LYS D 1 198 ? 12.199  24.099  -6.983  1.00 46.35 ?  190 LYS C CD    1 
ATOM   8286 C CE    . LYS D 1 198 ? 12.327  24.480  -5.517  1.00 53.86 ?  190 LYS C CE    1 
ATOM   8287 N NZ    . LYS D 1 198 ? 11.044  24.292  -4.780  1.00 56.62 ?  190 LYS C NZ    1 
ATOM   8288 N N     . VAL D 1 199 ? 15.710  21.605  -9.254  1.00 33.76 ?  191 VAL C N     1 
ATOM   8289 C CA    . VAL D 1 199 ? 16.686  20.763  -8.572  1.00 37.88 ?  191 VAL C CA    1 
ATOM   8290 C C     . VAL D 1 199 ? 18.052  20.878  -9.240  1.00 43.96 ?  191 VAL C C     1 
ATOM   8291 O O     . VAL D 1 199 ? 19.086  20.930  -8.562  1.00 44.60 ?  191 VAL C O     1 
ATOM   8292 C CB    . VAL D 1 199 ? 16.180  19.309  -8.530  1.00 42.15 ?  191 VAL C CB    1 
ATOM   8293 C CG1   . VAL D 1 199 ? 17.316  18.343  -8.247  1.00 34.25 ?  191 VAL C CG1   1 
ATOM   8294 C CG2   . VAL D 1 199 ? 15.086  19.166  -7.485  1.00 37.77 ?  191 VAL C CG2   1 
ATOM   8295 N N     . LEU D 1 200 ? 18.080  20.952  -10.574 1.00 40.83 ?  192 LEU C N     1 
ATOM   8296 C CA    . LEU D 1 200 ? 19.349  20.984  -11.296 1.00 38.46 ?  192 LEU C CA    1 
ATOM   8297 C C     . LEU D 1 200 ? 20.031  22.344  -11.191 1.00 46.40 ?  192 LEU C C     1 
ATOM   8298 O O     . LEU D 1 200 ? 21.257  22.414  -11.051 1.00 39.88 ?  192 LEU C O     1 
ATOM   8299 C CB    . LEU D 1 200 ? 19.128  20.614  -12.763 1.00 33.35 ?  192 LEU C CB    1 
ATOM   8300 C CG    . LEU D 1 200 ? 18.987  19.123  -13.074 1.00 38.25 ?  192 LEU C CG    1 
ATOM   8301 C CD1   . LEU D 1 200 ? 19.301  18.853  -14.536 1.00 33.37 ?  192 LEU C CD1   1 
ATOM   8302 C CD2   . LEU D 1 200 ? 19.879  18.288  -12.171 1.00 40.05 ?  192 LEU C CD2   1 
ATOM   8303 N N     . LYS D 1 201 ? 19.258  23.431  -11.271 1.00 45.23 ?  193 LYS C N     1 
ATOM   8304 C CA    . LYS D 1 201 ? 19.834  24.762  -11.099 1.00 47.93 ?  193 LYS C CA    1 
ATOM   8305 C C     . LYS D 1 201 ? 20.456  24.922  -9.718  1.00 46.91 ?  193 LYS C C     1 
ATOM   8306 O O     . LYS D 1 201 ? 21.426  25.671  -9.556  1.00 52.86 ?  193 LYS C O     1 
ATOM   8307 C CB    . LYS D 1 201 ? 18.763  25.830  -11.330 1.00 46.33 ?  193 LYS C CB    1 
ATOM   8308 C CG    . LYS D 1 201 ? 19.272  27.127  -11.943 1.00 55.99 ?  193 LYS C CG    1 
ATOM   8309 C CD    . LYS D 1 201 ? 18.115  27.997  -12.416 1.00 47.41 ?  193 LYS C CD    1 
ATOM   8310 C CE    . LYS D 1 201 ? 18.538  28.914  -13.550 1.00 53.34 ?  193 LYS C CE    1 
ATOM   8311 N NZ    . LYS D 1 201 ? 18.723  28.158  -14.822 1.00 56.04 ?  193 LYS C NZ    1 
ATOM   8312 N N     . LYS D 1 202 ? 19.912  24.227  -8.718  1.00 46.66 ?  194 LYS C N     1 
ATOM   8313 C CA    . LYS D 1 202 ? 20.478  24.252  -7.373  1.00 47.65 ?  194 LYS C CA    1 
ATOM   8314 C C     . LYS D 1 202 ? 21.921  23.761  -7.375  1.00 52.64 ?  194 LYS C C     1 
ATOM   8315 O O     . LYS D 1 202 ? 22.840  24.478  -6.964  1.00 52.98 ?  194 LYS C O     1 
ATOM   8316 C CB    . LYS D 1 202 ? 19.617  23.391  -6.449  1.00 53.45 ?  194 LYS C CB    1 
ATOM   8317 C CG    . LYS D 1 202 ? 19.565  23.833  -5.000  1.00 54.43 ?  194 LYS C CG    1 
ATOM   8318 C CD    . LYS D 1 202 ? 18.218  23.479  -4.373  1.00 53.21 ?  194 LYS C CD    1 
ATOM   8319 C CE    . LYS D 1 202 ? 17.651  22.153  -4.895  1.00 57.22 ?  194 LYS C CE    1 
ATOM   8320 N NZ    . LYS D 1 202 ? 18.560  20.979  -4.721  1.00 59.74 ?  194 LYS C NZ    1 
ATOM   8321 N N     . GLU D 1 203 ? 22.137  22.535  -7.853  1.00 51.11 ?  195 GLU C N     1 
ATOM   8322 C CA    . GLU D 1 203 ? 23.457  21.917  -7.807  1.00 46.49 ?  195 GLU C CA    1 
ATOM   8323 C C     . GLU D 1 203 ? 24.402  22.480  -8.862  1.00 48.61 ?  195 GLU C C     1 
ATOM   8324 O O     . GLU D 1 203 ? 25.612  22.563  -8.620  1.00 49.03 ?  195 GLU C O     1 
ATOM   8325 C CB    . GLU D 1 203 ? 23.322  20.402  -7.978  1.00 41.07 ?  195 GLU C CB    1 
ATOM   8326 C CG    . GLU D 1 203 ? 24.633  19.636  -7.936  1.00 46.35 ?  195 GLU C CG    1 
ATOM   8327 C CD    . GLU D 1 203 ? 25.100  19.362  -6.520  1.00 51.77 ?  195 GLU C CD    1 
ATOM   8328 O OE1   . GLU D 1 203 ? 24.396  19.765  -5.571  1.00 49.03 ?  195 GLU C OE1   1 
ATOM   8329 O OE2   . GLU D 1 203 ? 26.170  18.738  -6.357  1.00 53.60 ?  195 GLU C OE2   1 
ATOM   8330 N N     . TYR D 1 204 ? 23.882  22.863  -10.030 1.00 47.03 ?  196 TYR C N     1 
ATOM   8331 C CA    . TYR D 1 204 ? 24.688  23.398  -11.127 1.00 44.56 ?  196 TYR C CA    1 
ATOM   8332 C C     . TYR D 1 204 ? 24.257  24.836  -11.379 1.00 44.34 ?  196 TYR C C     1 
ATOM   8333 O O     . TYR D 1 204 ? 23.357  25.091  -12.194 1.00 44.14 ?  196 TYR C O     1 
ATOM   8334 C CB    . TYR D 1 204 ? 24.533  22.549  -12.387 1.00 46.12 ?  196 TYR C CB    1 
ATOM   8335 C CG    . TYR D 1 204 ? 24.863  21.087  -12.190 1.00 41.80 ?  196 TYR C CG    1 
ATOM   8336 C CD1   . TYR D 1 204 ? 26.180  20.659  -12.081 1.00 36.43 ?  196 TYR C CD1   1 
ATOM   8337 C CD2   . TYR D 1 204 ? 23.855  20.135  -12.112 1.00 39.28 ?  196 TYR C CD2   1 
ATOM   8338 C CE1   . TYR D 1 204 ? 26.483  19.321  -11.901 1.00 39.47 ?  196 TYR C CE1   1 
ATOM   8339 C CE2   . TYR D 1 204 ? 24.148  18.796  -11.932 1.00 39.42 ?  196 TYR C CE2   1 
ATOM   8340 C CZ    . TYR D 1 204 ? 25.464  18.395  -11.827 1.00 45.06 ?  196 TYR C CZ    1 
ATOM   8341 O OH    . TYR D 1 204 ? 25.760  17.062  -11.649 1.00 36.97 ?  196 TYR C OH    1 
ATOM   8342 N N     . PRO D 1 205 ? 24.877  25.811  -10.708 1.00 49.76 ?  197 PRO C N     1 
ATOM   8343 C CA    . PRO D 1 205 ? 24.423  27.207  -10.844 1.00 47.65 ?  197 PRO C CA    1 
ATOM   8344 C C     . PRO D 1 205 ? 24.613  27.797  -12.236 1.00 43.04 ?  197 PRO C C     1 
ATOM   8345 O O     . PRO D 1 205 ? 24.050  28.865  -12.509 1.00 50.83 ?  197 PRO C O     1 
ATOM   8346 C CB    . PRO D 1 205 ? 25.270  27.960  -9.807  1.00 46.14 ?  197 PRO C CB    1 
ATOM   8347 C CG    . PRO D 1 205 ? 25.834  26.911  -8.903  1.00 46.63 ?  197 PRO C CG    1 
ATOM   8348 C CD    . PRO D 1 205 ? 25.952  25.663  -9.714  1.00 41.44 ?  197 PRO C CD    1 
ATOM   8349 N N     . ASN D 1 206 ? 25.376  27.152  -13.118 1.00 47.36 ?  198 ASN C N     1 
ATOM   8350 C CA    . ASN D 1 206 ? 25.630  27.671  -14.457 1.00 46.42 ?  198 ASN C CA    1 
ATOM   8351 C C     . ASN D 1 206 ? 24.940  26.858  -15.545 1.00 46.18 ?  198 ASN C C     1 
ATOM   8352 O O     . ASN D 1 206 ? 25.271  27.013  -16.726 1.00 38.00 ?  198 ASN C O     1 
ATOM   8353 C CB    . ASN D 1 206 ? 27.137  27.728  -14.724 1.00 46.39 ?  198 ASN C CB    1 
ATOM   8354 C CG    . ASN D 1 206 ? 27.851  28.731  -13.838 1.00 52.95 ?  198 ASN C CG    1 
ATOM   8355 O OD1   . ASN D 1 206 ? 27.264  29.718  -13.395 1.00 55.79 ?  198 ASN C OD1   1 
ATOM   8356 N ND2   . ASN D 1 206 ? 29.128  28.480  -13.574 1.00 48.34 ?  198 ASN C ND2   1 
ATOM   8357 N N     . ILE D 1 207 ? 23.992  26.001  -15.181 1.00 48.08 ?  199 ILE C N     1 
ATOM   8358 C CA    . ILE D 1 207 ? 23.320  25.145  -16.151 1.00 42.41 ?  199 ILE C CA    1 
ATOM   8359 C C     . ILE D 1 207 ? 22.324  25.969  -16.957 1.00 42.19 ?  199 ILE C C     1 
ATOM   8360 O O     . ILE D 1 207 ? 21.768  26.964  -16.478 1.00 48.37 ?  199 ILE C O     1 
ATOM   8361 C CB    . ILE D 1 207 ? 22.630  23.960  -15.443 1.00 46.41 ?  199 ILE C CB    1 
ATOM   8362 C CG1   . ILE D 1 207 ? 22.231  22.880  -16.451 1.00 43.13 ?  199 ILE C CG1   1 
ATOM   8363 C CG2   . ILE D 1 207 ? 21.409  24.432  -14.661 1.00 40.10 ?  199 ILE C CG2   1 
ATOM   8364 C CD1   . ILE D 1 207 ? 21.422  21.752  -15.847 1.00 35.35 ?  199 ILE C CD1   1 
ATOM   8365 N N     . GLU D 1 208 ? 22.105  25.558  -18.200 1.00 41.11 ?  200 GLU C N     1 
ATOM   8366 C CA    . GLU D 1 208 ? 21.064  26.127  -19.043 1.00 39.35 ?  200 GLU C CA    1 
ATOM   8367 C C     . GLU D 1 208 ? 19.840  25.223  -19.008 1.00 38.98 ?  200 GLU C C     1 
ATOM   8368 O O     . GLU D 1 208 ? 19.934  24.028  -19.309 1.00 36.30 ?  200 GLU C O     1 
ATOM   8369 C CB    . GLU D 1 208 ? 21.548  26.299  -20.483 1.00 34.97 ?  200 GLU C CB    1 
ATOM   8370 C CG    . GLU D 1 208 ? 20.900  27.466  -21.211 1.00 39.50 ?  200 GLU C CG    1 
ATOM   8371 C CD    . GLU D 1 208 ? 21.124  27.415  -22.709 1.00 49.68 ?  200 GLU C CD    1 
ATOM   8372 O OE1   . GLU D 1 208 ? 22.227  27.012  -23.134 1.00 40.56 ?  200 GLU C OE1   1 
ATOM   8373 O OE2   . GLU D 1 208 ? 20.193  27.772  -23.462 1.00 47.94 ?  200 GLU C OE2   1 
ATOM   8374 N N     . ILE D 1 209 ? 18.698  25.790  -18.635 1.00 38.59 ?  201 ILE C N     1 
ATOM   8375 C CA    . ILE D 1 209 ? 17.431  25.071  -18.623 1.00 38.13 ?  201 ILE C CA    1 
ATOM   8376 C C     . ILE D 1 209 ? 16.646  25.505  -19.851 1.00 39.75 ?  201 ILE C C     1 
ATOM   8377 O O     . ILE D 1 209 ? 16.340  26.693  -20.013 1.00 38.57 ?  201 ILE C O     1 
ATOM   8378 C CB    . ILE D 1 209 ? 16.646  25.338  -17.330 1.00 37.43 ?  201 ILE C CB    1 
ATOM   8379 C CG1   . ILE D 1 209 ? 17.495  24.971  -16.111 1.00 40.77 ?  201 ILE C CG1   1 
ATOM   8380 C CG2   . ILE D 1 209 ? 15.339  24.562  -17.329 1.00 38.94 ?  201 ILE C CG2   1 
ATOM   8381 C CD1   . ILE D 1 209 ? 17.903  23.513  -16.065 1.00 38.45 ?  201 ILE C CD1   1 
ATOM   8382 N N     . VAL D 1 210 ? 16.330  24.554  -20.726 1.00 37.93 ?  202 VAL C N     1 
ATOM   8383 C CA    . VAL D 1 210 ? 15.743  24.845  -22.029 1.00 38.49 ?  202 VAL C CA    1 
ATOM   8384 C C     . VAL D 1 210 ? 14.386  24.162  -22.123 1.00 40.91 ?  202 VAL C C     1 
ATOM   8385 O O     . VAL D 1 210 ? 14.278  22.947  -21.910 1.00 39.44 ?  202 VAL C O     1 
ATOM   8386 C CB    . VAL D 1 210 ? 16.656  24.393  -23.179 1.00 35.29 ?  202 VAL C CB    1 
ATOM   8387 C CG1   . VAL D 1 210 ? 16.186  25.001  -24.490 1.00 37.47 ?  202 VAL C CG1   1 
ATOM   8388 C CG2   . VAL D 1 210 ? 18.102  24.775  -22.896 1.00 38.62 ?  202 VAL C CG2   1 
ATOM   8389 N N     . ALA D 1 211 ? 13.358  24.940  -22.454 1.00 36.77 ?  203 ALA C N     1 
ATOM   8390 C CA    . ALA D 1 211 ? 12.041  24.393  -22.738 1.00 37.77 ?  203 ALA C CA    1 
ATOM   8391 C C     . ALA D 1 211 ? 11.940  24.044  -24.216 1.00 38.19 ?  203 ALA C C     1 
ATOM   8392 O O     . ALA D 1 211 ? 12.514  24.729  -25.066 1.00 37.50 ?  203 ALA C O     1 
ATOM   8393 C CB    . ALA D 1 211 ? 10.946  25.387  -22.354 1.00 37.18 ?  203 ALA C CB    1 
ATOM   8394 N N     . ILE D 1 212 ? 11.215  22.969  -24.517 1.00 34.31 ?  204 ILE C N     1 
ATOM   8395 C CA    . ILE D 1 212 ? 10.995  22.524  -25.887 1.00 29.90 ?  204 ILE C CA    1 
ATOM   8396 C C     . ILE D 1 212 ? 9.496   22.506  -26.144 1.00 37.88 ?  204 ILE C C     1 
ATOM   8397 O O     . ILE D 1 212 ? 8.738   21.894  -25.383 1.00 35.24 ?  204 ILE C O     1 
ATOM   8398 C CB    . ILE D 1 212 ? 11.614  21.139  -26.147 1.00 38.65 ?  204 ILE C CB    1 
ATOM   8399 C CG1   . ILE D 1 212 ? 13.140  21.208  -26.051 1.00 39.91 ?  204 ILE C CG1   1 
ATOM   8400 C CG2   . ILE D 1 212 ? 11.198  20.617  -27.514 1.00 35.18 ?  204 ILE C CG2   1 
ATOM   8401 C CD1   . ILE D 1 212 ? 13.782  19.916  -25.592 1.00 30.76 ?  204 ILE C CD1   1 
ATOM   8402 N N     . GLU D 1 213 ? 9.074   23.175  -27.207 1.00 44.15 ?  205 GLU C N     1 
ATOM   8403 C CA    . GLU D 1 213 ? 7.671   23.271  -27.574 1.00 45.11 ?  205 GLU C CA    1 
ATOM   8404 C C     . GLU D 1 213 ? 7.561   23.197  -29.087 1.00 40.75 ?  205 GLU C C     1 
ATOM   8405 O O     . GLU D 1 213 ? 8.539   23.453  -29.798 1.00 41.49 ?  205 GLU C O     1 
ATOM   8406 C CB    . GLU D 1 213 ? 7.046   24.571  -27.045 1.00 39.87 ?  205 GLU C CB    1 
ATOM   8407 C CG    . GLU D 1 213 ? 7.619   25.845  -27.635 1.00 46.44 ?  205 GLU C CG    1 
ATOM   8408 C CD    . GLU D 1 213 ? 6.756   27.053  -27.324 1.00 48.09 ?  205 GLU C CD    1 
ATOM   8409 O OE1   . GLU D 1 213 ? 5.644   26.866  -26.784 1.00 44.83 ?  205 GLU C OE1   1 
ATOM   8410 O OE2   . GLU D 1 213 ? 7.187   28.188  -27.615 1.00 44.94 ?  205 GLU C OE2   1 
ATOM   8411 N N     . PRO D 1 214 ? 6.388   22.837  -29.614 1.00 40.32 ?  206 PRO C N     1 
ATOM   8412 C CA    . PRO D 1 214 ? 6.256   22.712  -31.070 1.00 42.53 ?  206 PRO C CA    1 
ATOM   8413 C C     . PRO D 1 214 ? 6.356   24.060  -31.764 1.00 40.92 ?  206 PRO C C     1 
ATOM   8414 O O     . PRO D 1 214 ? 5.795   25.060  -31.309 1.00 40.75 ?  206 PRO C O     1 
ATOM   8415 C CB    . PRO D 1 214 ? 4.865   22.087  -31.258 1.00 38.98 ?  206 PRO C CB    1 
ATOM   8416 C CG    . PRO D 1 214 ? 4.427   21.639  -29.894 1.00 40.49 ?  206 PRO C CG    1 
ATOM   8417 C CD    . PRO D 1 214 ? 5.128   22.519  -28.921 1.00 44.12 ?  206 PRO C CD    1 
ATOM   8418 N N     . GLU D 1 215 ? 7.088   24.078  -32.881 1.00 43.83 ?  207 GLU C N     1 
ATOM   8419 C CA    . GLU D 1 215 ? 7.164   25.289  -33.690 1.00 44.06 ?  207 GLU C CA    1 
ATOM   8420 C C     . GLU D 1 215 ? 5.801   25.656  -34.263 1.00 44.33 ?  207 GLU C C     1 
ATOM   8421 O O     . GLU D 1 215 ? 5.536   26.834  -34.526 1.00 46.33 ?  207 GLU C O     1 
ATOM   8422 C CB    . GLU D 1 215 ? 8.184   25.110  -34.815 1.00 42.18 ?  207 GLU C CB    1 
ATOM   8423 C CG    . GLU D 1 215 ? 7.674   24.286  -35.986 1.00 50.38 ?  207 GLU C CG    1 
ATOM   8424 C CD    . GLU D 1 215 ? 8.473   24.498  -37.258 1.00 54.89 ?  207 GLU C CD    1 
ATOM   8425 O OE1   . GLU D 1 215 ? 9.532   25.160  -37.200 1.00 58.01 ?  207 GLU C OE1   1 
ATOM   8426 O OE2   . GLU D 1 215 ? 8.040   23.997  -38.318 1.00 58.85 ?  207 GLU C OE2   1 
ATOM   8427 N N     . ALA D 1 216 ? 4.925   24.667  -34.455 1.00 43.75 ?  208 ALA C N     1 
ATOM   8428 C CA    . ALA D 1 216 ? 3.591   24.914  -34.979 1.00 40.03 ?  208 ALA C CA    1 
ATOM   8429 C C     . ALA D 1 216 ? 2.625   25.414  -33.916 1.00 36.95 ?  208 ALA C C     1 
ATOM   8430 O O     . ALA D 1 216 ? 1.503   25.806  -34.255 1.00 39.11 ?  208 ALA C O     1 
ATOM   8431 C CB    . ALA D 1 216 ? 3.035   23.643  -35.625 1.00 37.48 ?  208 ALA C CB    1 
ATOM   8432 N N     . SER D 1 217 ? 3.029   25.405  -32.649 1.00 41.08 ?  209 SER C N     1 
ATOM   8433 C CA    . SER D 1 217 ? 2.233   25.958  -31.553 1.00 41.92 ?  209 SER C CA    1 
ATOM   8434 C C     . SER D 1 217 ? 3.194   26.582  -30.550 1.00 45.72 ?  209 SER C C     1 
ATOM   8435 O O     . SER D 1 217 ? 3.336   26.110  -29.415 1.00 44.91 ?  209 SER C O     1 
ATOM   8436 C CB    . SER D 1 217 ? 1.369   24.874  -30.905 1.00 41.67 ?  209 SER C CB    1 
ATOM   8437 O OG    . SER D 1 217 ? 0.351   25.441  -30.097 1.00 46.67 ?  209 SER C OG    1 
ATOM   8438 N N     . PRO D 1 218 ? 3.877   27.662  -30.943 1.00 45.81 ?  210 PRO C N     1 
ATOM   8439 C CA    . PRO D 1 218 ? 4.969   28.215  -30.125 1.00 46.55 ?  210 PRO C CA    1 
ATOM   8440 C C     . PRO D 1 218 ? 4.457   29.169  -29.047 1.00 45.34 ?  210 PRO C C     1 
ATOM   8441 O O     . PRO D 1 218 ? 4.789   30.360  -29.020 1.00 46.64 ?  210 PRO C O     1 
ATOM   8442 C CB    . PRO D 1 218 ? 5.829   28.925  -31.176 1.00 45.28 ?  210 PRO C CB    1 
ATOM   8443 C CG    . PRO D 1 218 ? 4.824   29.407  -32.199 1.00 46.30 ?  210 PRO C CG    1 
ATOM   8444 C CD    . PRO D 1 218 ? 3.620   28.488  -32.137 1.00 43.48 ?  210 PRO C CD    1 
ATOM   8445 N N     . VAL D 1 219 ? 3.639   28.635  -28.138 1.00 47.10 ?  211 VAL C N     1 
ATOM   8446 C CA    . VAL D 1 219 ? 2.943   29.492  -27.185 1.00 48.25 ?  211 VAL C CA    1 
ATOM   8447 C C     . VAL D 1 219 ? 3.919   30.058  -26.159 1.00 49.58 ?  211 VAL C C     1 
ATOM   8448 O O     . VAL D 1 219 ? 3.818   31.227  -25.769 1.00 47.92 ?  211 VAL C O     1 
ATOM   8449 C CB    . VAL D 1 219 ? 1.787   28.717  -26.526 1.00 48.70 ?  211 VAL C CB    1 
ATOM   8450 C CG1   . VAL D 1 219 ? 1.392   29.348  -25.200 1.00 45.54 ?  211 VAL C CG1   1 
ATOM   8451 C CG2   . VAL D 1 219 ? 0.595   28.638  -27.478 1.00 49.72 ?  211 VAL C CG2   1 
ATOM   8452 N N     . LEU D 1 220 ? 4.887   29.251  -25.716 1.00 49.41 ?  212 LEU C N     1 
ATOM   8453 C CA    . LEU D 1 220 ? 5.915   29.775  -24.820 1.00 46.71 ?  212 LEU C CA    1 
ATOM   8454 C C     . LEU D 1 220 ? 6.781   30.821  -25.508 1.00 46.57 ?  212 LEU C C     1 
ATOM   8455 O O     . LEU D 1 220 ? 7.240   31.766  -24.859 1.00 43.98 ?  212 LEU C O     1 
ATOM   8456 C CB    . LEU D 1 220 ? 6.795   28.645  -24.286 1.00 46.60 ?  212 LEU C CB    1 
ATOM   8457 C CG    . LEU D 1 220 ? 6.106   27.477  -23.588 1.00 50.73 ?  212 LEU C CG    1 
ATOM   8458 C CD1   . LEU D 1 220 ? 7.126   26.430  -23.192 1.00 44.34 ?  212 LEU C CD1   1 
ATOM   8459 C CD2   . LEU D 1 220 ? 5.365   27.970  -22.371 1.00 48.98 ?  212 LEU C CD2   1 
ATOM   8460 N N     . SER D 1 221 ? 7.016   30.672  -26.813 1.00 49.38 ?  213 SER C N     1 
ATOM   8461 C CA    . SER D 1 221 ? 7.801   31.648  -27.559 1.00 52.19 ?  213 SER C CA    1 
ATOM   8462 C C     . SER D 1 221 ? 7.093   32.989  -27.704 1.00 55.04 ?  213 SER C C     1 
ATOM   8463 O O     . SER D 1 221 ? 7.725   33.960  -28.135 1.00 45.01 ?  213 SER C O     1 
ATOM   8464 C CB    . SER D 1 221 ? 8.139   31.094  -28.945 1.00 47.49 ?  213 SER C CB    1 
ATOM   8465 O OG    . SER D 1 221 ? 9.081   30.039  -28.856 1.00 51.49 ?  213 SER C OG    1 
ATOM   8466 N N     . GLY D 1 222 ? 5.811   33.068  -27.353 1.00 51.84 ?  214 GLY C N     1 
ATOM   8467 C CA    . GLY D 1 222 ? 5.028   34.268  -27.542 1.00 51.13 ?  214 GLY C CA    1 
ATOM   8468 C C     . GLY D 1 222 ? 4.097   34.234  -28.732 1.00 56.89 ?  214 GLY C C     1 
ATOM   8469 O O     . GLY D 1 222 ? 3.386   35.219  -28.969 1.00 46.49 ?  214 GLY C O     1 
ATOM   8470 N N     . GLY D 1 223 ? 4.075   33.137  -29.486 1.00 54.67 ?  215 GLY C N     1 
ATOM   8471 C CA    . GLY D 1 223 ? 3.235   33.019  -30.657 1.00 51.58 ?  215 GLY C CA    1 
ATOM   8472 C C     . GLY D 1 223 ? 1.852   32.490  -30.330 1.00 49.93 ?  215 GLY C C     1 
ATOM   8473 O O     . GLY D 1 223 ? 1.476   32.298  -29.172 1.00 47.50 ?  215 GLY C O     1 
ATOM   8474 N N     . GLU D 1 224 ? 1.085   32.250  -31.388 1.00 55.83 ?  216 GLU C N     1 
ATOM   8475 C CA    . GLU D 1 224 ? -0.298  31.792  -31.404 1.00 56.10 ?  216 GLU C CA    1 
ATOM   8476 C C     . GLU D 1 224 ? -0.356  30.268  -31.335 1.00 53.02 ?  216 GLU C C     1 
ATOM   8477 O O     . GLU D 1 224 ? 0.487   29.587  -31.927 1.00 49.34 ?  216 GLU C O     1 
ATOM   8478 C CB    . GLU D 1 224 ? -1.002  32.275  -32.671 1.00 57.66 ?  216 GLU C CB    1 
ATOM   8479 C CG    . GLU D 1 224 ? -2.460  32.686  -32.486 1.00 62.89 ?  216 GLU C CG    1 
ATOM   8480 C CD    . GLU D 1 224 ? -2.618  34.018  -31.773 1.00 67.93 ?  216 GLU C CD    1 
ATOM   8481 O OE1   . GLU D 1 224 ? -2.348  34.085  -30.554 1.00 78.09 ?  216 GLU C OE1   1 
ATOM   8482 O OE2   . GLU D 1 224 ? -3.012  35.004  -32.431 1.00 67.44 ?  216 GLU C OE2   1 
ATOM   8483 N N     . PRO D 1 225 ? -1.331  29.708  -30.622 1.00 53.79 ?  217 PRO C N     1 
ATOM   8484 C CA    . PRO D 1 225 ? -1.479  28.250  -30.608 1.00 47.18 ?  217 PRO C CA    1 
ATOM   8485 C C     . PRO D 1 225 ? -2.010  27.738  -31.935 1.00 49.83 ?  217 PRO C C     1 
ATOM   8486 O O     . PRO D 1 225 ? -2.781  28.408  -32.626 1.00 49.39 ?  217 PRO C O     1 
ATOM   8487 C CB    . PRO D 1 225 ? -2.482  27.992  -29.474 1.00 49.11 ?  217 PRO C CB    1 
ATOM   8488 C CG    . PRO D 1 225 ? -2.793  29.324  -28.864 1.00 50.15 ?  217 PRO C CG    1 
ATOM   8489 C CD    . PRO D 1 225 ? -2.355  30.385  -29.811 1.00 54.50 ?  217 PRO C CD    1 
ATOM   8490 N N     . GLY D 1 226 ? -1.587  26.529  -32.287 1.00 38.74 ?  218 GLY C N     1 
ATOM   8491 C CA    . GLY D 1 226 ? -2.012  25.912  -33.518 1.00 36.73 ?  218 GLY C CA    1 
ATOM   8492 C C     . GLY D 1 226 ? -1.834  24.409  -33.504 1.00 38.13 ?  218 GLY C C     1 
ATOM   8493 O O     . GLY D 1 226 ? -1.244  23.836  -32.582 1.00 41.32 ?  218 GLY C O     1 
ATOM   8494 N N     . PRO D 1 227 ? -2.347  23.741  -34.533 1.00 41.56 ?  219 PRO C N     1 
ATOM   8495 C CA    . PRO D 1 227 ? -2.224  22.283  -34.598 1.00 41.41 ?  219 PRO C CA    1 
ATOM   8496 C C     . PRO D 1 227 ? -0.786  21.845  -34.813 1.00 39.00 ?  219 PRO C C     1 
ATOM   8497 O O     . PRO D 1 227 ? -0.010  22.491  -35.520 1.00 37.08 ?  219 PRO C O     1 
ATOM   8498 C CB    . PRO D 1 227 ? -3.106  21.910  -35.794 1.00 35.03 ?  219 PRO C CB    1 
ATOM   8499 C CG    . PRO D 1 227 ? -3.078  23.134  -36.653 1.00 35.60 ?  219 PRO C CG    1 
ATOM   8500 C CD    . PRO D 1 227 ? -3.086  24.283  -35.686 1.00 36.32 ?  219 PRO C CD    1 
ATOM   8501 N N     . HIS D 1 228 ? -0.438  20.722  -34.192 1.00 37.79 ?  220 HIS C N     1 
ATOM   8502 C CA    . HIS D 1 228 ? 0.902   20.165  -34.293 1.00 40.94 ?  220 HIS C CA    1 
ATOM   8503 C C     . HIS D 1 228 ? 0.817   18.659  -34.080 1.00 39.72 ?  220 HIS C C     1 
ATOM   8504 O O     . HIS D 1 228 ? -0.240  18.116  -33.744 1.00 41.32 ?  220 HIS C O     1 
ATOM   8505 C CB    . HIS D 1 228 ? 1.853   20.815  -33.283 1.00 35.19 ?  220 HIS C CB    1 
ATOM   8506 C CG    . HIS D 1 228 ? 1.464   20.582  -31.858 1.00 37.67 ?  220 HIS C CG    1 
ATOM   8507 N ND1   . HIS D 1 228 ? 1.869   19.473  -31.148 1.00 37.10 ?  220 HIS C ND1   1 
ATOM   8508 C CD2   . HIS D 1 228 ? 0.688   21.305  -31.017 1.00 40.70 ?  220 HIS C CD2   1 
ATOM   8509 C CE1   . HIS D 1 228 ? 1.367   19.528  -29.927 1.00 41.25 ?  220 HIS C CE1   1 
ATOM   8510 N NE2   . HIS D 1 228 ? 0.646   20.629  -29.822 1.00 36.24 ?  220 HIS C NE2   1 
ATOM   8511 N N     . LYS D 1 229 ? 1.950   17.986  -34.280 1.00 38.73 ?  221 LYS C N     1 
ATOM   8512 C CA    . LYS D 1 229 ? 2.019   16.531  -34.218 1.00 40.85 ?  221 LYS C CA    1 
ATOM   8513 C C     . LYS D 1 229 ? 2.882   16.027  -33.069 1.00 42.43 ?  221 LYS C C     1 
ATOM   8514 O O     . LYS D 1 229 ? 3.136   14.821  -32.980 1.00 40.85 ?  221 LYS C O     1 
ATOM   8515 C CB    . LYS D 1 229 ? 2.538   15.974  -35.545 1.00 40.00 ?  221 LYS C CB    1 
ATOM   8516 C CG    . LYS D 1 229 ? 1.829   16.530  -36.771 1.00 41.75 ?  221 LYS C CG    1 
ATOM   8517 C CD    . LYS D 1 229 ? 1.900   15.570  -37.952 1.00 51.37 ?  221 LYS C CD    1 
ATOM   8518 C CE    . LYS D 1 229 ? 3.116   15.843  -38.827 1.00 58.63 ?  221 LYS C CE    1 
ATOM   8519 N NZ    . LYS D 1 229 ? 2.786   16.713  -39.991 1.00 60.05 ?  221 LYS C NZ    1 
ATOM   8520 N N     . LEU D 1 230 ? 3.341   16.915  -32.187 1.00 33.76 ?  222 LEU C N     1 
ATOM   8521 C CA    . LEU D 1 230 ? 4.214   16.518  -31.083 1.00 35.34 ?  222 LEU C CA    1 
ATOM   8522 C C     . LEU D 1 230 ? 3.341   16.077  -29.912 1.00 34.23 ?  222 LEU C C     1 
ATOM   8523 O O     . LEU D 1 230 ? 3.018   16.846  -29.004 1.00 30.89 ?  222 LEU C O     1 
ATOM   8524 C CB    . LEU D 1 230 ? 5.154   17.656  -30.705 1.00 34.70 ?  222 LEU C CB    1 
ATOM   8525 C CG    . LEU D 1 230 ? 5.975   18.285  -31.835 1.00 30.68 ?  222 LEU C CG    1 
ATOM   8526 C CD1   . LEU D 1 230 ? 7.106   19.123  -31.266 1.00 37.27 ?  222 LEU C CD1   1 
ATOM   8527 C CD2   . LEU D 1 230 ? 6.523   17.227  -32.785 1.00 34.29 ?  222 LEU C CD2   1 
ATOM   8528 N N     . GLN D 1 231 ? 2.950   14.804  -29.949 1.00 33.67 ?  223 GLN C N     1 
ATOM   8529 C CA    . GLN D 1 231 ? 2.104   14.237  -28.907 1.00 38.53 ?  223 GLN C CA    1 
ATOM   8530 C C     . GLN D 1 231 ? 2.796   14.327  -27.556 1.00 36.22 ?  223 GLN C C     1 
ATOM   8531 O O     . GLN D 1 231 ? 3.919   13.842  -27.388 1.00 33.64 ?  223 GLN C O     1 
ATOM   8532 C CB    . GLN D 1 231 ? 1.762   12.785  -29.235 1.00 42.21 ?  223 GLN C CB    1 
ATOM   8533 C CG    . GLN D 1 231 ? 0.802   12.618  -30.396 1.00 43.86 ?  223 GLN C CG    1 
ATOM   8534 C CD    . GLN D 1 231 ? -0.079  11.395  -30.246 1.00 49.04 ?  223 GLN C CD    1 
ATOM   8535 O OE1   . GLN D 1 231 ? -0.540  11.075  -29.149 1.00 53.44 ?  223 GLN C OE1   1 
ATOM   8536 N NE2   . GLN D 1 231 ? -0.315  10.699  -31.352 1.00 47.75 ?  223 GLN C NE2   1 
ATOM   8537 N N     . GLY D 1 232 ? 2.123   14.949  -26.593 1.00 34.72 ?  224 GLY C N     1 
ATOM   8538 C CA    . GLY D 1 232 ? 2.671   15.194  -25.277 1.00 34.97 ?  224 GLY C CA    1 
ATOM   8539 C C     . GLY D 1 232 ? 3.061   16.634  -25.026 1.00 35.24 ?  224 GLY C C     1 
ATOM   8540 O O     . GLY D 1 232 ? 3.111   17.052  -23.862 1.00 40.40 ?  224 GLY C O     1 
ATOM   8541 N N     . LEU D 1 233 ? 3.331   17.404  -26.077 1.00 36.56 ?  225 LEU C N     1 
ATOM   8542 C CA    . LEU D 1 233 ? 3.706   18.805  -25.970 1.00 33.48 ?  225 LEU C CA    1 
ATOM   8543 C C     . LEU D 1 233 ? 2.568   19.688  -26.477 1.00 39.13 ?  225 LEU C C     1 
ATOM   8544 O O     . LEU D 1 233 ? 1.479   19.207  -26.809 1.00 36.51 ?  225 LEU C O     1 
ATOM   8545 C CB    . LEU D 1 233 ? 4.994   19.066  -26.750 1.00 34.33 ?  225 LEU C CB    1 
ATOM   8546 C CG    . LEU D 1 233 ? 6.109   18.029  -26.626 1.00 35.79 ?  225 LEU C CG    1 
ATOM   8547 C CD1   . LEU D 1 233 ? 7.317   18.470  -27.433 1.00 32.11 ?  225 LEU C CD1   1 
ATOM   8548 C CD2   . LEU D 1 233 ? 6.487   17.816  -25.172 1.00 31.76 ?  225 LEU C CD2   1 
ATOM   8549 N N     . GLY D 1 234 ? 2.832   20.993  -26.542 1.00 36.11 ?  226 GLY C N     1 
ATOM   8550 C CA    . GLY D 1 234 ? 1.907   21.952  -27.117 1.00 44.11 ?  226 GLY C CA    1 
ATOM   8551 C C     . GLY D 1 234 ? 0.486   21.891  -26.593 1.00 40.07 ?  226 GLY C C     1 
ATOM   8552 O O     . GLY D 1 234 ? -0.431  21.485  -27.313 1.00 39.23 ?  226 GLY C O     1 
ATOM   8553 N N     . ALA D 1 235 ? 0.290   22.298  -25.338 1.00 41.55 ?  227 ALA C N     1 
ATOM   8554 C CA    . ALA D 1 235 ? -1.048  22.298  -24.760 1.00 34.19 ?  227 ALA C CA    1 
ATOM   8555 C C     . ALA D 1 235 ? -1.918  23.421  -25.307 1.00 38.48 ?  227 ALA C C     1 
ATOM   8556 O O     . ALA D 1 235 ? -3.147  23.339  -25.207 1.00 35.77 ?  227 ALA C O     1 
ATOM   8557 C CB    . ALA D 1 235 ? -0.963  22.406  -23.237 1.00 36.58 ?  227 ALA C CB    1 
ATOM   8558 N N     . GLY D 1 236 ? -1.316  24.458  -25.881 1.00 41.51 ?  228 GLY C N     1 
ATOM   8559 C CA    . GLY D 1 236 ? -2.057  25.607  -26.354 1.00 42.87 ?  228 GLY C CA    1 
ATOM   8560 C C     . GLY D 1 236 ? -2.229  26.713  -25.341 1.00 43.20 ?  228 GLY C C     1 
ATOM   8561 O O     . GLY D 1 236 ? -2.969  27.667  -25.610 1.00 48.56 ?  228 GLY C O     1 
ATOM   8562 N N     . PHE D 1 237 ? -1.570  26.620  -24.190 1.00 41.11 ?  229 PHE C N     1 
ATOM   8563 C CA    . PHE D 1 237 ? -1.681  27.622  -23.138 1.00 40.68 ?  229 PHE C CA    1 
ATOM   8564 C C     . PHE D 1 237 ? -0.490  27.466  -22.202 1.00 44.95 ?  229 PHE C C     1 
ATOM   8565 O O     . PHE D 1 237 ? 0.339   26.564  -22.363 1.00 42.91 ?  229 PHE C O     1 
ATOM   8566 C CB    . PHE D 1 237 ? -3.013  27.492  -22.390 1.00 42.65 ?  229 PHE C CB    1 
ATOM   8567 C CG    . PHE D 1 237 ? -3.240  26.134  -21.787 1.00 41.00 ?  229 PHE C CG    1 
ATOM   8568 C CD1   . PHE D 1 237 ? -2.767  25.829  -20.519 1.00 42.81 ?  229 PHE C CD1   1 
ATOM   8569 C CD2   . PHE D 1 237 ? -3.922  25.158  -22.494 1.00 37.96 ?  229 PHE C CD2   1 
ATOM   8570 C CE1   . PHE D 1 237 ? -2.974  24.577  -19.969 1.00 40.64 ?  229 PHE C CE1   1 
ATOM   8571 C CE2   . PHE D 1 237 ? -4.132  23.905  -21.950 1.00 41.70 ?  229 PHE C CE2   1 
ATOM   8572 C CZ    . PHE D 1 237 ? -3.657  23.614  -20.686 1.00 43.48 ?  229 PHE C CZ    1 
ATOM   8573 N N     . ILE D 1 238 ? -0.408  28.360  -21.219 1.00 42.41 ?  230 ILE C N     1 
ATOM   8574 C CA    . ILE D 1 238 ? 0.616   28.301  -20.183 1.00 46.75 ?  230 ILE C CA    1 
ATOM   8575 C C     . ILE D 1 238 ? 0.045   27.503  -19.013 1.00 42.97 ?  230 ILE C C     1 
ATOM   8576 O O     . ILE D 1 238 ? -0.825  28.025  -18.293 1.00 48.05 ?  230 ILE C O     1 
ATOM   8577 C CB    . ILE D 1 238 ? 1.049   29.702  -19.727 1.00 50.35 ?  230 ILE C CB    1 
ATOM   8578 C CG1   . ILE D 1 238 ? 1.638   30.532  -20.872 1.00 48.19 ?  230 ILE C CG1   1 
ATOM   8579 C CG2   . ILE D 1 238 ? 2.083   29.598  -18.632 1.00 44.90 ?  230 ILE C CG2   1 
ATOM   8580 C CD1   . ILE D 1 238 ? 2.390   29.743  -21.910 1.00 55.13 ?  230 ILE C CD1   1 
ATOM   8581 N N     . PRO D 1 239 ? 0.489   26.269  -18.782 1.00 43.20 ?  231 PRO C N     1 
ATOM   8582 C CA    . PRO D 1 239 ? -0.044  25.498  -17.655 1.00 43.95 ?  231 PRO C CA    1 
ATOM   8583 C C     . PRO D 1 239 ? 0.320   26.142  -16.326 1.00 42.09 ?  231 PRO C C     1 
ATOM   8584 O O     . PRO D 1 239 ? 1.371   26.770  -16.181 1.00 38.13 ?  231 PRO C O     1 
ATOM   8585 C CB    . PRO D 1 239 ? 0.624   24.125  -17.810 1.00 39.36 ?  231 PRO C CB    1 
ATOM   8586 C CG    . PRO D 1 239 ? 1.144   24.092  -19.219 1.00 40.76 ?  231 PRO C CG    1 
ATOM   8587 C CD    . PRO D 1 239 ? 1.484   25.507  -19.553 1.00 38.22 ?  231 PRO C CD    1 
ATOM   8588 N N     . GLY D 1 240 ? -0.575  25.992  -15.348 1.00 41.85 ?  232 GLY C N     1 
ATOM   8589 C CA    . GLY D 1 240 ? -0.266  26.456  -14.008 1.00 44.34 ?  232 GLY C CA    1 
ATOM   8590 C C     . GLY D 1 240 ? 0.900   25.714  -13.388 1.00 44.08 ?  232 GLY C C     1 
ATOM   8591 O O     . GLY D 1 240 ? 1.648   26.280  -12.586 1.00 42.26 ?  232 GLY C O     1 
ATOM   8592 N N     . THR D 1 241 ? 1.081   24.449  -13.759 1.00 39.87 ?  233 THR C N     1 
ATOM   8593 C CA    . THR D 1 241 ? 2.175   23.632  -13.255 1.00 34.59 ?  233 THR C CA    1 
ATOM   8594 C C     . THR D 1 241 ? 3.518   23.975  -13.888 1.00 38.10 ?  233 THR C C     1 
ATOM   8595 O O     . THR D 1 241 ? 4.531   23.374  -13.514 1.00 33.68 ?  233 THR C O     1 
ATOM   8596 C CB    . THR D 1 241 ? 1.869   22.149  -13.480 1.00 36.30 ?  233 THR C CB    1 
ATOM   8597 O OG1   . THR D 1 241 ? 1.395   21.958  -14.818 1.00 36.80 ?  233 THR C OG1   1 
ATOM   8598 C CG2   . THR D 1 241 ? 0.809   21.674  -12.501 1.00 33.73 ?  233 THR C CG2   1 
ATOM   8599 N N     . LEU D 1 242 ? 3.555   24.913  -14.831 1.00 41.21 ?  234 LEU C N     1 
ATOM   8600 C CA    . LEU D 1 242 ? 4.790   25.308  -15.495 1.00 38.26 ?  234 LEU C CA    1 
ATOM   8601 C C     . LEU D 1 242 ? 5.350   26.555  -14.826 1.00 42.83 ?  234 LEU C C     1 
ATOM   8602 O O     . LEU D 1 242 ? 4.682   27.595  -14.776 1.00 42.69 ?  234 LEU C O     1 
ATOM   8603 C CB    . LEU D 1 242 ? 4.564   25.561  -16.986 1.00 39.50 ?  234 LEU C CB    1 
ATOM   8604 C CG    . LEU D 1 242 ? 5.779   26.116  -17.736 1.00 40.42 ?  234 LEU C CG    1 
ATOM   8605 C CD1   . LEU D 1 242 ? 6.985   25.194  -17.601 1.00 38.93 ?  234 LEU C CD1   1 
ATOM   8606 C CD2   . LEU D 1 242 ? 5.451   26.352  -19.199 1.00 40.18 ?  234 LEU C CD2   1 
ATOM   8607 N N     . ASN D 1 243 ? 6.572   26.446  -14.313 1.00 41.04 ?  235 ASN C N     1 
ATOM   8608 C CA    . ASN D 1 243 ? 7.294   27.594  -13.776 1.00 41.52 ?  235 ASN C CA    1 
ATOM   8609 C C     . ASN D 1 243 ? 7.898   28.337  -14.959 1.00 43.16 ?  235 ASN C C     1 
ATOM   8610 O O     . ASN D 1 243 ? 8.905   27.910  -15.527 1.00 41.86 ?  235 ASN C O     1 
ATOM   8611 C CB    . ASN D 1 243 ? 8.361   27.138  -12.787 1.00 42.50 ?  235 ASN C CB    1 
ATOM   8612 C CG    . ASN D 1 243 ? 9.110   28.295  -12.151 1.00 43.39 ?  235 ASN C CG    1 
ATOM   8613 O OD1   . ASN D 1 243 ? 8.933   29.454  -12.525 1.00 43.42 ?  235 ASN C OD1   1 
ATOM   8614 N ND2   . ASN D 1 243 ? 9.957   27.982  -11.177 1.00 38.70 ?  235 ASN C ND2   1 
ATOM   8615 N N     . THR D 1 244 ? 7.278   29.453  -15.342 1.00 39.78 ?  236 THR C N     1 
ATOM   8616 C CA    . THR D 1 244 ? 7.751   30.220  -16.489 1.00 42.71 ?  236 THR C CA    1 
ATOM   8617 C C     . THR D 1 244 ? 9.110   30.867  -16.251 1.00 45.85 ?  236 THR C C     1 
ATOM   8618 O O     . THR D 1 244 ? 9.700   31.390  -17.201 1.00 42.91 ?  236 THR C O     1 
ATOM   8619 C CB    . THR D 1 244 ? 6.726   31.293  -16.860 1.00 46.22 ?  236 THR C CB    1 
ATOM   8620 O OG1   . THR D 1 244 ? 6.106   31.796  -15.669 1.00 50.87 ?  236 THR C OG1   1 
ATOM   8621 C CG2   . THR D 1 244 ? 5.658   30.712  -17.774 1.00 34.75 ?  236 THR C CG2   1 
ATOM   8622 N N     . GLU D 1 245 ? 9.617   30.842  -15.019 1.00 44.90 ?  237 GLU C N     1 
ATOM   8623 C CA    . GLU D 1 245 ? 10.914  31.418  -14.697 1.00 46.41 ?  237 GLU C CA    1 
ATOM   8624 C C     . GLU D 1 245 ? 12.045  30.397  -14.700 1.00 50.12 ?  237 GLU C C     1 
ATOM   8625 O O     . GLU D 1 245 ? 13.205  30.785  -14.523 1.00 50.13 ?  237 GLU C O     1 
ATOM   8626 C CB    . GLU D 1 245 ? 10.861  32.100  -13.323 1.00 53.72 ?  237 GLU C CB    1 
ATOM   8627 C CG    . GLU D 1 245 ? 10.438  33.561  -13.354 1.00 63.44 ?  237 GLU C CG    1 
ATOM   8628 C CD    . GLU D 1 245 ? 11.561  34.500  -12.954 1.00 77.48 ?  237 GLU C CD    1 
ATOM   8629 O OE1   . GLU D 1 245 ? 11.266  35.653  -12.576 1.00 76.34 ?  237 GLU C OE1   1 
ATOM   8630 O OE2   . GLU D 1 245 ? 12.738  34.085  -13.015 1.00 73.40 ?  237 GLU C OE2   1 
ATOM   8631 N N     . ILE D 1 246 ? 11.745  29.114  -14.906 1.00 46.57 ?  238 ILE C N     1 
ATOM   8632 C CA    . ILE D 1 246 ? 12.766  28.089  -14.713 1.00 41.89 ?  238 ILE C CA    1 
ATOM   8633 C C     . ILE D 1 246 ? 13.662  27.940  -15.938 1.00 41.71 ?  238 ILE C C     1 
ATOM   8634 O O     . ILE D 1 246 ? 14.838  27.581  -15.803 1.00 45.20 ?  238 ILE C O     1 
ATOM   8635 C CB    . ILE D 1 246 ? 12.117  26.747  -14.325 1.00 43.74 ?  238 ILE C CB    1 
ATOM   8636 C CG1   . ILE D 1 246 ? 13.152  25.832  -13.670 1.00 40.36 ?  238 ILE C CG1   1 
ATOM   8637 C CG2   . ILE D 1 246 ? 11.497  26.063  -15.537 1.00 38.55 ?  238 ILE C CG2   1 
ATOM   8638 C CD1   . ILE D 1 246 ? 13.626  26.327  -12.324 1.00 44.36 ?  238 ILE C CD1   1 
ATOM   8639 N N     . TYR D 1 247 ? 13.153  28.212  -17.137 1.00 42.82 ?  239 TYR C N     1 
ATOM   8640 C CA    . TYR D 1 247 ? 13.916  27.986  -18.355 1.00 41.42 ?  239 TYR C CA    1 
ATOM   8641 C C     . TYR D 1 247 ? 14.579  29.274  -18.821 1.00 43.91 ?  239 TYR C C     1 
ATOM   8642 O O     . TYR D 1 247 ? 13.978  30.352  -18.776 1.00 42.99 ?  239 TYR C O     1 
ATOM   8643 C CB    . TYR D 1 247 ? 13.042  27.413  -19.476 1.00 40.49 ?  239 TYR C CB    1 
ATOM   8644 C CG    . TYR D 1 247 ? 11.711  28.101  -19.704 1.00 40.63 ?  239 TYR C CG    1 
ATOM   8645 C CD1   . TYR D 1 247 ? 11.600  29.172  -20.584 1.00 42.64 ?  239 TYR C CD1   1 
ATOM   8646 C CD2   . TYR D 1 247 ? 10.559  27.655  -19.070 1.00 42.46 ?  239 TYR C CD2   1 
ATOM   8647 C CE1   . TYR D 1 247 ? 10.382  29.793  -20.807 1.00 39.98 ?  239 TYR C CE1   1 
ATOM   8648 C CE2   . TYR D 1 247 ? 9.338   28.269  -19.287 1.00 42.62 ?  239 TYR C CE2   1 
ATOM   8649 C CZ    . TYR D 1 247 ? 9.255   29.337  -20.156 1.00 44.30 ?  239 TYR C CZ    1 
ATOM   8650 O OH    . TYR D 1 247 ? 8.041   29.947  -20.372 1.00 43.40 ?  239 TYR C OH    1 
ATOM   8651 N N     . ASP D 1 248 ? 15.830  29.149  -19.267 1.00 42.54 ?  240 ASP C N     1 
ATOM   8652 C CA    . ASP D 1 248 ? 16.602  30.278  -19.765 1.00 45.80 ?  240 ASP C CA    1 
ATOM   8653 C C     . ASP D 1 248 ? 16.371  30.550  -21.244 1.00 44.61 ?  240 ASP C C     1 
ATOM   8654 O O     . ASP D 1 248 ? 16.623  31.672  -21.700 1.00 48.73 ?  240 ASP C O     1 
ATOM   8655 C CB    . ASP D 1 248 ? 18.097  30.039  -19.523 1.00 45.54 ?  240 ASP C CB    1 
ATOM   8656 C CG    . ASP D 1 248 ? 18.414  29.761  -18.066 1.00 46.64 ?  240 ASP C CG    1 
ATOM   8657 O OD1   . ASP D 1 248 ? 18.238  30.674  -17.233 1.00 58.96 ?  240 ASP C OD1   1 
ATOM   8658 O OD2   . ASP D 1 248 ? 18.840  28.629  -17.754 1.00 47.62 ?  240 ASP C OD2   1 
ATOM   8659 N N     . SER D 1 249 ? 15.900  29.561  -21.999 1.00 49.65 ?  241 SER C N     1 
ATOM   8660 C CA    . SER D 1 249 ? 15.674  29.728  -23.427 1.00 44.69 ?  241 SER C CA    1 
ATOM   8661 C C     . SER D 1 249 ? 14.664  28.687  -23.888 1.00 42.59 ?  241 SER C C     1 
ATOM   8662 O O     . SER D 1 249 ? 14.308  27.765  -23.150 1.00 39.09 ?  241 SER C O     1 
ATOM   8663 C CB    . SER D 1 249 ? 16.981  29.612  -24.219 1.00 38.62 ?  241 SER C CB    1 
ATOM   8664 O OG    . SER D 1 249 ? 17.603  28.359  -23.992 1.00 39.80 ?  241 SER C OG    1 
ATOM   8665 N N     . ILE D 1 250 ? 14.208  28.849  -25.127 1.00 39.54 ?  242 ILE C N     1 
ATOM   8666 C CA    . ILE D 1 250 ? 13.233  27.956  -25.739 1.00 40.10 ?  242 ILE C CA    1 
ATOM   8667 C C     . ILE D 1 250 ? 13.778  27.494  -27.082 1.00 40.12 ?  242 ILE C C     1 
ATOM   8668 O O     . ILE D 1 250 ? 14.368  28.284  -27.827 1.00 41.58 ?  242 ILE C O     1 
ATOM   8669 C CB    . ILE D 1 250 ? 11.861  28.644  -25.920 1.00 38.92 ?  242 ILE C CB    1 
ATOM   8670 C CG1   . ILE D 1 250 ? 11.255  29.001  -24.564 1.00 37.98 ?  242 ILE C CG1   1 
ATOM   8671 C CG2   . ILE D 1 250 ? 10.901  27.757  -26.702 1.00 41.94 ?  242 ILE C CG2   1 
ATOM   8672 C CD1   . ILE D 1 250 ? 10.311  30.175  -24.622 1.00 40.08 ?  242 ILE C CD1   1 
ATOM   8673 N N     . ILE D 1 251 ? 13.590  26.213  -27.384 1.00 40.23 ?  243 ILE C N     1 
ATOM   8674 C CA    . ILE D 1 251 ? 13.890  25.660  -28.698 1.00 38.43 ?  243 ILE C CA    1 
ATOM   8675 C C     . ILE D 1 251 ? 12.593  25.123  -29.285 1.00 41.99 ?  243 ILE C C     1 
ATOM   8676 O O     . ILE D 1 251 ? 11.938  24.265  -28.679 1.00 38.29 ?  243 ILE C O     1 
ATOM   8677 C CB    . ILE D 1 251 ? 14.959  24.559  -28.637 1.00 34.61 ?  243 ILE C CB    1 
ATOM   8678 C CG1   . ILE D 1 251 ? 16.313  25.144  -28.231 1.00 37.03 ?  243 ILE C CG1   1 
ATOM   8679 C CG2   . ILE D 1 251 ? 15.070  23.859  -29.981 1.00 37.19 ?  243 ILE C CG2   1 
ATOM   8680 C CD1   . ILE D 1 251 ? 17.341  24.096  -27.862 1.00 29.26 ?  243 ILE C CD1   1 
ATOM   8681 N N     . LYS D 1 252 ? 12.222  25.632  -30.456 1.00 42.78 ?  244 LYS C N     1 
ATOM   8682 C CA    . LYS D 1 252 ? 11.046  25.158  -31.168 1.00 36.19 ?  244 LYS C CA    1 
ATOM   8683 C C     . LYS D 1 252 ? 11.437  24.039  -32.123 1.00 38.26 ?  244 LYS C C     1 
ATOM   8684 O O     . LYS D 1 252 ? 12.446  24.133  -32.829 1.00 44.21 ?  244 LYS C O     1 
ATOM   8685 C CB    . LYS D 1 252 ? 10.383  26.300  -31.939 1.00 39.69 ?  244 LYS C CB    1 
ATOM   8686 C CG    . LYS D 1 252 ? 10.025  27.500  -31.079 1.00 44.88 ?  244 LYS C CG    1 
ATOM   8687 C CD    . LYS D 1 252 ? 9.378   28.599  -31.906 1.00 42.85 ?  244 LYS C CD    1 
ATOM   8688 C CE    . LYS D 1 252 ? 10.415  29.388  -32.687 1.00 51.57 ?  244 LYS C CE    1 
ATOM   8689 N NZ    . LYS D 1 252 ? 9.857   29.928  -33.958 1.00 59.05 ?  244 LYS C NZ    1 
ATOM   8690 N N     . VAL D 1 253 ? 10.635  22.978  -32.140 1.00 45.48 ?  245 VAL C N     1 
ATOM   8691 C CA    . VAL D 1 253 ? 10.902  21.796  -32.950 1.00 38.89 ?  245 VAL C CA    1 
ATOM   8692 C C     . VAL D 1 253 ? 9.750   21.607  -33.925 1.00 38.51 ?  245 VAL C C     1 
ATOM   8693 O O     . VAL D 1 253 ? 8.579   21.705  -33.538 1.00 39.23 ?  245 VAL C O     1 
ATOM   8694 C CB    . VAL D 1 253 ? 11.090  20.542  -32.077 1.00 35.38 ?  245 VAL C CB    1 
ATOM   8695 C CG1   . VAL D 1 253 ? 11.334  19.321  -32.948 1.00 34.55 ?  245 VAL C CG1   1 
ATOM   8696 C CG2   . VAL D 1 253 ? 12.236  20.744  -31.099 1.00 36.11 ?  245 VAL C CG2   1 
ATOM   8697 N N     . GLY D 1 254 ? 10.083  21.339  -35.188 1.00 40.77 ?  246 GLY C N     1 
ATOM   8698 C CA    . GLY D 1 254 ? 9.064   21.083  -36.180 1.00 41.71 ?  246 GLY C CA    1 
ATOM   8699 C C     . GLY D 1 254 ? 8.499   19.679  -36.090 1.00 38.26 ?  246 GLY C C     1 
ATOM   8700 O O     . GLY D 1 254 ? 9.059   18.787  -35.454 1.00 41.59 ?  246 GLY C O     1 
ATOM   8701 N N     . ASN D 1 255 ? 7.354   19.492  -36.748 1.00 34.94 ?  247 ASN C N     1 
ATOM   8702 C CA    . ASN D 1 255 ? 6.698   18.189  -36.741 1.00 43.54 ?  247 ASN C CA    1 
ATOM   8703 C C     . ASN D 1 255 ? 7.547   17.141  -37.450 1.00 43.90 ?  247 ASN C C     1 
ATOM   8704 O O     . ASN D 1 255 ? 7.741   16.031  -36.941 1.00 37.79 ?  247 ASN C O     1 
ATOM   8705 C CB    . ASN D 1 255 ? 5.323   18.294  -37.402 1.00 41.84 ?  247 ASN C CB    1 
ATOM   8706 C CG    . ASN D 1 255 ? 4.370   19.184  -36.632 1.00 44.75 ?  247 ASN C CG    1 
ATOM   8707 O OD1   . ASN D 1 255 ? 4.537   19.411  -35.435 1.00 37.92 ?  247 ASN C OD1   1 
ATOM   8708 N ND2   . ASN D 1 255 ? 3.357   19.697  -37.324 1.00 48.45 ?  247 ASN C ND2   1 
ATOM   8709 N N     . ASP D 1 256 ? 8.067   17.481  -38.632 1.00 35.79 ?  248 ASP C N     1 
ATOM   8710 C CA    . ASP D 1 256 ? 8.760   16.487  -39.445 1.00 36.87 ?  248 ASP C CA    1 
ATOM   8711 C C     . ASP D 1 256 ? 10.124  16.138  -38.861 1.00 38.84 ?  248 ASP C C     1 
ATOM   8712 O O     . ASP D 1 256 ? 10.526  14.968  -38.870 1.00 41.13 ?  248 ASP C O     1 
ATOM   8713 C CB    . ASP D 1 256 ? 8.900   16.994  -40.878 1.00 42.17 ?  248 ASP C CB    1 
ATOM   8714 C CG    . ASP D 1 256 ? 7.672   16.707  -41.716 1.00 47.44 ?  248 ASP C CG    1 
ATOM   8715 O OD1   . ASP D 1 256 ? 6.563   16.651  -41.142 1.00 50.74 ?  248 ASP C OD1   1 
ATOM   8716 O OD2   . ASP D 1 256 ? 7.812   16.543  -42.947 1.00 57.78 ?  248 ASP C OD2   1 
ATOM   8717 N N     . THR D 1 257 ? 10.850  17.133  -38.347 1.00 36.43 ?  249 THR C N     1 
ATOM   8718 C CA    . THR D 1 257 ? 12.180  16.868  -37.812 1.00 38.61 ?  249 THR C CA    1 
ATOM   8719 C C     . THR D 1 257 ? 12.125  16.028  -36.541 1.00 36.50 ?  249 THR C C     1 
ATOM   8720 O O     . THR D 1 257 ? 13.029  15.220  -36.296 1.00 34.49 ?  249 THR C O     1 
ATOM   8721 C CB    . THR D 1 257 ? 12.913  18.180  -37.544 1.00 40.77 ?  249 THR C CB    1 
ATOM   8722 O OG1   . THR D 1 257 ? 14.038  17.930  -36.692 1.00 48.02 ?  249 THR C OG1   1 
ATOM   8723 C CG2   . THR D 1 257 ? 11.988  19.176  -36.875 1.00 40.31 ?  249 THR C CG2   1 
ATOM   8724 N N     . ALA D 1 258 ? 11.088  16.209  -35.721 1.00 31.09 ?  250 ALA C N     1 
ATOM   8725 C CA    . ALA D 1 258 ? 10.948  15.389  -34.523 1.00 32.84 ?  250 ALA C CA    1 
ATOM   8726 C C     . ALA D 1 258 ? 10.652  13.940  -34.882 1.00 35.39 ?  250 ALA C C     1 
ATOM   8727 O O     . ALA D 1 258 ? 11.186  13.016  -34.257 1.00 35.90 ?  250 ALA C O     1 
ATOM   8728 C CB    . ALA D 1 258 ? 9.846   15.949  -33.626 1.00 35.34 ?  250 ALA C CB    1 
ATOM   8729 N N     . MET D 1 259 ? 9.803   13.724  -35.886 1.00 31.65 ?  251 MET C N     1 
ATOM   8730 C CA    . MET D 1 259 ? 9.459   12.363  -36.280 1.00 33.67 ?  251 MET C CA    1 
ATOM   8731 C C     . MET D 1 259 ? 10.637  11.675  -36.958 1.00 32.36 ?  251 MET C C     1 
ATOM   8732 O O     . MET D 1 259 ? 10.873  10.480  -36.742 1.00 34.72 ?  251 MET C O     1 
ATOM   8733 C CB    . MET D 1 259 ? 8.235   12.379  -37.195 1.00 43.70 ?  251 MET C CB    1 
ATOM   8734 C CG    . MET D 1 259 ? 8.103   11.165  -38.097 1.00 51.33 ?  251 MET C CG    1 
ATOM   8735 S SD    . MET D 1 259 ? 6.527   11.146  -38.970 1.00 67.17 ?  251 MET C SD    1 
ATOM   8736 C CE    . MET D 1 259 ? 5.426   11.744  -37.688 1.00 52.57 ?  251 MET C CE    1 
ATOM   8737 N N     . GLU D 1 260 ? 11.390  12.418  -37.774 1.00 35.31 ?  252 GLU C N     1 
ATOM   8738 C CA    . GLU D 1 260 ? 12.569  11.849  -38.417 1.00 33.41 ?  252 GLU C CA    1 
ATOM   8739 C C     . GLU D 1 260 ? 13.630  11.474  -37.390 1.00 30.19 ?  252 GLU C C     1 
ATOM   8740 O O     . GLU D 1 260 ? 14.305  10.447  -37.529 1.00 33.97 ?  252 GLU C O     1 
ATOM   8741 C CB    . GLU D 1 260 ? 13.135  12.836  -39.437 1.00 33.75 ?  252 GLU C CB    1 
ATOM   8742 N N     . MET D 1 261 ? 13.790  12.295  -36.349 1.00 33.19 ?  253 MET C N     1 
ATOM   8743 C CA    . MET D 1 261 ? 14.774  11.992  -35.313 1.00 33.71 ?  253 MET C CA    1 
ATOM   8744 C C     . MET D 1 261 ? 14.373  10.759  -34.514 1.00 31.76 ?  253 MET C C     1 
ATOM   8745 O O     . MET D 1 261 ? 15.225  9.926   -34.182 1.00 29.95 ?  253 MET C O     1 
ATOM   8746 C CB    . MET D 1 261 ? 14.953  13.198  -34.391 1.00 28.73 ?  253 MET C CB    1 
ATOM   8747 C CG    . MET D 1 261 ? 15.995  12.998  -33.305 1.00 35.52 ?  253 MET C CG    1 
ATOM   8748 S SD    . MET D 1 261 ? 17.652  12.749  -33.971 1.00 43.58 ?  253 MET C SD    1 
ATOM   8749 C CE    . MET D 1 261 ? 17.951  14.347  -34.720 1.00 34.83 ?  253 MET C CE    1 
ATOM   8750 N N     . SER D 1 262 ? 13.082  10.626  -34.195 1.00 29.14 ?  254 SER C N     1 
ATOM   8751 C CA    . SER D 1 262 ? 12.609  9.438   -33.489 1.00 30.94 ?  254 SER C CA    1 
ATOM   8752 C C     . SER D 1 262 ? 12.927  8.169   -34.270 1.00 28.46 ?  254 SER C C     1 
ATOM   8753 O O     . SER D 1 262 ? 13.342  7.160   -33.687 1.00 29.11 ?  254 SER C O     1 
ATOM   8754 C CB    . SER D 1 262 ? 11.106  9.542   -33.230 1.00 27.21 ?  254 SER C CB    1 
ATOM   8755 O OG    . SER D 1 262 ? 10.832  10.263  -32.042 1.00 36.05 ?  254 SER C OG    1 
ATOM   8756 N N     . ARG D 1 263 ? 12.740  8.203   -35.593 1.00 28.36 ?  255 ARG C N     1 
ATOM   8757 C CA    . ARG D 1 263 ? 13.061  7.047   -36.422 1.00 29.82 ?  255 ARG C CA    1 
ATOM   8758 C C     . ARG D 1 263 ? 14.564  6.799   -36.462 1.00 31.60 ?  255 ARG C C     1 
ATOM   8759 O O     . ARG D 1 263 ? 15.010  5.645   -36.454 1.00 32.32 ?  255 ARG C O     1 
ATOM   8760 C CB    . ARG D 1 263 ? 12.518  7.252   -37.835 1.00 27.96 ?  255 ARG C CB    1 
ATOM   8761 C CG    . ARG D 1 263 ? 11.004  7.242   -37.925 1.00 34.73 ?  255 ARG C CG    1 
ATOM   8762 C CD    . ARG D 1 263 ? 10.526  7.934   -39.190 1.00 43.11 ?  255 ARG C CD    1 
ATOM   8763 N NE    . ARG D 1 263 ? 9.218   7.447   -39.614 1.00 52.81 ?  255 ARG C NE    1 
ATOM   8764 C CZ    . ARG D 1 263 ? 8.481   8.004   -40.565 1.00 59.98 ?  255 ARG C CZ    1 
ATOM   8765 N NH1   . ARG D 1 263 ? 8.887   9.084   -41.212 1.00 59.32 ?  255 ARG C NH1   1 
ATOM   8766 N NH2   . ARG D 1 263 ? 7.305   7.465   -40.872 1.00 57.52 ?  255 ARG C NH2   1 
ATOM   8767 N N     . ARG D 1 264 ? 15.358  7.871   -36.506 1.00 33.58 ?  256 ARG C N     1 
ATOM   8768 C CA    . ARG D 1 264 ? 16.810  7.726   -36.529 1.00 32.64 ?  256 ARG C CA    1 
ATOM   8769 C C     . ARG D 1 264 ? 17.320  7.106   -35.233 1.00 34.15 ?  256 ARG C C     1 
ATOM   8770 O O     . ARG D 1 264 ? 18.133  6.175   -35.254 1.00 32.65 ?  256 ARG C O     1 
ATOM   8771 C CB    . ARG D 1 264 ? 17.465  9.086   -36.770 1.00 31.01 ?  256 ARG C CB    1 
ATOM   8772 C CG    . ARG D 1 264 ? 18.006  9.292   -38.174 1.00 41.63 ?  256 ARG C CG    1 
ATOM   8773 C CD    . ARG D 1 264 ? 19.062  10.388  -38.184 1.00 44.08 ?  256 ARG C CD    1 
ATOM   8774 N NE    . ARG D 1 264 ? 20.413  9.839   -38.196 1.00 48.88 ?  256 ARG C NE    1 
ATOM   8775 C CZ    . ARG D 1 264 ? 21.519  10.570  -38.183 1.00 47.52 ?  256 ARG C CZ    1 
ATOM   8776 N NH1   . ARG D 1 264 ? 21.474  11.892  -38.147 1.00 51.24 ?  256 ARG C NH1   1 
ATOM   8777 N NH2   . ARG D 1 264 ? 22.701  9.960   -38.198 1.00 45.71 ?  256 ARG C NH2   1 
ATOM   8778 N N     . VAL D 1 265 ? 16.847  7.612   -34.090 1.00 34.26 ?  257 VAL C N     1 
ATOM   8779 C CA    . VAL D 1 265 ? 17.310  7.110   -32.798 1.00 29.67 ?  257 VAL C CA    1 
ATOM   8780 C C     . VAL D 1 265 ? 16.925  5.646   -32.621 1.00 33.80 ?  257 VAL C C     1 
ATOM   8781 O O     . VAL D 1 265 ? 17.698  4.845   -32.080 1.00 27.47 ?  257 VAL C O     1 
ATOM   8782 C CB    . VAL D 1 265 ? 16.754  7.985   -31.659 1.00 30.20 ?  257 VAL C CB    1 
ATOM   8783 C CG1   . VAL D 1 265 ? 17.049  7.357   -30.305 1.00 28.46 ?  257 VAL C CG1   1 
ATOM   8784 C CG2   . VAL D 1 265 ? 17.332  9.390   -31.736 1.00 32.18 ?  257 VAL C CG2   1 
ATOM   8785 N N     . ALA D 1 266 ? 15.727  5.273   -33.078 1.00 30.80 ?  258 ALA C N     1 
ATOM   8786 C CA    . ALA D 1 266 ? 15.295  3.885   -32.962 1.00 28.47 ?  258 ALA C CA    1 
ATOM   8787 C C     . ALA D 1 266 ? 16.177  2.961   -33.791 1.00 31.57 ?  258 ALA C C     1 
ATOM   8788 O O     . ALA D 1 266 ? 16.553  1.874   -33.334 1.00 29.47 ?  258 ALA C O     1 
ATOM   8789 C CB    . ALA D 1 266 ? 13.831  3.757   -33.386 1.00 26.79 ?  258 ALA C CB    1 
ATOM   8790 N N     . LYS D 1 267 ? 16.535  3.381   -35.005 1.00 31.47 ?  259 LYS C N     1 
ATOM   8791 C CA    . LYS D 1 267 ? 17.291  2.506   -35.892 1.00 32.33 ?  259 LYS C CA    1 
ATOM   8792 C C     . LYS D 1 267 ? 18.778  2.491   -35.556 1.00 29.35 ?  259 LYS C C     1 
ATOM   8793 O O     . LYS D 1 267 ? 19.433  1.451   -35.686 1.00 33.18 ?  259 LYS C O     1 
ATOM   8794 C CB    . LYS D 1 267 ? 17.083  2.929   -37.346 1.00 34.53 ?  259 LYS C CB    1 
ATOM   8795 C CG    . LYS D 1 267 ? 15.733  2.533   -37.921 1.00 35.89 ?  259 LYS C CG    1 
ATOM   8796 C CD    . LYS D 1 267 ? 15.511  3.155   -39.291 1.00 38.39 ?  259 LYS C CD    1 
ATOM   8797 C CE    . LYS D 1 267 ? 14.094  3.686   -39.429 1.00 44.01 ?  259 LYS C CE    1 
ATOM   8798 N NZ    . LYS D 1 267 ? 13.454  3.230   -40.690 1.00 49.17 ?  259 LYS C NZ    1 
ATOM   8799 N N     . GLU D 1 268 ? 19.328  3.627   -35.122 1.00 29.85 ?  260 GLU C N     1 
ATOM   8800 C CA    . GLU D 1 268 ? 20.770  3.759   -34.956 1.00 28.28 ?  260 GLU C CA    1 
ATOM   8801 C C     . GLU D 1 268 ? 21.241  3.647   -33.512 1.00 32.15 ?  260 GLU C C     1 
ATOM   8802 O O     . GLU D 1 268 ? 22.429  3.391   -33.288 1.00 33.40 ?  260 GLU C O     1 
ATOM   8803 C CB    . GLU D 1 268 ? 21.250  5.093   -35.540 1.00 28.15 ?  260 GLU C CB    1 
ATOM   8804 C CG    . GLU D 1 268 ? 21.130  5.159   -37.053 1.00 30.02 ?  260 GLU C CG    1 
ATOM   8805 C CD    . GLU D 1 268 ? 21.161  6.576   -37.589 1.00 42.31 ?  260 GLU C CD    1 
ATOM   8806 O OE1   . GLU D 1 268 ? 22.133  7.306   -37.298 1.00 39.92 ?  260 GLU C OE1   1 
ATOM   8807 O OE2   . GLU D 1 268 ? 20.214  6.955   -38.308 1.00 45.66 ?  260 GLU C OE2   1 
ATOM   8808 N N     . GLU D 1 269 ? 20.355  3.831   -32.534 1.00 28.40 ?  261 GLU C N     1 
ATOM   8809 C CA    . GLU D 1 269 ? 20.702  3.646   -31.132 1.00 31.93 ?  261 GLU C CA    1 
ATOM   8810 C C     . GLU D 1 269 ? 19.981  2.476   -30.482 1.00 31.86 ?  261 GLU C C     1 
ATOM   8811 O O     . GLU D 1 269 ? 20.388  2.048   -29.396 1.00 33.08 ?  261 GLU C O     1 
ATOM   8812 C CB    . GLU D 1 269 ? 20.401  4.920   -30.326 1.00 28.40 ?  261 GLU C CB    1 
ATOM   8813 C CG    . GLU D 1 269 ? 20.791  6.217   -31.014 1.00 29.15 ?  261 GLU C CG    1 
ATOM   8814 C CD    . GLU D 1 269 ? 22.252  6.568   -30.806 1.00 35.59 ?  261 GLU C CD    1 
ATOM   8815 O OE1   . GLU D 1 269 ? 22.879  5.998   -29.887 1.00 31.72 ?  261 GLU C OE1   1 
ATOM   8816 O OE2   . GLU D 1 269 ? 22.773  7.423   -31.555 1.00 37.09 ?  261 GLU C OE2   1 
ATOM   8817 N N     . GLY D 1 270 ? 18.936  1.944   -31.111 1.00 31.67 ?  262 GLY C N     1 
ATOM   8818 C CA    . GLY D 1 270 ? 18.124  0.933   -30.467 1.00 31.22 ?  262 GLY C CA    1 
ATOM   8819 C C     . GLY D 1 270 ? 17.180  1.476   -29.422 1.00 29.79 ?  262 GLY C C     1 
ATOM   8820 O O     . GLY D 1 270 ? 16.664  0.707   -28.604 1.00 28.28 ?  262 GLY C O     1 
ATOM   8821 N N     . ILE D 1 271 ? 16.940  2.781   -29.422 1.00 27.05 ?  263 ILE C N     1 
ATOM   8822 C CA    . ILE D 1 271 ? 16.072  3.440   -28.456 1.00 28.46 ?  263 ILE C CA    1 
ATOM   8823 C C     . ILE D 1 271 ? 14.809  3.845   -29.204 1.00 30.52 ?  263 ILE C C     1 
ATOM   8824 O O     . ILE D 1 271 ? 14.799  4.833   -29.948 1.00 30.67 ?  263 ILE C O     1 
ATOM   8825 C CB    . ILE D 1 271 ? 16.756  4.646   -27.804 1.00 29.96 ?  263 ILE C CB    1 
ATOM   8826 C CG1   . ILE D 1 271 ? 17.985  4.196   -27.015 1.00 30.67 ?  263 ILE C CG1   1 
ATOM   8827 C CG2   . ILE D 1 271 ? 15.786  5.384   -26.900 1.00 27.02 ?  263 ILE C CG2   1 
ATOM   8828 C CD1   . ILE D 1 271 ? 18.971  5.308   -26.728 1.00 31.29 ?  263 ILE C CD1   1 
ATOM   8829 N N     . LEU D 1 272 ? 13.736  3.083   -29.011 1.00 29.33 ?  264 LEU C N     1 
ATOM   8830 C CA    . LEU D 1 272 ? 12.467  3.311   -29.694 1.00 29.23 ?  264 LEU C CA    1 
ATOM   8831 C C     . LEU D 1 272 ? 11.576  4.144   -28.779 1.00 30.55 ?  264 LEU C C     1 
ATOM   8832 O O     . LEU D 1 272 ? 11.098  3.652   -27.751 1.00 34.39 ?  264 LEU C O     1 
ATOM   8833 C CB    . LEU D 1 272 ? 11.807  1.984   -30.050 1.00 28.49 ?  264 LEU C CB    1 
ATOM   8834 C CG    . LEU D 1 272 ? 10.372  2.048   -30.557 1.00 31.37 ?  264 LEU C CG    1 
ATOM   8835 C CD1   . LEU D 1 272 ? 10.357  2.420   -32.025 1.00 33.20 ?  264 LEU C CD1   1 
ATOM   8836 C CD2   . LEU D 1 272 ? 9.688   0.718   -30.326 1.00 31.55 ?  264 LEU C CD2   1 
ATOM   8837 N N     . ALA D 1 273 ? 11.349  5.400   -29.152 1.00 29.45 ?  265 ALA C N     1 
ATOM   8838 C CA    . ALA D 1 273 ? 10.656  6.345   -28.291 1.00 29.61 ?  265 ALA C CA    1 
ATOM   8839 C C     . ALA D 1 273 ? 9.617   7.121   -29.093 1.00 29.95 ?  265 ALA C C     1 
ATOM   8840 O O     . ALA D 1 273 ? 9.593   7.084   -30.326 1.00 30.41 ?  265 ALA C O     1 
ATOM   8841 C CB    . ALA D 1 273 ? 11.652  7.300   -27.619 1.00 31.47 ?  265 ALA C CB    1 
ATOM   8842 N N     . GLY D 1 274 ? 8.750   7.827   -28.373 1.00 27.56 ?  266 GLY C N     1 
ATOM   8843 C CA    . GLY D 1 274 ? 7.681   8.586   -28.990 1.00 29.32 ?  266 GLY C CA    1 
ATOM   8844 C C     . GLY D 1 274 ? 8.191   9.795   -29.757 1.00 28.54 ?  266 GLY C C     1 
ATOM   8845 O O     . GLY D 1 274 ? 9.387   10.085  -29.820 1.00 26.73 ?  266 GLY C O     1 
ATOM   8846 N N     . ILE D 1 275 ? 7.243   10.525  -30.350 1.00 30.03 ?  267 ILE C N     1 
ATOM   8847 C CA    . ILE D 1 275 ? 7.604   11.662  -31.194 1.00 29.07 ?  267 ILE C CA    1 
ATOM   8848 C C     . ILE D 1 275 ? 8.152   12.810  -30.350 1.00 30.03 ?  267 ILE C C     1 
ATOM   8849 O O     . ILE D 1 275 ? 9.106   13.488  -30.749 1.00 30.86 ?  267 ILE C O     1 
ATOM   8850 C CB    . ILE D 1 275 ? 6.402   12.101  -32.054 1.00 32.32 ?  267 ILE C CB    1 
ATOM   8851 C CG1   . ILE D 1 275 ? 6.766   13.315  -32.916 1.00 38.71 ?  267 ILE C CG1   1 
ATOM   8852 C CG2   . ILE D 1 275 ? 5.181   12.394  -31.190 1.00 32.46 ?  267 ILE C CG2   1 
ATOM   8853 C CD1   . ILE D 1 275 ? 6.203   13.260  -34.323 1.00 45.15 ?  267 ILE C CD1   1 
ATOM   8854 N N     . SER D 1 276 ? 7.570   13.042  -29.170 1.00 24.93 ?  268 SER C N     1 
ATOM   8855 C CA    . SER D 1 276 ? 8.071   14.100  -28.297 1.00 27.96 ?  268 SER C CA    1 
ATOM   8856 C C     . SER D 1 276 ? 9.490   13.810  -27.828 1.00 33.89 ?  268 SER C C     1 
ATOM   8857 O O     . SER D 1 276 ? 10.250  14.741  -27.536 1.00 32.28 ?  268 SER C O     1 
ATOM   8858 C CB    . SER D 1 276 ? 7.141   14.275  -27.097 1.00 27.54 ?  268 SER C CB    1 
ATOM   8859 O OG    . SER D 1 276 ? 7.295   13.205  -26.183 1.00 30.25 ?  268 SER C OG    1 
ATOM   8860 N N     . SER D 1 277 ? 9.863   12.532  -27.745 1.00 31.59 ?  269 SER C N     1 
ATOM   8861 C CA    . SER D 1 277 ? 11.247  12.190  -27.440 1.00 26.78 ?  269 SER C CA    1 
ATOM   8862 C C     . SER D 1 277 ? 12.159  12.536  -28.607 1.00 31.57 ?  269 SER C C     1 
ATOM   8863 O O     . SER D 1 277 ? 13.300  12.966  -28.406 1.00 29.59 ?  269 SER C O     1 
ATOM   8864 C CB    . SER D 1 277 ? 11.358  10.708  -27.096 1.00 29.36 ?  269 SER C CB    1 
ATOM   8865 O OG    . SER D 1 277 ? 10.552  10.373  -25.982 1.00 32.53 ?  269 SER C OG    1 
ATOM   8866 N N     . GLY D 1 278 ? 11.674  12.349  -29.837 1.00 26.85 ?  270 GLY C N     1 
ATOM   8867 C CA    . GLY D 1 278 ? 12.440  12.781  -30.993 1.00 31.05 ?  270 GLY C CA    1 
ATOM   8868 C C     . GLY D 1 278 ? 12.643  14.282  -31.018 1.00 33.20 ?  270 GLY C C     1 
ATOM   8869 O O     . GLY D 1 278 ? 13.702  14.769  -31.419 1.00 34.09 ?  270 GLY C O     1 
ATOM   8870 N N     . ALA D 1 279 ? 11.628  15.036  -30.587 1.00 33.11 ?  271 ALA C N     1 
ATOM   8871 C CA    . ALA D 1 279 ? 11.783  16.482  -30.469 1.00 34.80 ?  271 ALA C CA    1 
ATOM   8872 C C     . ALA D 1 279 ? 12.794  16.836  -29.387 1.00 35.83 ?  271 ALA C C     1 
ATOM   8873 O O     . ALA D 1 279 ? 13.623  17.736  -29.571 1.00 35.41 ?  271 ALA C O     1 
ATOM   8874 C CB    . ALA D 1 279 ? 10.431  17.134  -30.178 1.00 29.20 ?  271 ALA C CB    1 
ATOM   8875 N N     . ALA D 1 280 ? 12.748  16.130  -28.253 1.00 34.24 ?  272 ALA C N     1 
ATOM   8876 C CA    . ALA D 1 280 ? 13.690  16.394  -27.170 1.00 35.97 ?  272 ALA C CA    1 
ATOM   8877 C C     . ALA D 1 280 ? 15.118  16.056  -27.579 1.00 34.34 ?  272 ALA C C     1 
ATOM   8878 O O     . ALA D 1 280 ? 16.057  16.781  -27.230 1.00 30.91 ?  272 ALA C O     1 
ATOM   8879 C CB    . ALA D 1 280 ? 13.289  15.607  -25.923 1.00 31.02 ?  272 ALA C CB    1 
ATOM   8880 N N     . ILE D 1 281 ? 15.303  14.958  -28.316 1.00 32.11 ?  273 ILE C N     1 
ATOM   8881 C CA    . ILE D 1 281 ? 16.648  14.575  -28.734 1.00 35.97 ?  273 ILE C CA    1 
ATOM   8882 C C     . ILE D 1 281 ? 17.160  15.506  -29.827 1.00 36.16 ?  273 ILE C C     1 
ATOM   8883 O O     . ILE D 1 281 ? 18.356  15.821  -29.872 1.00 37.18 ?  273 ILE C O     1 
ATOM   8884 C CB    . ILE D 1 281 ? 16.666  13.100  -29.180 1.00 36.23 ?  273 ILE C CB    1 
ATOM   8885 C CG1   . ILE D 1 281 ? 16.474  12.185  -27.969 1.00 32.33 ?  273 ILE C CG1   1 
ATOM   8886 C CG2   . ILE D 1 281 ? 17.964  12.763  -29.909 1.00 33.09 ?  273 ILE C CG2   1 
ATOM   8887 C CD1   . ILE D 1 281 ? 16.614  10.714  -28.282 1.00 28.05 ?  273 ILE C CD1   1 
ATOM   8888 N N     . TYR D 1 282 ? 16.276  15.974  -30.712 1.00 37.34 ?  274 TYR C N     1 
ATOM   8889 C CA    . TYR D 1 282 ? 16.708  16.905  -31.750 1.00 35.75 ?  274 TYR C CA    1 
ATOM   8890 C C     . TYR D 1 282 ? 17.145  18.237  -31.154 1.00 41.60 ?  274 TYR C C     1 
ATOM   8891 O O     . TYR D 1 282 ? 18.144  18.821  -31.592 1.00 39.55 ?  274 TYR C O     1 
ATOM   8892 C CB    . TYR D 1 282 ? 15.596  17.111  -32.780 1.00 35.06 ?  274 TYR C CB    1 
ATOM   8893 C CG    . TYR D 1 282 ? 15.965  18.087  -33.878 1.00 36.32 ?  274 TYR C CG    1 
ATOM   8894 C CD1   . TYR D 1 282 ? 16.591  17.646  -35.036 1.00 43.35 ?  274 TYR C CD1   1 
ATOM   8895 C CD2   . TYR D 1 282 ? 15.661  19.441  -33.773 1.00 38.07 ?  274 TYR C CD2   1 
ATOM   8896 C CE1   . TYR D 1 282 ? 16.934  18.529  -36.046 1.00 47.94 ?  274 TYR C CE1   1 
ATOM   8897 C CE2   . TYR D 1 282 ? 15.996  20.332  -34.781 1.00 43.76 ?  274 TYR C CE2   1 
ATOM   8898 C CZ    . TYR D 1 282 ? 16.630  19.868  -35.917 1.00 43.20 ?  274 TYR C CZ    1 
ATOM   8899 O OH    . TYR D 1 282 ? 16.963  20.748  -36.923 1.00 47.37 ?  274 TYR C OH    1 
ATOM   8900 N N     . ALA D 1 283 ? 16.414  18.731  -30.156 1.00 35.00 ?  275 ALA C N     1 
ATOM   8901 C CA    . ALA D 1 283 ? 16.796  19.986  -29.522 1.00 34.69 ?  275 ALA C CA    1 
ATOM   8902 C C     . ALA D 1 283 ? 18.058  19.820  -28.686 1.00 38.90 ?  275 ALA C C     1 
ATOM   8903 O O     . ALA D 1 283 ? 18.884  20.736  -28.611 1.00 34.42 ?  275 ALA C O     1 
ATOM   8904 C CB    . ALA D 1 283 ? 15.648  20.514  -28.664 1.00 37.44 ?  275 ALA C CB    1 
ATOM   8905 N N     . ALA D 1 284 ? 18.224  18.659  -28.047 1.00 35.55 ?  276 ALA C N     1 
ATOM   8906 C CA    . ALA D 1 284 ? 19.423  18.427  -27.249 1.00 36.72 ?  276 ALA C CA    1 
ATOM   8907 C C     . ALA D 1 284 ? 20.661  18.324  -28.130 1.00 39.79 ?  276 ALA C C     1 
ATOM   8908 O O     . ALA D 1 284 ? 21.737  18.806  -27.758 1.00 37.99 ?  276 ALA C O     1 
ATOM   8909 C CB    . ALA D 1 284 ? 19.257  17.167  -26.400 1.00 36.38 ?  276 ALA C CB    1 
ATOM   8910 N N     . ILE D 1 285 ? 20.529  17.697  -29.302 1.00 38.72 ?  277 ILE C N     1 
ATOM   8911 C CA    . ILE D 1 285 ? 21.640  17.655  -30.246 1.00 38.73 ?  277 ILE C CA    1 
ATOM   8912 C C     . ILE D 1 285 ? 21.935  19.051  -30.777 1.00 38.33 ?  277 ILE C C     1 
ATOM   8913 O O     . ILE D 1 285 ? 23.100  19.437  -30.939 1.00 39.39 ?  277 ILE C O     1 
ATOM   8914 C CB    . ILE D 1 285 ? 21.336  16.660  -31.380 1.00 36.61 ?  277 ILE C CB    1 
ATOM   8915 C CG1   . ILE D 1 285 ? 21.375  15.228  -30.848 1.00 39.30 ?  277 ILE C CG1   1 
ATOM   8916 C CG2   . ILE D 1 285 ? 22.324  16.824  -32.526 1.00 38.80 ?  277 ILE C CG2   1 
ATOM   8917 C CD1   . ILE D 1 285 ? 20.935  14.195  -31.854 1.00 36.25 ?  277 ILE C CD1   1 
ATOM   8918 N N     . GLN D 1 286 ? 20.887  19.831  -31.052 1.00 40.07 ?  278 GLN C N     1 
ATOM   8919 C CA    . GLN D 1 286 ? 21.066  21.234  -31.411 1.00 40.63 ?  278 GLN C CA    1 
ATOM   8920 C C     . GLN D 1 286 ? 21.866  21.972  -30.344 1.00 38.29 ?  278 GLN C C     1 
ATOM   8921 O O     . GLN D 1 286 ? 22.806  22.712  -30.652 1.00 41.51 ?  278 GLN C O     1 
ATOM   8922 C CB    . GLN D 1 286 ? 19.703  21.894  -31.611 1.00 40.51 ?  278 GLN C CB    1 
ATOM   8923 C CG    . GLN D 1 286 ? 19.681  22.986  -32.662 1.00 47.15 ?  278 GLN C CG    1 
ATOM   8924 C CD    . GLN D 1 286 ? 18.510  23.930  -32.484 1.00 48.04 ?  278 GLN C CD    1 
ATOM   8925 O OE1   . GLN D 1 286 ? 17.585  23.951  -33.296 1.00 48.31 ?  278 GLN C OE1   1 
ATOM   8926 N NE2   . GLN D 1 286 ? 18.542  24.718  -31.415 1.00 43.15 ?  278 GLN C NE2   1 
ATOM   8927 N N     . LYS D 1 287 ? 21.502  21.772  -29.075 1.00 39.04 ?  279 LYS C N     1 
ATOM   8928 C CA    . LYS D 1 287 ? 22.231  22.407  -27.982 1.00 37.83 ?  279 LYS C CA    1 
ATOM   8929 C C     . LYS D 1 287 ? 23.648  21.856  -27.870 1.00 40.24 ?  279 LYS C C     1 
ATOM   8930 O O     . LYS D 1 287 ? 24.592  22.604  -27.589 1.00 39.00 ?  279 LYS C O     1 
ATOM   8931 C CB    . LYS D 1 287 ? 21.470  22.212  -26.670 1.00 38.47 ?  279 LYS C CB    1 
ATOM   8932 C CG    . LYS D 1 287 ? 22.163  22.792  -25.449 1.00 31.31 ?  279 LYS C CG    1 
ATOM   8933 C CD    . LYS D 1 287 ? 22.449  24.271  -25.627 1.00 40.45 ?  279 LYS C CD    1 
ATOM   8934 C CE    . LYS D 1 287 ? 21.165  25.081  -25.685 1.00 44.05 ?  279 LYS C CE    1 
ATOM   8935 N NZ    . LYS D 1 287 ? 21.447  26.541  -25.732 1.00 41.20 ?  279 LYS C NZ    1 
ATOM   8936 N N     . ALA D 1 288 ? 23.816  20.549  -28.091 1.00 33.92 ?  280 ALA C N     1 
ATOM   8937 C CA    . ALA D 1 288 ? 25.141  19.944  -27.999 1.00 39.50 ?  280 ALA C CA    1 
ATOM   8938 C C     . ALA D 1 288 ? 26.071  20.469  -29.085 1.00 40.10 ?  280 ALA C C     1 
ATOM   8939 O O     . ALA D 1 288 ? 27.261  20.694  -28.834 1.00 43.63 ?  280 ALA C O     1 
ATOM   8940 C CB    . ALA D 1 288 ? 25.032  18.422  -28.078 1.00 38.17 ?  280 ALA C CB    1 
ATOM   8941 N N     . LYS D 1 289 ? 25.553  20.655  -30.302 1.00 39.71 ?  281 LYS C N     1 
ATOM   8942 C CA    . LYS D 1 289 ? 26.351  21.280  -31.352 1.00 40.94 ?  281 LYS C CA    1 
ATOM   8943 C C     . LYS D 1 289 ? 26.801  22.673  -30.933 1.00 43.95 ?  281 LYS C C     1 
ATOM   8944 O O     . LYS D 1 289 ? 27.941  23.075  -31.195 1.00 42.47 ?  281 LYS C O     1 
ATOM   8945 C CB    . LYS D 1 289 ? 25.550  21.354  -32.651 1.00 34.87 ?  281 LYS C CB    1 
ATOM   8946 C CG    . LYS D 1 289 ? 25.218  20.013  -33.279 1.00 40.20 ?  281 LYS C CG    1 
ATOM   8947 C CD    . LYS D 1 289 ? 24.462  20.215  -34.583 1.00 41.36 ?  281 LYS C CD    1 
ATOM   8948 C CE    . LYS D 1 289 ? 24.210  18.900  -35.298 1.00 35.68 ?  281 LYS C CE    1 
ATOM   8949 N NZ    . LYS D 1 289 ? 23.195  19.054  -36.378 1.00 45.82 ?  281 LYS C NZ    1 
ATOM   8950 N N     . GLU D 1 290 ? 25.915  23.418  -30.269 1.00 41.00 ?  282 GLU C N     1 
ATOM   8951 C CA    . GLU D 1 290 ? 26.239  24.768  -29.822 1.00 42.21 ?  282 GLU C CA    1 
ATOM   8952 C C     . GLU D 1 290 ? 27.294  24.755  -28.722 1.00 43.95 ?  282 GLU C C     1 
ATOM   8953 O O     . GLU D 1 290 ? 28.151  25.645  -28.666 1.00 42.75 ?  282 GLU C O     1 
ATOM   8954 C CB    . GLU D 1 290 ? 24.962  25.461  -29.344 1.00 42.10 ?  282 GLU C CB    1 
ATOM   8955 C CG    . GLU D 1 290 ? 25.174  26.686  -28.472 1.00 45.55 ?  282 GLU C CG    1 
ATOM   8956 C CD    . GLU D 1 290 ? 23.865  27.284  -27.990 1.00 52.34 ?  282 GLU C CD    1 
ATOM   8957 O OE1   . GLU D 1 290 ? 22.799  26.889  -28.510 1.00 45.80 ?  282 GLU C OE1   1 
ATOM   8958 O OE2   . GLU D 1 290 ? 23.900  28.144  -27.084 1.00 53.15 ?  282 GLU C OE2   1 
ATOM   8959 N N     . LEU D 1 291 ? 27.254  23.751  -27.845 1.00 44.18 ?  283 LEU C N     1 
ATOM   8960 C CA    . LEU D 1 291 ? 28.121  23.723  -26.674 1.00 42.76 ?  283 LEU C CA    1 
ATOM   8961 C C     . LEU D 1 291 ? 29.498  23.133  -26.951 1.00 45.06 ?  283 LEU C C     1 
ATOM   8962 O O     . LEU D 1 291 ? 30.448  23.452  -26.227 1.00 47.08 ?  283 LEU C O     1 
ATOM   8963 C CB    . LEU D 1 291 ? 27.445  22.942  -25.541 1.00 43.14 ?  283 LEU C CB    1 
ATOM   8964 C CG    . LEU D 1 291 ? 26.767  23.785  -24.455 1.00 42.23 ?  283 LEU C CG    1 
ATOM   8965 C CD1   . LEU D 1 291 ? 25.996  24.946  -25.066 1.00 48.05 ?  283 LEU C CD1   1 
ATOM   8966 C CD2   . LEU D 1 291 ? 25.846  22.926  -23.600 1.00 43.44 ?  283 LEU C CD2   1 
ATOM   8967 N N     . GLY D 1 292 ? 29.633  22.287  -27.970 1.00 49.81 ?  284 GLY C N     1 
ATOM   8968 C CA    . GLY D 1 292 ? 30.924  21.756  -28.353 1.00 44.07 ?  284 GLY C CA    1 
ATOM   8969 C C     . GLY D 1 292 ? 31.336  20.538  -27.544 1.00 43.10 ?  284 GLY C C     1 
ATOM   8970 O O     . GLY D 1 292 ? 30.744  20.187  -26.523 1.00 40.09 ?  284 GLY C O     1 
ATOM   8971 N N     . LYS D 1 293 ? 32.396  19.889  -28.022 1.00 48.18 ?  285 LYS C N     1 
ATOM   8972 C CA    . LYS D 1 293 ? 32.877  18.658  -27.410 1.00 42.54 ?  285 LYS C CA    1 
ATOM   8973 C C     . LYS D 1 293 ? 33.331  18.903  -25.976 1.00 46.19 ?  285 LYS C C     1 
ATOM   8974 O O     . LYS D 1 293 ? 33.908  19.947  -25.658 1.00 49.58 ?  285 LYS C O     1 
ATOM   8975 C CB    . LYS D 1 293 ? 34.034  18.091  -28.230 1.00 45.39 ?  285 LYS C CB    1 
ATOM   8976 C CG    . LYS D 1 293 ? 34.918  19.170  -28.846 1.00 56.11 ?  285 LYS C CG    1 
ATOM   8977 C CD    . LYS D 1 293 ? 35.476  18.758  -30.198 1.00 51.59 ?  285 LYS C CD    1 
ATOM   8978 C CE    . LYS D 1 293 ? 36.199  17.423  -30.117 1.00 54.01 ?  285 LYS C CE    1 
ATOM   8979 N NZ    . LYS D 1 293 ? 36.618  16.935  -31.460 1.00 53.76 ?  285 LYS C NZ    1 
ATOM   8980 N N     . GLY D 1 294 ? 33.067  17.929  -25.106 1.00 44.47 ?  286 GLY C N     1 
ATOM   8981 C CA    . GLY D 1 294 ? 33.513  17.980  -23.729 1.00 41.90 ?  286 GLY C CA    1 
ATOM   8982 C C     . GLY D 1 294 ? 32.464  18.402  -22.722 1.00 44.49 ?  286 GLY C C     1 
ATOM   8983 O O     . GLY D 1 294 ? 32.705  18.271  -21.516 1.00 52.94 ?  286 GLY C O     1 
ATOM   8984 N N     . LYS D 1 295 ? 31.321  18.908  -23.171 1.00 44.27 ?  287 LYS C N     1 
ATOM   8985 C CA    . LYS D 1 295 ? 30.241  19.309  -22.283 1.00 45.65 ?  287 LYS C CA    1 
ATOM   8986 C C     . LYS D 1 295 ? 29.194  18.203  -22.192 1.00 43.67 ?  287 LYS C C     1 
ATOM   8987 O O     . LYS D 1 295 ? 29.252  17.193  -22.898 1.00 45.12 ?  287 LYS C O     1 
ATOM   8988 C CB    . LYS D 1 295 ? 29.611  20.619  -22.759 1.00 46.17 ?  287 LYS C CB    1 
ATOM   8989 C CG    . LYS D 1 295 ? 30.585  21.532  -23.484 1.00 50.64 ?  287 LYS C CG    1 
ATOM   8990 C CD    . LYS D 1 295 ? 31.560  22.187  -22.512 1.00 51.01 ?  287 LYS C CD    1 
ATOM   8991 C CE    . LYS D 1 295 ? 32.999  21.783  -22.810 1.00 57.25 ?  287 LYS C CE    1 
ATOM   8992 N NZ    . LYS D 1 295 ? 33.984  22.360  -21.848 1.00 54.20 ?  287 LYS C NZ    1 
ATOM   8993 N N     . THR D 1 296 ? 28.221  18.404  -21.305 1.00 41.43 ?  288 THR C N     1 
ATOM   8994 C CA    . THR D 1 296 ? 27.231  17.380  -20.999 1.00 40.65 ?  288 THR C CA    1 
ATOM   8995 C C     . THR D 1 296 ? 25.831  17.956  -21.151 1.00 38.28 ?  288 THR C C     1 
ATOM   8996 O O     . THR D 1 296 ? 25.516  18.999  -20.571 1.00 40.35 ?  288 THR C O     1 
ATOM   8997 C CB    . THR D 1 296 ? 27.435  16.828  -19.585 1.00 36.87 ?  288 THR C CB    1 
ATOM   8998 O OG1   . THR D 1 296 ? 28.724  16.208  -19.496 1.00 35.84 ?  288 THR C OG1   1 
ATOM   8999 C CG2   . THR D 1 296 ? 26.368  15.798  -19.252 1.00 37.38 ?  288 THR C CG2   1 
ATOM   9000 N N     . VAL D 1 297 ? 24.996  17.265  -21.925 1.00 38.03 ?  289 VAL C N     1 
ATOM   9001 C CA    . VAL D 1 297 ? 23.630  17.682  -22.218 1.00 35.40 ?  289 VAL C CA    1 
ATOM   9002 C C     . VAL D 1 297 ? 22.692  16.530  -21.874 1.00 37.02 ?  289 VAL C C     1 
ATOM   9003 O O     . VAL D 1 297 ? 22.922  15.392  -22.296 1.00 35.58 ?  289 VAL C O     1 
ATOM   9004 C CB    . VAL D 1 297 ? 23.479  18.100  -23.694 1.00 44.26 ?  289 VAL C CB    1 
ATOM   9005 C CG1   . VAL D 1 297 ? 22.028  18.074  -24.118 1.00 33.87 ?  289 VAL C CG1   1 
ATOM   9006 C CG2   . VAL D 1 297 ? 24.078  19.485  -23.916 1.00 34.69 ?  289 VAL C CG2   1 
ATOM   9007 N N     . VAL D 1 298 ? 21.644  16.824  -21.105 1.00 34.81 ?  290 VAL C N     1 
ATOM   9008 C CA    . VAL D 1 298 ? 20.717  15.817  -20.596 1.00 30.79 ?  290 VAL C CA    1 
ATOM   9009 C C     . VAL D 1 298 ? 19.302  16.181  -21.029 1.00 35.71 ?  290 VAL C C     1 
ATOM   9010 O O     . VAL D 1 298 ? 18.912  17.354  -20.986 1.00 33.86 ?  290 VAL C O     1 
ATOM   9011 C CB    . VAL D 1 298 ? 20.806  15.701  -19.058 1.00 32.74 ?  290 VAL C CB    1 
ATOM   9012 C CG1   . VAL D 1 298 ? 19.789  14.699  -18.525 1.00 33.53 ?  290 VAL C CG1   1 
ATOM   9013 C CG2   . VAL D 1 298 ? 22.218  15.323  -18.631 1.00 36.16 ?  290 VAL C CG2   1 
ATOM   9014 N N     . THR D 1 299 ? 18.534  15.173  -21.452 1.00 31.10 ?  291 THR C N     1 
ATOM   9015 C CA    . THR D 1 299 ? 17.130  15.347  -21.807 1.00 34.65 ?  291 THR C CA    1 
ATOM   9016 C C     . THR D 1 299 ? 16.349  14.118  -21.350 1.00 34.23 ?  291 THR C C     1 
ATOM   9017 O O     . THR D 1 299 ? 16.915  13.158  -20.819 1.00 32.70 ?  291 THR C O     1 
ATOM   9018 C CB    . THR D 1 299 ? 16.958  15.599  -23.311 1.00 29.24 ?  291 THR C CB    1 
ATOM   9019 O OG1   . THR D 1 299 ? 15.641  16.108  -23.563 1.00 35.32 ?  291 THR C OG1   1 
ATOM   9020 C CG2   . THR D 1 299 ? 17.161  14.317  -24.103 1.00 31.33 ?  291 THR C CG2   1 
ATOM   9021 N N     . VAL D 1 300 ? 15.033  14.151  -21.562 1.00 31.79 ?  292 VAL C N     1 
ATOM   9022 C CA    . VAL D 1 300 ? 14.112  13.143  -21.045 1.00 29.93 ?  292 VAL C CA    1 
ATOM   9023 C C     . VAL D 1 300 ? 13.292  12.582  -22.201 1.00 31.60 ?  292 VAL C C     1 
ATOM   9024 O O     . VAL D 1 300 ? 12.784  13.342  -23.032 1.00 30.28 ?  292 VAL C O     1 
ATOM   9025 C CB    . VAL D 1 300 ? 13.187  13.733  -19.961 1.00 33.23 ?  292 VAL C CB    1 
ATOM   9026 C CG1   . VAL D 1 300 ? 11.927  12.896  -19.802 1.00 33.23 ?  292 VAL C CG1   1 
ATOM   9027 C CG2   . VAL D 1 300 ? 13.928  13.852  -18.638 1.00 31.31 ?  292 VAL C CG2   1 
ATOM   9028 N N     . LEU D 1 301 ? 13.163  11.251  -22.252 1.00 29.72 ?  293 LEU C N     1 
ATOM   9029 C CA    . LEU D 1 301 ? 12.318  10.593  -23.240 1.00 28.39 ?  293 LEU C CA    1 
ATOM   9030 C C     . LEU D 1 301 ? 11.024  10.167  -22.562 1.00 30.12 ?  293 LEU C C     1 
ATOM   9031 O O     . LEU D 1 301 ? 11.013  9.163   -21.834 1.00 32.93 ?  293 LEU C O     1 
ATOM   9032 C CB    . LEU D 1 301 ? 13.031  9.385   -23.852 1.00 25.43 ?  293 LEU C CB    1 
ATOM   9033 C CG    . LEU D 1 301 ? 14.448  9.625   -24.367 1.00 30.80 ?  293 LEU C CG    1 
ATOM   9034 C CD1   . LEU D 1 301 ? 14.905  8.445   -25.200 1.00 29.38 ?  293 LEU C CD1   1 
ATOM   9035 C CD2   . LEU D 1 301 ? 14.512  10.907  -25.179 1.00 23.55 ?  293 LEU C CD2   1 
ATOM   9036 N N     . PRO D 1 302 ? 9.916   10.885  -22.756 1.00 28.36 ?  294 PRO C N     1 
ATOM   9037 C CA    . PRO D 1 302 ? 8.744   10.646  -21.901 1.00 27.63 ?  294 PRO C CA    1 
ATOM   9038 C C     . PRO D 1 302 ? 8.018   9.336   -22.168 1.00 27.90 ?  294 PRO C C     1 
ATOM   9039 O O     . PRO D 1 302 ? 7.374   8.818   -21.248 1.00 27.75 ?  294 PRO C O     1 
ATOM   9040 C CB    . PRO D 1 302 ? 7.848   11.858  -22.194 1.00 29.54 ?  294 PRO C CB    1 
ATOM   9041 C CG    . PRO D 1 302 ? 8.785   12.905  -22.723 1.00 29.55 ?  294 PRO C CG    1 
ATOM   9042 C CD    . PRO D 1 302 ? 9.783   12.133  -23.526 1.00 29.06 ?  294 PRO C CD    1 
ATOM   9043 N N     . SER D 1 303 ? 8.089   8.775   -23.375 1.00 27.14 ?  295 SER C N     1 
ATOM   9044 C CA    . SER D 1 303 ? 7.286   7.596   -23.676 1.00 28.26 ?  295 SER C CA    1 
ATOM   9045 C C     . SER D 1 303 ? 7.966   6.744   -24.740 1.00 29.73 ?  295 SER C C     1 
ATOM   9046 O O     . SER D 1 303 ? 8.901   7.176   -25.420 1.00 32.67 ?  295 SER C O     1 
ATOM   9047 C CB    . SER D 1 303 ? 5.876   7.986   -24.124 1.00 29.60 ?  295 SER C CB    1 
ATOM   9048 O OG    . SER D 1 303 ? 5.920   8.762   -25.308 1.00 30.47 ?  295 SER C OG    1 
ATOM   9049 N N     . ASN D 1 304 ? 7.464   5.519   -24.882 1.00 26.97 ?  296 ASN C N     1 
ATOM   9050 C CA    . ASN D 1 304 ? 8.013   4.529   -25.796 1.00 30.70 ?  296 ASN C CA    1 
ATOM   9051 C C     . ASN D 1 304 ? 7.308   4.591   -27.146 1.00 32.06 ?  296 ASN C C     1 
ATOM   9052 O O     . ASN D 1 304 ? 6.111   4.876   -27.232 1.00 27.41 ?  296 ASN C O     1 
ATOM   9053 C CB    . ASN D 1 304 ? 7.874   3.126   -25.201 1.00 26.51 ?  296 ASN C CB    1 
ATOM   9054 C CG    . ASN D 1 304 ? 8.700   2.095   -25.939 1.00 33.78 ?  296 ASN C CG    1 
ATOM   9055 O OD1   . ASN D 1 304 ? 8.347   1.671   -27.039 1.00 26.63 ?  296 ASN C OD1   1 
ATOM   9056 N ND2   . ASN D 1 304 ? 9.807   1.680   -25.333 1.00 38.54 ?  296 ASN C ND2   1 
ATOM   9057 N N     . GLY D 1 305 ? 8.067   4.305   -28.206 1.00 30.18 ?  297 GLY C N     1 
ATOM   9058 C CA    . GLY D 1 305 ? 7.522   4.361   -29.552 1.00 32.05 ?  297 GLY C CA    1 
ATOM   9059 C C     . GLY D 1 305 ? 6.458   3.320   -29.834 1.00 36.35 ?  297 GLY C C     1 
ATOM   9060 O O     . GLY D 1 305 ? 5.679   3.482   -30.779 1.00 32.10 ?  297 GLY C O     1 
ATOM   9061 N N     . GLU D 1 306 ? 6.406   2.251   -29.035 1.00 29.32 ?  298 GLU C N     1 
ATOM   9062 C CA    . GLU D 1 306 ? 5.401   1.215   -29.245 1.00 34.34 ?  298 GLU C CA    1 
ATOM   9063 C C     . GLU D 1 306 ? 3.992   1.738   -28.993 1.00 35.48 ?  298 GLU C C     1 
ATOM   9064 O O     . GLU D 1 306 ? 3.025   1.213   -29.556 1.00 37.02 ?  298 GLU C O     1 
ATOM   9065 C CB    . GLU D 1 306 ? 5.697   0.014   -28.345 1.00 31.26 ?  298 GLU C CB    1 
ATOM   9066 C CG    . GLU D 1 306 ? 4.904   -1.241  -28.681 1.00 32.26 ?  298 GLU C CG    1 
ATOM   9067 C CD    . GLU D 1 306 ? 5.346   -2.446  -27.870 1.00 32.89 ?  298 GLU C CD    1 
ATOM   9068 O OE1   . GLU D 1 306 ? 6.442   -2.393  -27.273 1.00 32.45 ?  298 GLU C OE1   1 
ATOM   9069 O OE2   . GLU D 1 306 ? 4.603   -3.450  -27.829 1.00 32.38 ?  298 GLU C OE2   1 
ATOM   9070 N N     . ARG D 1 307 ? 3.856   2.773   -28.162 1.00 30.17 ?  299 ARG C N     1 
ATOM   9071 C CA    . ARG D 1 307 ? 2.552   3.363   -27.886 1.00 35.15 ?  299 ARG C CA    1 
ATOM   9072 C C     . ARG D 1 307 ? 2.007   4.162   -29.066 1.00 37.95 ?  299 ARG C C     1 
ATOM   9073 O O     . ARG D 1 307 ? 0.837   4.558   -29.041 1.00 44.02 ?  299 ARG C O     1 
ATOM   9074 C CB    . ARG D 1 307 ? 2.652   4.251   -26.640 1.00 33.11 ?  299 ARG C CB    1 
ATOM   9075 C CG    . ARG D 1 307 ? 1.319   4.700   -26.060 1.00 31.41 ?  299 ARG C CG    1 
ATOM   9076 C CD    . ARG D 1 307 ? 1.446   5.128   -24.606 1.00 31.39 ?  299 ARG C CD    1 
ATOM   9077 N NE    . ARG D 1 307 ? 1.637   3.998   -23.705 1.00 26.18 ?  299 ARG C NE    1 
ATOM   9078 C CZ    . ARG D 1 307 ? 1.904   4.110   -22.411 1.00 30.61 ?  299 ARG C CZ    1 
ATOM   9079 N NH1   . ARG D 1 307 ? 2.030   5.293   -21.831 1.00 24.74 ?  299 ARG C NH1   1 
ATOM   9080 N NH2   . ARG D 1 307 ? 2.041   3.008   -21.679 1.00 25.38 ?  299 ARG C NH2   1 
ATOM   9081 N N     . TYR D 1 308 ? 2.810   4.388   -30.101 1.00 35.37 ?  300 TYR C N     1 
ATOM   9082 C CA    . TYR D 1 308 ? 2.440   5.251   -31.214 1.00 39.65 ?  300 TYR C CA    1 
ATOM   9083 C C     . TYR D 1 308 ? 2.574   4.510   -32.535 1.00 41.83 ?  300 TYR C C     1 
ATOM   9084 O O     . TYR D 1 308 ? 2.988   5.079   -33.550 1.00 50.66 ?  300 TYR C O     1 
ATOM   9085 C CB    . TYR D 1 308 ? 3.288   6.523   -31.228 1.00 42.29 ?  300 TYR C CB    1 
ATOM   9086 C CG    . TYR D 1 308 ? 3.377   7.243   -29.897 1.00 44.14 ?  300 TYR C CG    1 
ATOM   9087 C CD1   . TYR D 1 308 ? 4.183   6.762   -28.869 1.00 39.01 ?  300 TYR C CD1   1 
ATOM   9088 C CD2   . TYR D 1 308 ? 2.650   8.403   -29.667 1.00 45.72 ?  300 TYR C CD2   1 
ATOM   9089 C CE1   . TYR D 1 308 ? 4.261   7.418   -27.653 1.00 40.87 ?  300 TYR C CE1   1 
ATOM   9090 C CE2   . TYR D 1 308 ? 2.723   9.066   -28.454 1.00 45.79 ?  300 TYR C CE2   1 
ATOM   9091 C CZ    . TYR D 1 308 ? 3.529   8.569   -27.452 1.00 41.29 ?  300 TYR C CZ    1 
ATOM   9092 O OH    . TYR D 1 308 ? 3.603   9.225   -26.245 1.00 39.69 ?  300 TYR C OH    1 
ATOM   9093 N N     . LEU D 1 309 ? 2.222   3.224   -32.547 1.00 47.89 ?  301 LEU C N     1 
ATOM   9094 C CA    . LEU D 1 309 ? 2.410   2.416   -33.745 1.00 49.11 ?  301 LEU C CA    1 
ATOM   9095 C C     . LEU D 1 309 ? 1.349   2.673   -34.806 1.00 50.07 ?  301 LEU C C     1 
ATOM   9096 O O     . LEU D 1 309 ? 1.588   2.378   -35.982 1.00 49.93 ?  301 LEU C O     1 
ATOM   9097 C CB    . LEU D 1 309 ? 2.436   0.932   -33.377 1.00 43.58 ?  301 LEU C CB    1 
ATOM   9098 C CG    . LEU D 1 309 ? 3.736   0.476   -32.709 1.00 39.89 ?  301 LEU C CG    1 
ATOM   9099 C CD1   . LEU D 1 309 ? 3.739   -1.030  -32.495 1.00 37.64 ?  301 LEU C CD1   1 
ATOM   9100 C CD2   . LEU D 1 309 ? 4.946   0.911   -33.527 1.00 32.56 ?  301 LEU C CD2   1 
ATOM   9101 N N     . SER D 1 310 ? 0.192   3.213   -34.427 1.00 52.98 ?  302 SER C N     1 
ATOM   9102 C CA    . SER D 1 310 ? -0.857  3.576   -35.380 1.00 55.63 ?  302 SER C CA    1 
ATOM   9103 C C     . SER D 1 310 ? -0.926  5.084   -35.589 1.00 53.28 ?  302 SER C C     1 
ATOM   9104 O O     . SER D 1 310 ? -2.008  5.661   -35.737 1.00 52.39 ?  302 SER C O     1 
ATOM   9105 C CB    . SER D 1 310 ? -2.207  3.027   -34.926 1.00 54.75 ?  302 SER C CB    1 
ATOM   9106 O OG    . SER D 1 310 ? -2.800  3.861   -33.948 1.00 62.06 ?  302 SER C OG    1 
ATOM   9107 N N     . THR D 1 311 ? 0.233   5.736   -35.583 1.00 53.81 ?  303 THR C N     1 
ATOM   9108 C CA    . THR D 1 311 ? 0.411   7.135   -35.942 1.00 53.76 ?  303 THR C CA    1 
ATOM   9109 C C     . THR D 1 311 ? 1.411   7.165   -37.095 1.00 52.86 ?  303 THR C C     1 
ATOM   9110 O O     . THR D 1 311 ? 2.103   6.163   -37.323 1.00 47.02 ?  303 THR C O     1 
ATOM   9111 C CB    . THR D 1 311 ? 0.902   7.948   -34.737 1.00 48.07 ?  303 THR C CB    1 
ATOM   9112 O OG1   . THR D 1 311 ? 2.272   7.629   -34.458 1.00 51.22 ?  303 THR C OG1   1 
ATOM   9113 C CG2   . THR D 1 311 ? 0.050   7.654   -33.505 1.00 47.19 ?  303 THR C CG2   1 
ATOM   9114 N N     . PRO D 1 312 ? 1.525   8.263   -37.853 1.00 55.16 ?  304 PRO C N     1 
ATOM   9115 C CA    . PRO D 1 312 ? 2.508   8.290   -38.949 1.00 56.73 ?  304 PRO C CA    1 
ATOM   9116 C C     . PRO D 1 312 ? 3.957   8.288   -38.484 1.00 54.79 ?  304 PRO C C     1 
ATOM   9117 O O     . PRO D 1 312 ? 4.860   8.329   -39.329 1.00 57.16 ?  304 PRO C O     1 
ATOM   9118 C CB    . PRO D 1 312 ? 2.176   9.589   -39.710 1.00 50.88 ?  304 PRO C CB    1 
ATOM   9119 C CG    . PRO D 1 312 ? 1.114   10.276  -38.943 1.00 53.70 ?  304 PRO C CG    1 
ATOM   9120 C CD    . PRO D 1 312 ? 0.891   9.573   -37.655 1.00 59.12 ?  304 PRO C CD    1 
ATOM   9121 N N     . LEU D 1 313 ? 4.206   8.235   -37.175 1.00 52.43 ?  305 LEU C N     1 
ATOM   9122 C CA    . LEU D 1 313 ? 5.576   8.177   -36.675 1.00 53.40 ?  305 LEU C CA    1 
ATOM   9123 C C     . LEU D 1 313 ? 6.270   6.890   -37.107 1.00 48.40 ?  305 LEU C C     1 
ATOM   9124 O O     . LEU D 1 313 ? 7.466   6.896   -37.422 1.00 48.57 ?  305 LEU C O     1 
ATOM   9125 C CB    . LEU D 1 313 ? 5.576   8.309   -35.149 1.00 54.29 ?  305 LEU C CB    1 
ATOM   9126 C CG    . LEU D 1 313 ? 6.907   8.166   -34.410 1.00 49.59 ?  305 LEU C CG    1 
ATOM   9127 C CD1   . LEU D 1 313 ? 7.879   9.254   -34.832 1.00 42.51 ?  305 LEU C CD1   1 
ATOM   9128 C CD2   . LEU D 1 313 ? 6.699   8.191   -32.900 1.00 44.68 ?  305 LEU C CD2   1 
ATOM   9129 N N     . TYR D 1 314 ? 5.535   5.782   -37.146 1.00 46.10 ?  306 TYR C N     1 
ATOM   9130 C CA    . TYR D 1 314 ? 6.112   4.475   -37.440 1.00 49.57 ?  306 TYR C CA    1 
ATOM   9131 C C     . TYR D 1 314 ? 5.216   3.707   -38.407 1.00 55.25 ?  306 TYR C C     1 
ATOM   9132 O O     . TYR D 1 314 ? 4.893   2.537   -38.198 1.00 55.40 ?  306 TYR C O     1 
ATOM   9133 C CB    . TYR D 1 314 ? 6.330   3.680   -36.154 1.00 50.89 ?  306 TYR C CB    1 
ATOM   9134 C CG    . TYR D 1 314 ? 7.396   4.252   -35.249 1.00 42.29 ?  306 TYR C CG    1 
ATOM   9135 C CD1   . TYR D 1 314 ? 8.644   4.603   -35.746 1.00 44.76 ?  306 TYR C CD1   1 
ATOM   9136 C CD2   . TYR D 1 314 ? 7.152   4.445   -33.896 1.00 40.88 ?  306 TYR C CD2   1 
ATOM   9137 C CE1   . TYR D 1 314 ? 9.622   5.128   -34.921 1.00 42.94 ?  306 TYR C CE1   1 
ATOM   9138 C CE2   . TYR D 1 314 ? 8.123   4.969   -33.063 1.00 44.29 ?  306 TYR C CE2   1 
ATOM   9139 C CZ    . TYR D 1 314 ? 9.356   5.310   -33.580 1.00 41.66 ?  306 TYR C CZ    1 
ATOM   9140 O OH    . TYR D 1 314 ? 10.325  5.831   -32.753 1.00 37.93 ?  306 TYR C OH    1 
ATOM   9141 N N     . SER D 1 315 ? 4.802   4.362   -39.487 1.00 60.20 ?  307 SER C N     1 
ATOM   9142 C CA    . SER D 1 315 ? 3.984   3.701   -40.500 1.00 63.77 ?  307 SER C CA    1 
ATOM   9143 C C     . SER D 1 315 ? 4.840   3.191   -41.657 1.00 63.91 ?  307 SER C C     1 
ATOM   9144 O O     . SER D 1 315 ? 5.394   3.974   -42.428 1.00 70.27 ?  307 SER C O     1 
ATOM   9145 C CB    . SER D 1 315 ? 2.902   4.645   -41.025 1.00 60.25 ?  307 SER C CB    1 
ATOM   9146 O OG    . SER D 1 315 ? 1.765   4.633   -40.179 1.00 62.97 ?  307 SER C OG    1 
ATOM   9147 N N     . TYR E 2 1   ? 22.343  33.973  41.092  1.00 45.83 ?  1   TYR E N     1 
ATOM   9148 C CA    . TYR E 2 1   ? 21.363  33.011  40.606  1.00 50.78 ?  1   TYR E CA    1 
ATOM   9149 C C     . TYR E 2 1   ? 22.034  31.819  39.930  1.00 49.26 ?  1   TYR E C     1 
ATOM   9150 O O     . TYR E 2 1   ? 23.071  31.965  39.283  1.00 50.89 ?  1   TYR E O     1 
ATOM   9151 C CB    . TYR E 2 1   ? 20.394  33.684  39.631  1.00 41.57 ?  1   TYR E CB    1 
ATOM   9152 N N     . MET E 2 2   ? 21.430  30.642  40.080  0.96 43.16 ?  2   MET E N     1 
ATOM   9153 C CA    . MET E 2 2   ? 21.954  29.417  39.480  0.96 41.57 ?  2   MET E CA    1 
ATOM   9154 C C     . MET E 2 2   ? 22.001  29.504  37.956  0.96 36.75 ?  2   MET E C     1 
ATOM   9155 O O     . MET E 2 2   ? 21.073  30.009  37.321  0.96 35.11 ?  2   MET E O     1 
ATOM   9156 C CB    . MET E 2 2   ? 21.112  28.212  39.908  0.96 35.58 ?  2   MET E CB    1 
ATOM   9157 C CG    . MET E 2 2   ? 21.771  26.870  39.638  0.96 38.81 ?  2   MET E CG    1 
ATOM   9158 S SD    . MET E 2 2   ? 23.289  26.612  40.579  0.96 41.29 ?  2   MET E SD    1 
ATOM   9159 C CE    . MET E 2 2   ? 23.617  24.887  40.222  0.96 40.18 ?  2   MET E CE    1 
HETATM 9160 C C1    . NAL E 2 3   ? 26.598  28.527  35.674  0.80 33.56 ?  3   NAL E C1    1 
HETATM 9161 C C2    . NAL E 2 3   ? 25.567  29.447  35.803  0.80 35.75 ?  3   NAL E C2    1 
HETATM 9162 C C3    . NAL E 2 3   ? 25.758  30.605  36.555  0.80 33.61 ?  3   NAL E C3    1 
HETATM 9163 C C4    . NAL E 2 3   ? 26.979  30.834  37.175  0.80 35.09 ?  3   NAL E C4    1 
HETATM 9164 C C4A   . NAL E 2 3   ? 28.023  29.899  37.043  0.80 32.47 ?  3   NAL E C4A   1 
HETATM 9165 C C5    . NAL E 2 3   ? 29.266  30.124  37.667  0.80 34.21 ?  3   NAL E C5    1 
HETATM 9166 C C6    . NAL E 2 3   ? 30.290  29.196  37.531  0.80 35.98 ?  3   NAL E C6    1 
HETATM 9167 C C7    . NAL E 2 3   ? 30.095  28.042  36.779  0.80 34.62 ?  3   NAL E C7    1 
HETATM 9168 C C8    . NAL E 2 3   ? 28.870  27.819  36.163  0.80 34.11 ?  3   NAL E C8    1 
HETATM 9169 C C8A   . NAL E 2 3   ? 27.833  28.758  36.301  0.80 33.87 ?  3   NAL E C8A   1 
HETATM 9170 C C9    . NAL E 2 3   ? 24.229  29.173  35.115  0.80 28.92 ?  3   NAL E C9    1 
HETATM 9171 C CA    . NAL E 2 3   ? 23.278  28.383  36.011  0.80 31.52 ?  3   NAL E CA    1 
HETATM 9172 C C     . NAL E 2 3   ? 23.746  26.938  36.193  0.80 36.24 ?  3   NAL E C     1 
HETATM 9173 N N     . NAL E 2 3   ? 23.184  29.017  37.316  0.80 33.29 ?  3   NAL E N     1 
HETATM 9174 O O     . NAL E 2 3   ? 24.459  26.658  37.194  0.80 36.64 ?  3   NAL E O     1 
ATOM   9175 N N     . TYR E 2 4   ? 23.845  26.161  34.996  0.90 33.51 ?  4   TYR E N     1 
ATOM   9176 C CA    . TYR E 2 4   ? 24.177  24.780  34.647  0.90 32.91 ?  4   TYR E CA    1 
ATOM   9177 C C     . TYR E 2 4   ? 25.051  24.744  33.399  0.90 36.26 ?  4   TYR E C     1 
ATOM   9178 O O     . TYR E 2 4   ? 24.585  24.459  32.296  0.90 34.27 ?  4   TYR E O     1 
ATOM   9179 C CB    . TYR E 2 4   ? 22.900  23.962  34.456  0.90 33.15 ?  4   TYR E CB    1 
ATOM   9180 C CG    . TYR E 2 4   ? 22.048  23.910  35.706  0.90 37.75 ?  4   TYR E CG    1 
ATOM   9181 C CD1   . TYR E 2 4   ? 22.279  22.957  36.694  0.90 36.56 ?  4   TYR E CD1   1 
ATOM   9182 C CD2   . TYR E 2 4   ? 21.039  24.839  35.921  0.90 32.81 ?  4   TYR E CD2   1 
ATOM   9183 C CE1   . TYR E 2 4   ? 21.508  22.916  37.846  0.90 36.50 ?  4   TYR E CE1   1 
ATOM   9184 C CE2   . TYR E 2 4   ? 20.266  24.807  37.069  0.90 34.54 ?  4   TYR E CE2   1 
ATOM   9185 C CZ    . TYR E 2 4   ? 20.504  23.846  38.026  0.90 37.11 ?  4   TYR E CZ    1 
ATOM   9186 O OH    . TYR E 2 4   ? 19.735  23.814  39.167  0.90 45.00 ?  4   TYR E OH    1 
ATOM   9187 N N     . ILE E 2 5   ? 26.330  25.050  33.594  1.00 34.48 ?  5   ILE E N     1 
ATOM   9188 C CA    . ILE E 2 5   ? 27.273  25.173  32.494  1.00 33.88 ?  5   ILE E CA    1 
ATOM   9189 C C     . ILE E 2 5   ? 28.539  24.387  32.810  1.00 36.26 ?  5   ILE E C     1 
ATOM   9190 O O     . ILE E 2 5   ? 29.154  24.570  33.862  1.00 34.86 ?  5   ILE E O     1 
ATOM   9191 C CB    . ILE E 2 5   ? 27.596  26.651  32.211  1.00 35.56 ?  5   ILE E CB    1 
ATOM   9192 C CG1   . ILE E 2 5   ? 26.321  27.424  31.855  1.00 31.03 ?  5   ILE E CG1   1 
ATOM   9193 C CG2   . ILE E 2 5   ? 28.625  26.769  31.104  1.00 32.52 ?  5   ILE E CG2   1 
ATOM   9194 C CD1   . ILE E 2 5   ? 26.501  28.927  31.820  1.00 26.40 ?  5   ILE E CD1   1 
ATOM   9195 O OXT   . ILE E 2 5   ? 28.973  23.551  32.018  1.00 30.33 ?  5   ILE E OXT   1 
ATOM   9196 N N     . TYR F 2 1   ? 12.099  -15.327 31.224  0.88 36.78 ?  1   TYR F N     1 
ATOM   9197 C CA    . TYR F 2 1   ? 12.951  -14.368 31.915  0.88 40.58 ?  1   TYR F CA    1 
ATOM   9198 C C     . TYR F 2 1   ? 12.933  -13.013 31.216  0.88 41.40 ?  1   TYR F C     1 
ATOM   9199 O O     . TYR F 2 1   ? 12.568  -12.912 30.045  0.88 41.58 ?  1   TYR F O     1 
ATOM   9200 C CB    . TYR F 2 1   ? 14.382  -14.899 32.011  0.88 38.88 ?  1   TYR F CB    1 
ATOM   9201 C CG    . TYR F 2 1   ? 14.479  -16.228 32.721  0.88 43.86 ?  1   TYR F CG    1 
ATOM   9202 C CD1   . TYR F 2 1   ? 14.510  -16.294 34.108  0.88 38.46 ?  1   TYR F CD1   1 
ATOM   9203 C CD2   . TYR F 2 1   ? 14.524  -17.418 32.008  0.88 43.26 ?  1   TYR F CD2   1 
ATOM   9204 C CE1   . TYR F 2 1   ? 14.590  -17.507 34.763  0.88 39.64 ?  1   TYR F CE1   1 
ATOM   9205 C CE2   . TYR F 2 1   ? 14.605  -18.636 32.655  0.88 40.62 ?  1   TYR F CE2   1 
ATOM   9206 C CZ    . TYR F 2 1   ? 14.639  -18.675 34.033  0.88 39.62 ?  1   TYR F CZ    1 
ATOM   9207 O OH    . TYR F 2 1   ? 14.720  -19.885 34.682  0.88 43.35 ?  1   TYR F OH    1 
ATOM   9208 N N     . MET F 2 2   ? 13.328  -11.975 31.945  1.00 39.40 ?  2   MET F N     1 
ATOM   9209 C CA    . MET F 2 2   ? 13.328  -10.616 31.417  1.00 41.01 ?  2   MET F CA    1 
ATOM   9210 C C     . MET F 2 2   ? 14.470  -10.408 30.426  1.00 41.38 ?  2   MET F C     1 
ATOM   9211 O O     . MET F 2 2   ? 15.429  -11.181 30.400  1.00 33.86 ?  2   MET F O     1 
ATOM   9212 C CB    . MET F 2 2   ? 13.427  -9.605  32.561  1.00 38.72 ?  2   MET F CB    1 
ATOM   9213 C CG    . MET F 2 2   ? 12.947  -8.208  32.212  1.00 38.37 ?  2   MET F CG    1 
ATOM   9214 S SD    . MET F 2 2   ? 11.644  -8.200  30.968  1.00 38.80 ?  2   MET F SD    1 
ATOM   9215 C CE    . MET F 2 2   ? 11.826  -6.542  30.317  1.00 36.46 ?  2   MET F CE    1 
HETATM 9216 C C1    . NAL F 2 3   ? 14.387  -9.308  25.347  0.95 30.32 ?  3   NAL F C1    1 
HETATM 9217 C C2    . NAL F 2 3   ? 14.672  -10.422 26.125  0.95 33.48 ?  3   NAL F C2    1 
HETATM 9218 C C3    . NAL F 2 3   ? 13.882  -11.565 26.020  0.95 33.03 ?  3   NAL F C3    1 
HETATM 9219 C C4    . NAL F 2 3   ? 12.805  -11.590 25.145  0.95 31.34 ?  3   NAL F C4    1 
HETATM 9220 C C4A   . NAL F 2 3   ? 12.517  -10.458 24.361  0.95 33.83 ?  3   NAL F C4A   1 
HETATM 9221 C C5    . NAL F 2 3   ? 11.425  -10.476 23.474  0.95 39.56 ?  3   NAL F C5    1 
HETATM 9222 C C6    . NAL F 2 3   ? 11.140  -9.357  22.702  0.95 36.34 ?  3   NAL F C6    1 
HETATM 9223 C C7    . NAL F 2 3   ? 11.930  -8.217  22.803  0.95 36.58 ?  3   NAL F C7    1 
HETATM 9224 C C8    . NAL F 2 3   ? 13.007  -8.196  23.679  0.95 33.71 ?  3   NAL F C8    1 
HETATM 9225 C C8A   . NAL F 2 3   ? 13.296  -9.330  24.461  0.95 35.39 ?  3   NAL F C8A   1 
HETATM 9226 C C9    . NAL F 2 3   ? 15.863  -10.389 27.085  0.95 35.36 ?  3   NAL F C9    1 
HETATM 9227 C CA    . NAL F 2 3   ? 15.580  -9.649  28.396  0.95 36.47 ?  3   NAL F CA    1 
HETATM 9228 C C     . NAL F 2 3   ? 15.477  -8.134  28.205  0.95 36.52 ?  3   NAL F C     1 
HETATM 9229 N N     . NAL F 2 3   ? 14.369  -10.154 29.022  0.95 38.76 ?  3   NAL F N     1 
HETATM 9230 O O     . NAL F 2 3   ? 14.359  -7.593  27.997  0.95 34.73 -1 3   NAL F O     1 
ATOM   9231 N N     . TYR F 2 4   ? 16.463  -7.220  27.720  1.00 32.09 ?  4   TYR F N     1 
ATOM   9232 C CA    . TYR F 2 4   ? 16.292  -5.814  27.381  1.00 30.18 ?  4   TYR F CA    1 
ATOM   9233 C C     . TYR F 2 4   ? 16.892  -5.528  26.012  1.00 39.21 ?  4   TYR F C     1 
ATOM   9234 O O     . TYR F 2 4   ? 18.030  -5.070  25.903  1.00 37.93 ?  4   TYR F O     1 
ATOM   9235 C CB    . TYR F 2 4   ? 16.931  -4.925  28.449  1.00 32.94 ?  4   TYR F CB    1 
ATOM   9236 C CG    . TYR F 2 4   ? 16.281  -5.068  29.806  1.00 36.58 ?  4   TYR F CG    1 
ATOM   9237 C CD1   . TYR F 2 4   ? 15.197  -4.278  30.164  1.00 36.57 ?  4   TYR F CD1   1 
ATOM   9238 C CD2   . TYR F 2 4   ? 16.743  -6.002  30.725  1.00 41.85 ?  4   TYR F CD2   1 
ATOM   9239 C CE1   . TYR F 2 4   ? 14.594  -4.408  31.400  1.00 37.43 ?  4   TYR F CE1   1 
ATOM   9240 C CE2   . TYR F 2 4   ? 16.145  -6.140  31.965  1.00 38.63 ?  4   TYR F CE2   1 
ATOM   9241 C CZ    . TYR F 2 4   ? 15.071  -5.339  32.296  1.00 40.54 ?  4   TYR F CZ    1 
ATOM   9242 O OH    . TYR F 2 4   ? 14.470  -5.468  33.527  1.00 52.17 ?  4   TYR F OH    1 
ATOM   9243 N N     . ILE F 2 5   ? 16.120  -5.813  24.968  1.00 30.27 ?  5   ILE F N     1 
ATOM   9244 C CA    . ILE F 2 5   ? 16.585  -5.637  23.600  1.00 35.37 ?  5   ILE F CA    1 
ATOM   9245 C C     . ILE F 2 5   ? 15.599  -4.790  22.808  1.00 38.37 ?  5   ILE F C     1 
ATOM   9246 O O     . ILE F 2 5   ? 15.992  -3.832  22.144  1.00 35.33 ?  5   ILE F O     1 
ATOM   9247 C CB    . ILE F 2 5   ? 16.810  -6.995  22.918  1.00 33.96 ?  5   ILE F CB    1 
ATOM   9248 C CG1   . ILE F 2 5   ? 17.823  -7.824  23.712  1.00 34.56 ?  5   ILE F CG1   1 
ATOM   9249 C CG2   . ILE F 2 5   ? 17.272  -6.796  21.483  1.00 30.53 ?  5   ILE F CG2   1 
ATOM   9250 C CD1   . ILE F 2 5   ? 17.824  -9.290  23.360  1.00 30.58 ?  5   ILE F CD1   1 
ATOM   9251 O OXT   . ILE F 2 5   ? 14.392  -5.040  22.821  1.00 32.78 ?  5   ILE F OXT   1 
ATOM   9252 N N     . TYR G 2 1   ? 0.759   -25.866 -36.971 1.00 51.51 ?  1   TYR G N     1 
ATOM   9253 C CA    . TYR G 2 1   ? -0.100  -24.765 -36.547 1.00 53.12 ?  1   TYR G CA    1 
ATOM   9254 C C     . TYR G 2 1   ? 0.716   -23.691 -35.834 1.00 48.15 ?  1   TYR G C     1 
ATOM   9255 O O     . TYR G 2 1   ? 1.769   -23.977 -35.264 1.00 49.40 ?  1   TYR G O     1 
ATOM   9256 C CB    . TYR G 2 1   ? -1.217  -25.278 -35.635 1.00 51.78 ?  1   TYR G CB    1 
ATOM   9257 N N     . MET G 2 2   ? 0.221   -22.458 -35.875 1.00 44.88 ?  2   MET G N     1 
ATOM   9258 C CA    . MET G 2 2   ? 0.900   -21.323 -35.255 1.00 46.06 ?  2   MET G CA    1 
ATOM   9259 C C     . MET G 2 2   ? 1.071   -21.509 -33.750 1.00 43.60 ?  2   MET G C     1 
ATOM   9260 O O     . MET G 2 2   ? 0.268   -22.187 -33.105 1.00 48.37 ?  2   MET G O     1 
ATOM   9261 C CB    . MET G 2 2   ? 0.132   -20.027 -35.538 1.00 42.70 ?  2   MET G CB    1 
ATOM   9262 C CG    . MET G 2 2   ? 0.070   -19.651 -37.004 1.00 46.20 ?  2   MET G CG    1 
ATOM   9263 S SD    . MET G 2 2   ? 1.674   -19.152 -37.655 1.00 49.10 ?  2   MET G SD    1 
ATOM   9264 C CE    . MET G 2 2   ? 2.040   -17.739 -36.621 1.00 34.33 ?  2   MET G CE    1 
HETATM 9265 C C1    . NAL G 2 3   ? 6.151   -20.464 -32.747 0.90 36.50 ?  3   NAL G C1    1 
HETATM 9266 C C2    . NAL G 2 3   ? 5.132   -21.403 -32.644 0.90 36.59 ?  3   NAL G C2    1 
HETATM 9267 C C3    . NAL G 2 3   ? 5.225   -22.607 -33.336 0.90 35.38 ?  3   NAL G C3    1 
HETATM 9268 C C4    . NAL G 2 3   ? 6.332   -22.865 -34.132 0.90 35.03 ?  3   NAL G C4    1 
HETATM 9269 C C4A   . NAL G 2 3   ? 7.363   -21.913 -34.240 0.90 33.99 ?  3   NAL G C4A   1 
HETATM 9270 C C5    . NAL G 2 3   ? 8.488   -22.172 -35.049 0.90 35.68 ?  3   NAL G C5    1 
HETATM 9271 C C6    . NAL G 2 3   ? 9.503   -21.229 -35.153 0.90 32.83 ?  3   NAL G C6    1 
HETATM 9272 C C7    . NAL G 2 3   ? 9.409   -20.028 -34.458 0.90 34.07 ?  3   NAL G C7    1 
HETATM 9273 C C8    . NAL G 2 3   ? 8.300   -19.771 -33.661 0.90 30.70 ?  3   NAL G C8    1 
HETATM 9274 C C8A   . NAL G 2 3   ? 7.271   -20.725 -33.555 0.90 32.54 ?  3   NAL G C8A   1 
HETATM 9275 C C9    . NAL G 2 3   ? 3.915   -21.112 -31.765 0.90 34.47 ?  3   NAL G C9    1 
HETATM 9276 C CA    . NAL G 2 3   ? 2.790   -20.408 -32.525 0.90 37.83 ?  3   NAL G CA    1 
HETATM 9277 C C     . NAL G 2 3   ? 3.152   -18.964 -32.879 0.90 38.20 ?  3   NAL G C     1 
HETATM 9278 N N     . NAL G 2 3   ? 2.453   -21.138 -33.737 0.90 36.67 ?  3   NAL G N     1 
HETATM 9279 O O     . NAL G 2 3   ? 3.620   -18.688 -34.016 0.90 39.29 -1 3   NAL G O     1 
ATOM   9280 N N     . TYR G 2 4   ? 3.675   -18.057 -31.904 0.87 32.35 ?  4   TYR G N     1 
ATOM   9281 C CA    . TYR G 2 4   ? 4.046   -16.658 -31.721 0.87 33.66 ?  4   TYR G CA    1 
ATOM   9282 C C     . TYR G 2 4   ? 5.160   -16.528 -30.686 0.87 35.58 ?  4   TYR G C     1 
ATOM   9283 O O     . TYR G 2 4   ? 4.942   -16.059 -29.569 0.87 30.78 ?  4   TYR G O     1 
ATOM   9284 C CB    . TYR G 2 4   ? 2.822   -15.837 -31.318 0.87 35.31 ?  4   TYR G CB    1 
ATOM   9285 C CG    . TYR G 2 4   ? 1.782   -15.751 -32.414 0.87 35.24 ?  4   TYR G CG    1 
ATOM   9286 C CD1   . TYR G 2 4   ? 1.895   -14.816 -33.435 0.87 39.75 ?  4   TYR G CD1   1 
ATOM   9287 C CD2   . TYR G 2 4   ? 0.705   -16.628 -32.447 0.87 38.75 ?  4   TYR G CD2   1 
ATOM   9288 C CE1   . TYR G 2 4   ? 0.954   -14.741 -34.445 0.87 37.70 ?  4   TYR G CE1   1 
ATOM   9289 C CE2   . TYR G 2 4   ? -0.240  -16.562 -33.455 0.87 34.10 ?  4   TYR G CE2   1 
ATOM   9290 C CZ    . TYR G 2 4   ? -0.111  -15.617 -34.451 0.87 38.69 ?  4   TYR G CZ    1 
ATOM   9291 O OH    . TYR G 2 4   ? -1.048  -15.546 -35.457 0.87 51.18 ?  4   TYR G OH    1 
ATOM   9292 N N     . ILE G 2 5   ? 6.355   -16.959 -31.078 0.92 32.73 ?  5   ILE G N     1 
ATOM   9293 C CA    . ILE G 2 5   ? 7.531   -16.896 -30.222 0.92 32.01 ?  5   ILE G CA    1 
ATOM   9294 C C     . ILE G 2 5   ? 8.654   -16.180 -30.960 0.92 34.43 ?  5   ILE G C     1 
ATOM   9295 O O     . ILE G 2 5   ? 8.925   -16.467 -32.128 0.92 30.63 ?  5   ILE G O     1 
ATOM   9296 C CB    . ILE G 2 5   ? 7.970   -18.302 -29.779 0.92 34.34 ?  5   ILE G CB    1 
ATOM   9297 C CG1   . ILE G 2 5   ? 6.830   -19.013 -29.049 0.92 32.12 ?  5   ILE G CG1   1 
ATOM   9298 C CG2   . ILE G 2 5   ? 9.206   -18.225 -28.897 0.92 27.53 ?  5   ILE G CG2   1 
ATOM   9299 C CD1   . ILE G 2 5   ? 7.029   -20.505 -28.920 0.92 26.28 ?  5   ILE G CD1   1 
ATOM   9300 O OXT   . ILE G 2 5   ? 9.312   -15.298 -30.410 0.92 29.43 ?  5   ILE G OXT   1 
ATOM   9301 N N     . TYR H 2 1   ? -8.589  22.872  -29.845 1.00 53.62 ?  1   TYR H N     1 
ATOM   9302 C CA    . TYR H 2 1   ? -7.284  22.463  -30.350 1.00 58.10 ?  1   TYR H CA    1 
ATOM   9303 C C     . TYR H 2 1   ? -6.758  21.246  -29.594 1.00 56.57 ?  1   TYR H C     1 
ATOM   9304 O O     . TYR H 2 1   ? -6.547  21.303  -28.382 1.00 59.36 ?  1   TYR H O     1 
ATOM   9305 C CB    . TYR H 2 1   ? -6.284  23.618  -30.250 1.00 46.01 ?  1   TYR H CB    1 
ATOM   9306 N N     . MET H 2 2   ? -6.552  20.149  -30.318 0.94 50.72 ?  2   MET H N     1 
ATOM   9307 C CA    . MET H 2 2   ? -6.040  18.914  -29.731 0.94 48.39 ?  2   MET H CA    1 
ATOM   9308 C C     . MET H 2 2   ? -4.654  19.121  -29.130 0.94 48.97 ?  2   MET H C     1 
ATOM   9309 O O     . MET H 2 2   ? -3.713  19.491  -29.832 0.94 44.93 ?  2   MET H O     1 
ATOM   9310 C CB    . MET H 2 2   ? -5.991  17.799  -30.779 0.94 47.62 ?  2   MET H CB    1 
ATOM   9311 C CG    . MET H 2 2   ? -7.203  16.882  -30.775 0.94 49.88 ?  2   MET H CG    1 
ATOM   9312 S SD    . MET H 2 2   ? -7.871  16.611  -29.123 0.94 48.73 ?  2   MET H SD    1 
ATOM   9313 C CE    . MET H 2 2   ? -7.203  14.994  -28.740 0.94 42.62 ?  2   MET H CE    1 
HETATM 9314 C C1    . NAL H 2 3   ? -3.953  18.234  -24.260 0.91 39.13 ?  3   NAL H C1    1 
HETATM 9315 C C2    . NAL H 2 3   ? -3.739  19.189  -25.244 0.91 41.93 ?  3   NAL H C2    1 
HETATM 9316 C C3    . NAL H 2 3   ? -4.430  20.396  -25.211 0.91 40.78 ?  3   NAL H C3    1 
HETATM 9317 C C4    . NAL H 2 3   ? -5.339  20.647  -24.193 0.91 46.37 ?  3   NAL H C4    1 
HETATM 9318 C C4A   . NAL H 2 3   ? -5.556  19.678  -23.195 0.91 42.91 ?  3   NAL H C4A   1 
HETATM 9319 C C5    . NAL H 2 3   ? -6.477  19.930  -22.161 0.91 40.21 ?  3   NAL H C5    1 
HETATM 9320 C C6    . NAL H 2 3   ? -6.690  18.973  -21.178 0.91 44.51 ?  3   NAL H C6    1 
HETATM 9321 C C7    . NAL H 2 3   ? -5.997  17.767  -21.213 0.91 42.56 ?  3   NAL H C7    1 
HETATM 9322 C C8    . NAL H 2 3   ? -5.088  17.517  -22.233 0.91 45.53 ?  3   NAL H C8    1 
HETATM 9323 C C8A   . NAL H 2 3   ? -4.872  18.487  -23.229 0.91 42.91 ?  3   NAL H C8A   1 
HETATM 9324 C C9    . NAL H 2 3   ? -2.739  18.902  -26.363 0.91 42.17 ?  3   NAL H C9    1 
HETATM 9325 C CA    . NAL H 2 3   ? -3.378  18.090  -27.489 0.91 39.06 ?  3   NAL H CA    1 
HETATM 9326 C C     . NAL H 2 3   ? -3.502  16.611  -27.123 0.91 42.18 ?  3   NAL H C     1 
HETATM 9327 N N     . NAL H 2 3   ? -4.695  18.619  -27.792 0.91 47.10 ?  3   NAL H N     1 
HETATM 9328 O O     . NAL H 2 3   ? -4.497  16.212  -26.462 0.91 41.18 -1 3   NAL H O     1 
ATOM   9329 N N     . TYR H 2 4   ? -2.310  15.877  -26.833 0.97 36.97 ?  4   TYR H N     1 
ATOM   9330 C CA    . TYR H 2 4   ? -2.487  14.545  -26.267 0.97 36.06 ?  4   TYR H CA    1 
ATOM   9331 C C     . TYR H 2 4   ? -1.652  14.395  -24.999 0.97 44.27 ?  4   TYR H C     1 
ATOM   9332 O O     . TYR H 2 4   ? -0.536  13.877  -25.034 0.97 41.51 ?  4   TYR H O     1 
ATOM   9333 C CB    . TYR H 2 4   ? -2.119  13.467  -27.293 0.97 42.04 ?  4   TYR H CB    1 
ATOM   9334 C CG    . TYR H 2 4   ? -2.921  13.544  -28.579 0.97 43.28 ?  4   TYR H CG    1 
ATOM   9335 C CD1   . TYR H 2 4   ? -2.592  14.455  -29.576 0.97 40.80 ?  4   TYR H CD1   1 
ATOM   9336 C CD2   . TYR H 2 4   ? -4.011  12.708  -28.792 0.97 38.98 ?  4   TYR H CD2   1 
ATOM   9337 C CE1   . TYR H 2 4   ? -3.323  14.531  -30.747 0.97 45.27 ?  4   TYR H CE1   1 
ATOM   9338 C CE2   . TYR H 2 4   ? -4.748  12.777  -29.963 0.97 42.83 ?  4   TYR H CE2   1 
ATOM   9339 C CZ    . TYR H 2 4   ? -4.399  13.691  -30.936 0.97 47.87 ?  4   TYR H CZ    1 
ATOM   9340 O OH    . TYR H 2 4   ? -5.126  13.768  -32.102 0.97 50.57 ?  4   TYR H OH    1 
ATOM   9341 N N     . ILE H 2 5   ? -2.201  14.861  -23.881 1.00 43.91 ?  5   ILE H N     1 
ATOM   9342 C CA    . ILE H 2 5   ? -1.492  14.837  -22.609 1.00 39.70 ?  5   ILE H CA    1 
ATOM   9343 C C     . ILE H 2 5   ? -2.325  14.129  -21.550 1.00 43.96 ?  5   ILE H C     1 
ATOM   9344 O O     . ILE H 2 5   ? -3.495  14.454  -21.340 1.00 42.97 ?  5   ILE H O     1 
ATOM   9345 C CB    . ILE H 2 5   ? -1.131  16.260  -22.158 1.00 43.35 ?  5   ILE H CB    1 
ATOM   9346 C CG1   . ILE H 2 5   ? -0.260  16.941  -23.215 1.00 38.08 ?  5   ILE H CG1   1 
ATOM   9347 C CG2   . ILE H 2 5   ? -0.421  16.227  -20.813 1.00 37.07 ?  5   ILE H CG2   1 
ATOM   9348 C CD1   . ILE H 2 5   ? -0.067  18.418  -22.988 1.00 35.46 ?  5   ILE H CD1   1 
ATOM   9349 O OXT   . ILE H 2 5   ? -1.844  13.216  -20.879 1.00 42.56 ?  5   ILE H OXT   1 
HETATM 9350 O O     . HOH I 3 .   ? 5.524   20.941  21.560  1.00 43.41 ?  401 HOH A O     1 
HETATM 9351 O O     . HOH I 3 .   ? 34.171  35.915  33.275  1.00 36.47 ?  402 HOH A O     1 
HETATM 9352 O O     . HOH I 3 .   ? 19.633  39.860  9.245   1.00 41.91 ?  403 HOH A O     1 
HETATM 9353 O O     . HOH I 3 .   ? 10.171  34.715  29.889  1.00 44.53 ?  404 HOH A O     1 
HETATM 9354 O O     . HOH I 3 .   ? 29.753  28.390  50.935  1.00 54.53 ?  405 HOH A O     1 
HETATM 9355 O O     . HOH I 3 .   ? 26.864  6.356   42.888  1.00 49.00 ?  406 HOH A O     1 
HETATM 9356 O O     . HOH I 3 .   ? 28.760  40.951  8.909   1.00 45.39 ?  407 HOH A O     1 
HETATM 9357 O O     . HOH I 3 .   ? 45.462  15.903  23.107  1.00 33.38 ?  408 HOH A O     1 
HETATM 9358 O O     . HOH I 3 .   ? 37.347  19.620  13.693  1.00 38.79 ?  409 HOH A O     1 
HETATM 9359 O O     . HOH I 3 .   ? 45.236  22.028  21.090  1.00 41.33 ?  410 HOH A O     1 
HETATM 9360 O O     . HOH I 3 .   ? 10.711  40.211  26.746  1.00 46.85 ?  411 HOH A O     1 
HETATM 9361 O O     . HOH I 3 .   ? 33.355  26.827  35.685  1.00 29.76 ?  412 HOH A O     1 
HETATM 9362 O O     . HOH I 3 .   ? 19.343  9.959   22.929  1.00 28.71 ?  413 HOH A O     1 
HETATM 9363 O O     . HOH I 3 .   ? 46.827  29.952  20.707  1.00 36.10 ?  414 HOH A O     1 
HETATM 9364 O O     . HOH I 3 .   ? 27.263  26.279  46.592  1.00 34.13 ?  415 HOH A O     1 
HETATM 9365 O O     . HOH I 3 .   ? 15.000  17.501  9.557   1.00 32.24 ?  416 HOH A O     1 
HETATM 9366 O O     . HOH I 3 .   ? 48.287  21.121  39.336  1.00 43.27 ?  417 HOH A O     1 
HETATM 9367 O O     . HOH I 3 .   ? 28.036  30.758  22.617  1.00 20.56 ?  418 HOH A O     1 
HETATM 9368 O O     . HOH I 3 .   ? 31.821  21.844  50.228  1.00 39.38 ?  419 HOH A O     1 
HETATM 9369 O O     . HOH I 3 .   ? 24.142  15.391  25.776  1.00 24.34 ?  420 HOH A O     1 
HETATM 9370 O O     . HOH I 3 .   ? 13.193  39.800  29.826  1.00 39.86 ?  421 HOH A O     1 
HETATM 9371 O O     . HOH I 3 .   ? 36.967  28.350  37.269  1.00 39.46 ?  422 HOH A O     1 
HETATM 9372 O O     . HOH I 3 .   ? 16.771  40.708  18.108  1.00 40.59 ?  423 HOH A O     1 
HETATM 9373 O O     . HOH I 3 .   ? 40.221  11.147  36.121  1.00 34.15 ?  424 HOH A O     1 
HETATM 9374 O O     . HOH I 3 .   ? 17.594  12.472  17.778  1.00 30.25 ?  425 HOH A O     1 
HETATM 9375 O O     . HOH I 3 .   ? 10.235  32.996  24.436  1.00 35.68 ?  426 HOH A O     1 
HETATM 9376 O O     . HOH I 3 .   ? 47.608  14.874  40.857  1.00 40.33 ?  427 HOH A O     1 
HETATM 9377 O O     . HOH I 3 .   ? 52.976  19.855  29.773  1.00 30.62 ?  428 HOH A O     1 
HETATM 9378 O O     . HOH I 3 .   ? 32.068  26.801  49.211  1.00 36.34 ?  429 HOH A O     1 
HETATM 9379 O O     . HOH I 3 .   ? 48.119  21.077  50.817  1.00 43.40 ?  430 HOH A O     1 
HETATM 9380 O O     . HOH I 3 .   ? 37.749  18.623  16.180  1.00 30.83 ?  431 HOH A O     1 
HETATM 9381 O O     . HOH I 3 .   ? 25.456  42.842  24.895  1.00 34.68 ?  432 HOH A O     1 
HETATM 9382 O O     . HOH I 3 .   ? 19.815  27.305  2.068   1.00 35.94 ?  433 HOH A O     1 
HETATM 9383 O O     . HOH I 3 .   ? 8.814   34.499  26.358  1.00 42.04 ?  434 HOH A O     1 
HETATM 9384 O O     . HOH I 3 .   ? 32.273  26.913  24.347  1.00 20.92 ?  435 HOH A O     1 
HETATM 9385 O O     . HOH I 3 .   ? 19.897  12.717  17.120  1.00 31.12 ?  436 HOH A O     1 
HETATM 9386 O O     . HOH I 3 .   ? 33.717  7.272   11.622  1.00 37.24 ?  437 HOH A O     1 
HETATM 9387 O O     . HOH I 3 .   ? 56.145  27.197  30.234  1.00 33.42 ?  438 HOH A O     1 
HETATM 9388 O O     . HOH I 3 .   ? 17.611  39.303  15.667  1.00 34.02 ?  439 HOH A O     1 
HETATM 9389 O O     . HOH I 3 .   ? 44.472  25.824  29.702  1.00 28.54 ?  440 HOH A O     1 
HETATM 9390 O O     . HOH I 3 .   ? 40.140  29.917  11.990  1.00 29.06 ?  441 HOH A O     1 
HETATM 9391 O O     . HOH I 3 .   ? 29.609  40.707  33.862  1.00 32.12 ?  442 HOH A O     1 
HETATM 9392 O O     . HOH I 3 .   ? 32.052  28.655  3.215   1.00 39.89 ?  443 HOH A O     1 
HETATM 9393 O O     . HOH I 3 .   ? 10.708  36.137  24.723  1.00 43.18 ?  444 HOH A O     1 
HETATM 9394 O O     . HOH I 3 .   ? 12.606  31.450  35.283  1.00 32.48 ?  445 HOH A O     1 
HETATM 9395 O O     . HOH I 3 .   ? 35.918  35.378  22.893  1.00 32.20 ?  446 HOH A O     1 
HETATM 9396 O O     . HOH I 3 .   ? 21.058  21.638  24.272  1.00 29.64 ?  447 HOH A O     1 
HETATM 9397 O O     . HOH I 3 .   ? 45.633  32.307  28.754  1.00 32.95 ?  448 HOH A O     1 
HETATM 9398 O O     . HOH I 3 .   ? 8.353   30.182  30.444  1.00 34.92 ?  449 HOH A O     1 
HETATM 9399 O O     . HOH I 3 .   ? 20.737  21.439  1.868   1.00 42.98 ?  450 HOH A O     1 
HETATM 9400 O O     . HOH I 3 .   ? 30.055  11.384  28.317  1.00 25.92 ?  451 HOH A O     1 
HETATM 9401 O O     . HOH I 3 .   ? 22.374  35.713  32.108  1.00 26.72 ?  452 HOH A O     1 
HETATM 9402 O O     . HOH I 3 .   ? 14.620  24.781  0.845   1.00 39.63 ?  453 HOH A O     1 
HETATM 9403 O O     . HOH I 3 .   ? 10.128  15.720  5.475   1.00 45.99 ?  454 HOH A O     1 
HETATM 9404 O O     . HOH I 3 .   ? 15.725  14.963  10.735  1.00 25.68 ?  455 HOH A O     1 
HETATM 9405 O O     . HOH I 3 .   ? 27.814  43.757  19.791  1.00 34.30 ?  456 HOH A O     1 
HETATM 9406 O O     . HOH I 3 .   ? 40.492  6.227   24.262  1.00 33.43 ?  457 HOH A O     1 
HETATM 9407 O O     . HOH I 3 .   ? 46.765  27.467  30.308  1.00 28.79 ?  458 HOH A O     1 
HETATM 9408 O O     . HOH I 3 .   ? 25.639  33.130  29.582  1.00 25.80 ?  459 HOH A O     1 
HETATM 9409 O O     . HOH I 3 .   ? 27.885  18.263  35.549  1.00 40.36 ?  460 HOH A O     1 
HETATM 9410 O O     . HOH I 3 .   ? 20.305  22.505  27.588  1.00 35.45 ?  461 HOH A O     1 
HETATM 9411 O O     . HOH I 3 .   ? 37.630  33.333  5.227   1.00 39.08 ?  462 HOH A O     1 
HETATM 9412 O O     . HOH I 3 .   ? 23.113  27.285  20.343  1.00 25.57 ?  463 HOH A O     1 
HETATM 9413 O O     . HOH I 3 .   ? 39.038  20.148  21.120  1.00 34.49 ?  464 HOH A O     1 
HETATM 9414 O O     . HOH I 3 .   ? 22.668  33.546  28.056  1.00 29.36 ?  465 HOH A O     1 
HETATM 9415 O O     . HOH I 3 .   ? 9.761   34.703  22.417  1.00 37.84 ?  466 HOH A O     1 
HETATM 9416 O O     . HOH I 3 .   ? 37.815  5.934   13.801  1.00 33.21 ?  467 HOH A O     1 
HETATM 9417 O O     . HOH I 3 .   ? 21.719  23.439  -1.838  1.00 55.27 ?  468 HOH A O     1 
HETATM 9418 O O     . HOH I 3 .   ? 12.602  26.609  5.582   1.00 48.07 ?  469 HOH A O     1 
HETATM 9419 O O     . HOH I 3 .   ? 27.440  25.843  22.262  1.00 26.23 ?  470 HOH A O     1 
HETATM 9420 O O     . HOH I 3 .   ? 35.077  36.379  18.480  1.00 30.24 ?  471 HOH A O     1 
HETATM 9421 O O     . HOH I 3 .   ? 25.619  9.898   19.400  1.00 28.26 ?  472 HOH A O     1 
HETATM 9422 O O     . HOH I 3 .   ? 8.651   33.437  6.122   1.00 50.95 ?  473 HOH A O     1 
HETATM 9423 O O     . HOH I 3 .   ? 39.387  36.028  29.688  1.00 34.71 ?  474 HOH A O     1 
HETATM 9424 O O     . HOH I 3 .   ? 27.936  37.792  3.324   1.00 36.64 ?  475 HOH A O     1 
HETATM 9425 O O     . HOH I 3 .   ? 22.925  36.057  29.506  1.00 29.84 ?  476 HOH A O     1 
HETATM 9426 O O     . HOH I 3 .   ? 14.806  24.543  6.654   1.00 31.65 ?  477 HOH A O     1 
HETATM 9427 O O     . HOH I 3 .   ? 28.189  9.909   23.349  1.00 30.61 ?  478 HOH A O     1 
HETATM 9428 O O     . HOH I 3 .   ? 41.426  9.348   12.075  1.00 48.68 ?  479 HOH A O     1 
HETATM 9429 O O     . HOH I 3 .   ? 4.002   32.173  6.411   1.00 44.76 ?  480 HOH A O     1 
HETATM 9430 O O     . HOH I 3 .   ? 14.795  18.310  20.536  1.00 23.43 ?  481 HOH A O     1 
HETATM 9431 O O     . HOH I 3 .   ? 8.224   12.763  27.553  1.00 40.29 ?  482 HOH A O     1 
HETATM 9432 O O     . HOH I 3 .   ? 39.044  36.817  19.881  1.00 30.78 ?  483 HOH A O     1 
HETATM 9433 O O     . HOH I 3 .   ? 42.040  25.836  21.469  1.00 36.25 ?  484 HOH A O     1 
HETATM 9434 O O     . HOH I 3 .   ? 15.833  41.318  21.690  1.00 41.51 ?  485 HOH A O     1 
HETATM 9435 O O     . HOH I 3 .   ? 37.454  12.189  35.187  1.00 31.74 ?  486 HOH A O     1 
HETATM 9436 O O     . HOH I 3 .   ? 49.240  27.104  45.667  1.00 45.37 ?  487 HOH A O     1 
HETATM 9437 O O     . HOH I 3 .   ? 10.480  32.595  30.658  1.00 42.83 ?  488 HOH A O     1 
HETATM 9438 O O     . HOH I 3 .   ? 41.622  20.756  20.730  1.00 36.59 ?  489 HOH A O     1 
HETATM 9439 O O     . HOH I 3 .   ? 24.874  31.571  -2.554  1.00 47.31 ?  490 HOH A O     1 
HETATM 9440 O O     . HOH I 3 .   ? 23.158  20.756  30.796  1.00 38.27 ?  491 HOH A O     1 
HETATM 9441 O O     . HOH I 3 .   ? 24.328  12.427  21.832  1.00 30.79 ?  492 HOH A O     1 
HETATM 9442 O O     . HOH I 3 .   ? 44.792  27.284  37.849  1.00 38.56 ?  493 HOH A O     1 
HETATM 9443 O O     . HOH I 3 .   ? 23.536  37.873  3.650   1.00 36.75 ?  494 HOH A O     1 
HETATM 9444 O O     . HOH I 3 .   ? 23.207  43.823  32.200  1.00 41.83 ?  495 HOH A O     1 
HETATM 9445 O O     . HOH I 3 .   ? 8.221   31.160  27.284  1.00 33.23 ?  496 HOH A O     1 
HETATM 9446 O O     . HOH I 3 .   ? 11.678  36.465  21.201  1.00 46.67 ?  497 HOH A O     1 
HETATM 9447 O O     . HOH I 3 .   ? 35.172  12.811  13.661  1.00 44.32 ?  498 HOH A O     1 
HETATM 9448 O O     . HOH I 3 .   ? 31.123  10.088  7.227   1.00 53.25 ?  499 HOH A O     1 
HETATM 9449 O O     . HOH I 3 .   ? 33.137  42.668  15.462  1.00 47.40 ?  500 HOH A O     1 
HETATM 9450 O O     . HOH I 3 .   ? 25.688  27.676  21.456  1.00 27.01 ?  501 HOH A O     1 
HETATM 9451 O O     . HOH I 3 .   ? 36.536  37.008  24.451  1.00 35.94 ?  502 HOH A O     1 
HETATM 9452 O O     . HOH I 3 .   ? 25.883  36.748  4.538   1.00 37.08 ?  503 HOH A O     1 
HETATM 9453 O O     . HOH I 3 .   ? 28.755  6.074   6.037   1.00 45.52 ?  504 HOH A O     1 
HETATM 9454 O O     . HOH I 3 .   ? 33.378  11.821  44.808  1.00 43.97 ?  505 HOH A O     1 
HETATM 9455 O O     . HOH I 3 .   ? 47.981  13.152  27.805  1.00 42.67 ?  506 HOH A O     1 
HETATM 9456 O O     . HOH I 3 .   ? 25.642  35.846  29.563  1.00 27.73 ?  507 HOH A O     1 
HETATM 9457 O O     . HOH I 3 .   ? 44.003  1.216   9.543   1.00 42.70 ?  508 HOH A O     1 
HETATM 9458 O O     . HOH I 3 .   ? 37.261  32.827  7.835   1.00 41.63 ?  509 HOH A O     1 
HETATM 9459 O O     . HOH I 3 .   ? 21.798  27.323  23.016  1.00 27.55 ?  510 HOH A O     1 
HETATM 9460 O O     . HOH I 3 .   ? 6.678   30.405  32.999  1.00 50.99 ?  511 HOH A O     1 
HETATM 9461 O O     . HOH I 3 .   ? 32.841  12.793  12.876  1.00 39.13 ?  512 HOH A O     1 
HETATM 9462 O O     . HOH I 3 .   ? 14.049  32.544  30.083  1.00 32.53 ?  513 HOH A O     1 
HETATM 9463 O O     . HOH I 3 .   ? 38.562  32.183  9.693   1.00 46.39 ?  514 HOH A O     1 
HETATM 9464 O O     . HOH I 3 .   ? 15.792  42.548  33.805  1.00 46.94 ?  515 HOH A O     1 
HETATM 9465 O O     . HOH I 3 .   ? 35.837  30.575  34.765  1.00 27.67 ?  516 HOH A O     1 
HETATM 9466 O O     . HOH I 3 .   ? 7.811   26.776  21.303  1.00 33.18 ?  517 HOH A O     1 
HETATM 9467 O O     . HOH I 3 .   ? 23.078  7.038   25.637  1.00 26.75 ?  518 HOH A O     1 
HETATM 9468 O O     . HOH I 3 .   ? 4.965   17.511  22.962  1.00 45.70 ?  519 HOH A O     1 
HETATM 9469 O O     . HOH I 3 .   ? 54.789  23.559  23.202  1.00 40.67 ?  520 HOH A O     1 
HETATM 9470 O O     . HOH I 3 .   ? 44.039  24.676  22.624  1.00 38.34 ?  521 HOH A O     1 
HETATM 9471 O O     . HOH I 3 .   ? 37.261  20.558  18.557  1.00 34.48 ?  522 HOH A O     1 
HETATM 9472 O O     . HOH I 3 .   ? 32.370  29.093  0.421   1.00 46.97 ?  523 HOH A O     1 
HETATM 9473 O O     . HOH I 3 .   ? 45.632  7.363   15.595  1.00 49.73 ?  524 HOH A O     1 
HETATM 9474 O O     . HOH I 3 .   ? 35.615  38.493  12.573  1.00 42.00 ?  525 HOH A O     1 
HETATM 9475 O O     . HOH I 3 .   ? 13.702  39.633  18.833  1.00 41.27 ?  526 HOH A O     1 
HETATM 9476 O O     . HOH I 3 .   ? 28.269  12.117  13.365  1.00 35.09 ?  527 HOH A O     1 
HETATM 9477 O O     . HOH I 3 .   ? 45.080  7.511   13.389  1.00 42.68 ?  528 HOH A O     1 
HETATM 9478 O O     . HOH I 3 .   ? 21.637  33.888  36.008  1.00 40.44 ?  529 HOH A O     1 
HETATM 9479 O O     . HOH I 3 .   ? 40.045  17.127  47.402  1.00 49.09 ?  530 HOH A O     1 
HETATM 9480 O O     . HOH I 3 .   ? 33.920  9.831   13.574  1.00 39.60 ?  531 HOH A O     1 
HETATM 9481 O O     . HOH I 3 .   ? 38.840  34.270  26.627  1.00 39.72 ?  532 HOH A O     1 
HETATM 9482 O O     . HOH I 3 .   ? 45.571  3.414   16.040  1.00 41.24 ?  533 HOH A O     1 
HETATM 9483 O O     . HOH I 3 .   ? 19.294  27.095  33.881  1.00 35.07 ?  534 HOH A O     1 
HETATM 9484 O O     . HOH I 3 .   ? 45.651  20.230  18.743  1.00 47.10 ?  535 HOH A O     1 
HETATM 9485 O O     . HOH I 3 .   ? 8.607   13.484  8.250   1.00 40.71 ?  536 HOH A O     1 
HETATM 9486 O O     . HOH I 3 .   ? 27.256  11.006  25.323  1.00 33.63 ?  537 HOH A O     1 
HETATM 9487 O O     . HOH I 3 .   ? 40.489  12.520  42.649  1.00 54.23 ?  538 HOH A O     1 
HETATM 9488 O O     . HOH I 3 .   ? 6.437   24.768  19.972  1.00 52.30 ?  539 HOH A O     1 
HETATM 9489 O O     . HOH I 3 .   ? 50.636  21.348  39.742  1.00 53.61 ?  540 HOH A O     1 
HETATM 9490 O O     . HOH I 3 .   ? 17.520  25.143  35.273  1.00 37.08 ?  541 HOH A O     1 
HETATM 9491 O O     . HOH I 3 .   ? 5.186   27.263  24.998  1.00 39.54 ?  542 HOH A O     1 
HETATM 9492 O O     . HOH I 3 .   ? 34.519  29.133  36.441  1.00 39.47 ?  543 HOH A O     1 
HETATM 9493 O O     . HOH I 3 .   ? 43.683  29.593  33.588  1.00 36.74 ?  544 HOH A O     1 
HETATM 9494 O O     . HOH I 3 .   ? 5.217   18.396  20.728  1.00 42.64 ?  545 HOH A O     1 
HETATM 9495 O O     . HOH I 3 .   ? 12.360  30.124  37.252  1.00 33.33 ?  546 HOH A O     1 
HETATM 9496 O O     . HOH I 3 .   ? 26.407  11.723  49.244  1.00 51.04 ?  547 HOH A O     1 
HETATM 9497 O O     . HOH I 3 .   ? 36.965  35.303  20.353  1.00 33.36 ?  548 HOH A O     1 
HETATM 9498 O O     . HOH I 3 .   ? 43.573  8.909   12.484  1.00 47.93 ?  549 HOH A O     1 
HETATM 9499 O O     . HOH I 3 .   ? 47.527  14.291  43.834  1.00 57.31 ?  550 HOH A O     1 
HETATM 9500 O O     . HOH I 3 .   ? 24.252  34.009  52.318  1.00 43.43 ?  551 HOH A O     1 
HETATM 9501 O O     . HOH I 3 .   ? 43.149  31.557  32.237  1.00 43.19 ?  552 HOH A O     1 
HETATM 9502 O O     . HOH I 3 .   ? 5.731   13.038  28.697  1.00 46.14 ?  553 HOH A O     1 
HETATM 9503 O O     . HOH I 3 .   ? 39.014  35.324  24.024  1.00 38.48 ?  554 HOH A O     1 
HETATM 9504 O O     . HOH I 3 .   ? 31.961  24.458  50.943  1.00 33.63 ?  555 HOH A O     1 
HETATM 9505 O O     . HOH I 3 .   ? 42.422  23.826  20.017  1.00 43.31 ?  556 HOH A O     1 
HETATM 9506 O O     . HOH I 3 .   ? 46.106  29.332  34.860  1.00 46.91 ?  557 HOH A O     1 
HETATM 9507 O O     . HOH I 3 .   ? 26.083  9.138   48.899  1.00 46.28 ?  558 HOH A O     1 
HETATM 9508 O O     . HOH I 3 .   ? 20.053  45.976  11.630  1.00 73.82 ?  559 HOH A O     1 
HETATM 9509 O O     . HOH J 3 .   ? 49.674  -5.935  21.324  1.00 49.52 ?  401 HOH D O     1 
HETATM 9510 O O     . HOH J 3 .   ? 40.188  -5.035  5.390   1.00 42.60 ?  402 HOH D O     1 
HETATM 9511 O O     . HOH J 3 .   ? 27.546  -14.888 36.082  1.00 43.81 ?  403 HOH D O     1 
HETATM 9512 O O     . HOH J 3 .   ? 15.166  6.461   4.591   1.00 33.24 ?  404 HOH D O     1 
HETATM 9513 O O     . HOH J 3 .   ? 33.480  3.669   36.204  1.00 42.30 ?  405 HOH D O     1 
HETATM 9514 O O     . HOH J 3 .   ? 39.934  8.071   35.078  1.00 41.41 ?  406 HOH D O     1 
HETATM 9515 O O     . HOH J 3 .   ? -5.390  -6.796  23.018  1.00 43.97 ?  407 HOH D O     1 
HETATM 9516 O O     . HOH J 3 .   ? 26.807  -1.767  25.534  1.00 28.05 ?  408 HOH D O     1 
HETATM 9517 O O     . HOH J 3 .   ? 32.161  19.103  4.988   1.00 49.21 ?  409 HOH D O     1 
HETATM 9518 O O     . HOH J 3 .   ? 4.514   -8.276  29.933  1.00 30.28 ?  410 HOH D O     1 
HETATM 9519 O O     . HOH J 3 .   ? -1.628  3.603   25.044  1.00 50.12 ?  411 HOH D O     1 
HETATM 9520 O O     . HOH J 3 .   ? 42.065  3.957   24.065  1.00 34.24 ?  412 HOH D O     1 
HETATM 9521 O O     . HOH J 3 .   ? 4.666   -15.431 31.690  1.00 33.82 ?  413 HOH D O     1 
HETATM 9522 O O     . HOH J 3 .   ? 16.318  -7.417  3.333   1.00 43.60 ?  414 HOH D O     1 
HETATM 9523 O O     . HOH J 3 .   ? 19.051  2.991   20.409  1.00 32.15 ?  415 HOH D O     1 
HETATM 9524 O O     . HOH J 3 .   ? 0.593   -13.038 34.911  1.00 30.52 ?  416 HOH D O     1 
HETATM 9525 O O     . HOH J 3 .   ? 10.926  -4.344  7.214   1.00 32.91 ?  417 HOH D O     1 
HETATM 9526 O O     . HOH J 3 .   ? 10.928  -7.488  19.605  1.00 33.58 ?  418 HOH D O     1 
HETATM 9527 O O     . HOH J 3 .   ? 27.751  9.908   27.800  1.00 29.72 ?  419 HOH D O     1 
HETATM 9528 O O     . HOH J 3 .   ? 25.226  -10.039 17.586  1.00 26.38 ?  420 HOH D O     1 
HETATM 9529 O O     . HOH J 3 .   ? 45.171  -2.546  22.378  1.00 38.87 ?  421 HOH D O     1 
HETATM 9530 O O     . HOH J 3 .   ? 42.913  7.147   29.275  1.00 42.10 ?  422 HOH D O     1 
HETATM 9531 O O     . HOH J 3 .   ? 33.404  8.131   26.327  1.00 28.89 ?  423 HOH D O     1 
HETATM 9532 O O     . HOH J 3 .   ? 30.808  -20.410 8.929   1.00 49.09 ?  424 HOH D O     1 
HETATM 9533 O O     . HOH J 3 .   ? 9.750   8.580   5.030   1.00 38.57 ?  425 HOH D O     1 
HETATM 9534 O O     . HOH J 3 .   ? 13.110  0.702   25.157  1.00 35.81 ?  426 HOH D O     1 
HETATM 9535 O O     . HOH J 3 .   ? 9.947   13.835  10.711  1.00 39.19 ?  427 HOH D O     1 
HETATM 9536 O O     . HOH J 3 .   ? 49.771  -6.441  18.880  1.00 47.44 ?  428 HOH D O     1 
HETATM 9537 O O     . HOH J 3 .   ? 21.247  -5.951  14.981  1.00 29.34 ?  429 HOH D O     1 
HETATM 9538 O O     . HOH J 3 .   ? 8.748   15.502  22.602  1.00 39.42 ?  430 HOH D O     1 
HETATM 9539 O O     . HOH J 3 .   ? 17.980  8.648   21.271  1.00 28.79 ?  431 HOH D O     1 
HETATM 9540 O O     . HOH J 3 .   ? 26.301  16.547  7.978   1.00 33.76 ?  432 HOH D O     1 
HETATM 9541 O O     . HOH J 3 .   ? 8.377   -8.447  17.212  1.00 42.17 ?  433 HOH D O     1 
HETATM 9542 O O     . HOH J 3 .   ? 23.387  -13.412 24.494  1.00 35.67 ?  434 HOH D O     1 
HETATM 9543 O O     . HOH J 3 .   ? 41.754  -7.599  -0.642  1.00 58.06 ?  435 HOH D O     1 
HETATM 9544 O O     . HOH J 3 .   ? 32.743  1.922   29.755  1.00 31.04 ?  436 HOH D O     1 
HETATM 9545 O O     . HOH J 3 .   ? 23.433  4.563   24.451  1.00 26.38 ?  437 HOH D O     1 
HETATM 9546 O O     . HOH J 3 .   ? 32.505  7.878   24.161  1.00 36.00 ?  438 HOH D O     1 
HETATM 9547 O O     . HOH J 3 .   ? 46.954  -3.929  15.299  1.00 40.51 ?  439 HOH D O     1 
HETATM 9548 O O     . HOH J 3 .   ? -0.449  7.177   5.784   1.00 40.25 ?  440 HOH D O     1 
HETATM 9549 O O     . HOH J 3 .   ? 13.473  -15.762 16.603  1.00 40.47 ?  441 HOH D O     1 
HETATM 9550 O O     . HOH J 3 .   ? 11.329  4.890   37.118  1.00 41.49 ?  442 HOH D O     1 
HETATM 9551 O O     . HOH J 3 .   ? 18.171  5.144   18.876  1.00 33.49 ?  443 HOH D O     1 
HETATM 9552 O O     . HOH J 3 .   ? 22.319  -4.436  34.167  1.00 47.42 ?  444 HOH D O     1 
HETATM 9553 O O     . HOH J 3 .   ? 30.542  -21.984 25.882  1.00 43.47 ?  445 HOH D O     1 
HETATM 9554 O O     . HOH J 3 .   ? 17.360  -15.514 29.615  1.00 37.04 ?  446 HOH D O     1 
HETATM 9555 O O     . HOH J 3 .   ? 1.528   -16.454 30.315  1.00 37.18 ?  447 HOH D O     1 
HETATM 9556 O O     . HOH J 3 .   ? 31.876  9.691   15.221  1.00 34.36 ?  448 HOH D O     1 
HETATM 9557 O O     . HOH J 3 .   ? 8.585   7.821   17.806  1.00 32.22 ?  449 HOH D O     1 
HETATM 9558 O O     . HOH J 3 .   ? 26.202  -13.602 32.947  1.00 35.89 ?  450 HOH D O     1 
HETATM 9559 O O     . HOH J 3 .   ? 25.460  -5.302  18.558  1.00 29.78 ?  451 HOH D O     1 
HETATM 9560 O O     . HOH J 3 .   ? 5.282   -9.847  19.161  1.00 38.99 ?  452 HOH D O     1 
HETATM 9561 O O     . HOH J 3 .   ? 47.258  -4.662  22.862  1.00 46.01 ?  453 HOH D O     1 
HETATM 9562 O O     . HOH J 3 .   ? -0.103  -8.966  27.355  1.00 32.92 ?  454 HOH D O     1 
HETATM 9563 O O     . HOH J 3 .   ? -0.686  -5.797  35.594  1.00 29.30 ?  455 HOH D O     1 
HETATM 9564 O O     . HOH J 3 .   ? -0.647  0.899   28.816  1.00 38.45 ?  456 HOH D O     1 
HETATM 9565 O O     . HOH J 3 .   ? 24.579  3.817   7.194   1.00 42.51 ?  457 HOH D O     1 
HETATM 9566 O O     . HOH J 3 .   ? 29.273  -6.533  21.137  1.00 24.33 ?  458 HOH D O     1 
HETATM 9567 O O     . HOH J 3 .   ? 22.574  12.186  31.791  1.00 40.31 ?  459 HOH D O     1 
HETATM 9568 O O     . HOH J 3 .   ? 1.719   -13.285 28.491  1.00 38.99 ?  460 HOH D O     1 
HETATM 9569 O O     . HOH J 3 .   ? 20.445  -13.259 22.583  1.00 33.43 ?  461 HOH D O     1 
HETATM 9570 O O     . HOH J 3 .   ? 27.868  3.365   6.325   1.00 44.36 ?  462 HOH D O     1 
HETATM 9571 O O     . HOH J 3 .   ? 20.211  -24.052 24.924  1.00 45.43 ?  463 HOH D O     1 
HETATM 9572 O O     . HOH J 3 .   ? 19.521  4.618   3.666   1.00 48.37 ?  464 HOH D O     1 
HETATM 9573 O O     . HOH J 3 .   ? 22.406  -16.061 24.542  1.00 37.17 ?  465 HOH D O     1 
HETATM 9574 O O     . HOH J 3 .   ? 19.586  3.956   33.595  1.00 41.64 ?  466 HOH D O     1 
HETATM 9575 O O     . HOH J 3 .   ? 20.617  -15.912 22.373  1.00 39.98 ?  467 HOH D O     1 
HETATM 9576 O O     . HOH J 3 .   ? 24.126  -2.818  27.804  1.00 34.20 ?  468 HOH D O     1 
HETATM 9577 O O     . HOH J 3 .   ? 17.766  7.934   5.415   1.00 42.89 ?  469 HOH D O     1 
HETATM 9578 O O     . HOH J 3 .   ? 25.719  -14.513 8.833   1.00 38.01 ?  470 HOH D O     1 
HETATM 9579 O O     . HOH J 3 .   ? 28.074  -6.962  23.532  1.00 29.72 ?  471 HOH D O     1 
HETATM 9580 O O     . HOH J 3 .   ? 39.080  -5.371  34.980  1.00 47.44 ?  472 HOH D O     1 
HETATM 9581 O O     . HOH J 3 .   ? 27.082  -6.941  19.550  1.00 32.76 ?  473 HOH D O     1 
HETATM 9582 O O     . HOH J 3 .   ? 0.917   8.775   20.299  1.00 47.72 ?  474 HOH D O     1 
HETATM 9583 O O     . HOH J 3 .   ? 20.131  -16.289 26.206  1.00 35.75 ?  475 HOH D O     1 
HETATM 9584 O O     . HOH J 3 .   ? -0.405  2.218   3.664   1.00 40.34 ?  476 HOH D O     1 
HETATM 9585 O O     . HOH J 3 .   ? 16.192  -13.563 28.866  1.00 36.65 ?  477 HOH D O     1 
HETATM 9586 O O     . HOH J 3 .   ? 33.163  -9.407  2.337   1.00 48.63 ?  478 HOH D O     1 
HETATM 9587 O O     . HOH J 3 .   ? 18.741  -4.290  5.639   1.00 35.75 ?  479 HOH D O     1 
HETATM 9588 O O     . HOH J 3 .   ? 18.542  -19.071 13.467  1.00 39.68 ?  480 HOH D O     1 
HETATM 9589 O O     . HOH J 3 .   ? 29.774  5.768   39.154  1.00 46.15 ?  481 HOH D O     1 
HETATM 9590 O O     . HOH J 3 .   ? 23.820  1.445   8.713   1.00 35.36 ?  482 HOH D O     1 
HETATM 9591 O O     . HOH J 3 .   ? -0.999  -3.396  33.256  1.00 44.70 ?  483 HOH D O     1 
HETATM 9592 O O     . HOH J 3 .   ? 37.552  -15.966 1.214   1.00 45.04 ?  484 HOH D O     1 
HETATM 9593 O O     . HOH J 3 .   ? 13.403  6.274   35.989  1.00 45.08 ?  485 HOH D O     1 
HETATM 9594 O O     . HOH J 3 .   ? 46.331  6.837   30.256  1.00 48.50 ?  486 HOH D O     1 
HETATM 9595 O O     . HOH J 3 .   ? 27.702  -23.764 29.721  1.00 44.87 ?  487 HOH D O     1 
HETATM 9596 O O     . HOH J 3 .   ? 38.266  21.671  9.222   1.00 36.46 ?  488 HOH D O     1 
HETATM 9597 O O     . HOH J 3 .   ? 6.223   -10.445 2.736   1.00 50.38 ?  489 HOH D O     1 
HETATM 9598 O O     . HOH J 3 .   ? 24.607  19.400  1.392   1.00 40.29 ?  490 HOH D O     1 
HETATM 9599 O O     . HOH J 3 .   ? 45.439  1.700   14.454  1.00 43.31 ?  491 HOH D O     1 
HETATM 9600 O O     . HOH J 3 .   ? 48.882  -2.398  22.320  1.00 47.80 ?  492 HOH D O     1 
HETATM 9601 O O     . HOH J 3 .   ? 15.271  -21.096 20.717  1.00 35.24 ?  493 HOH D O     1 
HETATM 9602 O O     . HOH J 3 .   ? 42.504  -13.607 9.940   1.00 45.93 ?  494 HOH D O     1 
HETATM 9603 O O     . HOH J 3 .   ? 26.147  8.036   22.859  1.00 28.11 ?  495 HOH D O     1 
HETATM 9604 O O     . HOH J 3 .   ? 21.516  -14.365 10.121  1.00 31.23 ?  496 HOH D O     1 
HETATM 9605 O O     . HOH J 3 .   ? 23.340  12.814  26.469  1.00 28.85 ?  497 HOH D O     1 
HETATM 9606 O O     . HOH J 3 .   ? 31.121  -15.418 4.455   1.00 47.68 ?  498 HOH D O     1 
HETATM 9607 O O     . HOH J 3 .   ? -1.078  1.649   10.434  1.00 32.34 ?  499 HOH D O     1 
HETATM 9608 O O     . HOH J 3 .   ? -2.801  4.026   5.198   1.00 42.14 ?  500 HOH D O     1 
HETATM 9609 O O     . HOH J 3 .   ? 4.035   -7.181  10.262  1.00 43.38 ?  501 HOH D O     1 
HETATM 9610 O O     . HOH J 3 .   ? 42.502  -16.139 15.408  1.00 43.31 ?  502 HOH D O     1 
HETATM 9611 O O     . HOH J 3 .   ? -1.780  -4.491  28.054  1.00 40.11 ?  503 HOH D O     1 
HETATM 9612 O O     . HOH J 3 .   ? 16.215  -19.804 15.137  1.00 46.12 ?  504 HOH D O     1 
HETATM 9613 O O     . HOH J 3 .   ? 33.904  21.487  0.478   1.00 52.94 ?  505 HOH D O     1 
HETATM 9614 O O     . HOH J 3 .   ? 11.596  -3.408  32.872  1.00 41.42 ?  506 HOH D O     1 
HETATM 9615 O O     . HOH J 3 .   ? 42.580  -14.386 7.054   1.00 45.83 ?  507 HOH D O     1 
HETATM 9616 O O     . HOH J 3 .   ? 44.412  0.321   11.708  1.00 46.87 ?  508 HOH D O     1 
HETATM 9617 O O     . HOH J 3 .   ? 21.093  19.280  2.618   1.00 39.10 ?  509 HOH D O     1 
HETATM 9618 O O     . HOH J 3 .   ? 16.759  -11.572 33.527  1.00 41.28 ?  510 HOH D O     1 
HETATM 9619 O O     . HOH J 3 .   ? 33.593  -18.870 28.532  1.00 38.64 ?  511 HOH D O     1 
HETATM 9620 O O     . HOH J 3 .   ? 10.671  -10.790 16.375  1.00 29.77 ?  512 HOH D O     1 
HETATM 9621 O O     . HOH J 3 .   ? 48.295  -6.846  9.739   1.00 54.78 ?  513 HOH D O     1 
HETATM 9622 O O     . HOH J 3 .   ? 4.920   -7.887  7.057   1.00 51.98 ?  514 HOH D O     1 
HETATM 9623 O O     . HOH J 3 .   ? 19.239  -8.284  30.966  1.00 44.42 ?  515 HOH D O     1 
HETATM 9624 O O     . HOH J 3 .   ? 22.516  10.011  0.868   1.00 53.57 ?  516 HOH D O     1 
HETATM 9625 O O     . HOH J 3 .   ? 21.949  9.425   21.804  1.00 30.21 ?  517 HOH D O     1 
HETATM 9626 O O     . HOH J 3 .   ? 40.635  -11.896 30.815  1.00 47.77 ?  518 HOH D O     1 
HETATM 9627 O O     . HOH J 3 .   ? 12.656  -18.256 18.097  1.00 49.83 ?  519 HOH D O     1 
HETATM 9628 O O     . HOH J 3 .   ? 20.811  10.964  -0.634  1.00 53.49 ?  520 HOH D O     1 
HETATM 9629 O O     . HOH J 3 .   ? 33.424  -19.114 30.796  1.00 42.48 ?  521 HOH D O     1 
HETATM 9630 O O     . HOH J 3 .   ? -6.529  -5.383  10.036  1.00 43.70 ?  522 HOH D O     1 
HETATM 9631 O O     . HOH J 3 .   ? 9.935   -13.534 19.330  1.00 46.20 ?  523 HOH D O     1 
HETATM 9632 O O     . HOH J 3 .   ? 2.392   -6.607  6.330   1.00 49.52 ?  524 HOH D O     1 
HETATM 9633 O O     . HOH J 3 .   ? 24.643  11.342  24.550  1.00 34.03 ?  525 HOH D O     1 
HETATM 9634 O O     . HOH J 3 .   ? -1.428  -11.389 33.994  1.00 39.04 ?  526 HOH D O     1 
HETATM 9635 O O     . HOH J 3 .   ? -3.811  -2.402  27.531  1.00 46.01 ?  527 HOH D O     1 
HETATM 9636 O O     . HOH J 3 .   ? -8.364  -3.166  10.137  1.00 54.23 ?  528 HOH D O     1 
HETATM 9637 O O     . HOH J 3 .   ? 16.503  -22.529 22.327  1.00 44.53 ?  529 HOH D O     1 
HETATM 9638 O O     . HOH J 3 .   ? 23.169  -13.365 8.407   1.00 33.99 ?  530 HOH D O     1 
HETATM 9639 O O     . HOH J 3 .   ? 0.088   -11.199 29.303  1.00 37.54 ?  531 HOH D O     1 
HETATM 9640 O O     . HOH J 3 .   ? 41.795  -14.337 31.109  1.00 52.50 ?  532 HOH D O     1 
HETATM 9641 O O     . HOH J 3 .   ? -2.727  -4.791  31.994  1.00 46.32 ?  533 HOH D O     1 
HETATM 9642 O O     . HOH J 3 .   ? -2.361  -11.302 30.706  1.00 43.78 ?  534 HOH D O     1 
HETATM 9643 O O     . HOH J 3 .   ? 26.336  20.253  -0.149  1.00 47.67 ?  535 HOH D O     1 
HETATM 9644 O O     . HOH J 3 .   ? 16.147  -22.570 15.701  1.00 47.33 ?  536 HOH D O     1 
HETATM 9645 O O     . HOH J 3 .   ? -2.004  -6.776  28.379  1.00 41.34 ?  537 HOH D O     1 
HETATM 9646 O O     . HOH J 3 .   ? 10.690  -16.099 20.357  1.00 46.89 ?  538 HOH D O     1 
HETATM 9647 O O     . HOH J 3 .   ? -3.313  -7.824  29.960  1.00 44.94 ?  539 HOH D O     1 
HETATM 9648 O O     . HOH J 3 .   ? 10.852  -18.779 21.245  1.00 43.60 ?  540 HOH D O     1 
HETATM 9649 O O     . HOH K 3 .   ? 14.184  -27.696 -31.223 1.00 38.25 ?  401 HOH B O     1 
HETATM 9650 O O     . HOH K 3 .   ? 17.561  -17.847 -50.858 1.00 38.67 ?  402 HOH B O     1 
HETATM 9651 O O     . HOH K 3 .   ? -2.991  -28.993 -12.288 1.00 50.08 ?  403 HOH B O     1 
HETATM 9652 O O     . HOH K 3 .   ? 4.713   -19.515 -43.628 1.00 31.79 ?  404 HOH B O     1 
HETATM 9653 O O     . HOH K 3 .   ? -14.106 -21.145 -21.664 1.00 30.42 ?  405 HOH B O     1 
HETATM 9654 O O     . HOH K 3 .   ? -11.344 -8.327  -11.676 1.00 42.70 ?  406 HOH B O     1 
HETATM 9655 O O     . HOH K 3 .   ? 23.427  -21.834 -4.615  1.00 47.13 ?  407 HOH B O     1 
HETATM 9656 O O     . HOH K 3 .   ? 16.776  1.553   -7.251  1.00 58.05 ?  408 HOH B O     1 
HETATM 9657 O O     . HOH K 3 .   ? 23.172  -10.361 -48.487 1.00 39.64 ?  409 HOH B O     1 
HETATM 9658 O O     . HOH K 3 .   ? 27.119  -6.686  -25.686 1.00 31.71 ?  410 HOH B O     1 
HETATM 9659 O O     . HOH K 3 .   ? 14.856  -18.631 -50.758 1.00 43.66 ?  411 HOH B O     1 
HETATM 9660 O O     . HOH K 3 .   ? 18.447  -0.495  -37.195 1.00 34.43 ?  412 HOH B O     1 
HETATM 9661 O O     . HOH K 3 .   ? 0.385   -2.384  -15.125 1.00 31.16 ?  413 HOH B O     1 
HETATM 9662 O O     . HOH K 3 .   ? 18.308  -16.683 -2.384  1.00 39.42 ?  414 HOH B O     1 
HETATM 9663 O O     . HOH K 3 .   ? 16.009  -30.937 -24.405 1.00 35.61 ?  415 HOH B O     1 
HETATM 9664 O O     . HOH K 3 .   ? 3.850   -12.124 -27.690 1.00 38.50 ?  416 HOH B O     1 
HETATM 9665 O O     . HOH K 3 .   ? 24.130  -16.768 -22.523 1.00 35.70 ?  417 HOH B O     1 
HETATM 9666 O O     . HOH K 3 .   ? 12.640  -19.433 -34.403 1.00 37.65 ?  418 HOH B O     1 
HETATM 9667 O O     . HOH K 3 .   ? 9.125   -27.706 -1.244  1.00 41.94 ?  419 HOH B O     1 
HETATM 9668 O O     . HOH K 3 .   ? 31.027  -19.910 -26.666 1.00 40.19 ?  420 HOH B O     1 
HETATM 9669 O O     . HOH K 3 .   ? 6.524   -15.104 1.116   1.00 42.70 ?  421 HOH B O     1 
HETATM 9670 O O     . HOH K 3 .   ? 2.858   -12.549 -21.032 1.00 23.82 ?  422 HOH B O     1 
HETATM 9671 O O     . HOH K 3 .   ? 9.992   -25.998 0.354   1.00 38.73 ?  423 HOH B O     1 
HETATM 9672 O O     . HOH K 3 .   ? 9.832   -16.539 -20.162 1.00 26.50 ?  424 HOH B O     1 
HETATM 9673 O O     . HOH K 3 .   ? 11.385  -6.108  -7.036  1.00 36.42 ?  425 HOH B O     1 
HETATM 9674 O O     . HOH K 3 .   ? -4.825  -23.447 -23.987 1.00 29.56 ?  426 HOH B O     1 
HETATM 9675 O O     . HOH K 3 .   ? 3.623   -34.929 -26.613 1.00 39.67 ?  427 HOH B O     1 
HETATM 9676 O O     . HOH K 3 .   ? 10.637  -3.020  -28.028 1.00 30.09 ?  428 HOH B O     1 
HETATM 9677 O O     . HOH K 3 .   ? 6.675   -24.196 -26.178 1.00 21.94 ?  429 HOH B O     1 
HETATM 9678 O O     . HOH K 3 .   ? 16.239  -32.716 -22.023 1.00 46.19 ?  430 HOH B O     1 
HETATM 9679 O O     . HOH K 3 .   ? 2.624   -19.203 -29.040 1.00 30.63 ?  431 HOH B O     1 
HETATM 9680 O O     . HOH K 3 .   ? 10.391  -21.230 -19.980 1.00 25.97 ?  432 HOH B O     1 
HETATM 9681 O O     . HOH K 3 .   ? 24.638  -17.612 -30.848 1.00 25.58 ?  433 HOH B O     1 
HETATM 9682 O O     . HOH K 3 .   ? -9.695  -1.866  -11.598 1.00 34.61 ?  434 HOH B O     1 
HETATM 9683 O O     . HOH K 3 .   ? 14.108  -17.664 -23.092 1.00 24.95 ?  435 HOH B O     1 
HETATM 9684 O O     . HOH K 3 .   ? 21.398  4.362   -16.327 1.00 36.60 ?  436 HOH B O     1 
HETATM 9685 O O     . HOH K 3 .   ? 5.183   -27.605 -4.042  1.00 39.99 ?  437 HOH B O     1 
HETATM 9686 O O     . HOH K 3 .   ? -7.121  -23.527 -28.920 1.00 38.94 ?  438 HOH B O     1 
HETATM 9687 O O     . HOH K 3 .   ? 19.344  -32.495 -18.763 1.00 44.96 ?  439 HOH B O     1 
HETATM 9688 O O     . HOH K 3 .   ? 32.712  -20.632 -33.857 1.00 37.87 ?  440 HOH B O     1 
HETATM 9689 O O     . HOH K 3 .   ? -8.059  -23.636 -24.147 1.00 38.79 ?  441 HOH B O     1 
HETATM 9690 O O     . HOH K 3 .   ? 25.932  -4.673  -24.029 1.00 35.93 ?  442 HOH B O     1 
HETATM 9691 O O     . HOH K 3 .   ? -10.304 -15.415 -28.220 1.00 53.65 ?  443 HOH B O     1 
HETATM 9692 O O     . HOH K 3 .   ? 2.152   -28.689 -10.188 1.00 29.85 ?  444 HOH B O     1 
HETATM 9693 O O     . HOH K 3 .   ? 29.246  -20.415 -22.584 1.00 40.77 ?  445 HOH B O     1 
HETATM 9694 O O     . HOH K 3 .   ? 7.623   -33.673 -20.558 1.00 38.91 ?  446 HOH B O     1 
HETATM 9695 O O     . HOH K 3 .   ? 11.976  -14.953 6.005   1.00 47.88 ?  447 HOH B O     1 
HETATM 9696 O O     . HOH K 3 .   ? 5.563   -6.402  -23.989 1.00 27.73 ?  448 HOH B O     1 
HETATM 9697 O O     . HOH K 3 .   ? 10.908  -5.375  -44.713 1.00 38.95 ?  449 HOH B O     1 
HETATM 9698 O O     . HOH K 3 .   ? -5.079  -3.095  -6.487  1.00 32.91 ?  450 HOH B O     1 
HETATM 9699 O O     . HOH K 3 .   ? 27.065  -18.586 -31.348 1.00 40.06 ?  451 HOH B O     1 
HETATM 9700 O O     . HOH K 3 .   ? -9.594  -3.742  -22.356 1.00 45.53 ?  452 HOH B O     1 
HETATM 9701 O O     . HOH K 3 .   ? 24.600  -18.934 -12.301 1.00 31.86 ?  453 HOH B O     1 
HETATM 9702 O O     . HOH K 3 .   ? -2.403  -8.571  -16.668 1.00 24.23 ?  454 HOH B O     1 
HETATM 9703 O O     . HOH K 3 .   ? 24.029  -11.563 -22.388 1.00 33.15 ?  455 HOH B O     1 
HETATM 9704 O O     . HOH K 3 .   ? 4.136   -24.714 -23.883 1.00 33.41 ?  456 HOH B O     1 
HETATM 9705 O O     . HOH K 3 .   ? 13.549  -31.106 -10.862 1.00 39.24 ?  457 HOH B O     1 
HETATM 9706 O O     . HOH K 3 .   ? 30.164  -6.829  -41.048 1.00 36.46 ?  458 HOH B O     1 
HETATM 9707 O O     . HOH K 3 .   ? 1.511   -0.936  -20.319 1.00 31.29 ?  459 HOH B O     1 
HETATM 9708 O O     . HOH K 3 .   ? 5.882   -17.796 -17.300 1.00 25.63 ?  460 HOH B O     1 
HETATM 9709 O O     . HOH K 3 .   ? 16.712  -4.146  -36.185 1.00 26.74 ?  461 HOH B O     1 
HETATM 9710 O O     . HOH K 3 .   ? 11.696  -8.186  -47.664 1.00 30.24 ?  462 HOH B O     1 
HETATM 9711 O O     . HOH K 3 .   ? 8.229   -19.858 2.114   1.00 47.23 ?  463 HOH B O     1 
HETATM 9712 O O     . HOH K 3 .   ? 0.114   -6.449  -6.102  1.00 32.52 ?  464 HOH B O     1 
HETATM 9713 O O     . HOH K 3 .   ? -2.127  -6.273  -30.177 1.00 40.68 ?  465 HOH B O     1 
HETATM 9714 O O     . HOH K 3 .   ? 10.686  -8.576  -27.284 1.00 36.83 ?  466 HOH B O     1 
HETATM 9715 O O     . HOH K 3 .   ? -5.821  -30.504 -26.073 1.00 39.19 ?  467 HOH B O     1 
HETATM 9716 O O     . HOH K 3 .   ? 21.203  -8.723  -17.381 1.00 26.55 ?  468 HOH B O     1 
HETATM 9717 O O     . HOH K 3 .   ? 14.554  -26.116 -0.493  1.00 39.01 ?  469 HOH B O     1 
HETATM 9718 O O     . HOH K 3 .   ? -6.459  -27.411 -18.181 1.00 40.56 ?  470 HOH B O     1 
HETATM 9719 O O     . HOH K 3 .   ? 10.212  -1.685  -20.555 1.00 30.40 ?  471 HOH B O     1 
HETATM 9720 O O     . HOH K 3 .   ? 17.888  -17.029 1.781   1.00 48.46 ?  472 HOH B O     1 
HETATM 9721 O O     . HOH K 3 .   ? -4.001  -30.877 -28.644 1.00 46.07 ?  473 HOH B O     1 
HETATM 9722 O O     . HOH K 3 .   ? 20.884  -23.223 -18.641 1.00 36.44 ?  474 HOH B O     1 
HETATM 9723 O O     . HOH K 3 .   ? 7.228   -10.779 -34.212 1.00 37.34 ?  475 HOH B O     1 
HETATM 9724 O O     . HOH K 3 .   ? 0.392   -13.406 -2.698  1.00 38.16 ?  476 HOH B O     1 
HETATM 9725 O O     . HOH K 3 .   ? 1.420   -13.614 -24.045 1.00 25.82 ?  477 HOH B O     1 
HETATM 9726 O O     . HOH K 3 .   ? 7.146   -27.341 -2.489  1.00 32.69 ?  478 HOH B O     1 
HETATM 9727 O O     . HOH K 3 .   ? 18.118  -26.280 -21.578 1.00 30.40 ?  479 HOH B O     1 
HETATM 9728 O O     . HOH K 3 .   ? 7.943   -10.609 -48.128 1.00 37.82 ?  480 HOH B O     1 
HETATM 9729 O O     . HOH K 3 .   ? 18.583  -6.849  -45.164 1.00 36.92 ?  481 HOH B O     1 
HETATM 9730 O O     . HOH K 3 .   ? 21.745  -27.185 -19.204 1.00 30.37 ?  482 HOH B O     1 
HETATM 9731 O O     . HOH K 3 .   ? 18.282  -26.549 -17.045 1.00 24.31 ?  483 HOH B O     1 
HETATM 9732 O O     . HOH K 3 .   ? 32.013  -11.583 -40.157 1.00 39.16 ?  484 HOH B O     1 
HETATM 9733 O O     . HOH K 3 .   ? -9.119  -17.251 -14.912 1.00 29.35 ?  485 HOH B O     1 
HETATM 9734 O O     . HOH K 3 .   ? 26.117  -15.505 -24.128 1.00 33.58 ?  486 HOH B O     1 
HETATM 9735 O O     . HOH K 3 .   ? 3.139   -27.217 -27.516 1.00 29.61 ?  487 HOH B O     1 
HETATM 9736 O O     . HOH K 3 .   ? 4.369   2.080   -24.556 1.00 28.91 ?  488 HOH B O     1 
HETATM 9737 O O     . HOH K 3 .   ? 1.492   -25.706 -31.023 1.00 39.34 ?  489 HOH B O     1 
HETATM 9738 O O     . HOH K 3 .   ? 6.701   -11.729 -36.519 1.00 34.80 ?  490 HOH B O     1 
HETATM 9739 O O     . HOH K 3 .   ? -0.085  -10.600 -35.519 1.00 44.98 ?  491 HOH B O     1 
HETATM 9740 O O     . HOH K 3 .   ? -5.938  -20.798 -10.166 1.00 39.38 ?  492 HOH B O     1 
HETATM 9741 O O     . HOH K 3 .   ? 20.018  -25.679 -25.493 1.00 30.04 ?  493 HOH B O     1 
HETATM 9742 O O     . HOH K 3 .   ? 24.767  2.020   -11.376 1.00 50.23 ?  494 HOH B O     1 
HETATM 9743 O O     . HOH K 3 .   ? 36.457  -14.329 -27.428 1.00 38.78 ?  495 HOH B O     1 
HETATM 9744 O O     . HOH K 3 .   ? 4.056   -17.835 -19.478 1.00 31.42 ?  496 HOH B O     1 
HETATM 9745 O O     . HOH K 3 .   ? 15.442  -22.766 -33.328 1.00 26.51 ?  497 HOH B O     1 
HETATM 9746 O O     . HOH K 3 .   ? 29.217  1.691   -20.472 1.00 45.94 ?  498 HOH B O     1 
HETATM 9747 O O     . HOH K 3 .   ? 21.622  -9.459  -14.531 1.00 40.21 ?  499 HOH B O     1 
HETATM 9748 O O     . HOH K 3 .   ? -7.561  -23.783 -17.314 1.00 42.24 ?  500 HOH B O     1 
HETATM 9749 O O     . HOH K 3 .   ? 8.214   -20.287 -47.414 1.00 39.13 ?  501 HOH B O     1 
HETATM 9750 O O     . HOH K 3 .   ? 4.116   -27.338 -25.161 1.00 30.63 ?  502 HOH B O     1 
HETATM 9751 O O     . HOH K 3 .   ? 2.584   -33.183 -13.630 1.00 41.61 ?  503 HOH B O     1 
HETATM 9752 O O     . HOH K 3 .   ? -1.301  -19.345 -48.283 1.00 43.71 ?  504 HOH B O     1 
HETATM 9753 O O     . HOH K 3 .   ? 8.225   -18.036 -18.867 1.00 22.61 ?  505 HOH B O     1 
HETATM 9754 O O     . HOH K 3 .   ? 6.407   -27.536 1.214   1.00 47.07 ?  506 HOH B O     1 
HETATM 9755 O O     . HOH K 3 .   ? 12.201  -25.282 -1.437  1.00 41.36 ?  507 HOH B O     1 
HETATM 9756 O O     . HOH K 3 .   ? 6.297   -24.361 -46.429 1.00 47.28 ?  508 HOH B O     1 
HETATM 9757 O O     . HOH K 3 .   ? 30.205  -9.959  -27.095 1.00 45.22 ?  509 HOH B O     1 
HETATM 9758 O O     . HOH K 3 .   ? 22.932  -6.390  -19.911 1.00 43.47 ?  510 HOH B O     1 
HETATM 9759 O O     . HOH K 3 .   ? 28.791  -17.249 -21.107 1.00 44.66 ?  511 HOH B O     1 
HETATM 9760 O O     . HOH K 3 .   ? 3.417   -24.151 -38.145 1.00 42.56 ?  512 HOH B O     1 
HETATM 9761 O O     . HOH K 3 .   ? 4.205   -34.922 -11.405 1.00 40.87 ?  513 HOH B O     1 
HETATM 9762 O O     . HOH K 3 .   ? -2.957  -29.117 -14.994 1.00 41.14 ?  514 HOH B O     1 
HETATM 9763 O O     . HOH K 3 .   ? 20.258  -10.629 -19.044 1.00 37.74 ?  515 HOH B O     1 
HETATM 9764 O O     . HOH K 3 .   ? 13.801  -33.760 -11.486 1.00 49.40 ?  516 HOH B O     1 
HETATM 9765 O O     . HOH K 3 .   ? 19.404  -32.049 -15.854 1.00 40.09 ?  517 HOH B O     1 
HETATM 9766 O O     . HOH K 3 .   ? 7.636   -27.725 4.029   1.00 56.86 ?  518 HOH B O     1 
HETATM 9767 O O     . HOH K 3 .   ? 25.921  -21.172 -23.836 1.00 41.46 ?  519 HOH B O     1 
HETATM 9768 O O     . HOH K 3 .   ? 28.323  2.208   -18.248 1.00 47.49 ?  520 HOH B O     1 
HETATM 9769 O O     . HOH K 3 .   ? 10.065  -18.165 4.264   1.00 52.48 ?  521 HOH B O     1 
HETATM 9770 O O     . HOH K 3 .   ? 10.187  -20.641 -49.246 1.00 44.34 ?  522 HOH B O     1 
HETATM 9771 O O     . HOH K 3 .   ? 9.130   -1.854  -24.469 1.00 37.25 ?  523 HOH B O     1 
HETATM 9772 O O     . HOH K 3 .   ? 21.198  -5.038  -15.311 1.00 46.55 ?  524 HOH B O     1 
HETATM 9773 O O     . HOH K 3 .   ? 22.673  -0.090  -36.456 1.00 38.98 ?  525 HOH B O     1 
HETATM 9774 O O     . HOH K 3 .   ? 25.703  -22.875 -22.044 1.00 38.57 ?  526 HOH B O     1 
HETATM 9775 O O     . HOH K 3 .   ? -8.732  -3.821  -6.278  1.00 45.51 ?  527 HOH B O     1 
HETATM 9776 O O     . HOH K 3 .   ? 23.205  -22.535 -32.929 1.00 37.73 ?  528 HOH B O     1 
HETATM 9777 O O     . HOH K 3 .   ? 24.409  -19.179 -9.507  1.00 42.44 ?  529 HOH B O     1 
HETATM 9778 O O     . HOH K 3 .   ? 22.834  -1.507  -38.523 1.00 41.78 ?  530 HOH B O     1 
HETATM 9779 O O     . HOH K 3 .   ? 9.905   -9.782  -49.025 1.00 36.02 ?  531 HOH B O     1 
HETATM 9780 O O     . HOH K 3 .   ? 9.287   -15.944 4.686   1.00 52.92 ?  532 HOH B O     1 
HETATM 9781 O O     . HOH K 3 .   ? 13.999  -21.422 -35.262 1.00 41.11 ?  533 HOH B O     1 
HETATM 9782 O O     . HOH K 3 .   ? 28.360  -14.724 -20.514 1.00 44.58 ?  534 HOH B O     1 
HETATM 9783 O O     . HOH K 3 .   ? 19.481  -25.503 -19.294 1.00 27.62 ?  535 HOH B O     1 
HETATM 9784 O O     . HOH K 3 .   ? 20.665  -26.314 -23.196 1.00 35.61 ?  536 HOH B O     1 
HETATM 9785 O O     . HOH K 3 .   ? 22.956  -25.182 -32.243 1.00 35.16 ?  537 HOH B O     1 
HETATM 9786 O O     . HOH K 3 .   ? 6.469   -22.142 -47.725 1.00 49.82 ?  538 HOH B O     1 
HETATM 9787 O O     . HOH K 3 .   ? 24.441  -1.815  -41.049 1.00 43.66 ?  539 HOH B O     1 
HETATM 9788 O O     . HOH K 3 .   ? 25.756  -25.884 -4.834  1.00 41.96 ?  540 HOH B O     1 
HETATM 9789 O O     . HOH K 3 .   ? 24.335  -17.363 -8.102  1.00 41.66 ?  541 HOH B O     1 
HETATM 9790 O O     . HOH K 3 .   ? 24.923  -28.157 -5.778  1.00 51.69 ?  542 HOH B O     1 
HETATM 9791 O O     . HOH K 3 .   ? 6.676   -21.483 -50.498 1.00 49.22 ?  543 HOH B O     1 
HETATM 9792 O O     . HOH L 3 .   ? -21.585 22.640  -18.431 1.00 53.05 ?  401 HOH C O     1 
HETATM 9793 O O     . HOH L 3 .   ? 31.187  15.590  -26.812 1.00 45.88 ?  402 HOH C O     1 
HETATM 9794 O O     . HOH L 3 .   ? -1.217  2.623   -0.967  1.00 50.74 ?  403 HOH C O     1 
HETATM 9795 O O     . HOH L 3 .   ? 4.064   18.488  -40.947 1.00 46.11 ?  404 HOH C O     1 
HETATM 9796 O O     . HOH L 3 .   ? 22.193  28.609  -14.008 1.00 45.60 ?  405 HOH C O     1 
HETATM 9797 O O     . HOH L 3 .   ? 1.210   21.493  -37.340 1.00 41.25 ?  406 HOH C O     1 
HETATM 9798 O O     . HOH L 3 .   ? 14.392  0.482   -27.707 1.00 27.79 ?  407 HOH C O     1 
HETATM 9799 O O     . HOH L 3 .   ? 15.402  31.253  -13.534 1.00 53.27 ?  408 HOH C O     1 
HETATM 9800 O O     . HOH L 3 .   ? -12.098 17.410  -7.200  1.00 48.24 ?  409 HOH C O     1 
HETATM 9801 O O     . HOH L 3 .   ? 5.146   4.539   -23.631 1.00 32.59 ?  410 HOH C O     1 
HETATM 9802 O O     . HOH L 3 .   ? -14.883 16.861  -26.922 1.00 39.23 ?  411 HOH C O     1 
HETATM 9803 O O     . HOH L 3 .   ? 24.605  26.934  -22.432 1.00 47.97 ?  412 HOH C O     1 
HETATM 9804 O O     . HOH L 3 .   ? 1.353   5.083   -17.457 1.00 34.94 ?  413 HOH C O     1 
HETATM 9805 O O     . HOH L 3 .   ? 11.479  30.754  -28.944 1.00 45.09 ?  414 HOH C O     1 
HETATM 9806 O O     . HOH L 3 .   ? 23.473  1.350   -32.248 1.00 40.25 ?  415 HOH C O     1 
HETATM 9807 O O     . HOH L 3 .   ? 25.239  15.620  -9.648  1.00 40.30 ?  416 HOH C O     1 
HETATM 9808 O O     . HOH L 3 .   ? -8.447  -5.969  -17.878 1.00 30.99 ?  417 HOH C O     1 
HETATM 9809 O O     . HOH L 3 .   ? 12.207  32.106  -18.221 1.00 43.92 ?  418 HOH C O     1 
HETATM 9810 O O     . HOH L 3 .   ? 2.489   22.378  -23.073 1.00 36.97 ?  419 HOH C O     1 
HETATM 9811 O O     . HOH L 3 .   ? 8.177   19.670  -18.867 1.00 35.23 ?  420 HOH C O     1 
HETATM 9812 O O     . HOH L 3 .   ? 13.205  6.604   -30.943 1.00 35.45 ?  421 HOH C O     1 
HETATM 9813 O O     . HOH L 3 .   ? 2.164   28.818  -14.821 1.00 48.12 ?  422 HOH C O     1 
HETATM 9814 O O     . HOH L 3 .   ? 8.708   -1.134  -27.292 1.00 27.98 ?  423 HOH C O     1 
HETATM 9815 O O     . HOH L 3 .   ? 4.051   4.346   -44.630 1.00 61.80 ?  424 HOH C O     1 
HETATM 9816 O O     . HOH L 3 .   ? 5.068   22.474  -25.579 1.00 40.94 ?  425 HOH C O     1 
HETATM 9817 O O     . HOH L 3 .   ? 23.362  4.835   -27.290 1.00 26.62 ?  426 HOH C O     1 
HETATM 9818 O O     . HOH L 3 .   ? 8.273   14.646  -19.253 1.00 32.10 ?  427 HOH C O     1 
HETATM 9819 O O     . HOH L 3 .   ? 4.986   15.964  -15.343 1.00 30.36 ?  428 HOH C O     1 
HETATM 9820 O O     . HOH L 3 .   ? 21.721  2.683   -27.213 1.00 30.28 ?  429 HOH C O     1 
HETATM 9821 O O     . HOH L 3 .   ? 14.275  0.963   -25.180 1.00 32.22 ?  430 HOH C O     1 
HETATM 9822 O O     . HOH L 3 .   ? -19.064 6.126   -19.571 1.00 50.47 ?  431 HOH C O     1 
HETATM 9823 O O     . HOH L 3 .   ? 30.325  18.737  -18.840 1.00 50.19 ?  432 HOH C O     1 
HETATM 9824 O O     . HOH L 3 .   ? 25.664  25.816  -20.179 1.00 43.66 ?  433 HOH C O     1 
HETATM 9825 O O     . HOH L 3 .   ? 0.340   0.929   -18.899 1.00 25.92 ?  434 HOH C O     1 
HETATM 9826 O O     . HOH L 3 .   ? 7.898   10.362  -26.136 1.00 24.68 ?  435 HOH C O     1 
HETATM 9827 O O     . HOH L 3 .   ? 2.549   25.321  -23.194 1.00 37.27 ?  436 HOH C O     1 
HETATM 9828 O O     . HOH L 3 .   ? -18.724 17.323  -23.431 1.00 45.67 ?  437 HOH C O     1 
HETATM 9829 O O     . HOH L 3 .   ? 14.835  31.239  -26.188 1.00 39.54 ?  438 HOH C O     1 
HETATM 9830 O O     . HOH L 3 .   ? 1.234   10.432  -25.840 1.00 38.90 ?  439 HOH C O     1 
HETATM 9831 O O     . HOH L 3 .   ? 27.127  25.133  -12.757 1.00 45.70 ?  440 HOH C O     1 
HETATM 9832 O O     . HOH L 3 .   ? 11.440  15.678  -22.868 1.00 27.28 ?  441 HOH C O     1 
HETATM 9833 O O     . HOH L 3 .   ? 4.516   15.393  -5.209  1.00 43.44 ?  442 HOH C O     1 
HETATM 9834 O O     . HOH L 3 .   ? -3.881  15.870  -5.546  1.00 44.83 ?  443 HOH C O     1 
HETATM 9835 O O     . HOH L 3 .   ? 10.744  25.270  -10.980 1.00 35.47 ?  444 HOH C O     1 
HETATM 9836 O O     . HOH L 3 .   ? 3.732   25.178  -25.792 1.00 45.10 ?  445 HOH C O     1 
HETATM 9837 O O     . HOH L 3 .   ? 5.131   11.452  -28.003 1.00 28.66 ?  446 HOH C O     1 
HETATM 9838 O O     . HOH L 3 .   ? 29.743  13.866  -20.541 1.00 36.62 ?  447 HOH C O     1 
HETATM 9839 O O     . HOH L 3 .   ? 33.430  22.654  -25.925 1.00 49.73 ?  448 HOH C O     1 
HETATM 9840 O O     . HOH L 3 .   ? 0.581   -4.290  -7.481  1.00 30.22 ?  449 HOH C O     1 
HETATM 9841 O O     . HOH L 3 .   ? 22.964  -10.920 -10.184 1.00 34.76 ?  450 HOH C O     1 
HETATM 9842 O O     . HOH L 3 .   ? 13.113  8.111   -6.953  1.00 37.60 ?  451 HOH C O     1 
HETATM 9843 O O     . HOH L 3 .   ? 35.747  20.305  -21.112 1.00 52.76 ?  452 HOH C O     1 
HETATM 9844 O O     . HOH L 3 .   ? 11.742  -0.054  -26.400 1.00 37.36 ?  453 HOH C O     1 
HETATM 9845 O O     . HOH L 3 .   ? -17.354 21.863  -25.921 1.00 44.09 ?  454 HOH C O     1 
HETATM 9846 O O     . HOH L 3 .   ? 26.207  23.830  -15.275 1.00 46.70 ?  455 HOH C O     1 
HETATM 9847 O O     . HOH L 3 .   ? -1.530  23.577  -29.116 1.00 42.36 ?  456 HOH C O     1 
HETATM 9848 O O     . HOH L 3 .   ? -10.262 18.878  -7.156  1.00 44.32 ?  457 HOH C O     1 
HETATM 9849 O O     . HOH L 3 .   ? 0.417   1.425   -30.634 1.00 42.23 ?  458 HOH C O     1 
HETATM 9850 O O     . HOH L 3 .   ? 5.851   21.718  -34.455 1.00 41.10 ?  459 HOH C O     1 
HETATM 9851 O O     . HOH L 3 .   ? 27.819  24.418  -16.824 1.00 47.05 ?  460 HOH C O     1 
HETATM 9852 O O     . HOH L 3 .   ? 26.614  11.708  -26.797 1.00 37.05 ?  461 HOH C O     1 
HETATM 9853 O O     . HOH L 3 .   ? 1.250   25.116  -26.988 1.00 41.29 ?  462 HOH C O     1 
HETATM 9854 O O     . HOH L 3 .   ? 15.451  15.197  -37.840 1.00 41.00 ?  463 HOH C O     1 
HETATM 9855 O O     . HOH L 3 .   ? 6.082   21.935  -37.902 1.00 53.01 ?  464 HOH C O     1 
HETATM 9856 O O     . HOH L 3 .   ? 21.450  -6.481  -13.189 1.00 41.64 ?  465 HOH C O     1 
HETATM 9857 O O     . HOH L 3 .   ? -8.308  2.287   -13.807 1.00 31.05 ?  466 HOH C O     1 
HETATM 9858 O O     . HOH L 3 .   ? 7.255   13.973  -44.211 1.00 51.17 ?  467 HOH C O     1 
HETATM 9859 O O     . HOH L 3 .   ? -16.592 3.155   -24.251 1.00 47.32 ?  468 HOH C O     1 
HETATM 9860 O O     . HOH L 3 .   ? -2.688  16.635  -34.373 1.00 44.93 ?  469 HOH C O     1 
HETATM 9861 O O     . HOH L 3 .   ? 9.617   16.338  -20.974 1.00 31.65 ?  470 HOH C O     1 
HETATM 9862 O O     . HOH L 3 .   ? 22.172  20.931  -3.972  1.00 54.86 ?  471 HOH C O     1 
HETATM 9863 O O     . HOH L 3 .   ? -5.750  7.676   -30.208 1.00 52.84 ?  472 HOH C O     1 
HETATM 9864 O O     . HOH L 3 .   ? 34.308  19.187  -19.176 1.00 53.06 ?  473 HOH C O     1 
HETATM 9865 O O     . HOH L 3 .   ? 7.607   20.029  -40.165 1.00 47.37 ?  474 HOH C O     1 
HETATM 9866 O O     . HOH L 3 .   ? 11.865  30.170  -10.364 1.00 44.20 ?  475 HOH C O     1 
HETATM 9867 O O     . HOH L 3 .   ? -20.303 13.422  -23.201 1.00 44.84 ?  476 HOH C O     1 
HETATM 9868 O O     . HOH L 3 .   ? 10.247  17.977  -44.100 1.00 40.61 ?  477 HOH C O     1 
HETATM 9869 O O     . HOH L 3 .   ? 12.812  22.235  -36.233 1.00 53.29 ?  478 HOH C O     1 
HETATM 9870 O O     . HOH L 3 .   ? -5.185  17.526  -3.640  1.00 42.61 ?  479 HOH C O     1 
HETATM 9871 O O     . HOH L 3 .   ? 1.335   12.608  -34.126 1.00 45.17 ?  480 HOH C O     1 
HETATM 9872 O O     . HOH L 3 .   ? 28.635  13.290  -27.976 1.00 41.37 ?  481 HOH C O     1 
HETATM 9873 O O     . HOH L 3 .   ? 9.468   16.022  -24.829 1.00 30.40 ?  482 HOH C O     1 
HETATM 9874 O O     . HOH L 3 .   ? -8.392  13.609  -34.599 1.00 50.85 ?  483 HOH C O     1 
HETATM 9875 O O     . HOH L 3 .   ? 5.617   -1.238  -19.341 1.00 30.01 ?  484 HOH C O     1 
HETATM 9876 O O     . HOH L 3 .   ? 30.219  8.089   -30.067 1.00 49.05 ?  485 HOH C O     1 
HETATM 9877 O O     . HOH L 3 .   ? 10.010  19.919  -39.466 1.00 39.10 ?  486 HOH C O     1 
HETATM 9878 O O     . HOH L 3 .   ? 3.401   10.143  -32.809 1.00 45.26 ?  487 HOH C O     1 
HETATM 9879 O O     . HOH L 3 .   ? 3.386   3.760   -0.473  1.00 37.92 ?  488 HOH C O     1 
HETATM 9880 O O     . HOH L 3 .   ? -6.023  20.853  -14.918 1.00 39.05 ?  489 HOH C O     1 
HETATM 9881 O O     . HOH L 3 .   ? -1.073  -1.907  -1.259  1.00 45.54 ?  490 HOH C O     1 
HETATM 9882 O O     . HOH L 3 .   ? -8.927  -1.695  -7.666  1.00 38.14 ?  491 HOH C O     1 
HETATM 9883 O O     . HOH L 3 .   ? 6.339   -2.434  -23.751 1.00 31.49 ?  492 HOH C O     1 
HETATM 9884 O O     . HOH L 3 .   ? 23.796  1.941   -36.284 1.00 46.63 ?  493 HOH C O     1 
HETATM 9885 O O     . HOH L 3 .   ? -15.146 2.254   -25.851 1.00 49.45 ?  494 HOH C O     1 
HETATM 9886 O O     . HOH L 3 .   ? -7.469  19.265  -16.567 1.00 41.18 ?  495 HOH C O     1 
HETATM 9887 O O     . HOH L 3 .   ? -10.960 -0.576  -7.985  1.00 43.64 ?  496 HOH C O     1 
HETATM 9888 O O     . HOH L 3 .   ? 31.318  25.012  -31.293 1.00 45.75 ?  497 HOH C O     1 
HETATM 9889 O O     . HOH L 3 .   ? 11.706  22.495  -39.048 1.00 47.14 ?  498 HOH C O     1 
HETATM 9890 O O     . HOH L 3 .   ? -2.677  -0.262  -1.429  1.00 43.22 ?  499 HOH C O     1 
HETATM 9891 O O     . HOH L 3 .   ? 32.114  26.875  -29.436 1.00 49.86 ?  500 HOH C O     1 
HETATM 9892 O O     . HOH L 3 .   ? -13.019 -0.611  -6.846  1.00 45.21 ?  501 HOH C O     1 
HETATM 9893 O O     . HOH L 3 .   ? -18.623 23.872  -24.419 1.00 38.18 ?  502 HOH C O     1 
HETATM 9894 O O     . HOH L 3 .   ? -17.584 24.853  -22.469 1.00 50.43 ?  503 HOH C O     1 
HETATM 9895 O O     . HOH L 3 .   ? -12.562 -1.912  -10.223 1.00 53.10 ?  504 HOH C O     1 
HETATM 9896 O O     . HOH L 3 .   ? -11.642 -3.228  -5.710  1.00 53.41 ?  505 HOH C O     1 
HETATM 9897 O O     . HOH M 3 .   ? 25.617  22.623  30.708  1.00 27.49 ?  101 HOH E O     1 
HETATM 9898 O O     . HOH M 3 .   ? 22.063  27.346  33.045  1.00 29.24 ?  102 HOH E O     1 
HETATM 9899 O O     . HOH M 3 .   ? 22.425  36.224  43.000  1.00 45.32 ?  103 HOH E O     1 
HETATM 9900 O O     . HOH M 3 .   ? 24.905  32.016  42.258  1.00 43.28 ?  104 HOH E O     1 
HETATM 9901 O O     . HOH N 3 .   ? 11.306  -16.258 29.288  1.00 47.84 ?  101 HOH F O     1 
HETATM 9902 O O     . HOH N 3 .   ? 18.913  -8.088  28.049  1.00 32.47 ?  102 HOH F O     1 
HETATM 9903 O O     . HOH N 3 .   ? 19.070  -3.019  24.379  1.00 31.77 ?  103 HOH F O     1 
HETATM 9904 O O     . HOH N 3 .   ? 9.873   -13.072 29.000  1.00 39.15 ?  104 HOH F O     1 
HETATM 9905 O O     . HOH N 3 .   ? 12.915  -11.879 35.042  1.00 41.74 ?  105 HOH F O     1 
HETATM 9906 O O     . HOH O 3 .   ? 6.150   -13.971 -28.299 1.00 30.25 ?  101 HOH G O     1 
HETATM 9907 O O     . HOH P 3 .   ? -0.101  16.648  -27.492 1.00 32.81 ?  101 HOH H O     1 
HETATM 9908 O O     . HOH P 3 .   ? 0.490   12.059  -23.481 1.00 38.64 ?  102 HOH H O     1 
HETATM 9909 O O     . HOH P 3 .   ? -9.592  24.230  -27.719 1.00 49.17 ?  103 HOH H O     1 
# 
