data_9DFW
# 
_entry.id   9DFW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DFW         pdb_00009dfw 10.2210/pdb9dfw/pdb 
WWPDB D_1000288014 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-12 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.country'                 
2 2 'Structure model' '_citation.journal_abbrev'          
3 2 'Structure model' '_citation.journal_id_ASTM'         
4 2 'Structure model' '_citation.journal_id_CSD'          
5 2 'Structure model' '_citation.journal_id_ISSN'         
6 2 'Structure model' '_citation.pdbx_database_id_DOI'    
7 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8 2 'Structure model' '_citation.title'                   
9 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DFW 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-30 
_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 'PDB entry same citation' 9DFN unspecified 
PDB 'PDB entry same citation' 9DFU unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tyler.grove@einsteinmed.edu 
_pdbx_contact_author.name_first         Tyler 
_pdbx_contact_author.name_last          Grove 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4763-0646 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lachowicz, J.C.' 1 ? 
'Bonanno, J.B.'   2 ? 
'Grove, T.L.'     3 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural insights from active site variants and beta-8 loop interactions in viperin-like enzymes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2025.04.009 
_citation.pdbx_database_id_PubMed   40373765 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lachowicz, J.C.' 1 ? 
primary 'Grudman, S.'     2 ? 
primary 'Bonanno, J.B.'   3 ? 
primary 'Fiser, A.'       4 ? 
primary 'Grove, T.L.'     5 ? 
# 
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 'Radical SAM core domain-containing protein'          36369.113 3   ? 
;residues 256-261 (Uniprot numbering) DRNGQQ mutated to NCTGGRKD, residues 197-198 (Uniprot numbering) mutated from VT to IE (residue numbers 198-199 in the model)
;
? 'residues have been swapped with mus musculus viperin (Uniprot: Q8CBB9)' 
2 non-polymer nat 'IRON/SULFUR CLUSTER'                                 351.640   3   ? ? ? ? 
3 non-polymer syn S-ADENOSYLMETHIONINE                                  398.437   3   ? ? ? ? 
4 non-polymer syn "CYTIDINE-5'-TRIPHOSPHATE"                            483.156   3   ? ? ? ? 
5 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   2   ? ? ? ? 
6 non-polymer syn 'MAGNESIUM ION'                                       24.305    3   ? ? ? ? 
7 non-polymer syn GLYCEROL                                              92.094    1   ? ? ? ? 
8 water       nat water                                                 18.015    710 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MHHHHHHSSGVDLGTENLYFQSMGQVPVSVNYHFSRKCNKECLFCFHTATTSHVEKPENAKRGLTLLKQAGMKKINFAGG
EPFLYPKFLGEMIDFCKETLQLESVSIVTNGSLVKEQFLQKHGRNIDILAVSCDSFNEATNIKIGRGSGDNVQKLYEIGS
WCQKYDIKFKLNTVVNKFNHLEDMNDHLNALQPFRWKCFQVLIIEGENDSDKTLRNAHSLTISDDEFDRFCERHSSQTCL
VPEPNRLMAKSYLILDEYMRFLNCTGGRKDPSKSILEVGVQQALQAVFWDEEAFVERGGIYDWNKSSCSSDSKDLEW
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHSSGVDLGTENLYFQSMGQVPVSVNYHFSRKCNKECLFCFHTATTSHVEKPENAKRGLTLLKQAGMKKINFAGG
EPFLYPKFLGEMIDFCKETLQLESVSIVTNGSLVKEQFLQKHGRNIDILAVSCDSFNEATNIKIGRGSGDNVQKLYEIGS
WCQKYDIKFKLNTVVNKFNHLEDMNDHLNALQPFRWKCFQVLIIEGENDSDKTLRNAHSLTISDDEFDRFCERHSSQTCL
VPEPNRLMAKSYLILDEYMRFLNCTGGRKDPSKSILEVGVQQALQAVFWDEEAFVERGGIYDWNKSSCSSDSKDLEW
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'IRON/SULFUR CLUSTER'                                 SF4 
3 S-ADENOSYLMETHIONINE                                  SAM 
4 "CYTIDINE-5'-TRIPHOSPHATE"                            CTP 
5 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 
6 'MAGNESIUM ION'                                       MG  
7 GLYCEROL                                              GOL 
8 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   SER n 
1 9   SER n 
1 10  GLY n 
1 11  VAL n 
1 12  ASP n 
1 13  LEU n 
1 14  GLY n 
1 15  THR n 
1 16  GLU n 
1 17  ASN n 
1 18  LEU n 
1 19  TYR n 
1 20  PHE n 
1 21  GLN n 
1 22  SER n 
1 23  MET n 
1 24  GLY n 
1 25  GLN n 
1 26  VAL n 
1 27  PRO n 
1 28  VAL n 
1 29  SER n 
1 30  VAL n 
1 31  ASN n 
1 32  TYR n 
1 33  HIS n 
1 34  PHE n 
1 35  SER n 
1 36  ARG n 
1 37  LYS n 
1 38  CYS n 
1 39  ASN n 
1 40  LYS n 
1 41  GLU n 
1 42  CYS n 
1 43  LEU n 
1 44  PHE n 
1 45  CYS n 
1 46  PHE n 
1 47  HIS n 
1 48  THR n 
1 49  ALA n 
1 50  THR n 
1 51  THR n 
1 52  SER n 
1 53  HIS n 
1 54  VAL n 
1 55  GLU n 
1 56  LYS n 
1 57  PRO n 
1 58  GLU n 
1 59  ASN n 
1 60  ALA n 
1 61  LYS n 
1 62  ARG n 
1 63  GLY n 
1 64  LEU n 
1 65  THR n 
1 66  LEU n 
1 67  LEU n 
1 68  LYS n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  MET n 
1 73  LYS n 
1 74  LYS n 
1 75  ILE n 
1 76  ASN n 
1 77  PHE n 
1 78  ALA n 
1 79  GLY n 
1 80  GLY n 
1 81  GLU n 
1 82  PRO n 
1 83  PHE n 
1 84  LEU n 
1 85  TYR n 
1 86  PRO n 
1 87  LYS n 
1 88  PHE n 
1 89  LEU n 
1 90  GLY n 
1 91  GLU n 
1 92  MET n 
1 93  ILE n 
1 94  ASP n 
1 95  PHE n 
1 96  CYS n 
1 97  LYS n 
1 98  GLU n 
1 99  THR n 
1 100 LEU n 
1 101 GLN n 
1 102 LEU n 
1 103 GLU n 
1 104 SER n 
1 105 VAL n 
1 106 SER n 
1 107 ILE n 
1 108 VAL n 
1 109 THR n 
1 110 ASN n 
1 111 GLY n 
1 112 SER n 
1 113 LEU n 
1 114 VAL n 
1 115 LYS n 
1 116 GLU n 
1 117 GLN n 
1 118 PHE n 
1 119 LEU n 
1 120 GLN n 
1 121 LYS n 
1 122 HIS n 
1 123 GLY n 
1 124 ARG n 
1 125 ASN n 
1 126 ILE n 
1 127 ASP n 
1 128 ILE n 
1 129 LEU n 
1 130 ALA n 
1 131 VAL n 
1 132 SER n 
1 133 CYS n 
1 134 ASP n 
1 135 SER n 
1 136 PHE n 
1 137 ASN n 
1 138 GLU n 
1 139 ALA n 
1 140 THR n 
1 141 ASN n 
1 142 ILE n 
1 143 LYS n 
1 144 ILE n 
1 145 GLY n 
1 146 ARG n 
1 147 GLY n 
1 148 SER n 
1 149 GLY n 
1 150 ASP n 
1 151 ASN n 
1 152 VAL n 
1 153 GLN n 
1 154 LYS n 
1 155 LEU n 
1 156 TYR n 
1 157 GLU n 
1 158 ILE n 
1 159 GLY n 
1 160 SER n 
1 161 TRP n 
1 162 CYS n 
1 163 GLN n 
1 164 LYS n 
1 165 TYR n 
1 166 ASP n 
1 167 ILE n 
1 168 LYS n 
1 169 PHE n 
1 170 LYS n 
1 171 LEU n 
1 172 ASN n 
1 173 THR n 
1 174 VAL n 
1 175 VAL n 
1 176 ASN n 
1 177 LYS n 
1 178 PHE n 
1 179 ASN n 
1 180 HIS n 
1 181 LEU n 
1 182 GLU n 
1 183 ASP n 
1 184 MET n 
1 185 ASN n 
1 186 ASP n 
1 187 HIS n 
1 188 LEU n 
1 189 ASN n 
1 190 ALA n 
1 191 LEU n 
1 192 GLN n 
1 193 PRO n 
1 194 PHE n 
1 195 ARG n 
1 196 TRP n 
1 197 LYS n 
1 198 CYS n 
1 199 PHE n 
1 200 GLN n 
1 201 VAL n 
1 202 LEU n 
1 203 ILE n 
1 204 ILE n 
1 205 GLU n 
1 206 GLY n 
1 207 GLU n 
1 208 ASN n 
1 209 ASP n 
1 210 SER n 
1 211 ASP n 
1 212 LYS n 
1 213 THR n 
1 214 LEU n 
1 215 ARG n 
1 216 ASN n 
1 217 ALA n 
1 218 HIS n 
1 219 SER n 
1 220 LEU n 
1 221 THR n 
1 222 ILE n 
1 223 SER n 
1 224 ASP n 
1 225 ASP n 
1 226 GLU n 
1 227 PHE n 
1 228 ASP n 
1 229 ARG n 
1 230 PHE n 
1 231 CYS n 
1 232 GLU n 
1 233 ARG n 
1 234 HIS n 
1 235 SER n 
1 236 SER n 
1 237 GLN n 
1 238 THR n 
1 239 CYS n 
1 240 LEU n 
1 241 VAL n 
1 242 PRO n 
1 243 GLU n 
1 244 PRO n 
1 245 ASN n 
1 246 ARG n 
1 247 LEU n 
1 248 MET n 
1 249 ALA n 
1 250 LYS n 
1 251 SER n 
1 252 TYR n 
1 253 LEU n 
1 254 ILE n 
1 255 LEU n 
1 256 ASP n 
1 257 GLU n 
1 258 TYR n 
1 259 MET n 
1 260 ARG n 
1 261 PHE n 
1 262 LEU n 
1 263 ASN n 
1 264 CYS n 
1 265 THR n 
1 266 GLY n 
1 267 GLY n 
1 268 ARG n 
1 269 LYS n 
1 270 ASP n 
1 271 PRO n 
1 272 SER n 
1 273 LYS n 
1 274 SER n 
1 275 ILE n 
1 276 LEU n 
1 277 GLU n 
1 278 VAL n 
1 279 GLY n 
1 280 VAL n 
1 281 GLN n 
1 282 GLN n 
1 283 ALA n 
1 284 LEU n 
1 285 GLN n 
1 286 ALA n 
1 287 VAL n 
1 288 PHE n 
1 289 TRP n 
1 290 ASP n 
1 291 GLU n 
1 292 GLU n 
1 293 ALA n 
1 294 PHE n 
1 295 VAL n 
1 296 GLU n 
1 297 ARG n 
1 298 GLY n 
1 299 GLY n 
1 300 ILE n 
1 301 TYR n 
1 302 ASP n 
1 303 TRP n 
1 304 ASN n 
1 305 LYS n 
1 306 SER n 
1 307 SER n 
1 308 CYS n 
1 309 SER n 
1 310 SER n 
1 311 ASP n 
1 312 SER n 
1 313 LYS n 
1 314 ASP n 
1 315 LEU n 
1 316 GLU n 
1 317 TRP 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                   317 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 TRIVIDRAFT_58105 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    Gv29-8 
_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      'Trichoderma virens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     413071 
_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                   ? 
# 
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 
CTP non-polymer         . "CYTIDINE-5'-TRIPHOSPHATE"                            ?                               'C9 H16 N3 O14 P3' 
483.156 
CYS 'L-peptide linking' y CYSTEINE                                              ?                               'C3 H7 N O2 S'     
121.158 
EPE non-polymer         . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES                           'C8 H18 N2 O4 S'   
238.305 
GLN 'L-peptide linking' y GLUTAMINE                                             ?                               'C5 H10 N2 O3'     
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                       ?                               'C5 H9 N O4'       
147.129 
GLY 'peptide linking'   y GLYCINE                                               ?                               'C2 H5 N O2'       
75.067  
GOL non-polymer         . GLYCEROL                                              'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         
92.094  
HIS 'L-peptide linking' y HISTIDINE                                             ?                               'C6 H10 N3 O2 1'   
156.162 
HOH non-polymer         . WATER                                                 ?                               'H2 O'             
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                            ?                               'C6 H13 N O2'      
131.173 
LEU 'L-peptide linking' y LEUCINE                                               ?                               'C6 H13 N O2'      
131.173 
LYS 'L-peptide linking' y LYSINE                                                ?                               'C6 H15 N2 O2 1'   
147.195 
MET 'L-peptide linking' y METHIONINE                                            ?                               'C5 H11 N O2 S'    
149.211 
MG  non-polymer         . 'MAGNESIUM ION'                                       ?                               'Mg 2'             
24.305  
PHE 'L-peptide linking' y PHENYLALANINE                                         ?                               'C9 H11 N O2'      
165.189 
PRO 'L-peptide linking' y PROLINE                                               ?                               'C5 H9 N O2'       
115.130 
SAM non-polymer         . S-ADENOSYLMETHIONINE                                  ?                               'C15 H22 N6 O5 S'  
398.437 
SER 'L-peptide linking' y SERINE                                                ?                               'C3 H7 N O3'       
105.093 
SF4 non-polymer         . 'IRON/SULFUR CLUSTER'                                 ?                               'Fe4 S4'           
351.640 
THR 'L-peptide linking' y THREONINE                                             ?                               'C4 H9 N O3'       
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                            ?                               'C11 H12 N2 O2'    
204.225 
TYR 'L-peptide linking' y TYROSINE                                              ?                               'C9 H11 N O3'      
181.189 
VAL 'L-peptide linking' y VALINE                                                ?                               'C5 H11 N O2'      
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -5  ?   ?   ?   A . n 
A 1 2   HIS 2   -4  ?   ?   ?   A . n 
A 1 3   HIS 3   -3  ?   ?   ?   A . n 
A 1 4   HIS 4   -2  ?   ?   ?   A . n 
A 1 5   HIS 5   -1  ?   ?   ?   A . n 
A 1 6   HIS 6   0   ?   ?   ?   A . n 
A 1 7   HIS 7   1   ?   ?   ?   A . n 
A 1 8   SER 8   2   ?   ?   ?   A . n 
A 1 9   SER 9   3   ?   ?   ?   A . n 
A 1 10  GLY 10  4   ?   ?   ?   A . n 
A 1 11  VAL 11  5   ?   ?   ?   A . n 
A 1 12  ASP 12  6   ?   ?   ?   A . n 
A 1 13  LEU 13  7   ?   ?   ?   A . n 
A 1 14  GLY 14  8   ?   ?   ?   A . n 
A 1 15  THR 15  9   ?   ?   ?   A . n 
A 1 16  GLU 16  10  ?   ?   ?   A . n 
A 1 17  ASN 17  11  ?   ?   ?   A . n 
A 1 18  LEU 18  12  ?   ?   ?   A . n 
A 1 19  TYR 19  13  ?   ?   ?   A . n 
A 1 20  PHE 20  14  ?   ?   ?   A . n 
A 1 21  GLN 21  15  ?   ?   ?   A . n 
A 1 22  SER 22  16  ?   ?   ?   A . n 
A 1 23  MET 23  17  ?   ?   ?   A . n 
A 1 24  GLY 24  18  18  GLY GLY A . n 
A 1 25  GLN 25  19  19  GLN GLN A . n 
A 1 26  VAL 26  20  20  VAL VAL A . n 
A 1 27  PRO 27  21  21  PRO PRO A . n 
A 1 28  VAL 28  22  22  VAL VAL A . n 
A 1 29  SER 29  23  23  SER SER A . n 
A 1 30  VAL 30  24  24  VAL VAL A . n 
A 1 31  ASN 31  25  25  ASN ASN A . n 
A 1 32  TYR 32  26  26  TYR TYR A . n 
A 1 33  HIS 33  27  27  HIS HIS A . n 
A 1 34  PHE 34  28  28  PHE PHE A . n 
A 1 35  SER 35  29  29  SER SER A . n 
A 1 36  ARG 36  30  30  ARG ARG A . n 
A 1 37  LYS 37  31  31  LYS LYS A . n 
A 1 38  CYS 38  32  32  CYS CYS A . n 
A 1 39  ASN 39  33  33  ASN ASN A . n 
A 1 40  LYS 40  34  34  LYS LYS A . n 
A 1 41  GLU 41  35  35  GLU GLU A . n 
A 1 42  CYS 42  36  36  CYS CYS A . n 
A 1 43  LEU 43  37  37  LEU LEU A . n 
A 1 44  PHE 44  38  38  PHE PHE A . n 
A 1 45  CYS 45  39  39  CYS CYS A . n 
A 1 46  PHE 46  40  40  PHE PHE A . n 
A 1 47  HIS 47  41  41  HIS HIS A . n 
A 1 48  THR 48  42  42  THR THR A . n 
A 1 49  ALA 49  43  43  ALA ALA A . n 
A 1 50  THR 50  44  44  THR THR A . n 
A 1 51  THR 51  45  45  THR THR A . n 
A 1 52  SER 52  46  46  SER SER A . n 
A 1 53  HIS 53  47  47  HIS HIS A . n 
A 1 54  VAL 54  48  48  VAL VAL A . n 
A 1 55  GLU 55  49  49  GLU GLU A . n 
A 1 56  LYS 56  50  50  LYS LYS A . n 
A 1 57  PRO 57  51  51  PRO PRO A . n 
A 1 58  GLU 58  52  52  GLU GLU A . n 
A 1 59  ASN 59  53  53  ASN ASN A . n 
A 1 60  ALA 60  54  54  ALA ALA A . n 
A 1 61  LYS 61  55  55  LYS LYS A . n 
A 1 62  ARG 62  56  56  ARG ARG A . n 
A 1 63  GLY 63  57  57  GLY GLY A . n 
A 1 64  LEU 64  58  58  LEU LEU A . n 
A 1 65  THR 65  59  59  THR THR A . n 
A 1 66  LEU 66  60  60  LEU LEU A . n 
A 1 67  LEU 67  61  61  LEU LEU A . n 
A 1 68  LYS 68  62  62  LYS LYS A . n 
A 1 69  GLN 69  63  63  GLN GLN A . n 
A 1 70  ALA 70  64  64  ALA ALA A . n 
A 1 71  GLY 71  65  65  GLY GLY A . n 
A 1 72  MET 72  66  66  MET MET A . n 
A 1 73  LYS 73  67  67  LYS LYS A . n 
A 1 74  LYS 74  68  68  LYS LYS A . n 
A 1 75  ILE 75  69  69  ILE ILE A . n 
A 1 76  ASN 76  70  70  ASN ASN A . n 
A 1 77  PHE 77  71  71  PHE PHE A . n 
A 1 78  ALA 78  72  72  ALA ALA A . n 
A 1 79  GLY 79  73  73  GLY GLY A . n 
A 1 80  GLY 80  74  74  GLY GLY A . n 
A 1 81  GLU 81  75  75  GLU GLU A . n 
A 1 82  PRO 82  76  76  PRO PRO A . n 
A 1 83  PHE 83  77  77  PHE PHE A . n 
A 1 84  LEU 84  78  78  LEU LEU A . n 
A 1 85  TYR 85  79  79  TYR TYR A . n 
A 1 86  PRO 86  80  80  PRO PRO A . n 
A 1 87  LYS 87  81  81  LYS LYS A . n 
A 1 88  PHE 88  82  82  PHE PHE A . n 
A 1 89  LEU 89  83  83  LEU LEU A . n 
A 1 90  GLY 90  84  84  GLY GLY A . n 
A 1 91  GLU 91  85  85  GLU GLU A . n 
A 1 92  MET 92  86  86  MET MET A . n 
A 1 93  ILE 93  87  87  ILE ILE A . n 
A 1 94  ASP 94  88  88  ASP ASP A . n 
A 1 95  PHE 95  89  89  PHE PHE A . n 
A 1 96  CYS 96  90  90  CYS CYS A . n 
A 1 97  LYS 97  91  91  LYS LYS A . n 
A 1 98  GLU 98  92  92  GLU GLU A . n 
A 1 99  THR 99  93  93  THR THR A . n 
A 1 100 LEU 100 94  94  LEU LEU A . n 
A 1 101 GLN 101 95  95  GLN GLN A . n 
A 1 102 LEU 102 96  96  LEU LEU A . n 
A 1 103 GLU 103 97  97  GLU GLU A . n 
A 1 104 SER 104 98  98  SER SER A . n 
A 1 105 VAL 105 99  99  VAL VAL A . n 
A 1 106 SER 106 100 100 SER SER A . n 
A 1 107 ILE 107 101 101 ILE ILE A . n 
A 1 108 VAL 108 102 102 VAL VAL A . n 
A 1 109 THR 109 103 103 THR THR A . n 
A 1 110 ASN 110 104 104 ASN ASN A . n 
A 1 111 GLY 111 105 105 GLY GLY A . n 
A 1 112 SER 112 106 106 SER SER A . n 
A 1 113 LEU 113 107 107 LEU LEU A . n 
A 1 114 VAL 114 108 108 VAL VAL A . n 
A 1 115 LYS 115 109 109 LYS LYS A . n 
A 1 116 GLU 116 110 110 GLU GLU A . n 
A 1 117 GLN 117 111 111 GLN GLN A . n 
A 1 118 PHE 118 112 112 PHE PHE A . n 
A 1 119 LEU 119 113 113 LEU LEU A . n 
A 1 120 GLN 120 114 114 GLN GLN A . n 
A 1 121 LYS 121 115 115 LYS LYS A . n 
A 1 122 HIS 122 116 116 HIS HIS A . n 
A 1 123 GLY 123 117 117 GLY GLY A . n 
A 1 124 ARG 124 118 118 ARG ARG A . n 
A 1 125 ASN 125 119 119 ASN ASN A . n 
A 1 126 ILE 126 120 120 ILE ILE A . n 
A 1 127 ASP 127 121 121 ASP ASP A . n 
A 1 128 ILE 128 122 122 ILE ILE A . n 
A 1 129 LEU 129 123 123 LEU LEU A . n 
A 1 130 ALA 130 124 124 ALA ALA A . n 
A 1 131 VAL 131 125 125 VAL VAL A . n 
A 1 132 SER 132 126 126 SER SER A . n 
A 1 133 CYS 133 127 127 CYS CYS A . n 
A 1 134 ASP 134 128 128 ASP ASP A . n 
A 1 135 SER 135 129 129 SER SER A . n 
A 1 136 PHE 136 130 130 PHE PHE A . n 
A 1 137 ASN 137 131 131 ASN ASN A . n 
A 1 138 GLU 138 132 132 GLU GLU A . n 
A 1 139 ALA 139 133 133 ALA ALA A . n 
A 1 140 THR 140 134 134 THR THR A . n 
A 1 141 ASN 141 135 135 ASN ASN A . n 
A 1 142 ILE 142 136 136 ILE ILE A . n 
A 1 143 LYS 143 137 137 LYS LYS A . n 
A 1 144 ILE 144 138 138 ILE ILE A . n 
A 1 145 GLY 145 139 139 GLY GLY A . n 
A 1 146 ARG 146 140 140 ARG ARG A . n 
A 1 147 GLY 147 141 141 GLY GLY A . n 
A 1 148 SER 148 142 142 SER SER A . n 
A 1 149 GLY 149 143 143 GLY GLY A . n 
A 1 150 ASP 150 144 144 ASP ASP A . n 
A 1 151 ASN 151 145 145 ASN ASN A . n 
A 1 152 VAL 152 146 146 VAL VAL A . n 
A 1 153 GLN 153 147 147 GLN GLN A . n 
A 1 154 LYS 154 148 148 LYS LYS A . n 
A 1 155 LEU 155 149 149 LEU LEU A . n 
A 1 156 TYR 156 150 150 TYR TYR A . n 
A 1 157 GLU 157 151 151 GLU GLU A . n 
A 1 158 ILE 158 152 152 ILE ILE A . n 
A 1 159 GLY 159 153 153 GLY GLY A . n 
A 1 160 SER 160 154 154 SER SER A . n 
A 1 161 TRP 161 155 155 TRP TRP A . n 
A 1 162 CYS 162 156 156 CYS CYS A . n 
A 1 163 GLN 163 157 157 GLN GLN A . n 
A 1 164 LYS 164 158 158 LYS LYS A . n 
A 1 165 TYR 165 159 159 TYR TYR A . n 
A 1 166 ASP 166 160 160 ASP ASP A . n 
A 1 167 ILE 167 161 161 ILE ILE A . n 
A 1 168 LYS 168 162 162 LYS LYS A . n 
A 1 169 PHE 169 163 163 PHE PHE A . n 
A 1 170 LYS 170 164 164 LYS LYS A . n 
A 1 171 LEU 171 165 165 LEU LEU A . n 
A 1 172 ASN 172 166 166 ASN ASN A . n 
A 1 173 THR 173 167 167 THR THR A . n 
A 1 174 VAL 174 168 168 VAL VAL A . n 
A 1 175 VAL 175 169 169 VAL VAL A . n 
A 1 176 ASN 176 170 170 ASN ASN A . n 
A 1 177 LYS 177 171 171 LYS LYS A . n 
A 1 178 PHE 178 172 172 PHE PHE A . n 
A 1 179 ASN 179 173 173 ASN ASN A . n 
A 1 180 HIS 180 174 174 HIS HIS A . n 
A 1 181 LEU 181 175 175 LEU LEU A . n 
A 1 182 GLU 182 176 176 GLU GLU A . n 
A 1 183 ASP 183 177 177 ASP ASP A . n 
A 1 184 MET 184 178 178 MET MET A . n 
A 1 185 ASN 185 179 179 ASN ASN A . n 
A 1 186 ASP 186 180 180 ASP ASP A . n 
A 1 187 HIS 187 181 181 HIS HIS A . n 
A 1 188 LEU 188 182 182 LEU LEU A . n 
A 1 189 ASN 189 183 183 ASN ASN A . n 
A 1 190 ALA 190 184 184 ALA ALA A . n 
A 1 191 LEU 191 185 185 LEU LEU A . n 
A 1 192 GLN 192 186 186 GLN GLN A . n 
A 1 193 PRO 193 187 187 PRO PRO A . n 
A 1 194 PHE 194 188 188 PHE PHE A . n 
A 1 195 ARG 195 189 189 ARG ARG A . n 
A 1 196 TRP 196 190 190 TRP TRP A . n 
A 1 197 LYS 197 191 191 LYS LYS A . n 
A 1 198 CYS 198 192 192 CYS CYS A . n 
A 1 199 PHE 199 193 193 PHE PHE A . n 
A 1 200 GLN 200 194 194 GLN GLN A . n 
A 1 201 VAL 201 195 195 VAL VAL A . n 
A 1 202 LEU 202 196 196 LEU LEU A . n 
A 1 203 ILE 203 197 197 ILE ILE A . n 
A 1 204 ILE 204 198 198 ILE ILE A . n 
A 1 205 GLU 205 199 199 GLU GLU A . n 
A 1 206 GLY 206 200 200 GLY GLY A . n 
A 1 207 GLU 207 201 201 GLU GLU A . n 
A 1 208 ASN 208 202 202 ASN ASN A . n 
A 1 209 ASP 209 203 203 ASP ASP A . n 
A 1 210 SER 210 204 204 SER SER A . n 
A 1 211 ASP 211 205 205 ASP ASP A . n 
A 1 212 LYS 212 206 206 LYS LYS A . n 
A 1 213 THR 213 207 207 THR THR A . n 
A 1 214 LEU 214 208 208 LEU LEU A . n 
A 1 215 ARG 215 209 209 ARG ARG A . n 
A 1 216 ASN 216 210 210 ASN ASN A . n 
A 1 217 ALA 217 211 211 ALA ALA A . n 
A 1 218 HIS 218 212 212 HIS HIS A . n 
A 1 219 SER 219 213 213 SER SER A . n 
A 1 220 LEU 220 214 214 LEU LEU A . n 
A 1 221 THR 221 215 215 THR THR A . n 
A 1 222 ILE 222 216 216 ILE ILE A . n 
A 1 223 SER 223 217 217 SER SER A . n 
A 1 224 ASP 224 218 218 ASP ASP A . n 
A 1 225 ASP 225 219 219 ASP ASP A . n 
A 1 226 GLU 226 220 220 GLU GLU A . n 
A 1 227 PHE 227 221 221 PHE PHE A . n 
A 1 228 ASP 228 222 222 ASP ASP A . n 
A 1 229 ARG 229 223 223 ARG ARG A . n 
A 1 230 PHE 230 224 224 PHE PHE A . n 
A 1 231 CYS 231 225 225 CYS CYS A . n 
A 1 232 GLU 232 226 226 GLU GLU A . n 
A 1 233 ARG 233 227 227 ARG ARG A . n 
A 1 234 HIS 234 228 228 HIS HIS A . n 
A 1 235 SER 235 229 229 SER SER A . n 
A 1 236 SER 236 230 230 SER SER A . n 
A 1 237 GLN 237 231 231 GLN GLN A . n 
A 1 238 THR 238 232 232 THR THR A . n 
A 1 239 CYS 239 233 233 CYS CYS A . n 
A 1 240 LEU 240 234 234 LEU LEU A . n 
A 1 241 VAL 241 235 235 VAL VAL A . n 
A 1 242 PRO 242 236 236 PRO PRO A . n 
A 1 243 GLU 243 237 237 GLU GLU A . n 
A 1 244 PRO 244 238 238 PRO PRO A . n 
A 1 245 ASN 245 239 239 ASN ASN A . n 
A 1 246 ARG 246 240 240 ARG ARG A . n 
A 1 247 LEU 247 241 241 LEU LEU A . n 
A 1 248 MET 248 242 242 MET MET A . n 
A 1 249 ALA 249 243 243 ALA ALA A . n 
A 1 250 LYS 250 244 244 LYS LYS A . n 
A 1 251 SER 251 245 245 SER SER A . n 
A 1 252 TYR 252 246 246 TYR TYR A . n 
A 1 253 LEU 253 247 247 LEU LEU A . n 
A 1 254 ILE 254 248 248 ILE ILE A . n 
A 1 255 LEU 255 249 249 LEU LEU A . n 
A 1 256 ASP 256 250 250 ASP ASP A . n 
A 1 257 GLU 257 251 251 GLU GLU A . n 
A 1 258 TYR 258 252 252 TYR TYR A . n 
A 1 259 MET 259 253 253 MET MET A . n 
A 1 260 ARG 260 254 254 ARG ARG A . n 
A 1 261 PHE 261 255 255 PHE PHE A . n 
A 1 262 LEU 262 256 256 LEU LEU A . n 
A 1 263 ASN 263 257 257 ASN ASN A . n 
A 1 264 CYS 264 258 258 CYS CYS A . n 
A 1 265 THR 265 259 259 THR THR A . n 
A 1 266 GLY 266 260 260 GLY GLY A . n 
A 1 267 GLY 267 261 261 GLY GLY A . n 
A 1 268 ARG 268 262 262 ARG ARG A . n 
A 1 269 LYS 269 263 263 LYS LYS A . n 
A 1 270 ASP 270 264 264 ASP ASP A . n 
A 1 271 PRO 271 265 265 PRO PRO A . n 
A 1 272 SER 272 266 266 SER SER A . n 
A 1 273 LYS 273 267 267 LYS LYS A . n 
A 1 274 SER 274 268 268 SER SER A . n 
A 1 275 ILE 275 269 269 ILE ILE A . n 
A 1 276 LEU 276 270 270 LEU LEU A . n 
A 1 277 GLU 277 271 271 GLU GLU A . n 
A 1 278 VAL 278 272 272 VAL VAL A . n 
A 1 279 GLY 279 273 273 GLY GLY A . n 
A 1 280 VAL 280 274 274 VAL VAL A . n 
A 1 281 GLN 281 275 275 GLN GLN A . n 
A 1 282 GLN 282 276 276 GLN GLN A . n 
A 1 283 ALA 283 277 277 ALA ALA A . n 
A 1 284 LEU 284 278 278 LEU LEU A . n 
A 1 285 GLN 285 279 279 GLN GLN A . n 
A 1 286 ALA 286 280 280 ALA ALA A . n 
A 1 287 VAL 287 281 281 VAL VAL A . n 
A 1 288 PHE 288 282 282 PHE PHE A . n 
A 1 289 TRP 289 283 283 TRP TRP A . n 
A 1 290 ASP 290 284 284 ASP ASP A . n 
A 1 291 GLU 291 285 285 GLU GLU A . n 
A 1 292 GLU 292 286 286 GLU GLU A . n 
A 1 293 ALA 293 287 287 ALA ALA A . n 
A 1 294 PHE 294 288 288 PHE PHE A . n 
A 1 295 VAL 295 289 289 VAL VAL A . n 
A 1 296 GLU 296 290 290 GLU GLU A . n 
A 1 297 ARG 297 291 291 ARG ARG A . n 
A 1 298 GLY 298 292 292 GLY GLY A . n 
A 1 299 GLY 299 293 293 GLY GLY A . n 
A 1 300 ILE 300 294 294 ILE ILE A . n 
A 1 301 TYR 301 295 295 TYR TYR A . n 
A 1 302 ASP 302 296 296 ASP ASP A . n 
A 1 303 TRP 303 297 297 TRP TRP A . n 
A 1 304 ASN 304 298 298 ASN ASN A . n 
A 1 305 LYS 305 299 299 LYS LYS A . n 
A 1 306 SER 306 300 300 SER SER A . n 
A 1 307 SER 307 301 301 SER SER A . n 
A 1 308 CYS 308 302 ?   ?   ?   A . n 
A 1 309 SER 309 303 ?   ?   ?   A . n 
A 1 310 SER 310 304 ?   ?   ?   A . n 
A 1 311 ASP 311 305 ?   ?   ?   A . n 
A 1 312 SER 312 306 ?   ?   ?   A . n 
A 1 313 LYS 313 307 ?   ?   ?   A . n 
A 1 314 ASP 314 308 ?   ?   ?   A . n 
A 1 315 LEU 315 309 ?   ?   ?   A . n 
A 1 316 GLU 316 310 ?   ?   ?   A . n 
A 1 317 TRP 317 311 ?   ?   ?   A . n 
B 1 1   MET 1   -5  ?   ?   ?   B . n 
B 1 2   HIS 2   -4  ?   ?   ?   B . n 
B 1 3   HIS 3   -3  ?   ?   ?   B . n 
B 1 4   HIS 4   -2  ?   ?   ?   B . n 
B 1 5   HIS 5   -1  ?   ?   ?   B . n 
B 1 6   HIS 6   0   ?   ?   ?   B . n 
B 1 7   HIS 7   1   ?   ?   ?   B . n 
B 1 8   SER 8   2   ?   ?   ?   B . n 
B 1 9   SER 9   3   ?   ?   ?   B . n 
B 1 10  GLY 10  4   ?   ?   ?   B . n 
B 1 11  VAL 11  5   ?   ?   ?   B . n 
B 1 12  ASP 12  6   ?   ?   ?   B . n 
B 1 13  LEU 13  7   ?   ?   ?   B . n 
B 1 14  GLY 14  8   ?   ?   ?   B . n 
B 1 15  THR 15  9   ?   ?   ?   B . n 
B 1 16  GLU 16  10  ?   ?   ?   B . n 
B 1 17  ASN 17  11  ?   ?   ?   B . n 
B 1 18  LEU 18  12  ?   ?   ?   B . n 
B 1 19  TYR 19  13  ?   ?   ?   B . n 
B 1 20  PHE 20  14  ?   ?   ?   B . n 
B 1 21  GLN 21  15  ?   ?   ?   B . n 
B 1 22  SER 22  16  ?   ?   ?   B . n 
B 1 23  MET 23  17  ?   ?   ?   B . n 
B 1 24  GLY 24  18  18  GLY GLY B . n 
B 1 25  GLN 25  19  19  GLN GLN B . n 
B 1 26  VAL 26  20  20  VAL VAL B . n 
B 1 27  PRO 27  21  21  PRO PRO B . n 
B 1 28  VAL 28  22  22  VAL VAL B . n 
B 1 29  SER 29  23  23  SER SER B . n 
B 1 30  VAL 30  24  24  VAL VAL B . n 
B 1 31  ASN 31  25  25  ASN ASN B . n 
B 1 32  TYR 32  26  26  TYR TYR B . n 
B 1 33  HIS 33  27  27  HIS HIS B . n 
B 1 34  PHE 34  28  28  PHE PHE B . n 
B 1 35  SER 35  29  29  SER SER B . n 
B 1 36  ARG 36  30  30  ARG ARG B . n 
B 1 37  LYS 37  31  31  LYS LYS B . n 
B 1 38  CYS 38  32  32  CYS CYS B . n 
B 1 39  ASN 39  33  33  ASN ASN B . n 
B 1 40  LYS 40  34  34  LYS LYS B . n 
B 1 41  GLU 41  35  35  GLU GLU B . n 
B 1 42  CYS 42  36  36  CYS CYS B . n 
B 1 43  LEU 43  37  37  LEU LEU B . n 
B 1 44  PHE 44  38  38  PHE PHE B . n 
B 1 45  CYS 45  39  39  CYS CYS B . n 
B 1 46  PHE 46  40  40  PHE PHE B . n 
B 1 47  HIS 47  41  41  HIS HIS B . n 
B 1 48  THR 48  42  42  THR THR B . n 
B 1 49  ALA 49  43  43  ALA ALA B . n 
B 1 50  THR 50  44  44  THR THR B . n 
B 1 51  THR 51  45  45  THR THR B . n 
B 1 52  SER 52  46  46  SER SER B . n 
B 1 53  HIS 53  47  47  HIS HIS B . n 
B 1 54  VAL 54  48  48  VAL VAL B . n 
B 1 55  GLU 55  49  49  GLU GLU B . n 
B 1 56  LYS 56  50  50  LYS LYS B . n 
B 1 57  PRO 57  51  51  PRO PRO B . n 
B 1 58  GLU 58  52  52  GLU GLU B . n 
B 1 59  ASN 59  53  53  ASN ASN B . n 
B 1 60  ALA 60  54  54  ALA ALA B . n 
B 1 61  LYS 61  55  55  LYS LYS B . n 
B 1 62  ARG 62  56  56  ARG ARG B . n 
B 1 63  GLY 63  57  57  GLY GLY B . n 
B 1 64  LEU 64  58  58  LEU LEU B . n 
B 1 65  THR 65  59  59  THR THR B . n 
B 1 66  LEU 66  60  60  LEU LEU B . n 
B 1 67  LEU 67  61  61  LEU LEU B . n 
B 1 68  LYS 68  62  62  LYS LYS B . n 
B 1 69  GLN 69  63  63  GLN GLN B . n 
B 1 70  ALA 70  64  64  ALA ALA B . n 
B 1 71  GLY 71  65  65  GLY GLY B . n 
B 1 72  MET 72  66  66  MET MET B . n 
B 1 73  LYS 73  67  67  LYS LYS B . n 
B 1 74  LYS 74  68  68  LYS LYS B . n 
B 1 75  ILE 75  69  69  ILE ILE B . n 
B 1 76  ASN 76  70  70  ASN ASN B . n 
B 1 77  PHE 77  71  71  PHE PHE B . n 
B 1 78  ALA 78  72  72  ALA ALA B . n 
B 1 79  GLY 79  73  73  GLY GLY B . n 
B 1 80  GLY 80  74  74  GLY GLY B . n 
B 1 81  GLU 81  75  75  GLU GLU B . n 
B 1 82  PRO 82  76  76  PRO PRO B . n 
B 1 83  PHE 83  77  77  PHE PHE B . n 
B 1 84  LEU 84  78  78  LEU LEU B . n 
B 1 85  TYR 85  79  79  TYR TYR B . n 
B 1 86  PRO 86  80  80  PRO PRO B . n 
B 1 87  LYS 87  81  81  LYS LYS B . n 
B 1 88  PHE 88  82  82  PHE PHE B . n 
B 1 89  LEU 89  83  83  LEU LEU B . n 
B 1 90  GLY 90  84  84  GLY GLY B . n 
B 1 91  GLU 91  85  85  GLU GLU B . n 
B 1 92  MET 92  86  86  MET MET B . n 
B 1 93  ILE 93  87  87  ILE ILE B . n 
B 1 94  ASP 94  88  88  ASP ASP B . n 
B 1 95  PHE 95  89  89  PHE PHE B . n 
B 1 96  CYS 96  90  90  CYS CYS B . n 
B 1 97  LYS 97  91  91  LYS LYS B . n 
B 1 98  GLU 98  92  92  GLU GLU B . n 
B 1 99  THR 99  93  93  THR THR B . n 
B 1 100 LEU 100 94  94  LEU LEU B . n 
B 1 101 GLN 101 95  95  GLN GLN B . n 
B 1 102 LEU 102 96  96  LEU LEU B . n 
B 1 103 GLU 103 97  97  GLU GLU B . n 
B 1 104 SER 104 98  98  SER SER B . n 
B 1 105 VAL 105 99  99  VAL VAL B . n 
B 1 106 SER 106 100 100 SER SER B . n 
B 1 107 ILE 107 101 101 ILE ILE B . n 
B 1 108 VAL 108 102 102 VAL VAL B . n 
B 1 109 THR 109 103 103 THR THR B . n 
B 1 110 ASN 110 104 104 ASN ASN B . n 
B 1 111 GLY 111 105 105 GLY GLY B . n 
B 1 112 SER 112 106 106 SER SER B . n 
B 1 113 LEU 113 107 107 LEU LEU B . n 
B 1 114 VAL 114 108 108 VAL VAL B . n 
B 1 115 LYS 115 109 109 LYS LYS B . n 
B 1 116 GLU 116 110 110 GLU GLU B . n 
B 1 117 GLN 117 111 111 GLN GLN B . n 
B 1 118 PHE 118 112 112 PHE PHE B . n 
B 1 119 LEU 119 113 113 LEU LEU B . n 
B 1 120 GLN 120 114 114 GLN GLN B . n 
B 1 121 LYS 121 115 115 LYS LYS B . n 
B 1 122 HIS 122 116 116 HIS HIS B . n 
B 1 123 GLY 123 117 117 GLY GLY B . n 
B 1 124 ARG 124 118 118 ARG ARG B . n 
B 1 125 ASN 125 119 119 ASN ASN B . n 
B 1 126 ILE 126 120 120 ILE ILE B . n 
B 1 127 ASP 127 121 121 ASP ASP B . n 
B 1 128 ILE 128 122 122 ILE ILE B . n 
B 1 129 LEU 129 123 123 LEU LEU B . n 
B 1 130 ALA 130 124 124 ALA ALA B . n 
B 1 131 VAL 131 125 125 VAL VAL B . n 
B 1 132 SER 132 126 126 SER SER B . n 
B 1 133 CYS 133 127 127 CYS CYS B . n 
B 1 134 ASP 134 128 128 ASP ASP B . n 
B 1 135 SER 135 129 129 SER SER B . n 
B 1 136 PHE 136 130 130 PHE PHE B . n 
B 1 137 ASN 137 131 131 ASN ASN B . n 
B 1 138 GLU 138 132 132 GLU GLU B . n 
B 1 139 ALA 139 133 133 ALA ALA B . n 
B 1 140 THR 140 134 134 THR THR B . n 
B 1 141 ASN 141 135 135 ASN ASN B . n 
B 1 142 ILE 142 136 136 ILE ILE B . n 
B 1 143 LYS 143 137 137 LYS LYS B . n 
B 1 144 ILE 144 138 138 ILE ILE B . n 
B 1 145 GLY 145 139 139 GLY GLY B . n 
B 1 146 ARG 146 140 140 ARG ARG B . n 
B 1 147 GLY 147 141 141 GLY GLY B . n 
B 1 148 SER 148 142 142 SER SER B . n 
B 1 149 GLY 149 143 143 GLY GLY B . n 
B 1 150 ASP 150 144 144 ASP ASP B . n 
B 1 151 ASN 151 145 145 ASN ASN B . n 
B 1 152 VAL 152 146 146 VAL VAL B . n 
B 1 153 GLN 153 147 147 GLN GLN B . n 
B 1 154 LYS 154 148 148 LYS LYS B . n 
B 1 155 LEU 155 149 149 LEU LEU B . n 
B 1 156 TYR 156 150 150 TYR TYR B . n 
B 1 157 GLU 157 151 151 GLU GLU B . n 
B 1 158 ILE 158 152 152 ILE ILE B . n 
B 1 159 GLY 159 153 153 GLY GLY B . n 
B 1 160 SER 160 154 154 SER SER B . n 
B 1 161 TRP 161 155 155 TRP TRP B . n 
B 1 162 CYS 162 156 156 CYS CYS B . n 
B 1 163 GLN 163 157 157 GLN GLN B . n 
B 1 164 LYS 164 158 158 LYS LYS B . n 
B 1 165 TYR 165 159 159 TYR TYR B . n 
B 1 166 ASP 166 160 160 ASP ASP B . n 
B 1 167 ILE 167 161 161 ILE ILE B . n 
B 1 168 LYS 168 162 162 LYS LYS B . n 
B 1 169 PHE 169 163 163 PHE PHE B . n 
B 1 170 LYS 170 164 164 LYS LYS B . n 
B 1 171 LEU 171 165 165 LEU LEU B . n 
B 1 172 ASN 172 166 166 ASN ASN B . n 
B 1 173 THR 173 167 167 THR THR B . n 
B 1 174 VAL 174 168 168 VAL VAL B . n 
B 1 175 VAL 175 169 169 VAL VAL B . n 
B 1 176 ASN 176 170 170 ASN ASN B . n 
B 1 177 LYS 177 171 171 LYS LYS B . n 
B 1 178 PHE 178 172 172 PHE PHE B . n 
B 1 179 ASN 179 173 173 ASN ASN B . n 
B 1 180 HIS 180 174 174 HIS HIS B . n 
B 1 181 LEU 181 175 175 LEU LEU B . n 
B 1 182 GLU 182 176 176 GLU GLU B . n 
B 1 183 ASP 183 177 177 ASP ASP B . n 
B 1 184 MET 184 178 178 MET MET B . n 
B 1 185 ASN 185 179 179 ASN ASN B . n 
B 1 186 ASP 186 180 180 ASP ASP B . n 
B 1 187 HIS 187 181 181 HIS HIS B . n 
B 1 188 LEU 188 182 182 LEU LEU B . n 
B 1 189 ASN 189 183 183 ASN ASN B . n 
B 1 190 ALA 190 184 184 ALA ALA B . n 
B 1 191 LEU 191 185 185 LEU LEU B . n 
B 1 192 GLN 192 186 186 GLN GLN B . n 
B 1 193 PRO 193 187 187 PRO PRO B . n 
B 1 194 PHE 194 188 188 PHE PHE B . n 
B 1 195 ARG 195 189 189 ARG ARG B . n 
B 1 196 TRP 196 190 190 TRP TRP B . n 
B 1 197 LYS 197 191 191 LYS LYS B . n 
B 1 198 CYS 198 192 192 CYS CYS B . n 
B 1 199 PHE 199 193 193 PHE PHE B . n 
B 1 200 GLN 200 194 194 GLN GLN B . n 
B 1 201 VAL 201 195 195 VAL VAL B . n 
B 1 202 LEU 202 196 196 LEU LEU B . n 
B 1 203 ILE 203 197 197 ILE ILE B . n 
B 1 204 ILE 204 198 198 ILE ILE B . n 
B 1 205 GLU 205 199 199 GLU GLU B . n 
B 1 206 GLY 206 200 200 GLY GLY B . n 
B 1 207 GLU 207 201 201 GLU GLU B . n 
B 1 208 ASN 208 202 202 ASN ASN B . n 
B 1 209 ASP 209 203 203 ASP ASP B . n 
B 1 210 SER 210 204 204 SER SER B . n 
B 1 211 ASP 211 205 205 ASP ASP B . n 
B 1 212 LYS 212 206 206 LYS LYS B . n 
B 1 213 THR 213 207 207 THR THR B . n 
B 1 214 LEU 214 208 208 LEU LEU B . n 
B 1 215 ARG 215 209 209 ARG ARG B . n 
B 1 216 ASN 216 210 210 ASN ASN B . n 
B 1 217 ALA 217 211 211 ALA ALA B . n 
B 1 218 HIS 218 212 212 HIS HIS B . n 
B 1 219 SER 219 213 213 SER SER B . n 
B 1 220 LEU 220 214 214 LEU LEU B . n 
B 1 221 THR 221 215 215 THR THR B . n 
B 1 222 ILE 222 216 216 ILE ILE B . n 
B 1 223 SER 223 217 217 SER SER B . n 
B 1 224 ASP 224 218 218 ASP ASP B . n 
B 1 225 ASP 225 219 219 ASP ASP B . n 
B 1 226 GLU 226 220 220 GLU GLU B . n 
B 1 227 PHE 227 221 221 PHE PHE B . n 
B 1 228 ASP 228 222 222 ASP ASP B . n 
B 1 229 ARG 229 223 223 ARG ARG B . n 
B 1 230 PHE 230 224 224 PHE PHE B . n 
B 1 231 CYS 231 225 225 CYS CYS B . n 
B 1 232 GLU 232 226 226 GLU GLU B . n 
B 1 233 ARG 233 227 227 ARG ARG B . n 
B 1 234 HIS 234 228 228 HIS HIS B . n 
B 1 235 SER 235 229 229 SER SER B . n 
B 1 236 SER 236 230 230 SER SER B . n 
B 1 237 GLN 237 231 231 GLN GLN B . n 
B 1 238 THR 238 232 232 THR THR B . n 
B 1 239 CYS 239 233 233 CYS CYS B . n 
B 1 240 LEU 240 234 234 LEU LEU B . n 
B 1 241 VAL 241 235 235 VAL VAL B . n 
B 1 242 PRO 242 236 236 PRO PRO B . n 
B 1 243 GLU 243 237 237 GLU GLU B . n 
B 1 244 PRO 244 238 238 PRO PRO B . n 
B 1 245 ASN 245 239 239 ASN ASN B . n 
B 1 246 ARG 246 240 240 ARG ARG B . n 
B 1 247 LEU 247 241 241 LEU LEU B . n 
B 1 248 MET 248 242 242 MET MET B . n 
B 1 249 ALA 249 243 243 ALA ALA B . n 
B 1 250 LYS 250 244 244 LYS LYS B . n 
B 1 251 SER 251 245 245 SER SER B . n 
B 1 252 TYR 252 246 246 TYR TYR B . n 
B 1 253 LEU 253 247 247 LEU LEU B . n 
B 1 254 ILE 254 248 248 ILE ILE B . n 
B 1 255 LEU 255 249 249 LEU LEU B . n 
B 1 256 ASP 256 250 250 ASP ASP B . n 
B 1 257 GLU 257 251 251 GLU GLU B . n 
B 1 258 TYR 258 252 252 TYR TYR B . n 
B 1 259 MET 259 253 253 MET MET B . n 
B 1 260 ARG 260 254 254 ARG ARG B . n 
B 1 261 PHE 261 255 255 PHE PHE B . n 
B 1 262 LEU 262 256 256 LEU LEU B . n 
B 1 263 ASN 263 257 257 ASN ASN B . n 
B 1 264 CYS 264 258 258 CYS CYS B . n 
B 1 265 THR 265 259 259 THR THR B . n 
B 1 266 GLY 266 260 260 GLY GLY B . n 
B 1 267 GLY 267 261 261 GLY GLY B . n 
B 1 268 ARG 268 262 262 ARG ARG B . n 
B 1 269 LYS 269 263 263 LYS LYS B . n 
B 1 270 ASP 270 264 264 ASP ASP B . n 
B 1 271 PRO 271 265 265 PRO PRO B . n 
B 1 272 SER 272 266 266 SER SER B . n 
B 1 273 LYS 273 267 267 LYS LYS B . n 
B 1 274 SER 274 268 268 SER SER B . n 
B 1 275 ILE 275 269 269 ILE ILE B . n 
B 1 276 LEU 276 270 270 LEU LEU B . n 
B 1 277 GLU 277 271 271 GLU GLU B . n 
B 1 278 VAL 278 272 272 VAL VAL B . n 
B 1 279 GLY 279 273 273 GLY GLY B . n 
B 1 280 VAL 280 274 274 VAL VAL B . n 
B 1 281 GLN 281 275 275 GLN GLN B . n 
B 1 282 GLN 282 276 276 GLN GLN B . n 
B 1 283 ALA 283 277 277 ALA ALA B . n 
B 1 284 LEU 284 278 278 LEU LEU B . n 
B 1 285 GLN 285 279 279 GLN GLN B . n 
B 1 286 ALA 286 280 280 ALA ALA B . n 
B 1 287 VAL 287 281 281 VAL VAL B . n 
B 1 288 PHE 288 282 282 PHE PHE B . n 
B 1 289 TRP 289 283 283 TRP TRP B . n 
B 1 290 ASP 290 284 284 ASP ASP B . n 
B 1 291 GLU 291 285 285 GLU GLU B . n 
B 1 292 GLU 292 286 286 GLU GLU B . n 
B 1 293 ALA 293 287 287 ALA ALA B . n 
B 1 294 PHE 294 288 288 PHE PHE B . n 
B 1 295 VAL 295 289 289 VAL VAL B . n 
B 1 296 GLU 296 290 290 GLU GLU B . n 
B 1 297 ARG 297 291 291 ARG ARG B . n 
B 1 298 GLY 298 292 292 GLY GLY B . n 
B 1 299 GLY 299 293 293 GLY GLY B . n 
B 1 300 ILE 300 294 294 ILE ILE B . n 
B 1 301 TYR 301 295 295 TYR TYR B . n 
B 1 302 ASP 302 296 296 ASP ASP B . n 
B 1 303 TRP 303 297 297 TRP TRP B . n 
B 1 304 ASN 304 298 298 ASN ASN B . n 
B 1 305 LYS 305 299 299 LYS LYS B . n 
B 1 306 SER 306 300 300 SER SER B . n 
B 1 307 SER 307 301 301 SER SER B . n 
B 1 308 CYS 308 302 302 CYS CYS B . n 
B 1 309 SER 309 303 303 SER SER B . n 
B 1 310 SER 310 304 304 SER SER B . n 
B 1 311 ASP 311 305 305 ASP ASP B . n 
B 1 312 SER 312 306 306 SER SER B . n 
B 1 313 LYS 313 307 307 LYS LYS B . n 
B 1 314 ASP 314 308 308 ASP ASP B . n 
B 1 315 LEU 315 309 309 LEU LEU B . n 
B 1 316 GLU 316 310 310 GLU GLU B . n 
B 1 317 TRP 317 311 311 TRP TRP B . n 
C 1 1   MET 1   -5  ?   ?   ?   C . n 
C 1 2   HIS 2   -4  ?   ?   ?   C . n 
C 1 3   HIS 3   -3  ?   ?   ?   C . n 
C 1 4   HIS 4   -2  ?   ?   ?   C . n 
C 1 5   HIS 5   -1  ?   ?   ?   C . n 
C 1 6   HIS 6   0   ?   ?   ?   C . n 
C 1 7   HIS 7   1   ?   ?   ?   C . n 
C 1 8   SER 8   2   ?   ?   ?   C . n 
C 1 9   SER 9   3   ?   ?   ?   C . n 
C 1 10  GLY 10  4   ?   ?   ?   C . n 
C 1 11  VAL 11  5   ?   ?   ?   C . n 
C 1 12  ASP 12  6   ?   ?   ?   C . n 
C 1 13  LEU 13  7   ?   ?   ?   C . n 
C 1 14  GLY 14  8   ?   ?   ?   C . n 
C 1 15  THR 15  9   ?   ?   ?   C . n 
C 1 16  GLU 16  10  ?   ?   ?   C . n 
C 1 17  ASN 17  11  ?   ?   ?   C . n 
C 1 18  LEU 18  12  ?   ?   ?   C . n 
C 1 19  TYR 19  13  ?   ?   ?   C . n 
C 1 20  PHE 20  14  ?   ?   ?   C . n 
C 1 21  GLN 21  15  ?   ?   ?   C . n 
C 1 22  SER 22  16  ?   ?   ?   C . n 
C 1 23  MET 23  17  ?   ?   ?   C . n 
C 1 24  GLY 24  18  18  GLY GLY C . n 
C 1 25  GLN 25  19  19  GLN GLN C . n 
C 1 26  VAL 26  20  20  VAL VAL C . n 
C 1 27  PRO 27  21  21  PRO PRO C . n 
C 1 28  VAL 28  22  22  VAL VAL C . n 
C 1 29  SER 29  23  23  SER SER C . n 
C 1 30  VAL 30  24  24  VAL VAL C . n 
C 1 31  ASN 31  25  25  ASN ASN C . n 
C 1 32  TYR 32  26  26  TYR TYR C . n 
C 1 33  HIS 33  27  27  HIS HIS C . n 
C 1 34  PHE 34  28  28  PHE PHE C . n 
C 1 35  SER 35  29  29  SER SER C . n 
C 1 36  ARG 36  30  30  ARG ARG C . n 
C 1 37  LYS 37  31  31  LYS LYS C . n 
C 1 38  CYS 38  32  32  CYS CYS C . n 
C 1 39  ASN 39  33  33  ASN ASN C . n 
C 1 40  LYS 40  34  34  LYS LYS C . n 
C 1 41  GLU 41  35  35  GLU GLU C . n 
C 1 42  CYS 42  36  36  CYS CYS C . n 
C 1 43  LEU 43  37  37  LEU LEU C . n 
C 1 44  PHE 44  38  38  PHE PHE C . n 
C 1 45  CYS 45  39  39  CYS CYS C . n 
C 1 46  PHE 46  40  40  PHE PHE C . n 
C 1 47  HIS 47  41  41  HIS HIS C . n 
C 1 48  THR 48  42  42  THR THR C . n 
C 1 49  ALA 49  43  43  ALA ALA C . n 
C 1 50  THR 50  44  44  THR THR C . n 
C 1 51  THR 51  45  45  THR THR C . n 
C 1 52  SER 52  46  46  SER SER C . n 
C 1 53  HIS 53  47  47  HIS HIS C . n 
C 1 54  VAL 54  48  48  VAL VAL C . n 
C 1 55  GLU 55  49  49  GLU GLU C . n 
C 1 56  LYS 56  50  50  LYS LYS C . n 
C 1 57  PRO 57  51  51  PRO PRO C . n 
C 1 58  GLU 58  52  52  GLU GLU C . n 
C 1 59  ASN 59  53  53  ASN ASN C . n 
C 1 60  ALA 60  54  54  ALA ALA C . n 
C 1 61  LYS 61  55  55  LYS LYS C . n 
C 1 62  ARG 62  56  56  ARG ARG C . n 
C 1 63  GLY 63  57  57  GLY GLY C . n 
C 1 64  LEU 64  58  58  LEU LEU C . n 
C 1 65  THR 65  59  59  THR THR C . n 
C 1 66  LEU 66  60  60  LEU LEU C . n 
C 1 67  LEU 67  61  61  LEU LEU C . n 
C 1 68  LYS 68  62  62  LYS LYS C . n 
C 1 69  GLN 69  63  63  GLN GLN C . n 
C 1 70  ALA 70  64  64  ALA ALA C . n 
C 1 71  GLY 71  65  65  GLY GLY C . n 
C 1 72  MET 72  66  66  MET MET C . n 
C 1 73  LYS 73  67  67  LYS LYS C . n 
C 1 74  LYS 74  68  68  LYS LYS C . n 
C 1 75  ILE 75  69  69  ILE ILE C . n 
C 1 76  ASN 76  70  70  ASN ASN C . n 
C 1 77  PHE 77  71  71  PHE PHE C . n 
C 1 78  ALA 78  72  72  ALA ALA C . n 
C 1 79  GLY 79  73  73  GLY GLY C . n 
C 1 80  GLY 80  74  74  GLY GLY C . n 
C 1 81  GLU 81  75  75  GLU GLU C . n 
C 1 82  PRO 82  76  76  PRO PRO C . n 
C 1 83  PHE 83  77  77  PHE PHE C . n 
C 1 84  LEU 84  78  78  LEU LEU C . n 
C 1 85  TYR 85  79  79  TYR TYR C . n 
C 1 86  PRO 86  80  80  PRO PRO C . n 
C 1 87  LYS 87  81  81  LYS LYS C . n 
C 1 88  PHE 88  82  82  PHE PHE C . n 
C 1 89  LEU 89  83  83  LEU LEU C . n 
C 1 90  GLY 90  84  84  GLY GLY C . n 
C 1 91  GLU 91  85  85  GLU GLU C . n 
C 1 92  MET 92  86  86  MET MET C . n 
C 1 93  ILE 93  87  87  ILE ILE C . n 
C 1 94  ASP 94  88  88  ASP ASP C . n 
C 1 95  PHE 95  89  89  PHE PHE C . n 
C 1 96  CYS 96  90  90  CYS CYS C . n 
C 1 97  LYS 97  91  91  LYS LYS C . n 
C 1 98  GLU 98  92  92  GLU GLU C . n 
C 1 99  THR 99  93  93  THR THR C . n 
C 1 100 LEU 100 94  94  LEU LEU C . n 
C 1 101 GLN 101 95  95  GLN GLN C . n 
C 1 102 LEU 102 96  96  LEU LEU C . n 
C 1 103 GLU 103 97  97  GLU GLU C . n 
C 1 104 SER 104 98  98  SER SER C . n 
C 1 105 VAL 105 99  99  VAL VAL C . n 
C 1 106 SER 106 100 100 SER SER C . n 
C 1 107 ILE 107 101 101 ILE ILE C . n 
C 1 108 VAL 108 102 102 VAL VAL C . n 
C 1 109 THR 109 103 103 THR THR C . n 
C 1 110 ASN 110 104 104 ASN ASN C . n 
C 1 111 GLY 111 105 105 GLY GLY C . n 
C 1 112 SER 112 106 106 SER SER C . n 
C 1 113 LEU 113 107 107 LEU LEU C . n 
C 1 114 VAL 114 108 108 VAL VAL C . n 
C 1 115 LYS 115 109 109 LYS LYS C . n 
C 1 116 GLU 116 110 110 GLU GLU C . n 
C 1 117 GLN 117 111 111 GLN GLN C . n 
C 1 118 PHE 118 112 112 PHE PHE C . n 
C 1 119 LEU 119 113 113 LEU LEU C . n 
C 1 120 GLN 120 114 114 GLN GLN C . n 
C 1 121 LYS 121 115 115 LYS LYS C . n 
C 1 122 HIS 122 116 116 HIS HIS C . n 
C 1 123 GLY 123 117 117 GLY GLY C . n 
C 1 124 ARG 124 118 118 ARG ARG C . n 
C 1 125 ASN 125 119 119 ASN ASN C . n 
C 1 126 ILE 126 120 120 ILE ILE C . n 
C 1 127 ASP 127 121 121 ASP ASP C . n 
C 1 128 ILE 128 122 122 ILE ILE C . n 
C 1 129 LEU 129 123 123 LEU LEU C . n 
C 1 130 ALA 130 124 124 ALA ALA C . n 
C 1 131 VAL 131 125 125 VAL VAL C . n 
C 1 132 SER 132 126 126 SER SER C . n 
C 1 133 CYS 133 127 127 CYS CYS C . n 
C 1 134 ASP 134 128 128 ASP ASP C . n 
C 1 135 SER 135 129 129 SER SER C . n 
C 1 136 PHE 136 130 130 PHE PHE C . n 
C 1 137 ASN 137 131 131 ASN ASN C . n 
C 1 138 GLU 138 132 132 GLU GLU C . n 
C 1 139 ALA 139 133 133 ALA ALA C . n 
C 1 140 THR 140 134 134 THR THR C . n 
C 1 141 ASN 141 135 135 ASN ASN C . n 
C 1 142 ILE 142 136 136 ILE ILE C . n 
C 1 143 LYS 143 137 137 LYS LYS C . n 
C 1 144 ILE 144 138 138 ILE ILE C . n 
C 1 145 GLY 145 139 139 GLY GLY C . n 
C 1 146 ARG 146 140 140 ARG ARG C . n 
C 1 147 GLY 147 141 141 GLY GLY C . n 
C 1 148 SER 148 142 142 SER SER C . n 
C 1 149 GLY 149 143 143 GLY GLY C . n 
C 1 150 ASP 150 144 144 ASP ASP C . n 
C 1 151 ASN 151 145 145 ASN ASN C . n 
C 1 152 VAL 152 146 146 VAL VAL C . n 
C 1 153 GLN 153 147 147 GLN GLN C . n 
C 1 154 LYS 154 148 148 LYS LYS C . n 
C 1 155 LEU 155 149 149 LEU LEU C . n 
C 1 156 TYR 156 150 150 TYR TYR C . n 
C 1 157 GLU 157 151 151 GLU GLU C . n 
C 1 158 ILE 158 152 152 ILE ILE C . n 
C 1 159 GLY 159 153 153 GLY GLY C . n 
C 1 160 SER 160 154 154 SER SER C . n 
C 1 161 TRP 161 155 155 TRP TRP C . n 
C 1 162 CYS 162 156 156 CYS CYS C . n 
C 1 163 GLN 163 157 157 GLN GLN C . n 
C 1 164 LYS 164 158 158 LYS LYS C . n 
C 1 165 TYR 165 159 159 TYR TYR C . n 
C 1 166 ASP 166 160 160 ASP ASP C . n 
C 1 167 ILE 167 161 161 ILE ILE C . n 
C 1 168 LYS 168 162 162 LYS LYS C . n 
C 1 169 PHE 169 163 163 PHE PHE C . n 
C 1 170 LYS 170 164 164 LYS LYS C . n 
C 1 171 LEU 171 165 165 LEU LEU C . n 
C 1 172 ASN 172 166 166 ASN ASN C . n 
C 1 173 THR 173 167 167 THR THR C . n 
C 1 174 VAL 174 168 168 VAL VAL C . n 
C 1 175 VAL 175 169 169 VAL VAL C . n 
C 1 176 ASN 176 170 170 ASN ASN C . n 
C 1 177 LYS 177 171 171 LYS LYS C . n 
C 1 178 PHE 178 172 172 PHE PHE C . n 
C 1 179 ASN 179 173 173 ASN ASN C . n 
C 1 180 HIS 180 174 174 HIS HIS C . n 
C 1 181 LEU 181 175 175 LEU LEU C . n 
C 1 182 GLU 182 176 176 GLU GLU C . n 
C 1 183 ASP 183 177 177 ASP ASP C . n 
C 1 184 MET 184 178 178 MET MET C . n 
C 1 185 ASN 185 179 179 ASN ASN C . n 
C 1 186 ASP 186 180 180 ASP ASP C . n 
C 1 187 HIS 187 181 181 HIS HIS C . n 
C 1 188 LEU 188 182 182 LEU LEU C . n 
C 1 189 ASN 189 183 183 ASN ASN C . n 
C 1 190 ALA 190 184 184 ALA ALA C . n 
C 1 191 LEU 191 185 185 LEU LEU C . n 
C 1 192 GLN 192 186 186 GLN GLN C . n 
C 1 193 PRO 193 187 187 PRO PRO C . n 
C 1 194 PHE 194 188 188 PHE PHE C . n 
C 1 195 ARG 195 189 189 ARG ARG C . n 
C 1 196 TRP 196 190 190 TRP TRP C . n 
C 1 197 LYS 197 191 191 LYS LYS C . n 
C 1 198 CYS 198 192 192 CYS CYS C . n 
C 1 199 PHE 199 193 193 PHE PHE C . n 
C 1 200 GLN 200 194 194 GLN GLN C . n 
C 1 201 VAL 201 195 195 VAL VAL C . n 
C 1 202 LEU 202 196 196 LEU LEU C . n 
C 1 203 ILE 203 197 197 ILE ILE C . n 
C 1 204 ILE 204 198 198 ILE ILE C . n 
C 1 205 GLU 205 199 199 GLU GLU C . n 
C 1 206 GLY 206 200 200 GLY GLY C . n 
C 1 207 GLU 207 201 201 GLU GLU C . n 
C 1 208 ASN 208 202 202 ASN ASN C . n 
C 1 209 ASP 209 203 203 ASP ASP C . n 
C 1 210 SER 210 204 204 SER SER C . n 
C 1 211 ASP 211 205 205 ASP ASP C . n 
C 1 212 LYS 212 206 206 LYS LYS C . n 
C 1 213 THR 213 207 207 THR THR C . n 
C 1 214 LEU 214 208 208 LEU LEU C . n 
C 1 215 ARG 215 209 209 ARG ARG C . n 
C 1 216 ASN 216 210 210 ASN ASN C . n 
C 1 217 ALA 217 211 211 ALA ALA C . n 
C 1 218 HIS 218 212 212 HIS HIS C . n 
C 1 219 SER 219 213 213 SER SER C . n 
C 1 220 LEU 220 214 214 LEU LEU C . n 
C 1 221 THR 221 215 215 THR THR C . n 
C 1 222 ILE 222 216 216 ILE ILE C . n 
C 1 223 SER 223 217 217 SER SER C . n 
C 1 224 ASP 224 218 218 ASP ASP C . n 
C 1 225 ASP 225 219 219 ASP ASP C . n 
C 1 226 GLU 226 220 220 GLU GLU C . n 
C 1 227 PHE 227 221 221 PHE PHE C . n 
C 1 228 ASP 228 222 222 ASP ASP C . n 
C 1 229 ARG 229 223 223 ARG ARG C . n 
C 1 230 PHE 230 224 224 PHE PHE C . n 
C 1 231 CYS 231 225 225 CYS CYS C . n 
C 1 232 GLU 232 226 226 GLU GLU C . n 
C 1 233 ARG 233 227 227 ARG ARG C . n 
C 1 234 HIS 234 228 228 HIS HIS C . n 
C 1 235 SER 235 229 229 SER SER C . n 
C 1 236 SER 236 230 230 SER SER C . n 
C 1 237 GLN 237 231 231 GLN GLN C . n 
C 1 238 THR 238 232 232 THR THR C . n 
C 1 239 CYS 239 233 233 CYS CYS C . n 
C 1 240 LEU 240 234 234 LEU LEU C . n 
C 1 241 VAL 241 235 235 VAL VAL C . n 
C 1 242 PRO 242 236 236 PRO PRO C . n 
C 1 243 GLU 243 237 237 GLU GLU C . n 
C 1 244 PRO 244 238 238 PRO PRO C . n 
C 1 245 ASN 245 239 239 ASN ASN C . n 
C 1 246 ARG 246 240 240 ARG ARG C . n 
C 1 247 LEU 247 241 241 LEU LEU C . n 
C 1 248 MET 248 242 242 MET MET C . n 
C 1 249 ALA 249 243 243 ALA ALA C . n 
C 1 250 LYS 250 244 244 LYS LYS C . n 
C 1 251 SER 251 245 245 SER SER C . n 
C 1 252 TYR 252 246 246 TYR TYR C . n 
C 1 253 LEU 253 247 247 LEU LEU C . n 
C 1 254 ILE 254 248 248 ILE ILE C . n 
C 1 255 LEU 255 249 249 LEU LEU C . n 
C 1 256 ASP 256 250 250 ASP ASP C . n 
C 1 257 GLU 257 251 251 GLU GLU C . n 
C 1 258 TYR 258 252 252 TYR TYR C . n 
C 1 259 MET 259 253 253 MET MET C . n 
C 1 260 ARG 260 254 254 ARG ARG C . n 
C 1 261 PHE 261 255 255 PHE PHE C . n 
C 1 262 LEU 262 256 256 LEU LEU C . n 
C 1 263 ASN 263 257 257 ASN ASN C . n 
C 1 264 CYS 264 258 258 CYS CYS C . n 
C 1 265 THR 265 259 259 THR THR C . n 
C 1 266 GLY 266 260 260 GLY GLY C . n 
C 1 267 GLY 267 261 261 GLY GLY C . n 
C 1 268 ARG 268 262 262 ARG ARG C . n 
C 1 269 LYS 269 263 263 LYS LYS C . n 
C 1 270 ASP 270 264 264 ASP ASP C . n 
C 1 271 PRO 271 265 265 PRO PRO C . n 
C 1 272 SER 272 266 266 SER SER C . n 
C 1 273 LYS 273 267 267 LYS LYS C . n 
C 1 274 SER 274 268 268 SER SER C . n 
C 1 275 ILE 275 269 269 ILE ILE C . n 
C 1 276 LEU 276 270 270 LEU LEU C . n 
C 1 277 GLU 277 271 271 GLU GLU C . n 
C 1 278 VAL 278 272 272 VAL VAL C . n 
C 1 279 GLY 279 273 273 GLY GLY C . n 
C 1 280 VAL 280 274 274 VAL VAL C . n 
C 1 281 GLN 281 275 275 GLN GLN C . n 
C 1 282 GLN 282 276 276 GLN GLN C . n 
C 1 283 ALA 283 277 277 ALA ALA C . n 
C 1 284 LEU 284 278 278 LEU LEU C . n 
C 1 285 GLN 285 279 279 GLN GLN C . n 
C 1 286 ALA 286 280 280 ALA ALA C . n 
C 1 287 VAL 287 281 281 VAL VAL C . n 
C 1 288 PHE 288 282 282 PHE PHE C . n 
C 1 289 TRP 289 283 283 TRP TRP C . n 
C 1 290 ASP 290 284 284 ASP ASP C . n 
C 1 291 GLU 291 285 285 GLU GLU C . n 
C 1 292 GLU 292 286 286 GLU GLU C . n 
C 1 293 ALA 293 287 287 ALA ALA C . n 
C 1 294 PHE 294 288 288 PHE PHE C . n 
C 1 295 VAL 295 289 289 VAL VAL C . n 
C 1 296 GLU 296 290 290 GLU GLU C . n 
C 1 297 ARG 297 291 291 ARG ARG C . n 
C 1 298 GLY 298 292 292 GLY GLY C . n 
C 1 299 GLY 299 293 293 GLY GLY C . n 
C 1 300 ILE 300 294 294 ILE ILE C . n 
C 1 301 TYR 301 295 295 TYR TYR C . n 
C 1 302 ASP 302 296 296 ASP ASP C . n 
C 1 303 TRP 303 297 297 TRP TRP C . n 
C 1 304 ASN 304 298 298 ASN ASN C . n 
C 1 305 LYS 305 299 299 LYS LYS C . n 
C 1 306 SER 306 300 300 SER SER C . n 
C 1 307 SER 307 301 ?   ?   ?   C . n 
C 1 308 CYS 308 302 ?   ?   ?   C . n 
C 1 309 SER 309 303 ?   ?   ?   C . n 
C 1 310 SER 310 304 ?   ?   ?   C . n 
C 1 311 ASP 311 305 ?   ?   ?   C . n 
C 1 312 SER 312 306 ?   ?   ?   C . n 
C 1 313 LYS 313 307 ?   ?   ?   C . n 
C 1 314 ASP 314 308 ?   ?   ?   C . n 
C 1 315 LEU 315 309 ?   ?   ?   C . n 
C 1 316 GLU 316 310 ?   ?   ?   C . n 
C 1 317 TRP 317 311 ?   ?   ?   C . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CTP ? ? CTP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SAM ? ? SAM ? ? 'SUBJECT OF INVESTIGATION' ? 
3 SF4 ? ? SF4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SF4 1   401 401 SF4 SF4 A . 
E 3 SAM 1   402 402 SAM SAM A . 
F 4 CTP 1   403 403 CTP CTP A . 
G 5 EPE 1   404 404 EPE EPE A . 
H 5 EPE 1   405 405 EPE EPE A . 
I 6 MG  1   406 1   MG  MG  A . 
J 6 MG  1   407 3   MG  MG  A . 
K 2 SF4 1   401 401 SF4 SF4 B . 
L 3 SAM 1   402 402 SAM SAM B . 
M 4 CTP 1   403 403 CTP CTP B . 
N 2 SF4 1   401 401 SF4 SF4 C . 
O 3 SAM 1   402 402 SAM SAM C . 
P 4 CTP 1   403 403 CTP CTP C . 
Q 7 GOL 1   404 404 GOL GOL C . 
R 6 MG  1   405 2   MG  MG  C . 
S 8 HOH 1   501 439 HOH HOH A . 
S 8 HOH 2   502 761 HOH HOH A . 
S 8 HOH 3   503 90  HOH HOH A . 
S 8 HOH 4   504 798 HOH HOH A . 
S 8 HOH 5   505 289 HOH HOH A . 
S 8 HOH 6   506 109 HOH HOH A . 
S 8 HOH 7   507 369 HOH HOH A . 
S 8 HOH 8   508 396 HOH HOH A . 
S 8 HOH 9   509 354 HOH HOH A . 
S 8 HOH 10  510 486 HOH HOH A . 
S 8 HOH 11  511 422 HOH HOH A . 
S 8 HOH 12  512 178 HOH HOH A . 
S 8 HOH 13  513 585 HOH HOH A . 
S 8 HOH 14  514 508 HOH HOH A . 
S 8 HOH 15  515 271 HOH HOH A . 
S 8 HOH 16  516 435 HOH HOH A . 
S 8 HOH 17  517 531 HOH HOH A . 
S 8 HOH 18  518 292 HOH HOH A . 
S 8 HOH 19  519 338 HOH HOH A . 
S 8 HOH 20  520 609 HOH HOH A . 
S 8 HOH 21  521 86  HOH HOH A . 
S 8 HOH 22  522 412 HOH HOH A . 
S 8 HOH 23  523 312 HOH HOH A . 
S 8 HOH 24  524 196 HOH HOH A . 
S 8 HOH 25  525 395 HOH HOH A . 
S 8 HOH 26  526 555 HOH HOH A . 
S 8 HOH 27  527 664 HOH HOH A . 
S 8 HOH 28  528 11  HOH HOH A . 
S 8 HOH 29  529 74  HOH HOH A . 
S 8 HOH 30  530 203 HOH HOH A . 
S 8 HOH 31  531 323 HOH HOH A . 
S 8 HOH 32  532 503 HOH HOH A . 
S 8 HOH 33  533 128 HOH HOH A . 
S 8 HOH 34  534 60  HOH HOH A . 
S 8 HOH 35  535 390 HOH HOH A . 
S 8 HOH 36  536 401 HOH HOH A . 
S 8 HOH 37  537 83  HOH HOH A . 
S 8 HOH 38  538 113 HOH HOH A . 
S 8 HOH 39  539 466 HOH HOH A . 
S 8 HOH 40  540 322 HOH HOH A . 
S 8 HOH 41  541 44  HOH HOH A . 
S 8 HOH 42  542 221 HOH HOH A . 
S 8 HOH 43  543 9   HOH HOH A . 
S 8 HOH 44  544 23  HOH HOH A . 
S 8 HOH 45  545 268 HOH HOH A . 
S 8 HOH 46  546 2   HOH HOH A . 
S 8 HOH 47  547 210 HOH HOH A . 
S 8 HOH 48  548 760 HOH HOH A . 
S 8 HOH 49  549 27  HOH HOH A . 
S 8 HOH 50  550 350 HOH HOH A . 
S 8 HOH 51  551 216 HOH HOH A . 
S 8 HOH 52  552 650 HOH HOH A . 
S 8 HOH 53  553 273 HOH HOH A . 
S 8 HOH 54  554 389 HOH HOH A . 
S 8 HOH 55  555 13  HOH HOH A . 
S 8 HOH 56  556 270 HOH HOH A . 
S 8 HOH 57  557 141 HOH HOH A . 
S 8 HOH 58  558 630 HOH HOH A . 
S 8 HOH 59  559 741 HOH HOH A . 
S 8 HOH 60  560 174 HOH HOH A . 
S 8 HOH 61  561 406 HOH HOH A . 
S 8 HOH 62  562 296 HOH HOH A . 
S 8 HOH 63  563 417 HOH HOH A . 
S 8 HOH 64  564 440 HOH HOH A . 
S 8 HOH 65  565 104 HOH HOH A . 
S 8 HOH 66  566 218 HOH HOH A . 
S 8 HOH 67  567 360 HOH HOH A . 
S 8 HOH 68  568 100 HOH HOH A . 
S 8 HOH 69  569 303 HOH HOH A . 
S 8 HOH 70  570 378 HOH HOH A . 
S 8 HOH 71  571 105 HOH HOH A . 
S 8 HOH 72  572 694 HOH HOH A . 
S 8 HOH 73  573 306 HOH HOH A . 
S 8 HOH 74  574 497 HOH HOH A . 
S 8 HOH 75  575 732 HOH HOH A . 
S 8 HOH 76  576 500 HOH HOH A . 
S 8 HOH 77  577 644 HOH HOH A . 
S 8 HOH 78  578 16  HOH HOH A . 
S 8 HOH 79  579 43  HOH HOH A . 
S 8 HOH 80  580 55  HOH HOH A . 
S 8 HOH 81  581 397 HOH HOH A . 
S 8 HOH 82  582 245 HOH HOH A . 
S 8 HOH 83  583 68  HOH HOH A . 
S 8 HOH 84  584 725 HOH HOH A . 
S 8 HOH 85  585 34  HOH HOH A . 
S 8 HOH 86  586 239 HOH HOH A . 
S 8 HOH 87  587 637 HOH HOH A . 
S 8 HOH 88  588 31  HOH HOH A . 
S 8 HOH 89  589 54  HOH HOH A . 
S 8 HOH 90  590 771 HOH HOH A . 
S 8 HOH 91  591 483 HOH HOH A . 
S 8 HOH 92  592 35  HOH HOH A . 
S 8 HOH 93  593 277 HOH HOH A . 
S 8 HOH 94  594 137 HOH HOH A . 
S 8 HOH 95  595 119 HOH HOH A . 
S 8 HOH 96  596 347 HOH HOH A . 
S 8 HOH 97  597 489 HOH HOH A . 
S 8 HOH 98  598 563 HOH HOH A . 
S 8 HOH 99  599 529 HOH HOH A . 
S 8 HOH 100 600 20  HOH HOH A . 
S 8 HOH 101 601 249 HOH HOH A . 
S 8 HOH 102 602 538 HOH HOH A . 
S 8 HOH 103 603 280 HOH HOH A . 
S 8 HOH 104 604 169 HOH HOH A . 
S 8 HOH 105 605 40  HOH HOH A . 
S 8 HOH 106 606 467 HOH HOH A . 
S 8 HOH 107 607 305 HOH HOH A . 
S 8 HOH 108 608 208 HOH HOH A . 
S 8 HOH 109 609 172 HOH HOH A . 
S 8 HOH 110 610 253 HOH HOH A . 
S 8 HOH 111 611 266 HOH HOH A . 
S 8 HOH 112 612 364 HOH HOH A . 
S 8 HOH 113 613 363 HOH HOH A . 
S 8 HOH 114 614 116 HOH HOH A . 
S 8 HOH 115 615 236 HOH HOH A . 
S 8 HOH 116 616 436 HOH HOH A . 
S 8 HOH 117 617 130 HOH HOH A . 
S 8 HOH 118 618 368 HOH HOH A . 
S 8 HOH 119 619 67  HOH HOH A . 
S 8 HOH 120 620 219 HOH HOH A . 
S 8 HOH 121 621 571 HOH HOH A . 
S 8 HOH 122 622 336 HOH HOH A . 
S 8 HOH 123 623 17  HOH HOH A . 
S 8 HOH 124 624 789 HOH HOH A . 
S 8 HOH 125 625 788 HOH HOH A . 
S 8 HOH 126 626 510 HOH HOH A . 
S 8 HOH 127 627 518 HOH HOH A . 
S 8 HOH 128 628 320 HOH HOH A . 
S 8 HOH 129 629 220 HOH HOH A . 
S 8 HOH 130 630 648 HOH HOH A . 
S 8 HOH 131 631 79  HOH HOH A . 
S 8 HOH 132 632 152 HOH HOH A . 
S 8 HOH 133 633 442 HOH HOH A . 
S 8 HOH 134 634 187 HOH HOH A . 
S 8 HOH 135 635 660 HOH HOH A . 
S 8 HOH 136 636 672 HOH HOH A . 
S 8 HOH 137 637 155 HOH HOH A . 
S 8 HOH 138 638 415 HOH HOH A . 
S 8 HOH 139 639 416 HOH HOH A . 
S 8 HOH 140 640 89  HOH HOH A . 
S 8 HOH 141 641 115 HOH HOH A . 
S 8 HOH 142 642 200 HOH HOH A . 
S 8 HOH 143 643 357 HOH HOH A . 
S 8 HOH 144 644 562 HOH HOH A . 
S 8 HOH 145 645 490 HOH HOH A . 
S 8 HOH 146 646 745 HOH HOH A . 
S 8 HOH 147 647 504 HOH HOH A . 
S 8 HOH 148 648 537 HOH HOH A . 
S 8 HOH 149 649 215 HOH HOH A . 
S 8 HOH 150 650 107 HOH HOH A . 
S 8 HOH 151 651 108 HOH HOH A . 
S 8 HOH 152 652 112 HOH HOH A . 
S 8 HOH 153 653 118 HOH HOH A . 
S 8 HOH 154 654 387 HOH HOH A . 
S 8 HOH 155 655 393 HOH HOH A . 
S 8 HOH 156 656 612 HOH HOH A . 
S 8 HOH 157 657 286 HOH HOH A . 
S 8 HOH 158 658 403 HOH HOH A . 
S 8 HOH 159 659 719 HOH HOH A . 
S 8 HOH 160 660 744 HOH HOH A . 
S 8 HOH 161 661 621 HOH HOH A . 
S 8 HOH 162 662 477 HOH HOH A . 
S 8 HOH 163 663 156 HOH HOH A . 
S 8 HOH 164 664 325 HOH HOH A . 
S 8 HOH 165 665 696 HOH HOH A . 
S 8 HOH 166 666 181 HOH HOH A . 
S 8 HOH 167 667 515 HOH HOH A . 
S 8 HOH 168 668 101 HOH HOH A . 
S 8 HOH 169 669 226 HOH HOH A . 
S 8 HOH 170 670 373 HOH HOH A . 
S 8 HOH 171 671 199 HOH HOH A . 
S 8 HOH 172 672 321 HOH HOH A . 
S 8 HOH 173 673 670 HOH HOH A . 
S 8 HOH 174 674 223 HOH HOH A . 
S 8 HOH 175 675 791 HOH HOH A . 
S 8 HOH 176 676 158 HOH HOH A . 
S 8 HOH 177 677 587 HOH HOH A . 
S 8 HOH 178 678 260 HOH HOH A . 
S 8 HOH 179 679 767 HOH HOH A . 
S 8 HOH 180 680 263 HOH HOH A . 
S 8 HOH 181 681 624 HOH HOH A . 
S 8 HOH 182 682 183 HOH HOH A . 
S 8 HOH 183 683 498 HOH HOH A . 
S 8 HOH 184 684 640 HOH HOH A . 
S 8 HOH 185 685 797 HOH HOH A . 
S 8 HOH 186 686 711 HOH HOH A . 
S 8 HOH 187 687 688 HOH HOH A . 
S 8 HOH 188 688 550 HOH HOH A . 
S 8 HOH 189 689 457 HOH HOH A . 
S 8 HOH 190 690 790 HOH HOH A . 
S 8 HOH 191 691 241 HOH HOH A . 
S 8 HOH 192 692 411 HOH HOH A . 
S 8 HOH 193 693 469 HOH HOH A . 
S 8 HOH 194 694 400 HOH HOH A . 
S 8 HOH 195 695 552 HOH HOH A . 
S 8 HOH 196 696 687 HOH HOH A . 
S 8 HOH 197 697 589 HOH HOH A . 
S 8 HOH 198 698 317 HOH HOH A . 
S 8 HOH 199 699 75  HOH HOH A . 
S 8 HOH 200 700 668 HOH HOH A . 
S 8 HOH 201 701 111 HOH HOH A . 
S 8 HOH 202 702 480 HOH HOH A . 
S 8 HOH 203 703 450 HOH HOH A . 
S 8 HOH 204 704 690 HOH HOH A . 
S 8 HOH 205 705 528 HOH HOH A . 
S 8 HOH 206 706 638 HOH HOH A . 
S 8 HOH 207 707 530 HOH HOH A . 
S 8 HOH 208 708 516 HOH HOH A . 
S 8 HOH 209 709 722 HOH HOH A . 
S 8 HOH 210 710 642 HOH HOH A . 
S 8 HOH 211 711 738 HOH HOH A . 
S 8 HOH 212 712 752 HOH HOH A . 
S 8 HOH 213 713 730 HOH HOH A . 
S 8 HOH 214 714 365 HOH HOH A . 
S 8 HOH 215 715 484 HOH HOH A . 
S 8 HOH 216 716 22  HOH HOH A . 
S 8 HOH 217 717 616 HOH HOH A . 
S 8 HOH 218 718 520 HOH HOH A . 
S 8 HOH 219 719 209 HOH HOH A . 
S 8 HOH 220 720 126 HOH HOH A . 
S 8 HOH 221 721 556 HOH HOH A . 
S 8 HOH 222 722 541 HOH HOH A . 
S 8 HOH 223 723 458 HOH HOH A . 
S 8 HOH 224 724 580 HOH HOH A . 
S 8 HOH 225 725 766 HOH HOH A . 
S 8 HOH 226 726 478 HOH HOH A . 
S 8 HOH 227 727 340 HOH HOH A . 
S 8 HOH 228 728 639 HOH HOH A . 
S 8 HOH 229 729 685 HOH HOH A . 
S 8 HOH 230 730 474 HOH HOH A . 
S 8 HOH 231 731 246 HOH HOH A . 
S 8 HOH 232 732 512 HOH HOH A . 
S 8 HOH 233 733 479 HOH HOH A . 
S 8 HOH 234 734 600 HOH HOH A . 
S 8 HOH 235 735 546 HOH HOH A . 
S 8 HOH 236 736 718 HOH HOH A . 
S 8 HOH 237 737 284 HOH HOH A . 
S 8 HOH 238 738 777 HOH HOH A . 
S 8 HOH 239 739 724 HOH HOH A . 
S 8 HOH 240 740 493 HOH HOH A . 
S 8 HOH 241 741 654 HOH HOH A . 
T 8 HOH 1   501 124 HOH HOH B . 
T 8 HOH 2   502 728 HOH HOH B . 
T 8 HOH 3   503 65  HOH HOH B . 
T 8 HOH 4   504 362 HOH HOH B . 
T 8 HOH 5   505 285 HOH HOH B . 
T 8 HOH 6   506 248 HOH HOH B . 
T 8 HOH 7   507 213 HOH HOH B . 
T 8 HOH 8   508 759 HOH HOH B . 
T 8 HOH 9   509 625 HOH HOH B . 
T 8 HOH 10  510 345 HOH HOH B . 
T 8 HOH 11  511 243 HOH HOH B . 
T 8 HOH 12  512 97  HOH HOH B . 
T 8 HOH 13  513 511 HOH HOH B . 
T 8 HOH 14  514 620 HOH HOH B . 
T 8 HOH 15  515 194 HOH HOH B . 
T 8 HOH 16  516 247 HOH HOH B . 
T 8 HOH 17  517 37  HOH HOH B . 
T 8 HOH 18  518 449 HOH HOH B . 
T 8 HOH 19  519 327 HOH HOH B . 
T 8 HOH 20  520 235 HOH HOH B . 
T 8 HOH 21  521 472 HOH HOH B . 
T 8 HOH 22  522 76  HOH HOH B . 
T 8 HOH 23  523 184 HOH HOH B . 
T 8 HOH 24  524 14  HOH HOH B . 
T 8 HOH 25  525 434 HOH HOH B . 
T 8 HOH 26  526 351 HOH HOH B . 
T 8 HOH 27  527 700 HOH HOH B . 
T 8 HOH 28  528 405 HOH HOH B . 
T 8 HOH 29  529 73  HOH HOH B . 
T 8 HOH 30  530 5   HOH HOH B . 
T 8 HOH 31  531 721 HOH HOH B . 
T 8 HOH 32  532 385 HOH HOH B . 
T 8 HOH 33  533 255 HOH HOH B . 
T 8 HOH 34  534 211 HOH HOH B . 
T 8 HOH 35  535 753 HOH HOH B . 
T 8 HOH 36  536 293 HOH HOH B . 
T 8 HOH 37  537 544 HOH HOH B . 
T 8 HOH 38  538 316 HOH HOH B . 
T 8 HOH 39  539 427 HOH HOH B . 
T 8 HOH 40  540 180 HOH HOH B . 
T 8 HOH 41  541 576 HOH HOH B . 
T 8 HOH 42  542 662 HOH HOH B . 
T 8 HOH 43  543 794 HOH HOH B . 
T 8 HOH 44  544 302 HOH HOH B . 
T 8 HOH 45  545 507 HOH HOH B . 
T 8 HOH 46  546 676 HOH HOH B . 
T 8 HOH 47  547 12  HOH HOH B . 
T 8 HOH 48  548 591 HOH HOH B . 
T 8 HOH 49  549 604 HOH HOH B . 
T 8 HOH 50  550 38  HOH HOH B . 
T 8 HOH 51  551 46  HOH HOH B . 
T 8 HOH 52  552 551 HOH HOH B . 
T 8 HOH 53  553 579 HOH HOH B . 
T 8 HOH 54  554 50  HOH HOH B . 
T 8 HOH 55  555 212 HOH HOH B . 
T 8 HOH 56  556 132 HOH HOH B . 
T 8 HOH 57  557 110 HOH HOH B . 
T 8 HOH 58  558 288 HOH HOH B . 
T 8 HOH 59  559 313 HOH HOH B . 
T 8 HOH 60  560 134 HOH HOH B . 
T 8 HOH 61  561 48  HOH HOH B . 
T 8 HOH 62  562 383 HOH HOH B . 
T 8 HOH 63  563 796 HOH HOH B . 
T 8 HOH 64  564 62  HOH HOH B . 
T 8 HOH 65  565 98  HOH HOH B . 
T 8 HOH 66  566 188 HOH HOH B . 
T 8 HOH 67  567 71  HOH HOH B . 
T 8 HOH 68  568 114 HOH HOH B . 
T 8 HOH 69  569 28  HOH HOH B . 
T 8 HOH 70  570 53  HOH HOH B . 
T 8 HOH 71  571 164 HOH HOH B . 
T 8 HOH 72  572 240 HOH HOH B . 
T 8 HOH 73  573 80  HOH HOH B . 
T 8 HOH 74  574 3   HOH HOH B . 
T 8 HOH 75  575 333 HOH HOH B . 
T 8 HOH 76  576 420 HOH HOH B . 
T 8 HOH 77  577 250 HOH HOH B . 
T 8 HOH 78  578 186 HOH HOH B . 
T 8 HOH 79  579 297 HOH HOH B . 
T 8 HOH 80  580 444 HOH HOH B . 
T 8 HOH 81  581 173 HOH HOH B . 
T 8 HOH 82  582 659 HOH HOH B . 
T 8 HOH 83  583 227 HOH HOH B . 
T 8 HOH 84  584 153 HOH HOH B . 
T 8 HOH 85  585 502 HOH HOH B . 
T 8 HOH 86  586 123 HOH HOH B . 
T 8 HOH 87  587 348 HOH HOH B . 
T 8 HOH 88  588 161 HOH HOH B . 
T 8 HOH 89  589 743 HOH HOH B . 
T 8 HOH 90  590 143 HOH HOH B . 
T 8 HOH 91  591 147 HOH HOH B . 
T 8 HOH 92  592 689 HOH HOH B . 
T 8 HOH 93  593 583 HOH HOH B . 
T 8 HOH 94  594 201 HOH HOH B . 
T 8 HOH 95  595 18  HOH HOH B . 
T 8 HOH 96  596 162 HOH HOH B . 
T 8 HOH 97  597 57  HOH HOH B . 
T 8 HOH 98  598 254 HOH HOH B . 
T 8 HOH 99  599 33  HOH HOH B . 
T 8 HOH 100 600 346 HOH HOH B . 
T 8 HOH 101 601 106 HOH HOH B . 
T 8 HOH 102 602 372 HOH HOH B . 
T 8 HOH 103 603 233 HOH HOH B . 
T 8 HOH 104 604 179 HOH HOH B . 
T 8 HOH 105 605 30  HOH HOH B . 
T 8 HOH 106 606 281 HOH HOH B . 
T 8 HOH 107 607 136 HOH HOH B . 
T 8 HOH 108 608 596 HOH HOH B . 
T 8 HOH 109 609 524 HOH HOH B . 
T 8 HOH 110 610 145 HOH HOH B . 
T 8 HOH 111 611 256 HOH HOH B . 
T 8 HOH 112 612 663 HOH HOH B . 
T 8 HOH 113 613 93  HOH HOH B . 
T 8 HOH 114 614 308 HOH HOH B . 
T 8 HOH 115 615 10  HOH HOH B . 
T 8 HOH 116 616 394 HOH HOH B . 
T 8 HOH 117 617 593 HOH HOH B . 
T 8 HOH 118 618 573 HOH HOH B . 
T 8 HOH 119 619 177 HOH HOH B . 
T 8 HOH 120 620 232 HOH HOH B . 
T 8 HOH 121 621 335 HOH HOH B . 
T 8 HOH 122 622 29  HOH HOH B . 
T 8 HOH 123 623 41  HOH HOH B . 
T 8 HOH 124 624 61  HOH HOH B . 
T 8 HOH 125 625 441 HOH HOH B . 
T 8 HOH 126 626 167 HOH HOH B . 
T 8 HOH 127 627 51  HOH HOH B . 
T 8 HOH 128 628 135 HOH HOH B . 
T 8 HOH 129 629 231 HOH HOH B . 
T 8 HOH 130 630 343 HOH HOH B . 
T 8 HOH 131 631 142 HOH HOH B . 
T 8 HOH 132 632 356 HOH HOH B . 
T 8 HOH 133 633 384 HOH HOH B . 
T 8 HOH 134 634 234 HOH HOH B . 
T 8 HOH 135 635 429 HOH HOH B . 
T 8 HOH 136 636 749 HOH HOH B . 
T 8 HOH 137 637 460 HOH HOH B . 
T 8 HOH 138 638 623 HOH HOH B . 
T 8 HOH 139 639 103 HOH HOH B . 
T 8 HOH 140 640 265 HOH HOH B . 
T 8 HOH 141 641 386 HOH HOH B . 
T 8 HOH 142 642 176 HOH HOH B . 
T 8 HOH 143 643 146 HOH HOH B . 
T 8 HOH 144 644 414 HOH HOH B . 
T 8 HOH 145 645 291 HOH HOH B . 
T 8 HOH 146 646 459 HOH HOH B . 
T 8 HOH 147 647 377 HOH HOH B . 
T 8 HOH 148 648 464 HOH HOH B . 
T 8 HOH 149 649 499 HOH HOH B . 
T 8 HOH 150 650 204 HOH HOH B . 
T 8 HOH 151 651 168 HOH HOH B . 
T 8 HOH 152 652 391 HOH HOH B . 
T 8 HOH 153 653 117 HOH HOH B . 
T 8 HOH 154 654 565 HOH HOH B . 
T 8 HOH 155 655 380 HOH HOH B . 
T 8 HOH 156 656 334 HOH HOH B . 
T 8 HOH 157 657 501 HOH HOH B . 
T 8 HOH 158 658 47  HOH HOH B . 
T 8 HOH 159 659 632 HOH HOH B . 
T 8 HOH 160 660 59  HOH HOH B . 
T 8 HOH 161 661 433 HOH HOH B . 
T 8 HOH 162 662 276 HOH HOH B . 
T 8 HOH 163 663 535 HOH HOH B . 
T 8 HOH 164 664 778 HOH HOH B . 
T 8 HOH 165 665 274 HOH HOH B . 
T 8 HOH 166 666 52  HOH HOH B . 
T 8 HOH 167 667 229 HOH HOH B . 
T 8 HOH 168 668 594 HOH HOH B . 
T 8 HOH 169 669 328 HOH HOH B . 
T 8 HOH 170 670 704 HOH HOH B . 
T 8 HOH 171 671 355 HOH HOH B . 
T 8 HOH 172 672 379 HOH HOH B . 
T 8 HOH 173 673 407 HOH HOH B . 
T 8 HOH 174 674 121 HOH HOH B . 
T 8 HOH 175 675 425 HOH HOH B . 
T 8 HOH 176 676 617 HOH HOH B . 
T 8 HOH 177 677 144 HOH HOH B . 
T 8 HOH 178 678 613 HOH HOH B . 
T 8 HOH 179 679 755 HOH HOH B . 
T 8 HOH 180 680 643 HOH HOH B . 
T 8 HOH 181 681 339 HOH HOH B . 
T 8 HOH 182 682 102 HOH HOH B . 
T 8 HOH 183 683 404 HOH HOH B . 
T 8 HOH 184 684 258 HOH HOH B . 
T 8 HOH 185 685 66  HOH HOH B . 
T 8 HOH 186 686 278 HOH HOH B . 
T 8 HOH 187 687 496 HOH HOH B . 
T 8 HOH 188 688 230 HOH HOH B . 
T 8 HOH 189 689 376 HOH HOH B . 
T 8 HOH 190 690 523 HOH HOH B . 
T 8 HOH 191 691 267 HOH HOH B . 
T 8 HOH 192 692 782 HOH HOH B . 
T 8 HOH 193 693 197 HOH HOH B . 
T 8 HOH 194 694 793 HOH HOH B . 
T 8 HOH 195 695 468 HOH HOH B . 
T 8 HOH 196 696 304 HOH HOH B . 
T 8 HOH 197 697 716 HOH HOH B . 
T 8 HOH 198 698 481 HOH HOH B . 
T 8 HOH 199 699 581 HOH HOH B . 
T 8 HOH 200 700 750 HOH HOH B . 
T 8 HOH 201 701 611 HOH HOH B . 
T 8 HOH 202 702 431 HOH HOH B . 
T 8 HOH 203 703 133 HOH HOH B . 
T 8 HOH 204 704 454 HOH HOH B . 
T 8 HOH 205 705 509 HOH HOH B . 
T 8 HOH 206 706 527 HOH HOH B . 
T 8 HOH 207 707 614 HOH HOH B . 
T 8 HOH 208 708 491 HOH HOH B . 
T 8 HOH 209 709 603 HOH HOH B . 
T 8 HOH 210 710 318 HOH HOH B . 
T 8 HOH 211 711 572 HOH HOH B . 
T 8 HOH 212 712 310 HOH HOH B . 
T 8 HOH 213 713 160 HOH HOH B . 
T 8 HOH 214 714 692 HOH HOH B . 
T 8 HOH 215 715 138 HOH HOH B . 
T 8 HOH 216 716 575 HOH HOH B . 
T 8 HOH 217 717 681 HOH HOH B . 
T 8 HOH 218 718 785 HOH HOH B . 
T 8 HOH 219 719 58  HOH HOH B . 
T 8 HOH 220 720 682 HOH HOH B . 
T 8 HOH 221 721 569 HOH HOH B . 
T 8 HOH 222 722 657 HOH HOH B . 
T 8 HOH 223 723 554 HOH HOH B . 
T 8 HOH 224 724 666 HOH HOH B . 
T 8 HOH 225 725 597 HOH HOH B . 
T 8 HOH 226 726 419 HOH HOH B . 
T 8 HOH 227 727 568 HOH HOH B . 
T 8 HOH 228 728 577 HOH HOH B . 
T 8 HOH 229 729 424 HOH HOH B . 
T 8 HOH 230 730 228 HOH HOH B . 
T 8 HOH 231 731 533 HOH HOH B . 
T 8 HOH 232 732 703 HOH HOH B . 
T 8 HOH 233 733 461 HOH HOH B . 
T 8 HOH 234 734 534 HOH HOH B . 
T 8 HOH 235 735 720 HOH HOH B . 
T 8 HOH 236 736 712 HOH HOH B . 
T 8 HOH 237 737 299 HOH HOH B . 
T 8 HOH 238 738 275 HOH HOH B . 
T 8 HOH 239 739 656 HOH HOH B . 
T 8 HOH 240 740 560 HOH HOH B . 
T 8 HOH 241 741 709 HOH HOH B . 
T 8 HOH 242 742 207 HOH HOH B . 
T 8 HOH 243 743 768 HOH HOH B . 
T 8 HOH 244 744 170 HOH HOH B . 
T 8 HOH 245 745 470 HOH HOH B . 
T 8 HOH 246 746 588 HOH HOH B . 
T 8 HOH 247 747 582 HOH HOH B . 
T 8 HOH 248 748 628 HOH HOH B . 
T 8 HOH 249 749 298 HOH HOH B . 
T 8 HOH 250 750 423 HOH HOH B . 
T 8 HOH 251 751 780 HOH HOH B . 
T 8 HOH 252 752 684 HOH HOH B . 
U 8 HOH 1   501 532 HOH HOH C . 
U 8 HOH 2   502 543 HOH HOH C . 
U 8 HOH 3   503 140 HOH HOH C . 
U 8 HOH 4   504 506 HOH HOH C . 
U 8 HOH 5   505 87  HOH HOH C . 
U 8 HOH 6   506 193 HOH HOH C . 
U 8 HOH 7   507 522 HOH HOH C . 
U 8 HOH 8   508 283 HOH HOH C . 
U 8 HOH 9   509 651 HOH HOH C . 
U 8 HOH 10  510 269 HOH HOH C . 
U 8 HOH 11  511 680 HOH HOH C . 
U 8 HOH 12  512 353 HOH HOH C . 
U 8 HOH 13  513 157 HOH HOH C . 
U 8 HOH 14  514 608 HOH HOH C . 
U 8 HOH 15  515 163 HOH HOH C . 
U 8 HOH 16  516 131 HOH HOH C . 
U 8 HOH 17  517 324 HOH HOH C . 
U 8 HOH 18  518 191 HOH HOH C . 
U 8 HOH 19  519 566 HOH HOH C . 
U 8 HOH 20  520 264 HOH HOH C . 
U 8 HOH 21  521 408 HOH HOH C . 
U 8 HOH 22  522 32  HOH HOH C . 
U 8 HOH 23  523 545 HOH HOH C . 
U 8 HOH 24  524 122 HOH HOH C . 
U 8 HOH 25  525 242 HOH HOH C . 
U 8 HOH 26  526 540 HOH HOH C . 
U 8 HOH 27  527 149 HOH HOH C . 
U 8 HOH 28  528 514 HOH HOH C . 
U 8 HOH 29  529 438 HOH HOH C . 
U 8 HOH 30  530 224 HOH HOH C . 
U 8 HOH 31  531 6   HOH HOH C . 
U 8 HOH 32  532 81  HOH HOH C . 
U 8 HOH 33  533 521 HOH HOH C . 
U 8 HOH 34  534 251 HOH HOH C . 
U 8 HOH 35  535 214 HOH HOH C . 
U 8 HOH 36  536 349 HOH HOH C . 
U 8 HOH 37  537 476 HOH HOH C . 
U 8 HOH 38  538 463 HOH HOH C . 
U 8 HOH 39  539 548 HOH HOH C . 
U 8 HOH 40  540 26  HOH HOH C . 
U 8 HOH 41  541 361 HOH HOH C . 
U 8 HOH 42  542 78  HOH HOH C . 
U 8 HOH 43  543 192 HOH HOH C . 
U 8 HOH 44  544 202 HOH HOH C . 
U 8 HOH 45  545 39  HOH HOH C . 
U 8 HOH 46  546 63  HOH HOH C . 
U 8 HOH 47  547 723 HOH HOH C . 
U 8 HOH 48  548 367 HOH HOH C . 
U 8 HOH 49  549 8   HOH HOH C . 
U 8 HOH 50  550 4   HOH HOH C . 
U 8 HOH 51  551 139 HOH HOH C . 
U 8 HOH 52  552 25  HOH HOH C . 
U 8 HOH 53  553 91  HOH HOH C . 
U 8 HOH 54  554 331 HOH HOH C . 
U 8 HOH 55  555 206 HOH HOH C . 
U 8 HOH 56  556 557 HOH HOH C . 
U 8 HOH 57  557 488 HOH HOH C . 
U 8 HOH 58  558 315 HOH HOH C . 
U 8 HOH 59  559 601 HOH HOH C . 
U 8 HOH 60  560 570 HOH HOH C . 
U 8 HOH 61  561 453 HOH HOH C . 
U 8 HOH 62  562 7   HOH HOH C . 
U 8 HOH 63  563 45  HOH HOH C . 
U 8 HOH 64  564 634 HOH HOH C . 
U 8 HOH 65  565 418 HOH HOH C . 
U 8 HOH 66  566 473 HOH HOH C . 
U 8 HOH 67  567 189 HOH HOH C . 
U 8 HOH 68  568 326 HOH HOH C . 
U 8 HOH 69  569 69  HOH HOH C . 
U 8 HOH 70  570 148 HOH HOH C . 
U 8 HOH 71  571 392 HOH HOH C . 
U 8 HOH 72  572 382 HOH HOH C . 
U 8 HOH 73  573 96  HOH HOH C . 
U 8 HOH 74  574 300 HOH HOH C . 
U 8 HOH 75  575 475 HOH HOH C . 
U 8 HOH 76  576 82  HOH HOH C . 
U 8 HOH 77  577 129 HOH HOH C . 
U 8 HOH 78  578 652 HOH HOH C . 
U 8 HOH 79  579 237 HOH HOH C . 
U 8 HOH 80  580 381 HOH HOH C . 
U 8 HOH 81  581 185 HOH HOH C . 
U 8 HOH 82  582 150 HOH HOH C . 
U 8 HOH 83  583 222 HOH HOH C . 
U 8 HOH 84  584 402 HOH HOH C . 
U 8 HOH 85  585 252 HOH HOH C . 
U 8 HOH 86  586 727 HOH HOH C . 
U 8 HOH 87  587 301 HOH HOH C . 
U 8 HOH 88  588 159 HOH HOH C . 
U 8 HOH 89  589 375 HOH HOH C . 
U 8 HOH 90  590 182 HOH HOH C . 
U 8 HOH 91  591 629 HOH HOH C . 
U 8 HOH 92  592 494 HOH HOH C . 
U 8 HOH 93  593 366 HOH HOH C . 
U 8 HOH 94  594 15  HOH HOH C . 
U 8 HOH 95  595 244 HOH HOH C . 
U 8 HOH 96  596 217 HOH HOH C . 
U 8 HOH 97  597 190 HOH HOH C . 
U 8 HOH 98  598 92  HOH HOH C . 
U 8 HOH 99  599 36  HOH HOH C . 
U 8 HOH 100 600 319 HOH HOH C . 
U 8 HOH 101 601 344 HOH HOH C . 
U 8 HOH 102 602 447 HOH HOH C . 
U 8 HOH 103 603 19  HOH HOH C . 
U 8 HOH 104 604 699 HOH HOH C . 
U 8 HOH 105 605 165 HOH HOH C . 
U 8 HOH 106 606 698 HOH HOH C . 
U 8 HOH 107 607 733 HOH HOH C . 
U 8 HOH 108 608 329 HOH HOH C . 
U 8 HOH 109 609 259 HOH HOH C . 
U 8 HOH 110 610 24  HOH HOH C . 
U 8 HOH 111 611 94  HOH HOH C . 
U 8 HOH 112 612 337 HOH HOH C . 
U 8 HOH 113 613 21  HOH HOH C . 
U 8 HOH 114 614 359 HOH HOH C . 
U 8 HOH 115 615 88  HOH HOH C . 
U 8 HOH 116 616 238 HOH HOH C . 
U 8 HOH 117 617 772 HOH HOH C . 
U 8 HOH 118 618 607 HOH HOH C . 
U 8 HOH 119 619 598 HOH HOH C . 
U 8 HOH 120 620 561 HOH HOH C . 
U 8 HOH 121 621 262 HOH HOH C . 
U 8 HOH 122 622 84  HOH HOH C . 
U 8 HOH 123 623 125 HOH HOH C . 
U 8 HOH 124 624 358 HOH HOH C . 
U 8 HOH 125 625 309 HOH HOH C . 
U 8 HOH 126 626 615 HOH HOH C . 
U 8 HOH 127 627 64  HOH HOH C . 
U 8 HOH 128 628 445 HOH HOH C . 
U 8 HOH 129 629 127 HOH HOH C . 
U 8 HOH 130 630 584 HOH HOH C . 
U 8 HOH 131 631 399 HOH HOH C . 
U 8 HOH 132 632 731 HOH HOH C . 
U 8 HOH 133 633 70  HOH HOH C . 
U 8 HOH 134 634 669 HOH HOH C . 
U 8 HOH 135 635 49  HOH HOH C . 
U 8 HOH 136 636 693 HOH HOH C . 
U 8 HOH 137 637 655 HOH HOH C . 
U 8 HOH 138 638 729 HOH HOH C . 
U 8 HOH 139 639 519 HOH HOH C . 
U 8 HOH 140 640 371 HOH HOH C . 
U 8 HOH 141 641 649 HOH HOH C . 
U 8 HOH 142 642 330 HOH HOH C . 
U 8 HOH 143 643 42  HOH HOH C . 
U 8 HOH 144 644 740 HOH HOH C . 
U 8 HOH 145 645 294 HOH HOH C . 
U 8 HOH 146 646 370 HOH HOH C . 
U 8 HOH 147 647 332 HOH HOH C . 
U 8 HOH 148 648 290 HOH HOH C . 
U 8 HOH 149 649 482 HOH HOH C . 
U 8 HOH 150 650 707 HOH HOH C . 
U 8 HOH 151 651 342 HOH HOH C . 
U 8 HOH 152 652 95  HOH HOH C . 
U 8 HOH 153 653 154 HOH HOH C . 
U 8 HOH 154 654 695 HOH HOH C . 
U 8 HOH 155 655 455 HOH HOH C . 
U 8 HOH 156 656 225 HOH HOH C . 
U 8 HOH 157 657 456 HOH HOH C . 
U 8 HOH 158 658 261 HOH HOH C . 
U 8 HOH 159 659 279 HOH HOH C . 
U 8 HOH 160 660 776 HOH HOH C . 
U 8 HOH 161 661 314 HOH HOH C . 
U 8 HOH 162 662 120 HOH HOH C . 
U 8 HOH 163 663 590 HOH HOH C . 
U 8 HOH 164 664 627 HOH HOH C . 
U 8 HOH 165 665 388 HOH HOH C . 
U 8 HOH 166 666 517 HOH HOH C . 
U 8 HOH 167 667 352 HOH HOH C . 
U 8 HOH 168 668 795 HOH HOH C . 
U 8 HOH 169 669 635 HOH HOH C . 
U 8 HOH 170 670 432 HOH HOH C . 
U 8 HOH 171 671 257 HOH HOH C . 
U 8 HOH 172 672 717 HOH HOH C . 
U 8 HOH 173 673 559 HOH HOH C . 
U 8 HOH 174 674 542 HOH HOH C . 
U 8 HOH 175 675 430 HOH HOH C . 
U 8 HOH 176 676 647 HOH HOH C . 
U 8 HOH 177 677 605 HOH HOH C . 
U 8 HOH 178 678 175 HOH HOH C . 
U 8 HOH 179 679 525 HOH HOH C . 
U 8 HOH 180 680 311 HOH HOH C . 
U 8 HOH 181 681 549 HOH HOH C . 
U 8 HOH 182 682 85  HOH HOH C . 
U 8 HOH 183 683 784 HOH HOH C . 
U 8 HOH 184 684 553 HOH HOH C . 
U 8 HOH 185 685 526 HOH HOH C . 
U 8 HOH 186 686 195 HOH HOH C . 
U 8 HOH 187 687 536 HOH HOH C . 
U 8 HOH 188 688 567 HOH HOH C . 
U 8 HOH 189 689 626 HOH HOH C . 
U 8 HOH 190 690 742 HOH HOH C . 
U 8 HOH 191 691 443 HOH HOH C . 
U 8 HOH 192 692 72  HOH HOH C . 
U 8 HOH 193 693 151 HOH HOH C . 
U 8 HOH 194 694 633 HOH HOH C . 
U 8 HOH 195 695 564 HOH HOH C . 
U 8 HOH 196 696 558 HOH HOH C . 
U 8 HOH 197 697 674 HOH HOH C . 
U 8 HOH 198 698 679 HOH HOH C . 
U 8 HOH 199 699 462 HOH HOH C . 
U 8 HOH 200 700 645 HOH HOH C . 
U 8 HOH 201 701 715 HOH HOH C . 
U 8 HOH 202 702 398 HOH HOH C . 
U 8 HOH 203 703 452 HOH HOH C . 
U 8 HOH 204 704 667 HOH HOH C . 
U 8 HOH 205 705 505 HOH HOH C . 
U 8 HOH 206 706 282 HOH HOH C . 
U 8 HOH 207 707 746 HOH HOH C . 
U 8 HOH 208 708 307 HOH HOH C . 
U 8 HOH 209 709 513 HOH HOH C . 
U 8 HOH 210 710 574 HOH HOH C . 
U 8 HOH 211 711 287 HOH HOH C . 
U 8 HOH 212 712 702 HOH HOH C . 
U 8 HOH 213 713 658 HOH HOH C . 
U 8 HOH 214 714 779 HOH HOH C . 
U 8 HOH 215 715 295 HOH HOH C . 
U 8 HOH 216 716 413 HOH HOH C . 
U 8 HOH 217 717 426 HOH HOH C . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0258 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DFW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.131 
_cell.length_a_esd                 ? 
_cell.length_b                     85.131 
_cell.length_b_esd                 ? 
_cell.length_c                     110.471 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        9 
_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                         9DFW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                144 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31' 
_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                   9DFW 
_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             2.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.93 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES (pH 7.0), 10% (w/v) PEG 6K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-05 
_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   0.9793 
_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                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9793 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DFW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.677 
_reflns.d_resolution_low                               61.323 
_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                                     102720 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.17 
_reflns.pdbx_Rpim_I_all                                0.076 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.152 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.677 
_reflns_shell.d_res_low                                     1.705 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5167 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               2.612 
_reflns_shell.pdbx_Rpim_I_all                               1.167 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.358 
_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                                  2.332 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.37 
_refine.aniso_B[1][2]                            0.18 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.37 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.19 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               26.960 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.977 
_refine.correlation_coeff_Fo_to_Fc_free          0.966 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DFW 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.677 
_refine.ls_d_res_low                             19.86 
_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                     97622 
_refine.ls_number_reflns_R_free                  4939 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.90 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15675 
_refine.ls_R_factor_R_free                       0.18793 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15520 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.092 
_refine.pdbx_overall_ESU_R_Free                  0.091 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.532 
_refine.overall_SU_ML                            0.078 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.677 
_refine_hist.d_res_low                        19.86 
_refine_hist.number_atoms_solvent             710 
_refine_hist.number_atoms_total               7861 
_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        6920 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         231 
_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' ? 0.011  0.013  7427  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  6645  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.575  1.642  10057 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.411  1.583  15513 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.060  5.000  882   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 34.296 23.317 401   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.437 15.000 1311  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.768 15.000 39    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.119  0.200  948   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  8184  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1543  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.185  2.619  3504  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.185  2.619  3504  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.063  3.920  4388  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.063  3.920  4389  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.469  2.975  3923  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.461  2.973  3921  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.272  4.309  5632  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.424  31.528 8335  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.340  30.981 8160  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.677 
_refine_ls_shell.d_res_low                        1.720 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             333 
_refine_ls_shell.number_reflns_R_work             7182 
_refine_ls_shell.percent_reflns_obs               99.64 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.310 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.314 
# 
_struct.entry_id                     9DFW 
_struct.title                        
'X-ray crystal structure of an engineered Viperin-like enzyme from T. virens with bound CTP and SAM' 
_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        9DFW 
_struct_keywords.text            
'engineered viperin-like enzyme, viperin-like enzyme, CTP, SAM, 4Fe-4S cluster, ddhCTP, ANTIVIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'ANTIVIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
I N N 6 ? 
J N N 6 ? 
K N N 2 ? 
L N N 3 ? 
M N N 4 ? 
N N N 2 ? 
O N N 3 ? 
P N N 4 ? 
Q N N 7 ? 
R N N 6 ? 
S N N 8 ? 
T N N 8 ? 
U N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    G9MQB8_HYPVG 
_struct_ref.pdbx_db_accession          G9MQB8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GQVPVSVNYHFSRKCNKECLFCFHTATTSHVEKPENAKRGLTLLKQAGMKKINFAGGEPFLYPKFLGEMIDFCKETLQLE
SVSIVTNGSLVKEQFLQKHGRNIDILAVSCDSFNEATNIKIGRGSGDNVQKLYEIGSWCQKYDIKFKLNTVVNKFNHLED
MNDHLNALQPFRWKCFQVLIVTGENDSDKTLRNAHSLTISDDEFDRFCERHSSQTCLVPEPNRLMAKSYLILDEYMRFLD
RNGQQPSKSILEVGVQQALQAVFWDEEAFVERGGIYDWNKSSCSSDSKDLEW
;
_struct_ref.pdbx_align_begin           17 
# 
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 9DFW A 24 ? 317 ? G9MQB8 17 ? 308 ? 18 311 
2 1 9DFW B 24 ? 317 ? G9MQB8 17 ? 308 ? 18 311 
3 1 9DFW C 24 ? 317 ? G9MQB8 17 ? 308 ? 18 311 
# 
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 9DFW MET A 1   ? UNP G9MQB8 ?   ?   'initiating methionine' -5  1  
1 9DFW HIS A 2   ? UNP G9MQB8 ?   ?   'expression tag'        -4  2  
1 9DFW HIS A 3   ? UNP G9MQB8 ?   ?   'expression tag'        -3  3  
1 9DFW HIS A 4   ? UNP G9MQB8 ?   ?   'expression tag'        -2  4  
1 9DFW HIS A 5   ? UNP G9MQB8 ?   ?   'expression tag'        -1  5  
1 9DFW HIS A 6   ? UNP G9MQB8 ?   ?   'expression tag'        0   6  
1 9DFW HIS A 7   ? UNP G9MQB8 ?   ?   'expression tag'        1   7  
1 9DFW SER A 8   ? UNP G9MQB8 ?   ?   'expression tag'        2   8  
1 9DFW SER A 9   ? UNP G9MQB8 ?   ?   'expression tag'        3   9  
1 9DFW GLY A 10  ? UNP G9MQB8 ?   ?   'expression tag'        4   10 
1 9DFW VAL A 11  ? UNP G9MQB8 ?   ?   'expression tag'        5   11 
1 9DFW ASP A 12  ? UNP G9MQB8 ?   ?   'expression tag'        6   12 
1 9DFW LEU A 13  ? UNP G9MQB8 ?   ?   'expression tag'        7   13 
1 9DFW GLY A 14  ? UNP G9MQB8 ?   ?   'expression tag'        8   14 
1 9DFW THR A 15  ? UNP G9MQB8 ?   ?   'expression tag'        9   15 
1 9DFW GLU A 16  ? UNP G9MQB8 ?   ?   'expression tag'        10  16 
1 9DFW ASN A 17  ? UNP G9MQB8 ?   ?   'expression tag'        11  17 
1 9DFW LEU A 18  ? UNP G9MQB8 ?   ?   'expression tag'        12  18 
1 9DFW TYR A 19  ? UNP G9MQB8 ?   ?   'expression tag'        13  19 
1 9DFW PHE A 20  ? UNP G9MQB8 ?   ?   'expression tag'        14  20 
1 9DFW GLN A 21  ? UNP G9MQB8 ?   ?   'expression tag'        15  21 
1 9DFW SER A 22  ? UNP G9MQB8 ?   ?   'expression tag'        16  22 
1 9DFW MET A 23  ? UNP G9MQB8 ?   ?   'expression tag'        17  23 
1 9DFW ILE A 204 ? UNP G9MQB8 VAL 197 'engineered mutation'   198 24 
1 9DFW GLU A 205 ? UNP G9MQB8 THR 198 'engineered mutation'   199 25 
1 9DFW ASN A 263 ? UNP G9MQB8 ASP 256 'engineered mutation'   257 26 
1 9DFW CYS A 264 ? UNP G9MQB8 ARG 257 'engineered mutation'   258 27 
1 9DFW THR A 265 ? UNP G9MQB8 ASN 258 'engineered mutation'   259 28 
1 9DFW GLY A 267 ? UNP G9MQB8 ?   ?   insertion               261 29 
1 9DFW ARG A 268 ? UNP G9MQB8 ?   ?   insertion               262 30 
1 9DFW LYS A 269 ? UNP G9MQB8 GLN 260 'engineered mutation'   263 31 
1 9DFW ASP A 270 ? UNP G9MQB8 GLN 261 'engineered mutation'   264 32 
2 9DFW MET B 1   ? UNP G9MQB8 ?   ?   'initiating methionine' -5  33 
2 9DFW HIS B 2   ? UNP G9MQB8 ?   ?   'expression tag'        -4  34 
2 9DFW HIS B 3   ? UNP G9MQB8 ?   ?   'expression tag'        -3  35 
2 9DFW HIS B 4   ? UNP G9MQB8 ?   ?   'expression tag'        -2  36 
2 9DFW HIS B 5   ? UNP G9MQB8 ?   ?   'expression tag'        -1  37 
2 9DFW HIS B 6   ? UNP G9MQB8 ?   ?   'expression tag'        0   38 
2 9DFW HIS B 7   ? UNP G9MQB8 ?   ?   'expression tag'        1   39 
2 9DFW SER B 8   ? UNP G9MQB8 ?   ?   'expression tag'        2   40 
2 9DFW SER B 9   ? UNP G9MQB8 ?   ?   'expression tag'        3   41 
2 9DFW GLY B 10  ? UNP G9MQB8 ?   ?   'expression tag'        4   42 
2 9DFW VAL B 11  ? UNP G9MQB8 ?   ?   'expression tag'        5   43 
2 9DFW ASP B 12  ? UNP G9MQB8 ?   ?   'expression tag'        6   44 
2 9DFW LEU B 13  ? UNP G9MQB8 ?   ?   'expression tag'        7   45 
2 9DFW GLY B 14  ? UNP G9MQB8 ?   ?   'expression tag'        8   46 
2 9DFW THR B 15  ? UNP G9MQB8 ?   ?   'expression tag'        9   47 
2 9DFW GLU B 16  ? UNP G9MQB8 ?   ?   'expression tag'        10  48 
2 9DFW ASN B 17  ? UNP G9MQB8 ?   ?   'expression tag'        11  49 
2 9DFW LEU B 18  ? UNP G9MQB8 ?   ?   'expression tag'        12  50 
2 9DFW TYR B 19  ? UNP G9MQB8 ?   ?   'expression tag'        13  51 
2 9DFW PHE B 20  ? UNP G9MQB8 ?   ?   'expression tag'        14  52 
2 9DFW GLN B 21  ? UNP G9MQB8 ?   ?   'expression tag'        15  53 
2 9DFW SER B 22  ? UNP G9MQB8 ?   ?   'expression tag'        16  54 
2 9DFW MET B 23  ? UNP G9MQB8 ?   ?   'expression tag'        17  55 
2 9DFW ILE B 204 ? UNP G9MQB8 VAL 197 'engineered mutation'   198 56 
2 9DFW GLU B 205 ? UNP G9MQB8 THR 198 'engineered mutation'   199 57 
2 9DFW ASN B 263 ? UNP G9MQB8 ASP 256 'engineered mutation'   257 58 
2 9DFW CYS B 264 ? UNP G9MQB8 ARG 257 'engineered mutation'   258 59 
2 9DFW THR B 265 ? UNP G9MQB8 ASN 258 'engineered mutation'   259 60 
2 9DFW GLY B 267 ? UNP G9MQB8 ?   ?   insertion               261 61 
2 9DFW ARG B 268 ? UNP G9MQB8 ?   ?   insertion               262 62 
2 9DFW LYS B 269 ? UNP G9MQB8 GLN 260 'engineered mutation'   263 63 
2 9DFW ASP B 270 ? UNP G9MQB8 GLN 261 'engineered mutation'   264 64 
3 9DFW MET C 1   ? UNP G9MQB8 ?   ?   'initiating methionine' -5  65 
3 9DFW HIS C 2   ? UNP G9MQB8 ?   ?   'expression tag'        -4  66 
3 9DFW HIS C 3   ? UNP G9MQB8 ?   ?   'expression tag'        -3  67 
3 9DFW HIS C 4   ? UNP G9MQB8 ?   ?   'expression tag'        -2  68 
3 9DFW HIS C 5   ? UNP G9MQB8 ?   ?   'expression tag'        -1  69 
3 9DFW HIS C 6   ? UNP G9MQB8 ?   ?   'expression tag'        0   70 
3 9DFW HIS C 7   ? UNP G9MQB8 ?   ?   'expression tag'        1   71 
3 9DFW SER C 8   ? UNP G9MQB8 ?   ?   'expression tag'        2   72 
3 9DFW SER C 9   ? UNP G9MQB8 ?   ?   'expression tag'        3   73 
3 9DFW GLY C 10  ? UNP G9MQB8 ?   ?   'expression tag'        4   74 
3 9DFW VAL C 11  ? UNP G9MQB8 ?   ?   'expression tag'        5   75 
3 9DFW ASP C 12  ? UNP G9MQB8 ?   ?   'expression tag'        6   76 
3 9DFW LEU C 13  ? UNP G9MQB8 ?   ?   'expression tag'        7   77 
3 9DFW GLY C 14  ? UNP G9MQB8 ?   ?   'expression tag'        8   78 
3 9DFW THR C 15  ? UNP G9MQB8 ?   ?   'expression tag'        9   79 
3 9DFW GLU C 16  ? UNP G9MQB8 ?   ?   'expression tag'        10  80 
3 9DFW ASN C 17  ? UNP G9MQB8 ?   ?   'expression tag'        11  81 
3 9DFW LEU C 18  ? UNP G9MQB8 ?   ?   'expression tag'        12  82 
3 9DFW TYR C 19  ? UNP G9MQB8 ?   ?   'expression tag'        13  83 
3 9DFW PHE C 20  ? UNP G9MQB8 ?   ?   'expression tag'        14  84 
3 9DFW GLN C 21  ? UNP G9MQB8 ?   ?   'expression tag'        15  85 
3 9DFW SER C 22  ? UNP G9MQB8 ?   ?   'expression tag'        16  86 
3 9DFW MET C 23  ? UNP G9MQB8 ?   ?   'expression tag'        17  87 
3 9DFW ILE C 204 ? UNP G9MQB8 VAL 197 'engineered mutation'   198 88 
3 9DFW GLU C 205 ? UNP G9MQB8 THR 198 'engineered mutation'   199 89 
3 9DFW ASN C 263 ? UNP G9MQB8 ASP 256 'engineered mutation'   257 90 
3 9DFW CYS C 264 ? UNP G9MQB8 ARG 257 'engineered mutation'   258 91 
3 9DFW THR C 265 ? UNP G9MQB8 ASN 258 'engineered mutation'   259 92 
3 9DFW GLY C 267 ? UNP G9MQB8 ?   ?   insertion               261 93 
3 9DFW ARG C 268 ? UNP G9MQB8 ?   ?   insertion               262 94 
3 9DFW LYS C 269 ? UNP G9MQB8 GLN 260 'engineered mutation'   263 95 
3 9DFW ASP C 270 ? UNP G9MQB8 GLN 261 'engineered mutation'   264 96 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,H,I,J,S 
2 1 B,K,L,M,T         
3 1 C,N,O,P,Q,R,U     
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 56  ? GLY A 71  ? LYS A 50  GLY A 65  1 ? 16 
HELX_P HELX_P2  AA2 GLU A 81  ? LEU A 84  ? GLU A 75  LEU A 78  5 ? 4  
HELX_P HELX_P3  AA3 TYR A 85  ? THR A 99  ? TYR A 79  THR A 93  1 ? 15 
HELX_P HELX_P4  AA4 LYS A 115 ? GLY A 123 ? LYS A 109 GLY A 117 1 ? 9  
HELX_P HELX_P5  AA5 ARG A 124 ? ILE A 126 ? ARG A 118 ILE A 120 5 ? 3  
HELX_P HELX_P6  AA6 ASN A 137 ? GLY A 145 ? ASN A 131 GLY A 139 1 ? 9  
HELX_P HELX_P7  AA7 ASP A 150 ? ASP A 166 ? ASP A 144 ASP A 160 1 ? 17 
HELX_P HELX_P8  AA8 MET A 184 ? GLN A 192 ? MET A 178 GLN A 186 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 217 ? THR A 221 ? ALA A 211 THR A 215 5 ? 5  
HELX_P HELX_P10 AB1 SER A 223 ? HIS A 234 ? SER A 217 HIS A 228 1 ? 12 
HELX_P HELX_P11 AB2 PRO A 244 ? ALA A 249 ? PRO A 238 ALA A 243 1 ? 6  
HELX_P HELX_P12 AB3 ILE A 275 ? ALA A 286 ? ILE A 269 ALA A 280 1 ? 12 
HELX_P HELX_P13 AB4 ASP A 290 ? ARG A 297 ? ASP A 284 ARG A 291 1 ? 8  
HELX_P HELX_P14 AB5 LYS B 56  ? ALA B 70  ? LYS B 50  ALA B 64  1 ? 15 
HELX_P HELX_P15 AB6 GLU B 81  ? LEU B 84  ? GLU B 75  LEU B 78  5 ? 4  
HELX_P HELX_P16 AB7 TYR B 85  ? THR B 99  ? TYR B 79  THR B 93  1 ? 15 
HELX_P HELX_P17 AB8 LYS B 115 ? GLY B 123 ? LYS B 109 GLY B 117 1 ? 9  
HELX_P HELX_P18 AB9 ARG B 124 ? ILE B 126 ? ARG B 118 ILE B 120 5 ? 3  
HELX_P HELX_P19 AC1 ASN B 137 ? GLY B 145 ? ASN B 131 GLY B 139 1 ? 9  
HELX_P HELX_P20 AC2 ASP B 150 ? ASP B 166 ? ASP B 144 ASP B 160 1 ? 17 
HELX_P HELX_P21 AC3 MET B 184 ? GLN B 192 ? MET B 178 GLN B 186 1 ? 9  
HELX_P HELX_P22 AC4 ASN B 216 ? THR B 221 ? ASN B 210 THR B 215 5 ? 6  
HELX_P HELX_P23 AC5 SER B 223 ? HIS B 234 ? SER B 217 HIS B 228 1 ? 12 
HELX_P HELX_P24 AC6 PRO B 244 ? ALA B 249 ? PRO B 238 ALA B 243 1 ? 6  
HELX_P HELX_P25 AC7 CYS B 264 ? ARG B 268 ? CYS B 258 ARG B 262 5 ? 5  
HELX_P HELX_P26 AC8 ILE B 275 ? GLY B 279 ? ILE B 269 GLY B 273 1 ? 5  
HELX_P HELX_P27 AC9 GLY B 279 ? ALA B 286 ? GLY B 273 ALA B 280 1 ? 8  
HELX_P HELX_P28 AD1 ASP B 290 ? ARG B 297 ? ASP B 284 ARG B 291 1 ? 8  
HELX_P HELX_P29 AD2 CYS B 308 ? LEU B 315 ? CYS B 302 LEU B 309 5 ? 8  
HELX_P HELX_P30 AD3 LYS C 56  ? GLY C 71  ? LYS C 50  GLY C 65  1 ? 16 
HELX_P HELX_P31 AD4 GLU C 81  ? LEU C 84  ? GLU C 75  LEU C 78  5 ? 4  
HELX_P HELX_P32 AD5 TYR C 85  ? THR C 99  ? TYR C 79  THR C 93  1 ? 15 
HELX_P HELX_P33 AD6 LYS C 115 ? GLY C 123 ? LYS C 109 GLY C 117 1 ? 9  
HELX_P HELX_P34 AD7 ARG C 124 ? ILE C 126 ? ARG C 118 ILE C 120 5 ? 3  
HELX_P HELX_P35 AD8 ASN C 137 ? GLY C 145 ? ASN C 131 GLY C 139 1 ? 9  
HELX_P HELX_P36 AD9 ASP C 150 ? ASP C 166 ? ASP C 144 ASP C 160 1 ? 17 
HELX_P HELX_P37 AE1 MET C 184 ? GLN C 192 ? MET C 178 GLN C 186 1 ? 9  
HELX_P HELX_P38 AE2 ALA C 217 ? THR C 221 ? ALA C 211 THR C 215 5 ? 5  
HELX_P HELX_P39 AE3 SER C 223 ? HIS C 234 ? SER C 217 HIS C 228 1 ? 12 
HELX_P HELX_P40 AE4 PRO C 244 ? ALA C 249 ? PRO C 238 ALA C 243 1 ? 6  
HELX_P HELX_P41 AE5 CYS C 264 ? ARG C 268 ? CYS C 258 ARG C 262 5 ? 5  
HELX_P HELX_P42 AE6 ILE C 275 ? GLY C 279 ? ILE C 269 GLY C 273 1 ? 5  
HELX_P HELX_P43 AE7 GLY C 279 ? ALA C 286 ? GLY C 273 ALA C 280 1 ? 8  
HELX_P HELX_P44 AE8 ASP C 290 ? ARG C 297 ? ASP C 284 ARG C 291 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 38  SG  ? ? ? 1_555 D SF4 . FE4 ? ? A CYS 32  A SF4 401 1_555 ? ? ? ? ? ? ? 2.284 ? ? 
metalc2  metalc ? ? A CYS 42  SG  ? ? ? 1_555 D SF4 . FE2 ? ? A CYS 36  A SF4 401 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc3  metalc ? ? A CYS 45  SG  ? ? ? 1_555 D SF4 . FE1 ? ? A CYS 39  A SF4 401 1_555 ? ? ? ? ? ? ? 2.285 ? ? 
metalc4  metalc ? ? A GLY 123 O   ? ? ? 1_555 I MG  . MG  ? ? A GLY 117 A MG  406 1_555 ? ? ? ? ? ? ? 2.776 ? ? 
metalc5  metalc ? ? A ILE 126 O   ? ? ? 1_555 I MG  . MG  ? ? A ILE 120 A MG  406 1_555 ? ? ? ? ? ? ? 2.689 ? ? 
metalc6  metalc ? ? A ASP 166 O   ? ? ? 1_555 I MG  . MG  ? ? A ASP 160 A MG  406 1_555 ? ? ? ? ? ? ? 2.810 ? ? 
metalc7  metalc ? ? A GLU 232 O   ? ? ? 1_555 J MG  . MG  ? ? A GLU 226 A MG  407 1_555 ? ? ? ? ? ? ? 2.509 ? ? 
metalc8  metalc ? ? A SER 235 OG  ? ? ? 1_555 J MG  . MG  ? ? A SER 229 A MG  407 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc9  metalc ? ? D SF4 .   FE3 ? ? ? 1_555 E SAM . N   ? ? A SF4 401 A SAM 402 1_555 ? ? ? ? ? ? ? 2.378 ? ? 
metalc10 metalc ? ? D SF4 .   FE3 ? ? ? 1_555 E SAM . OXT ? ? A SF4 401 A SAM 402 1_555 ? ? ? ? ? ? ? 2.139 ? ? 
metalc11 metalc ? ? I MG  .   MG  ? ? ? 1_555 S HOH . O   ? ? A MG  406 A HOH 624 1_555 ? ? ? ? ? ? ? 2.612 ? ? 
metalc12 metalc ? ? J MG  .   MG  ? ? ? 1_555 S HOH . O   ? ? A MG  407 A HOH 504 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc13 metalc ? ? J MG  .   MG  ? ? ? 1_555 S HOH . O   ? ? A MG  407 A HOH 685 1_555 ? ? ? ? ? ? ? 2.002 ? ? 
metalc14 metalc ? ? J MG  .   MG  ? ? ? 1_555 S HOH . O   ? ? A MG  407 A HOH 703 1_555 ? ? ? ? ? ? ? 2.421 ? ? 
metalc15 metalc ? ? B CYS 38  SG  ? ? ? 1_555 K SF4 . FE3 ? ? B CYS 32  B SF4 401 1_555 ? ? ? ? ? ? ? 2.227 ? ? 
metalc16 metalc ? ? B CYS 42  SG  ? ? ? 1_555 K SF4 . FE1 ? ? B CYS 36  B SF4 401 1_555 ? ? ? ? ? ? ? 2.263 ? ? 
metalc17 metalc ? ? B CYS 45  SG  ? ? ? 1_555 K SF4 . FE2 ? ? B CYS 39  B SF4 401 1_555 ? ? ? ? ? ? ? 2.281 ? ? 
metalc18 metalc ? ? K SF4 .   FE4 ? ? ? 1_555 L SAM . N   ? ? B SF4 401 B SAM 402 1_555 ? ? ? ? ? ? ? 2.255 ? ? 
metalc19 metalc ? ? K SF4 .   FE4 ? ? ? 1_555 L SAM . O   ? ? B SF4 401 B SAM 402 1_555 ? ? ? ? ? ? ? 2.262 ? ? 
metalc20 metalc ? ? C CYS 38  SG  ? ? ? 1_555 N SF4 . FE1 ? ? C CYS 32  C SF4 401 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc21 metalc ? ? C CYS 42  SG  ? ? ? 1_555 N SF4 . FE4 ? ? C CYS 36  C SF4 401 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc22 metalc ? ? C CYS 45  SG  ? ? ? 1_555 N SF4 . FE2 ? ? C CYS 39  C SF4 401 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc23 metalc ? ? C GLY 123 O   ? ? ? 1_555 R MG  . MG  ? ? C GLY 117 C MG  405 1_555 ? ? ? ? ? ? ? 2.783 ? ? 
metalc24 metalc ? ? C ILE 126 O   ? ? ? 1_555 R MG  . MG  ? ? C ILE 120 C MG  405 1_555 ? ? ? ? ? ? ? 2.662 ? ? 
metalc25 metalc ? ? C ASP 166 O   ? ? ? 1_555 R MG  . MG  ? ? C ASP 160 C MG  405 1_555 ? ? ? ? ? ? ? 2.823 ? ? 
metalc26 metalc ? ? N SF4 .   FE3 ? ? ? 1_555 O SAM . N   ? ? C SF4 401 C SAM 402 1_555 ? ? ? ? ? ? ? 2.380 ? ? 
metalc27 metalc ? ? N SF4 .   FE3 ? ? ? 1_555 O SAM . O   ? ? C SF4 401 C SAM 402 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   SG ? A CYS 38  ? A CYS 32  ? 1_555 FE4 ? D SF4 . ? A SF4 401 ? 1_555 S1  ? D SF4 .   ? A SF4 401 ? 1_555 100.5 ? 
2   SG ? A CYS 38  ? A CYS 32  ? 1_555 FE4 ? D SF4 . ? A SF4 401 ? 1_555 S2  ? D SF4 .   ? A SF4 401 ? 1_555 112.1 ? 
3   S1 ? D SF4 .   ? A SF4 401 ? 1_555 FE4 ? D SF4 . ? A SF4 401 ? 1_555 S2  ? D SF4 .   ? A SF4 401 ? 1_555 110.5 ? 
4   SG ? A CYS 38  ? A CYS 32  ? 1_555 FE4 ? D SF4 . ? A SF4 401 ? 1_555 S3  ? D SF4 .   ? A SF4 401 ? 1_555 123.9 ? 
5   S1 ? D SF4 .   ? A SF4 401 ? 1_555 FE4 ? D SF4 . ? A SF4 401 ? 1_555 S3  ? D SF4 .   ? A SF4 401 ? 1_555 102.8 ? 
6   S2 ? D SF4 .   ? A SF4 401 ? 1_555 FE4 ? D SF4 . ? A SF4 401 ? 1_555 S3  ? D SF4 .   ? A SF4 401 ? 1_555 106.1 ? 
7   SG ? A CYS 42  ? A CYS 36  ? 1_555 FE2 ? D SF4 . ? A SF4 401 ? 1_555 S1  ? D SF4 .   ? A SF4 401 ? 1_555 117.4 ? 
8   SG ? A CYS 42  ? A CYS 36  ? 1_555 FE2 ? D SF4 . ? A SF4 401 ? 1_555 S3  ? D SF4 .   ? A SF4 401 ? 1_555 108.8 ? 
9   S1 ? D SF4 .   ? A SF4 401 ? 1_555 FE2 ? D SF4 . ? A SF4 401 ? 1_555 S3  ? D SF4 .   ? A SF4 401 ? 1_555 104.0 ? 
10  SG ? A CYS 42  ? A CYS 36  ? 1_555 FE2 ? D SF4 . ? A SF4 401 ? 1_555 S4  ? D SF4 .   ? A SF4 401 ? 1_555 114.5 ? 
11  S1 ? D SF4 .   ? A SF4 401 ? 1_555 FE2 ? D SF4 . ? A SF4 401 ? 1_555 S4  ? D SF4 .   ? A SF4 401 ? 1_555 104.3 ? 
12  S3 ? D SF4 .   ? A SF4 401 ? 1_555 FE2 ? D SF4 . ? A SF4 401 ? 1_555 S4  ? D SF4 .   ? A SF4 401 ? 1_555 106.8 ? 
13  SG ? A CYS 45  ? A CYS 39  ? 1_555 FE1 ? D SF4 . ? A SF4 401 ? 1_555 S2  ? D SF4 .   ? A SF4 401 ? 1_555 115.5 ? 
14  SG ? A CYS 45  ? A CYS 39  ? 1_555 FE1 ? D SF4 . ? A SF4 401 ? 1_555 S3  ? D SF4 .   ? A SF4 401 ? 1_555 104.9 ? 
15  S2 ? D SF4 .   ? A SF4 401 ? 1_555 FE1 ? D SF4 . ? A SF4 401 ? 1_555 S3  ? D SF4 .   ? A SF4 401 ? 1_555 103.8 ? 
16  SG ? A CYS 45  ? A CYS 39  ? 1_555 FE1 ? D SF4 . ? A SF4 401 ? 1_555 S4  ? D SF4 .   ? A SF4 401 ? 1_555 121.4 ? 
17  S2 ? D SF4 .   ? A SF4 401 ? 1_555 FE1 ? D SF4 . ? A SF4 401 ? 1_555 S4  ? D SF4 .   ? A SF4 401 ? 1_555 103.8 ? 
18  S3 ? D SF4 .   ? A SF4 401 ? 1_555 FE1 ? D SF4 . ? A SF4 401 ? 1_555 S4  ? D SF4 .   ? A SF4 401 ? 1_555 105.8 ? 
19  O  ? A GLY 123 ? A GLY 117 ? 1_555 MG  ? I MG  . ? A MG  406 ? 1_555 O   ? A ILE 126 ? A ILE 120 ? 1_555 78.3  ? 
20  O  ? A GLY 123 ? A GLY 117 ? 1_555 MG  ? I MG  . ? A MG  406 ? 1_555 O   ? A ASP 166 ? A ASP 160 ? 1_555 117.6 ? 
21  O  ? A ILE 126 ? A ILE 120 ? 1_555 MG  ? I MG  . ? A MG  406 ? 1_555 O   ? A ASP 166 ? A ASP 160 ? 1_555 108.6 ? 
22  O  ? A GLY 123 ? A GLY 117 ? 1_555 MG  ? I MG  . ? A MG  406 ? 1_555 O   ? S HOH .   ? A HOH 624 ? 1_555 101.7 ? 
23  O  ? A ILE 126 ? A ILE 120 ? 1_555 MG  ? I MG  . ? A MG  406 ? 1_555 O   ? S HOH .   ? A HOH 624 ? 1_555 75.1  ? 
24  O  ? A ASP 166 ? A ASP 160 ? 1_555 MG  ? I MG  . ? A MG  406 ? 1_555 O   ? S HOH .   ? A HOH 624 ? 1_555 140.6 ? 
25  O  ? A GLU 232 ? A GLU 226 ? 1_555 MG  ? J MG  . ? A MG  407 ? 1_555 OG  ? A SER 235 ? A SER 229 ? 1_555 84.0  ? 
26  O  ? A GLU 232 ? A GLU 226 ? 1_555 MG  ? J MG  . ? A MG  407 ? 1_555 O   ? S HOH .   ? A HOH 504 ? 1_555 86.8  ? 
27  OG ? A SER 235 ? A SER 229 ? 1_555 MG  ? J MG  . ? A MG  407 ? 1_555 O   ? S HOH .   ? A HOH 504 ? 1_555 91.0  ? 
28  O  ? A GLU 232 ? A GLU 226 ? 1_555 MG  ? J MG  . ? A MG  407 ? 1_555 O   ? S HOH .   ? A HOH 685 ? 1_555 99.1  ? 
29  OG ? A SER 235 ? A SER 229 ? 1_555 MG  ? J MG  . ? A MG  407 ? 1_555 O   ? S HOH .   ? A HOH 685 ? 1_555 93.3  ? 
30  O  ? S HOH .   ? A HOH 504 ? 1_555 MG  ? J MG  . ? A MG  407 ? 1_555 O   ? S HOH .   ? A HOH 685 ? 1_555 173.0 ? 
31  O  ? A GLU 232 ? A GLU 226 ? 1_555 MG  ? J MG  . ? A MG  407 ? 1_555 O   ? S HOH .   ? A HOH 703 ? 1_555 90.1  ? 
32  OG ? A SER 235 ? A SER 229 ? 1_555 MG  ? J MG  . ? A MG  407 ? 1_555 O   ? S HOH .   ? A HOH 703 ? 1_555 172.6 ? 
33  O  ? S HOH .   ? A HOH 504 ? 1_555 MG  ? J MG  . ? A MG  407 ? 1_555 O   ? S HOH .   ? A HOH 703 ? 1_555 93.2  ? 
34  O  ? S HOH .   ? A HOH 685 ? 1_555 MG  ? J MG  . ? A MG  407 ? 1_555 O   ? S HOH .   ? A HOH 703 ? 1_555 83.0  ? 
35  N  ? E SAM .   ? A SAM 402 ? 1_555 FE3 ? D SF4 . ? A SF4 401 ? 1_555 S1  ? D SF4 .   ? A SF4 401 ? 1_555 97.9  ? 
36  N  ? E SAM .   ? A SAM 402 ? 1_555 FE3 ? D SF4 . ? A SF4 401 ? 1_555 S2  ? D SF4 .   ? A SF4 401 ? 1_555 83.7  ? 
37  S1 ? D SF4 .   ? A SF4 401 ? 1_555 FE3 ? D SF4 . ? A SF4 401 ? 1_555 S2  ? D SF4 .   ? A SF4 401 ? 1_555 105.0 ? 
38  N  ? E SAM .   ? A SAM 402 ? 1_555 FE3 ? D SF4 . ? A SF4 401 ? 1_555 S4  ? D SF4 .   ? A SF4 401 ? 1_555 159.5 ? 
39  S1 ? D SF4 .   ? A SF4 401 ? 1_555 FE3 ? D SF4 . ? A SF4 401 ? 1_555 S4  ? D SF4 .   ? A SF4 401 ? 1_555 101.3 ? 
40  S2 ? D SF4 .   ? A SF4 401 ? 1_555 FE3 ? D SF4 . ? A SF4 401 ? 1_555 S4  ? D SF4 .   ? A SF4 401 ? 1_555 98.1  ? 
41  N  ? E SAM .   ? A SAM 402 ? 1_555 FE3 ? D SF4 . ? A SF4 401 ? 1_555 OXT ? E SAM .   ? A SAM 402 ? 1_555 73.3  ? 
42  S1 ? D SF4 .   ? A SF4 401 ? 1_555 FE3 ? D SF4 . ? A SF4 401 ? 1_555 OXT ? E SAM .   ? A SAM 402 ? 1_555 96.8  ? 
43  S2 ? D SF4 .   ? A SF4 401 ? 1_555 FE3 ? D SF4 . ? A SF4 401 ? 1_555 OXT ? E SAM .   ? A SAM 402 ? 1_555 150.2 ? 
44  S4 ? D SF4 .   ? A SF4 401 ? 1_555 FE3 ? D SF4 . ? A SF4 401 ? 1_555 OXT ? E SAM .   ? A SAM 402 ? 1_555 97.2  ? 
45  SG ? B CYS 38  ? B CYS 32  ? 1_555 FE3 ? K SF4 . ? B SF4 401 ? 1_555 S1  ? K SF4 .   ? B SF4 401 ? 1_555 113.8 ? 
46  SG ? B CYS 38  ? B CYS 32  ? 1_555 FE3 ? K SF4 . ? B SF4 401 ? 1_555 S2  ? K SF4 .   ? B SF4 401 ? 1_555 100.8 ? 
47  S1 ? K SF4 .   ? B SF4 401 ? 1_555 FE3 ? K SF4 . ? B SF4 401 ? 1_555 S2  ? K SF4 .   ? B SF4 401 ? 1_555 109.8 ? 
48  SG ? B CYS 38  ? B CYS 32  ? 1_555 FE3 ? K SF4 . ? B SF4 401 ? 1_555 S4  ? K SF4 .   ? B SF4 401 ? 1_555 124.4 ? 
49  S1 ? K SF4 .   ? B SF4 401 ? 1_555 FE3 ? K SF4 . ? B SF4 401 ? 1_555 S4  ? K SF4 .   ? B SF4 401 ? 1_555 104.7 ? 
50  S2 ? K SF4 .   ? B SF4 401 ? 1_555 FE3 ? K SF4 . ? B SF4 401 ? 1_555 S4  ? K SF4 .   ? B SF4 401 ? 1_555 102.1 ? 
51  SG ? B CYS 42  ? B CYS 36  ? 1_555 FE1 ? K SF4 . ? B SF4 401 ? 1_555 S2  ? K SF4 .   ? B SF4 401 ? 1_555 117.2 ? 
52  SG ? B CYS 42  ? B CYS 36  ? 1_555 FE1 ? K SF4 . ? B SF4 401 ? 1_555 S3  ? K SF4 .   ? B SF4 401 ? 1_555 116.0 ? 
53  S2 ? K SF4 .   ? B SF4 401 ? 1_555 FE1 ? K SF4 . ? B SF4 401 ? 1_555 S3  ? K SF4 .   ? B SF4 401 ? 1_555 103.1 ? 
54  SG ? B CYS 42  ? B CYS 36  ? 1_555 FE1 ? K SF4 . ? B SF4 401 ? 1_555 S4  ? K SF4 .   ? B SF4 401 ? 1_555 110.5 ? 
55  S2 ? K SF4 .   ? B SF4 401 ? 1_555 FE1 ? K SF4 . ? B SF4 401 ? 1_555 S4  ? K SF4 .   ? B SF4 401 ? 1_555 103.8 ? 
56  S3 ? K SF4 .   ? B SF4 401 ? 1_555 FE1 ? K SF4 . ? B SF4 401 ? 1_555 S4  ? K SF4 .   ? B SF4 401 ? 1_555 104.8 ? 
57  SG ? B CYS 45  ? B CYS 39  ? 1_555 FE2 ? K SF4 . ? B SF4 401 ? 1_555 S1  ? K SF4 .   ? B SF4 401 ? 1_555 115.9 ? 
58  SG ? B CYS 45  ? B CYS 39  ? 1_555 FE2 ? K SF4 . ? B SF4 401 ? 1_555 S3  ? K SF4 .   ? B SF4 401 ? 1_555 122.6 ? 
59  S1 ? K SF4 .   ? B SF4 401 ? 1_555 FE2 ? K SF4 . ? B SF4 401 ? 1_555 S3  ? K SF4 .   ? B SF4 401 ? 1_555 102.8 ? 
60  SG ? B CYS 45  ? B CYS 39  ? 1_555 FE2 ? K SF4 . ? B SF4 401 ? 1_555 S4  ? K SF4 .   ? B SF4 401 ? 1_555 105.6 ? 
61  S1 ? K SF4 .   ? B SF4 401 ? 1_555 FE2 ? K SF4 . ? B SF4 401 ? 1_555 S4  ? K SF4 .   ? B SF4 401 ? 1_555 102.6 ? 
62  S3 ? K SF4 .   ? B SF4 401 ? 1_555 FE2 ? K SF4 . ? B SF4 401 ? 1_555 S4  ? K SF4 .   ? B SF4 401 ? 1_555 105.3 ? 
63  N  ? L SAM .   ? B SAM 402 ? 1_555 FE4 ? K SF4 . ? B SF4 401 ? 1_555 S1  ? K SF4 .   ? B SF4 401 ? 1_555 83.7  ? 
64  N  ? L SAM .   ? B SAM 402 ? 1_555 FE4 ? K SF4 . ? B SF4 401 ? 1_555 S2  ? K SF4 .   ? B SF4 401 ? 1_555 98.4  ? 
65  S1 ? K SF4 .   ? B SF4 401 ? 1_555 FE4 ? K SF4 . ? B SF4 401 ? 1_555 S2  ? K SF4 .   ? B SF4 401 ? 1_555 105.7 ? 
66  N  ? L SAM .   ? B SAM 402 ? 1_555 FE4 ? K SF4 . ? B SF4 401 ? 1_555 S3  ? K SF4 .   ? B SF4 401 ? 1_555 158.5 ? 
67  S1 ? K SF4 .   ? B SF4 401 ? 1_555 FE4 ? K SF4 . ? B SF4 401 ? 1_555 S3  ? K SF4 .   ? B SF4 401 ? 1_555 99.5  ? 
68  S2 ? K SF4 .   ? B SF4 401 ? 1_555 FE4 ? K SF4 . ? B SF4 401 ? 1_555 S3  ? K SF4 .   ? B SF4 401 ? 1_555 101.1 ? 
69  N  ? L SAM .   ? B SAM 402 ? 1_555 FE4 ? K SF4 . ? B SF4 401 ? 1_555 O   ? L SAM .   ? B SAM 402 ? 1_555 74.3  ? 
70  S1 ? K SF4 .   ? B SF4 401 ? 1_555 FE4 ? K SF4 . ? B SF4 401 ? 1_555 O   ? L SAM .   ? B SAM 402 ? 1_555 153.4 ? 
71  S2 ? K SF4 .   ? B SF4 401 ? 1_555 FE4 ? K SF4 . ? B SF4 401 ? 1_555 O   ? L SAM .   ? B SAM 402 ? 1_555 92.3  ? 
72  S3 ? K SF4 .   ? B SF4 401 ? 1_555 FE4 ? K SF4 . ? B SF4 401 ? 1_555 O   ? L SAM .   ? B SAM 402 ? 1_555 96.0  ? 
73  SG ? C CYS 38  ? C CYS 32  ? 1_555 FE1 ? N SF4 . ? C SF4 401 ? 1_555 S2  ? N SF4 .   ? C SF4 401 ? 1_555 101.0 ? 
74  SG ? C CYS 38  ? C CYS 32  ? 1_555 FE1 ? N SF4 . ? C SF4 401 ? 1_555 S3  ? N SF4 .   ? C SF4 401 ? 1_555 127.0 ? 
75  S2 ? N SF4 .   ? C SF4 401 ? 1_555 FE1 ? N SF4 . ? C SF4 401 ? 1_555 S3  ? N SF4 .   ? C SF4 401 ? 1_555 104.2 ? 
76  SG ? C CYS 38  ? C CYS 32  ? 1_555 FE1 ? N SF4 . ? C SF4 401 ? 1_555 S4  ? N SF4 .   ? C SF4 401 ? 1_555 109.8 ? 
77  S2 ? N SF4 .   ? C SF4 401 ? 1_555 FE1 ? N SF4 . ? C SF4 401 ? 1_555 S4  ? N SF4 .   ? C SF4 401 ? 1_555 109.3 ? 
78  S3 ? N SF4 .   ? C SF4 401 ? 1_555 FE1 ? N SF4 . ? C SF4 401 ? 1_555 S4  ? N SF4 .   ? C SF4 401 ? 1_555 104.5 ? 
79  SG ? C CYS 42  ? C CYS 36  ? 1_555 FE4 ? N SF4 . ? C SF4 401 ? 1_555 S1  ? N SF4 .   ? C SF4 401 ? 1_555 116.8 ? 
80  SG ? C CYS 42  ? C CYS 36  ? 1_555 FE4 ? N SF4 . ? C SF4 401 ? 1_555 S2  ? N SF4 .   ? C SF4 401 ? 1_555 115.7 ? 
81  S1 ? N SF4 .   ? C SF4 401 ? 1_555 FE4 ? N SF4 . ? C SF4 401 ? 1_555 S2  ? N SF4 .   ? C SF4 401 ? 1_555 103.8 ? 
82  SG ? C CYS 42  ? C CYS 36  ? 1_555 FE4 ? N SF4 . ? C SF4 401 ? 1_555 S3  ? N SF4 .   ? C SF4 401 ? 1_555 109.5 ? 
83  S1 ? N SF4 .   ? C SF4 401 ? 1_555 FE4 ? N SF4 . ? C SF4 401 ? 1_555 S3  ? N SF4 .   ? C SF4 401 ? 1_555 105.4 ? 
84  S2 ? N SF4 .   ? C SF4 401 ? 1_555 FE4 ? N SF4 . ? C SF4 401 ? 1_555 S3  ? N SF4 .   ? C SF4 401 ? 1_555 104.4 ? 
85  SG ? C CYS 45  ? C CYS 39  ? 1_555 FE2 ? N SF4 . ? C SF4 401 ? 1_555 S1  ? N SF4 .   ? C SF4 401 ? 1_555 121.1 ? 
86  SG ? C CYS 45  ? C CYS 39  ? 1_555 FE2 ? N SF4 . ? C SF4 401 ? 1_555 S3  ? N SF4 .   ? C SF4 401 ? 1_555 103.8 ? 
87  S1 ? N SF4 .   ? C SF4 401 ? 1_555 FE2 ? N SF4 . ? C SF4 401 ? 1_555 S3  ? N SF4 .   ? C SF4 401 ? 1_555 103.3 ? 
88  SG ? C CYS 45  ? C CYS 39  ? 1_555 FE2 ? N SF4 . ? C SF4 401 ? 1_555 S4  ? N SF4 .   ? C SF4 401 ? 1_555 117.0 ? 
89  S1 ? N SF4 .   ? C SF4 401 ? 1_555 FE2 ? N SF4 . ? C SF4 401 ? 1_555 S4  ? N SF4 .   ? C SF4 401 ? 1_555 104.7 ? 
90  S3 ? N SF4 .   ? C SF4 401 ? 1_555 FE2 ? N SF4 . ? C SF4 401 ? 1_555 S4  ? N SF4 .   ? C SF4 401 ? 1_555 104.9 ? 
91  O  ? C GLY 123 ? C GLY 117 ? 1_555 MG  ? R MG  . ? C MG  405 ? 1_555 O   ? C ILE 126 ? C ILE 120 ? 1_555 75.3  ? 
92  O  ? C GLY 123 ? C GLY 117 ? 1_555 MG  ? R MG  . ? C MG  405 ? 1_555 O   ? C ASP 166 ? C ASP 160 ? 1_555 128.2 ? 
93  O  ? C ILE 126 ? C ILE 120 ? 1_555 MG  ? R MG  . ? C MG  405 ? 1_555 O   ? C ASP 166 ? C ASP 160 ? 1_555 108.0 ? 
94  N  ? O SAM .   ? C SAM 402 ? 1_555 FE3 ? N SF4 . ? C SF4 401 ? 1_555 S1  ? N SF4 .   ? C SF4 401 ? 1_555 162.5 ? 
95  N  ? O SAM .   ? C SAM 402 ? 1_555 FE3 ? N SF4 . ? C SF4 401 ? 1_555 S2  ? N SF4 .   ? C SF4 401 ? 1_555 94.1  ? 
96  S1 ? N SF4 .   ? C SF4 401 ? 1_555 FE3 ? N SF4 . ? C SF4 401 ? 1_555 S2  ? N SF4 .   ? C SF4 401 ? 1_555 101.5 ? 
97  N  ? O SAM .   ? C SAM 402 ? 1_555 FE3 ? N SF4 . ? C SF4 401 ? 1_555 S4  ? N SF4 .   ? C SF4 401 ? 1_555 86.3  ? 
98  S1 ? N SF4 .   ? C SF4 401 ? 1_555 FE3 ? N SF4 . ? C SF4 401 ? 1_555 S4  ? N SF4 .   ? C SF4 401 ? 1_555 97.6  ? 
99  S2 ? N SF4 .   ? C SF4 401 ? 1_555 FE3 ? N SF4 . ? C SF4 401 ? 1_555 S4  ? N SF4 .   ? C SF4 401 ? 1_555 103.0 ? 
100 N  ? O SAM .   ? C SAM 402 ? 1_555 FE3 ? N SF4 . ? C SF4 401 ? 1_555 O   ? O SAM .   ? C SAM 402 ? 1_555 72.8  ? 
101 S1 ? N SF4 .   ? C SF4 401 ? 1_555 FE3 ? N SF4 . ? C SF4 401 ? 1_555 O   ? O SAM .   ? C SAM 402 ? 1_555 97.4  ? 
102 S2 ? N SF4 .   ? C SF4 401 ? 1_555 FE3 ? N SF4 . ? C SF4 401 ? 1_555 O   ? O SAM .   ? C SAM 402 ? 1_555 96.7  ? 
103 S4 ? N SF4 .   ? C SF4 401 ? 1_555 FE3 ? N SF4 . ? C SF4 401 ? 1_555 O   ? O SAM .   ? C SAM 402 ? 1_555 152.3 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 79 A . ? GLY 73 A GLY 80 A ? GLY 74 A 1 14.73 
2 GLY 79 B . ? GLY 73 B GLY 80 B ? GLY 74 B 1 19.01 
3 GLY 79 C . ? GLY 73 C GLY 80 C ? GLY 74 C 1 12.23 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 8 ? 
AA4 ? 2 ? 
AA5 ? 8 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? parallel      
AA5 7 8 ? parallel      
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 240 ? GLU A 243 ? LEU A 234 GLU A 237 
AA1 2 ARG A 195 ? GLN A 200 ? ARG A 189 GLN A 194 
AA1 3 LYS A 168 ? VAL A 175 ? LYS A 162 VAL A 169 
AA1 4 ILE A 128 ? SER A 132 ? ILE A 122 SER A 126 
AA1 5 SER A 104 ? THR A 109 ? SER A 98  THR A 103 
AA1 6 LYS A 74  ? ALA A 78  ? LYS A 68  ALA A 72  
AA1 7 SER A 29  ? HIS A 33  ? SER A 23  HIS A 27  
AA1 8 ILE A 254 ? LEU A 255 ? ILE A 248 LEU A 249 
AA2 1 ARG A 260 ? ASN A 263 ? ARG A 254 ASN A 257 
AA2 2 ASP A 270 ? SER A 274 ? ASP A 264 SER A 268 
AA3 1 LEU B 240 ? GLU B 243 ? LEU B 234 GLU B 237 
AA3 2 ARG B 195 ? GLN B 200 ? ARG B 189 GLN B 194 
AA3 3 LYS B 168 ? VAL B 175 ? LYS B 162 VAL B 169 
AA3 4 ILE B 128 ? SER B 132 ? ILE B 122 SER B 126 
AA3 5 SER B 104 ? THR B 109 ? SER B 98  THR B 103 
AA3 6 LYS B 74  ? ALA B 78  ? LYS B 68  ALA B 72  
AA3 7 SER B 29  ? HIS B 33  ? SER B 23  HIS B 27  
AA3 8 LEU B 253 ? LEU B 255 ? LEU B 247 LEU B 249 
AA4 1 ARG B 260 ? ASN B 263 ? ARG B 254 ASN B 257 
AA4 2 ASP B 270 ? SER B 274 ? ASP B 264 SER B 268 
AA5 1 LEU C 240 ? GLU C 243 ? LEU C 234 GLU C 237 
AA5 2 ARG C 195 ? GLN C 200 ? ARG C 189 GLN C 194 
AA5 3 LYS C 168 ? VAL C 175 ? LYS C 162 VAL C 169 
AA5 4 ILE C 128 ? SER C 132 ? ILE C 122 SER C 126 
AA5 5 SER C 104 ? THR C 109 ? SER C 98  THR C 103 
AA5 6 LYS C 74  ? ALA C 78  ? LYS C 68  ALA C 72  
AA5 7 SER C 29  ? HIS C 33  ? SER C 23  HIS C 27  
AA5 8 ILE C 254 ? LEU C 255 ? ILE C 248 LEU C 249 
AA6 1 ARG C 260 ? ASN C 263 ? ARG C 254 ASN C 257 
AA6 2 ASP C 270 ? SER C 274 ? ASP C 264 SER C 268 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 241 ? O VAL A 235 N TRP A 196 ? N TRP A 190 
AA1 2 3 O PHE A 199 ? O PHE A 193 N VAL A 175 ? N VAL A 169 
AA1 3 4 O LYS A 170 ? O LYS A 164 N LEU A 129 ? N LEU A 123 
AA1 4 5 O ALA A 130 ? O ALA A 124 N ILE A 107 ? N ILE A 101 
AA1 5 6 O SER A 106 ? O SER A 100 N ILE A 75  ? N ILE A 69  
AA1 6 7 O ASN A 76  ? O ASN A 70  N TYR A 32  ? N TYR A 26  
AA1 7 8 N ASN A 31  ? N ASN A 25  O LEU A 255 ? O LEU A 249 
AA2 1 2 N ASN A 263 ? N ASN A 257 O ASP A 270 ? O ASP A 264 
AA3 1 2 O VAL B 241 ? O VAL B 235 N TRP B 196 ? N TRP B 190 
AA3 2 3 O LYS B 197 ? O LYS B 191 N THR B 173 ? N THR B 167 
AA3 3 4 O LYS B 168 ? O LYS B 162 N LEU B 129 ? N LEU B 123 
AA3 4 5 O ALA B 130 ? O ALA B 124 N ILE B 107 ? N ILE B 101 
AA3 5 6 O SER B 106 ? O SER B 100 N ILE B 75  ? N ILE B 69  
AA3 6 7 O ASN B 76  ? O ASN B 70  N TYR B 32  ? N TYR B 26  
AA3 7 8 N ASN B 31  ? N ASN B 25  O LEU B 255 ? O LEU B 249 
AA4 1 2 N ASN B 263 ? N ASN B 257 O ASP B 270 ? O ASP B 264 
AA5 1 2 O GLU C 243 ? O GLU C 237 N CYS C 198 ? N CYS C 192 
AA5 2 3 O PHE C 199 ? O PHE C 193 N VAL C 175 ? N VAL C 169 
AA5 3 4 O LYS C 170 ? O LYS C 164 N LEU C 129 ? N LEU C 123 
AA5 4 5 O ALA C 130 ? O ALA C 124 N ILE C 107 ? N ILE C 101 
AA5 5 6 O SER C 106 ? O SER C 100 N ILE C 75  ? N ILE C 69  
AA5 6 7 O ASN C 76  ? O ASN C 70  N TYR C 32  ? N TYR C 26  
AA5 7 8 N ASN C 31  ? N ASN C 25  O LEU C 255 ? O LEU C 249 
AA6 1 2 N ASN C 263 ? N ASN C 257 O ASP C 270 ? O ASP C 264 
# 
_pdbx_entry_details.entry_id                   9DFW 
_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   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   C 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    29 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   C 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    501 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.07 
# 
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 SER A 266 ? ? -69.33  -174.56 
2 1 ASN B 202 ? ? -141.97 29.11   
3 1 ASP C 144 ? ? -93.90  58.43   
4 1 ASP C 160 ? ? 70.68   41.38   
# 
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 -5  ? A MET 1   
2  1 Y 1 A HIS -4  ? A HIS 2   
3  1 Y 1 A HIS -3  ? A HIS 3   
4  1 Y 1 A HIS -2  ? A HIS 4   
5  1 Y 1 A HIS -1  ? A HIS 5   
6  1 Y 1 A HIS 0   ? A HIS 6   
7  1 Y 1 A HIS 1   ? A HIS 7   
8  1 Y 1 A SER 2   ? A SER 8   
9  1 Y 1 A SER 3   ? A SER 9   
10 1 Y 1 A GLY 4   ? A GLY 10  
11 1 Y 1 A VAL 5   ? A VAL 11  
12 1 Y 1 A ASP 6   ? A ASP 12  
13 1 Y 1 A LEU 7   ? A LEU 13  
14 1 Y 1 A GLY 8   ? A GLY 14  
15 1 Y 1 A THR 9   ? A THR 15  
16 1 Y 1 A GLU 10  ? A GLU 16  
17 1 Y 1 A ASN 11  ? A ASN 17  
18 1 Y 1 A LEU 12  ? A LEU 18  
19 1 Y 1 A TYR 13  ? A TYR 19  
20 1 Y 1 A PHE 14  ? A PHE 20  
21 1 Y 1 A GLN 15  ? A GLN 21  
22 1 Y 1 A SER 16  ? A SER 22  
23 1 Y 1 A MET 17  ? A MET 23  
24 1 Y 1 A CYS 302 ? A CYS 308 
25 1 Y 1 A SER 303 ? A SER 309 
26 1 Y 1 A SER 304 ? A SER 310 
27 1 Y 1 A ASP 305 ? A ASP 311 
28 1 Y 1 A SER 306 ? A SER 312 
29 1 Y 1 A LYS 307 ? A LYS 313 
30 1 Y 1 A ASP 308 ? A ASP 314 
31 1 Y 1 A LEU 309 ? A LEU 315 
32 1 Y 1 A GLU 310 ? A GLU 316 
33 1 Y 1 A TRP 311 ? A TRP 317 
34 1 Y 1 B MET -5  ? B MET 1   
35 1 Y 1 B HIS -4  ? B HIS 2   
36 1 Y 1 B HIS -3  ? B HIS 3   
37 1 Y 1 B HIS -2  ? B HIS 4   
38 1 Y 1 B HIS -1  ? B HIS 5   
39 1 Y 1 B HIS 0   ? B HIS 6   
40 1 Y 1 B HIS 1   ? B HIS 7   
41 1 Y 1 B SER 2   ? B SER 8   
42 1 Y 1 B SER 3   ? B SER 9   
43 1 Y 1 B GLY 4   ? B GLY 10  
44 1 Y 1 B VAL 5   ? B VAL 11  
45 1 Y 1 B ASP 6   ? B ASP 12  
46 1 Y 1 B LEU 7   ? B LEU 13  
47 1 Y 1 B GLY 8   ? B GLY 14  
48 1 Y 1 B THR 9   ? B THR 15  
49 1 Y 1 B GLU 10  ? B GLU 16  
50 1 Y 1 B ASN 11  ? B ASN 17  
51 1 Y 1 B LEU 12  ? B LEU 18  
52 1 Y 1 B TYR 13  ? B TYR 19  
53 1 Y 1 B PHE 14  ? B PHE 20  
54 1 Y 1 B GLN 15  ? B GLN 21  
55 1 Y 1 B SER 16  ? B SER 22  
56 1 Y 1 B MET 17  ? B MET 23  
57 1 Y 1 C MET -5  ? C MET 1   
58 1 Y 1 C HIS -4  ? C HIS 2   
59 1 Y 1 C HIS -3  ? C HIS 3   
60 1 Y 1 C HIS -2  ? C HIS 4   
61 1 Y 1 C HIS -1  ? C HIS 5   
62 1 Y 1 C HIS 0   ? C HIS 6   
63 1 Y 1 C HIS 1   ? C HIS 7   
64 1 Y 1 C SER 2   ? C SER 8   
65 1 Y 1 C SER 3   ? C SER 9   
66 1 Y 1 C GLY 4   ? C GLY 10  
67 1 Y 1 C VAL 5   ? C VAL 11  
68 1 Y 1 C ASP 6   ? C ASP 12  
69 1 Y 1 C LEU 7   ? C LEU 13  
70 1 Y 1 C GLY 8   ? C GLY 14  
71 1 Y 1 C THR 9   ? C THR 15  
72 1 Y 1 C GLU 10  ? C GLU 16  
73 1 Y 1 C ASN 11  ? C ASN 17  
74 1 Y 1 C LEU 12  ? C LEU 18  
75 1 Y 1 C TYR 13  ? C TYR 19  
76 1 Y 1 C PHE 14  ? C PHE 20  
77 1 Y 1 C GLN 15  ? C GLN 21  
78 1 Y 1 C SER 16  ? C SER 22  
79 1 Y 1 C MET 17  ? C MET 23  
80 1 Y 1 C SER 301 ? C SER 307 
81 1 Y 1 C CYS 302 ? C CYS 308 
82 1 Y 1 C SER 303 ? C SER 309 
83 1 Y 1 C SER 304 ? C SER 310 
84 1 Y 1 C ASP 305 ? C ASP 311 
85 1 Y 1 C SER 306 ? C SER 312 
86 1 Y 1 C LYS 307 ? C LYS 313 
87 1 Y 1 C ASP 308 ? C ASP 314 
88 1 Y 1 C LEU 309 ? C LEU 315 
89 1 Y 1 C GLU 310 ? C GLU 316 
90 1 Y 1 C TRP 311 ? C TRP 317 
# 
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  
CTP N1     N  N N 74  
CTP C2     C  N N 75  
CTP N3     N  N N 76  
CTP C4     C  N N 77  
CTP C5     C  N N 78  
CTP C6     C  N N 79  
CTP O2     O  N N 80  
CTP N4     N  N N 81  
CTP "C1'"  C  N R 82  
CTP "C2'"  C  N R 83  
CTP "O2'"  O  N N 84  
CTP "C3'"  C  N S 85  
CTP "C4'"  C  N R 86  
CTP "O4'"  O  N N 87  
CTP "O3'"  O  N N 88  
CTP "C5'"  C  N N 89  
CTP "O5'"  O  N N 90  
CTP PA     P  N S 91  
CTP O1A    O  N N 92  
CTP O2A    O  N N 93  
CTP O3A    O  N N 94  
CTP PB     P  N R 95  
CTP O1B    O  N N 96  
CTP O2B    O  N N 97  
CTP O3B    O  N N 98  
CTP PG     P  N N 99  
CTP O1G    O  N N 100 
CTP O2G    O  N N 101 
CTP O3G    O  N N 102 
CTP H5     H  N N 103 
CTP H6     H  N N 104 
CTP HN41   H  N N 105 
CTP HN42   H  N N 106 
CTP "H1'"  H  N N 107 
CTP "H2'"  H  N N 108 
CTP "HO2'" H  N N 109 
CTP "H3'"  H  N N 110 
CTP "H4'"  H  N N 111 
CTP "HO3'" H  N N 112 
CTP "H5'1" H  N N 113 
CTP "H5'2" H  N N 114 
CTP HOA2   H  N N 115 
CTP HOB2   H  N N 116 
CTP HOG2   H  N N 117 
CTP HOG3   H  N N 118 
CYS N      N  N N 119 
CYS CA     C  N R 120 
CYS C      C  N N 121 
CYS O      O  N N 122 
CYS CB     C  N N 123 
CYS SG     S  N N 124 
CYS OXT    O  N N 125 
CYS H      H  N N 126 
CYS H2     H  N N 127 
CYS HA     H  N N 128 
CYS HB2    H  N N 129 
CYS HB3    H  N N 130 
CYS HG     H  N N 131 
CYS HXT    H  N N 132 
EPE N1     N  N N 133 
EPE C2     C  N N 134 
EPE C3     C  N N 135 
EPE N4     N  N N 136 
EPE C5     C  N N 137 
EPE C6     C  N N 138 
EPE C7     C  N N 139 
EPE C8     C  N N 140 
EPE O8     O  N N 141 
EPE C9     C  N N 142 
EPE C10    C  N N 143 
EPE S      S  N N 144 
EPE O1S    O  N N 145 
EPE O2S    O  N N 146 
EPE O3S    O  N N 147 
EPE H21    H  N N 148 
EPE H22    H  N N 149 
EPE H31    H  N N 150 
EPE H32    H  N N 151 
EPE H51    H  N N 152 
EPE H52    H  N N 153 
EPE H61    H  N N 154 
EPE H62    H  N N 155 
EPE H71    H  N N 156 
EPE H72    H  N N 157 
EPE H81    H  N N 158 
EPE H82    H  N N 159 
EPE HO8    H  N N 160 
EPE H91    H  N N 161 
EPE H92    H  N N 162 
EPE H101   H  N N 163 
EPE H102   H  N N 164 
EPE HOS3   H  N N 165 
GLN N      N  N N 166 
GLN CA     C  N S 167 
GLN C      C  N N 168 
GLN O      O  N N 169 
GLN CB     C  N N 170 
GLN CG     C  N N 171 
GLN CD     C  N N 172 
GLN OE1    O  N N 173 
GLN NE2    N  N N 174 
GLN OXT    O  N N 175 
GLN H      H  N N 176 
GLN H2     H  N N 177 
GLN HA     H  N N 178 
GLN HB2    H  N N 179 
GLN HB3    H  N N 180 
GLN HG2    H  N N 181 
GLN HG3    H  N N 182 
GLN HE21   H  N N 183 
GLN HE22   H  N N 184 
GLN HXT    H  N N 185 
GLU N      N  N N 186 
GLU CA     C  N S 187 
GLU C      C  N N 188 
GLU O      O  N N 189 
GLU CB     C  N N 190 
GLU CG     C  N N 191 
GLU CD     C  N N 192 
GLU OE1    O  N N 193 
GLU OE2    O  N N 194 
GLU OXT    O  N N 195 
GLU H      H  N N 196 
GLU H2     H  N N 197 
GLU HA     H  N N 198 
GLU HB2    H  N N 199 
GLU HB3    H  N N 200 
GLU HG2    H  N N 201 
GLU HG3    H  N N 202 
GLU HE2    H  N N 203 
GLU HXT    H  N N 204 
GLY N      N  N N 205 
GLY CA     C  N N 206 
GLY C      C  N N 207 
GLY O      O  N N 208 
GLY OXT    O  N N 209 
GLY H      H  N N 210 
GLY H2     H  N N 211 
GLY HA2    H  N N 212 
GLY HA3    H  N N 213 
GLY HXT    H  N N 214 
GOL C1     C  N N 215 
GOL O1     O  N N 216 
GOL C2     C  N N 217 
GOL O2     O  N N 218 
GOL C3     C  N N 219 
GOL O3     O  N N 220 
GOL H11    H  N N 221 
GOL H12    H  N N 222 
GOL HO1    H  N N 223 
GOL H2     H  N N 224 
GOL HO2    H  N N 225 
GOL H31    H  N N 226 
GOL H32    H  N N 227 
GOL HO3    H  N N 228 
HIS N      N  N N 229 
HIS CA     C  N S 230 
HIS C      C  N N 231 
HIS O      O  N N 232 
HIS CB     C  N N 233 
HIS CG     C  Y N 234 
HIS ND1    N  Y N 235 
HIS CD2    C  Y N 236 
HIS CE1    C  Y N 237 
HIS NE2    N  Y N 238 
HIS OXT    O  N N 239 
HIS H      H  N N 240 
HIS H2     H  N N 241 
HIS HA     H  N N 242 
HIS HB2    H  N N 243 
HIS HB3    H  N N 244 
HIS HD1    H  N N 245 
HIS HD2    H  N N 246 
HIS HE1    H  N N 247 
HIS HE2    H  N N 248 
HIS HXT    H  N N 249 
HOH O      O  N N 250 
HOH H1     H  N N 251 
HOH H2     H  N N 252 
ILE N      N  N N 253 
ILE CA     C  N S 254 
ILE C      C  N N 255 
ILE O      O  N N 256 
ILE CB     C  N S 257 
ILE CG1    C  N N 258 
ILE CG2    C  N N 259 
ILE CD1    C  N N 260 
ILE OXT    O  N N 261 
ILE H      H  N N 262 
ILE H2     H  N N 263 
ILE HA     H  N N 264 
ILE HB     H  N N 265 
ILE HG12   H  N N 266 
ILE HG13   H  N N 267 
ILE HG21   H  N N 268 
ILE HG22   H  N N 269 
ILE HG23   H  N N 270 
ILE HD11   H  N N 271 
ILE HD12   H  N N 272 
ILE HD13   H  N N 273 
ILE HXT    H  N N 274 
LEU N      N  N N 275 
LEU CA     C  N S 276 
LEU C      C  N N 277 
LEU O      O  N N 278 
LEU CB     C  N N 279 
LEU CG     C  N N 280 
LEU CD1    C  N N 281 
LEU CD2    C  N N 282 
LEU OXT    O  N N 283 
LEU H      H  N N 284 
LEU H2     H  N N 285 
LEU HA     H  N N 286 
LEU HB2    H  N N 287 
LEU HB3    H  N N 288 
LEU HG     H  N N 289 
LEU HD11   H  N N 290 
LEU HD12   H  N N 291 
LEU HD13   H  N N 292 
LEU HD21   H  N N 293 
LEU HD22   H  N N 294 
LEU HD23   H  N N 295 
LEU HXT    H  N N 296 
LYS N      N  N N 297 
LYS CA     C  N S 298 
LYS C      C  N N 299 
LYS O      O  N N 300 
LYS CB     C  N N 301 
LYS CG     C  N N 302 
LYS CD     C  N N 303 
LYS CE     C  N N 304 
LYS NZ     N  N N 305 
LYS OXT    O  N N 306 
LYS H      H  N N 307 
LYS H2     H  N N 308 
LYS HA     H  N N 309 
LYS HB2    H  N N 310 
LYS HB3    H  N N 311 
LYS HG2    H  N N 312 
LYS HG3    H  N N 313 
LYS HD2    H  N N 314 
LYS HD3    H  N N 315 
LYS HE2    H  N N 316 
LYS HE3    H  N N 317 
LYS HZ1    H  N N 318 
LYS HZ2    H  N N 319 
LYS HZ3    H  N N 320 
LYS HXT    H  N N 321 
MET N      N  N N 322 
MET CA     C  N S 323 
MET C      C  N N 324 
MET O      O  N N 325 
MET CB     C  N N 326 
MET CG     C  N N 327 
MET SD     S  N N 328 
MET CE     C  N N 329 
MET OXT    O  N N 330 
MET H      H  N N 331 
MET H2     H  N N 332 
MET HA     H  N N 333 
MET HB2    H  N N 334 
MET HB3    H  N N 335 
MET HG2    H  N N 336 
MET HG3    H  N N 337 
MET HE1    H  N N 338 
MET HE2    H  N N 339 
MET HE3    H  N N 340 
MET HXT    H  N N 341 
MG  MG     MG N N 342 
PHE N      N  N N 343 
PHE CA     C  N S 344 
PHE C      C  N N 345 
PHE O      O  N N 346 
PHE CB     C  N N 347 
PHE CG     C  Y N 348 
PHE CD1    C  Y N 349 
PHE CD2    C  Y N 350 
PHE CE1    C  Y N 351 
PHE CE2    C  Y N 352 
PHE CZ     C  Y N 353 
PHE OXT    O  N N 354 
PHE H      H  N N 355 
PHE H2     H  N N 356 
PHE HA     H  N N 357 
PHE HB2    H  N N 358 
PHE HB3    H  N N 359 
PHE HD1    H  N N 360 
PHE HD2    H  N N 361 
PHE HE1    H  N N 362 
PHE HE2    H  N N 363 
PHE HZ     H  N N 364 
PHE HXT    H  N N 365 
PRO N      N  N N 366 
PRO CA     C  N S 367 
PRO C      C  N N 368 
PRO O      O  N N 369 
PRO CB     C  N N 370 
PRO CG     C  N N 371 
PRO CD     C  N N 372 
PRO OXT    O  N N 373 
PRO H      H  N N 374 
PRO HA     H  N N 375 
PRO HB2    H  N N 376 
PRO HB3    H  N N 377 
PRO HG2    H  N N 378 
PRO HG3    H  N N 379 
PRO HD2    H  N N 380 
PRO HD3    H  N N 381 
PRO HXT    H  N N 382 
SAM N      N  N N 383 
SAM CA     C  N S 384 
SAM C      C  N N 385 
SAM O      O  N N 386 
SAM OXT    O  N N 387 
SAM CB     C  N N 388 
SAM CG     C  N N 389 
SAM SD     S  N S 390 
SAM CE     C  N N 391 
SAM "C5'"  C  N N 392 
SAM "C4'"  C  N S 393 
SAM "O4'"  O  N N 394 
SAM "C3'"  C  N S 395 
SAM "O3'"  O  N N 396 
SAM "C2'"  C  N R 397 
SAM "O2'"  O  N N 398 
SAM "C1'"  C  N R 399 
SAM N9     N  Y N 400 
SAM C8     C  Y N 401 
SAM N7     N  Y N 402 
SAM C5     C  Y N 403 
SAM C6     C  Y N 404 
SAM N6     N  N N 405 
SAM N1     N  Y N 406 
SAM C2     C  Y N 407 
SAM N3     N  Y N 408 
SAM C4     C  Y N 409 
SAM HN1    H  N N 410 
SAM HN2    H  N N 411 
SAM HA     H  N N 412 
SAM HB1    H  N N 413 
SAM HB2    H  N N 414 
SAM HG1    H  N N 415 
SAM HG2    H  N N 416 
SAM HE1    H  N N 417 
SAM HE2    H  N N 418 
SAM HE3    H  N N 419 
SAM "H5'1" H  N N 420 
SAM "H5'2" H  N N 421 
SAM "H4'"  H  N N 422 
SAM "H3'"  H  N N 423 
SAM "HO3'" H  N N 424 
SAM "H2'"  H  N N 425 
SAM "HO2'" H  N N 426 
SAM "H1'"  H  N N 427 
SAM H8     H  N N 428 
SAM HN61   H  N N 429 
SAM HN62   H  N N 430 
SAM H2     H  N N 431 
SER N      N  N N 432 
SER CA     C  N S 433 
SER C      C  N N 434 
SER O      O  N N 435 
SER CB     C  N N 436 
SER OG     O  N N 437 
SER OXT    O  N N 438 
SER H      H  N N 439 
SER H2     H  N N 440 
SER HA     H  N N 441 
SER HB2    H  N N 442 
SER HB3    H  N N 443 
SER HG     H  N N 444 
SER HXT    H  N N 445 
SF4 FE1    FE N N 446 
SF4 FE2    FE N N 447 
SF4 FE3    FE N N 448 
SF4 FE4    FE N N 449 
SF4 S1     S  N N 450 
SF4 S2     S  N N 451 
SF4 S3     S  N N 452 
SF4 S4     S  N N 453 
THR N      N  N N 454 
THR CA     C  N S 455 
THR C      C  N N 456 
THR O      O  N N 457 
THR CB     C  N R 458 
THR OG1    O  N N 459 
THR CG2    C  N N 460 
THR OXT    O  N N 461 
THR H      H  N N 462 
THR H2     H  N N 463 
THR HA     H  N N 464 
THR HB     H  N N 465 
THR HG1    H  N N 466 
THR HG21   H  N N 467 
THR HG22   H  N N 468 
THR HG23   H  N N 469 
THR HXT    H  N N 470 
TRP N      N  N N 471 
TRP CA     C  N S 472 
TRP C      C  N N 473 
TRP O      O  N N 474 
TRP CB     C  N N 475 
TRP CG     C  Y N 476 
TRP CD1    C  Y N 477 
TRP CD2    C  Y N 478 
TRP NE1    N  Y N 479 
TRP CE2    C  Y N 480 
TRP CE3    C  Y N 481 
TRP CZ2    C  Y N 482 
TRP CZ3    C  Y N 483 
TRP CH2    C  Y N 484 
TRP OXT    O  N N 485 
TRP H      H  N N 486 
TRP H2     H  N N 487 
TRP HA     H  N N 488 
TRP HB2    H  N N 489 
TRP HB3    H  N N 490 
TRP HD1    H  N N 491 
TRP HE1    H  N N 492 
TRP HE3    H  N N 493 
TRP HZ2    H  N N 494 
TRP HZ3    H  N N 495 
TRP HH2    H  N N 496 
TRP HXT    H  N N 497 
TYR N      N  N N 498 
TYR CA     C  N S 499 
TYR C      C  N N 500 
TYR O      O  N N 501 
TYR CB     C  N N 502 
TYR CG     C  Y N 503 
TYR CD1    C  Y N 504 
TYR CD2    C  Y N 505 
TYR CE1    C  Y N 506 
TYR CE2    C  Y N 507 
TYR CZ     C  Y N 508 
TYR OH     O  N N 509 
TYR OXT    O  N N 510 
TYR H      H  N N 511 
TYR H2     H  N N 512 
TYR HA     H  N N 513 
TYR HB2    H  N N 514 
TYR HB3    H  N N 515 
TYR HD1    H  N N 516 
TYR HD2    H  N N 517 
TYR HE1    H  N N 518 
TYR HE2    H  N N 519 
TYR HH     H  N N 520 
TYR HXT    H  N N 521 
VAL N      N  N N 522 
VAL CA     C  N S 523 
VAL C      C  N N 524 
VAL O      O  N N 525 
VAL CB     C  N N 526 
VAL CG1    C  N N 527 
VAL CG2    C  N N 528 
VAL OXT    O  N N 529 
VAL H      H  N N 530 
VAL H2     H  N N 531 
VAL HA     H  N N 532 
VAL HB     H  N N 533 
VAL HG11   H  N N 534 
VAL HG12   H  N N 535 
VAL HG13   H  N N 536 
VAL HG21   H  N N 537 
VAL HG22   H  N N 538 
VAL HG23   H  N N 539 
VAL HXT    H  N N 540 
# 
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  
CTP N1    C2     sing N N 70  
CTP N1    C6     sing N N 71  
CTP N1    "C1'"  sing N N 72  
CTP C2    N3     sing N N 73  
CTP C2    O2     doub N N 74  
CTP N3    C4     doub N N 75  
CTP C4    C5     sing N N 76  
CTP C4    N4     sing N N 77  
CTP C5    C6     doub N N 78  
CTP C5    H5     sing N N 79  
CTP C6    H6     sing N N 80  
CTP N4    HN41   sing N N 81  
CTP N4    HN42   sing N N 82  
CTP "C1'" "C2'"  sing N N 83  
CTP "C1'" "O4'"  sing N N 84  
CTP "C1'" "H1'"  sing N N 85  
CTP "C2'" "O2'"  sing N N 86  
CTP "C2'" "C3'"  sing N N 87  
CTP "C2'" "H2'"  sing N N 88  
CTP "O2'" "HO2'" sing N N 89  
CTP "C3'" "C4'"  sing N N 90  
CTP "C3'" "O3'"  sing N N 91  
CTP "C3'" "H3'"  sing N N 92  
CTP "C4'" "O4'"  sing N N 93  
CTP "C4'" "C5'"  sing N N 94  
CTP "C4'" "H4'"  sing N N 95  
CTP "O3'" "HO3'" sing N N 96  
CTP "C5'" "O5'"  sing N N 97  
CTP "C5'" "H5'1" sing N N 98  
CTP "C5'" "H5'2" sing N N 99  
CTP "O5'" PA     sing N N 100 
CTP PA    O1A    doub N N 101 
CTP PA    O2A    sing N N 102 
CTP PA    O3A    sing N N 103 
CTP O2A   HOA2   sing N N 104 
CTP O3A   PB     sing N N 105 
CTP PB    O1B    doub N N 106 
CTP PB    O2B    sing N N 107 
CTP PB    O3B    sing N N 108 
CTP O2B   HOB2   sing N N 109 
CTP O3B   PG     sing N N 110 
CTP PG    O1G    doub N N 111 
CTP PG    O2G    sing N N 112 
CTP PG    O3G    sing N N 113 
CTP O2G   HOG2   sing N N 114 
CTP O3G   HOG3   sing N N 115 
CYS N     CA     sing N N 116 
CYS N     H      sing N N 117 
CYS N     H2     sing N N 118 
CYS CA    C      sing N N 119 
CYS CA    CB     sing N N 120 
CYS CA    HA     sing N N 121 
CYS C     O      doub N N 122 
CYS C     OXT    sing N N 123 
CYS CB    SG     sing N N 124 
CYS CB    HB2    sing N N 125 
CYS CB    HB3    sing N N 126 
CYS SG    HG     sing N N 127 
CYS OXT   HXT    sing N N 128 
EPE N1    C2     sing N N 129 
EPE N1    C6     sing N N 130 
EPE N1    C9     sing N N 131 
EPE C2    C3     sing N N 132 
EPE C2    H21    sing N N 133 
EPE C2    H22    sing N N 134 
EPE C3    N4     sing N N 135 
EPE C3    H31    sing N N 136 
EPE C3    H32    sing N N 137 
EPE N4    C5     sing N N 138 
EPE N4    C7     sing N N 139 
EPE C5    C6     sing N N 140 
EPE C5    H51    sing N N 141 
EPE C5    H52    sing N N 142 
EPE C6    H61    sing N N 143 
EPE C6    H62    sing N N 144 
EPE C7    C8     sing N N 145 
EPE C7    H71    sing N N 146 
EPE C7    H72    sing N N 147 
EPE C8    O8     sing N N 148 
EPE C8    H81    sing N N 149 
EPE C8    H82    sing N N 150 
EPE O8    HO8    sing N N 151 
EPE C9    C10    sing N N 152 
EPE C9    H91    sing N N 153 
EPE C9    H92    sing N N 154 
EPE C10   S      sing N N 155 
EPE C10   H101   sing N N 156 
EPE C10   H102   sing N N 157 
EPE S     O1S    doub N N 158 
EPE S     O2S    doub N N 159 
EPE S     O3S    sing N N 160 
EPE O3S   HOS3   sing N N 161 
GLN N     CA     sing N N 162 
GLN N     H      sing N N 163 
GLN N     H2     sing N N 164 
GLN CA    C      sing N N 165 
GLN CA    CB     sing N N 166 
GLN CA    HA     sing N N 167 
GLN C     O      doub N N 168 
GLN C     OXT    sing N N 169 
GLN CB    CG     sing N N 170 
GLN CB    HB2    sing N N 171 
GLN CB    HB3    sing N N 172 
GLN CG    CD     sing N N 173 
GLN CG    HG2    sing N N 174 
GLN CG    HG3    sing N N 175 
GLN CD    OE1    doub N N 176 
GLN CD    NE2    sing N N 177 
GLN NE2   HE21   sing N N 178 
GLN NE2   HE22   sing N N 179 
GLN OXT   HXT    sing N N 180 
GLU N     CA     sing N N 181 
GLU N     H      sing N N 182 
GLU N     H2     sing N N 183 
GLU CA    C      sing N N 184 
GLU CA    CB     sing N N 185 
GLU CA    HA     sing N N 186 
GLU C     O      doub N N 187 
GLU C     OXT    sing N N 188 
GLU CB    CG     sing N N 189 
GLU CB    HB2    sing N N 190 
GLU CB    HB3    sing N N 191 
GLU CG    CD     sing N N 192 
GLU CG    HG2    sing N N 193 
GLU CG    HG3    sing N N 194 
GLU CD    OE1    doub N N 195 
GLU CD    OE2    sing N N 196 
GLU OE2   HE2    sing N N 197 
GLU OXT   HXT    sing N N 198 
GLY N     CA     sing N N 199 
GLY N     H      sing N N 200 
GLY N     H2     sing N N 201 
GLY CA    C      sing N N 202 
GLY CA    HA2    sing N N 203 
GLY CA    HA3    sing N N 204 
GLY C     O      doub N N 205 
GLY C     OXT    sing N N 206 
GLY OXT   HXT    sing N N 207 
GOL C1    O1     sing N N 208 
GOL C1    C2     sing N N 209 
GOL C1    H11    sing N N 210 
GOL C1    H12    sing N N 211 
GOL O1    HO1    sing N N 212 
GOL C2    O2     sing N N 213 
GOL C2    C3     sing N N 214 
GOL C2    H2     sing N N 215 
GOL O2    HO2    sing N N 216 
GOL C3    O3     sing N N 217 
GOL C3    H31    sing N N 218 
GOL C3    H32    sing N N 219 
GOL O3    HO3    sing N N 220 
HIS N     CA     sing N N 221 
HIS N     H      sing N N 222 
HIS N     H2     sing N N 223 
HIS CA    C      sing N N 224 
HIS CA    CB     sing N N 225 
HIS CA    HA     sing N N 226 
HIS C     O      doub N N 227 
HIS C     OXT    sing N N 228 
HIS CB    CG     sing N N 229 
HIS CB    HB2    sing N N 230 
HIS CB    HB3    sing N N 231 
HIS CG    ND1    sing Y N 232 
HIS CG    CD2    doub Y N 233 
HIS ND1   CE1    doub Y N 234 
HIS ND1   HD1    sing N N 235 
HIS CD2   NE2    sing Y N 236 
HIS CD2   HD2    sing N N 237 
HIS CE1   NE2    sing Y N 238 
HIS CE1   HE1    sing N N 239 
HIS NE2   HE2    sing N N 240 
HIS OXT   HXT    sing N N 241 
HOH O     H1     sing N N 242 
HOH O     H2     sing N N 243 
ILE N     CA     sing N N 244 
ILE N     H      sing N N 245 
ILE N     H2     sing N N 246 
ILE CA    C      sing N N 247 
ILE CA    CB     sing N N 248 
ILE CA    HA     sing N N 249 
ILE C     O      doub N N 250 
ILE C     OXT    sing N N 251 
ILE CB    CG1    sing N N 252 
ILE CB    CG2    sing N N 253 
ILE CB    HB     sing N N 254 
ILE CG1   CD1    sing N N 255 
ILE CG1   HG12   sing N N 256 
ILE CG1   HG13   sing N N 257 
ILE CG2   HG21   sing N N 258 
ILE CG2   HG22   sing N N 259 
ILE CG2   HG23   sing N N 260 
ILE CD1   HD11   sing N N 261 
ILE CD1   HD12   sing N N 262 
ILE CD1   HD13   sing N N 263 
ILE OXT   HXT    sing N N 264 
LEU N     CA     sing N N 265 
LEU N     H      sing N N 266 
LEU N     H2     sing N N 267 
LEU CA    C      sing N N 268 
LEU CA    CB     sing N N 269 
LEU CA    HA     sing N N 270 
LEU C     O      doub N N 271 
LEU C     OXT    sing N N 272 
LEU CB    CG     sing N N 273 
LEU CB    HB2    sing N N 274 
LEU CB    HB3    sing N N 275 
LEU CG    CD1    sing N N 276 
LEU CG    CD2    sing N N 277 
LEU CG    HG     sing N N 278 
LEU CD1   HD11   sing N N 279 
LEU CD1   HD12   sing N N 280 
LEU CD1   HD13   sing N N 281 
LEU CD2   HD21   sing N N 282 
LEU CD2   HD22   sing N N 283 
LEU CD2   HD23   sing N N 284 
LEU OXT   HXT    sing N N 285 
LYS N     CA     sing N N 286 
LYS N     H      sing N N 287 
LYS N     H2     sing N N 288 
LYS CA    C      sing N N 289 
LYS CA    CB     sing N N 290 
LYS CA    HA     sing N N 291 
LYS C     O      doub N N 292 
LYS C     OXT    sing N N 293 
LYS CB    CG     sing N N 294 
LYS CB    HB2    sing N N 295 
LYS CB    HB3    sing N N 296 
LYS CG    CD     sing N N 297 
LYS CG    HG2    sing N N 298 
LYS CG    HG3    sing N N 299 
LYS CD    CE     sing N N 300 
LYS CD    HD2    sing N N 301 
LYS CD    HD3    sing N N 302 
LYS CE    NZ     sing N N 303 
LYS CE    HE2    sing N N 304 
LYS CE    HE3    sing N N 305 
LYS NZ    HZ1    sing N N 306 
LYS NZ    HZ2    sing N N 307 
LYS NZ    HZ3    sing N N 308 
LYS OXT   HXT    sing N N 309 
MET N     CA     sing N N 310 
MET N     H      sing N N 311 
MET N     H2     sing N N 312 
MET CA    C      sing N N 313 
MET CA    CB     sing N N 314 
MET CA    HA     sing N N 315 
MET C     O      doub N N 316 
MET C     OXT    sing N N 317 
MET CB    CG     sing N N 318 
MET CB    HB2    sing N N 319 
MET CB    HB3    sing N N 320 
MET CG    SD     sing N N 321 
MET CG    HG2    sing N N 322 
MET CG    HG3    sing N N 323 
MET SD    CE     sing N N 324 
MET CE    HE1    sing N N 325 
MET CE    HE2    sing N N 326 
MET CE    HE3    sing N N 327 
MET OXT   HXT    sing N N 328 
PHE N     CA     sing N N 329 
PHE N     H      sing N N 330 
PHE N     H2     sing N N 331 
PHE CA    C      sing N N 332 
PHE CA    CB     sing N N 333 
PHE CA    HA     sing N N 334 
PHE C     O      doub N N 335 
PHE C     OXT    sing N N 336 
PHE CB    CG     sing N N 337 
PHE CB    HB2    sing N N 338 
PHE CB    HB3    sing N N 339 
PHE CG    CD1    doub Y N 340 
PHE CG    CD2    sing Y N 341 
PHE CD1   CE1    sing Y N 342 
PHE CD1   HD1    sing N N 343 
PHE CD2   CE2    doub Y N 344 
PHE CD2   HD2    sing N N 345 
PHE CE1   CZ     doub Y N 346 
PHE CE1   HE1    sing N N 347 
PHE CE2   CZ     sing Y N 348 
PHE CE2   HE2    sing N N 349 
PHE CZ    HZ     sing N N 350 
PHE OXT   HXT    sing N N 351 
PRO N     CA     sing N N 352 
PRO N     CD     sing N N 353 
PRO N     H      sing N N 354 
PRO CA    C      sing N N 355 
PRO CA    CB     sing N N 356 
PRO CA    HA     sing N N 357 
PRO C     O      doub N N 358 
PRO C     OXT    sing N N 359 
PRO CB    CG     sing N N 360 
PRO CB    HB2    sing N N 361 
PRO CB    HB3    sing N N 362 
PRO CG    CD     sing N N 363 
PRO CG    HG2    sing N N 364 
PRO CG    HG3    sing N N 365 
PRO CD    HD2    sing N N 366 
PRO CD    HD3    sing N N 367 
PRO OXT   HXT    sing N N 368 
SAM N     CA     sing N N 369 
SAM N     HN1    sing N N 370 
SAM N     HN2    sing N N 371 
SAM CA    C      sing N N 372 
SAM CA    CB     sing N N 373 
SAM CA    HA     sing N N 374 
SAM C     O      doub N N 375 
SAM C     OXT    sing N N 376 
SAM CB    CG     sing N N 377 
SAM CB    HB1    sing N N 378 
SAM CB    HB2    sing N N 379 
SAM CG    SD     sing N N 380 
SAM CG    HG1    sing N N 381 
SAM CG    HG2    sing N N 382 
SAM SD    CE     sing N N 383 
SAM SD    "C5'"  sing N N 384 
SAM CE    HE1    sing N N 385 
SAM CE    HE2    sing N N 386 
SAM CE    HE3    sing N N 387 
SAM "C5'" "C4'"  sing N N 388 
SAM "C5'" "H5'1" sing N N 389 
SAM "C5'" "H5'2" sing N N 390 
SAM "C4'" "O4'"  sing N N 391 
SAM "C4'" "C3'"  sing N N 392 
SAM "C4'" "H4'"  sing N N 393 
SAM "O4'" "C1'"  sing N N 394 
SAM "C3'" "O3'"  sing N N 395 
SAM "C3'" "C2'"  sing N N 396 
SAM "C3'" "H3'"  sing N N 397 
SAM "O3'" "HO3'" sing N N 398 
SAM "C2'" "O2'"  sing N N 399 
SAM "C2'" "C1'"  sing N N 400 
SAM "C2'" "H2'"  sing N N 401 
SAM "O2'" "HO2'" sing N N 402 
SAM "C1'" N9     sing N N 403 
SAM "C1'" "H1'"  sing N N 404 
SAM N9    C8     sing Y N 405 
SAM N9    C4     sing Y N 406 
SAM C8    N7     doub Y N 407 
SAM C8    H8     sing N N 408 
SAM N7    C5     sing Y N 409 
SAM C5    C6     sing Y N 410 
SAM C5    C4     doub Y N 411 
SAM C6    N6     sing N N 412 
SAM C6    N1     doub Y N 413 
SAM N6    HN61   sing N N 414 
SAM N6    HN62   sing N N 415 
SAM N1    C2     sing Y N 416 
SAM C2    N3     doub Y N 417 
SAM C2    H2     sing N N 418 
SAM N3    C4     sing Y N 419 
SER N     CA     sing N N 420 
SER N     H      sing N N 421 
SER N     H2     sing N N 422 
SER CA    C      sing N N 423 
SER CA    CB     sing N N 424 
SER CA    HA     sing N N 425 
SER C     O      doub N N 426 
SER C     OXT    sing N N 427 
SER CB    OG     sing N N 428 
SER CB    HB2    sing N N 429 
SER CB    HB3    sing N N 430 
SER OG    HG     sing N N 431 
SER OXT   HXT    sing N N 432 
SF4 FE1   S2     sing N N 433 
SF4 FE1   S3     sing N N 434 
SF4 FE1   S4     sing N N 435 
SF4 FE2   S1     sing N N 436 
SF4 FE2   S3     sing N N 437 
SF4 FE2   S4     sing N N 438 
SF4 FE3   S1     sing N N 439 
SF4 FE3   S2     sing N N 440 
SF4 FE3   S4     sing N N 441 
SF4 FE4   S1     sing N N 442 
SF4 FE4   S2     sing N N 443 
SF4 FE4   S3     sing N N 444 
THR N     CA     sing N N 445 
THR N     H      sing N N 446 
THR N     H2     sing N N 447 
THR CA    C      sing N N 448 
THR CA    CB     sing N N 449 
THR CA    HA     sing N N 450 
THR C     O      doub N N 451 
THR C     OXT    sing N N 452 
THR CB    OG1    sing N N 453 
THR CB    CG2    sing N N 454 
THR CB    HB     sing N N 455 
THR OG1   HG1    sing N N 456 
THR CG2   HG21   sing N N 457 
THR CG2   HG22   sing N N 458 
THR CG2   HG23   sing N N 459 
THR OXT   HXT    sing N N 460 
TRP N     CA     sing N N 461 
TRP N     H      sing N N 462 
TRP N     H2     sing N N 463 
TRP CA    C      sing N N 464 
TRP CA    CB     sing N N 465 
TRP CA    HA     sing N N 466 
TRP C     O      doub N N 467 
TRP C     OXT    sing N N 468 
TRP CB    CG     sing N N 469 
TRP CB    HB2    sing N N 470 
TRP CB    HB3    sing N N 471 
TRP CG    CD1    doub Y N 472 
TRP CG    CD2    sing Y N 473 
TRP CD1   NE1    sing Y N 474 
TRP CD1   HD1    sing N N 475 
TRP CD2   CE2    doub Y N 476 
TRP CD2   CE3    sing Y N 477 
TRP NE1   CE2    sing Y N 478 
TRP NE1   HE1    sing N N 479 
TRP CE2   CZ2    sing Y N 480 
TRP CE3   CZ3    doub Y N 481 
TRP CE3   HE3    sing N N 482 
TRP CZ2   CH2    doub Y N 483 
TRP CZ2   HZ2    sing N N 484 
TRP CZ3   CH2    sing Y N 485 
TRP CZ3   HZ3    sing N N 486 
TRP CH2   HH2    sing N N 487 
TRP OXT   HXT    sing N N 488 
TYR N     CA     sing N N 489 
TYR N     H      sing N N 490 
TYR N     H2     sing N N 491 
TYR CA    C      sing N N 492 
TYR CA    CB     sing N N 493 
TYR CA    HA     sing N N 494 
TYR C     O      doub N N 495 
TYR C     OXT    sing N N 496 
TYR CB    CG     sing N N 497 
TYR CB    HB2    sing N N 498 
TYR CB    HB3    sing N N 499 
TYR CG    CD1    doub Y N 500 
TYR CG    CD2    sing Y N 501 
TYR CD1   CE1    sing Y N 502 
TYR CD1   HD1    sing N N 503 
TYR CD2   CE2    doub Y N 504 
TYR CD2   HD2    sing N N 505 
TYR CE1   CZ     doub Y N 506 
TYR CE1   HE1    sing N N 507 
TYR CE2   CZ     sing Y N 508 
TYR CE2   HE2    sing N N 509 
TYR CZ    OH     sing N N 510 
TYR OH    HH     sing N N 511 
TYR OXT   HXT    sing N N 512 
VAL N     CA     sing N N 513 
VAL N     H      sing N N 514 
VAL N     H2     sing N N 515 
VAL CA    C      sing N N 516 
VAL CA    CB     sing N N 517 
VAL CA    HA     sing N N 518 
VAL C     O      doub N N 519 
VAL C     OXT    sing N N 520 
VAL CB    CG1    sing N N 521 
VAL CB    CG2    sing N N 522 
VAL CB    HB     sing N N 523 
VAL CG1   HG11   sing N N 524 
VAL CG1   HG12   sing N N 525 
VAL CG1   HG13   sing N N 526 
VAL CG2   HG21   sing N N 527 
VAL CG2   HG22   sing N N 528 
VAL CG2   HG23   sing N N 529 
VAL OXT   HXT    sing N N 530 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM007491 
_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   7N7I 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DFW 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.011747 
_atom_sites.fract_transf_matrix[1][2]   0.006782 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013564 
_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]   0.009052 
_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  
FE 
MG 
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     . GLY A 1 24  ? 22.506  -1.874  4.809   1.00 41.38 ? 18  GLY A N     1 
ATOM   2    C  CA    . GLY A 1 24  ? 21.514  -0.983  4.182   1.00 37.17 ? 18  GLY A CA    1 
ATOM   3    C  C     . GLY A 1 24  ? 20.109  -1.556  4.325   1.00 36.55 ? 18  GLY A C     1 
ATOM   4    O  O     . GLY A 1 24  ? 19.944  -2.687  4.815   1.00 34.50 ? 18  GLY A O     1 
ATOM   5    N  N     . GLN A 1 25  ? 19.102  -0.814  3.881   1.00 32.64 ? 19  GLN A N     1 
ATOM   6    C  CA    . GLN A 1 25  ? 17.685  -1.201  4.063   1.00 27.32 ? 19  GLN A CA    1 
ATOM   7    C  C     . GLN A 1 25  ? 17.356  -2.368  3.123   1.00 28.18 ? 19  GLN A C     1 
ATOM   8    O  O     . GLN A 1 25  ? 17.980  -2.485  2.063   1.00 30.81 ? 19  GLN A O     1 
ATOM   9    C  CB    . GLN A 1 25  ? 16.788  0.018   3.865   1.00 28.27 ? 19  GLN A CB    1 
ATOM   10   C  CG    . GLN A 1 25  ? 17.082  1.155   4.826   1.00 28.26 ? 19  GLN A CG    1 
ATOM   11   C  CD    . GLN A 1 25  ? 16.191  2.353   4.616   1.00 29.94 ? 19  GLN A CD    1 
ATOM   12   O  OE1   . GLN A 1 25  ? 16.512  3.283   3.861   1.00 27.92 ? 19  GLN A OE1   1 
ATOM   13   N  NE2   . GLN A 1 25  ? 15.094  2.376   5.361   1.00 27.05 ? 19  GLN A NE2   1 
ATOM   14   N  N     . VAL A 1 26  ? 16.448  -3.226  3.563   1.00 26.08 ? 20  VAL A N     1 
ATOM   15   C  CA    . VAL A 1 26  ? 15.898  -4.405  2.846   1.00 28.25 ? 20  VAL A CA    1 
ATOM   16   C  C     . VAL A 1 26  ? 14.622  -3.995  2.125   1.00 26.25 ? 20  VAL A C     1 
ATOM   17   O  O     . VAL A 1 26  ? 13.591  -3.708  2.757   1.00 25.64 ? 20  VAL A O     1 
ATOM   18   C  CB    . VAL A 1 26  ? 15.654  -5.580  3.803   1.00 27.60 ? 20  VAL A CB    1 
ATOM   19   C  CG1   . VAL A 1 26  ? 15.147  -6.797  3.066   1.00 28.72 ? 20  VAL A CG1   1 
ATOM   20   C  CG2   . VAL A 1 26  ? 16.924  -5.905  4.600   1.00 31.87 ? 20  VAL A CG2   1 
ATOM   21   N  N     . PRO A 1 27  ? 14.666  -3.988  0.776   1.00 24.52 ? 21  PRO A N     1 
ATOM   22   C  CA    . PRO A 1 27  ? 13.534  -3.520  -0.020  1.00 23.90 ? 21  PRO A CA    1 
ATOM   23   C  C     . PRO A 1 27  ? 12.412  -4.556  -0.117  1.00 23.90 ? 21  PRO A C     1 
ATOM   24   O  O     . PRO A 1 27  ? 12.194  -5.123  -1.157  1.00 23.20 ? 21  PRO A O     1 
ATOM   25   C  CB    . PRO A 1 27  ? 14.195  -3.247  -1.375  1.00 24.46 ? 21  PRO A CB    1 
ATOM   26   C  CG    . PRO A 1 27  ? 15.273  -4.314  -1.472  1.00 25.66 ? 21  PRO A CG    1 
ATOM   27   C  CD    . PRO A 1 27  ? 15.814  -4.384  -0.060  1.00 24.22 ? 21  PRO A CD    1 
ATOM   28   N  N     . VAL A 1 28  ? 11.654  -4.737  0.955   1.00 22.79 ? 22  VAL A N     1 
ATOM   29   C  CA    . VAL A 1 28  ? 10.751  -5.902  1.099   1.00 21.19 ? 22  VAL A CA    1 
ATOM   30   C  C     . VAL A 1 28  ? 9.548   -5.787  0.140   1.00 21.69 ? 22  VAL A C     1 
ATOM   31   O  O     . VAL A 1 28  ? 8.958   -6.848  -0.240  1.00 20.69 ? 22  VAL A O     1 
ATOM   32   C  CB    . VAL A 1 28  ? 10.294  -6.034  2.559   1.00 23.14 ? 22  VAL A CB    1 
ATOM   33   C  CG1   . VAL A 1 28  ? 9.425   -4.868  2.994   1.00 23.80 ? 22  VAL A CG1   1 
ATOM   34   C  CG2   . VAL A 1 28  ? 9.545   -7.335  2.795   1.00 25.72 ? 22  VAL A CG2   1 
ATOM   35   N  N     . SER A 1 29  ? 9.108   -4.560  -0.166  1.00 20.18 ? 23  SER A N     1 
ATOM   36   C  CA    . SER A 1 29  ? 7.864   -4.308  -0.932  1.00 19.43 ? 23  SER A CA    1 
ATOM   37   C  C     . SER A 1 29  ? 8.129   -3.137  -1.871  1.00 20.04 ? 23  SER A C     1 
ATOM   38   O  O     . SER A 1 29  ? 8.435   -2.066  -1.355  1.00 20.09 ? 23  SER A O     1 
ATOM   39   C  CB    . SER A 1 29  ? 6.709   -3.996  -0.035  1.00 20.07 ? 23  SER A CB    1 
ATOM   40   O  OG    . SER A 1 29  ? 5.514   -4.005  -0.795  1.00 21.30 ? 23  SER A OG    1 
ATOM   41   N  N     . VAL A 1 30  ? 8.138   -3.384  -3.173  1.00 19.56 ? 24  VAL A N     1 
ATOM   42   C  CA    . VAL A 1 30  ? 8.625   -2.406  -4.179  1.00 20.84 ? 24  VAL A CA    1 
ATOM   43   C  C     . VAL A 1 30  ? 7.536   -2.122  -5.203  1.00 18.87 ? 24  VAL A C     1 
ATOM   44   O  O     . VAL A 1 30  ? 6.842   -3.059  -5.628  1.00 19.49 ? 24  VAL A O     1 
ATOM   45   C  CB    . VAL A 1 30  ? 9.908   -2.913  -4.854  1.00 20.90 ? 24  VAL A CB    1 
ATOM   46   C  CG1   . VAL A 1 30  ? 10.356  -2.004  -5.982  1.00 20.54 ? 24  VAL A CG1   1 
ATOM   47   C  CG2   . VAL A 1 30  ? 11.026  -3.094  -3.818  1.00 22.61 ? 24  VAL A CG2   1 
ATOM   48   N  N     . ASN A 1 31  ? 7.422   -0.849  -5.565  1.00 18.11 ? 25  ASN A N     1 
ATOM   49   C  CA    . ASN A 1 31  ? 6.539   -0.352  -6.641  1.00 18.66 ? 25  ASN A CA    1 
ATOM   50   C  C     . ASN A 1 31  ? 7.381   -0.118  -7.895  1.00 18.17 ? 25  ASN A C     1 
ATOM   51   O  O     . ASN A 1 31  ? 8.288   0.731   -7.844  1.00 20.99 ? 25  ASN A O     1 
ATOM   52   C  CB    . ASN A 1 31  ? 5.845   0.923   -6.181  1.00 19.07 ? 25  ASN A CB    1 
ATOM   53   C  CG    . ASN A 1 31  ? 4.597   0.581   -5.414  1.00 21.20 ? 25  ASN A CG    1 
ATOM   54   O  OD1   . ASN A 1 31  ? 3.512   0.526   -6.002  1.00 24.93 ? 25  ASN A OD1   1 
ATOM   55   N  ND2   . ASN A 1 31  ? 4.761   0.281   -4.139  1.00 20.16 ? 25  ASN A ND2   1 
ATOM   56   N  N     . TYR A 1 32  ? 7.091   -0.838  -8.966  1.00 19.35 ? 26  TYR A N     1 
ATOM   57   C  CA    . TYR A 1 32  ? 7.799   -0.682  -10.259 1.00 18.12 ? 26  TYR A CA    1 
ATOM   58   C  C     . TYR A 1 32  ? 6.871   0.087   -11.221 1.00 16.37 ? 26  TYR A C     1 
ATOM   59   O  O     . TYR A 1 32  ? 5.899   -0.443  -11.711 1.00 18.00 ? 26  TYR A O     1 
ATOM   60   C  CB    . TYR A 1 32  ? 8.310   -2.029  -10.768 1.00 20.06 ? 26  TYR A CB    1 
ATOM   61   C  CG    . TYR A 1 32  ? 8.989   -1.986  -12.127 1.00 19.28 ? 26  TYR A CG    1 
ATOM   62   C  CD1   . TYR A 1 32  ? 9.585   -0.840  -12.616 1.00 17.36 ? 26  TYR A CD1   1 
ATOM   63   C  CD2   . TYR A 1 32  ? 9.124   -3.135  -12.891 1.00 18.38 ? 26  TYR A CD2   1 
ATOM   64   C  CE1   . TYR A 1 32  ? 10.276  -0.833  -13.821 1.00 18.42 ? 26  TYR A CE1   1 
ATOM   65   C  CE2   . TYR A 1 32  ? 9.771   -3.135  -14.117 1.00 19.60 ? 26  TYR A CE2   1 
ATOM   66   C  CZ    . TYR A 1 32  ? 10.324  -1.975  -14.606 1.00 19.21 ? 26  TYR A CZ    1 
ATOM   67   O  OH    . TYR A 1 32  ? 10.950  -1.988  -15.822 1.00 21.53 ? 26  TYR A OH    1 
ATOM   68   N  N     . HIS A 1 33  ? 7.082   1.395   -11.299 1.00 16.69 ? 27  HIS A N     1 
ATOM   69   C  CA    . HIS A 1 33  ? 6.391   2.308   -12.248 1.00 17.56 ? 27  HIS A CA    1 
ATOM   70   C  C     . HIS A 1 33  ? 7.070   2.138   -13.622 1.00 16.53 ? 27  HIS A C     1 
ATOM   71   O  O     . HIS A 1 33  ? 7.970   2.955   -13.982 1.00 17.16 ? 27  HIS A O     1 
ATOM   72   C  CB    . HIS A 1 33  ? 6.395   3.731   -11.688 1.00 17.42 ? 27  HIS A CB    1 
ATOM   73   C  CG    . HIS A 1 33  ? 5.623   3.889   -10.432 1.00 20.69 ? 27  HIS A CG    1 
ATOM   74   N  ND1   . HIS A 1 33  ? 4.507   4.707   -10.357 1.00 24.00 ? 27  HIS A ND1   1 
ATOM   75   C  CD2   . HIS A 1 33  ? 5.777   3.338   -9.192  1.00 21.17 ? 27  HIS A CD2   1 
ATOM   76   C  CE1   . HIS A 1 33  ? 3.997   4.623   -9.130  1.00 23.73 ? 27  HIS A CE1   1 
ATOM   77   N  NE2   . HIS A 1 33  ? 4.809   3.879   -8.368  1.00 20.98 ? 27  HIS A NE2   1 
ATOM   78   N  N     . PHE A 1 34  ? 6.765   1.049   -14.309 1.00 17.12 ? 28  PHE A N     1 
ATOM   79   C  CA    . PHE A 1 34  ? 7.604   0.585   -15.449 1.00 17.75 ? 28  PHE A CA    1 
ATOM   80   C  C     . PHE A 1 34  ? 7.373   1.453   -16.692 1.00 18.78 ? 28  PHE A C     1 
ATOM   81   O  O     . PHE A 1 34  ? 8.232   1.396   -17.605 1.00 20.40 ? 28  PHE A O     1 
ATOM   82   C  CB    . PHE A 1 34  ? 7.408   -0.914  -15.701 1.00 17.74 ? 28  PHE A CB    1 
ATOM   83   C  CG    . PHE A 1 34  ? 6.043   -1.276  -16.203 1.00 18.57 ? 28  PHE A CG    1 
ATOM   84   C  CD1   . PHE A 1 34  ? 5.750   -1.154  -17.554 1.00 19.19 ? 28  PHE A CD1   1 
ATOM   85   C  CD2   . PHE A 1 34  ? 5.054   -1.712  -15.330 1.00 18.76 ? 28  PHE A CD2   1 
ATOM   86   C  CE1   . PHE A 1 34  ? 4.507   -1.528  -18.030 1.00 19.97 ? 28  PHE A CE1   1 
ATOM   87   C  CE2   . PHE A 1 34  ? 3.798   -2.028  -15.814 1.00 19.26 ? 28  PHE A CE2   1 
ATOM   88   C  CZ    . PHE A 1 34  ? 3.543   -1.972  -17.162 1.00 18.98 ? 28  PHE A CZ    1 
ATOM   89   N  N     . SER A 1 35  ? 6.301   2.251   -16.740 1.00 16.94 ? 29  SER A N     1 
ATOM   90   C  CA    . SER A 1 35  ? 6.025   3.222   -17.827 1.00 19.49 ? 29  SER A CA    1 
ATOM   91   C  C     . SER A 1 35  ? 5.284   4.417   -17.237 1.00 19.62 ? 29  SER A C     1 
ATOM   92   O  O     . SER A 1 35  ? 4.572   4.213   -16.253 1.00 20.82 ? 29  SER A O     1 
ATOM   93   C  CB    . SER A 1 35  ? 5.182   2.610   -18.920 1.00 22.37 ? 29  SER A CB    1 
ATOM   94   O  OG    . SER A 1 35  ? 4.942   3.589   -19.933 1.00 26.87 ? 29  SER A OG    1 
ATOM   95   N  N     . ARG A 1 36  ? 5.451   5.603   -17.819 1.00 19.13 ? 30  ARG A N     1 
ATOM   96   C  CA    . ARG A 1 36  ? 4.696   6.803   -17.415 1.00 19.55 ? 30  ARG A CA    1 
ATOM   97   C  C     . ARG A 1 36  ? 3.521   7.085   -18.350 1.00 21.08 ? 30  ARG A C     1 
ATOM   98   O  O     . ARG A 1 36  ? 2.781   8.017   -18.058 1.00 20.94 ? 30  ARG A O     1 
ATOM   99   C  CB    . ARG A 1 36  ? 5.688   7.940   -17.307 1.00 19.19 ? 30  ARG A CB    1 
ATOM   100  C  CG    . ARG A 1 36  ? 6.570   7.862   -16.073 1.00 18.96 ? 30  ARG A CG    1 
ATOM   101  C  CD    . ARG A 1 36  ? 7.509   9.043   -16.064 1.00 22.00 ? 30  ARG A CD    1 
ATOM   102  N  NE    . ARG A 1 36  ? 8.255   9.247   -14.832 1.00 22.44 ? 30  ARG A NE    1 
ATOM   103  C  CZ    . ARG A 1 36  ? 7.890   10.054  -13.841 1.00 22.05 ? 30  ARG A CZ    1 
ATOM   104  N  NH1   . ARG A 1 36  ? 6.756   10.743  -13.902 1.00 19.82 ? 30  ARG A NH1   1 
ATOM   105  N  NH2   . ARG A 1 36  ? 8.679   10.191  -12.794 1.00 22.49 ? 30  ARG A NH2   1 
ATOM   106  N  N     . LYS A 1 37  ? 3.309   6.285   -19.392 1.00 22.59 ? 31  LYS A N     1 
ATOM   107  C  CA    . LYS A 1 37  ? 2.199   6.493   -20.357 1.00 23.22 ? 31  LYS A CA    1 
ATOM   108  C  C     . LYS A 1 37  ? 0.864   6.188   -19.676 1.00 21.28 ? 31  LYS A C     1 
ATOM   109  O  O     . LYS A 1 37  ? 0.768   5.206   -18.916 1.00 19.60 ? 31  LYS A O     1 
ATOM   110  C  CB    . LYS A 1 37  ? 2.451   5.595   -21.574 1.00 29.01 ? 31  LYS A CB    1 
ATOM   111  C  CG    . LYS A 1 37  ? 1.500   5.742   -22.749 1.00 43.45 ? 31  LYS A CG    1 
ATOM   112  C  CD    . LYS A 1 37  ? 1.755   4.721   -23.897 1.00 47.14 ? 31  LYS A CD    1 
ATOM   113  C  CE    . LYS A 1 37  ? 0.695   4.804   -24.982 1.00 56.53 ? 31  LYS A CE    1 
ATOM   114  N  NZ    . LYS A 1 37  ? 0.378   3.478   -25.571 1.00 60.77 ? 31  LYS A NZ    1 
ATOM   115  N  N     . CYS A 1 38  ? -0.162  6.973   -19.973 1.00 19.64 ? 32  CYS A N     1 
ATOM   116  C  CA    . CYS A 1 38  ? -1.524  6.752   -19.433 1.00 21.55 ? 32  CYS A CA    1 
ATOM   117  C  C     . CYS A 1 38  ? -2.631  7.210   -20.390 1.00 23.39 ? 32  CYS A C     1 
ATOM   118  O  O     . CYS A 1 38  ? -2.447  8.194   -21.071 1.00 27.79 ? 32  CYS A O     1 
ATOM   119  C  CB    . CYS A 1 38  ? -1.709  7.448   -18.093 1.00 21.34 ? 32  CYS A CB    1 
ATOM   120  S  SG    . CYS A 1 38  ? -3.282  6.978   -17.366 1.00 22.88 ? 32  CYS A SG    1 
ATOM   121  N  N     . ASN A 1 39  ? -3.752  6.492   -20.360 1.00 25.22 ? 33  ASN A N     1 
ATOM   122  C  CA    . ASN A 1 39  ? -4.946  6.771   -21.204 1.00 30.38 ? 33  ASN A CA    1 
ATOM   123  C  C     . ASN A 1 39  ? -5.892  7.813   -20.554 1.00 31.88 ? 33  ASN A C     1 
ATOM   124  O  O     . ASN A 1 39  ? -6.857  8.214   -21.238 1.00 32.30 ? 33  ASN A O     1 
ATOM   125  C  CB    . ASN A 1 39  ? -5.633  5.458   -21.609 1.00 30.96 ? 33  ASN A CB    1 
ATOM   126  C  CG    . ASN A 1 39  ? -6.190  4.618   -20.471 1.00 32.05 ? 33  ASN A CG    1 
ATOM   127  O  OD1   . ASN A 1 39  ? -5.598  4.526   -19.405 1.00 29.26 ? 33  ASN A OD1   1 
ATOM   128  N  ND2   . ASN A 1 39  ? -7.347  4.004   -20.690 1.00 32.34 ? 33  ASN A ND2   1 
ATOM   129  N  N     A LYS A 1 40  ? -5.640  8.255   -19.309 0.47 28.29 ? 34  LYS A N     1 
ATOM   130  N  N     B LYS A 1 40  ? -5.601  8.308   -19.342 0.53 27.14 ? 34  LYS A N     1 
ATOM   131  C  CA    A LYS A 1 40  ? -6.594  9.099   -18.529 0.47 26.57 ? 34  LYS A CA    1 
ATOM   132  C  CA    B LYS A 1 40  ? -6.568  9.137   -18.571 0.53 25.06 ? 34  LYS A CA    1 
ATOM   133  C  C     A LYS A 1 40  ? -5.952  10.454  -18.198 0.47 25.73 ? 34  LYS A C     1 
ATOM   134  C  C     B LYS A 1 40  ? -5.924  10.467  -18.171 0.53 24.89 ? 34  LYS A C     1 
ATOM   135  O  O     A LYS A 1 40  ? -4.801  10.678  -18.602 0.47 25.71 ? 34  LYS A O     1 
ATOM   136  O  O     B LYS A 1 40  ? -4.760  10.704  -18.529 0.53 25.09 ? 34  LYS A O     1 
ATOM   137  C  CB    A LYS A 1 40  ? -7.060  8.368   -17.263 0.47 28.52 ? 34  LYS A CB    1 
ATOM   138  C  CB    B LYS A 1 40  ? -7.118  8.329   -17.389 0.53 25.87 ? 34  LYS A CB    1 
ATOM   139  C  CG    A LYS A 1 40  ? -7.841  7.072   -17.460 0.47 30.01 ? 34  LYS A CG    1 
ATOM   140  C  CG    B LYS A 1 40  ? -8.053  7.169   -17.726 0.53 26.89 ? 34  LYS A CG    1 
ATOM   141  C  CD    A LYS A 1 40  ? -9.012  7.146   -18.409 0.47 32.29 ? 34  LYS A CD    1 
ATOM   142  C  CD    B LYS A 1 40  ? -9.034  7.424   -18.861 0.53 28.85 ? 34  LYS A CD    1 
ATOM   143  C  CE    A LYS A 1 40  ? -9.796  5.851   -18.470 0.47 33.87 ? 34  LYS A CE    1 
ATOM   144  C  CE    B LYS A 1 40  ? -9.643  6.149   -19.397 0.53 31.55 ? 34  LYS A CE    1 
ATOM   145  N  NZ    A LYS A 1 40  ? -10.460 5.528   -17.184 0.47 33.98 ? 34  LYS A NZ    1 
ATOM   146  N  NZ    B LYS A 1 40  ? -10.610 6.432   -20.481 0.53 31.47 ? 34  LYS A NZ    1 
ATOM   147  N  N     . GLU A 1 41  ? -6.697  11.332  -17.515 1.00 23.47 ? 35  GLU A N     1 
ATOM   148  C  CA    . GLU A 1 41  ? -6.378  12.769  -17.335 1.00 26.51 ? 35  GLU A CA    1 
ATOM   149  C  C     . GLU A 1 41  ? -6.610  13.215  -15.881 1.00 21.70 ? 35  GLU A C     1 
ATOM   150  O  O     . GLU A 1 41  ? -6.897  14.404  -15.679 1.00 19.66 ? 35  GLU A O     1 
ATOM   151  C  CB    . GLU A 1 41  ? -7.264  13.588  -18.278 1.00 32.78 ? 35  GLU A CB    1 
ATOM   152  C  CG    . GLU A 1 41  ? -6.955  13.365  -19.751 1.00 44.54 ? 35  GLU A CG    1 
ATOM   153  C  CD    . GLU A 1 41  ? -5.879  14.287  -20.305 1.00 59.57 ? 35  GLU A CD    1 
ATOM   154  O  OE1   . GLU A 1 41  ? -4.722  14.216  -19.828 1.00 58.60 ? 35  GLU A OE1   1 
ATOM   155  O  OE2   . GLU A 1 41  ? -6.210  15.096  -21.200 1.00 73.04 ? 35  GLU A OE2   1 
ATOM   156  N  N     . CYS A 1 42  ? -6.463  12.331  -14.896 1.00 20.25 ? 36  CYS A N     1 
ATOM   157  C  CA    . CYS A 1 42  ? -6.726  12.660  -13.479 1.00 20.75 ? 36  CYS A CA    1 
ATOM   158  C  C     . CYS A 1 42  ? -6.043  13.977  -13.121 1.00 20.74 ? 36  CYS A C     1 
ATOM   159  O  O     . CYS A 1 42  ? -4.817  14.085  -13.271 1.00 17.57 ? 36  CYS A O     1 
ATOM   160  C  CB    . CYS A 1 42  ? -6.212  11.584  -12.540 1.00 21.47 ? 36  CYS A CB    1 
ATOM   161  S  SG    . CYS A 1 42  ? -6.912  10.003  -13.002 1.00 20.45 ? 36  CYS A SG    1 
ATOM   162  N  N     . LEU A 1 43  ? -6.803  14.952  -12.625 1.00 17.78 ? 37  LEU A N     1 
ATOM   163  C  CA    . LEU A 1 43  ? -6.275  16.319  -12.403 1.00 18.76 ? 37  LEU A CA    1 
ATOM   164  C  C     . LEU A 1 43  ? -5.172  16.317  -11.347 1.00 17.62 ? 37  LEU A C     1 
ATOM   165  O  O     . LEU A 1 43  ? -4.388  17.261  -11.364 1.00 21.11 ? 37  LEU A O     1 
ATOM   166  C  CB    . LEU A 1 43  ? -7.406  17.249  -11.950 1.00 19.33 ? 37  LEU A CB    1 
ATOM   167  C  CG    . LEU A 1 43  ? -8.408  17.612  -13.040 1.00 22.61 ? 37  LEU A CG    1 
ATOM   168  C  CD1   . LEU A 1 43  ? -9.508  18.521  -12.483 1.00 24.87 ? 37  LEU A CD1   1 
ATOM   169  C  CD2   . LEU A 1 43  ? -7.701  18.298  -14.197 1.00 24.60 ? 37  LEU A CD2   1 
ATOM   170  N  N     . PHE A 1 44  ? -5.132  15.321  -10.455 1.00 18.03 ? 38  PHE A N     1 
ATOM   171  C  CA    . PHE A 1 44  ? -4.183  15.316  -9.321  1.00 20.57 ? 38  PHE A CA    1 
ATOM   172  C  C     . PHE A 1 44  ? -2.975  14.428  -9.599  1.00 17.94 ? 38  PHE A C     1 
ATOM   173  O  O     . PHE A 1 44  ? -2.081  14.444  -8.766  1.00 18.87 ? 38  PHE A O     1 
ATOM   174  C  CB    . PHE A 1 44  ? -4.889  14.867  -8.043  1.00 21.35 ? 38  PHE A CB    1 
ATOM   175  C  CG    . PHE A 1 44  ? -5.700  13.619  -8.203  1.00 21.20 ? 38  PHE A CG    1 
ATOM   176  C  CD1   . PHE A 1 44  ? -5.100  12.417  -8.522  1.00 22.37 ? 38  PHE A CD1   1 
ATOM   177  C  CD2   . PHE A 1 44  ? -7.073  13.646  -8.010  1.00 23.75 ? 38  PHE A CD2   1 
ATOM   178  C  CE1   . PHE A 1 44  ? -5.854  11.274  -8.693  1.00 24.11 ? 38  PHE A CE1   1 
ATOM   179  C  CE2   . PHE A 1 44  ? -7.830  12.497  -8.168  1.00 24.66 ? 38  PHE A CE2   1 
ATOM   180  C  CZ    . PHE A 1 44  ? -7.218  11.313  -8.495  1.00 27.77 ? 38  PHE A CZ    1 
ATOM   181  N  N     . CYS A 1 45  ? -2.883  13.794  -10.765 1.00 18.98 ? 39  CYS A N     1 
ATOM   182  C  CA    . CYS A 1 45  ? -1.892  12.708  -10.984 1.00 16.23 ? 39  CYS A CA    1 
ATOM   183  C  C     . CYS A 1 45  ? -0.507  13.130  -10.466 1.00 16.10 ? 39  CYS A C     1 
ATOM   184  O  O     . CYS A 1 45  ? 0.052   14.163  -10.936 1.00 16.51 ? 39  CYS A O     1 
ATOM   185  C  CB    . CYS A 1 45  ? -1.831  12.303  -12.439 1.00 17.69 ? 39  CYS A CB    1 
ATOM   186  S  SG    . CYS A 1 45  ? -0.770  10.862  -12.737 1.00 18.52 ? 39  CYS A SG    1 
ATOM   187  N  N     . PHE A 1 46  ? 0.116   12.291  -9.621  1.00 16.53 ? 40  PHE A N     1 
ATOM   188  C  CA    . PHE A 1 46  ? 1.467   12.579  -9.076  1.00 15.13 ? 40  PHE A CA    1 
ATOM   189  C  C     . PHE A 1 46  ? 2.554   11.735  -9.734  1.00 16.32 ? 40  PHE A C     1 
ATOM   190  O  O     . PHE A 1 46  ? 3.687   11.770  -9.229  1.00 17.11 ? 40  PHE A O     1 
ATOM   191  C  CB    . PHE A 1 46  ? 1.567   12.463  -7.562  1.00 15.81 ? 40  PHE A CB    1 
ATOM   192  C  CG    . PHE A 1 46  ? 1.294   11.129  -6.906  1.00 15.37 ? 40  PHE A CG    1 
ATOM   193  C  CD1   . PHE A 1 46  ? 1.169   9.966   -7.626  1.00 15.12 ? 40  PHE A CD1   1 
ATOM   194  C  CD2   . PHE A 1 46  ? 1.195   11.049  -5.530  1.00 16.86 ? 40  PHE A CD2   1 
ATOM   195  C  CE1   . PHE A 1 46  ? 0.930   8.761   -6.971  1.00 16.22 ? 40  PHE A CE1   1 
ATOM   196  C  CE2   . PHE A 1 46  ? 0.943   9.850   -4.885  1.00 17.24 ? 40  PHE A CE2   1 
ATOM   197  C  CZ    . PHE A 1 46  ? 0.828   8.703   -5.614  1.00 17.33 ? 40  PHE A CZ    1 
ATOM   198  N  N     . HIS A 1 47  ? 2.267   11.066  -10.833 1.00 16.20 ? 41  HIS A N     1 
ATOM   199  C  CA    . HIS A 1 47  ? 3.290   10.267  -11.560 1.00 17.18 ? 41  HIS A CA    1 
ATOM   200  C  C     . HIS A 1 47  ? 3.012   10.377  -13.062 1.00 17.61 ? 41  HIS A C     1 
ATOM   201  O  O     . HIS A 1 47  ? 2.429   9.445   -13.632 1.00 18.02 ? 41  HIS A O     1 
ATOM   202  C  CB    . HIS A 1 47  ? 3.326   8.824   -11.067 1.00 15.92 ? 41  HIS A CB    1 
ATOM   203  C  CG    . HIS A 1 47  ? 4.621   8.207   -11.436 1.00 16.49 ? 41  HIS A CG    1 
ATOM   204  N  ND1   . HIS A 1 47  ? 5.716   8.326   -10.599 1.00 18.43 ? 41  HIS A ND1   1 
ATOM   205  C  CD2   . HIS A 1 47  ? 5.013   7.481   -12.500 1.00 18.39 ? 41  HIS A CD2   1 
ATOM   206  C  CE1   . HIS A 1 47  ? 6.746   7.717   -11.183 1.00 19.51 ? 41  HIS A CE1   1 
ATOM   207  N  NE2   . HIS A 1 47  ? 6.334   7.204   -12.347 1.00 17.98 ? 41  HIS A NE2   1 
ATOM   208  N  N     . THR A 1 48  ? 3.378   11.531  -13.630 1.00 19.17 ? 42  THR A N     1 
ATOM   209  C  CA    . THR A 1 48  ? 2.814   12.068  -14.890 1.00 19.55 ? 42  THR A CA    1 
ATOM   210  C  C     . THR A 1 48  ? 3.561   11.525  -16.109 1.00 19.96 ? 42  THR A C     1 
ATOM   211  O  O     . THR A 1 48  ? 4.664   10.963  -15.956 1.00 19.82 ? 42  THR A O     1 
ATOM   212  C  CB    . THR A 1 48  ? 2.805   13.593  -14.855 1.00 18.54 ? 42  THR A CB    1 
ATOM   213  O  OG1   . THR A 1 48  ? 4.111   14.131  -14.677 1.00 21.00 ? 42  THR A OG1   1 
ATOM   214  C  CG2   . THR A 1 48  ? 1.899   14.128  -13.774 1.00 21.12 ? 42  THR A CG2   1 
ATOM   215  N  N     . ALA A 1 49  ? 3.036   11.780  -17.289 1.00 21.09 ? 43  ALA A N     1 
ATOM   216  C  CA    . ALA A 1 49  ? 3.514   11.161  -18.555 1.00 21.95 ? 43  ALA A CA    1 
ATOM   217  C  C     . ALA A 1 49  ? 4.659   11.970  -19.147 1.00 24.82 ? 43  ALA A C     1 
ATOM   218  O  O     . ALA A 1 49  ? 4.510   12.469  -20.269 1.00 27.90 ? 43  ALA A O     1 
ATOM   219  C  CB    . ALA A 1 49  ? 2.384   10.999  -19.504 1.00 21.49 ? 43  ALA A CB    1 
ATOM   220  N  N     . THR A 1 50  ? 5.751   12.113  -18.406 1.00 24.36 ? 44  THR A N     1 
ATOM   221  C  CA    . THR A 1 50  ? 6.910   12.947  -18.804 1.00 26.98 ? 44  THR A CA    1 
ATOM   222  C  C     . THR A 1 50  ? 7.850   12.194  -19.743 1.00 28.09 ? 44  THR A C     1 
ATOM   223  O  O     . THR A 1 50  ? 8.717   12.854  -20.295 1.00 29.81 ? 44  THR A O     1 
ATOM   224  C  CB    . THR A 1 50  ? 7.689   13.416  -17.584 1.00 27.23 ? 44  THR A CB    1 
ATOM   225  O  OG1   . THR A 1 50  ? 7.993   12.255  -16.809 1.00 28.00 ? 44  THR A OG1   1 
ATOM   226  C  CG2   . THR A 1 50  ? 6.905   14.444  -16.793 1.00 30.82 ? 44  THR A CG2   1 
ATOM   227  N  N     . THR A 1 51  ? 7.754   10.869  -19.828 1.00 27.66 ? 45  THR A N     1 
ATOM   228  C  CA    . THR A 1 51  ? 8.565   10.024  -20.746 1.00 29.20 ? 45  THR A CA    1 
ATOM   229  C  C     . THR A 1 51  ? 7.685   8.906   -21.299 1.00 27.13 ? 45  THR A C     1 
ATOM   230  O  O     . THR A 1 51  ? 6.519   8.757   -20.849 1.00 32.48 ? 45  THR A O     1 
ATOM   231  C  CB    . THR A 1 51  ? 9.804   9.414   -20.068 1.00 28.26 ? 45  THR A CB    1 
ATOM   232  O  OG1   . THR A 1 51  ? 9.366   8.346   -19.231 1.00 28.96 ? 45  THR A OG1   1 
ATOM   233  C  CG2   . THR A 1 51  ? 10.635  10.372  -19.249 1.00 27.43 ? 45  THR A CG2   1 
ATOM   234  N  N     . SER A 1 52  ? 8.207   8.139   -22.257 1.00 29.48 ? 46  SER A N     1 
ATOM   235  C  CA    . SER A 1 52  ? 7.528   6.907   -22.730 1.00 30.20 ? 46  SER A CA    1 
ATOM   236  C  C     . SER A 1 52  ? 8.502   5.729   -22.758 1.00 26.57 ? 46  SER A C     1 
ATOM   237  O  O     . SER A 1 52  ? 8.046   4.642   -23.155 1.00 27.03 ? 46  SER A O     1 
ATOM   238  C  CB    . SER A 1 52  ? 6.872   7.119   -24.069 1.00 38.96 ? 46  SER A CB    1 
ATOM   239  O  OG    . SER A 1 52  ? 7.851   7.481   -25.023 1.00 42.66 ? 46  SER A OG    1 
ATOM   240  N  N     . HIS A 1 53  ? 9.729   5.902   -22.249 1.00 26.68 ? 47  HIS A N     1 
ATOM   241  C  CA    . HIS A 1 53  ? 10.699  4.783   -22.093 1.00 25.66 ? 47  HIS A CA    1 
ATOM   242  C  C     . HIS A 1 53  ? 10.103  3.645   -21.232 1.00 25.14 ? 47  HIS A C     1 
ATOM   243  O  O     . HIS A 1 53  ? 9.506   3.919   -20.162 1.00 23.81 ? 47  HIS A O     1 
ATOM   244  C  CB    . HIS A 1 53  ? 12.004  5.302   -21.506 1.00 28.17 ? 47  HIS A CB    1 
ATOM   245  C  CG    . HIS A 1 53  ? 12.956  4.196   -21.212 1.00 31.74 ? 47  HIS A CG    1 
ATOM   246  N  ND1   . HIS A 1 53  ? 13.791  3.647   -22.193 1.00 35.22 ? 47  HIS A ND1   1 
ATOM   247  C  CD2   . HIS A 1 53  ? 13.156  3.468   -20.090 1.00 30.73 ? 47  HIS A CD2   1 
ATOM   248  C  CE1   . HIS A 1 53  ? 14.487  2.655   -21.658 1.00 34.97 ? 47  HIS A CE1   1 
ATOM   249  N  NE2   . HIS A 1 53  ? 14.104  2.515   -20.381 1.00 32.32 ? 47  HIS A NE2   1 
ATOM   250  N  N     . VAL A 1 54  ? 10.279  2.406   -21.679 1.00 23.71 ? 48  VAL A N     1 
ATOM   251  C  CA    . VAL A 1 54  ? 10.022  1.156   -20.917 1.00 23.06 ? 48  VAL A CA    1 
ATOM   252  C  C     . VAL A 1 54  ? 11.245  0.254   -21.103 1.00 26.89 ? 48  VAL A C     1 
ATOM   253  O  O     . VAL A 1 54  ? 11.752  0.181   -22.241 1.00 24.03 ? 48  VAL A O     1 
ATOM   254  C  CB    . VAL A 1 54  ? 8.739   0.444   -21.359 1.00 23.33 ? 48  VAL A CB    1 
ATOM   255  C  CG1   . VAL A 1 54  ? 8.518   -0.816  -20.529 1.00 24.10 ? 48  VAL A CG1   1 
ATOM   256  C  CG2   . VAL A 1 54  ? 7.525   1.358   -21.312 1.00 25.14 ? 48  VAL A CG2   1 
ATOM   257  N  N     . GLU A 1 55  ? 11.715  -0.400  -20.041 1.00 25.58 ? 49  GLU A N     1 
ATOM   258  C  CA    . GLU A 1 55  ? 12.890  -1.307  -20.135 1.00 28.06 ? 49  GLU A CA    1 
ATOM   259  C  C     . GLU A 1 55  ? 12.522  -2.463  -21.056 1.00 26.60 ? 49  GLU A C     1 
ATOM   260  O  O     . GLU A 1 55  ? 11.361  -2.972  -20.998 1.00 24.75 ? 49  GLU A O     1 
ATOM   261  C  CB    . GLU A 1 55  ? 13.358  -1.780  -18.752 1.00 26.49 ? 49  GLU A CB    1 
ATOM   262  C  CG    . GLU A 1 55  ? 14.137  -0.699  -18.002 1.00 30.42 ? 49  GLU A CG    1 
ATOM   263  C  CD    . GLU A 1 55  ? 15.430  -0.222  -18.647 1.00 35.56 ? 49  GLU A CD    1 
ATOM   264  O  OE1   . GLU A 1 55  ? 16.140  -1.059  -19.253 1.00 37.55 ? 49  GLU A OE1   1 
ATOM   265  O  OE2   . GLU A 1 55  ? 15.726  0.993   -18.557 1.00 41.33 ? 49  GLU A OE2   1 
ATOM   266  N  N     . LYS A 1 56  ? 13.480  -2.939  -21.853 1.00 26.07 ? 50  LYS A N     1 
ATOM   267  C  CA    . LYS A 1 56  ? 13.232  -4.209  -22.584 1.00 29.91 ? 50  LYS A CA    1 
ATOM   268  C  C     . LYS A 1 56  ? 13.100  -5.336  -21.561 1.00 28.29 ? 50  LYS A C     1 
ATOM   269  O  O     . LYS A 1 56  ? 13.724  -5.276  -20.507 1.00 28.27 ? 50  LYS A O     1 
ATOM   270  C  CB    . LYS A 1 56  ? 14.338  -4.456  -23.612 1.00 33.83 ? 50  LYS A CB    1 
ATOM   271  C  CG    . LYS A 1 56  ? 15.732  -4.664  -23.049 1.00 36.10 ? 50  LYS A CG    1 
ATOM   272  C  CD    . LYS A 1 56  ? 16.747  -4.791  -24.172 1.00 40.34 ? 50  LYS A CD    1 
ATOM   273  C  CE    . LYS A 1 56  ? 17.937  -5.641  -23.791 1.00 46.37 ? 50  LYS A CE    1 
ATOM   274  N  NZ    . LYS A 1 56  ? 19.154  -5.209  -24.518 1.00 47.02 ? 50  LYS A NZ    1 
ATOM   275  N  N     . PRO A 1 57  ? 12.300  -6.387  -21.842 1.00 28.77 ? 51  PRO A N     1 
ATOM   276  C  CA    . PRO A 1 57  ? 12.026  -7.452  -20.880 1.00 29.74 ? 51  PRO A CA    1 
ATOM   277  C  C     . PRO A 1 57  ? 13.280  -8.082  -20.243 1.00 30.39 ? 51  PRO A C     1 
ATOM   278  O  O     . PRO A 1 57  ? 13.227  -8.350  -19.078 1.00 25.59 ? 51  PRO A O     1 
ATOM   279  C  CB    . PRO A 1 57  ? 11.278  -8.514  -21.699 1.00 33.37 ? 51  PRO A CB    1 
ATOM   280  C  CG    . PRO A 1 57  ? 10.591  -7.704  -22.778 1.00 31.98 ? 51  PRO A CG    1 
ATOM   281  C  CD    . PRO A 1 57  ? 11.582  -6.610  -23.116 1.00 30.95 ? 51  PRO A CD    1 
ATOM   282  N  N     . GLU A 1 58  ? 14.359  -8.299  -20.989 1.00 31.51 ? 52  GLU A N     1 
ATOM   283  C  CA    . GLU A 1 58  ? 15.582  -8.938  -20.418 1.00 34.14 ? 52  GLU A CA    1 
ATOM   284  C  C     . GLU A 1 58  ? 16.134  -8.048  -19.281 1.00 30.92 ? 52  GLU A C     1 
ATOM   285  O  O     . GLU A 1 58  ? 16.578  -8.609  -18.259 1.00 27.24 ? 52  GLU A O     1 
ATOM   286  C  CB    . GLU A 1 58  ? 16.610  -9.221  -21.521 1.00 39.08 ? 52  GLU A CB    1 
ATOM   287  C  CG    . GLU A 1 58  ? 18.060  -9.301  -21.026 1.00 46.19 ? 52  GLU A CG    1 
ATOM   288  C  CD    . GLU A 1 58  ? 19.110  -9.660  -22.081 1.00 59.36 ? 52  GLU A CD    1 
ATOM   289  O  OE1   . GLU A 1 58  ? 19.226  -8.921  -23.096 1.00 58.60 ? 52  GLU A OE1   1 
ATOM   290  O  OE2   . GLU A 1 58  ? 19.814  -10.688 -21.894 1.00 66.00 ? 52  GLU A OE2   1 
ATOM   291  N  N     . ASN A 1 59  ? 16.144  -6.723  -19.466 1.00 26.94 ? 53  ASN A N     1 
ATOM   292  C  CA    . ASN A 1 59  ? 16.624  -5.720  -18.475 1.00 29.94 ? 53  ASN A CA    1 
ATOM   293  C  C     . ASN A 1 59  ? 15.650  -5.713  -17.290 1.00 28.17 ? 53  ASN A C     1 
ATOM   294  O  O     . ASN A 1 59  ? 16.130  -5.724  -16.142 1.00 25.29 ? 53  ASN A O     1 
ATOM   295  C  CB    . ASN A 1 59  ? 16.775  -4.306  -19.060 1.00 29.33 ? 53  ASN A CB    1 
ATOM   296  C  CG    . ASN A 1 59  ? 18.020  -4.084  -19.914 1.00 35.20 ? 53  ASN A CG    1 
ATOM   297  O  OD1   . ASN A 1 59  ? 18.870  -4.962  -20.057 1.00 34.40 ? 53  ASN A OD1   1 
ATOM   298  N  ND2   . ASN A 1 59  ? 18.152  -2.886  -20.464 1.00 32.15 ? 53  ASN A ND2   1 
ATOM   299  N  N     . ALA A 1 60  ? 14.327  -5.681  -17.515 1.00 24.20 ? 54  ALA A N     1 
ATOM   300  C  CA    . ALA A 1 60  ? 13.374  -5.632  -16.386 1.00 23.60 ? 54  ALA A CA    1 
ATOM   301  C  C     . ALA A 1 60  ? 13.547  -6.904  -15.539 1.00 24.57 ? 54  ALA A C     1 
ATOM   302  O  O     . ALA A 1 60  ? 13.533  -6.823  -14.298 1.00 22.67 ? 54  ALA A O     1 
ATOM   303  C  CB    . ALA A 1 60  ? 11.959  -5.476  -16.879 1.00 22.57 ? 54  ALA A CB    1 
ATOM   304  N  N     . LYS A 1 61  ? 13.715  -8.059  -16.186 1.00 25.28 ? 55  LYS A N     1 
ATOM   305  C  CA    . LYS A 1 61  ? 13.848  -9.345  -15.469 1.00 24.64 ? 55  LYS A CA    1 
ATOM   306  C  C     . LYS A 1 61  ? 15.125  -9.315  -14.633 1.00 25.25 ? 55  LYS A C     1 
ATOM   307  O  O     . LYS A 1 61  ? 15.071  -9.776  -13.478 1.00 26.74 ? 55  LYS A O     1 
ATOM   308  C  CB    . LYS A 1 61  ? 13.819  -10.550 -16.416 1.00 26.26 ? 55  LYS A CB    1 
ATOM   309  C  CG    . LYS A 1 61  ? 12.436  -10.822 -16.970 1.00 29.69 ? 55  LYS A CG    1 
ATOM   310  C  CD    . LYS A 1 61  ? 12.254  -12.179 -17.618 1.00 35.47 ? 55  LYS A CD    1 
ATOM   311  C  CE    . LYS A 1 61  ? 12.561  -12.205 -19.088 1.00 41.49 ? 55  LYS A CE    1 
ATOM   312  N  NZ    . LYS A 1 61  ? 12.071  -13.476 -19.679 1.00 43.93 ? 55  LYS A NZ    1 
ATOM   313  N  N     . ARG A 1 62  ? 16.222  -8.832  -15.193 1.00 23.04 ? 56  ARG A N     1 
ATOM   314  C  CA    . ARG A 1 62  ? 17.484  -8.661  -14.437 1.00 26.43 ? 56  ARG A CA    1 
ATOM   315  C  C     . ARG A 1 62  ? 17.228  -7.797  -13.191 1.00 24.34 ? 56  ARG A C     1 
ATOM   316  O  O     . ARG A 1 62  ? 17.649  -8.198  -12.091 1.00 23.76 ? 56  ARG A O     1 
ATOM   317  C  CB    . ARG A 1 62  ? 18.584  -8.047  -15.295 1.00 27.14 ? 56  ARG A CB    1 
ATOM   318  C  CG    . ARG A 1 62  ? 19.909  -7.944  -14.562 1.00 29.89 ? 56  ARG A CG    1 
ATOM   319  C  CD    . ARG A 1 62  ? 21.171  -7.809  -15.398 1.00 32.52 ? 56  ARG A CD    1 
ATOM   320  N  NE    . ARG A 1 62  ? 22.239  -7.842  -14.399 1.00 34.80 ? 56  ARG A NE    1 
ATOM   321  C  CZ    . ARG A 1 62  ? 22.795  -6.793  -13.796 1.00 35.28 ? 56  ARG A CZ    1 
ATOM   322  N  NH1   . ARG A 1 62  ? 22.457  -5.551  -14.109 1.00 34.58 ? 56  ARG A NH1   1 
ATOM   323  N  NH2   . ARG A 1 62  ? 23.725  -7.003  -12.876 1.00 36.32 ? 56  ARG A NH2   1 
ATOM   324  N  N     . GLY A 1 63  ? 16.601  -6.636  -13.341 1.00 22.66 ? 57  GLY A N     1 
ATOM   325  C  CA    . GLY A 1 63  ? 16.305  -5.736  -12.203 1.00 21.83 ? 57  GLY A CA    1 
ATOM   326  C  C     . GLY A 1 63  ? 15.497  -6.403  -11.102 1.00 21.42 ? 57  GLY A C     1 
ATOM   327  O  O     . GLY A 1 63  ? 15.864  -6.264  -9.916  1.00 22.72 ? 57  GLY A O     1 
ATOM   328  N  N     . LEU A 1 64  ? 14.402  -7.065  -11.453 1.00 20.37 ? 58  LEU A N     1 
ATOM   329  C  CA    . LEU A 1 64  ? 13.515  -7.797  -10.527 1.00 22.95 ? 58  LEU A CA    1 
ATOM   330  C  C     . LEU A 1 64  ? 14.296  -8.933  -9.838  1.00 24.00 ? 58  LEU A C     1 
ATOM   331  O  O     . LEU A 1 64  ? 14.071  -9.137  -8.642  1.00 22.34 ? 58  LEU A O     1 
ATOM   332  C  CB    . LEU A 1 64  ? 12.299  -8.349  -11.262 1.00 23.16 ? 58  LEU A CB    1 
ATOM   333  C  CG    . LEU A 1 64  ? 11.321  -7.306  -11.822 1.00 26.76 ? 58  LEU A CG    1 
ATOM   334  C  CD1   . LEU A 1 64  ? 10.310  -7.932  -12.765 1.00 25.92 ? 58  LEU A CD1   1 
ATOM   335  C  CD2   . LEU A 1 64  ? 10.584  -6.611  -10.706 1.00 27.91 ? 58  LEU A CD2   1 
ATOM   336  N  N     . THR A 1 65  ? 15.229  -9.583  -10.545 1.00 25.70 ? 59  THR A N     1 
ATOM   337  C  CA    . THR A 1 65  ? 16.130  -10.610 -9.961  1.00 26.22 ? 59  THR A CA    1 
ATOM   338  C  C     . THR A 1 65  ? 17.012  -9.976  -8.869  1.00 24.97 ? 59  THR A C     1 
ATOM   339  O  O     . THR A 1 65  ? 17.088  -10.555 -7.758  1.00 24.52 ? 59  THR A O     1 
ATOM   340  C  CB    . THR A 1 65  ? 16.963  -11.302 -11.052 1.00 29.82 ? 59  THR A CB    1 
ATOM   341  O  OG1   . THR A 1 65  ? 16.079  -11.963 -11.964 1.00 26.55 ? 59  THR A OG1   1 
ATOM   342  C  CG2   . THR A 1 65  ? 17.933  -12.292 -10.447 1.00 30.91 ? 59  THR A CG2   1 
ATOM   343  N  N     . LEU A 1 66  ? 17.631  -8.830  -9.139  1.00 24.06 ? 60  LEU A N     1 
ATOM   344  C  CA    . LEU A 1 66  ? 18.491  -8.108  -8.169  1.00 23.96 ? 60  LEU A CA    1 
ATOM   345  C  C     . LEU A 1 66  ? 17.649  -7.739  -6.927  1.00 26.90 ? 60  LEU A C     1 
ATOM   346  O  O     . LEU A 1 66  ? 18.161  -7.840  -5.776  1.00 24.54 ? 60  LEU A O     1 
ATOM   347  C  CB    . LEU A 1 66  ? 19.065  -6.849  -8.819  1.00 25.01 ? 60  LEU A CB    1 
ATOM   348  C  CG    . LEU A 1 66  ? 20.003  -7.036  -10.018 1.00 26.15 ? 60  LEU A CG    1 
ATOM   349  C  CD1   . LEU A 1 66  ? 20.538  -5.719  -10.479 1.00 26.65 ? 60  LEU A CD1   1 
ATOM   350  C  CD2   . LEU A 1 66  ? 21.162  -7.982  -9.689  1.00 28.08 ? 60  LEU A CD2   1 
ATOM   351  N  N     . LEU A 1 67  ? 16.412  -7.273  -7.124  1.00 25.58 ? 61  LEU A N     1 
ATOM   352  C  CA    . LEU A 1 67  ? 15.519  -6.933  -5.987  1.00 24.03 ? 61  LEU A CA    1 
ATOM   353  C  C     . LEU A 1 67  ? 15.195  -8.184  -5.159  1.00 25.20 ? 61  LEU A C     1 
ATOM   354  O  O     . LEU A 1 67  ? 15.271  -8.075  -3.932  1.00 25.02 ? 61  LEU A O     1 
ATOM   355  C  CB    . LEU A 1 67  ? 14.251  -6.256  -6.503  1.00 23.13 ? 61  LEU A CB    1 
ATOM   356  C  CG    . LEU A 1 67  ? 14.471  -4.866  -7.083  1.00 23.71 ? 61  LEU A CG    1 
ATOM   357  C  CD1   . LEU A 1 67  ? 13.219  -4.398  -7.802  1.00 25.53 ? 61  LEU A CD1   1 
ATOM   358  C  CD2   . LEU A 1 67  ? 14.854  -3.876  -6.011  1.00 23.01 ? 61  LEU A CD2   1 
ATOM   359  N  N     . LYS A 1 68  ? 14.841  -9.311  -5.784  1.00 23.78 ? 62  LYS A N     1 
ATOM   360  C  CA    . LYS A 1 68  ? 14.538  -10.591 -5.098  1.00 26.47 ? 62  LYS A CA    1 
ATOM   361  C  C     . LYS A 1 68  ? 15.757  -10.943 -4.233  1.00 26.49 ? 62  LYS A C     1 
ATOM   362  O  O     . LYS A 1 68  ? 15.578  -11.284 -3.056  1.00 28.64 ? 62  LYS A O     1 
ATOM   363  C  CB    . LYS A 1 68  ? 14.209  -11.697 -6.107  1.00 27.59 ? 62  LYS A CB    1 
ATOM   364  C  CG    . LYS A 1 68  ? 14.348  -13.127 -5.593  1.00 33.10 ? 62  LYS A CG    1 
ATOM   365  C  CD    . LYS A 1 68  ? 13.236  -13.476 -4.681  1.00 37.74 ? 62  LYS A CD    1 
ATOM   366  C  CE    . LYS A 1 68  ? 13.396  -14.830 -4.006  1.00 39.54 ? 62  LYS A CE    1 
ATOM   367  N  NZ    . LYS A 1 68  ? 12.069  -15.326 -3.567  1.00 40.22 ? 62  LYS A NZ    1 
ATOM   368  N  N     . GLN A 1 69  ? 16.956  -10.795 -4.778  1.00 27.49 ? 63  GLN A N     1 
ATOM   369  C  CA    . GLN A 1 69  ? 18.211  -11.167 -4.077  1.00 29.11 ? 63  GLN A CA    1 
ATOM   370  C  C     . GLN A 1 69  ? 18.453  -10.239 -2.898  1.00 30.21 ? 63  GLN A C     1 
ATOM   371  O  O     . GLN A 1 69  ? 19.080  -10.696 -1.929  1.00 30.33 ? 63  GLN A O     1 
ATOM   372  C  CB    . GLN A 1 69  ? 19.420  -11.105 -5.002  1.00 27.14 ? 63  GLN A CB    1 
ATOM   373  C  CG    . GLN A 1 69  ? 19.384  -12.249 -5.972  1.00 30.64 ? 63  GLN A CG    1 
ATOM   374  C  CD    . GLN A 1 69  ? 20.385  -12.075 -7.083  1.00 30.10 ? 63  GLN A CD    1 
ATOM   375  O  OE1   . GLN A 1 69  ? 21.258  -11.189 -7.076  1.00 33.79 ? 63  GLN A OE1   1 
ATOM   376  N  NE2   . GLN A 1 69  ? 20.203  -12.924 -8.075  1.00 28.30 ? 63  GLN A NE2   1 
ATOM   377  N  N     . ALA A 1 70  ? 17.955  -9.009  -2.962  1.00 28.85 ? 64  ALA A N     1 
ATOM   378  C  CA    . ALA A 1 70  ? 18.110  -7.998  -1.884  1.00 27.55 ? 64  ALA A CA    1 
ATOM   379  C  C     . ALA A 1 70  ? 17.050  -8.201  -0.794  1.00 26.16 ? 64  ALA A C     1 
ATOM   380  O  O     . ALA A 1 70  ? 17.187  -7.550  0.224   1.00 25.90 ? 64  ALA A O     1 
ATOM   381  C  CB    . ALA A 1 70  ? 18.087  -6.591  -2.463  1.00 27.41 ? 64  ALA A CB    1 
ATOM   382  N  N     . GLY A 1 71  ? 16.057  -9.072  -0.983  1.00 25.21 ? 65  GLY A N     1 
ATOM   383  C  CA    . GLY A 1 71  ? 15.041  -9.454  0.014   1.00 25.22 ? 65  GLY A CA    1 
ATOM   384  C  C     . GLY A 1 71  ? 13.622  -9.007  -0.329  1.00 25.08 ? 65  GLY A C     1 
ATOM   385  O  O     . GLY A 1 71  ? 12.741  -9.088  0.561   1.00 24.34 ? 65  GLY A O     1 
ATOM   386  N  N     . MET A 1 72  ? 13.350  -8.601  -1.584  1.00 24.28 ? 66  MET A N     1 
ATOM   387  C  CA    . MET A 1 72  ? 11.984  -8.250  -2.028  1.00 22.51 ? 66  MET A CA    1 
ATOM   388  C  C     . MET A 1 72  ? 11.063  -9.467  -1.915  1.00 23.21 ? 66  MET A C     1 
ATOM   389  O  O     . MET A 1 72  ? 11.436  -10.546 -2.350  1.00 24.74 ? 66  MET A O     1 
ATOM   390  C  CB    . MET A 1 72  ? 11.975  -7.687  -3.452  1.00 22.21 ? 66  MET A CB    1 
ATOM   391  C  CG    . MET A 1 72  ? 10.589  -7.336  -3.899  1.00 25.90 ? 66  MET A CG    1 
ATOM   392  S  SD    . MET A 1 72  ? 10.565  -6.566  -5.535  1.00 24.87 ? 66  MET A SD    1 
ATOM   393  C  CE    . MET A 1 72  ? 11.048  -7.956  -6.558  1.00 24.31 ? 66  MET A CE    1 
ATOM   394  N  N     . LYS A 1 73  ? 9.932   -9.306  -1.247  1.00 22.07 ? 67  LYS A N     1 
ATOM   395  C  CA    . LYS A 1 73  ? 8.882   -10.336 -1.100  1.00 23.74 ? 67  LYS A CA    1 
ATOM   396  C  C     . LYS A 1 73  ? 7.643   -9.944  -1.901  1.00 22.15 ? 67  LYS A C     1 
ATOM   397  O  O     . LYS A 1 73  ? 6.915   -10.843 -2.302  1.00 21.43 ? 67  LYS A O     1 
ATOM   398  C  CB    . LYS A 1 73  ? 8.522   -10.507 0.371   1.00 28.12 ? 67  LYS A CB    1 
ATOM   399  C  CG    . LYS A 1 73  ? 9.642   -11.056 1.239   1.00 31.88 ? 67  LYS A CG    1 
ATOM   400  C  CD    . LYS A 1 73  ? 9.191   -11.250 2.668   1.00 35.01 ? 67  LYS A CD    1 
ATOM   401  C  CE    . LYS A 1 73  ? 10.143  -12.096 3.490   1.00 41.85 ? 67  LYS A CE    1 
ATOM   402  N  NZ    . LYS A 1 73  ? 10.347  -11.462 4.812   1.00 47.36 ? 67  LYS A NZ    1 
ATOM   403  N  N     . LYS A 1 74  ? 7.386   -8.644  -2.096  1.00 19.91 ? 68  LYS A N     1 
ATOM   404  C  CA    . LYS A 1 74  ? 6.183   -8.157  -2.798  1.00 20.45 ? 68  LYS A CA    1 
ATOM   405  C  C     . LYS A 1 74  ? 6.585   -7.118  -3.851  1.00 18.16 ? 68  LYS A C     1 
ATOM   406  O  O     . LYS A 1 74  ? 7.437   -6.296  -3.591  1.00 17.35 ? 68  LYS A O     1 
ATOM   407  C  CB    . LYS A 1 74  ? 5.174   -7.480  -1.869  1.00 20.81 ? 68  LYS A CB    1 
ATOM   408  C  CG    . LYS A 1 74  ? 3.942   -6.942  -2.590  1.00 21.02 ? 68  LYS A CG    1 
ATOM   409  C  CD    . LYS A 1 74  ? 2.861   -6.487  -1.647  1.00 20.34 ? 68  LYS A CD    1 
ATOM   410  C  CE    . LYS A 1 74  ? 1.590   -6.048  -2.331  1.00 21.64 ? 68  LYS A CE    1 
ATOM   411  N  NZ    . LYS A 1 74  ? 1.718   -4.656  -2.840  1.00 21.47 ? 68  LYS A NZ    1 
ATOM   412  N  N     . ILE A 1 75  ? 6.030   -7.256  -5.036  1.00 18.51 ? 69  ILE A N     1 
ATOM   413  C  CA    . ILE A 1 75  ? 6.236   -6.335  -6.181  1.00 18.38 ? 69  ILE A CA    1 
ATOM   414  C  C     . ILE A 1 75  ? 4.835   -5.860  -6.561  1.00 19.08 ? 69  ILE A C     1 
ATOM   415  O  O     . ILE A 1 75  ? 3.910   -6.699  -6.671  1.00 19.95 ? 69  ILE A O     1 
ATOM   416  C  CB    . ILE A 1 75  ? 7.012   -6.980  -7.365  1.00 20.63 ? 69  ILE A CB    1 
ATOM   417  C  CG1   . ILE A 1 75  ? 7.325   -5.992  -8.496  1.00 24.37 ? 69  ILE A CG1   1 
ATOM   418  C  CG2   . ILE A 1 75  ? 6.264   -8.177  -7.905  1.00 20.77 ? 69  ILE A CG2   1 
ATOM   419  C  CD1   . ILE A 1 75  ? 8.318   -4.942  -8.151  1.00 25.58 ? 69  ILE A CD1   1 
ATOM   420  N  N     . ASN A 1 76  ? 4.688   -4.547  -6.707  1.00 18.03 ? 70  ASN A N     1 
ATOM   421  C  CA    . ASN A 1 76  ? 3.465   -3.891  -7.213  1.00 19.73 ? 70  ASN A CA    1 
ATOM   422  C  C     . ASN A 1 76  ? 3.817   -3.236  -8.557  1.00 19.92 ? 70  ASN A C     1 
ATOM   423  O  O     . ASN A 1 76  ? 4.745   -2.416  -8.614  1.00 18.45 ? 70  ASN A O     1 
ATOM   424  C  CB    . ASN A 1 76  ? 2.907   -2.868  -6.237  1.00 20.99 ? 70  ASN A CB    1 
ATOM   425  C  CG    . ASN A 1 76  ? 1.552   -2.327  -6.673  1.00 21.90 ? 70  ASN A CG    1 
ATOM   426  O  OD1   . ASN A 1 76  ? 0.643   -3.091  -6.988  1.00 20.89 ? 70  ASN A OD1   1 
ATOM   427  N  ND2   . ASN A 1 76  ? 1.386   -1.013  -6.626  1.00 21.70 ? 70  ASN A ND2   1 
ATOM   428  N  N     . PHE A 1 77  ? 3.134   -3.644  -9.630  1.00 18.42 ? 71  PHE A N     1 
ATOM   429  C  CA    . PHE A 1 77  ? 3.318   -3.060  -10.982 1.00 19.02 ? 71  PHE A CA    1 
ATOM   430  C  C     . PHE A 1 77  ? 2.419   -1.840  -11.120 1.00 19.22 ? 71  PHE A C     1 
ATOM   431  O  O     . PHE A 1 77  ? 1.200   -1.961  -10.949 1.00 19.14 ? 71  PHE A O     1 
ATOM   432  C  CB    . PHE A 1 77  ? 3.052   -4.072  -12.090 1.00 18.74 ? 71  PHE A CB    1 
ATOM   433  C  CG    . PHE A 1 77  ? 4.107   -5.138  -12.153 1.00 18.93 ? 71  PHE A CG    1 
ATOM   434  C  CD1   . PHE A 1 77  ? 5.315   -4.901  -12.776 1.00 22.79 ? 71  PHE A CD1   1 
ATOM   435  C  CD2   . PHE A 1 77  ? 3.909   -6.359  -11.529 1.00 21.47 ? 71  PHE A CD2   1 
ATOM   436  C  CE1   . PHE A 1 77  ? 6.297   -5.889  -12.825 1.00 23.51 ? 71  PHE A CE1   1 
ATOM   437  C  CE2   . PHE A 1 77  ? 4.910   -7.317  -11.536 1.00 23.13 ? 71  PHE A CE2   1 
ATOM   438  C  CZ    . PHE A 1 77  ? 6.098   -7.088  -12.177 1.00 22.32 ? 71  PHE A CZ    1 
ATOM   439  N  N     . ALA A 1 78  ? 3.020   -0.684  -11.392 1.00 18.79 ? 72  ALA A N     1 
ATOM   440  C  CA    . ALA A 1 78  ? 2.277   0.592   -11.416 1.00 18.85 ? 72  ALA A CA    1 
ATOM   441  C  C     . ALA A 1 78  ? 2.754   1.414   -12.605 1.00 18.64 ? 72  ALA A C     1 
ATOM   442  O  O     . ALA A 1 78  ? 3.388   0.859   -13.475 1.00 19.72 ? 72  ALA A O     1 
ATOM   443  C  CB    . ALA A 1 78  ? 2.462   1.281   -10.077 1.00 21.41 ? 72  ALA A CB    1 
ATOM   444  N  N     . GLY A 1 79  ? 2.496   2.721   -12.605 1.00 20.12 ? 73  GLY A N     1 
ATOM   445  C  CA    . GLY A 1 79  ? 2.882   3.621   -13.710 1.00 19.46 ? 73  GLY A CA    1 
ATOM   446  C  C     . GLY A 1 79  ? 2.381   5.020   -13.429 1.00 18.68 ? 73  GLY A C     1 
ATOM   447  O  O     . GLY A 1 79  ? 2.477   5.449   -12.283 1.00 20.81 ? 73  GLY A O     1 
ATOM   448  N  N     . GLY A 1 80  ? 1.840   5.718   -14.451 1.00 18.12 ? 74  GLY A N     1 
ATOM   449  C  CA    . GLY A 1 80  ? 1.410   5.172   -15.733 1.00 19.27 ? 74  GLY A CA    1 
ATOM   450  C  C     . GLY A 1 80  ? 0.277   4.169   -15.586 1.00 19.28 ? 74  GLY A C     1 
ATOM   451  O  O     . GLY A 1 80  ? -0.048  3.777   -14.439 1.00 20.23 ? 74  GLY A O     1 
ATOM   452  N  N     . GLU A 1 81  ? -0.304  3.733   -16.695 1.00 18.35 ? 75  GLU A N     1 
ATOM   453  C  CA    . GLU A 1 81  ? -1.341  2.695   -16.717 1.00 18.44 ? 75  GLU A CA    1 
ATOM   454  C  C     . GLU A 1 81  ? -0.707  1.372   -17.123 1.00 21.65 ? 75  GLU A C     1 
ATOM   455  O  O     . GLU A 1 81  ? -0.309  1.210   -18.278 1.00 21.13 ? 75  GLU A O     1 
ATOM   456  C  CB    . GLU A 1 81  ? -2.505  3.096   -17.628 1.00 20.44 ? 75  GLU A CB    1 
ATOM   457  C  CG    . GLU A 1 81  ? -3.555  1.996   -17.689 1.00 20.25 ? 75  GLU A CG    1 
ATOM   458  C  CD    . GLU A 1 81  ? -3.954  1.364   -16.362 1.00 19.90 ? 75  GLU A CD    1 
ATOM   459  O  OE1   . GLU A 1 81  ? -4.198  2.123   -15.381 1.00 20.09 ? 75  GLU A OE1   1 
ATOM   460  O  OE2   . GLU A 1 81  ? -3.975  0.106   -16.268 1.00 21.84 ? 75  GLU A OE2   1 
ATOM   461  N  N     . PRO A 1 82  ? -0.587  0.374   -16.216 1.00 19.79 ? 76  PRO A N     1 
ATOM   462  C  CA    . PRO A 1 82  ? 0.073   -0.880  -16.584 1.00 19.13 ? 76  PRO A CA    1 
ATOM   463  C  C     . PRO A 1 82  ? -0.618  -1.654  -17.703 1.00 20.06 ? 76  PRO A C     1 
ATOM   464  O  O     . PRO A 1 82  ? 0.091   -2.304  -18.440 1.00 19.30 ? 76  PRO A O     1 
ATOM   465  C  CB    . PRO A 1 82  ? 0.055   -1.682  -15.283 1.00 18.34 ? 76  PRO A CB    1 
ATOM   466  C  CG    . PRO A 1 82  ? -0.006  -0.652  -14.205 1.00 19.34 ? 76  PRO A CG    1 
ATOM   467  C  CD    . PRO A 1 82  ? -0.898  0.431   -14.767 1.00 17.98 ? 76  PRO A CD    1 
ATOM   468  N  N     . PHE A 1 83  ? -1.951  -1.567  -17.835 1.00 20.48 ? 77  PHE A N     1 
ATOM   469  C  CA    . PHE A 1 83  ? -2.683  -2.391  -18.835 1.00 21.51 ? 77  PHE A CA    1 
ATOM   470  C  C     . PHE A 1 83  ? -2.605  -1.792  -20.239 1.00 20.18 ? 77  PHE A C     1 
ATOM   471  O  O     . PHE A 1 83  ? -3.163  -2.398  -21.156 1.00 19.94 ? 77  PHE A O     1 
ATOM   472  C  CB    . PHE A 1 83  ? -4.115  -2.667  -18.394 1.00 20.64 ? 77  PHE A CB    1 
ATOM   473  C  CG    . PHE A 1 83  ? -4.191  -3.793  -17.386 1.00 22.26 ? 77  PHE A CG    1 
ATOM   474  C  CD1   . PHE A 1 83  ? -4.084  -3.548  -16.020 1.00 21.12 ? 77  PHE A CD1   1 
ATOM   475  C  CD2   . PHE A 1 83  ? -4.356  -5.104  -17.796 1.00 22.74 ? 77  PHE A CD2   1 
ATOM   476  C  CE1   . PHE A 1 83  ? -4.140  -4.591  -15.108 1.00 23.31 ? 77  PHE A CE1   1 
ATOM   477  C  CE2   . PHE A 1 83  ? -4.389  -6.143  -16.880 1.00 23.87 ? 77  PHE A CE2   1 
ATOM   478  C  CZ    . PHE A 1 83  ? -4.256  -5.894  -15.537 1.00 22.94 ? 77  PHE A CZ    1 
ATOM   479  N  N     . LEU A 1 84  ? -1.885  -0.699  -20.428 1.00 20.39 ? 78  LEU A N     1 
ATOM   480  C  CA    . LEU A 1 84  ? -1.435  -0.279  -21.764 1.00 20.60 ? 78  LEU A CA    1 
ATOM   481  C  C     . LEU A 1 84  ? -0.375  -1.264  -22.279 1.00 22.66 ? 78  LEU A C     1 
ATOM   482  O  O     . LEU A 1 84  ? -0.065  -1.194  -23.475 1.00 23.38 ? 78  LEU A O     1 
ATOM   483  C  CB    . LEU A 1 84  ? -0.833  1.119   -21.681 1.00 20.02 ? 78  LEU A CB    1 
ATOM   484  C  CG    . LEU A 1 84  ? -1.857  2.252   -21.600 1.00 19.68 ? 78  LEU A CG    1 
ATOM   485  C  CD1   . LEU A 1 84  ? -1.161  3.562   -21.343 1.00 20.40 ? 78  LEU A CD1   1 
ATOM   486  C  CD2   . LEU A 1 84  ? -2.694  2.336   -22.870 1.00 23.83 ? 78  LEU A CD2   1 
ATOM   487  N  N     . TYR A 1 85  ? 0.237   -2.072  -21.414 1.00 23.05 ? 79  TYR A N     1 
ATOM   488  C  CA    . TYR A 1 85  ? 1.367   -2.960  -21.814 1.00 21.07 ? 79  TYR A CA    1 
ATOM   489  C  C     . TYR A 1 85  ? 1.112   -4.386  -21.372 1.00 20.56 ? 79  TYR A C     1 
ATOM   490  O  O     . TYR A 1 85  ? 1.870   -4.956  -20.582 1.00 21.49 ? 79  TYR A O     1 
ATOM   491  C  CB    . TYR A 1 85  ? 2.708   -2.512  -21.225 1.00 22.10 ? 79  TYR A CB    1 
ATOM   492  C  CG    . TYR A 1 85  ? 3.130   -1.126  -21.602 1.00 22.51 ? 79  TYR A CG    1 
ATOM   493  C  CD1   . TYR A 1 85  ? 2.597   -0.011  -20.981 1.00 23.51 ? 79  TYR A CD1   1 
ATOM   494  C  CD2   . TYR A 1 85  ? 4.049   -0.928  -22.614 1.00 26.80 ? 79  TYR A CD2   1 
ATOM   495  C  CE1   . TYR A 1 85  ? 2.980   1.265   -21.357 1.00 23.68 ? 79  TYR A CE1   1 
ATOM   496  C  CE2   . TYR A 1 85  ? 4.458   0.338   -22.991 1.00 27.55 ? 79  TYR A CE2   1 
ATOM   497  C  CZ    . TYR A 1 85  ? 3.926   1.439   -22.343 1.00 26.14 ? 79  TYR A CZ    1 
ATOM   498  O  OH    . TYR A 1 85  ? 4.322   2.683   -22.722 1.00 34.84 ? 79  TYR A OH    1 
ATOM   499  N  N     . PRO A 1 86  ? 0.067   -5.028  -21.899 1.00 19.26 ? 80  PRO A N     1 
ATOM   500  C  CA    . PRO A 1 86  ? -0.303  -6.353  -21.428 1.00 19.53 ? 80  PRO A CA    1 
ATOM   501  C  C     . PRO A 1 86  ? 0.740   -7.429  -21.724 1.00 20.45 ? 80  PRO A C     1 
ATOM   502  O  O     . PRO A 1 86  ? 0.809   -8.399  -20.951 1.00 21.68 ? 80  PRO A O     1 
ATOM   503  C  CB    . PRO A 1 86  ? -1.631  -6.631  -22.136 1.00 20.46 ? 80  PRO A CB    1 
ATOM   504  C  CG    . PRO A 1 86  ? -1.621  -5.754  -23.328 1.00 21.20 ? 80  PRO A CG    1 
ATOM   505  C  CD    . PRO A 1 86  ? -0.873  -4.512  -22.896 1.00 21.65 ? 80  PRO A CD    1 
ATOM   506  N  N     . LYS A 1 87  ? 1.467   -7.303  -22.831 1.00 22.65 ? 81  LYS A N     1 
ATOM   507  C  CA    . LYS A 1 87  ? 2.537   -8.264  -23.178 1.00 23.61 ? 81  LYS A CA    1 
ATOM   508  C  C     . LYS A 1 87  ? 3.652   -8.151  -22.132 1.00 23.82 ? 81  LYS A C     1 
ATOM   509  O  O     . LYS A 1 87  ? 3.964   -9.187  -21.471 1.00 24.48 ? 81  LYS A O     1 
ATOM   510  C  CB    . LYS A 1 87  ? 3.143   -8.081  -24.577 1.00 25.95 ? 81  LYS A CB    1 
ATOM   511  C  CG    . LYS A 1 87  ? 3.992   -9.293  -24.949 1.00 28.50 ? 81  LYS A CG    1 
ATOM   512  C  CD    . LYS A 1 87  ? 4.620   -9.237  -26.302 1.00 34.93 ? 81  LYS A CD    1 
ATOM   513  C  CE    . LYS A 1 87  ? 5.422   -10.490 -26.633 1.00 36.41 ? 81  LYS A CE    1 
ATOM   514  N  NZ    . LYS A 1 87  ? 4.596   -11.720 -26.514 1.00 36.49 ? 81  LYS A NZ    1 
ATOM   515  N  N     . PHE A 1 88  ? 4.185   -6.948  -21.914 1.00 21.65 ? 82  PHE A N     1 
ATOM   516  C  CA    . PHE A 1 88  ? 5.224   -6.723  -20.866 1.00 21.43 ? 82  PHE A CA    1 
ATOM   517  C  C     . PHE A 1 88  ? 4.722   -7.182  -19.490 1.00 21.52 ? 82  PHE A C     1 
ATOM   518  O  O     . PHE A 1 88  ? 5.399   -7.883  -18.766 1.00 22.22 ? 82  PHE A O     1 
ATOM   519  C  CB    . PHE A 1 88  ? 5.637   -5.257  -20.889 1.00 21.94 ? 82  PHE A CB    1 
ATOM   520  C  CG    . PHE A 1 88  ? 6.757   -4.888  -19.953 1.00 23.83 ? 82  PHE A CG    1 
ATOM   521  C  CD1   . PHE A 1 88  ? 6.487   -4.532  -18.639 1.00 25.54 ? 82  PHE A CD1   1 
ATOM   522  C  CD2   . PHE A 1 88  ? 8.070   -4.923  -20.366 1.00 25.70 ? 82  PHE A CD2   1 
ATOM   523  C  CE1   . PHE A 1 88  ? 7.506   -4.182  -17.765 1.00 27.78 ? 82  PHE A CE1   1 
ATOM   524  C  CE2   . PHE A 1 88  ? 9.086   -4.560  -19.491 1.00 26.84 ? 82  PHE A CE2   1 
ATOM   525  C  CZ    . PHE A 1 88  ? 8.800   -4.167  -18.201 1.00 27.35 ? 82  PHE A CZ    1 
ATOM   526  N  N     . LEU A 1 89  ? 3.519   -6.777  -19.123 1.00 23.08 ? 83  LEU A N     1 
ATOM   527  C  CA    . LEU A 1 89  ? 2.974   -6.951  -17.775 1.00 22.97 ? 83  LEU A CA    1 
ATOM   528  C  C     . LEU A 1 89  ? 2.807   -8.448  -17.551 1.00 25.14 ? 83  LEU A C     1 
ATOM   529  O  O     . LEU A 1 89  ? 3.316   -8.916  -16.550 1.00 24.86 ? 83  LEU A O     1 
ATOM   530  C  CB    . LEU A 1 89  ? 1.640   -6.222  -17.683 1.00 24.16 ? 83  LEU A CB    1 
ATOM   531  C  CG    . LEU A 1 89  ? 0.964   -6.272  -16.331 1.00 22.27 ? 83  LEU A CG    1 
ATOM   532  C  CD1   . LEU A 1 89  ? 1.852   -5.626  -15.289 1.00 22.92 ? 83  LEU A CD1   1 
ATOM   533  C  CD2   . LEU A 1 89  ? -0.380  -5.572  -16.398 1.00 24.01 ? 83  LEU A CD2   1 
ATOM   534  N  N     . GLY A 1 90  ? 2.184   -9.155  -18.497 1.00 23.10 ? 84  GLY A N     1 
ATOM   535  C  CA    . GLY A 1 90  ? 2.063   -10.629 -18.449 1.00 24.96 ? 84  GLY A CA    1 
ATOM   536  C  C     . GLY A 1 90  ? 3.392   -11.352 -18.297 1.00 25.28 ? 84  GLY A C     1 
ATOM   537  O  O     . GLY A 1 90  ? 3.494   -12.298 -17.452 1.00 26.77 ? 84  GLY A O     1 
ATOM   538  N  N     . GLU A 1 91  ? 4.401   -10.964 -19.069 1.00 26.12 ? 85  GLU A N     1 
ATOM   539  C  CA    . GLU A 1 91  ? 5.750   -11.553 -18.970 1.00 28.06 ? 85  GLU A CA    1 
ATOM   540  C  C     . GLU A 1 91  ? 6.326   -11.346 -17.561 1.00 27.84 ? 85  GLU A C     1 
ATOM   541  O  O     . GLU A 1 91  ? 6.977   -12.282 -17.029 1.00 25.85 ? 85  GLU A O     1 
ATOM   542  C  CB    . GLU A 1 91  ? 6.715   -10.912 -19.958 1.00 30.70 ? 85  GLU A CB    1 
ATOM   543  C  CG    . GLU A 1 91  ? 6.431   -11.269 -21.384 1.00 40.00 ? 85  GLU A CG    1 
ATOM   544  C  CD    . GLU A 1 91  ? 7.387   -10.556 -22.323 1.00 43.49 ? 85  GLU A CD    1 
ATOM   545  O  OE1   . GLU A 1 91  ? 8.488   -11.092 -22.529 1.00 49.26 ? 85  GLU A OE1   1 
ATOM   546  O  OE2   . GLU A 1 91  ? 7.061   -9.421  -22.759 1.00 47.14 ? 85  GLU A OE2   1 
ATOM   547  N  N     . MET A 1 92  ? 6.201   -10.133 -17.010 1.00 24.60 ? 86  MET A N     1 
ATOM   548  C  CA    . MET A 1 92  ? 6.889   -9.810  -15.727 1.00 23.18 ? 86  MET A CA    1 
ATOM   549  C  C     . MET A 1 92  ? 6.151   -10.522 -14.568 1.00 22.15 ? 86  MET A C     1 
ATOM   550  O  O     . MET A 1 92  ? 6.819   -11.096 -13.687 1.00 25.48 ? 86  MET A O     1 
ATOM   551  C  CB    . MET A 1 92  ? 6.957   -8.290  -15.514 1.00 24.56 ? 86  MET A CB    1 
ATOM   552  C  CG    . MET A 1 92  ? 7.841   -7.551  -16.522 1.00 29.69 ? 86  MET A CG    1 
ATOM   553  S  SD    . MET A 1 92  ? 9.486   -8.346  -16.771 1.00 35.68 ? 86  MET A SD    1 
ATOM   554  C  CE    . MET A 1 92  ? 9.404   -8.812  -18.494 1.00 41.21 ? 86  MET A CE    1 
ATOM   555  N  N     . ILE A 1 93  ? 4.817   -10.574 -14.609 1.00 22.47 ? 87  ILE A N     1 
ATOM   556  C  CA    . ILE A 1 93  ? 3.959   -11.235 -13.589 1.00 25.43 ? 87  ILE A CA    1 
ATOM   557  C  C     . ILE A 1 93  ? 4.363   -12.711 -13.549 1.00 28.54 ? 87  ILE A C     1 
ATOM   558  O  O     . ILE A 1 93  ? 4.625   -13.222 -12.465 1.00 27.49 ? 87  ILE A O     1 
ATOM   559  C  CB    . ILE A 1 93  ? 2.475   -11.042 -13.923 1.00 27.93 ? 87  ILE A CB    1 
ATOM   560  C  CG1   . ILE A 1 93  ? 2.011   -9.619  -13.589 1.00 28.36 ? 87  ILE A CG1   1 
ATOM   561  C  CG2   . ILE A 1 93  ? 1.606   -12.093 -13.251 1.00 30.76 ? 87  ILE A CG2   1 
ATOM   562  C  CD1   . ILE A 1 93  ? 0.615   -9.346  -14.131 1.00 32.63 ? 87  ILE A CD1   1 
ATOM   563  N  N     . ASP A 1 94  ? 4.470   -13.350 -14.716 1.00 26.62 ? 88  ASP A N     1 
ATOM   564  C  CA    . ASP A 1 94  ? 4.763   -14.804 -14.810 1.00 27.33 ? 88  ASP A CA    1 
ATOM   565  C  C     . ASP A 1 94  ? 6.193   -15.034 -14.301 1.00 27.30 ? 88  ASP A C     1 
ATOM   566  O  O     . ASP A 1 94  ? 6.453   -16.013 -13.520 1.00 29.92 ? 88  ASP A O     1 
ATOM   567  C  CB    . ASP A 1 94  ? 4.526   -15.309 -16.244 1.00 30.42 ? 88  ASP A CB    1 
ATOM   568  C  CG    . ASP A 1 94  ? 3.093   -15.222 -16.799 1.00 35.96 ? 88  ASP A CG    1 
ATOM   569  O  OD1   . ASP A 1 94  ? 2.114   -14.935 -16.017 1.00 32.13 ? 88  ASP A OD1   1 
ATOM   570  O  OD2   . ASP A 1 94  ? 2.951   -15.407 -18.053 1.00 35.43 ? 88  ASP A OD2   1 
ATOM   571  N  N     . PHE A 1 95  ? 7.127   -14.183 -14.681 1.00 26.09 ? 89  PHE A N     1 
ATOM   572  C  CA    . PHE A 1 95  ? 8.542   -14.306 -14.239 1.00 26.08 ? 89  PHE A CA    1 
ATOM   573  C  C     . PHE A 1 95  ? 8.631   -14.165 -12.707 1.00 29.16 ? 89  PHE A C     1 
ATOM   574  O  O     . PHE A 1 95  ? 9.162   -15.073 -12.046 1.00 28.45 ? 89  PHE A O     1 
ATOM   575  C  CB    . PHE A 1 95  ? 9.413   -13.279 -14.936 1.00 24.16 ? 89  PHE A CB    1 
ATOM   576  C  CG    . PHE A 1 95  ? 10.872  -13.333 -14.566 1.00 24.75 ? 89  PHE A CG    1 
ATOM   577  C  CD1   . PHE A 1 95  ? 11.692  -14.337 -15.071 1.00 26.28 ? 89  PHE A CD1   1 
ATOM   578  C  CD2   . PHE A 1 95  ? 11.436  -12.363 -13.759 1.00 26.40 ? 89  PHE A CD2   1 
ATOM   579  C  CE1   . PHE A 1 95  ? 13.040  -14.362 -14.766 1.00 25.75 ? 89  PHE A CE1   1 
ATOM   580  C  CE2   . PHE A 1 95  ? 12.785  -12.393 -13.444 1.00 30.55 ? 89  PHE A CE2   1 
ATOM   581  C  CZ    . PHE A 1 95  ? 13.591  -13.395 -13.967 1.00 27.89 ? 89  PHE A CZ    1 
ATOM   582  N  N     . CYS A 1 96  ? 8.066   -13.086 -12.137 1.00 25.91 ? 90  CYS A N     1 
ATOM   583  C  CA    . CYS A 1 96  ? 8.087   -12.812 -10.678 1.00 24.23 ? 90  CYS A CA    1 
ATOM   584  C  C     . CYS A 1 96  ? 7.506   -13.968 -9.857  1.00 26.81 ? 90  CYS A C     1 
ATOM   585  O  O     . CYS A 1 96  ? 8.078   -14.248 -8.829  1.00 27.97 ? 90  CYS A O     1 
ATOM   586  C  CB    . CYS A 1 96  ? 7.311   -11.545 -10.359 1.00 25.81 ? 90  CYS A CB    1 
ATOM   587  S  SG    . CYS A 1 96  ? 8.277   -10.112 -10.853 1.00 28.23 ? 90  CYS A SG    1 
ATOM   588  N  N     . LYS A 1 97  ? 6.386   -14.557 -10.271 1.00 28.23 ? 91  LYS A N     1 
ATOM   589  C  CA    . LYS A 1 97  ? 5.696   -15.631 -9.516  1.00 31.95 ? 91  LYS A CA    1 
ATOM   590  C  C     . LYS A 1 97  ? 6.397   -16.966 -9.805  1.00 35.22 ? 91  LYS A C     1 
ATOM   591  O  O     . LYS A 1 97  ? 6.663   -17.677 -8.837  1.00 39.25 ? 91  LYS A O     1 
ATOM   592  C  CB    . LYS A 1 97  ? 4.192   -15.614 -9.791  1.00 34.58 ? 91  LYS A CB    1 
ATOM   593  C  CG    . LYS A 1 97  ? 3.360   -16.594 -8.970  1.00 41.01 ? 91  LYS A CG    1 
ATOM   594  C  CD    . LYS A 1 97  ? 3.597   -16.539 -7.470  1.00 44.61 ? 91  LYS A CD    1 
ATOM   595  C  CE    . LYS A 1 97  ? 3.039   -15.298 -6.814  1.00 43.53 ? 91  LYS A CE    1 
ATOM   596  N  NZ    . LYS A 1 97  ? 2.835   -15.525 -5.358  1.00 41.60 ? 91  LYS A NZ    1 
ATOM   597  N  N     . GLU A 1 98  ? 6.763   -17.272 -11.052 1.00 33.49 ? 92  GLU A N     1 
ATOM   598  C  CA    . GLU A 1 98  ? 7.191   -18.660 -11.408 1.00 37.98 ? 92  GLU A CA    1 
ATOM   599  C  C     . GLU A 1 98  ? 8.701   -18.811 -11.180 1.00 37.41 ? 92  GLU A C     1 
ATOM   600  O  O     . GLU A 1 98  ? 9.113   -19.829 -10.617 1.00 41.72 ? 92  GLU A O     1 
ATOM   601  C  CB    . GLU A 1 98  ? 6.774   -19.024 -12.833 1.00 36.76 ? 92  GLU A CB    1 
ATOM   602  C  CG    . GLU A 1 98  ? 5.276   -19.231 -12.956 1.00 40.57 ? 92  GLU A CG    1 
ATOM   603  C  CD    . GLU A 1 98  ? 4.755   -19.363 -14.384 1.00 47.99 ? 92  GLU A CD    1 
ATOM   604  O  OE1   . GLU A 1 98  ? 5.583   -19.520 -15.318 1.00 55.72 ? 92  GLU A OE1   1 
ATOM   605  O  OE2   . GLU A 1 98  ? 3.521   -19.302 -14.567 1.00 45.17 ? 92  GLU A OE2   1 
ATOM   606  N  N     . THR A 1 99  ? 9.504   -17.851 -11.613 1.00 30.85 ? 93  THR A N     1 
ATOM   607  C  CA    . THR A 1 99  ? 10.978  -17.935 -11.558 1.00 30.17 ? 93  THR A CA    1 
ATOM   608  C  C     . THR A 1 99  ? 11.464  -17.381 -10.214 1.00 33.40 ? 93  THR A C     1 
ATOM   609  O  O     . THR A 1 99  ? 12.248  -18.058 -9.532  1.00 31.28 ? 93  THR A O     1 
ATOM   610  C  CB    . THR A 1 99  ? 11.554  -17.271 -12.809 1.00 33.84 ? 93  THR A CB    1 
ATOM   611  O  OG1   . THR A 1 99  ? 11.009  -18.048 -13.872 1.00 37.77 ? 93  THR A OG1   1 
ATOM   612  C  CG2   . THR A 1 99  ? 13.065  -17.222 -12.835 1.00 33.56 ? 93  THR A CG2   1 
ATOM   613  N  N     . LEU A 1 100 ? 11.038  -16.182 -9.830  1.00 29.52 ? 94  LEU A N     1 
ATOM   614  C  CA    . LEU A 1 100 ? 11.583  -15.503 -8.631  1.00 29.90 ? 94  LEU A CA    1 
ATOM   615  C  C     . LEU A 1 100 ? 10.861  -16.007 -7.380  1.00 29.19 ? 94  LEU A C     1 
ATOM   616  O  O     . LEU A 1 100 ? 11.408  -15.811 -6.294  1.00 31.61 ? 94  LEU A O     1 
ATOM   617  C  CB    . LEU A 1 100 ? 11.414  -13.986 -8.759  1.00 28.33 ? 94  LEU A CB    1 
ATOM   618  C  CG    . LEU A 1 100 ? 12.249  -13.305 -9.843  1.00 29.39 ? 94  LEU A CG    1 
ATOM   619  C  CD1   . LEU A 1 100 ? 12.082  -11.795 -9.732  1.00 29.71 ? 94  LEU A CD1   1 
ATOM   620  C  CD2   . LEU A 1 100 ? 13.734  -13.674 -9.735  1.00 29.71 ? 94  LEU A CD2   1 
ATOM   621  N  N     . GLN A 1 101 ? 9.682   -16.597 -7.533  1.00 29.10 ? 95  GLN A N     1 
ATOM   622  C  CA    . GLN A 1 101 ? 8.898   -17.157 -6.417  1.00 34.18 ? 95  GLN A CA    1 
ATOM   623  C  C     . GLN A 1 101 ? 8.672   -16.064 -5.362  1.00 33.89 ? 95  GLN A C     1 
ATOM   624  O  O     . GLN A 1 101 ? 8.926   -16.326 -4.200  1.00 31.75 ? 95  GLN A O     1 
ATOM   625  C  CB    . GLN A 1 101 ? 9.636   -18.372 -5.854  1.00 38.42 ? 95  GLN A CB    1 
ATOM   626  C  CG    . GLN A 1 101 ? 9.916   -19.419 -6.915  1.00 41.80 ? 95  GLN A CG    1 
ATOM   627  C  CD    . GLN A 1 101 ? 9.962   -20.780 -6.277  1.00 50.82 ? 95  GLN A CD    1 
ATOM   628  O  OE1   . GLN A 1 101 ? 11.031  -21.287 -5.942  1.00 50.97 ? 95  GLN A OE1   1 
ATOM   629  N  NE2   . GLN A 1 101 ? 8.788   -21.345 -6.055  1.00 51.66 ? 95  GLN A NE2   1 
ATOM   630  N  N     . LEU A 1 102 ? 8.215   -14.874 -5.773  1.00 30.93 ? 96  LEU A N     1 
ATOM   631  C  CA    . LEU A 1 102 ? 7.819   -13.785 -4.835  1.00 29.50 ? 96  LEU A CA    1 
ATOM   632  C  C     . LEU A 1 102 ? 6.571   -14.200 -4.065  1.00 27.55 ? 96  LEU A C     1 
ATOM   633  O  O     . LEU A 1 102 ? 5.697   -14.905 -4.613  1.00 26.56 ? 96  LEU A O     1 
ATOM   634  C  CB    . LEU A 1 102 ? 7.569   -12.489 -5.612  1.00 27.93 ? 96  LEU A CB    1 
ATOM   635  C  CG    . LEU A 1 102 ? 8.801   -11.902 -6.276  1.00 32.62 ? 96  LEU A CG    1 
ATOM   636  C  CD1   . LEU A 1 102 ? 8.434   -10.676 -7.092  1.00 35.42 ? 96  LEU A CD1   1 
ATOM   637  C  CD2   . LEU A 1 102 ? 9.854   -11.555 -5.232  1.00 33.96 ? 96  LEU A CD2   1 
ATOM   638  N  N     . GLU A 1 103 ? 6.452   -13.742 -2.827  1.00 28.88 ? 97  GLU A N     1 
ATOM   639  C  CA    . GLU A 1 103 ? 5.258   -14.051 -2.016  1.00 28.95 ? 97  GLU A CA    1 
ATOM   640  C  C     . GLU A 1 103 ? 4.068   -13.334 -2.620  1.00 27.94 ? 97  GLU A C     1 
ATOM   641  O  O     . GLU A 1 103 ? 2.960   -13.848 -2.489  1.00 26.84 ? 97  GLU A O     1 
ATOM   642  C  CB    . GLU A 1 103 ? 5.451   -13.623 -0.561  1.00 31.39 ? 97  GLU A CB    1 
ATOM   643  C  CG    . GLU A 1 103 ? 6.620   -14.305 0.104   1.00 36.11 ? 97  GLU A CG    1 
ATOM   644  C  CD    . GLU A 1 103 ? 6.801   -13.928 1.564   1.00 41.64 ? 97  GLU A CD    1 
ATOM   645  O  OE1   . GLU A 1 103 ? 5.860   -13.281 2.157   1.00 37.30 ? 97  GLU A OE1   1 
ATOM   646  O  OE2   . GLU A 1 103 ? 7.881   -14.276 2.094   1.00 42.09 ? 97  GLU A OE2   1 
ATOM   647  N  N     . SER A 1 104 ? 4.255   -12.133 -3.182  1.00 26.43 ? 98  SER A N     1 
ATOM   648  C  CA    . SER A 1 104 ? 3.081   -11.325 -3.574  1.00 22.83 ? 98  SER A CA    1 
ATOM   649  C  C     . SER A 1 104 ? 3.357   -10.582 -4.870  1.00 22.17 ? 98  SER A C     1 
ATOM   650  O  O     . SER A 1 104 ? 4.361   -9.829  -4.902  1.00 22.61 ? 98  SER A O     1 
ATOM   651  C  CB    . SER A 1 104 ? 2.697   -10.373 -2.494  1.00 23.00 ? 98  SER A CB    1 
ATOM   652  O  OG    . SER A 1 104 ? 1.453   -9.793  -2.830  1.00 23.47 ? 98  SER A OG    1 
ATOM   653  N  N     . VAL A 1 105 ? 2.479   -10.758 -5.860  1.00 22.32 ? 99  VAL A N     1 
ATOM   654  C  CA    . VAL A 1 105 ? 2.553   -9.987  -7.136  1.00 21.92 ? 99  VAL A CA    1 
ATOM   655  C  C     . VAL A 1 105 ? 1.266   -9.203  -7.220  1.00 22.38 ? 99  VAL A C     1 
ATOM   656  O  O     . VAL A 1 105 ? 0.220   -9.839  -7.212  1.00 22.17 ? 99  VAL A O     1 
ATOM   657  C  CB    . VAL A 1 105 ? 2.773   -10.875 -8.378  1.00 24.45 ? 99  VAL A CB    1 
ATOM   658  C  CG1   . VAL A 1 105 ? 2.691   -10.040 -9.651  1.00 25.82 ? 99  VAL A CG1   1 
ATOM   659  C  CG2   . VAL A 1 105 ? 4.102   -11.625 -8.319  1.00 26.05 ? 99  VAL A CG2   1 
ATOM   660  N  N     . SER A 1 106 ? 1.341   -7.871  -7.249  1.00 20.56 ? 100 SER A N     1 
ATOM   661  C  CA    . SER A 1 106 ? 0.137   -7.001  -7.306  1.00 22.00 ? 100 SER A CA    1 
ATOM   662  C  C     . SER A 1 106 ? 0.227   -6.065  -8.516  1.00 19.57 ? 100 SER A C     1 
ATOM   663  O  O     . SER A 1 106 ? 1.338   -5.823  -9.043  1.00 20.30 ? 100 SER A O     1 
ATOM   664  C  CB    . SER A 1 106 ? -0.142  -6.245  -5.999  1.00 21.67 ? 100 SER A CB    1 
ATOM   665  O  OG    . SER A 1 106 ? 0.926   -5.381  -5.615  1.00 24.33 ? 100 SER A OG    1 
ATOM   666  N  N     . ILE A 1 107 ? -0.928  -5.604  -8.968  1.00 20.89 ? 101 ILE A N     1 
ATOM   667  C  CA    . ILE A 1 107 ? -1.024  -4.582  -10.036 1.00 19.19 ? 101 ILE A CA    1 
ATOM   668  C  C     . ILE A 1 107 ? -1.966  -3.489  -9.540  1.00 20.71 ? 101 ILE A C     1 
ATOM   669  O  O     . ILE A 1 107 ? -2.943  -3.808  -8.867  1.00 22.54 ? 101 ILE A O     1 
ATOM   670  C  CB    . ILE A 1 107 ? -1.472  -5.185  -11.376 1.00 21.71 ? 101 ILE A CB    1 
ATOM   671  C  CG1   . ILE A 1 107 ? -0.745  -6.491  -11.703 1.00 23.73 ? 101 ILE A CG1   1 
ATOM   672  C  CG2   . ILE A 1 107 ? -1.291  -4.169  -12.493 1.00 23.16 ? 101 ILE A CG2   1 
ATOM   673  C  CD1   . ILE A 1 107 ? -1.523  -7.343  -12.671 1.00 27.13 ? 101 ILE A CD1   1 
ATOM   674  N  N     . VAL A 1 108 ? -1.645  -2.230  -9.810  1.00 20.74 ? 102 VAL A N     1 
ATOM   675  C  CA    . VAL A 1 108 ? -2.608  -1.120  -9.563  1.00 20.26 ? 102 VAL A CA    1 
ATOM   676  C  C     . VAL A 1 108 ? -3.008  -0.534  -10.926 1.00 19.38 ? 102 VAL A C     1 
ATOM   677  O  O     . VAL A 1 108 ? -2.120  -0.205  -11.710 1.00 19.30 ? 102 VAL A O     1 
ATOM   678  C  CB    . VAL A 1 108 ? -2.056  -0.097  -8.557  1.00 21.29 ? 102 VAL A CB    1 
ATOM   679  C  CG1   . VAL A 1 108 ? -0.707  0.461   -8.965  1.00 23.14 ? 102 VAL A CG1   1 
ATOM   680  C  CG2   . VAL A 1 108 ? -3.065  1.024   -8.326  1.00 19.16 ? 102 VAL A CG2   1 
ATOM   681  N  N     . THR A 1 109 ? -4.309  -0.387  -11.181 1.00 19.48 ? 103 THR A N     1 
ATOM   682  C  CA    . THR A 1 109 ? -4.836  -0.038  -12.515 1.00 20.15 ? 103 THR A CA    1 
ATOM   683  C  C     . THR A 1 109 ? -6.048  0.889   -12.419 1.00 19.61 ? 103 THR A C     1 
ATOM   684  O  O     . THR A 1 109 ? -6.807  0.787   -11.446 1.00 19.73 ? 103 THR A O     1 
ATOM   685  C  CB    . THR A 1 109 ? -5.205  -1.322  -13.285 1.00 24.14 ? 103 THR A CB    1 
ATOM   686  O  OG1   . THR A 1 109 ? -5.710  -0.918  -14.556 1.00 24.36 ? 103 THR A OG1   1 
ATOM   687  C  CG2   . THR A 1 109 ? -6.279  -2.150  -12.614 1.00 23.39 ? 103 THR A CG2   1 
ATOM   688  N  N     . ASN A 1 110 ? -6.265  1.715   -13.449 1.00 18.15 ? 104 ASN A N     1 
ATOM   689  C  CA    . ASN A 1 110 ? -7.480  2.552   -13.546 1.00 19.45 ? 104 ASN A CA    1 
ATOM   690  C  C     . ASN A 1 110 ? -8.639  1.659   -13.997 1.00 21.06 ? 104 ASN A C     1 
ATOM   691  O  O     . ASN A 1 110 ? -9.769  2.153   -14.001 1.00 23.58 ? 104 ASN A O     1 
ATOM   692  C  CB    . ASN A 1 110 ? -7.246  3.809   -14.391 1.00 22.17 ? 104 ASN A CB    1 
ATOM   693  C  CG    . ASN A 1 110 ? -6.999  3.544   -15.865 1.00 25.21 ? 104 ASN A CG    1 
ATOM   694  O  OD1   . ASN A 1 110 ? -7.555  2.579   -16.408 1.00 26.80 ? 104 ASN A OD1   1 
ATOM   695  N  ND2   . ASN A 1 110 ? -6.236  4.423   -16.520 1.00 22.18 ? 104 ASN A ND2   1 
ATOM   696  N  N     . GLY A 1 111 ? -8.356  0.420   -14.434 1.00 22.21 ? 105 GLY A N     1 
ATOM   697  C  CA    . GLY A 1 111 ? -9.378  -0.613  -14.702 1.00 22.62 ? 105 GLY A CA    1 
ATOM   698  C  C     . GLY A 1 111 ? -9.937  -0.575  -16.131 1.00 22.21 ? 105 GLY A C     1 
ATOM   699  O  O     . GLY A 1 111 ? -10.506 -1.617  -16.556 1.00 23.01 ? 105 GLY A O     1 
ATOM   700  N  N     . SER A 1 112 ? -9.787  0.529   -16.852 1.00 20.95 ? 106 SER A N     1 
ATOM   701  C  CA    . SER A 1 112 ? -10.450 0.760   -18.173 1.00 25.36 ? 106 SER A CA    1 
ATOM   702  C  C     . SER A 1 112 ? -9.998  -0.275  -19.219 1.00 25.22 ? 106 SER A C     1 
ATOM   703  O  O     . SER A 1 112 ? -10.829 -0.643  -20.047 1.00 25.93 ? 106 SER A O     1 
ATOM   704  C  CB    . SER A 1 112 ? -10.254 2.171   -18.653 1.00 28.53 ? 106 SER A CB    1 
ATOM   705  O  OG    . SER A 1 112 ? -8.870  2.452   -18.790 1.00 30.91 ? 106 SER A OG    1 
ATOM   706  N  N     . LEU A 1 113 ? -8.765  -0.775  -19.171 1.00 23.28 ? 107 LEU A N     1 
ATOM   707  C  CA    . LEU A 1 113 ? -8.235  -1.653  -20.232 1.00 25.19 ? 107 LEU A CA    1 
ATOM   708  C  C     . LEU A 1 113 ? -8.059  -3.077  -19.715 1.00 25.52 ? 107 LEU A C     1 
ATOM   709  O  O     . LEU A 1 113 ? -7.478  -3.884  -20.464 1.00 31.78 ? 107 LEU A O     1 
ATOM   710  C  CB    . LEU A 1 113 ? -6.905  -1.099  -20.736 1.00 25.32 ? 107 LEU A CB    1 
ATOM   711  C  CG    . LEU A 1 113 ? -6.943  0.304   -21.312 1.00 28.40 ? 107 LEU A CG    1 
ATOM   712  C  CD1   . LEU A 1 113 ? -5.541  0.886   -21.359 1.00 28.44 ? 107 LEU A CD1   1 
ATOM   713  C  CD2   . LEU A 1 113 ? -7.584  0.306   -22.688 1.00 31.67 ? 107 LEU A CD2   1 
ATOM   714  N  N     . VAL A 1 114 ? -8.514  -3.394  -18.499 1.00 25.98 ? 108 VAL A N     1 
ATOM   715  C  CA    . VAL A 1 114 ? -8.473  -4.786  -17.963 1.00 25.63 ? 108 VAL A CA    1 
ATOM   716  C  C     . VAL A 1 114 ? -9.496  -5.631  -18.745 1.00 28.01 ? 108 VAL A C     1 
ATOM   717  O  O     . VAL A 1 114 ? -10.672 -5.226  -18.825 1.00 26.68 ? 108 VAL A O     1 
ATOM   718  C  CB    . VAL A 1 114 ? -8.747  -4.848  -16.456 1.00 25.78 ? 108 VAL A CB    1 
ATOM   719  C  CG1   . VAL A 1 114 ? -8.705  -6.285  -15.950 1.00 28.66 ? 108 VAL A CG1   1 
ATOM   720  C  CG2   . VAL A 1 114 ? -7.762  -3.992  -15.681 1.00 26.95 ? 108 VAL A CG2   1 
ATOM   721  N  N     . LYS A 1 115 ? -9.028  -6.728  -19.339 1.00 31.43 ? 109 LYS A N     1 
ATOM   722  C  CA    . LYS A 1 115 ? -9.878  -7.702  -20.068 1.00 32.51 ? 109 LYS A CA    1 
ATOM   723  C  C     . LYS A 1 115 ? -9.851  -9.023  -19.326 1.00 25.84 ? 109 LYS A C     1 
ATOM   724  O  O     . LYS A 1 115 ? -8.800  -9.447  -18.867 1.00 26.48 ? 109 LYS A O     1 
ATOM   725  C  CB    . LYS A 1 115 ? -9.414  -7.901  -21.515 1.00 34.54 ? 109 LYS A CB    1 
ATOM   726  C  CG    . LYS A 1 115 ? -9.507  -6.655  -22.389 1.00 40.58 ? 109 LYS A CG    1 
ATOM   727  C  CD    . LYS A 1 115 ? -10.923 -6.126  -22.525 1.00 48.94 ? 109 LYS A CD    1 
ATOM   728  C  CE    . LYS A 1 115 ? -11.096 -5.162  -23.685 1.00 56.16 ? 109 LYS A CE    1 
ATOM   729  N  NZ    . LYS A 1 115 ? -10.244 -3.954  -23.531 1.00 62.16 ? 109 LYS A NZ    1 
ATOM   730  N  N     . GLU A 1 116 ? -10.994 -9.688  -19.293 1.00 28.14 ? 110 GLU A N     1 
ATOM   731  C  CA    . GLU A 1 116 ? -11.127 -10.986 -18.619 1.00 26.47 ? 110 GLU A CA    1 
ATOM   732  C  C     . GLU A 1 116 ? -10.067 -11.946 -19.150 1.00 27.21 ? 110 GLU A C     1 
ATOM   733  O  O     . GLU A 1 116 ? -9.538  -12.714 -18.342 1.00 27.76 ? 110 GLU A O     1 
ATOM   734  C  CB    . GLU A 1 116 ? -12.536 -11.551 -18.815 1.00 29.33 ? 110 GLU A CB    1 
ATOM   735  C  CG    . GLU A 1 116 ? -12.809 -12.731 -17.905 1.00 33.32 ? 110 GLU A CG    1 
ATOM   736  C  CD    . GLU A 1 116 ? -14.174 -13.390 -18.067 1.00 34.68 ? 110 GLU A CD    1 
ATOM   737  O  OE1   . GLU A 1 116 ? -15.026 -12.811 -18.778 1.00 37.07 ? 110 GLU A OE1   1 
ATOM   738  O  OE2   . GLU A 1 116 ? -14.382 -14.450 -17.423 1.00 37.74 ? 110 GLU A OE2   1 
ATOM   739  N  N     . GLN A 1 117 ? -9.748  -11.910 -20.441 1.00 28.11 ? 111 GLN A N     1 
ATOM   740  C  CA    . GLN A 1 117 ? -8.785  -12.878 -21.030 1.00 31.30 ? 111 GLN A CA    1 
ATOM   741  C  C     . GLN A 1 117 ? -7.428  -12.777 -20.328 1.00 30.14 ? 111 GLN A C     1 
ATOM   742  O  O     . GLN A 1 117 ? -6.748  -13.816 -20.213 1.00 26.34 ? 111 GLN A O     1 
ATOM   743  C  CB    . GLN A 1 117 ? -8.681  -12.692 -22.549 1.00 38.74 ? 111 GLN A CB    1 
ATOM   744  C  CG    . GLN A 1 117 ? -7.581  -13.539 -23.175 1.00 47.77 ? 111 GLN A CG    1 
ATOM   745  C  CD    . GLN A 1 117 ? -8.064  -14.498 -24.239 1.00 57.93 ? 111 GLN A CD    1 
ATOM   746  O  OE1   . GLN A 1 117 ? -9.104  -14.301 -24.872 1.00 68.50 ? 111 GLN A OE1   1 
ATOM   747  N  NE2   . GLN A 1 117 ? -7.285  -15.549 -24.453 1.00 57.54 ? 111 GLN A NE2   1 
ATOM   748  N  N     . PHE A 1 118 ? -6.990  -11.572 -19.942 1.00 26.54 ? 112 PHE A N     1 
ATOM   749  C  CA    . PHE A 1 118 ? -5.710  -11.378 -19.209 1.00 24.95 ? 112 PHE A CA    1 
ATOM   750  C  C     . PHE A 1 118 ? -5.752  -12.121 -17.867 1.00 23.18 ? 112 PHE A C     1 
ATOM   751  O  O     . PHE A 1 118 ? -4.780  -12.789 -17.487 1.00 25.91 ? 112 PHE A O     1 
ATOM   752  C  CB    . PHE A 1 118 ? -5.427  -9.883  -19.048 1.00 25.29 ? 112 PHE A CB    1 
ATOM   753  C  CG    . PHE A 1 118 ? -4.035  -9.614  -18.551 1.00 25.89 ? 112 PHE A CG    1 
ATOM   754  C  CD1   . PHE A 1 118 ? -3.736  -9.706  -17.198 1.00 26.26 ? 112 PHE A CD1   1 
ATOM   755  C  CD2   . PHE A 1 118 ? -3.010  -9.356  -19.445 1.00 24.58 ? 112 PHE A CD2   1 
ATOM   756  C  CE1   . PHE A 1 118 ? -2.454  -9.466  -16.739 1.00 23.97 ? 112 PHE A CE1   1 
ATOM   757  C  CE2   . PHE A 1 118 ? -1.734  -9.089  -18.979 1.00 25.07 ? 112 PHE A CE2   1 
ATOM   758  C  CZ    . PHE A 1 118 ? -1.453  -9.158  -17.626 1.00 23.59 ? 112 PHE A CZ    1 
ATOM   759  N  N     . LEU A 1 119 ? -6.850  -11.980 -17.134 1.00 27.43 ? 113 LEU A N     1 
ATOM   760  C  CA    . LEU A 1 119 ? -6.998  -12.618 -15.803 1.00 29.92 ? 113 LEU A CA    1 
ATOM   761  C  C     . LEU A 1 119 ? -7.062  -14.144 -15.964 1.00 31.98 ? 113 LEU A C     1 
ATOM   762  O  O     . LEU A 1 119 ? -6.400  -14.828 -15.166 1.00 31.46 ? 113 LEU A O     1 
ATOM   763  C  CB    . LEU A 1 119 ? -8.195  -11.990 -15.076 1.00 33.28 ? 113 LEU A CB    1 
ATOM   764  C  CG    . LEU A 1 119 ? -8.114  -10.466 -14.907 1.00 32.33 ? 113 LEU A CG    1 
ATOM   765  C  CD1   . LEU A 1 119 ? -9.283  -9.934  -14.109 1.00 35.80 ? 113 LEU A CD1   1 
ATOM   766  C  CD2   . LEU A 1 119 ? -6.813  -10.049 -14.238 1.00 35.29 ? 113 LEU A CD2   1 
ATOM   767  N  N     . GLN A 1 120 ? -7.719  -14.675 -17.004 1.00 32.75 ? 114 GLN A N     1 
ATOM   768  C  CA    . GLN A 1 120 ? -7.671  -16.136 -17.327 1.00 36.57 ? 114 GLN A CA    1 
ATOM   769  C  C     . GLN A 1 120 ? -6.222  -16.571 -17.585 1.00 35.77 ? 114 GLN A C     1 
ATOM   770  O  O     . GLN A 1 120 ? -5.797  -17.563 -17.002 1.00 35.05 ? 114 GLN A O     1 
ATOM   771  C  CB    . GLN A 1 120 ? -8.464  -16.535 -18.580 1.00 44.94 ? 114 GLN A CB    1 
ATOM   772  C  CG    . GLN A 1 120 ? -9.847  -15.911 -18.693 1.00 51.92 ? 114 GLN A CG    1 
ATOM   773  C  CD    . GLN A 1 120 ? -10.693 -16.440 -19.835 1.00 56.74 ? 114 GLN A CD    1 
ATOM   774  O  OE1   . GLN A 1 120 ? -10.478 -16.133 -21.012 1.00 55.52 ? 114 GLN A OE1   1 
ATOM   775  N  NE2   . GLN A 1 120 ? -11.718 -17.200 -19.481 1.00 59.39 ? 114 GLN A NE2   1 
ATOM   776  N  N     . LYS A 1 121 ? -5.478  -15.857 -18.437 1.00 31.55 ? 115 LYS A N     1 
ATOM   777  C  CA    . LYS A 1 121 ? -4.128  -16.305 -18.857 1.00 31.08 ? 115 LYS A CA    1 
ATOM   778  C  C     . LYS A 1 121 ? -3.140  -16.193 -17.688 1.00 32.98 ? 115 LYS A C     1 
ATOM   779  O  O     . LYS A 1 121 ? -2.313  -17.108 -17.539 1.00 35.32 ? 115 LYS A O     1 
ATOM   780  C  CB    . LYS A 1 121 ? -3.680  -15.511 -20.091 1.00 36.13 ? 115 LYS A CB    1 
ATOM   781  C  CG    . LYS A 1 121 ? -2.287  -15.852 -20.608 1.00 41.02 ? 115 LYS A CG    1 
ATOM   782  C  CD    . LYS A 1 121 ? -2.135  -15.655 -22.106 1.00 49.32 ? 115 LYS A CD    1 
ATOM   783  C  CE    . LYS A 1 121 ? -0.724  -15.887 -22.619 1.00 53.72 ? 115 LYS A CE    1 
ATOM   784  N  NZ    . LYS A 1 121 ? 0.062   -14.626 -22.675 1.00 53.05 ? 115 LYS A NZ    1 
ATOM   785  N  N     . HIS A 1 122 ? -3.157  -15.099 -16.909 1.00 29.21 ? 116 HIS A N     1 
ATOM   786  C  CA    . HIS A 1 122 ? -2.078  -14.815 -15.922 1.00 27.59 ? 116 HIS A CA    1 
ATOM   787  C  C     . HIS A 1 122 ? -2.544  -14.870 -14.457 1.00 25.73 ? 116 HIS A C     1 
ATOM   788  O  O     . HIS A 1 122 ? -1.675  -14.668 -13.578 1.00 27.91 ? 116 HIS A O     1 
ATOM   789  C  CB    . HIS A 1 122 ? -1.473  -13.436 -16.220 1.00 28.42 ? 116 HIS A CB    1 
ATOM   790  C  CG    . HIS A 1 122 ? -0.960  -13.315 -17.609 1.00 27.55 ? 116 HIS A CG    1 
ATOM   791  N  ND1   . HIS A 1 122 ? 0.239   -13.881 -18.002 1.00 29.17 ? 116 HIS A ND1   1 
ATOM   792  C  CD2   . HIS A 1 122 ? -1.475  -12.691 -18.686 1.00 27.29 ? 116 HIS A CD2   1 
ATOM   793  C  CE1   . HIS A 1 122 ? 0.447   -13.609 -19.281 1.00 29.24 ? 116 HIS A CE1   1 
ATOM   794  N  NE2   . HIS A 1 122 ? -0.590  -12.865 -19.723 1.00 28.52 ? 116 HIS A NE2   1 
ATOM   795  N  N     . GLY A 1 123 ? -3.835  -15.075 -14.207 1.00 28.12 ? 117 GLY A N     1 
ATOM   796  C  CA    . GLY A 1 123 ? -4.495  -14.933 -12.898 1.00 28.95 ? 117 GLY A CA    1 
ATOM   797  C  C     . GLY A 1 123 ? -3.871  -15.826 -11.845 1.00 30.28 ? 117 GLY A C     1 
ATOM   798  O  O     . GLY A 1 123 ? -3.921  -15.464 -10.665 1.00 30.88 ? 117 GLY A O     1 
ATOM   799  N  N     . ARG A 1 124 ? -3.304  -16.964 -12.232 1.00 31.84 ? 118 ARG A N     1 
ATOM   800  C  CA    . ARG A 1 124 ? -2.660  -17.892 -11.268 1.00 31.99 ? 118 ARG A CA    1 
ATOM   801  C  C     . ARG A 1 124 ? -1.439  -17.208 -10.632 1.00 31.24 ? 118 ARG A C     1 
ATOM   802  O  O     . ARG A 1 124 ? -1.035  -17.592 -9.521  1.00 31.05 ? 118 ARG A O     1 
ATOM   803  C  CB    . ARG A 1 124 ? -2.323  -19.217 -11.964 1.00 35.77 ? 118 ARG A CB    1 
ATOM   804  C  CG    . ARG A 1 124 ? -1.050  -19.179 -12.802 1.00 39.04 ? 118 ARG A CG    1 
ATOM   805  C  CD    . ARG A 1 124 ? -0.887  -20.413 -13.689 1.00 43.69 ? 118 ARG A CD    1 
ATOM   806  N  NE    . ARG A 1 124 ? 0.299   -20.314 -14.534 1.00 47.28 ? 118 ARG A NE    1 
ATOM   807  C  CZ    . ARG A 1 124 ? 0.378   -19.617 -15.679 1.00 47.95 ? 118 ARG A CZ    1 
ATOM   808  N  NH1   . ARG A 1 124 ? -0.657  -18.918 -16.121 1.00 45.89 ? 118 ARG A NH1   1 
ATOM   809  N  NH2   . ARG A 1 124 ? 1.508   -19.592 -16.364 1.00 43.59 ? 118 ARG A NH2   1 
ATOM   810  N  N     . ASN A 1 125 ? -0.847  -16.232 -11.319 1.00 28.18 ? 119 ASN A N     1 
ATOM   811  C  CA    . ASN A 1 125 ? 0.390   -15.536 -10.912 1.00 27.04 ? 119 ASN A CA    1 
ATOM   812  C  C     . ASN A 1 125 ? 0.084   -14.167 -10.278 1.00 28.09 ? 119 ASN A C     1 
ATOM   813  O  O     . ASN A 1 125 ? 1.070   -13.471 -9.899  1.00 29.98 ? 119 ASN A O     1 
ATOM   814  C  CB    . ASN A 1 125 ? 1.329   -15.380 -12.099 1.00 28.28 ? 119 ASN A CB    1 
ATOM   815  C  CG    . ASN A 1 125 ? 1.885   -16.725 -12.503 1.00 33.58 ? 119 ASN A CG    1 
ATOM   816  O  OD1   . ASN A 1 125 ? 1.948   -17.603 -11.646 1.00 32.22 ? 119 ASN A OD1   1 
ATOM   817  N  ND2   . ASN A 1 125 ? 2.181   -16.907 -13.789 1.00 29.88 ? 119 ASN A ND2   1 
ATOM   818  N  N     . ILE A 1 126 ? -1.183  -13.765 -10.245 1.00 27.30 ? 120 ILE A N     1 
ATOM   819  C  CA    . ILE A 1 126 ? -1.591  -12.441 -9.683  1.00 26.13 ? 120 ILE A CA    1 
ATOM   820  C  C     . ILE A 1 126 ? -2.152  -12.651 -8.278  1.00 23.40 ? 120 ILE A C     1 
ATOM   821  O  O     . ILE A 1 126 ? -3.267  -13.195 -8.150  1.00 27.06 ? 120 ILE A O     1 
ATOM   822  C  CB    . ILE A 1 126 ? -2.596  -11.711 -10.589 1.00 26.15 ? 120 ILE A CB    1 
ATOM   823  C  CG1   . ILE A 1 126 ? -2.022  -11.428 -11.981 1.00 24.24 ? 120 ILE A CG1   1 
ATOM   824  C  CG2   . ILE A 1 126 ? -3.055  -10.429 -9.895  1.00 25.70 ? 120 ILE A CG2   1 
ATOM   825  C  CD1   . ILE A 1 126 ? -3.051  -10.975 -13.005 1.00 24.04 ? 120 ILE A CD1   1 
ATOM   826  N  N     . ASP A 1 127 ? -1.460  -12.150 -7.254  1.00 23.78 ? 121 ASP A N     1 
ATOM   827  C  CA    . ASP A 1 127 ? -1.999  -12.243 -5.869  1.00 23.37 ? 121 ASP A CA    1 
ATOM   828  C  C     . ASP A 1 127 ? -3.117  -11.216 -5.670  1.00 21.98 ? 121 ASP A C     1 
ATOM   829  O  O     . ASP A 1 127 ? -4.147  -11.538 -5.075  1.00 22.73 ? 121 ASP A O     1 
ATOM   830  C  CB    . ASP A 1 127 ? -0.848  -12.196 -4.874  1.00 24.18 ? 121 ASP A CB    1 
ATOM   831  C  CG    . ASP A 1 127 ? 0.083   -13.366 -5.134  1.00 31.26 ? 121 ASP A CG    1 
ATOM   832  O  OD1   . ASP A 1 127 ? -0.376  -14.538 -4.949  1.00 36.23 ? 121 ASP A OD1   1 
ATOM   833  O  OD2   . ASP A 1 127 ? 1.237   -13.127 -5.519  1.00 30.88 ? 121 ASP A OD2   1 
ATOM   834  N  N     . ILE A 1 128 ? -2.915  -9.983  -6.116  1.00 21.11 ? 122 ILE A N     1 
ATOM   835  C  CA    . ILE A 1 128 ? -3.783  -8.828  -5.744  1.00 21.17 ? 122 ILE A CA    1 
ATOM   836  C  C     . ILE A 1 128 ? -3.932  -7.953  -6.973  1.00 19.93 ? 122 ILE A C     1 
ATOM   837  O  O     . ILE A 1 128 ? -2.909  -7.643  -7.585  1.00 20.93 ? 122 ILE A O     1 
ATOM   838  C  CB    . ILE A 1 128 ? -3.170  -8.016  -4.577  1.00 20.33 ? 122 ILE A CB    1 
ATOM   839  C  CG1   . ILE A 1 128 ? -3.043  -8.825  -3.290  1.00 22.73 ? 122 ILE A CG1   1 
ATOM   840  C  CG2   . ILE A 1 128 ? -3.923  -6.722  -4.313  1.00 21.05 ? 122 ILE A CG2   1 
ATOM   841  C  CD1   . ILE A 1 128 ? -1.986  -8.268  -2.365  1.00 24.84 ? 122 ILE A CD1   1 
ATOM   842  N  N     . LEU A 1 129 ? -5.161  -7.573  -7.288  1.00 20.43 ? 123 LEU A N     1 
ATOM   843  C  CA    . LEU A 1 129 ? -5.447  -6.529  -8.290  1.00 22.20 ? 123 LEU A CA    1 
ATOM   844  C  C     . LEU A 1 129 ? -6.144  -5.368  -7.576  1.00 22.18 ? 123 LEU A C     1 
ATOM   845  O  O     . LEU A 1 129 ? -7.265  -5.551  -7.063  1.00 21.75 ? 123 LEU A O     1 
ATOM   846  C  CB    . LEU A 1 129 ? -6.315  -7.140  -9.391  1.00 23.33 ? 123 LEU A CB    1 
ATOM   847  C  CG    . LEU A 1 129 ? -6.692  -6.192  -10.529 1.00 28.41 ? 123 LEU A CG    1 
ATOM   848  C  CD1   . LEU A 1 129 ? -5.441  -5.742  -11.270 1.00 29.54 ? 123 LEU A CD1   1 
ATOM   849  C  CD2   . LEU A 1 129 ? -7.641  -6.894  -11.510 1.00 30.34 ? 123 LEU A CD2   1 
ATOM   850  N  N     . ALA A 1 130 ? -5.532  -4.192  -7.645  1.00 20.32 ? 124 ALA A N     1 
ATOM   851  C  CA    . ALA A 1 130 ? -6.044  -2.922  -7.096  1.00 21.46 ? 124 ALA A CA    1 
ATOM   852  C  C     . ALA A 1 130 ? -6.618  -2.116  -8.249  1.00 21.94 ? 124 ALA A C     1 
ATOM   853  O  O     . ALA A 1 130 ? -5.896  -1.901  -9.215  1.00 20.79 ? 124 ALA A O     1 
ATOM   854  C  CB    . ALA A 1 130 ? -4.952  -2.151  -6.423  1.00 20.53 ? 124 ALA A CB    1 
ATOM   855  N  N     . VAL A 1 131 ? -7.865  -1.704  -8.135  1.00 19.39 ? 125 VAL A N     1 
ATOM   856  C  CA    . VAL A 1 131 ? -8.515  -0.801  -9.101  1.00 19.82 ? 125 VAL A CA    1 
ATOM   857  C  C     . VAL A 1 131 ? -8.662  0.557   -8.423  1.00 20.57 ? 125 VAL A C     1 
ATOM   858  O  O     . VAL A 1 131 ? -9.201  0.633   -7.279  1.00 18.57 ? 125 VAL A O     1 
ATOM   859  C  CB    . VAL A 1 131 ? -9.886  -1.335  -9.561  1.00 22.10 ? 125 VAL A CB    1 
ATOM   860  C  CG1   . VAL A 1 131 ? -10.486 -0.386  -10.574 1.00 21.27 ? 125 VAL A CG1   1 
ATOM   861  C  CG2   . VAL A 1 131 ? -9.804  -2.770  -10.078 1.00 25.04 ? 125 VAL A CG2   1 
ATOM   862  N  N     . SER A 1 132 ? -8.242  1.604   -9.116  1.00 18.96 ? 126 SER A N     1 
ATOM   863  C  CA    . SER A 1 132 ? -8.361  2.987   -8.646  1.00 20.69 ? 126 SER A CA    1 
ATOM   864  C  C     . SER A 1 132 ? -9.735  3.492   -9.050  1.00 23.79 ? 126 SER A C     1 
ATOM   865  O  O     . SER A 1 132 ? -9.992  3.592   -10.274 1.00 24.60 ? 126 SER A O     1 
ATOM   866  C  CB    . SER A 1 132 ? -7.258  3.820   -9.162  1.00 19.36 ? 126 SER A CB    1 
ATOM   867  O  OG    . SER A 1 132 ? -6.033  3.283   -8.681  1.00 21.34 ? 126 SER A OG    1 
ATOM   868  N  N     . CYS A 1 133 ? -10.570 3.816   -8.065  1.00 23.09 ? 127 CYS A N     1 
ATOM   869  C  CA    . CYS A 1 133 ? -11.895 4.455   -8.348  1.00 26.17 ? 127 CYS A CA    1 
ATOM   870  C  C     . CYS A 1 133 ? -12.186 5.454   -7.237  1.00 23.93 ? 127 CYS A C     1 
ATOM   871  O  O     . CYS A 1 133 ? -12.186 5.047   -6.096  1.00 24.96 ? 127 CYS A O     1 
ATOM   872  C  CB    . CYS A 1 133 ? -13.010 3.428   -8.425  1.00 32.92 ? 127 CYS A CB    1 
ATOM   873  S  SG    . CYS A 1 133 ? -14.514 4.117   -9.178  1.00 32.52 ? 127 CYS A SG    1 
ATOM   874  N  N     . ASP A 1 134 ? -12.247 6.736   -7.569  1.00 21.41 ? 128 ASP A N     1 
ATOM   875  C  CA    . ASP A 1 134 ? -12.259 7.795   -6.546  1.00 23.62 ? 128 ASP A CA    1 
ATOM   876  C  C     . ASP A 1 134 ? -13.688 8.102   -6.107  1.00 23.78 ? 128 ASP A C     1 
ATOM   877  O  O     . ASP A 1 134 ? -13.852 8.736   -5.046  1.00 25.70 ? 128 ASP A O     1 
ATOM   878  C  CB    . ASP A 1 134 ? -11.551 9.025   -7.068  1.00 23.12 ? 128 ASP A CB    1 
ATOM   879  C  CG    . ASP A 1 134 ? -10.115 8.700   -7.485  1.00 29.08 ? 128 ASP A CG    1 
ATOM   880  O  OD1   . ASP A 1 134 ? -9.382  7.956   -6.714  1.00 23.77 ? 128 ASP A OD1   1 
ATOM   881  O  OD2   . ASP A 1 134 ? -9.766  9.107   -8.614  1.00 28.88 ? 128 ASP A OD2   1 
ATOM   882  N  N     . SER A 1 135 ? -14.690 7.688   -6.874  1.00 24.16 ? 129 SER A N     1 
ATOM   883  C  CA    . SER A 1 135 ? -16.083 8.067   -6.571  1.00 22.53 ? 129 SER A CA    1 
ATOM   884  C  C     . SER A 1 135 ? -17.034 7.023   -7.143  1.00 24.82 ? 129 SER A C     1 
ATOM   885  O  O     . SER A 1 135 ? -16.699 6.337   -8.120  1.00 24.07 ? 129 SER A O     1 
ATOM   886  C  CB    . SER A 1 135 ? -16.366 9.432   -7.103  1.00 25.34 ? 129 SER A CB    1 
ATOM   887  O  OG    . SER A 1 135 ? -17.697 9.829   -6.803  1.00 24.06 ? 129 SER A OG    1 
ATOM   888  N  N     . PHE A 1 136 ? -18.199 6.911   -6.525  1.00 26.12 ? 130 PHE A N     1 
ATOM   889  C  CA    . PHE A 1 136 ? -19.314 6.105   -7.057  1.00 26.45 ? 130 PHE A CA    1 
ATOM   890  C  C     . PHE A 1 136 ? -20.292 7.017   -7.781  1.00 26.72 ? 130 PHE A C     1 
ATOM   891  O  O     . PHE A 1 136 ? -21.260 6.485   -8.363  1.00 29.63 ? 130 PHE A O     1 
ATOM   892  C  CB    . PHE A 1 136 ? -19.904 5.258   -5.934  1.00 26.97 ? 130 PHE A CB    1 
ATOM   893  C  CG    . PHE A 1 136 ? -18.909 4.219   -5.501  1.00 27.65 ? 130 PHE A CG    1 
ATOM   894  C  CD1   . PHE A 1 136 ? -18.774 3.039   -6.205  1.00 29.43 ? 130 PHE A CD1   1 
ATOM   895  C  CD2   . PHE A 1 136 ? -18.084 4.449   -4.416  1.00 28.46 ? 130 PHE A CD2   1 
ATOM   896  C  CE1   . PHE A 1 136 ? -17.840 2.091   -5.831  1.00 30.47 ? 130 PHE A CE1   1 
ATOM   897  C  CE2   . PHE A 1 136 ? -17.143 3.500   -4.044  1.00 30.20 ? 130 PHE A CE2   1 
ATOM   898  C  CZ    . PHE A 1 136 ? -17.019 2.330   -4.751  1.00 29.71 ? 130 PHE A CZ    1 
ATOM   899  N  N     . ASN A 1 137 ? -20.040 8.317   -7.787  1.00 24.53 ? 131 ASN A N     1 
ATOM   900  C  CA    . ASN A 1 137 ? -20.840 9.288   -8.571  1.00 26.54 ? 131 ASN A CA    1 
ATOM   901  C  C     . ASN A 1 137 ? -20.126 9.580   -9.894  1.00 27.46 ? 131 ASN A C     1 
ATOM   902  O  O     . ASN A 1 137 ? -19.029 10.200  -9.879  1.00 24.17 ? 131 ASN A O     1 
ATOM   903  C  CB    . ASN A 1 137 ? -21.130 10.547  -7.769  1.00 26.37 ? 131 ASN A CB    1 
ATOM   904  C  CG    . ASN A 1 137 ? -21.984 10.281  -6.543  1.00 28.34 ? 131 ASN A CG    1 
ATOM   905  O  OD1   . ASN A 1 137 ? -22.874 9.436   -6.551  1.00 29.59 ? 131 ASN A OD1   1 
ATOM   906  N  ND2   . ASN A 1 137 ? -21.650 10.928  -5.441  1.00 31.63 ? 131 ASN A ND2   1 
ATOM   907  N  N     . GLU A 1 138 ? -20.746 9.242   -11.029 1.00 28.39 ? 132 GLU A N     1 
ATOM   908  C  CA    . GLU A 1 138 ? -20.053 9.386   -12.331 1.00 29.10 ? 132 GLU A CA    1 
ATOM   909  C  C     . GLU A 1 138 ? -19.747 10.850  -12.629 1.00 29.50 ? 132 GLU A C     1 
ATOM   910  O  O     . GLU A 1 138 ? -18.661 11.094  -13.170 1.00 29.60 ? 132 GLU A O     1 
ATOM   911  C  CB    . GLU A 1 138 ? -20.773 8.609   -13.426 1.00 35.72 ? 132 GLU A CB    1 
ATOM   912  C  CG    . GLU A 1 138 ? -20.676 7.096   -13.183 1.00 40.25 ? 132 GLU A CG    1 
ATOM   913  C  CD    . GLU A 1 138 ? -19.324 6.365   -13.320 1.00 47.22 ? 132 GLU A CD    1 
ATOM   914  O  OE1   . GLU A 1 138 ? -18.203 7.012   -13.294 1.00 36.36 ? 132 GLU A OE1   1 
ATOM   915  O  OE2   . GLU A 1 138 ? -19.385 5.104   -13.467 1.00 46.43 ? 132 GLU A OE2   1 
ATOM   916  N  N     . ALA A 1 139 ? -20.562 11.821  -12.213 1.00 25.55 ? 133 ALA A N     1 
ATOM   917  C  CA    . ALA A 1 139 ? -20.251 13.239  -12.457 1.00 26.30 ? 133 ALA A CA    1 
ATOM   918  C  C     . ALA A 1 139 ? -18.919 13.599  -11.756 1.00 28.77 ? 133 ALA A C     1 
ATOM   919  O  O     . ALA A 1 139 ? -18.191 14.460  -12.286 1.00 26.31 ? 133 ALA A O     1 
ATOM   920  C  CB    . ALA A 1 139 ? -21.371 14.108  -11.989 1.00 28.72 ? 133 ALA A CB    1 
ATOM   921  N  N     . THR A 1 140 ? -18.598 12.959  -10.632 1.00 24.46 ? 134 THR A N     1 
ATOM   922  C  CA    . THR A 1 140 ? -17.331 13.216  -9.900  1.00 25.74 ? 134 THR A CA    1 
ATOM   923  C  C     . THR A 1 140 ? -16.141 12.599  -10.676 1.00 24.37 ? 134 THR A C     1 
ATOM   924  O  O     . THR A 1 140 ? -15.085 13.254  -10.790 1.00 25.52 ? 134 THR A O     1 
ATOM   925  C  CB    . THR A 1 140 ? -17.411 12.674  -8.461  1.00 26.51 ? 134 THR A CB    1 
ATOM   926  O  OG1   . THR A 1 140 ? -18.529 13.275  -7.799  1.00 24.28 ? 134 THR A OG1   1 
ATOM   927  C  CG2   . THR A 1 140 ? -16.140 12.986  -7.682  1.00 26.06 ? 134 THR A CG2   1 
ATOM   928  N  N     . ASN A 1 141 ? -16.282 11.350  -11.128 1.00 24.85 ? 135 ASN A N     1 
ATOM   929  C  CA    . ASN A 1 141 ? -15.227 10.653  -11.917 1.00 24.70 ? 135 ASN A CA    1 
ATOM   930  C  C     . ASN A 1 141 ? -14.906 11.496  -13.159 1.00 28.24 ? 135 ASN A C     1 
ATOM   931  O  O     . ASN A 1 141 ? -13.719 11.629  -13.488 1.00 23.08 ? 135 ASN A O     1 
ATOM   932  C  CB    . ASN A 1 141 ? -15.630 9.217   -12.241 1.00 23.48 ? 135 ASN A CB    1 
ATOM   933  C  CG    . ASN A 1 141 ? -15.596 8.355   -10.996 1.00 27.49 ? 135 ASN A CG    1 
ATOM   934  O  OD1   . ASN A 1 141 ? -14.769 8.578   -10.103 1.00 28.46 ? 135 ASN A OD1   1 
ATOM   935  N  ND2   . ASN A 1 141 ? -16.493 7.388   -10.909 1.00 23.63 ? 135 ASN A ND2   1 
ATOM   936  N  N     . ILE A 1 142 ? -15.932 12.059  -13.812 1.00 24.27 ? 136 ILE A N     1 
ATOM   937  C  CA    . ILE A 1 142 ? -15.752 12.889  -15.036 1.00 27.21 ? 136 ILE A CA    1 
ATOM   938  C  C     . ILE A 1 142 ? -15.022 14.177  -14.665 1.00 26.40 ? 136 ILE A C     1 
ATOM   939  O  O     . ILE A 1 142 ? -14.060 14.519  -15.376 1.00 27.07 ? 136 ILE A O     1 
ATOM   940  C  CB    . ILE A 1 142 ? -17.098 13.096  -15.761 1.00 28.34 ? 136 ILE A CB    1 
ATOM   941  C  CG1   . ILE A 1 142 ? -17.592 11.767  -16.333 1.00 31.35 ? 136 ILE A CG1   1 
ATOM   942  C  CG2   . ILE A 1 142 ? -16.972 14.161  -16.834 1.00 31.34 ? 136 ILE A CG2   1 
ATOM   943  C  CD1   . ILE A 1 142 ? -19.115 11.686  -16.527 1.00 36.50 ? 136 ILE A CD1   1 
ATOM   944  N  N     . LYS A 1 143 ? -15.412 14.861  -13.585 1.00 27.10 ? 137 LYS A N     1 
ATOM   945  C  CA    . LYS A 1 143 ? -14.768 16.124  -13.142 1.00 28.91 ? 137 LYS A CA    1 
ATOM   946  C  C     . LYS A 1 143 ? -13.298 15.859  -12.755 1.00 30.63 ? 137 LYS A C     1 
ATOM   947  O  O     . LYS A 1 143 ? -12.456 16.776  -12.930 1.00 27.37 ? 137 LYS A O     1 
ATOM   948  C  CB    . LYS A 1 143 ? -15.454 16.714  -11.912 1.00 34.47 ? 137 LYS A CB    1 
ATOM   949  C  CG    . LYS A 1 143 ? -16.639 17.619  -12.171 1.00 41.05 ? 137 LYS A CG    1 
ATOM   950  C  CD    . LYS A 1 143 ? -17.390 17.978  -10.900 1.00 47.03 ? 137 LYS A CD    1 
ATOM   951  C  CE    . LYS A 1 143 ? -18.870 18.250  -11.141 1.00 52.34 ? 137 LYS A CE    1 
ATOM   952  N  NZ    . LYS A 1 143 ? -19.710 17.784  -10.009 1.00 52.73 ? 137 LYS A NZ    1 
ATOM   953  N  N     . ILE A 1 144 ? -12.996 14.686  -12.180 1.00 27.32 ? 138 ILE A N     1 
ATOM   954  C  CA    . ILE A 1 144 ? -11.600 14.360  -11.745 1.00 25.63 ? 138 ILE A CA    1 
ATOM   955  C  C     . ILE A 1 144 ? -10.707 14.170  -12.979 1.00 27.64 ? 138 ILE A C     1 
ATOM   956  O  O     . ILE A 1 144 ? -9.487  14.494  -12.874 1.00 28.69 ? 138 ILE A O     1 
ATOM   957  C  CB    . ILE A 1 144 ? -11.612 13.110  -10.848 1.00 25.47 ? 138 ILE A CB    1 
ATOM   958  C  CG1   . ILE A 1 144 ? -12.037 13.510  -9.431  1.00 27.57 ? 138 ILE A CG1   1 
ATOM   959  C  CG2   . ILE A 1 144 ? -10.270 12.369  -10.905 1.00 26.84 ? 138 ILE A CG2   1 
ATOM   960  C  CD1   . ILE A 1 144 ? -12.432 12.353  -8.535  1.00 28.45 ? 138 ILE A CD1   1 
ATOM   961  N  N     . GLY A 1 145 ? -11.272 13.607  -14.054 1.00 26.33 ? 139 GLY A N     1 
ATOM   962  C  CA    . GLY A 1 145 ? -10.599 13.278  -15.323 1.00 26.65 ? 139 GLY A CA    1 
ATOM   963  C  C     . GLY A 1 145 ? -10.266 11.805  -15.461 1.00 26.86 ? 139 GLY A C     1 
ATOM   964  O  O     . GLY A 1 145 ? -9.436  11.446  -16.348 1.00 26.45 ? 139 GLY A O     1 
ATOM   965  N  N     . ARG A 1 146 ? -10.925 10.952  -14.694 1.00 30.87 ? 140 ARG A N     1 
ATOM   966  C  CA    . ARG A 1 146 ? -10.602 9.508   -14.689 1.00 31.82 ? 140 ARG A CA    1 
ATOM   967  C  C     . ARG A 1 146 ? -11.503 8.734   -15.651 1.00 39.28 ? 140 ARG A C     1 
ATOM   968  O  O     . ARG A 1 146 ? -11.234 7.559   -15.926 1.00 36.92 ? 140 ARG A O     1 
ATOM   969  C  CB    . ARG A 1 146 ? -10.723 8.853   -13.312 1.00 33.18 ? 140 ARG A CB    1 
ATOM   970  C  CG    . ARG A 1 146 ? -9.826  7.623   -13.302 1.00 35.89 ? 140 ARG A CG    1 
ATOM   971  C  CD    . ARG A 1 146 ? -9.882  6.814   -12.059 1.00 34.70 ? 140 ARG A CD    1 
ATOM   972  N  NE    . ARG A 1 146 ? -9.160  7.419   -10.966 1.00 28.64 ? 140 ARG A NE    1 
ATOM   973  C  CZ    . ARG A 1 146 ? -7.873  7.217   -10.707 1.00 26.19 ? 140 ARG A CZ    1 
ATOM   974  N  NH1   . ARG A 1 146 ? -7.122  6.508   -11.533 1.00 24.88 ? 140 ARG A NH1   1 
ATOM   975  N  NH2   . ARG A 1 146 ? -7.343  7.744   -9.620  1.00 28.07 ? 140 ARG A NH2   1 
ATOM   976  N  N     . GLY A 1 147 ? -12.560 9.328   -16.139 1.00 32.71 ? 141 GLY A N     1 
ATOM   977  C  CA    . GLY A 1 147 ? -13.377 8.542   -17.066 1.00 42.34 ? 141 GLY A CA    1 
ATOM   978  C  C     . GLY A 1 147 ? -14.439 9.382   -17.701 1.00 35.68 ? 141 GLY A C     1 
ATOM   979  O  O     . GLY A 1 147 ? -14.374 10.588  -17.546 1.00 36.97 ? 141 GLY A O     1 
ATOM   980  N  N     . SER A 1 148 ? -15.336 8.712   -18.412 1.00 40.44 ? 142 SER A N     1 
ATOM   981  C  CA    . SER A 1 148 ? -16.462 9.307   -19.159 1.00 44.08 ? 142 SER A CA    1 
ATOM   982  C  C     . SER A 1 148 ? -17.755 8.579   -18.772 1.00 44.22 ? 142 SER A C     1 
ATOM   983  O  O     . SER A 1 148 ? -18.711 8.688   -19.501 1.00 40.75 ? 142 SER A O     1 
ATOM   984  C  CB    . SER A 1 148 ? -16.172 9.240   -20.637 1.00 50.35 ? 142 SER A CB    1 
ATOM   985  O  OG    . SER A 1 148 ? -15.744 7.931   -20.987 1.00 61.94 ? 142 SER A OG    1 
ATOM   986  N  N     . GLY A 1 149 ? -17.778 7.863   -17.643 1.00 45.74 ? 143 GLY A N     1 
ATOM   987  C  CA    . GLY A 1 149 ? -19.036 7.490   -16.965 1.00 43.84 ? 143 GLY A CA    1 
ATOM   988  C  C     . GLY A 1 149 ? -19.209 6.004   -16.725 1.00 43.06 ? 143 GLY A C     1 
ATOM   989  O  O     . GLY A 1 149 ? -20.286 5.635   -16.182 1.00 47.21 ? 143 GLY A O     1 
ATOM   990  N  N     . ASP A 1 150 ? -18.230 5.155   -17.062 1.00 37.90 ? 144 ASP A N     1 
ATOM   991  C  CA    . ASP A 1 150 ? -18.400 3.682   -16.962 1.00 40.01 ? 144 ASP A CA    1 
ATOM   992  C  C     . ASP A 1 150 ? -17.483 3.085   -15.879 1.00 33.96 ? 144 ASP A C     1 
ATOM   993  O  O     . ASP A 1 150 ? -17.501 1.846   -15.736 1.00 27.15 ? 144 ASP A O     1 
ATOM   994  C  CB    . ASP A 1 150 ? -18.129 3.041   -18.322 1.00 48.90 ? 144 ASP A CB    1 
ATOM   995  C  CG    . ASP A 1 150 ? -19.150 3.414   -19.385 1.00 63.00 ? 144 ASP A CG    1 
ATOM   996  O  OD1   . ASP A 1 150 ? -20.343 3.635   -19.023 1.00 68.22 ? 144 ASP A OD1   1 
ATOM   997  O  OD2   . ASP A 1 150 ? -18.747 3.490   -20.572 1.00 74.05 ? 144 ASP A OD2   1 
ATOM   998  N  N     . ASN A 1 151 ? -16.752 3.920   -15.125 1.00 32.41 ? 145 ASN A N     1 
ATOM   999  C  CA    . ASN A 1 151 ? -15.762 3.453   -14.110 1.00 31.69 ? 145 ASN A CA    1 
ATOM   1000 C  C     . ASN A 1 151 ? -16.447 2.535   -13.100 1.00 28.15 ? 145 ASN A C     1 
ATOM   1001 O  O     . ASN A 1 151 ? -15.944 1.430   -12.841 1.00 25.46 ? 145 ASN A O     1 
ATOM   1002 C  CB    . ASN A 1 151 ? -15.085 4.617   -13.391 1.00 35.74 ? 145 ASN A CB    1 
ATOM   1003 C  CG    . ASN A 1 151 ? -14.262 5.443   -14.348 1.00 43.06 ? 145 ASN A CG    1 
ATOM   1004 O  OD1   . ASN A 1 151 ? -14.802 6.234   -15.108 1.00 47.62 ? 145 ASN A OD1   1 
ATOM   1005 N  ND2   . ASN A 1 151 ? -12.963 5.223   -14.341 1.00 46.96 ? 145 ASN A ND2   1 
ATOM   1006 N  N     . VAL A 1 152 ? -17.596 2.941   -12.571 1.00 28.42 ? 146 VAL A N     1 
ATOM   1007 C  CA    . VAL A 1 152 ? -18.272 2.136   -11.513 1.00 28.82 ? 146 VAL A CA    1 
ATOM   1008 C  C     . VAL A 1 152 ? -18.686 0.773   -12.071 1.00 27.83 ? 146 VAL A C     1 
ATOM   1009 O  O     . VAL A 1 152 ? -18.403 -0.246  -11.437 1.00 24.75 ? 146 VAL A O     1 
ATOM   1010 C  CB    . VAL A 1 152 ? -19.464 2.873   -10.880 1.00 28.12 ? 146 VAL A CB    1 
ATOM   1011 C  CG1   . VAL A 1 152 ? -20.117 1.966   -9.838  1.00 26.03 ? 146 VAL A CG1   1 
ATOM   1012 C  CG2   . VAL A 1 152 ? -19.022 4.189   -10.268 1.00 29.33 ? 146 VAL A CG2   1 
ATOM   1013 N  N     . GLN A 1 153 ? -19.346 0.730   -13.220 1.00 31.08 ? 147 GLN A N     1 
ATOM   1014 C  CA    . GLN A 1 153 ? -19.763 -0.574  -13.807 1.00 30.03 ? 147 GLN A CA    1 
ATOM   1015 C  C     . GLN A 1 153 ? -18.516 -1.443  -14.030 1.00 26.69 ? 147 GLN A C     1 
ATOM   1016 O  O     . GLN A 1 153 ? -18.561 -2.623  -13.744 1.00 24.06 ? 147 GLN A O     1 
ATOM   1017 C  CB    . GLN A 1 153 ? -20.575 -0.328  -15.088 1.00 34.30 ? 147 GLN A CB    1 
ATOM   1018 C  CG    . GLN A 1 153 ? -20.866 -1.567  -15.920 1.00 40.67 ? 147 GLN A CG    1 
ATOM   1019 C  CD    . GLN A 1 153 ? -21.592 -1.284  -17.227 1.00 48.54 ? 147 GLN A CD    1 
ATOM   1020 O  OE1   . GLN A 1 153 ? -21.679 -0.151  -17.708 1.00 53.32 ? 147 GLN A OE1   1 
ATOM   1021 N  NE2   . GLN A 1 153 ? -22.096 -2.335  -17.852 1.00 50.30 ? 147 GLN A NE2   1 
ATOM   1022 N  N     . LYS A 1 154 ? -17.440 -0.891  -14.570 1.00 26.06 ? 148 LYS A N     1 
ATOM   1023 C  CA    . LYS A 1 154 ? -16.205 -1.681  -14.814 1.00 26.30 ? 148 LYS A CA    1 
ATOM   1024 C  C     . LYS A 1 154 ? -15.657 -2.214  -13.481 1.00 23.40 ? 148 LYS A C     1 
ATOM   1025 O  O     . LYS A 1 154 ? -15.176 -3.358  -13.435 1.00 23.33 ? 148 LYS A O     1 
ATOM   1026 C  CB    . LYS A 1 154 ? -15.154 -0.848  -15.561 1.00 27.89 ? 148 LYS A CB    1 
ATOM   1027 C  CG    . LYS A 1 154 ? -13.988 -1.675  -16.103 1.00 31.41 ? 148 LYS A CG    1 
ATOM   1028 C  CD    . LYS A 1 154 ? -14.418 -2.752  -17.105 1.00 31.64 ? 148 LYS A CD    1 
ATOM   1029 C  CE    . LYS A 1 154 ? -13.291 -3.698  -17.492 1.00 33.27 ? 148 LYS A CE    1 
ATOM   1030 N  NZ    . LYS A 1 154 ? -12.207 -2.955  -18.161 1.00 33.45 ? 148 LYS A NZ    1 
ATOM   1031 N  N     . LEU A 1 155 ? -15.679 -1.399  -12.429 1.00 25.72 ? 149 LEU A N     1 
ATOM   1032 C  CA    . LEU A 1 155 ? -15.126 -1.790  -11.095 1.00 24.23 ? 149 LEU A CA    1 
ATOM   1033 C  C     . LEU A 1 155 ? -15.856 -3.040  -10.555 1.00 23.88 ? 149 LEU A C     1 
ATOM   1034 O  O     . LEU A 1 155 ? -15.196 -3.969  -10.088 1.00 23.44 ? 149 LEU A O     1 
ATOM   1035 C  CB    . LEU A 1 155 ? -15.254 -0.594  -10.147 1.00 24.89 ? 149 LEU A CB    1 
ATOM   1036 C  CG    . LEU A 1 155 ? -14.883 -0.879  -8.691  1.00 23.17 ? 149 LEU A CG    1 
ATOM   1037 C  CD1   . LEU A 1 155 ? -13.405 -1.150  -8.566  1.00 27.17 ? 149 LEU A CD1   1 
ATOM   1038 C  CD2   . LEU A 1 155 ? -15.311 0.257   -7.779  1.00 25.35 ? 149 LEU A CD2   1 
ATOM   1039 N  N     . TYR A 1 156 ? -17.190 -3.064  -10.596 1.00 27.44 ? 150 TYR A N     1 
ATOM   1040 C  CA    . TYR A 1 156 ? -18.022 -4.228  -10.172 1.00 27.77 ? 150 TYR A CA    1 
ATOM   1041 C  C     . TYR A 1 156 ? -17.687 -5.467  -11.013 1.00 26.97 ? 150 TYR A C     1 
ATOM   1042 O  O     . TYR A 1 156 ? -17.532 -6.565  -10.473 1.00 29.99 ? 150 TYR A O     1 
ATOM   1043 C  CB    . TYR A 1 156 ? -19.511 -3.855  -10.244 1.00 31.32 ? 150 TYR A CB    1 
ATOM   1044 C  CG    . TYR A 1 156 ? -20.053 -3.191  -9.003  1.00 29.08 ? 150 TYR A CG    1 
ATOM   1045 C  CD1   . TYR A 1 156 ? -20.554 -3.944  -7.952  1.00 31.57 ? 150 TYR A CD1   1 
ATOM   1046 C  CD2   . TYR A 1 156 ? -20.029 -1.815  -8.863  1.00 30.61 ? 150 TYR A CD2   1 
ATOM   1047 C  CE1   . TYR A 1 156 ? -21.066 -3.338  -6.810  1.00 32.21 ? 150 TYR A CE1   1 
ATOM   1048 C  CE2   . TYR A 1 156 ? -20.543 -1.192  -7.735  1.00 33.44 ? 150 TYR A CE2   1 
ATOM   1049 C  CZ    . TYR A 1 156 ? -21.055 -1.956  -6.694  1.00 30.88 ? 150 TYR A CZ    1 
ATOM   1050 O  OH    . TYR A 1 156 ? -21.554 -1.328  -5.583  1.00 30.88 ? 150 TYR A OH    1 
ATOM   1051 N  N     . GLU A 1 157 ? -17.446 -5.289  -12.313 1.00 29.42 ? 151 GLU A N     1 
ATOM   1052 C  CA    . GLU A 1 157 ? -17.103 -6.417  -13.219 1.00 29.60 ? 151 GLU A CA    1 
ATOM   1053 C  C     . GLU A 1 157 ? -15.722 -6.944  -12.839 1.00 27.54 ? 151 GLU A C     1 
ATOM   1054 O  O     . GLU A 1 157 ? -15.540 -8.153  -12.718 1.00 29.83 ? 151 GLU A O     1 
ATOM   1055 C  CB    . GLU A 1 157 ? -17.198 -5.930  -14.670 1.00 34.85 ? 151 GLU A CB    1 
ATOM   1056 C  CG    . GLU A 1 157 ? -16.848 -6.976  -15.717 1.00 37.28 ? 151 GLU A CG    1 
ATOM   1057 C  CD    . GLU A 1 157 ? -16.965 -6.521  -17.172 1.00 44.95 ? 151 GLU A CD    1 
ATOM   1058 O  OE1   . GLU A 1 157 ? -16.349 -5.483  -17.547 1.00 45.74 ? 151 GLU A OE1   1 
ATOM   1059 O  OE2   . GLU A 1 157 ? -17.676 -7.205  -17.944 1.00 46.22 ? 151 GLU A OE2   1 
ATOM   1060 N  N     . ILE A 1 158 ? -14.748 -6.059  -12.636 1.00 24.83 ? 152 ILE A N     1 
ATOM   1061 C  CA    . ILE A 1 158 ? -13.401 -6.539  -12.210 1.00 25.10 ? 152 ILE A CA    1 
ATOM   1062 C  C     . ILE A 1 158 ? -13.513 -7.291  -10.873 1.00 22.41 ? 152 ILE A C     1 
ATOM   1063 O  O     . ILE A 1 158 ? -12.860 -8.323  -10.726 1.00 25.15 ? 152 ILE A O     1 
ATOM   1064 C  CB    . ILE A 1 158 ? -12.394 -5.380  -12.178 1.00 25.84 ? 152 ILE A CB    1 
ATOM   1065 C  CG1   . ILE A 1 158 ? -12.204 -4.808  -13.591 1.00 25.96 ? 152 ILE A CG1   1 
ATOM   1066 C  CG2   . ILE A 1 158 ? -11.097 -5.856  -11.538 1.00 25.69 ? 152 ILE A CG2   1 
ATOM   1067 C  CD1   . ILE A 1 158 ? -11.415 -3.506  -13.692 1.00 28.38 ? 152 ILE A CD1   1 
ATOM   1068 N  N     . GLY A 1 159 ? -14.262 -6.768  -9.904  1.00 25.72 ? 153 GLY A N     1 
ATOM   1069 C  CA    . GLY A 1 159 ? -14.534 -7.469  -8.640  1.00 27.52 ? 153 GLY A CA    1 
ATOM   1070 C  C     . GLY A 1 159 ? -15.035 -8.893  -8.865  1.00 29.28 ? 153 GLY A C     1 
ATOM   1071 O  O     . GLY A 1 159 ? -14.537 -9.801  -8.198  1.00 28.52 ? 153 GLY A O     1 
ATOM   1072 N  N     . SER A 1 160 ? -15.986 -9.103  -9.776  1.00 33.09 ? 154 SER A N     1 
ATOM   1073 C  CA    . SER A 1 160 ? -16.492 -10.464 -10.124 1.00 34.10 ? 154 SER A CA    1 
ATOM   1074 C  C     . SER A 1 160 ? -15.364 -11.302 -10.695 1.00 30.91 ? 154 SER A C     1 
ATOM   1075 O  O     . SER A 1 160 ? -15.253 -12.461 -10.294 1.00 33.10 ? 154 SER A O     1 
ATOM   1076 C  CB    . SER A 1 160 ? -17.617 -10.420 -11.112 1.00 38.54 ? 154 SER A CB    1 
ATOM   1077 O  OG    . SER A 1 160 ? -18.598 -9.514  -10.658 1.00 51.24 ? 154 SER A OG    1 
ATOM   1078 N  N     . TRP A 1 161 ? -14.576 -10.751 -11.620 1.00 29.24 ? 155 TRP A N     1 
ATOM   1079 C  CA    . TRP A 1 161 ? -13.471 -11.508 -12.261 1.00 28.93 ? 155 TRP A CA    1 
ATOM   1080 C  C     . TRP A 1 161 ? -12.489 -11.952 -11.188 1.00 27.69 ? 155 TRP A C     1 
ATOM   1081 O  O     . TRP A 1 161 ? -11.977 -13.060 -11.314 1.00 30.01 ? 155 TRP A O     1 
ATOM   1082 C  CB    . TRP A 1 161 ? -12.759 -10.743 -13.380 1.00 29.56 ? 155 TRP A CB    1 
ATOM   1083 C  CG    . TRP A 1 161 ? -13.604 -10.454 -14.582 1.00 33.51 ? 155 TRP A CG    1 
ATOM   1084 C  CD1   . TRP A 1 161 ? -14.752 -11.090 -14.970 1.00 32.10 ? 155 TRP A CD1   1 
ATOM   1085 C  CD2   . TRP A 1 161 ? -13.378 -9.407  -15.542 1.00 33.34 ? 155 TRP A CD2   1 
ATOM   1086 N  NE1   . TRP A 1 161 ? -15.240 -10.513 -16.106 1.00 34.86 ? 155 TRP A NE1   1 
ATOM   1087 C  CE2   . TRP A 1 161 ? -14.416 -9.485  -16.491 1.00 34.60 ? 155 TRP A CE2   1 
ATOM   1088 C  CE3   . TRP A 1 161 ? -12.378 -8.443  -15.716 1.00 31.89 ? 155 TRP A CE3   1 
ATOM   1089 C  CZ2   . TRP A 1 161 ? -14.487 -8.620  -17.583 1.00 34.16 ? 155 TRP A CZ2   1 
ATOM   1090 C  CZ3   . TRP A 1 161 ? -12.461 -7.573  -16.776 1.00 32.73 ? 155 TRP A CZ3   1 
ATOM   1091 C  CH2   . TRP A 1 161 ? -13.498 -7.670  -17.708 1.00 37.00 ? 155 TRP A CH2   1 
ATOM   1092 N  N     . CYS A 1 162 ? -12.208 -11.121 -10.185 1.00 29.40 ? 156 CYS A N     1 
ATOM   1093 C  CA    . CYS A 1 162 ? -11.219 -11.463 -9.130  1.00 28.54 ? 156 CYS A CA    1 
ATOM   1094 C  C     . CYS A 1 162 ? -11.731 -12.668 -8.327  1.00 30.38 ? 156 CYS A C     1 
ATOM   1095 O  O     . CYS A 1 162 ? -10.943 -13.529 -7.975  1.00 30.74 ? 156 CYS A O     1 
ATOM   1096 C  CB    . CYS A 1 162 ? -10.958 -10.257 -8.234  1.00 30.60 ? 156 CYS A CB    1 
ATOM   1097 S  SG    . CYS A 1 162 ? -9.923  -9.012  -9.055  1.00 31.14 ? 156 CYS A SG    1 
ATOM   1098 N  N     . GLN A 1 163 ? -13.023 -12.714 -8.050  1.00 33.90 ? 157 GLN A N     1 
ATOM   1099 C  CA    . GLN A 1 163 ? -13.651 -13.882 -7.385  1.00 36.60 ? 157 GLN A CA    1 
ATOM   1100 C  C     . GLN A 1 163 ? -13.552 -15.123 -8.287  1.00 36.41 ? 157 GLN A C     1 
ATOM   1101 O  O     . GLN A 1 163 ? -13.198 -16.179 -7.759  1.00 35.65 ? 157 GLN A O     1 
ATOM   1102 C  CB    . GLN A 1 163 ? -15.088 -13.550 -7.015  1.00 40.06 ? 157 GLN A CB    1 
ATOM   1103 C  CG    . GLN A 1 163 ? -15.682 -14.551 -6.043  1.00 49.45 ? 157 GLN A CG    1 
ATOM   1104 C  CD    . GLN A 1 163 ? -17.157 -14.635 -6.313  1.00 57.18 ? 157 GLN A CD    1 
ATOM   1105 O  OE1   . GLN A 1 163 ? -17.892 -13.684 -6.059  1.00 62.98 ? 157 GLN A OE1   1 
ATOM   1106 N  NE2   . GLN A 1 163 ? -17.581 -15.747 -6.898  1.00 67.11 ? 157 GLN A NE2   1 
ATOM   1107 N  N     . LYS A 1 164 ? -13.834 -15.014 -9.592  1.00 39.67 ? 158 LYS A N     1 
ATOM   1108 C  CA    . LYS A 1 164 ? -13.765 -16.166 -10.538 1.00 39.21 ? 158 LYS A CA    1 
ATOM   1109 C  C     . LYS A 1 164 ? -12.334 -16.715 -10.643 1.00 41.90 ? 158 LYS A C     1 
ATOM   1110 O  O     . LYS A 1 164 ? -12.223 -17.936 -10.727 1.00 38.49 ? 158 LYS A O     1 
ATOM   1111 C  CB    . LYS A 1 164 ? -14.255 -15.821 -11.947 1.00 47.93 ? 158 LYS A CB    1 
ATOM   1112 C  CG    . LYS A 1 164 ? -15.670 -15.268 -12.070 1.00 56.59 ? 158 LYS A CG    1 
ATOM   1113 C  CD    . LYS A 1 164 ? -16.730 -15.895 -11.160 1.00 65.67 ? 158 LYS A CD    1 
ATOM   1114 C  CE    . LYS A 1 164 ? -17.988 -15.051 -11.057 1.00 67.82 ? 158 LYS A CE    1 
ATOM   1115 N  NZ    . LYS A 1 164 ? -17.848 -13.988 -10.028 1.00 61.93 ? 158 LYS A NZ    1 
ATOM   1116 N  N     . TYR A 1 165 ? -11.281 -15.872 -10.674 1.00 33.25 ? 159 TYR A N     1 
ATOM   1117 C  CA    . TYR A 1 165 ? -9.891  -16.301 -11.008 1.00 34.59 ? 159 TYR A CA    1 
ATOM   1118 C  C     . TYR A 1 165 ? -9.021  -16.295 -9.751  1.00 33.25 ? 159 TYR A C     1 
ATOM   1119 O  O     . TYR A 1 165 ? -7.779  -16.454 -9.886  1.00 33.75 ? 159 TYR A O     1 
ATOM   1120 C  CB    . TYR A 1 165 ? -9.320  -15.459 -12.160 1.00 36.03 ? 159 TYR A CB    1 
ATOM   1121 C  CG    . TYR A 1 165 ? -10.138 -15.595 -13.421 1.00 36.98 ? 159 TYR A CG    1 
ATOM   1122 C  CD1   . TYR A 1 165 ? -10.152 -16.789 -14.127 1.00 38.65 ? 159 TYR A CD1   1 
ATOM   1123 C  CD2   . TYR A 1 165 ? -10.994 -14.588 -13.832 1.00 36.05 ? 159 TYR A CD2   1 
ATOM   1124 C  CE1   . TYR A 1 165 ? -10.965 -16.960 -15.237 1.00 38.93 ? 159 TYR A CE1   1 
ATOM   1125 C  CE2   . TYR A 1 165 ? -11.802 -14.734 -14.947 1.00 37.12 ? 159 TYR A CE2   1 
ATOM   1126 C  CZ    . TYR A 1 165 ? -11.794 -15.929 -15.644 1.00 37.59 ? 159 TYR A CZ    1 
ATOM   1127 O  OH    . TYR A 1 165 ? -12.578 -16.053 -16.756 1.00 40.98 ? 159 TYR A OH    1 
ATOM   1128 N  N     . ASP A 1 166 ? -9.646  -16.151 -8.567  1.00 33.34 ? 160 ASP A N     1 
ATOM   1129 C  CA    . ASP A 1 166 ? -8.988  -16.342 -7.248  1.00 33.28 ? 160 ASP A CA    1 
ATOM   1130 C  C     . ASP A 1 166 ? -7.877  -15.303 -7.085  1.00 28.96 ? 160 ASP A C     1 
ATOM   1131 O  O     . ASP A 1 166 ? -6.739  -15.662 -6.812  1.00 29.91 ? 160 ASP A O     1 
ATOM   1132 C  CB    . ASP A 1 166 ? -8.498  -17.782 -7.099  1.00 39.97 ? 160 ASP A CB    1 
ATOM   1133 C  CG    . ASP A 1 166 ? -7.920  -18.079 -5.731  1.00 45.60 ? 160 ASP A CG    1 
ATOM   1134 O  OD1   . ASP A 1 166 ? -8.506  -17.608 -4.730  1.00 55.36 ? 160 ASP A OD1   1 
ATOM   1135 O  OD2   . ASP A 1 166 ? -6.859  -18.727 -5.680  1.00 52.51 ? 160 ASP A OD2   1 
ATOM   1136 N  N     . ILE A 1 167 ? -8.230  -14.038 -7.296  1.00 28.88 ? 161 ILE A N     1 
ATOM   1137 C  CA    . ILE A 1 167 ? -7.325  -12.869 -7.143  1.00 26.45 ? 161 ILE A CA    1 
ATOM   1138 C  C     . ILE A 1 167 ? -7.904  -12.036 -5.998  1.00 25.30 ? 161 ILE A C     1 
ATOM   1139 O  O     . ILE A 1 167 ? -9.144  -11.891 -5.956  1.00 24.25 ? 161 ILE A O     1 
ATOM   1140 C  CB    . ILE A 1 167 ? -7.251  -12.075 -8.456  1.00 27.15 ? 161 ILE A CB    1 
ATOM   1141 C  CG1   . ILE A 1 167 ? -6.623  -12.904 -9.584  1.00 28.54 ? 161 ILE A CG1   1 
ATOM   1142 C  CG2   . ILE A 1 167 ? -6.517  -10.749 -8.246  1.00 26.39 ? 161 ILE A CG2   1 
ATOM   1143 C  CD1   . ILE A 1 167 ? -6.824  -12.278 -10.943 1.00 29.76 ? 161 ILE A CD1   1 
ATOM   1144 N  N     . LYS A 1 168 ? -7.071  -11.553 -5.073  1.00 24.46 ? 162 LYS A N     1 
ATOM   1145 C  CA    . LYS A 1 168 ? -7.581  -10.672 -3.970  1.00 25.09 ? 162 LYS A CA    1 
ATOM   1146 C  C     . LYS A 1 168 ? -7.947  -9.311  -4.571  1.00 25.50 ? 162 LYS A C     1 
ATOM   1147 O  O     . LYS A 1 168 ? -7.129  -8.754  -5.366  1.00 23.21 ? 162 LYS A O     1 
ATOM   1148 C  CB    . LYS A 1 168 ? -6.541  -10.596 -2.845  1.00 25.46 ? 162 LYS A CB    1 
ATOM   1149 C  CG    . LYS A 1 168 ? -6.242  -11.954 -2.228  1.00 29.39 ? 162 LYS A CG    1 
ATOM   1150 C  CD    . LYS A 1 168 ? -5.041  -11.996 -1.293  1.00 33.48 ? 162 LYS A CD    1 
ATOM   1151 C  CE    . LYS A 1 168 ? -5.262  -11.308 0.032   1.00 37.11 ? 162 LYS A CE    1 
ATOM   1152 N  NZ    . LYS A 1 168 ? -6.535  -11.709 0.676   1.00 40.17 ? 162 LYS A NZ    1 
ATOM   1153 N  N     . PHE A 1 169 ? -9.116  -8.795  -4.237  1.00 22.90 ? 163 PHE A N     1 
ATOM   1154 C  CA    . PHE A 1 169 ? -9.657  -7.571  -4.855  1.00 25.54 ? 163 PHE A CA    1 
ATOM   1155 C  C     . PHE A 1 169 ? -9.405  -6.382  -3.924  1.00 23.78 ? 163 PHE A C     1 
ATOM   1156 O  O     . PHE A 1 169 ? -9.880  -6.379  -2.788  1.00 22.19 ? 163 PHE A O     1 
ATOM   1157 C  CB    . PHE A 1 169 ? -11.122 -7.771  -5.207  1.00 25.18 ? 163 PHE A CB    1 
ATOM   1158 C  CG    . PHE A 1 169 ? -11.815 -6.568  -5.775  1.00 26.97 ? 163 PHE A CG    1 
ATOM   1159 C  CD1   . PHE A 1 169 ? -11.346 -5.956  -6.926  1.00 27.34 ? 163 PHE A CD1   1 
ATOM   1160 C  CD2   . PHE A 1 169 ? -12.998 -6.110  -5.220  1.00 27.94 ? 163 PHE A CD2   1 
ATOM   1161 C  CE1   . PHE A 1 169 ? -12.015 -4.874  -7.471  1.00 29.59 ? 163 PHE A CE1   1 
ATOM   1162 C  CE2   . PHE A 1 169 ? -13.637 -4.998  -5.738  1.00 32.11 ? 163 PHE A CE2   1 
ATOM   1163 C  CZ    . PHE A 1 169 ? -13.157 -4.393  -6.876  1.00 30.11 ? 163 PHE A CZ    1 
ATOM   1164 N  N     . LYS A 1 170 ? -8.715  -5.374  -4.462  1.00 20.67 ? 164 LYS A N     1 
ATOM   1165 C  CA    . LYS A 1 170 ? -8.306  -4.160  -3.729  1.00 21.64 ? 164 LYS A CA    1 
ATOM   1166 C  C     . LYS A 1 170 ? -8.853  -2.915  -4.426  1.00 20.22 ? 164 LYS A C     1 
ATOM   1167 O  O     . LYS A 1 170 ? -8.881  -2.872  -5.639  1.00 20.67 ? 164 LYS A O     1 
ATOM   1168 C  CB    . LYS A 1 170 ? -6.784  -4.154  -3.663  1.00 21.28 ? 164 LYS A CB    1 
ATOM   1169 C  CG    . LYS A 1 170 ? -6.157  -2.890  -3.099  1.00 20.53 ? 164 LYS A CG    1 
ATOM   1170 C  CD    . LYS A 1 170 ? -4.680  -3.081  -2.812  1.00 21.88 ? 164 LYS A CD    1 
ATOM   1171 C  CE    . LYS A 1 170 ? -3.907  -1.767  -2.775  1.00 23.37 ? 164 LYS A CE    1 
ATOM   1172 N  NZ    . LYS A 1 170 ? -2.469  -1.998  -3.009  1.00 24.75 ? 164 LYS A NZ    1 
ATOM   1173 N  N     . LEU A 1 171 ? -9.302  -1.932  -3.654  1.00 19.35 ? 165 LEU A N     1 
ATOM   1174 C  CA    . LEU A 1 171 ? -9.827  -0.655  -4.149  1.00 18.30 ? 165 LEU A CA    1 
ATOM   1175 C  C     . LEU A 1 171 ? -8.909  0.482   -3.652  1.00 19.69 ? 165 LEU A C     1 
ATOM   1176 O  O     . LEU A 1 171 ? -8.575  0.513   -2.464  1.00 19.00 ? 165 LEU A O     1 
ATOM   1177 C  CB    . LEU A 1 171 ? -11.257 -0.541  -3.633  1.00 21.60 ? 165 LEU A CB    1 
ATOM   1178 C  CG    . LEU A 1 171 ? -11.951 0.793   -3.922  1.00 23.24 ? 165 LEU A CG    1 
ATOM   1179 C  CD1   . LEU A 1 171 ? -12.085 1.036   -5.419  1.00 25.26 ? 165 LEU A CD1   1 
ATOM   1180 C  CD2   . LEU A 1 171 ? -13.293 0.842   -3.246  1.00 25.67 ? 165 LEU A CD2   1 
ATOM   1181 N  N     . ASN A 1 172 ? -8.529  1.399   -4.536  1.00 19.44 ? 166 ASN A N     1 
ATOM   1182 C  CA    . ASN A 1 172 ? -7.699  2.592   -4.226  1.00 18.47 ? 166 ASN A CA    1 
ATOM   1183 C  C     . ASN A 1 172 ? -8.525  3.838   -4.499  1.00 18.56 ? 166 ASN A C     1 
ATOM   1184 O  O     . ASN A 1 172 ? -9.084  3.951   -5.598  1.00 18.61 ? 166 ASN A O     1 
ATOM   1185 C  CB    . ASN A 1 172 ? -6.387  2.638   -5.016  1.00 19.06 ? 166 ASN A CB    1 
ATOM   1186 C  CG    . ASN A 1 172 ? -5.316  1.661   -4.561  1.00 19.23 ? 166 ASN A CG    1 
ATOM   1187 O  OD1   . ASN A 1 172 ? -5.548  0.796   -3.714  1.00 21.66 ? 166 ASN A OD1   1 
ATOM   1188 N  ND2   . ASN A 1 172 ? -4.104  1.790   -5.110  1.00 18.33 ? 166 ASN A ND2   1 
ATOM   1189 N  N     . THR A 1 173 ? -8.601  4.734   -3.527  1.00 16.92 ? 167 THR A N     1 
ATOM   1190 C  CA    . THR A 1 173 ? -9.382  5.989   -3.580  1.00 18.73 ? 167 THR A CA    1 
ATOM   1191 C  C     . THR A 1 173 ? -8.447  7.120   -3.209  1.00 19.77 ? 167 THR A C     1 
ATOM   1192 O  O     . THR A 1 173 ? -7.879  7.014   -2.136  1.00 18.25 ? 167 THR A O     1 
ATOM   1193 C  CB    . THR A 1 173 ? -10.591 5.937   -2.635  1.00 20.33 ? 167 THR A CB    1 
ATOM   1194 O  OG1   . THR A 1 173 ? -11.387 4.885   -3.159  1.00 21.36 ? 167 THR A OG1   1 
ATOM   1195 C  CG2   . THR A 1 173 ? -11.386 7.224   -2.558  1.00 20.33 ? 167 THR A CG2   1 
ATOM   1196 N  N     . VAL A 1 174 ? -8.389  8.161   -4.036  1.00 18.61 ? 168 VAL A N     1 
ATOM   1197 C  CA    . VAL A 1 174 ? -7.728  9.437   -3.714  1.00 18.83 ? 168 VAL A CA    1 
ATOM   1198 C  C     . VAL A 1 174 ? -8.787  10.373  -3.144  1.00 18.50 ? 168 VAL A C     1 
ATOM   1199 O  O     . VAL A 1 174 ? -9.743  10.653  -3.849  1.00 19.06 ? 168 VAL A O     1 
ATOM   1200 C  CB    . VAL A 1 174 ? -7.044  10.054  -4.935  1.00 19.17 ? 168 VAL A CB    1 
ATOM   1201 C  CG1   . VAL A 1 174 ? -6.431  11.398  -4.619  1.00 18.80 ? 168 VAL A CG1   1 
ATOM   1202 C  CG2   . VAL A 1 174 ? -6.014  9.084   -5.506  1.00 19.79 ? 168 VAL A CG2   1 
ATOM   1203 N  N     . VAL A 1 175 ? -8.606  10.786  -1.908  1.00 17.60 ? 169 VAL A N     1 
ATOM   1204 C  CA    . VAL A 1 175 ? -9.599  11.653  -1.215  1.00 18.87 ? 169 VAL A CA    1 
ATOM   1205 C  C     . VAL A 1 175 ? -9.160  13.071  -1.541  1.00 19.11 ? 169 VAL A C     1 
ATOM   1206 O  O     . VAL A 1 175 ? -8.068  13.469  -1.158  1.00 19.86 ? 169 VAL A O     1 
ATOM   1207 C  CB    . VAL A 1 175 ? -9.681  11.386  0.300   1.00 18.61 ? 169 VAL A CB    1 
ATOM   1208 C  CG1   . VAL A 1 175 ? -10.781 12.178  0.953   1.00 18.79 ? 169 VAL A CG1   1 
ATOM   1209 C  CG2   . VAL A 1 175 ? -9.831  9.916   0.610   1.00 18.95 ? 169 VAL A CG2   1 
ATOM   1210 N  N     . ASN A 1 176 ? -10.010 13.804  -2.222  1.00 18.50 ? 170 ASN A N     1 
ATOM   1211 C  CA    . ASN A 1 176 ? -9.638  15.129  -2.778  1.00 19.44 ? 170 ASN A CA    1 
ATOM   1212 C  C     . ASN A 1 176 ? -10.844 16.072  -2.622  1.00 19.85 ? 170 ASN A C     1 
ATOM   1213 O  O     . ASN A 1 176 ? -11.899 15.651  -2.104  1.00 21.41 ? 170 ASN A O     1 
ATOM   1214 C  CB    . ASN A 1 176 ? -9.091  14.955  -4.201  1.00 21.71 ? 170 ASN A CB    1 
ATOM   1215 C  CG    . ASN A 1 176 ? -10.174 14.464  -5.132  1.00 23.49 ? 170 ASN A CG    1 
ATOM   1216 O  OD1   . ASN A 1 176 ? -10.932 15.291  -5.616  1.00 25.67 ? 170 ASN A OD1   1 
ATOM   1217 N  ND2   . ASN A 1 176 ? -10.266 13.150  -5.358  1.00 21.03 ? 170 ASN A ND2   1 
ATOM   1218 N  N     . LYS A 1 177 ? -10.697 17.310  -3.063  1.00 22.29 ? 171 LYS A N     1 
ATOM   1219 C  CA    . LYS A 1 177 ? -11.745 18.348  -2.909  1.00 25.05 ? 171 LYS A CA    1 
ATOM   1220 C  C     . LYS A 1 177 ? -13.045 17.892  -3.569  1.00 23.94 ? 171 LYS A C     1 
ATOM   1221 O  O     . LYS A 1 177 ? -14.120 18.259  -3.057  1.00 23.93 ? 171 LYS A O     1 
ATOM   1222 C  CB    . LYS A 1 177 ? -11.268 19.683  -3.481  1.00 29.32 ? 171 LYS A CB    1 
ATOM   1223 C  CG    . LYS A 1 177 ? -12.014 20.907  -2.973  1.00 39.48 ? 171 LYS A CG    1 
ATOM   1224 C  CD    . LYS A 1 177 ? -12.246 20.892  -1.461  1.00 44.67 ? 171 LYS A CD    1 
ATOM   1225 C  CE    . LYS A 1 177 ? -12.148 22.256  -0.821  1.00 51.73 ? 171 LYS A CE    1 
ATOM   1226 N  NZ    . LYS A 1 177 ? -10.793 22.441  -0.256  1.00 53.80 ? 171 LYS A NZ    1 
ATOM   1227 N  N     . PHE A 1 178 ? -13.006 17.082  -4.621  1.00 24.62 ? 172 PHE A N     1 
ATOM   1228 C  CA    . PHE A 1 178 ? -14.265 16.725  -5.349  1.00 25.93 ? 172 PHE A CA    1 
ATOM   1229 C  C     . PHE A 1 178 ? -15.023 15.601  -4.651  1.00 23.98 ? 172 PHE A C     1 
ATOM   1230 O  O     . PHE A 1 178 ? -16.225 15.447  -4.933  1.00 24.71 ? 172 PHE A O     1 
ATOM   1231 C  CB    . PHE A 1 178 ? -13.982 16.301  -6.793  1.00 28.86 ? 172 PHE A CB    1 
ATOM   1232 C  CG    . PHE A 1 178 ? -13.480 17.404  -7.696  1.00 31.91 ? 172 PHE A CG    1 
ATOM   1233 C  CD1   . PHE A 1 178 ? -14.017 18.683  -7.645  1.00 43.14 ? 172 PHE A CD1   1 
ATOM   1234 C  CD2   . PHE A 1 178 ? -12.509 17.147  -8.642  1.00 36.50 ? 172 PHE A CD2   1 
ATOM   1235 C  CE1   . PHE A 1 178 ? -13.575 19.684  -8.503  1.00 45.01 ? 172 PHE A CE1   1 
ATOM   1236 C  CE2   . PHE A 1 178 ? -12.062 18.146  -9.492  1.00 37.32 ? 172 PHE A CE2   1 
ATOM   1237 C  CZ    . PHE A 1 178 ? -12.583 19.413  -9.414  1.00 40.25 ? 172 PHE A CZ    1 
ATOM   1238 N  N     . ASN A 1 179 ? -14.385 14.748  -3.841  1.00 21.31 ? 173 ASN A N     1 
ATOM   1239 C  CA    . ASN A 1 179 ? -15.079 13.564  -3.283  1.00 20.00 ? 173 ASN A CA    1 
ATOM   1240 C  C     . ASN A 1 179 ? -15.037 13.484  -1.747  1.00 20.22 ? 173 ASN A C     1 
ATOM   1241 O  O     . ASN A 1 179 ? -15.539 12.528  -1.205  1.00 20.63 ? 173 ASN A O     1 
ATOM   1242 C  CB    . ASN A 1 179 ? -14.539 12.258  -3.881  1.00 20.79 ? 173 ASN A CB    1 
ATOM   1243 C  CG    . ASN A 1 179 ? -13.097 12.009  -3.497  1.00 21.85 ? 173 ASN A CG    1 
ATOM   1244 O  OD1   . ASN A 1 179 ? -12.482 12.833  -2.829  1.00 21.59 ? 173 ASN A OD1   1 
ATOM   1245 N  ND2   . ASN A 1 179 ? -12.570 10.853  -3.884  1.00 21.60 ? 173 ASN A ND2   1 
ATOM   1246 N  N     . HIS A 1 180 ? -14.446 14.422  -1.029  1.00 19.77 ? 174 HIS A N     1 
ATOM   1247 C  CA    . HIS A 1 180 ? -14.127 14.184  0.404   1.00 22.09 ? 174 HIS A CA    1 
ATOM   1248 C  C     . HIS A 1 180 ? -15.399 14.161  1.284   1.00 23.12 ? 174 HIS A C     1 
ATOM   1249 O  O     . HIS A 1 180 ? -15.314 13.656  2.386   1.00 20.83 ? 174 HIS A O     1 
ATOM   1250 C  CB    . HIS A 1 180 ? -13.087 15.196  0.871   1.00 21.82 ? 174 HIS A CB    1 
ATOM   1251 C  CG    . HIS A 1 180 ? -13.576 16.582  1.078   1.00 23.85 ? 174 HIS A CG    1 
ATOM   1252 N  ND1   . HIS A 1 180 ? -13.907 17.039  2.342   1.00 25.33 ? 174 HIS A ND1   1 
ATOM   1253 C  CD2   . HIS A 1 180 ? -13.820 17.582  0.215   1.00 23.32 ? 174 HIS A CD2   1 
ATOM   1254 C  CE1   . HIS A 1 180 ? -14.322 18.283  2.242   1.00 27.55 ? 174 HIS A CE1   1 
ATOM   1255 N  NE2   . HIS A 1 180 ? -14.270 18.649  0.938   1.00 27.08 ? 174 HIS A NE2   1 
ATOM   1256 N  N     . LEU A 1 181 ? -16.540 14.655  0.775   1.00 22.80 ? 175 LEU A N     1 
ATOM   1257 C  CA    . LEU A 1 181 ? -17.826 14.685  1.520   1.00 22.23 ? 175 LEU A CA    1 
ATOM   1258 C  C     . LEU A 1 181 ? -18.661 13.452  1.217   1.00 23.70 ? 175 LEU A C     1 
ATOM   1259 O  O     . LEU A 1 181 ? -19.688 13.296  1.867   1.00 23.64 ? 175 LEU A O     1 
ATOM   1260 C  CB    . LEU A 1 181 ? -18.572 15.941  1.108   1.00 23.54 ? 175 LEU A CB    1 
ATOM   1261 C  CG    . LEU A 1 181 ? -17.838 17.219  1.446   1.00 25.30 ? 175 LEU A CG    1 
ATOM   1262 C  CD1   . LEU A 1 181 ? -18.615 18.420  0.927   1.00 28.12 ? 175 LEU A CD1   1 
ATOM   1263 C  CD2   . LEU A 1 181 ? -17.610 17.297  2.948   1.00 28.49 ? 175 LEU A CD2   1 
ATOM   1264 N  N     . GLU A 1 182 ? -18.224 12.593  0.286   1.00 21.73 ? 176 GLU A N     1 
ATOM   1265 C  CA    . GLU A 1 182 ? -19.051 11.486  -0.225  1.00 22.66 ? 176 GLU A CA    1 
ATOM   1266 C  C     . GLU A 1 182 ? -19.122 10.381  0.831   1.00 24.80 ? 176 GLU A C     1 
ATOM   1267 O  O     . GLU A 1 182 ? -18.113 10.127  1.516   1.00 22.20 ? 176 GLU A O     1 
ATOM   1268 C  CB    . GLU A 1 182 ? -18.478 10.984  -1.554  1.00 22.23 ? 176 GLU A CB    1 
ATOM   1269 C  CG    . GLU A 1 182 ? -19.249 9.859   -2.231  1.00 22.65 ? 176 GLU A CG    1 
ATOM   1270 C  CD    . GLU A 1 182 ? -18.683 9.476   -3.601  1.00 22.05 ? 176 GLU A CD    1 
ATOM   1271 O  OE1   . GLU A 1 182 ? -18.069 10.362  -4.245  1.00 26.57 ? 176 GLU A OE1   1 
ATOM   1272 O  OE2   . GLU A 1 182 ? -18.856 8.312   -4.018  1.00 25.19 ? 176 GLU A OE2   1 
ATOM   1273 N  N     . ASP A 1 183 ? -20.308 9.788   0.977   1.00 22.55 ? 177 ASP A N     1 
ATOM   1274 C  CA    . ASP A 1 183 ? -20.585 8.529   1.729   1.00 24.44 ? 177 ASP A CA    1 
ATOM   1275 C  C     . ASP A 1 183 ? -20.607 7.369   0.727   1.00 23.98 ? 177 ASP A C     1 
ATOM   1276 O  O     . ASP A 1 183 ? -21.566 7.262   -0.097  1.00 24.01 ? 177 ASP A O     1 
ATOM   1277 C  CB    . ASP A 1 183 ? -21.898 8.650   2.513   1.00 26.60 ? 177 ASP A CB    1 
ATOM   1278 C  CG    . ASP A 1 183 ? -22.358 7.379   3.221   1.00 26.99 ? 177 ASP A CG    1 
ATOM   1279 O  OD1   . ASP A 1 183 ? -21.687 6.333   3.074   1.00 26.37 ? 177 ASP A OD1   1 
ATOM   1280 O  OD2   . ASP A 1 183 ? -23.366 7.467   3.971   1.00 32.39 ? 177 ASP A OD2   1 
ATOM   1281 N  N     . MET A 1 184 ? -19.584 6.509   0.787   1.00 22.44 ? 178 MET A N     1 
ATOM   1282 C  CA    . MET A 1 184 ? -19.382 5.374   -0.129  1.00 21.50 ? 178 MET A CA    1 
ATOM   1283 C  C     . MET A 1 184 ? -19.725 4.038   0.556   1.00 22.57 ? 178 MET A C     1 
ATOM   1284 O  O     . MET A 1 184 ? -19.478 2.993   -0.068  1.00 22.80 ? 178 MET A O     1 
ATOM   1285 C  CB    . MET A 1 184 ? -17.918 5.355   -0.563  1.00 23.00 ? 178 MET A CB    1 
ATOM   1286 C  CG    . MET A 1 184 ? -17.449 6.674   -1.136  1.00 24.80 ? 178 MET A CG    1 
ATOM   1287 S  SD    . MET A 1 184 ? -15.741 6.531   -1.760  1.00 26.80 ? 178 MET A SD    1 
ATOM   1288 C  CE    . MET A 1 184 ? -15.472 8.218   -2.276  1.00 24.50 ? 178 MET A CE    1 
ATOM   1289 N  N     . ASN A 1 185 ? -20.278 4.036   1.784   1.00 20.98 ? 179 ASN A N     1 
ATOM   1290 C  CA    . ASN A 1 185 ? -20.513 2.804   2.580   1.00 20.73 ? 179 ASN A CA    1 
ATOM   1291 C  C     . ASN A 1 185 ? -21.338 1.758   1.806   1.00 22.37 ? 179 ASN A C     1 
ATOM   1292 O  O     . ASN A 1 185 ? -20.983 0.565   1.826   1.00 21.86 ? 179 ASN A O     1 
ATOM   1293 C  CB    . ASN A 1 185 ? -21.152 3.160   3.931   1.00 23.68 ? 179 ASN A CB    1 
ATOM   1294 C  CG    . ASN A 1 185 ? -20.141 3.798   4.876   1.00 24.48 ? 179 ASN A CG    1 
ATOM   1295 O  OD1   . ASN A 1 185 ? -19.225 3.104   5.321   1.00 23.95 ? 179 ASN A OD1   1 
ATOM   1296 N  ND2   . ASN A 1 185 ? -20.249 5.096   5.122   1.00 22.22 ? 179 ASN A ND2   1 
ATOM   1297 N  N     . ASP A 1 186 ? -22.394 2.177   1.105   1.00 26.25 ? 180 ASP A N     1 
ATOM   1298 C  CA    . ASP A 1 186 ? -23.344 1.228   0.467   1.00 30.55 ? 180 ASP A CA    1 
ATOM   1299 C  C     . ASP A 1 186 ? -22.632 0.445   -0.642  1.00 27.86 ? 180 ASP A C     1 
ATOM   1300 O  O     . ASP A 1 186 ? -22.795 -0.766  -0.716  1.00 29.09 ? 180 ASP A O     1 
ATOM   1301 C  CB    . ASP A 1 186 ? -24.581 1.970   -0.037  1.00 38.71 ? 180 ASP A CB    1 
ATOM   1302 C  CG    . ASP A 1 186 ? -25.719 1.026   -0.400  1.00 49.00 ? 180 ASP A CG    1 
ATOM   1303 O  OD1   . ASP A 1 186 ? -26.134 0.238   0.475   1.00 58.96 ? 180 ASP A OD1   1 
ATOM   1304 O  OD2   . ASP A 1 186 ? -26.139 1.048   -1.562  1.00 57.03 ? 180 ASP A OD2   1 
ATOM   1305 N  N     . HIS A 1 187 ? -21.813 1.117   -1.448  1.00 29.62 ? 181 HIS A N     1 
ATOM   1306 C  CA    . HIS A 1 187 ? -20.974 0.480   -2.492  1.00 28.92 ? 181 HIS A CA    1 
ATOM   1307 C  C     . HIS A 1 187 ? -19.875 -0.377  -1.853  1.00 27.16 ? 181 HIS A C     1 
ATOM   1308 O  O     . HIS A 1 187 ? -19.682 -1.502  -2.311  1.00 27.41 ? 181 HIS A O     1 
ATOM   1309 C  CB    . HIS A 1 187 ? -20.423 1.546   -3.440  1.00 29.93 ? 181 HIS A CB    1 
ATOM   1310 C  CG    . HIS A 1 187 ? -21.448 2.093   -4.371  1.00 31.11 ? 181 HIS A CG    1 
ATOM   1311 N  ND1   . HIS A 1 187 ? -21.907 1.364   -5.433  1.00 33.04 ? 181 HIS A ND1   1 
ATOM   1312 C  CD2   . HIS A 1 187 ? -22.094 3.272   -4.403  1.00 33.35 ? 181 HIS A CD2   1 
ATOM   1313 C  CE1   . HIS A 1 187 ? -22.804 2.069   -6.089  1.00 38.34 ? 181 HIS A CE1   1 
ATOM   1314 N  NE2   . HIS A 1 187 ? -22.914 3.255   -5.490  1.00 34.16 ? 181 HIS A NE2   1 
ATOM   1315 N  N     . LEU A 1 188 ? -19.163 0.111   -0.828  1.00 26.43 ? 182 LEU A N     1 
ATOM   1316 C  CA    . LEU A 1 188 ? -18.129 -0.726  -0.169  1.00 24.46 ? 182 LEU A CA    1 
ATOM   1317 C  C     . LEU A 1 188 ? -18.748 -2.016  0.406   1.00 24.62 ? 182 LEU A C     1 
ATOM   1318 O  O     . LEU A 1 188 ? -18.066 -3.088  0.412   1.00 23.45 ? 182 LEU A O     1 
ATOM   1319 C  CB    . LEU A 1 188 ? -17.401 0.083   0.913   1.00 24.78 ? 182 LEU A CB    1 
ATOM   1320 C  CG    . LEU A 1 188 ? -16.084 0.734   0.464   1.00 26.52 ? 182 LEU A CG    1 
ATOM   1321 C  CD1   . LEU A 1 188 ? -14.997 -0.322  0.186   1.00 27.13 ? 182 LEU A CD1   1 
ATOM   1322 C  CD2   . LEU A 1 188 ? -16.290 1.616   -0.740  1.00 26.01 ? 182 LEU A CD2   1 
ATOM   1323 N  N     . ASN A 1 189 ? -19.968 -1.937  0.950   1.00 26.06 ? 183 ASN A N     1 
ATOM   1324 C  CA    . ASN A 1 189 ? -20.690 -3.109  1.544   1.00 27.08 ? 183 ASN A CA    1 
ATOM   1325 C  C     . ASN A 1 189 ? -21.052 -4.119  0.436   1.00 28.35 ? 183 ASN A C     1 
ATOM   1326 O  O     . ASN A 1 189 ? -21.037 -5.317  0.703   1.00 31.90 ? 183 ASN A O     1 
ATOM   1327 C  CB    . ASN A 1 189 ? -21.945 -2.666  2.312   1.00 27.93 ? 183 ASN A CB    1 
ATOM   1328 C  CG    . ASN A 1 189 ? -21.612 -1.968  3.614   1.00 30.87 ? 183 ASN A CG    1 
ATOM   1329 O  OD1   . ASN A 1 189 ? -20.489 -2.052  4.091   1.00 29.78 ? 183 ASN A OD1   1 
ATOM   1330 N  ND2   . ASN A 1 189 ? -22.563 -1.252  4.184   1.00 32.31 ? 183 ASN A ND2   1 
ATOM   1331 N  N     . ALA A 1 190 ? -21.325 -3.665  -0.787  1.00 28.88 ? 184 ALA A N     1 
ATOM   1332 C  CA    . ALA A 1 190 ? -21.605 -4.559  -1.937  1.00 28.04 ? 184 ALA A CA    1 
ATOM   1333 C  C     . ALA A 1 190 ? -20.286 -5.133  -2.498  1.00 31.06 ? 184 ALA A C     1 
ATOM   1334 O  O     . ALA A 1 190 ? -20.203 -6.349  -2.659  1.00 32.57 ? 184 ALA A O     1 
ATOM   1335 C  CB    . ALA A 1 190 ? -22.433 -3.817  -2.965  1.00 27.81 ? 184 ALA A CB    1 
ATOM   1336 N  N     . LEU A 1 191 ? -19.256 -4.307  -2.738  1.00 31.19 ? 185 LEU A N     1 
ATOM   1337 C  CA    . LEU A 1 191 ? -17.958 -4.709  -3.388  1.00 30.36 ? 185 LEU A CA    1 
ATOM   1338 C  C     . LEU A 1 191 ? -17.092 -5.555  -2.466  1.00 29.86 ? 185 LEU A C     1 
ATOM   1339 O  O     . LEU A 1 191 ? -16.418 -6.468  -2.976  1.00 29.13 ? 185 LEU A O     1 
ATOM   1340 C  CB    . LEU A 1 191 ? -17.153 -3.463  -3.759  1.00 29.99 ? 185 LEU A CB    1 
ATOM   1341 C  CG    . LEU A 1 191 ? -17.656 -2.723  -4.984  1.00 34.11 ? 185 LEU A CG    1 
ATOM   1342 C  CD1   . LEU A 1 191 ? -17.090 -1.309  -5.044  1.00 37.37 ? 185 LEU A CD1   1 
ATOM   1343 C  CD2   . LEU A 1 191 ? -17.319 -3.503  -6.251  1.00 36.26 ? 185 LEU A CD2   1 
ATOM   1344 N  N     . GLN A 1 192 ? -17.040 -5.209  -1.177  1.00 29.53 ? 186 GLN A N     1 
ATOM   1345 C  CA    . GLN A 1 192 ? -16.271 -5.960  -0.153  1.00 31.26 ? 186 GLN A CA    1 
ATOM   1346 C  C     . GLN A 1 192 ? -14.824 -6.217  -0.585  1.00 30.33 ? 186 GLN A C     1 
ATOM   1347 O  O     . GLN A 1 192 ? -14.328 -7.345  -0.523  1.00 28.04 ? 186 GLN A O     1 
ATOM   1348 C  CB    . GLN A 1 192 ? -16.988 -7.278  0.142   1.00 38.76 ? 186 GLN A CB    1 
ATOM   1349 C  CG    . GLN A 1 192 ? -18.389 -7.079  0.706   1.00 42.33 ? 186 GLN A CG    1 
ATOM   1350 C  CD    . GLN A 1 192 ? -19.066 -8.393  1.027   1.00 48.21 ? 186 GLN A CD    1 
ATOM   1351 O  OE1   . GLN A 1 192 ? -20.242 -8.582  0.747   1.00 52.10 ? 186 GLN A OE1   1 
ATOM   1352 N  NE2   . GLN A 1 192 ? -18.320 -9.317  1.612   1.00 49.66 ? 186 GLN A NE2   1 
ATOM   1353 N  N     . PRO A 1 193 ? -14.033 -5.173  -0.931  1.00 26.23 ? 187 PRO A N     1 
ATOM   1354 C  CA    . PRO A 1 193 ? -12.602 -5.391  -1.160  1.00 25.42 ? 187 PRO A CA    1 
ATOM   1355 C  C     . PRO A 1 193 ? -11.941 -5.824  0.146   1.00 25.71 ? 187 PRO A C     1 
ATOM   1356 O  O     . PRO A 1 193 ? -12.411 -5.407  1.172   1.00 27.61 ? 187 PRO A O     1 
ATOM   1357 C  CB    . PRO A 1 193 ? -12.097 -4.019  -1.626  1.00 23.13 ? 187 PRO A CB    1 
ATOM   1358 C  CG    . PRO A 1 193 ? -13.080 -3.037  -1.041  1.00 24.20 ? 187 PRO A CG    1 
ATOM   1359 C  CD    . PRO A 1 193 ? -14.427 -3.763  -1.032  1.00 24.23 ? 187 PRO A CD    1 
ATOM   1360 N  N     . PHE A 1 194 ? -10.905 -6.649  0.106   1.00 24.88 ? 188 PHE A N     1 
ATOM   1361 C  CA    . PHE A 1 194 ? -10.191 -7.069  1.324   1.00 24.38 ? 188 PHE A CA    1 
ATOM   1362 C  C     . PHE A 1 194 ? -9.364  -5.877  1.818   1.00 25.59 ? 188 PHE A C     1 
ATOM   1363 O  O     . PHE A 1 194 ? -9.061  -5.834  2.998   1.00 25.46 ? 188 PHE A O     1 
ATOM   1364 C  CB    . PHE A 1 194 ? -9.352  -8.327  1.088   1.00 25.64 ? 188 PHE A CB    1 
ATOM   1365 C  CG    . PHE A 1 194 ? -7.956  -8.050  0.593   1.00 25.57 ? 188 PHE A CG    1 
ATOM   1366 C  CD1   . PHE A 1 194 ? -7.749  -7.726  -0.744  1.00 25.50 ? 188 PHE A CD1   1 
ATOM   1367 C  CD2   . PHE A 1 194 ? -6.868  -8.073  1.449   1.00 25.84 ? 188 PHE A CD2   1 
ATOM   1368 C  CE1   . PHE A 1 194 ? -6.465  -7.484  -1.215  1.00 24.64 ? 188 PHE A CE1   1 
ATOM   1369 C  CE2   . PHE A 1 194 ? -5.596  -7.789  0.978   1.00 25.98 ? 188 PHE A CE2   1 
ATOM   1370 C  CZ    . PHE A 1 194 ? -5.399  -7.512  -0.352  1.00 25.29 ? 188 PHE A CZ    1 
ATOM   1371 N  N     . ARG A 1 195 ? -9.069  -4.904  0.950   1.00 22.48 ? 189 ARG A N     1 
ATOM   1372 C  CA    . ARG A 1 195 ? -8.150  -3.780  1.249   1.00 21.22 ? 189 ARG A CA    1 
ATOM   1373 C  C     . ARG A 1 195 ? -8.623  -2.572  0.450   1.00 20.86 ? 189 ARG A C     1 
ATOM   1374 O  O     . ARG A 1 195 ? -8.859  -2.722  -0.751  1.00 20.28 ? 189 ARG A O     1 
ATOM   1375 C  CB    . ARG A 1 195 ? -6.739  -4.207  0.870   1.00 21.50 ? 189 ARG A CB    1 
ATOM   1376 C  CG    . ARG A 1 195 ? -5.646  -3.249  1.293   1.00 21.38 ? 189 ARG A CG    1 
ATOM   1377 C  CD    . ARG A 1 195 ? -4.334  -3.967  1.094   1.00 20.55 ? 189 ARG A CD    1 
ATOM   1378 N  NE    . ARG A 1 195 ? -3.161  -3.171  1.472   1.00 20.60 ? 189 ARG A NE    1 
ATOM   1379 C  CZ    . ARG A 1 195 ? -2.672  -3.051  2.696   1.00 22.77 ? 189 ARG A CZ    1 
ATOM   1380 N  NH1   . ARG A 1 195 ? -3.268  -3.636  3.723   1.00 21.83 ? 189 ARG A NH1   1 
ATOM   1381 N  NH2   . ARG A 1 195 ? -1.571  -2.354  2.900   1.00 22.68 ? 189 ARG A NH2   1 
ATOM   1382 N  N     . TRP A 1 196 ? -8.876  -1.461  1.141   1.00 20.50 ? 190 TRP A N     1 
ATOM   1383 C  CA    . TRP A 1 196 ? -9.374  -0.198  0.572   1.00 20.68 ? 190 TRP A CA    1 
ATOM   1384 C  C     . TRP A 1 196 ? -8.417  0.909   0.980   1.00 23.03 ? 190 TRP A C     1 
ATOM   1385 O  O     . TRP A 1 196 ? -8.527  1.404   2.123   1.00 21.21 ? 190 TRP A O     1 
ATOM   1386 C  CB    . TRP A 1 196 ? -10.805 0.083   1.021   1.00 21.71 ? 190 TRP A CB    1 
ATOM   1387 C  CG    . TRP A 1 196 ? -11.362 1.363   0.495   1.00 19.95 ? 190 TRP A CG    1 
ATOM   1388 C  CD1   . TRP A 1 196 ? -11.036 1.950   -0.695  1.00 21.52 ? 190 TRP A CD1   1 
ATOM   1389 C  CD2   . TRP A 1 196 ? -12.371 2.192   1.096   1.00 20.04 ? 190 TRP A CD2   1 
ATOM   1390 N  NE1   . TRP A 1 196 ? -11.735 3.101   -0.858  1.00 21.82 ? 190 TRP A NE1   1 
ATOM   1391 C  CE2   . TRP A 1 196 ? -12.546 3.294   0.235   1.00 19.95 ? 190 TRP A CE2   1 
ATOM   1392 C  CE3   . TRP A 1 196 ? -13.082 2.153   2.304   1.00 21.74 ? 190 TRP A CE3   1 
ATOM   1393 C  CZ2   . TRP A 1 196 ? -13.463 4.316   0.494   1.00 20.06 ? 190 TRP A CZ2   1 
ATOM   1394 C  CZ3   . TRP A 1 196 ? -13.960 3.181   2.583   1.00 22.00 ? 190 TRP A CZ3   1 
ATOM   1395 C  CH2   . TRP A 1 196 ? -14.145 4.239   1.687   1.00 22.09 ? 190 TRP A CH2   1 
ATOM   1396 N  N     . LYS A 1 197 ? -7.519  1.283   0.064   1.00 20.07 ? 191 LYS A N     1 
ATOM   1397 C  CA    . LYS A 1 197 ? -6.567  2.377   0.318   1.00 20.34 ? 191 LYS A CA    1 
ATOM   1398 C  C     . LYS A 1 197 ? -7.294  3.701   0.150   1.00 20.38 ? 191 LYS A C     1 
ATOM   1399 O  O     . LYS A 1 197 ? -7.890  3.896   -0.915  1.00 19.12 ? 191 LYS A O     1 
ATOM   1400 C  CB    . LYS A 1 197 ? -5.412  2.305   -0.659  1.00 23.43 ? 191 LYS A CB    1 
ATOM   1401 C  CG    . LYS A 1 197 ? -4.553  1.073   -0.495  1.00 26.46 ? 191 LYS A CG    1 
ATOM   1402 C  CD    . LYS A 1 197 ? -3.771  1.062   0.767   1.00 29.35 ? 191 LYS A CD    1 
ATOM   1403 C  CE    . LYS A 1 197 ? -2.508  0.249   0.673   1.00 27.20 ? 191 LYS A CE    1 
ATOM   1404 N  NZ    . LYS A 1 197 ? -1.310  1.074   0.426   1.00 24.63 ? 191 LYS A NZ    1 
ATOM   1405 N  N     . CYS A 1 198 ? -7.209  4.583   1.139   1.00 18.63 ? 192 CYS A N     1 
ATOM   1406 C  CA    . CYS A 1 198 ? -7.751  5.961   1.048   1.00 17.67 ? 192 CYS A CA    1 
ATOM   1407 C  C     . CYS A 1 198 ? -6.574  6.919   1.180   1.00 18.22 ? 192 CYS A C     1 
ATOM   1408 O  O     . CYS A 1 198 ? -6.076  7.068   2.266   1.00 17.90 ? 192 CYS A O     1 
ATOM   1409 C  CB    . CYS A 1 198 ? -8.854  6.216   2.058   1.00 21.10 ? 192 CYS A CB    1 
ATOM   1410 S  SG    . CYS A 1 198 ? -10.340 5.261   1.656   1.00 23.98 ? 192 CYS A SG    1 
ATOM   1411 N  N     . PHE A 1 199 ? -6.145  7.485   0.052   1.00 19.08 ? 193 PHE A N     1 
ATOM   1412 C  CA    . PHE A 1 199 ? -4.967  8.383   0.009   1.00 18.71 ? 193 PHE A CA    1 
ATOM   1413 C  C     . PHE A 1 199 ? -5.465  9.820   0.130   1.00 19.43 ? 193 PHE A C     1 
ATOM   1414 O  O     . PHE A 1 199 ? -6.234  10.255  -0.723  1.00 20.80 ? 193 PHE A O     1 
ATOM   1415 C  CB    . PHE A 1 199 ? -4.232  8.227   -1.325  1.00 18.11 ? 193 PHE A CB    1 
ATOM   1416 C  CG    . PHE A 1 199 ? -3.883  6.806   -1.709  1.00 17.36 ? 193 PHE A CG    1 
ATOM   1417 C  CD1   . PHE A 1 199 ? -3.015  6.059   -0.945  1.00 17.95 ? 193 PHE A CD1   1 
ATOM   1418 C  CD2   . PHE A 1 199 ? -4.349  6.257   -2.890  1.00 18.95 ? 193 PHE A CD2   1 
ATOM   1419 C  CE1   . PHE A 1 199 ? -2.646  4.776   -1.330  1.00 17.86 ? 193 PHE A CE1   1 
ATOM   1420 C  CE2   . PHE A 1 199 ? -3.971  4.975   -3.284  1.00 19.50 ? 193 PHE A CE2   1 
ATOM   1421 C  CZ    . PHE A 1 199 ? -3.147  4.224   -2.482  1.00 18.27 ? 193 PHE A CZ    1 
ATOM   1422 N  N     . GLN A 1 200 ? -4.923  10.588  1.074   1.00 18.96 ? 194 GLN A N     1 
ATOM   1423 C  CA    . GLN A 1 200 ? -5.038  12.056  0.989   1.00 18.30 ? 194 GLN A CA    1 
ATOM   1424 C  C     . GLN A 1 200 ? -4.288  12.478  -0.268  1.00 18.54 ? 194 GLN A C     1 
ATOM   1425 O  O     . GLN A 1 200 ? -3.122  11.990  -0.512  1.00 18.81 ? 194 GLN A O     1 
ATOM   1426 C  CB    . GLN A 1 200 ? -4.441  12.726  2.232   1.00 17.49 ? 194 GLN A CB    1 
ATOM   1427 C  CG    . GLN A 1 200 ? -4.599  14.235  2.228   1.00 19.53 ? 194 GLN A CG    1 
ATOM   1428 C  CD    . GLN A 1 200 ? -4.044  14.884  3.470   1.00 22.49 ? 194 GLN A CD    1 
ATOM   1429 O  OE1   . GLN A 1 200 ? -3.377  14.248  4.276   1.00 21.63 ? 194 GLN A OE1   1 
ATOM   1430 N  NE2   . GLN A 1 200 ? -4.275  16.187  3.603   1.00 22.75 ? 194 GLN A NE2   1 
ATOM   1431 N  N     . VAL A 1 201 ? -4.866  13.373  -1.064  1.00 18.75 ? 195 VAL A N     1 
ATOM   1432 C  CA    . VAL A 1 201 ? -4.185  13.849  -2.289  1.00 19.86 ? 195 VAL A CA    1 
ATOM   1433 C  C     . VAL A 1 201 ? -2.831  14.472  -1.877  1.00 18.35 ? 195 VAL A C     1 
ATOM   1434 O  O     . VAL A 1 201 ? -2.725  15.219  -0.862  1.00 19.24 ? 195 VAL A O     1 
ATOM   1435 C  CB    . VAL A 1 201 ? -5.096  14.721  -3.167  1.00 23.22 ? 195 VAL A CB    1 
ATOM   1436 C  CG1   . VAL A 1 201 ? -5.470  16.010  -2.504  1.00 27.52 ? 195 VAL A CG1   1 
ATOM   1437 C  CG2   . VAL A 1 201 ? -4.487  14.949  -4.534  1.00 27.80 ? 195 VAL A CG2   1 
ATOM   1438 N  N     . LEU A 1 202 ? -1.788  14.096  -2.597  1.00 18.08 ? 196 LEU A N     1 
ATOM   1439 C  CA    . LEU A 1 202 ? -0.392  14.438  -2.262  1.00 17.97 ? 196 LEU A CA    1 
ATOM   1440 C  C     . LEU A 1 202 ? 0.201   15.266  -3.403  1.00 20.27 ? 196 LEU A C     1 
ATOM   1441 O  O     . LEU A 1 202 ? 0.031   14.888  -4.585  1.00 19.95 ? 196 LEU A O     1 
ATOM   1442 C  CB    . LEU A 1 202 ? 0.389   13.139  -2.053  1.00 19.40 ? 196 LEU A CB    1 
ATOM   1443 C  CG    . LEU A 1 202 ? 1.870   13.296  -1.744  1.00 19.59 ? 196 LEU A CG    1 
ATOM   1444 C  CD1   . LEU A 1 202 ? 2.080   13.917  -0.370  1.00 21.67 ? 196 LEU A CD1   1 
ATOM   1445 C  CD2   . LEU A 1 202 ? 2.570   11.960  -1.818  1.00 20.82 ? 196 LEU A CD2   1 
ATOM   1446 N  N     . ILE A 1 203 ? 0.870   16.361  -3.047  1.00 19.87 ? 197 ILE A N     1 
ATOM   1447 C  CA    . ILE A 1 203 ? 1.636   17.228  -3.979  1.00 21.01 ? 197 ILE A CA    1 
ATOM   1448 C  C     . ILE A 1 203 ? 3.079   16.729  -4.036  1.00 21.50 ? 197 ILE A C     1 
ATOM   1449 O  O     . ILE A 1 203 ? 3.653   16.460  -2.964  1.00 21.67 ? 197 ILE A O     1 
ATOM   1450 C  CB    . ILE A 1 203 ? 1.598   18.683  -3.510  1.00 21.54 ? 197 ILE A CB    1 
ATOM   1451 C  CG1   . ILE A 1 203 ? 0.169   19.204  -3.381  1.00 24.62 ? 197 ILE A CG1   1 
ATOM   1452 C  CG2   . ILE A 1 203 ? 2.479   19.525  -4.404  1.00 22.12 ? 197 ILE A CG2   1 
ATOM   1453 C  CD1   . ILE A 1 203 ? -0.582  19.309  -4.689  1.00 27.89 ? 197 ILE A CD1   1 
ATOM   1454 N  N     . ILE A 1 204 ? 3.586   16.521  -5.249  1.00 20.99 ? 198 ILE A N     1 
ATOM   1455 C  CA    . ILE A 1 204 ? 5.003   16.167  -5.525  1.00 21.13 ? 198 ILE A CA    1 
ATOM   1456 C  C     . ILE A 1 204 ? 5.597   17.213  -6.492  1.00 22.87 ? 198 ILE A C     1 
ATOM   1457 O  O     . ILE A 1 204 ? 5.103   17.387  -7.598  1.00 22.17 ? 198 ILE A O     1 
ATOM   1458 C  CB    . ILE A 1 204 ? 5.131   14.745  -6.065  1.00 21.94 ? 198 ILE A CB    1 
ATOM   1459 C  CG1   . ILE A 1 204 ? 4.496   13.723  -5.115  1.00 22.61 ? 198 ILE A CG1   1 
ATOM   1460 C  CG2   . ILE A 1 204 ? 6.594   14.416  -6.388  1.00 22.37 ? 198 ILE A CG2   1 
ATOM   1461 C  CD1   . ILE A 1 204 ? 4.787   12.301  -5.471  1.00 25.44 ? 198 ILE A CD1   1 
ATOM   1462 N  N     . GLU A 1 205 ? 6.675   17.865  -6.068  1.00 26.09 ? 199 GLU A N     1 
ATOM   1463 C  CA    . GLU A 1 205 ? 7.418   18.864  -6.882  1.00 28.81 ? 199 GLU A CA    1 
ATOM   1464 C  C     . GLU A 1 205 ? 7.900   18.182  -8.165  1.00 29.78 ? 199 GLU A C     1 
ATOM   1465 O  O     . GLU A 1 205 ? 8.409   17.040  -8.084  1.00 31.25 ? 199 GLU A O     1 
ATOM   1466 C  CB    . GLU A 1 205 ? 8.523   19.480  -6.022  1.00 34.86 ? 199 GLU A CB    1 
ATOM   1467 C  CG    . GLU A 1 205 ? 9.318   20.562  -6.736  1.00 40.57 ? 199 GLU A CG    1 
ATOM   1468 C  CD    . GLU A 1 205 ? 10.598  20.990  -6.022  1.00 46.55 ? 199 GLU A CD    1 
ATOM   1469 O  OE1   . GLU A 1 205 ? 10.519  21.468  -4.857  1.00 47.50 ? 199 GLU A OE1   1 
ATOM   1470 O  OE2   . GLU A 1 205 ? 11.676  20.836  -6.631  1.00 50.43 ? 199 GLU A OE2   1 
ATOM   1471 N  N     . GLY A 1 206 ? 7.622   18.805  -9.318  1.00 26.57 ? 200 GLY A N     1 
ATOM   1472 C  CA    . GLY A 1 206 ? 7.950   18.302  -10.667 1.00 26.58 ? 200 GLY A CA    1 
ATOM   1473 C  C     . GLY A 1 206 ? 6.857   17.437  -11.292 1.00 31.09 ? 200 GLY A C     1 
ATOM   1474 O  O     . GLY A 1 206 ? 6.986   17.093  -12.481 1.00 27.63 ? 200 GLY A O     1 
ATOM   1475 N  N     . GLU A 1 207 ? 5.786   17.101  -10.559 1.00 23.80 ? 201 GLU A N     1 
ATOM   1476 C  CA    . GLU A 1 207 ? 4.717   16.234  -11.069 1.00 23.22 ? 201 GLU A CA    1 
ATOM   1477 C  C     . GLU A 1 207 ? 3.434   17.041  -11.145 1.00 22.67 ? 201 GLU A C     1 
ATOM   1478 O  O     . GLU A 1 207 ? 2.892   17.156  -12.245 1.00 22.29 ? 201 GLU A O     1 
ATOM   1479 C  CB    . GLU A 1 207 ? 4.566   15.012  -10.175 1.00 22.24 ? 201 GLU A CB    1 
ATOM   1480 C  CG    . GLU A 1 207 ? 5.793   14.133  -10.186 1.00 23.68 ? 201 GLU A CG    1 
ATOM   1481 C  CD    . GLU A 1 207 ? 5.938   13.281  -11.440 1.00 26.56 ? 201 GLU A CD    1 
ATOM   1482 O  OE1   . GLU A 1 207 ? 5.020   13.282  -12.279 1.00 26.73 ? 201 GLU A OE1   1 
ATOM   1483 O  OE2   . GLU A 1 207 ? 6.983   12.615  -11.565 1.00 30.76 ? 201 GLU A OE2   1 
ATOM   1484 N  N     . ASN A 1 208 ? 2.963   17.565  -10.013 1.00 20.96 ? 202 ASN A N     1 
ATOM   1485 C  CA    . ASN A 1 208 ? 1.594   18.124  -9.962  1.00 19.26 ? 202 ASN A CA    1 
ATOM   1486 C  C     . ASN A 1 208 ? 1.564   19.417  -9.154  1.00 21.04 ? 202 ASN A C     1 
ATOM   1487 O  O     . ASN A 1 208 ? 0.496   19.717  -8.648  1.00 20.89 ? 202 ASN A O     1 
ATOM   1488 C  CB    . ASN A 1 208 ? 0.600   17.085  -9.430  1.00 19.38 ? 202 ASN A CB    1 
ATOM   1489 C  CG    . ASN A 1 208 ? 0.895   16.666  -8.007  1.00 17.81 ? 202 ASN A CG    1 
ATOM   1490 O  OD1   . ASN A 1 208 ? 1.900   17.116  -7.410  1.00 19.25 ? 202 ASN A OD1   1 
ATOM   1491 N  ND2   . ASN A 1 208 ? 0.011   15.819  -7.446  1.00 18.95 ? 202 ASN A ND2   1 
ATOM   1492 N  N     . ASP A 1 209 ? 2.659   20.180  -9.109  1.00 22.10 ? 203 ASP A N     1 
ATOM   1493 C  CA    . ASP A 1 209 ? 2.809   21.282  -8.117  1.00 24.11 ? 203 ASP A CA    1 
ATOM   1494 C  C     . ASP A 1 209 ? 2.829   22.668  -8.767  1.00 23.08 ? 203 ASP A C     1 
ATOM   1495 O  O     . ASP A 1 209 ? 2.878   23.668  -8.009  1.00 24.72 ? 203 ASP A O     1 
ATOM   1496 C  CB    . ASP A 1 209 ? 4.083   21.141  -7.295  1.00 25.11 ? 203 ASP A CB    1 
ATOM   1497 C  CG    . ASP A 1 209 ? 5.341   21.445  -8.104  1.00 32.05 ? 203 ASP A CG    1 
ATOM   1498 O  OD1   . ASP A 1 209 ? 5.402   21.042  -9.298  1.00 30.83 ? 203 ASP A OD1   1 
ATOM   1499 O  OD2   . ASP A 1 209 ? 6.277   22.070  -7.532  1.00 36.33 ? 203 ASP A OD2   1 
ATOM   1500 N  N     . SER A 1 210 ? 2.848   22.760  -10.093 1.00 23.26 ? 204 SER A N     1 
ATOM   1501 C  CA    . SER A 1 210 ? 3.243   24.003  -10.795 1.00 21.93 ? 204 SER A CA    1 
ATOM   1502 C  C     . SER A 1 210 ? 2.286   24.354  -11.928 1.00 23.31 ? 204 SER A C     1 
ATOM   1503 O  O     . SER A 1 210 ? 1.612   23.485  -12.497 1.00 22.69 ? 204 SER A O     1 
ATOM   1504 C  CB    . SER A 1 210 ? 4.676   23.892  -11.269 1.00 24.02 ? 204 SER A CB    1 
ATOM   1505 O  OG    . SER A 1 210 ? 4.989   24.847  -12.278 1.00 27.96 ? 204 SER A OG    1 
ATOM   1506 N  N     . ASP A 1 211 ? 2.278   25.634  -12.296 1.00 21.91 ? 205 ASP A N     1 
ATOM   1507 C  CA    . ASP A 1 211 ? 1.719   26.126  -13.582 1.00 24.71 ? 205 ASP A CA    1 
ATOM   1508 C  C     . ASP A 1 211 ? 2.367   25.376  -14.764 1.00 24.33 ? 205 ASP A C     1 
ATOM   1509 O  O     . ASP A 1 211 ? 1.752   25.304  -15.850 1.00 25.19 ? 205 ASP A O     1 
ATOM   1510 C  CB    . ASP A 1 211 ? 1.983   27.640  -13.694 1.00 24.39 ? 205 ASP A CB    1 
ATOM   1511 C  CG    . ASP A 1 211 ? 1.530   28.256  -15.005 1.00 27.38 ? 205 ASP A CG    1 
ATOM   1512 O  OD1   . ASP A 1 211 ? 0.291   28.264  -15.253 1.00 29.97 ? 205 ASP A OD1   1 
ATOM   1513 O  OD2   . ASP A 1 211 ? 2.432   28.633  -15.814 1.00 29.88 ? 205 ASP A OD2   1 
ATOM   1514 N  N     . LYS A 1 212 ? 3.595   24.893  -14.593 1.00 23.07 ? 206 LYS A N     1 
ATOM   1515 C  CA    . LYS A 1 212 ? 4.447   24.424  -15.717 1.00 26.70 ? 206 LYS A CA    1 
ATOM   1516 C  C     . LYS A 1 212 ? 4.446   22.901  -15.838 1.00 26.69 ? 206 LYS A C     1 
ATOM   1517 O  O     . LYS A 1 212 ? 4.969   22.414  -16.864 1.00 25.35 ? 206 LYS A O     1 
ATOM   1518 C  CB    . LYS A 1 212 ? 5.896   24.882  -15.510 1.00 29.91 ? 206 LYS A CB    1 
ATOM   1519 C  CG    . LYS A 1 212 ? 6.326   26.110  -16.286 1.00 36.23 ? 206 LYS A CG    1 
ATOM   1520 C  CD    . LYS A 1 212 ? 5.283   27.160  -16.446 1.00 32.13 ? 206 LYS A CD    1 
ATOM   1521 C  CE    . LYS A 1 212 ? 5.869   28.546  -16.341 1.00 31.53 ? 206 LYS A CE    1 
ATOM   1522 N  NZ    . LYS A 1 212 ? 5.117   29.366  -15.353 1.00 30.04 ? 206 LYS A NZ    1 
ATOM   1523 N  N     . THR A 1 213 ? 3.911   22.174  -14.856 1.00 24.67 ? 207 THR A N     1 
ATOM   1524 C  CA    . THR A 1 213 ? 3.971   20.683  -14.854 1.00 24.00 ? 207 THR A CA    1 
ATOM   1525 C  C     . THR A 1 213 ? 2.793   20.181  -15.677 1.00 22.36 ? 207 THR A C     1 
ATOM   1526 O  O     . THR A 1 213 ? 1.925   20.992  -16.029 1.00 23.18 ? 207 THR A O     1 
ATOM   1527 C  CB    . THR A 1 213 ? 4.043   20.142  -13.415 1.00 22.53 ? 207 THR A CB    1 
ATOM   1528 O  OG1   . THR A 1 213 ? 3.144   20.862  -12.574 1.00 23.63 ? 207 THR A OG1   1 
ATOM   1529 C  CG2   . THR A 1 213 ? 5.416   20.343  -12.821 1.00 26.61 ? 207 THR A CG2   1 
ATOM   1530 N  N     . LEU A 1 214 ? 2.699   18.874  -15.890 1.00 21.66 ? 208 LEU A N     1 
ATOM   1531 C  CA    . LEU A 1 214 ? 1.585   18.261  -16.659 1.00 22.68 ? 208 LEU A CA    1 
ATOM   1532 C  C     . LEU A 1 214 ? 0.290   18.353  -15.857 1.00 22.70 ? 208 LEU A C     1 
ATOM   1533 O  O     . LEU A 1 214 ? -0.807  18.252  -16.478 1.00 21.54 ? 208 LEU A O     1 
ATOM   1534 C  CB    . LEU A 1 214 ? 1.936   16.809  -16.988 1.00 23.26 ? 208 LEU A CB    1 
ATOM   1535 C  CG    . LEU A 1 214 ? 3.090   16.698  -17.983 1.00 25.69 ? 208 LEU A CG    1 
ATOM   1536 C  CD1   . LEU A 1 214 ? 3.471   15.243  -18.266 1.00 26.38 ? 208 LEU A CD1   1 
ATOM   1537 C  CD2   . LEU A 1 214 ? 2.743   17.462  -19.253 1.00 26.73 ? 208 LEU A CD2   1 
ATOM   1538 N  N     . ARG A 1 215 ? 0.402   18.451  -14.525 1.00 19.66 ? 209 ARG A N     1 
ATOM   1539 C  CA    . ARG A 1 215 ? -0.791  18.627  -13.674 1.00 21.59 ? 209 ARG A CA    1 
ATOM   1540 C  C     . ARG A 1 215 ? -0.491  19.709  -12.662 1.00 20.12 ? 209 ARG A C     1 
ATOM   1541 O  O     . ARG A 1 215 ? 0.682   19.956  -12.363 1.00 21.00 ? 209 ARG A O     1 
ATOM   1542 C  CB    . ARG A 1 215 ? -1.121  17.337  -12.916 1.00 22.15 ? 209 ARG A CB    1 
ATOM   1543 C  CG    . ARG A 1 215 ? -1.334  16.155  -13.837 1.00 24.61 ? 209 ARG A CG    1 
ATOM   1544 C  CD    . ARG A 1 215 ? -2.620  16.385  -14.601 1.00 27.82 ? 209 ARG A CD    1 
ATOM   1545 N  NE    . ARG A 1 215 ? -3.059  15.076  -14.984 1.00 36.82 ? 209 ARG A NE    1 
ATOM   1546 C  CZ    . ARG A 1 215 ? -2.811  14.483  -16.128 1.00 31.87 ? 209 ARG A CZ    1 
ATOM   1547 N  NH1   . ARG A 1 215 ? -2.179  15.109  -17.088 1.00 38.91 ? 209 ARG A NH1   1 
ATOM   1548 N  NH2   . ARG A 1 215 ? -3.189  13.238  -16.298 1.00 36.11 ? 209 ARG A NH2   1 
ATOM   1549 N  N     . ASN A 1 216 ? -1.553  20.233  -12.079 1.00 21.41 ? 210 ASN A N     1 
ATOM   1550 C  CA    . ASN A 1 216 ? -1.492  21.169  -10.941 1.00 21.41 ? 210 ASN A CA    1 
ATOM   1551 C  C     . ASN A 1 216 ? -2.630  20.761  -9.996  1.00 21.73 ? 210 ASN A C     1 
ATOM   1552 O  O     . ASN A 1 216 ? -3.830  20.991  -10.327 1.00 21.83 ? 210 ASN A O     1 
ATOM   1553 C  CB    . ASN A 1 216 ? -1.580  22.626  -11.401 1.00 23.34 ? 210 ASN A CB    1 
ATOM   1554 C  CG    . ASN A 1 216 ? -1.452  23.582  -10.239 1.00 23.63 ? 210 ASN A CG    1 
ATOM   1555 O  OD1   . ASN A 1 216 ? -1.562  23.183  -9.081  1.00 22.55 ? 210 ASN A OD1   1 
ATOM   1556 N  ND2   . ASN A 1 216 ? -1.194  24.838  -10.539 1.00 24.33 ? 210 ASN A ND2   1 
ATOM   1557 N  N     . ALA A 1 217 ? -2.279  20.091  -8.897  1.00 21.10 ? 211 ALA A N     1 
ATOM   1558 C  CA    . ALA A 1 217 ? -3.270  19.479  -7.992  1.00 21.53 ? 211 ALA A CA    1 
ATOM   1559 C  C     . ALA A 1 217 ? -3.635  20.460  -6.879  1.00 21.79 ? 211 ALA A C     1 
ATOM   1560 O  O     . ALA A 1 217 ? -4.383  20.050  -5.969  1.00 21.31 ? 211 ALA A O     1 
ATOM   1561 C  CB    . ALA A 1 217 ? -2.702  18.220  -7.385  1.00 20.90 ? 211 ALA A CB    1 
ATOM   1562 N  N     . HIS A 1 218 ? -3.033  21.653  -6.835  1.00 23.09 ? 212 HIS A N     1 
ATOM   1563 C  CA    . HIS A 1 218 ? -3.171  22.544  -5.645  1.00 22.34 ? 212 HIS A CA    1 
ATOM   1564 C  C     . HIS A 1 218 ? -4.630  22.870  -5.336  1.00 25.06 ? 212 HIS A C     1 
ATOM   1565 O  O     . HIS A 1 218 ? -4.959  22.960  -4.143  1.00 26.80 ? 212 HIS A O     1 
ATOM   1566 C  CB    . HIS A 1 218 ? -2.349  23.799  -5.811  1.00 21.93 ? 212 HIS A CB    1 
ATOM   1567 C  CG    . HIS A 1 218 ? -0.912  23.601  -5.485  1.00 25.13 ? 212 HIS A CG    1 
ATOM   1568 N  ND1   . HIS A 1 218 ? -0.468  23.506  -4.186  1.00 27.42 ? 212 HIS A ND1   1 
ATOM   1569 C  CD2   . HIS A 1 218 ? 0.167   23.465  -6.283  1.00 24.44 ? 212 HIS A CD2   1 
ATOM   1570 C  CE1   . HIS A 1 218 ? 0.845   23.344  -4.198  1.00 30.92 ? 212 HIS A CE1   1 
ATOM   1571 N  NE2   . HIS A 1 218 ? 1.257   23.337  -5.479  1.00 29.17 ? 212 HIS A NE2   1 
ATOM   1572 N  N     . SER A 1 219 ? -5.504  22.965  -6.332  1.00 22.89 ? 213 SER A N     1 
ATOM   1573 C  CA    . SER A 1 219 ? -6.943  23.283  -6.113  1.00 25.35 ? 213 SER A CA    1 
ATOM   1574 C  C     . SER A 1 219 ? -7.691  22.087  -5.526  1.00 27.13 ? 213 SER A C     1 
ATOM   1575 O  O     . SER A 1 219 ? -8.828  22.275  -5.037  1.00 27.69 ? 213 SER A O     1 
ATOM   1576 C  CB    . SER A 1 219 ? -7.626  23.770  -7.372  1.00 25.33 ? 213 SER A CB    1 
ATOM   1577 O  OG    . SER A 1 219 ? -7.740  22.741  -8.332  1.00 26.17 ? 213 SER A OG    1 
ATOM   1578 N  N     . LEU A 1 220 ? -7.103  20.891  -5.548  1.00 24.07 ? 214 LEU A N     1 
ATOM   1579 C  CA    . LEU A 1 220 ? -7.814  19.649  -5.174  1.00 24.04 ? 214 LEU A CA    1 
ATOM   1580 C  C     . LEU A 1 220 ? -7.390  19.180  -3.773  1.00 22.02 ? 214 LEU A C     1 
ATOM   1581 O  O     . LEU A 1 220 ? -7.957  18.200  -3.318  1.00 22.26 ? 214 LEU A O     1 
ATOM   1582 C  CB    . LEU A 1 220 ? -7.479  18.591  -6.227  1.00 26.23 ? 214 LEU A CB    1 
ATOM   1583 C  CG    . LEU A 1 220 ? -8.000  18.872  -7.634  1.00 31.29 ? 214 LEU A CG    1 
ATOM   1584 C  CD1   . LEU A 1 220 ? -8.105  17.575  -8.401  1.00 34.60 ? 214 LEU A CD1   1 
ATOM   1585 C  CD2   . LEU A 1 220 ? -9.363  19.535  -7.614  1.00 34.49 ? 214 LEU A CD2   1 
ATOM   1586 N  N     . THR A 1 221 ? -6.442  19.844  -3.126  1.00 21.40 ? 215 THR A N     1 
ATOM   1587 C  CA    . THR A 1 221 ? -5.935  19.438  -1.788  1.00 22.52 ? 215 THR A CA    1 
ATOM   1588 C  C     . THR A 1 221 ? -7.016  19.671  -0.718  1.00 24.36 ? 215 THR A C     1 
ATOM   1589 O  O     . THR A 1 221 ? -7.907  20.547  -0.887  1.00 22.91 ? 215 THR A O     1 
ATOM   1590 C  CB    . THR A 1 221 ? -4.603  20.106  -1.440  1.00 22.95 ? 215 THR A CB    1 
ATOM   1591 O  OG1   . THR A 1 221 ? -4.808  21.517  -1.473  1.00 27.49 ? 215 THR A OG1   1 
ATOM   1592 C  CG2   . THR A 1 221 ? -3.487  19.664  -2.357  1.00 24.96 ? 215 THR A CG2   1 
ATOM   1593 N  N     . ILE A 1 222 ? -6.957  18.854  0.324   1.00 22.67 ? 216 ILE A N     1 
ATOM   1594 C  CA    . ILE A 1 222 ? -7.860  18.943  1.498   1.00 24.11 ? 216 ILE A CA    1 
ATOM   1595 C  C     . ILE A 1 222 ? -7.008  19.033  2.756   1.00 23.79 ? 216 ILE A C     1 
ATOM   1596 O  O     . ILE A 1 222 ? -5.806  18.667  2.759   1.00 24.00 ? 216 ILE A O     1 
ATOM   1597 C  CB    . ILE A 1 222 ? -8.809  17.742  1.518   1.00 22.59 ? 216 ILE A CB    1 
ATOM   1598 C  CG1   . ILE A 1 222 ? -8.033  16.427  1.681   1.00 22.82 ? 216 ILE A CG1   1 
ATOM   1599 C  CG2   . ILE A 1 222 ? -9.691  17.758  0.285   1.00 24.34 ? 216 ILE A CG2   1 
ATOM   1600 C  CD1   . ILE A 1 222 ? -8.880  15.215  1.885   1.00 22.24 ? 216 ILE A CD1   1 
ATOM   1601 N  N     . SER A 1 223 ? -7.638  19.508  3.821   1.00 23.34 ? 217 SER A N     1 
ATOM   1602 C  CA    . SER A 1 223 ? -6.993  19.638  5.138   1.00 24.01 ? 217 SER A CA    1 
ATOM   1603 C  C     . SER A 1 223 ? -6.917  18.258  5.793   1.00 22.32 ? 217 SER A C     1 
ATOM   1604 O  O     . SER A 1 223 ? -7.655  17.334  5.409   1.00 21.19 ? 217 SER A O     1 
ATOM   1605 C  CB    . SER A 1 223 ? -7.733  20.653  5.994   1.00 25.00 ? 217 SER A CB    1 
ATOM   1606 O  OG    . SER A 1 223 ? -9.044  20.193  6.301   1.00 25.92 ? 217 SER A OG    1 
ATOM   1607 N  N     . ASP A 1 224 ? -6.037  18.134  6.776   1.00 25.63 ? 218 ASP A N     1 
ATOM   1608 C  CA    . ASP A 1 224 ? -5.917  16.950  7.651   1.00 26.75 ? 218 ASP A CA    1 
ATOM   1609 C  C     . ASP A 1 224 ? -7.286  16.634  8.290   1.00 24.59 ? 218 ASP A C     1 
ATOM   1610 O  O     . ASP A 1 224 ? -7.638  15.471  8.288   1.00 23.05 ? 218 ASP A O     1 
ATOM   1611 C  CB    . ASP A 1 224 ? -4.778  17.186  8.647   1.00 32.53 ? 218 ASP A CB    1 
ATOM   1612 C  CG    . ASP A 1 224 ? -3.409  17.365  7.983   1.00 35.34 ? 218 ASP A CG    1 
ATOM   1613 O  OD1   . ASP A 1 224 ? -3.323  17.239  6.741   1.00 46.13 ? 218 ASP A OD1   1 
ATOM   1614 O  OD2   . ASP A 1 224 ? -2.420  17.625  8.715   1.00 45.24 ? 218 ASP A OD2   1 
ATOM   1615 N  N     . ASP A 1 225 ? -8.066  17.633  8.730   1.00 23.04 ? 219 ASP A N     1 
ATOM   1616 C  CA    . ASP A 1 225 ? -9.389  17.455  9.388   1.00 27.28 ? 219 ASP A CA    1 
ATOM   1617 C  C     . ASP A 1 225 ? -10.432 16.942  8.371   1.00 22.03 ? 219 ASP A C     1 
ATOM   1618 O  O     . ASP A 1 225 ? -11.179 16.030  8.714   1.00 24.65 ? 219 ASP A O     1 
ATOM   1619 C  CB    . ASP A 1 225 ? -9.811  18.747  10.087  1.00 29.33 ? 219 ASP A CB    1 
ATOM   1620 C  CG    . ASP A 1 225 ? -8.980  19.105  11.331  1.00 37.02 ? 219 ASP A CG    1 
ATOM   1621 O  OD1   . ASP A 1 225 ? -7.970  18.381  11.655  1.00 35.24 ? 219 ASP A OD1   1 
ATOM   1622 O  OD2   . ASP A 1 225 ? -9.322  20.135  11.967  1.00 37.40 ? 219 ASP A OD2   1 
ATOM   1623 N  N     . GLU A 1 226 ? -10.424 17.432  7.140   1.00 23.15 ? 220 GLU A N     1 
ATOM   1624 C  CA    . GLU A 1 226 ? -11.330 16.969  6.050   1.00 23.79 ? 220 GLU A CA    1 
ATOM   1625 C  C     . GLU A 1 226 ? -11.039 15.499  5.744   1.00 21.40 ? 220 GLU A C     1 
ATOM   1626 O  O     . GLU A 1 226 ? -11.970 14.718  5.607   1.00 21.63 ? 220 GLU A O     1 
ATOM   1627 C  CB    . GLU A 1 226 ? -11.132 17.827  4.802   1.00 26.43 ? 220 GLU A CB    1 
ATOM   1628 C  CG    . GLU A 1 226 ? -11.728 19.219  4.923   1.00 28.15 ? 220 GLU A CG    1 
ATOM   1629 C  CD    . GLU A 1 226 ? -11.384 20.245  3.846   1.00 35.98 ? 220 GLU A CD    1 
ATOM   1630 O  OE1   . GLU A 1 226 ? -10.309 20.166  3.185   1.00 31.58 ? 220 GLU A OE1   1 
ATOM   1631 O  OE2   . GLU A 1 226 ? -12.194 21.163  3.691   1.00 35.36 ? 220 GLU A OE2   1 
ATOM   1632 N  N     . PHE A 1 227 ? -9.766  15.128  5.678   1.00 21.89 ? 221 PHE A N     1 
ATOM   1633 C  CA    . PHE A 1 227 ? -9.341  13.729  5.458   1.00 21.94 ? 221 PHE A CA    1 
ATOM   1634 C  C     . PHE A 1 227 ? -9.792  12.857  6.638   1.00 21.39 ? 221 PHE A C     1 
ATOM   1635 O  O     . PHE A 1 227 ? -10.364 11.798  6.402   1.00 21.23 ? 221 PHE A O     1 
ATOM   1636 C  CB    . PHE A 1 227 ? -7.828  13.637  5.238   1.00 22.19 ? 221 PHE A CB    1 
ATOM   1637 C  CG    . PHE A 1 227 ? -7.412  12.220  4.976   1.00 19.83 ? 221 PHE A CG    1 
ATOM   1638 C  CD1   . PHE A 1 227 ? -7.703  11.642  3.753   1.00 20.80 ? 221 PHE A CD1   1 
ATOM   1639 C  CD2   . PHE A 1 227 ? -6.786  11.458  5.957   1.00 21.51 ? 221 PHE A CD2   1 
ATOM   1640 C  CE1   . PHE A 1 227 ? -7.364  10.323  3.497   1.00 20.64 ? 221 PHE A CE1   1 
ATOM   1641 C  CE2   . PHE A 1 227 ? -6.461  10.128  5.707   1.00 20.89 ? 221 PHE A CE2   1 
ATOM   1642 C  CZ    . PHE A 1 227 ? -6.751  9.568   4.474   1.00 20.59 ? 221 PHE A CZ    1 
ATOM   1643 N  N     . ASP A 1 228 ? -9.573  13.305  7.880   1.00 23.65 ? 222 ASP A N     1 
ATOM   1644 C  CA    . ASP A 1 228 ? -10.027 12.563  9.092   1.00 27.04 ? 222 ASP A CA    1 
ATOM   1645 C  C     . ASP A 1 228 ? -11.557 12.397  9.057   1.00 23.97 ? 222 ASP A C     1 
ATOM   1646 O  O     . ASP A 1 228 ? -12.022 11.299  9.394   1.00 24.24 ? 222 ASP A O     1 
ATOM   1647 C  CB    . ASP A 1 228 ? -9.567  13.229  10.391  1.00 33.74 ? 222 ASP A CB    1 
ATOM   1648 C  CG    . ASP A 1 228 ? -10.060 12.491  11.632  1.00 43.60 ? 222 ASP A CG    1 
ATOM   1649 O  OD1   . ASP A 1 228 ? -9.913  11.256  11.681  1.00 52.78 ? 222 ASP A OD1   1 
ATOM   1650 O  OD2   . ASP A 1 228 ? -10.641 13.153  12.518  1.00 57.95 ? 222 ASP A OD2   1 
ATOM   1651 N  N     . ARG A 1 229 ? -12.313 13.410  8.602   1.00 23.28 ? 223 ARG A N     1 
ATOM   1652 C  CA    . ARG A 1 229 ? -13.806 13.322  8.550   1.00 23.16 ? 223 ARG A CA    1 
ATOM   1653 C  C     . ARG A 1 229 ? -14.241 12.313  7.496   1.00 21.55 ? 223 ARG A C     1 
ATOM   1654 O  O     . ARG A 1 229 ? -15.175 11.524  7.764   1.00 22.86 ? 223 ARG A O     1 
ATOM   1655 C  CB    . ARG A 1 229 ? -14.448 14.708  8.408   1.00 24.32 ? 223 ARG A CB    1 
ATOM   1656 C  CG    . ARG A 1 229 ? -14.339 15.531  9.685   1.00 26.65 ? 223 ARG A CG    1 
ATOM   1657 C  CD    . ARG A 1 229 ? -15.280 16.710  9.705   1.00 26.30 ? 223 ARG A CD    1 
ATOM   1658 N  NE    . ARG A 1 229 ? -14.884 17.731  8.755   1.00 27.17 ? 223 ARG A NE    1 
ATOM   1659 C  CZ    . ARG A 1 229 ? -14.069 18.748  9.005   1.00 27.43 ? 223 ARG A CZ    1 
ATOM   1660 N  NH1   . ARG A 1 229 ? -13.493 18.877  10.188  1.00 30.57 ? 223 ARG A NH1   1 
ATOM   1661 N  NH2   . ARG A 1 229 ? -13.793 19.613  8.052   1.00 30.63 ? 223 ARG A NH2   1 
ATOM   1662 N  N     . PHE A 1 230 ? -13.530 12.225  6.370   1.00 21.70 ? 224 PHE A N     1 
ATOM   1663 C  CA    . PHE A 1 230 ? -13.765 11.160  5.377   1.00 21.56 ? 224 PHE A CA    1 
ATOM   1664 C  C     . PHE A 1 230 ? -13.599 9.789   6.029   1.00 20.10 ? 224 PHE A C     1 
ATOM   1665 O  O     . PHE A 1 230 ? -14.445 8.907   5.844   1.00 21.57 ? 224 PHE A O     1 
ATOM   1666 C  CB    . PHE A 1 230 ? -12.859 11.332  4.149   1.00 21.69 ? 224 PHE A CB    1 
ATOM   1667 C  CG    . PHE A 1 230 ? -13.059 10.249  3.130   1.00 20.24 ? 224 PHE A CG    1 
ATOM   1668 C  CD1   . PHE A 1 230 ? -12.434 9.021   3.271   1.00 21.81 ? 224 PHE A CD1   1 
ATOM   1669 C  CD2   . PHE A 1 230 ? -13.896 10.452  2.046   1.00 21.71 ? 224 PHE A CD2   1 
ATOM   1670 C  CE1   . PHE A 1 230 ? -12.671 8.009   2.365   1.00 20.53 ? 224 PHE A CE1   1 
ATOM   1671 C  CE2   . PHE A 1 230 ? -14.115 9.438   1.125   1.00 23.98 ? 224 PHE A CE2   1 
ATOM   1672 C  CZ    . PHE A 1 230 ? -13.508 8.220   1.297   1.00 22.60 ? 224 PHE A CZ    1 
ATOM   1673 N  N     . CYS A 1 231 ? -12.496 9.545   6.725   1.00 20.49 ? 225 CYS A N     1 
ATOM   1674 C  CA    . CYS A 1 231 ? -12.258 8.236   7.381   1.00 21.92 ? 225 CYS A CA    1 
ATOM   1675 C  C     . CYS A 1 231 ? -13.354 7.962   8.447   1.00 21.60 ? 225 CYS A C     1 
ATOM   1676 O  O     . CYS A 1 231 ? -13.798 6.846   8.510   1.00 22.48 ? 225 CYS A O     1 
ATOM   1677 C  CB    . CYS A 1 231 ? -10.845 8.123   7.954   1.00 23.87 ? 225 CYS A CB    1 
ATOM   1678 S  SG    . CYS A 1 231 ? -9.555  8.386   6.698   1.00 27.89 ? 225 CYS A SG    1 
ATOM   1679 N  N     . GLU A 1 232 ? -13.718 8.929   9.281   1.00 23.90 ? 226 GLU A N     1 
ATOM   1680 C  CA    . GLU A 1 232 ? -14.756 8.786   10.326  1.00 26.08 ? 226 GLU A CA    1 
ATOM   1681 C  C     . GLU A 1 232 ? -16.074 8.436   9.633   1.00 24.25 ? 226 GLU A C     1 
ATOM   1682 O  O     . GLU A 1 232 ? -16.822 7.600   10.129  1.00 23.09 ? 226 GLU A O     1 
ATOM   1683 C  CB    . GLU A 1 232 ? -14.968 10.081  11.124  1.00 31.73 ? 226 GLU A CB    1 
ATOM   1684 C  CG    . GLU A 1 232 ? -13.881 10.373  12.141  1.00 39.62 ? 226 GLU A CG    1 
ATOM   1685 C  CD    . GLU A 1 232 ? -13.905 9.494   13.395  1.00 42.68 ? 226 GLU A CD    1 
ATOM   1686 O  OE1   . GLU A 1 232 ? -14.925 8.819   13.641  1.00 45.71 ? 226 GLU A OE1   1 
ATOM   1687 O  OE2   . GLU A 1 232 ? -12.894 9.473   14.113  1.00 58.37 ? 226 GLU A OE2   1 
ATOM   1688 N  N     . ARG A 1 233 ? -16.334 8.998   8.463   1.00 24.17 ? 227 ARG A N     1 
ATOM   1689 C  CA    . ARG A 1 233 ? -17.620 8.737   7.762   1.00 22.01 ? 227 ARG A CA    1 
ATOM   1690 C  C     . ARG A 1 233 ? -17.671 7.261   7.386   1.00 21.10 ? 227 ARG A C     1 
ATOM   1691 O  O     . ARG A 1 233 ? -18.766 6.730   7.181   1.00 25.05 ? 227 ARG A O     1 
ATOM   1692 C  CB    . ARG A 1 233 ? -17.762 9.668   6.549   1.00 22.83 ? 227 ARG A CB    1 
ATOM   1693 C  CG    . ARG A 1 233 ? -19.178 9.781   5.991   1.00 23.47 ? 227 ARG A CG    1 
ATOM   1694 C  CD    . ARG A 1 233 ? -19.273 10.770  4.834   1.00 23.05 ? 227 ARG A CD    1 
ATOM   1695 N  NE    . ARG A 1 233 ? -18.581 12.004  5.139   1.00 22.82 ? 227 ARG A NE    1 
ATOM   1696 C  CZ    . ARG A 1 233 ? -17.461 12.424  4.555   1.00 23.03 ? 227 ARG A CZ    1 
ATOM   1697 N  NH1   . ARG A 1 233 ? -16.955 11.765  3.521   1.00 24.35 ? 227 ARG A NH1   1 
ATOM   1698 N  NH2   . ARG A 1 233 ? -16.894 13.556  4.943   1.00 22.49 ? 227 ARG A NH2   1 
ATOM   1699 N  N     . HIS A 1 234 ? -16.520 6.611   7.284   1.00 19.72 ? 228 HIS A N     1 
ATOM   1700 C  CA    . HIS A 1 234 ? -16.394 5.215   6.819   1.00 20.52 ? 228 HIS A CA    1 
ATOM   1701 C  C     . HIS A 1 234 ? -15.816 4.315   7.924   1.00 23.79 ? 228 HIS A C     1 
ATOM   1702 O  O     . HIS A 1 234 ? -15.198 3.274   7.603   1.00 21.21 ? 228 HIS A O     1 
ATOM   1703 C  CB    . HIS A 1 234 ? -15.570 5.201   5.508   1.00 19.74 ? 228 HIS A CB    1 
ATOM   1704 C  CG    . HIS A 1 234 ? -16.195 5.940   4.389   1.00 17.79 ? 228 HIS A CG    1 
ATOM   1705 N  ND1   . HIS A 1 234 ? -15.946 7.268   4.156   1.00 18.58 ? 228 HIS A ND1   1 
ATOM   1706 C  CD2   . HIS A 1 234 ? -17.176 5.566   3.524   1.00 18.55 ? 228 HIS A CD2   1 
ATOM   1707 C  CE1   . HIS A 1 234 ? -16.688 7.672   3.127   1.00 19.30 ? 228 HIS A CE1   1 
ATOM   1708 N  NE2   . HIS A 1 234 ? -17.451 6.638   2.728   1.00 19.45 ? 228 HIS A NE2   1 
ATOM   1709 N  N     . SER A 1 235 ? -16.051 4.650   9.191   1.00 25.86 ? 229 SER A N     1 
ATOM   1710 C  CA    . SER A 1 235 ? -15.530 3.903   10.378  1.00 26.85 ? 229 SER A CA    1 
ATOM   1711 C  C     . SER A 1 235 ? -16.014 2.442   10.418  1.00 26.57 ? 229 SER A C     1 
ATOM   1712 O  O     . SER A 1 235 ? -15.293 1.612   10.975  1.00 29.43 ? 229 SER A O     1 
ATOM   1713 C  CB    . SER A 1 235 ? -15.881 4.633   11.649  1.00 28.96 ? 229 SER A CB    1 
ATOM   1714 O  OG    . SER A 1 235 ? -17.288 4.821   11.749  1.00 27.84 ? 229 SER A OG    1 
ATOM   1715 N  N     . SER A 1 236 ? -17.137 2.087   9.795   1.00 26.93 ? 230 SER A N     1 
ATOM   1716 C  CA    . SER A 1 236 ? -17.631 0.690   9.747   1.00 28.53 ? 230 SER A CA    1 
ATOM   1717 C  C     . SER A 1 236 ? -16.841 -0.152  8.734   1.00 28.94 ? 230 SER A C     1 
ATOM   1718 O  O     . SER A 1 236 ? -16.952 -1.382  8.780   1.00 27.30 ? 230 SER A O     1 
ATOM   1719 C  CB    . SER A 1 236 ? -19.133 0.649   9.519   1.00 31.26 ? 230 SER A CB    1 
ATOM   1720 O  OG    . SER A 1 236 ? -19.463 1.046   8.190   1.00 36.30 ? 230 SER A OG    1 
ATOM   1721 N  N     . GLN A 1 237 ? -16.014 0.443   7.874   1.00 24.72 ? 231 GLN A N     1 
ATOM   1722 C  CA    . GLN A 1 237 ? -15.272 -0.351  6.850   1.00 23.82 ? 231 GLN A CA    1 
ATOM   1723 C  C     . GLN A 1 237 ? -13.935 -0.795  7.438   1.00 25.62 ? 231 GLN A C     1 
ATOM   1724 O  O     . GLN A 1 237 ? -13.003 0.052   7.523   1.00 26.14 ? 231 GLN A O     1 
ATOM   1725 C  CB    . GLN A 1 237 ? -15.042 0.445   5.563   1.00 25.41 ? 231 GLN A CB    1 
ATOM   1726 C  CG    . GLN A 1 237 ? -16.326 1.004   4.962   1.00 26.75 ? 231 GLN A CG    1 
ATOM   1727 C  CD    . GLN A 1 237 ? -17.269 -0.084  4.517   1.00 27.76 ? 231 GLN A CD    1 
ATOM   1728 O  OE1   . GLN A 1 237 ? -16.862 -1.202  4.208   1.00 29.22 ? 231 GLN A OE1   1 
ATOM   1729 N  NE2   . GLN A 1 237 ? -18.548 0.243   4.486   1.00 23.24 ? 231 GLN A NE2   1 
ATOM   1730 N  N     . THR A 1 238 ? -13.868 -2.060  7.853   1.00 25.54 ? 232 THR A N     1 
ATOM   1731 C  CA    . THR A 1 238 ? -12.671 -2.667  8.488   1.00 28.12 ? 232 THR A CA    1 
ATOM   1732 C  C     . THR A 1 238 ? -11.562 -2.790  7.425   1.00 30.39 ? 232 THR A C     1 
ATOM   1733 O  O     . THR A 1 238 ? -10.374 -2.799  7.813   1.00 28.50 ? 232 THR A O     1 
ATOM   1734 C  CB    . THR A 1 238 ? -13.024 -3.989  9.196   1.00 33.69 ? 232 THR A CB    1 
ATOM   1735 O  OG1   . THR A 1 238 ? -13.322 -4.996  8.234   1.00 42.49 ? 232 THR A OG1   1 
ATOM   1736 C  CG2   . THR A 1 238 ? -14.214 -3.876  10.126  1.00 35.37 ? 232 THR A CG2   1 
ATOM   1737 N  N     . CYS A 1 239 ? -11.893 -2.794  6.127   1.00 24.46 ? 233 CYS A N     1 
ATOM   1738 C  CA    . CYS A 1 239 ? -10.880 -2.835  5.036   1.00 25.91 ? 233 CYS A CA    1 
ATOM   1739 C  C     . CYS A 1 239 ? -10.154 -1.483  4.810   1.00 22.13 ? 233 CYS A C     1 
ATOM   1740 O  O     . CYS A 1 239 ? -9.139  -1.469  4.070   1.00 20.76 ? 233 CYS A O     1 
ATOM   1741 C  CB    . CYS A 1 239 ? -11.511 -3.277  3.720   1.00 27.45 ? 233 CYS A CB    1 
ATOM   1742 S  SG    . CYS A 1 239 ? -12.833 -2.175  3.162   1.00 30.47 ? 233 CYS A SG    1 
ATOM   1743 N  N     A LEU A 1 240 ? -10.622 -0.398  5.427   0.32 22.09 ? 234 LEU A N     1 
ATOM   1744 N  N     B LEU A 1 240 ? -10.586 -0.393  5.448   0.68 22.53 ? 234 LEU A N     1 
ATOM   1745 C  CA    A LEU A 1 240 ? -10.071 0.966   5.224   0.32 21.63 ? 234 LEU A CA    1 
ATOM   1746 C  CA    B LEU A 1 240 ? -10.066 0.961   5.138   0.68 22.40 ? 234 LEU A CA    1 
ATOM   1747 C  C     A LEU A 1 240 ? -8.597  0.991   5.661   0.32 20.92 ? 234 LEU A C     1 
ATOM   1748 C  C     B LEU A 1 240 ? -8.626  1.075   5.663   0.68 21.12 ? 234 LEU A C     1 
ATOM   1749 O  O     A LEU A 1 240 ? -8.317  0.572   6.793   0.32 20.57 ? 234 LEU A O     1 
ATOM   1750 O  O     B LEU A 1 240 ? -8.422  0.891   6.867   0.68 20.44 ? 234 LEU A O     1 
ATOM   1751 C  CB    A LEU A 1 240 ? -10.926 1.956   6.023   0.32 21.62 ? 234 LEU A CB    1 
ATOM   1752 C  CB    B LEU A 1 240 ? -10.964 2.054   5.732   0.68 23.01 ? 234 LEU A CB    1 
ATOM   1753 C  CG    A LEU A 1 240 ? -10.531 3.424   5.896   0.32 21.54 ? 234 LEU A CG    1 
ATOM   1754 C  CG    B LEU A 1 240 ? -10.805 3.431   5.085   0.68 23.86 ? 234 LEU A CG    1 
ATOM   1755 C  CD1   A LEU A 1 240 ? -10.255 3.796   4.452   0.32 21.76 ? 234 LEU A CD1   1 
ATOM   1756 C  CD1   B LEU A 1 240 ? -11.991 4.325   5.373   0.68 24.21 ? 234 LEU A CD1   1 
ATOM   1757 C  CD2   A LEU A 1 240 ? -11.604 4.323   6.476   0.32 21.14 ? 234 LEU A CD2   1 
ATOM   1758 C  CD2   B LEU A 1 240 ? -9.527  4.123   5.533   0.68 23.38 ? 234 LEU A CD2   1 
ATOM   1759 N  N     . VAL A 1 241 ? -7.695  1.432   4.774   1.00 20.58 ? 235 VAL A N     1 
ATOM   1760 C  CA    . VAL A 1 241 ? -6.262  1.713   5.079   1.00 21.36 ? 235 VAL A CA    1 
ATOM   1761 C  C     . VAL A 1 241 ? -6.023  3.191   4.771   1.00 23.26 ? 235 VAL A C     1 
ATOM   1762 O  O     . VAL A 1 241 ? -5.929  3.596   3.611   1.00 19.73 ? 235 VAL A O     1 
ATOM   1763 C  CB    . VAL A 1 241 ? -5.327  0.800   4.277   1.00 21.98 ? 235 VAL A CB    1 
ATOM   1764 C  CG1   . VAL A 1 241 ? -3.879  0.996   4.666   1.00 24.61 ? 235 VAL A CG1   1 
ATOM   1765 C  CG2   . VAL A 1 241 ? -5.720  -0.646  4.456   1.00 22.44 ? 235 VAL A CG2   1 
ATOM   1766 N  N     . PRO A 1 242 ? -6.048  4.054   5.801   1.00 21.66 ? 236 PRO A N     1 
ATOM   1767 C  CA    . PRO A 1 242 ? -5.938  5.490   5.576   1.00 20.53 ? 236 PRO A CA    1 
ATOM   1768 C  C     . PRO A 1 242 ? -4.476  5.894   5.384   1.00 21.08 ? 236 PRO A C     1 
ATOM   1769 O  O     . PRO A 1 242 ? -3.598  5.412   6.124   1.00 20.72 ? 236 PRO A O     1 
ATOM   1770 C  CB    . PRO A 1 242 ? -6.524  6.099   6.845   1.00 23.82 ? 236 PRO A CB    1 
ATOM   1771 C  CG    . PRO A 1 242 ? -6.252  5.056   7.918   1.00 24.89 ? 236 PRO A CG    1 
ATOM   1772 C  CD    . PRO A 1 242 ? -6.277  3.713   7.211   1.00 25.11 ? 236 PRO A CD    1 
ATOM   1773 N  N     . GLU A 1 243 ? -4.240  6.821   4.463   1.00 19.29 ? 237 GLU A N     1 
ATOM   1774 C  CA    . GLU A 1 243 ? -2.871  7.305   4.201   1.00 18.82 ? 237 GLU A CA    1 
ATOM   1775 C  C     . GLU A 1 243 ? -2.889  8.812   4.044   1.00 18.89 ? 237 GLU A C     1 
ATOM   1776 O  O     . GLU A 1 243 ? -2.897  9.337   2.934   1.00 18.60 ? 237 GLU A O     1 
ATOM   1777 C  CB    . GLU A 1 243 ? -2.223  6.632   3.003   1.00 20.42 ? 237 GLU A CB    1 
ATOM   1778 C  CG    . GLU A 1 243 ? -2.155  5.145   3.142   1.00 20.13 ? 237 GLU A CG    1 
ATOM   1779 C  CD    . GLU A 1 243 ? -1.258  4.462   2.140   1.00 23.10 ? 237 GLU A CD    1 
ATOM   1780 O  OE1   . GLU A 1 243 ? -0.425  5.153   1.507   1.00 22.76 ? 237 GLU A OE1   1 
ATOM   1781 O  OE2   . GLU A 1 243 ? -1.402  3.250   2.008   1.00 25.79 ? 237 GLU A OE2   1 
ATOM   1782 N  N     . PRO A 1 244 ? -2.863  9.533   5.187   1.00 17.72 ? 238 PRO A N     1 
ATOM   1783 C  CA    . PRO A 1 244 ? -2.627  10.971  5.169   1.00 18.18 ? 238 PRO A CA    1 
ATOM   1784 C  C     . PRO A 1 244 ? -1.231  11.228  4.616   1.00 18.96 ? 238 PRO A C     1 
ATOM   1785 O  O     . PRO A 1 244 ? -0.424  10.318  4.570   1.00 17.97 ? 238 PRO A O     1 
ATOM   1786 C  CB    . PRO A 1 244 ? -2.679  11.389  6.640   1.00 19.52 ? 238 PRO A CB    1 
ATOM   1787 C  CG    . PRO A 1 244 ? -2.409  10.120  7.386   1.00 19.34 ? 238 PRO A CG    1 
ATOM   1788 C  CD    . PRO A 1 244 ? -2.957  8.998   6.545   1.00 18.87 ? 238 PRO A CD    1 
ATOM   1789 N  N     . ASN A 1 245 ? -0.977  12.453  4.170   1.00 18.04 ? 239 ASN A N     1 
ATOM   1790 C  CA    . ASN A 1 245 ? 0.308   12.801  3.537   1.00 18.79 ? 239 ASN A CA    1 
ATOM   1791 C  C     . ASN A 1 245 ? 1.464   12.343  4.414   1.00 19.41 ? 239 ASN A C     1 
ATOM   1792 O  O     . ASN A 1 245 ? 2.475   11.905  3.844   1.00 19.72 ? 239 ASN A O     1 
ATOM   1793 C  CB    . ASN A 1 245 ? 0.437   14.299  3.278   1.00 20.01 ? 239 ASN A CB    1 
ATOM   1794 C  CG    . ASN A 1 245 ? -0.508  14.820  2.208   1.00 21.66 ? 239 ASN A CG    1 
ATOM   1795 O  OD1   . ASN A 1 245 ? -1.138  14.063  1.447   1.00 22.90 ? 239 ASN A OD1   1 
ATOM   1796 N  ND2   . ASN A 1 245 ? -0.535  16.130  2.093   1.00 17.82 ? 239 ASN A ND2   1 
ATOM   1797 N  N     . ARG A 1 246 ? 1.358   12.502  5.743   1.00 20.57 ? 240 ARG A N     1 
ATOM   1798 C  CA    . ARG A 1 246 ? 2.509   12.214  6.648   1.00 22.20 ? 240 ARG A CA    1 
ATOM   1799 C  C     . ARG A 1 246 ? 2.876   10.738  6.553   1.00 21.80 ? 240 ARG A C     1 
ATOM   1800 O  O     . ARG A 1 246 ? 4.058   10.421  6.779   1.00 23.43 ? 240 ARG A O     1 
ATOM   1801 C  CB    . ARG A 1 246 ? 2.243   12.615  8.106   1.00 27.36 ? 240 ARG A CB    1 
ATOM   1802 C  CG    . ARG A 1 246 ? 1.089   11.872  8.754   1.00 31.34 ? 240 ARG A CG    1 
ATOM   1803 C  CD    . ARG A 1 246 ? 0.812   12.284  10.197  1.00 37.71 ? 240 ARG A CD    1 
ATOM   1804 N  NE    . ARG A 1 246 ? -0.483  11.726  10.615  1.00 45.30 ? 240 ARG A NE    1 
ATOM   1805 C  CZ    . ARG A 1 246 ? -1.687  12.268  10.387  1.00 40.62 ? 240 ARG A CZ    1 
ATOM   1806 N  NH1   . ARG A 1 246 ? -1.818  13.433  9.769   1.00 42.02 ? 240 ARG A NH1   1 
ATOM   1807 N  NH2   . ARG A 1 246 ? -2.761  11.638  10.825  1.00 45.75 ? 240 ARG A NH2   1 
ATOM   1808 N  N     . LEU A 1 247 ? 1.922   9.857   6.250   1.00 19.63 ? 241 LEU A N     1 
ATOM   1809 C  CA    . LEU A 1 247 ? 2.217   8.410   6.101   1.00 18.41 ? 241 LEU A CA    1 
ATOM   1810 C  C     . LEU A 1 247 ? 2.571   8.061   4.656   1.00 21.25 ? 241 LEU A C     1 
ATOM   1811 O  O     . LEU A 1 247 ? 3.349   7.109   4.485   1.00 24.78 ? 241 LEU A O     1 
ATOM   1812 C  CB    . LEU A 1 247 ? 1.046   7.561   6.577   1.00 20.26 ? 241 LEU A CB    1 
ATOM   1813 C  CG    . LEU A 1 247 ? 0.854   7.504   8.101   1.00 21.37 ? 241 LEU A CG    1 
ATOM   1814 C  CD1   . LEU A 1 247 ? -0.264  6.523   8.462   1.00 22.74 ? 241 LEU A CD1   1 
ATOM   1815 C  CD2   . LEU A 1 247 ? 2.153   7.154   8.822   1.00 22.23 ? 241 LEU A CD2   1 
ATOM   1816 N  N     . MET A 1 248 ? 1.981   8.731   3.658   1.00 19.30 ? 242 MET A N     1 
ATOM   1817 C  CA    . MET A 1 248 ? 2.149   8.335   2.238   1.00 21.08 ? 242 MET A CA    1 
ATOM   1818 C  C     . MET A 1 248 ? 3.484   8.803   1.642   1.00 19.68 ? 242 MET A C     1 
ATOM   1819 O  O     . MET A 1 248 ? 4.043   8.060   0.839   1.00 20.42 ? 242 MET A O     1 
ATOM   1820 C  CB    . MET A 1 248 ? 1.016   8.887   1.373   1.00 20.29 ? 242 MET A CB    1 
ATOM   1821 C  CG    . MET A 1 248 ? 0.942   8.177   0.046   1.00 21.30 ? 242 MET A CG    1 
ATOM   1822 S  SD    . MET A 1 248 ? -0.375  8.799   -0.998  1.00 20.17 ? 242 MET A SD    1 
ATOM   1823 C  CE    . MET A 1 248 ? -0.240  7.504   -2.244  1.00 19.02 ? 242 MET A CE    1 
ATOM   1824 N  N     . ALA A 1 249 ? 3.965   9.996   1.977   1.00 20.32 ? 243 ALA A N     1 
ATOM   1825 C  CA    . ALA A 1 249 ? 4.961   10.730  1.157   1.00 21.20 ? 243 ALA A CA    1 
ATOM   1826 C  C     . ALA A 1 249 ? 6.258   9.922   1.000   1.00 21.26 ? 243 ALA A C     1 
ATOM   1827 O  O     . ALA A 1 249 ? 6.757   9.810   -0.139  1.00 20.25 ? 243 ALA A O     1 
ATOM   1828 C  CB    . ALA A 1 249 ? 5.227   12.070  1.794   1.00 20.05 ? 243 ALA A CB    1 
ATOM   1829 N  N     . LYS A 1 250 ? 6.788   9.374   2.094   1.00 19.66 ? 244 LYS A N     1 
ATOM   1830 C  CA    . LYS A 1 250 ? 8.178   8.816   2.120   1.00 20.10 ? 244 LYS A CA    1 
ATOM   1831 C  C     . LYS A 1 250 ? 8.219   7.344   2.538   1.00 17.68 ? 244 LYS A C     1 
ATOM   1832 O  O     . LYS A 1 250 ? 9.320   6.814   2.887   1.00 20.81 ? 244 LYS A O     1 
ATOM   1833 C  CB    . LYS A 1 250 ? 9.030   9.688   3.051   1.00 22.92 ? 244 LYS A CB    1 
ATOM   1834 C  CG    . LYS A 1 250 ? 9.225   11.103  2.504   1.00 26.78 ? 244 LYS A CG    1 
ATOM   1835 C  CD    . LYS A 1 250 ? 9.501   12.122  3.586   1.00 34.70 ? 244 LYS A CD    1 
ATOM   1836 C  CE    . LYS A 1 250 ? 9.124   13.531  3.171   1.00 41.35 ? 244 LYS A CE    1 
ATOM   1837 N  NZ    . LYS A 1 250 ? 8.922   14.401  4.349   1.00 43.22 ? 244 LYS A NZ    1 
ATOM   1838 N  N     . SER A 1 251 ? 7.104   6.657   2.473   1.00 17.75 ? 245 SER A N     1 
ATOM   1839 C  CA    . SER A 1 251 ? 6.982   5.286   3.021   1.00 16.37 ? 245 SER A CA    1 
ATOM   1840 C  C     . SER A 1 251 ? 7.003   4.241   1.906   1.00 17.17 ? 245 SER A C     1 
ATOM   1841 O  O     . SER A 1 251 ? 6.715   3.063   2.236   1.00 17.47 ? 245 SER A O     1 
ATOM   1842 C  CB    . SER A 1 251 ? 5.709   5.210   3.862   1.00 17.40 ? 245 SER A CB    1 
ATOM   1843 O  OG    . SER A 1 251 ? 4.577   5.315   3.032   1.00 17.84 ? 245 SER A OG    1 
ATOM   1844 N  N     . TYR A 1 252 ? 7.246   4.629   0.638   1.00 18.46 ? 246 TYR A N     1 
ATOM   1845 C  CA    . TYR A 1 252 ? 7.222   3.706   -0.514  1.00 18.85 ? 246 TYR A CA    1 
ATOM   1846 C  C     . TYR A 1 252 ? 8.626   3.555   -1.057  1.00 19.38 ? 246 TYR A C     1 
ATOM   1847 O  O     . TYR A 1 252 ? 9.460   4.440   -0.922  1.00 19.36 ? 246 TYR A O     1 
ATOM   1848 C  CB    . TYR A 1 252 ? 6.247   4.113   -1.625  1.00 17.19 ? 246 TYR A CB    1 
ATOM   1849 C  CG    . TYR A 1 252 ? 4.796   3.969   -1.254  1.00 16.51 ? 246 TYR A CG    1 
ATOM   1850 C  CD1   . TYR A 1 252 ? 4.163   4.899   -0.425  1.00 17.62 ? 246 TYR A CD1   1 
ATOM   1851 C  CD2   . TYR A 1 252 ? 4.058   2.875   -1.687  1.00 16.91 ? 246 TYR A CD2   1 
ATOM   1852 C  CE1   . TYR A 1 252 ? 2.832   4.766   -0.062  1.00 17.16 ? 246 TYR A CE1   1 
ATOM   1853 C  CE2   . TYR A 1 252 ? 2.724   2.745   -1.363  1.00 17.61 ? 246 TYR A CE2   1 
ATOM   1854 C  CZ    . TYR A 1 252 ? 2.110   3.685   -0.548  1.00 17.90 ? 246 TYR A CZ    1 
ATOM   1855 O  OH    . TYR A 1 252 ? 0.798   3.546   -0.232  1.00 19.63 ? 246 TYR A OH    1 
ATOM   1856 N  N     . LEU A 1 253 ? 8.888   2.385   -1.611  1.00 19.85 ? 247 LEU A N     1 
ATOM   1857 C  CA    . LEU A 1 253 ? 10.102  2.144   -2.422  1.00 18.98 ? 247 LEU A CA    1 
ATOM   1858 C  C     . LEU A 1 253 ? 9.624   2.205   -3.869  1.00 20.79 ? 247 LEU A C     1 
ATOM   1859 O  O     . LEU A 1 253 ? 8.804   1.346   -4.277  1.00 20.31 ? 247 LEU A O     1 
ATOM   1860 C  CB    . LEU A 1 253 ? 10.722  0.801   -2.063  1.00 18.87 ? 247 LEU A CB    1 
ATOM   1861 C  CG    . LEU A 1 253 ? 11.372  0.744   -0.695  1.00 20.00 ? 247 LEU A CG    1 
ATOM   1862 C  CD1   . LEU A 1 253 ? 11.534  -0.678  -0.250  1.00 24.55 ? 247 LEU A CD1   1 
ATOM   1863 C  CD2   . LEU A 1 253 ? 12.696  1.471   -0.719  1.00 22.91 ? 247 LEU A CD2   1 
ATOM   1864 N  N     . ILE A 1 254 ? 10.067  3.242   -4.575  1.00 19.34 ? 248 ILE A N     1 
ATOM   1865 C  CA    . ILE A 1 254 ? 9.489   3.601   -5.896  1.00 19.22 ? 248 ILE A CA    1 
ATOM   1866 C  C     . ILE A 1 254 ? 10.581  3.457   -6.936  1.00 18.95 ? 248 ILE A C     1 
ATOM   1867 O  O     . ILE A 1 254 ? 11.526  4.215   -6.847  1.00 20.63 ? 248 ILE A O     1 
ATOM   1868 C  CB    . ILE A 1 254 ? 8.902   5.011   -5.874  1.00 18.55 ? 248 ILE A CB    1 
ATOM   1869 C  CG1   . ILE A 1 254 ? 7.849   5.134   -4.770  1.00 20.31 ? 248 ILE A CG1   1 
ATOM   1870 C  CG2   . ILE A 1 254 ? 8.347   5.373   -7.242  1.00 20.98 ? 248 ILE A CG2   1 
ATOM   1871 C  CD1   . ILE A 1 254 ? 7.363   6.537   -4.600  1.00 20.97 ? 248 ILE A CD1   1 
ATOM   1872 N  N     . LEU A 1 255 ? 10.445  2.488   -7.829  1.00 19.33 ? 249 LEU A N     1 
ATOM   1873 C  CA    . LEU A 1 255 ? 11.351  2.289   -8.978  1.00 20.70 ? 249 LEU A CA    1 
ATOM   1874 C  C     . LEU A 1 255 ? 10.706  2.905   -10.236 1.00 20.36 ? 249 LEU A C     1 
ATOM   1875 O  O     . LEU A 1 255 ? 9.572   2.515   -10.563 1.00 21.40 ? 249 LEU A O     1 
ATOM   1876 C  CB    . LEU A 1 255 ? 11.488  0.778   -9.125  1.00 25.61 ? 249 LEU A CB    1 
ATOM   1877 C  CG    . LEU A 1 255 ? 12.790  0.238   -9.663  1.00 30.74 ? 249 LEU A CG    1 
ATOM   1878 C  CD1   . LEU A 1 255 ? 13.952  0.727   -8.800  1.00 31.85 ? 249 LEU A CD1   1 
ATOM   1879 C  CD2   . LEU A 1 255 ? 12.696  -1.291  -9.714  1.00 33.73 ? 249 LEU A CD2   1 
ATOM   1880 N  N     . ASP A 1 256 ? 11.400  3.786   -10.930 1.00 19.71 ? 250 ASP A N     1 
ATOM   1881 C  CA    . ASP A 1 256 ? 10.873  4.477   -12.141 1.00 20.33 ? 250 ASP A CA    1 
ATOM   1882 C  C     . ASP A 1 256 ? 11.134  3.609   -13.381 1.00 21.13 ? 250 ASP A C     1 
ATOM   1883 O  O     . ASP A 1 256 ? 11.543  2.419   -13.268 1.00 18.65 ? 250 ASP A O     1 
ATOM   1884 C  CB    . ASP A 1 256 ? 11.419  5.912   -12.245 1.00 19.45 ? 250 ASP A CB    1 
ATOM   1885 C  CG    . ASP A 1 256 ? 12.850  6.057   -12.773 1.00 20.52 ? 250 ASP A CG    1 
ATOM   1886 O  OD1   . ASP A 1 256 ? 13.519  5.030   -13.021 1.00 20.14 ? 250 ASP A OD1   1 
ATOM   1887 O  OD2   . ASP A 1 256 ? 13.287  7.214   -12.928 1.00 22.72 ? 250 ASP A OD2   1 
ATOM   1888 N  N     . GLU A 1 257 ? 10.880  4.187   -14.543 1.00 19.26 ? 251 GLU A N     1 
ATOM   1889 C  CA    . GLU A 1 257 ? 10.838  3.450   -15.824 1.00 20.64 ? 251 GLU A CA    1 
ATOM   1890 C  C     . GLU A 1 257 ? 12.281  3.069   -16.252 1.00 19.95 ? 251 GLU A C     1 
ATOM   1891 O  O     . GLU A 1 257 ? 12.424  2.197   -17.158 1.00 20.40 ? 251 GLU A O     1 
ATOM   1892 C  CB    . GLU A 1 257 ? 10.060  4.264   -16.873 1.00 20.00 ? 251 GLU A CB    1 
ATOM   1893 C  CG    . GLU A 1 257 ? 10.749  5.553   -17.290 1.00 20.77 ? 251 GLU A CG    1 
ATOM   1894 C  CD    . GLU A 1 257 ? 10.513  6.831   -16.487 1.00 22.68 ? 251 GLU A CD    1 
ATOM   1895 O  OE1   . GLU A 1 257 ? 10.158  6.745   -15.313 1.00 20.99 ? 251 GLU A OE1   1 
ATOM   1896 O  OE2   . GLU A 1 257 ? 10.800  7.938   -17.009 1.00 24.91 ? 251 GLU A OE2   1 
ATOM   1897 N  N     . TYR A 1 258 ? 13.305  3.666   -15.627 1.00 20.75 ? 252 TYR A N     1 
ATOM   1898 C  CA    . TYR A 1 258 ? 14.737  3.296   -15.820 1.00 22.88 ? 252 TYR A CA    1 
ATOM   1899 C  C     . TYR A 1 258 ? 15.256  2.424   -14.672 1.00 23.94 ? 252 TYR A C     1 
ATOM   1900 O  O     . TYR A 1 258 ? 16.490  2.207   -14.605 1.00 25.04 ? 252 TYR A O     1 
ATOM   1901 C  CB    . TYR A 1 258 ? 15.582  4.561   -15.949 1.00 24.29 ? 252 TYR A CB    1 
ATOM   1902 C  CG    . TYR A 1 258 ? 15.231  5.402   -17.149 1.00 25.47 ? 252 TYR A CG    1 
ATOM   1903 C  CD1   . TYR A 1 258 ? 15.782  5.127   -18.392 1.00 30.94 ? 252 TYR A CD1   1 
ATOM   1904 C  CD2   . TYR A 1 258 ? 14.368  6.479   -17.044 1.00 29.21 ? 252 TYR A CD2   1 
ATOM   1905 C  CE1   . TYR A 1 258 ? 15.480  5.896   -19.510 1.00 34.13 ? 252 TYR A CE1   1 
ATOM   1906 C  CE2   . TYR A 1 258 ? 14.033  7.246   -18.154 1.00 32.95 ? 252 TYR A CE2   1 
ATOM   1907 C  CZ    . TYR A 1 258 ? 14.594  6.955   -19.392 1.00 35.28 ? 252 TYR A CZ    1 
ATOM   1908 O  OH    . TYR A 1 258 ? 14.303  7.705   -20.494 1.00 36.36 ? 252 TYR A OH    1 
ATOM   1909 N  N     . MET A 1 259 ? 14.365  1.938   -13.802 1.00 21.63 ? 253 MET A N     1 
ATOM   1910 C  CA    . MET A 1 259 ? 14.706  1.174   -12.571 1.00 20.98 ? 253 MET A CA    1 
ATOM   1911 C  C     . MET A 1 259 ? 15.694  1.969   -11.705 1.00 21.66 ? 253 MET A C     1 
ATOM   1912 O  O     . MET A 1 259 ? 16.640  1.379   -11.095 1.00 22.99 ? 253 MET A O     1 
ATOM   1913 C  CB    . MET A 1 259 ? 15.214  -0.229  -12.921 1.00 21.79 ? 253 MET A CB    1 
ATOM   1914 C  CG    . MET A 1 259 ? 14.261  -0.955  -13.823 1.00 24.98 ? 253 MET A CG    1 
ATOM   1915 S  SD    . MET A 1 259 ? 14.593  -2.726  -14.045 1.00 28.23 ? 253 MET A SD    1 
ATOM   1916 C  CE    . MET A 1 259 ? 13.568  -3.424  -12.762 1.00 27.86 ? 253 MET A CE    1 
ATOM   1917 N  N     . ARG A 1 260 ? 15.412  3.266   -11.562 1.00 20.73 ? 254 ARG A N     1 
ATOM   1918 C  CA    . ARG A 1 260 ? 16.016  4.158   -10.552 1.00 21.13 ? 254 ARG A CA    1 
ATOM   1919 C  C     . ARG A 1 260 ? 15.064  4.325   -9.356  1.00 22.71 ? 254 ARG A C     1 
ATOM   1920 O  O     . ARG A 1 260 ? 13.819  4.465   -9.580  1.00 18.87 ? 254 ARG A O     1 
ATOM   1921 C  CB    . ARG A 1 260 ? 16.306  5.510   -11.192 1.00 22.02 ? 254 ARG A CB    1 
ATOM   1922 C  CG    . ARG A 1 260 ? 17.120  5.388   -12.473 1.00 23.71 ? 254 ARG A CG    1 
ATOM   1923 C  CD    . ARG A 1 260 ? 17.404  6.751   -13.054 1.00 23.67 ? 254 ARG A CD    1 
ATOM   1924 N  NE    . ARG A 1 260 ? 16.151  7.379   -13.484 1.00 26.27 ? 254 ARG A NE    1 
ATOM   1925 C  CZ    . ARG A 1 260 ? 16.070  8.576   -14.044 1.00 31.52 ? 254 ARG A CZ    1 
ATOM   1926 N  NH1   . ARG A 1 260 ? 17.177  9.272   -14.297 1.00 29.08 ? 254 ARG A NH1   1 
ATOM   1927 N  NH2   . ARG A 1 260 ? 14.877  9.081   -14.342 1.00 28.76 ? 254 ARG A NH2   1 
ATOM   1928 N  N     . PHE A 1 261 ? 15.612  4.317   -8.138  1.00 20.73 ? 255 PHE A N     1 
ATOM   1929 C  CA    . PHE A 1 261 ? 14.792  4.586   -6.925  1.00 20.66 ? 255 PHE A CA    1 
ATOM   1930 C  C     . PHE A 1 261 ? 14.497  6.076   -6.903  1.00 20.53 ? 255 PHE A C     1 
ATOM   1931 O  O     . PHE A 1 261 ? 15.412  6.863   -7.126  1.00 23.34 ? 255 PHE A O     1 
ATOM   1932 C  CB    . PHE A 1 261 ? 15.456  4.111   -5.627  1.00 21.13 ? 255 PHE A CB    1 
ATOM   1933 C  CG    . PHE A 1 261 ? 15.333  2.632   -5.397  1.00 24.36 ? 255 PHE A CG    1 
ATOM   1934 C  CD1   . PHE A 1 261 ? 14.114  2.053   -5.106  1.00 24.58 ? 255 PHE A CD1   1 
ATOM   1935 C  CD2   . PHE A 1 261 ? 16.444  1.810   -5.519  1.00 26.89 ? 255 PHE A CD2   1 
ATOM   1936 C  CE1   . PHE A 1 261 ? 14.009  0.690   -4.905  1.00 26.34 ? 255 PHE A CE1   1 
ATOM   1937 C  CE2   . PHE A 1 261 ? 16.334  0.453   -5.300  1.00 25.53 ? 255 PHE A CE2   1 
ATOM   1938 C  CZ    . PHE A 1 261 ? 15.119  -0.105  -5.000  1.00 28.22 ? 255 PHE A CZ    1 
ATOM   1939 N  N     . LEU A 1 262 ? 13.250  6.444   -6.581  1.00 20.64 ? 256 LEU A N     1 
ATOM   1940 C  CA    . LEU A 1 262 ? 12.875  7.862   -6.421  1.00 21.53 ? 256 LEU A CA    1 
ATOM   1941 C  C     . LEU A 1 262 ? 12.852  8.227   -4.938  1.00 22.58 ? 256 LEU A C     1 
ATOM   1942 O  O     . LEU A 1 262 ? 12.124  7.584   -4.146  1.00 22.84 ? 256 LEU A O     1 
ATOM   1943 C  CB    . LEU A 1 262 ? 11.525  8.136   -7.087  1.00 21.20 ? 256 LEU A CB    1 
ATOM   1944 C  CG    . LEU A 1 262 ? 11.423  7.688   -8.550  1.00 20.10 ? 256 LEU A CG    1 
ATOM   1945 C  CD1   . LEU A 1 262 ? 10.106  8.103   -9.157  1.00 21.86 ? 256 LEU A CD1   1 
ATOM   1946 C  CD2   . LEU A 1 262 ? 12.547  8.237   -9.401  1.00 21.21 ? 256 LEU A CD2   1 
ATOM   1947 N  N     . ASN A 1 263 ? 13.589  9.287   -4.618  1.00 21.50 ? 257 ASN A N     1 
ATOM   1948 C  CA    . ASN A 1 263 ? 13.790  9.817   -3.257  1.00 25.16 ? 257 ASN A CA    1 
ATOM   1949 C  C     . ASN A 1 263 ? 12.768  10.924  -3.061  1.00 23.77 ? 257 ASN A C     1 
ATOM   1950 O  O     . ASN A 1 263 ? 12.809  11.914  -3.850  1.00 26.61 ? 257 ASN A O     1 
ATOM   1951 C  CB    . ASN A 1 263 ? 15.221  10.321  -3.068  1.00 27.26 ? 257 ASN A CB    1 
ATOM   1952 C  CG    . ASN A 1 263 ? 15.508  10.731  -1.641  1.00 32.30 ? 257 ASN A CG    1 
ATOM   1953 O  OD1   . ASN A 1 263 ? 14.783  10.353  -0.714  1.00 33.70 ? 257 ASN A OD1   1 
ATOM   1954 N  ND2   . ASN A 1 263 ? 16.567  11.495  -1.450  1.00 39.18 ? 257 ASN A ND2   1 
ATOM   1955 N  N     . CYS A 1 264 ? 11.878  10.789  -2.087  1.00 25.05 ? 258 CYS A N     1 
ATOM   1956 C  CA    . CYS A 1 264 ? 10.818  11.802  -1.848  1.00 26.10 ? 258 CYS A CA    1 
ATOM   1957 C  C     . CYS A 1 264 ? 11.155  12.710  -0.667  1.00 29.17 ? 258 CYS A C     1 
ATOM   1958 O  O     . CYS A 1 264 ? 10.292  13.500  -0.279  1.00 30.32 ? 258 CYS A O     1 
ATOM   1959 C  CB    . CYS A 1 264 ? 9.449   11.136  -1.744  1.00 29.55 ? 258 CYS A CB    1 
ATOM   1960 S  SG    . CYS A 1 264 ? 8.963   10.384  -3.322  1.00 29.45 ? 258 CYS A SG    1 
ATOM   1961 N  N     . THR A 1 265 ? 12.391  12.673  -0.186  1.00 31.07 ? 259 THR A N     1 
ATOM   1962 C  CA    . THR A 1 265 ? 12.817  13.442  1.001   1.00 42.05 ? 259 THR A CA    1 
ATOM   1963 C  C     . THR A 1 265 ? 12.451  14.910  0.748   1.00 47.76 ? 259 THR A C     1 
ATOM   1964 O  O     . THR A 1 265 ? 11.915  15.545  1.667   1.00 53.98 ? 259 THR A O     1 
ATOM   1965 C  CB    . THR A 1 265 ? 14.280  13.127  1.349   1.00 42.67 ? 259 THR A CB    1 
ATOM   1966 O  OG1   . THR A 1 265 ? 14.375  13.253  2.765   1.00 55.24 ? 259 THR A OG1   1 
ATOM   1967 C  CG2   . THR A 1 265 ? 15.270  14.040  0.666   1.00 46.34 ? 259 THR A CG2   1 
ATOM   1968 N  N     . GLY A 1 266 ? 12.614  15.410  -0.476  1.00 46.96 ? 260 GLY A N     1 
ATOM   1969 C  CA    . GLY A 1 266 ? 12.419  16.846  -0.761  1.00 52.29 ? 260 GLY A CA    1 
ATOM   1970 C  C     . GLY A 1 266 ? 10.958  17.242  -0.929  1.00 52.99 ? 260 GLY A C     1 
ATOM   1971 O  O     . GLY A 1 266 ? 10.694  18.451  -1.073  1.00 51.34 ? 260 GLY A O     1 
ATOM   1972 N  N     . GLY A 1 267 ? 10.029  16.281  -0.912  1.00 50.29 ? 261 GLY A N     1 
ATOM   1973 C  CA    . GLY A 1 267 ? 8.718   16.417  -1.575  1.00 42.27 ? 261 GLY A CA    1 
ATOM   1974 C  C     . GLY A 1 267 ? 8.887   16.443  -3.100  1.00 33.64 ? 261 GLY A C     1 
ATOM   1975 O  O     . GLY A 1 267 ? 8.011   16.960  -3.772  1.00 29.47 ? 261 GLY A O     1 
ATOM   1976 N  N     . ARG A 1 268 ? 10.010  15.948  -3.609  1.00 31.48 ? 262 ARG A N     1 
ATOM   1977 C  CA    . ARG A 1 268 ? 10.320  15.757  -5.042  1.00 31.84 ? 262 ARG A CA    1 
ATOM   1978 C  C     . ARG A 1 268 ? 10.269  14.255  -5.350  1.00 28.96 ? 262 ARG A C     1 
ATOM   1979 O  O     . ARG A 1 268 ? 9.918   13.465  -4.440  1.00 31.71 ? 262 ARG A O     1 
ATOM   1980 C  CB    . ARG A 1 268 ? 11.713  16.322  -5.345  1.00 41.00 ? 262 ARG A CB    1 
ATOM   1981 C  CG    . ARG A 1 268 ? 11.777  17.803  -5.696  1.00 48.98 ? 262 ARG A CG    1 
ATOM   1982 C  CD    . ARG A 1 268 ? 13.207  18.261  -6.040  1.00 55.49 ? 262 ARG A CD    1 
ATOM   1983 N  NE    . ARG A 1 268 ? 14.178  17.779  -5.059  1.00 60.74 ? 262 ARG A NE    1 
ATOM   1984 C  CZ    . ARG A 1 268 ? 14.292  18.216  -3.802  1.00 67.41 ? 262 ARG A CZ    1 
ATOM   1985 N  NH1   . ARG A 1 268 ? 13.525  19.195  -3.350  1.00 72.09 ? 262 ARG A NH1   1 
ATOM   1986 N  NH2   . ARG A 1 268 ? 15.190  17.678  -2.994  1.00 70.81 ? 262 ARG A NH2   1 
ATOM   1987 N  N     . LYS A 1 269 ? 10.601  13.860  -6.579  1.00 23.76 ? 263 LYS A N     1 
ATOM   1988 C  CA    . LYS A 1 269 ? 10.874  12.448  -6.939  1.00 26.75 ? 263 LYS A CA    1 
ATOM   1989 C  C     . LYS A 1 269 ? 12.258  12.399  -7.590  1.00 25.90 ? 263 LYS A C     1 
ATOM   1990 O  O     . LYS A 1 269 ? 12.319  12.445  -8.807  1.00 32.31 ? 263 LYS A O     1 
ATOM   1991 C  CB    . LYS A 1 269 ? 9.761   11.916  -7.855  1.00 26.21 ? 263 LYS A CB    1 
ATOM   1992 C  CG    . LYS A 1 269 ? 8.642   11.190  -7.126  1.00 23.21 ? 263 LYS A CG    1 
ATOM   1993 C  CD    . LYS A 1 269 ? 7.479   10.789  -8.021  1.00 22.54 ? 263 LYS A CD    1 
ATOM   1994 C  CE    . LYS A 1 269 ? 6.530   9.848   -7.304  1.00 21.57 ? 263 LYS A CE    1 
ATOM   1995 N  NZ    . LYS A 1 269 ? 5.264   9.639   -8.053  1.00 20.84 ? 263 LYS A NZ    1 
ATOM   1996 N  N     . ASP A 1 270 ? 13.317  12.451  -6.791  1.00 27.89 ? 264 ASP A N     1 
ATOM   1997 C  CA    . ASP A 1 270 ? 14.699  12.621  -7.297  1.00 27.35 ? 264 ASP A CA    1 
ATOM   1998 C  C     . ASP A 1 270 ? 15.268  11.233  -7.513  1.00 25.81 ? 264 ASP A C     1 
ATOM   1999 O  O     . ASP A 1 270 ? 15.324  10.434  -6.575  1.00 26.85 ? 264 ASP A O     1 
ATOM   2000 C  CB    . ASP A 1 270 ? 15.591  13.405  -6.327  1.00 32.24 ? 264 ASP A CB    1 
ATOM   2001 C  CG    . ASP A 1 270 ? 15.296  14.902  -6.228  1.00 38.89 ? 264 ASP A CG    1 
ATOM   2002 O  OD1   . ASP A 1 270 ? 14.928  15.506  -7.241  1.00 48.30 ? 264 ASP A OD1   1 
ATOM   2003 O  OD2   . ASP A 1 270 ? 15.451  15.458  -5.118  1.00 47.42 ? 264 ASP A OD2   1 
ATOM   2004 N  N     . PRO A 1 271 ? 15.692  10.904  -8.748  1.00 25.01 ? 265 PRO A N     1 
ATOM   2005 C  CA    . PRO A 1 271 ? 16.160  9.553   -9.047  1.00 24.44 ? 265 PRO A CA    1 
ATOM   2006 C  C     . PRO A 1 271 ? 17.595  9.259   -8.600  1.00 25.73 ? 265 PRO A C     1 
ATOM   2007 O  O     . PRO A 1 271 ? 18.470  10.098  -8.732  1.00 28.28 ? 265 PRO A O     1 
ATOM   2008 C  CB    . PRO A 1 271 ? 16.004  9.436   -10.569 1.00 23.64 ? 265 PRO A CB    1 
ATOM   2009 C  CG    . PRO A 1 271 ? 16.168  10.849  -11.048 1.00 27.39 ? 265 PRO A CG    1 
ATOM   2010 C  CD    . PRO A 1 271 ? 15.576  11.736  -9.962  1.00 26.31 ? 265 PRO A CD    1 
ATOM   2011 N  N     . SER A 1 272 ? 17.797  8.069   -8.070  1.00 24.44 ? 266 SER A N     1 
ATOM   2012 C  CA    . SER A 1 272 ? 19.126  7.458   -7.861  1.00 25.18 ? 266 SER A CA    1 
ATOM   2013 C  C     . SER A 1 272 ? 19.736  7.105   -9.233  1.00 27.95 ? 266 SER A C     1 
ATOM   2014 O  O     . SER A 1 272 ? 19.074  7.287   -10.255 1.00 26.26 ? 266 SER A O     1 
ATOM   2015 C  CB    . SER A 1 272 ? 18.983  6.231   -7.006  1.00 26.22 ? 266 SER A CB    1 
ATOM   2016 O  OG    . SER A 1 272 ? 18.422  5.155   -7.755  1.00 24.24 ? 266 SER A OG    1 
ATOM   2017 N  N     . LYS A 1 273 ? 20.889  6.442   -9.243  1.00 28.91 ? 267 LYS A N     1 
ATOM   2018 C  CA    . LYS A 1 273 ? 21.365  5.671   -10.424 1.00 30.01 ? 267 LYS A CA    1 
ATOM   2019 C  C     . LYS A 1 273 ? 20.507  4.421   -10.602 1.00 25.37 ? 267 LYS A C     1 
ATOM   2020 O  O     . LYS A 1 273 ? 19.894  3.982   -9.631  1.00 26.12 ? 267 LYS A O     1 
ATOM   2021 C  CB    . LYS A 1 273 ? 22.828  5.278   -10.223 1.00 32.98 ? 267 LYS A CB    1 
ATOM   2022 C  CG    . LYS A 1 273 ? 23.758  6.474   -10.171 1.00 39.22 ? 267 LYS A CG    1 
ATOM   2023 C  CD    . LYS A 1 273 ? 23.880  7.157   -11.499 1.00 45.64 ? 267 LYS A CD    1 
ATOM   2024 C  CE    . LYS A 1 273 ? 25.320  7.497   -11.836 1.00 57.37 ? 267 LYS A CE    1 
ATOM   2025 N  NZ    . LYS A 1 273 ? 25.996  8.217   -10.723 1.00 54.17 ? 267 LYS A NZ    1 
ATOM   2026 N  N     . SER A 1 274 ? 20.472  3.848   -11.796 1.00 24.21 ? 268 SER A N     1 
ATOM   2027 C  CA    . SER A 1 274 ? 19.681  2.615   -12.058 1.00 24.90 ? 268 SER A CA    1 
ATOM   2028 C  C     . SER A 1 274 ? 20.279  1.451   -11.280 1.00 25.12 ? 268 SER A C     1 
ATOM   2029 O  O     . SER A 1 274 ? 21.536  1.364   -11.178 1.00 26.93 ? 268 SER A O     1 
ATOM   2030 C  CB    . SER A 1 274 ? 19.550  2.318   -13.523 1.00 22.09 ? 268 SER A CB    1 
ATOM   2031 O  OG    . SER A 1 274 ? 18.889  1.093   -13.739 1.00 23.62 ? 268 SER A OG    1 
ATOM   2032 N  N     . ILE A 1 275 ? 19.417  0.589   -10.752 1.00 22.67 ? 269 ILE A N     1 
ATOM   2033 C  CA    . ILE A 1 275 ? 19.851  -0.694  -10.149 1.00 24.19 ? 269 ILE A CA    1 
ATOM   2034 C  C     . ILE A 1 275 ? 20.540  -1.541  -11.225 1.00 26.79 ? 269 ILE A C     1 
ATOM   2035 O  O     . ILE A 1 275 ? 21.409  -2.316  -10.844 1.00 24.95 ? 269 ILE A O     1 
ATOM   2036 C  CB    . ILE A 1 275 ? 18.724  -1.438  -9.448  1.00 23.07 ? 269 ILE A CB    1 
ATOM   2037 C  CG1   . ILE A 1 275 ? 17.697  -1.993  -10.443 1.00 21.72 ? 269 ILE A CG1   1 
ATOM   2038 C  CG2   . ILE A 1 275 ? 18.095  -0.544  -8.369  1.00 22.20 ? 269 ILE A CG2   1 
ATOM   2039 C  CD1   . ILE A 1 275 ? 16.566  -2.697  -9.781  1.00 22.07 ? 269 ILE A CD1   1 
ATOM   2040 N  N     . LEU A 1 276 ? 20.268  -1.316  -12.517 1.00 27.29 ? 270 LEU A N     1 
ATOM   2041 C  CA    . LEU A 1 276 ? 20.964  -2.023  -13.636 1.00 27.55 ? 270 LEU A CA    1 
ATOM   2042 C  C     . LEU A 1 276 ? 22.384  -1.473  -13.866 1.00 27.36 ? 270 LEU A C     1 
ATOM   2043 O  O     . LEU A 1 276 ? 23.169  -2.194  -14.522 1.00 31.90 ? 270 LEU A O     1 
ATOM   2044 C  CB    . LEU A 1 276 ? 20.107  -1.931  -14.903 1.00 26.11 ? 270 LEU A CB    1 
ATOM   2045 C  CG    . LEU A 1 276 ? 18.706  -2.527  -14.793 1.00 27.88 ? 270 LEU A CG    1 
ATOM   2046 C  CD1   . LEU A 1 276 ? 17.899  -2.226  -16.043 1.00 32.55 ? 270 LEU A CD1   1 
ATOM   2047 C  CD2   . LEU A 1 276 ? 18.757  -4.012  -14.560 1.00 30.07 ? 270 LEU A CD2   1 
ATOM   2048 N  N     . GLU A 1 277 ? 22.722  -0.279  -13.385 1.00 29.76 ? 271 GLU A N     1 
ATOM   2049 C  CA    . GLU A 1 277 ? 24.085  0.322   -13.451 1.00 35.30 ? 271 GLU A CA    1 
ATOM   2050 C  C     . GLU A 1 277 ? 24.869  0.021   -12.153 1.00 37.91 ? 271 GLU A C     1 
ATOM   2051 O  O     . GLU A 1 277 ? 25.980  -0.502  -12.278 1.00 34.29 ? 271 GLU A O     1 
ATOM   2052 C  CB    . GLU A 1 277 ? 24.019  1.828   -13.717 1.00 39.87 ? 271 GLU A CB    1 
ATOM   2053 C  CG    . GLU A 1 277 ? 25.382  2.524   -13.687 1.00 50.49 ? 271 GLU A CG    1 
ATOM   2054 C  CD    . GLU A 1 277 ? 25.372  4.020   -13.997 1.00 58.99 ? 271 GLU A CD    1 
ATOM   2055 O  OE1   . GLU A 1 277 ? 24.342  4.513   -14.510 1.00 66.94 ? 271 GLU A OE1   1 
ATOM   2056 O  OE2   . GLU A 1 277 ? 26.395  4.698   -13.712 1.00 68.87 ? 271 GLU A OE2   1 
ATOM   2057 N  N     . VAL A 1 278 ? 24.329  0.310   -10.954 1.00 33.99 ? 272 VAL A N     1 
ATOM   2058 C  CA    . VAL A 1 278 ? 25.125  0.310   -9.670  1.00 34.75 ? 272 VAL A CA    1 
ATOM   2059 C  C     . VAL A 1 278 ? 24.687  -0.793  -8.694  1.00 34.12 ? 272 VAL A C     1 
ATOM   2060 O  O     . VAL A 1 278 ? 25.338  -0.914  -7.614  1.00 35.60 ? 272 VAL A O     1 
ATOM   2061 C  CB    . VAL A 1 278 ? 25.075  1.682   -8.972  1.00 31.45 ? 272 VAL A CB    1 
ATOM   2062 C  CG1   . VAL A 1 278 ? 25.629  2.784   -9.856  1.00 33.57 ? 272 VAL A CG1   1 
ATOM   2063 C  CG2   . VAL A 1 278 ? 23.664  2.040   -8.505  1.00 33.35 ? 272 VAL A CG2   1 
ATOM   2064 N  N     . GLY A 1 279 ? 23.632  -1.558  -9.000  1.00 29.88 ? 273 GLY A N     1 
ATOM   2065 C  CA    . GLY A 1 279 ? 23.054  -2.545  -8.071  1.00 30.41 ? 273 GLY A CA    1 
ATOM   2066 C  C     . GLY A 1 279 ? 22.063  -1.928  -7.077  1.00 26.57 ? 273 GLY A C     1 
ATOM   2067 O  O     . GLY A 1 279 ? 22.044  -0.711  -6.895  1.00 27.00 ? 273 GLY A O     1 
ATOM   2068 N  N     . VAL A 1 280 ? 21.282  -2.766  -6.419  1.00 29.31 ? 274 VAL A N     1 
ATOM   2069 C  CA    . VAL A 1 280 ? 20.220  -2.317  -5.465  1.00 29.32 ? 274 VAL A CA    1 
ATOM   2070 C  C     . VAL A 1 280 ? 20.845  -1.570  -4.273  1.00 32.43 ? 274 VAL A C     1 
ATOM   2071 O  O     . VAL A 1 280 ? 20.363  -0.490  -3.906  1.00 27.58 ? 274 VAL A O     1 
ATOM   2072 C  CB    . VAL A 1 280 ? 19.390  -3.524  -5.008  1.00 28.24 ? 274 VAL A CB    1 
ATOM   2073 C  CG1   . VAL A 1 280 ? 18.457  -3.178  -3.871  1.00 26.88 ? 274 VAL A CG1   1 
ATOM   2074 C  CG2   . VAL A 1 280 ? 18.631  -4.139  -6.176  1.00 28.60 ? 274 VAL A CG2   1 
ATOM   2075 N  N     . GLN A 1 281 ? 21.897  -2.120  -3.672  1.00 31.88 ? 275 GLN A N     1 
ATOM   2076 C  CA    . GLN A 1 281 ? 22.446  -1.578  -2.405  1.00 35.31 ? 275 GLN A CA    1 
ATOM   2077 C  C     . GLN A 1 281 ? 22.952  -0.153  -2.635  1.00 30.36 ? 275 GLN A C     1 
ATOM   2078 O  O     . GLN A 1 281 ? 22.509  0.776   -1.913  1.00 28.48 ? 275 GLN A O     1 
ATOM   2079 C  CB    . GLN A 1 281 ? 23.500  -2.557  -1.881  1.00 40.79 ? 275 GLN A CB    1 
ATOM   2080 C  CG    . GLN A 1 281 ? 23.805  -2.394  -0.406  1.00 46.99 ? 275 GLN A CG    1 
ATOM   2081 C  CD    . GLN A 1 281 ? 25.211  -1.890  -0.222  1.00 56.14 ? 275 GLN A CD    1 
ATOM   2082 O  OE1   . GLN A 1 281 ? 26.095  -2.645  0.175   1.00 64.69 ? 275 GLN A OE1   1 
ATOM   2083 N  NE2   . GLN A 1 281 ? 25.428  -0.622  -0.549  1.00 57.12 ? 275 GLN A NE2   1 
ATOM   2084 N  N     . GLN A 1 282 ? 23.748  0.068   -3.679  1.00 29.36 ? 276 GLN A N     1 
ATOM   2085 C  CA    . GLN A 1 282 ? 24.270  1.415   -3.988  1.00 34.02 ? 276 GLN A CA    1 
ATOM   2086 C  C     . GLN A 1 282 ? 23.115  2.349   -4.351  1.00 30.31 ? 276 GLN A C     1 
ATOM   2087 O  O     . GLN A 1 282 ? 23.185  3.495   -3.969  1.00 29.50 ? 276 GLN A O     1 
ATOM   2088 C  CB    . GLN A 1 282 ? 25.307  1.359   -5.115  1.00 39.88 ? 276 GLN A CB    1 
ATOM   2089 C  CG    . GLN A 1 282 ? 26.025  2.681   -5.329  1.00 51.18 ? 276 GLN A CG    1 
ATOM   2090 C  CD    . GLN A 1 282 ? 27.522  2.570   -5.149  1.00 59.37 ? 276 GLN A CD    1 
ATOM   2091 O  OE1   . GLN A 1 282 ? 28.180  1.684   -5.704  1.00 63.60 ? 276 GLN A OE1   1 
ATOM   2092 N  NE2   . GLN A 1 282 ? 28.071  3.488   -4.369  1.00 60.84 ? 276 GLN A NE2   1 
ATOM   2093 N  N     . ALA A 1 283 ? 22.093  1.892   -5.088  1.00 28.26 ? 277 ALA A N     1 
ATOM   2094 C  CA    . ALA A 1 283 ? 21.001  2.792   -5.541  1.00 27.11 ? 277 ALA A CA    1 
ATOM   2095 C  C     . ALA A 1 283 ? 20.167  3.240   -4.330  1.00 26.94 ? 277 ALA A C     1 
ATOM   2096 O  O     . ALA A 1 283 ? 19.781  4.422   -4.254  1.00 28.36 ? 277 ALA A O     1 
ATOM   2097 C  CB    . ALA A 1 283 ? 20.165  2.095   -6.575  1.00 26.25 ? 277 ALA A CB    1 
ATOM   2098 N  N     . LEU A 1 284 ? 19.907  2.318   -3.409  1.00 27.13 ? 278 LEU A N     1 
ATOM   2099 C  CA    . LEU A 1 284 ? 19.058  2.548   -2.213  1.00 28.18 ? 278 LEU A CA    1 
ATOM   2100 C  C     . LEU A 1 284 ? 19.793  3.420   -1.191  1.00 33.22 ? 278 LEU A C     1 
ATOM   2101 O  O     . LEU A 1 284 ? 19.107  4.180   -0.441  1.00 27.83 ? 278 LEU A O     1 
ATOM   2102 C  CB    . LEU A 1 284 ? 18.719  1.186   -1.616  1.00 28.84 ? 278 LEU A CB    1 
ATOM   2103 C  CG    . LEU A 1 284 ? 17.333  1.010   -1.019  1.00 35.31 ? 278 LEU A CG    1 
ATOM   2104 C  CD1   . LEU A 1 284 ? 16.258  1.706   -1.851  1.00 35.01 ? 278 LEU A CD1   1 
ATOM   2105 C  CD2   . LEU A 1 284 ? 17.049  -0.490  -0.878  1.00 35.04 ? 278 LEU A CD2   1 
ATOM   2106 N  N     . GLN A 1 285 ? 21.131  3.367   -1.190  1.00 32.89 ? 279 GLN A N     1 
ATOM   2107 C  CA    . GLN A 1 285 ? 21.959  3.889   -0.072  1.00 39.62 ? 279 GLN A CA    1 
ATOM   2108 C  C     . GLN A 1 285 ? 21.533  5.309   0.281   1.00 37.49 ? 279 GLN A C     1 
ATOM   2109 O  O     . GLN A 1 285 ? 21.298  5.559   1.487   1.00 45.66 ? 279 GLN A O     1 
ATOM   2110 C  CB    . GLN A 1 285 ? 23.451  3.853   -0.394  1.00 44.69 ? 279 GLN A CB    1 
ATOM   2111 C  CG    . GLN A 1 285 ? 24.309  3.947   0.856   1.00 50.34 ? 279 GLN A CG    1 
ATOM   2112 C  CD    . GLN A 1 285 ? 25.713  3.492   0.557   1.00 56.27 ? 279 GLN A CD    1 
ATOM   2113 O  OE1   . GLN A 1 285 ? 26.595  4.306   0.304   1.00 60.53 ? 279 GLN A OE1   1 
ATOM   2114 N  NE2   . GLN A 1 285 ? 25.907  2.180   0.530   1.00 56.84 ? 279 GLN A NE2   1 
ATOM   2115 N  N     . ALA A 1 286 ? 21.421  6.197   -0.704  1.00 36.53 ? 280 ALA A N     1 
ATOM   2116 C  CA    . ALA A 1 286 ? 21.060  7.625   -0.509  1.00 39.69 ? 280 ALA A CA    1 
ATOM   2117 C  C     . ALA A 1 286 ? 19.601  7.875   -0.944  1.00 39.47 ? 280 ALA A C     1 
ATOM   2118 O  O     . ALA A 1 286 ? 19.297  8.908   -1.574  1.00 43.95 ? 280 ALA A O     1 
ATOM   2119 C  CB    . ALA A 1 286 ? 22.009  8.485   -1.295  1.00 42.63 ? 280 ALA A CB    1 
ATOM   2120 N  N     . VAL A 1 287 ? 18.736  6.895   -0.737  1.00 34.18 ? 281 VAL A N     1 
ATOM   2121 C  CA    . VAL A 1 287 ? 17.272  7.083   -0.878  1.00 32.05 ? 281 VAL A CA    1 
ATOM   2122 C  C     . VAL A 1 287 ? 16.708  7.039   0.543   1.00 28.05 ? 281 VAL A C     1 
ATOM   2123 O  O     . VAL A 1 287 ? 17.025  6.106   1.289   1.00 27.32 ? 281 VAL A O     1 
ATOM   2124 C  CB    . VAL A 1 287 ? 16.650  6.021   -1.807  1.00 34.58 ? 281 VAL A CB    1 
ATOM   2125 C  CG1   . VAL A 1 287 ? 15.147  6.076   -1.787  1.00 34.60 ? 281 VAL A CG1   1 
ATOM   2126 C  CG2   . VAL A 1 287 ? 17.160  6.194   -3.233  1.00 40.86 ? 281 VAL A CG2   1 
ATOM   2127 N  N     . PHE A 1 288 ? 15.830  7.980   0.870   1.00 24.28 ? 282 PHE A N     1 
ATOM   2128 C  CA    . PHE A 1 288 ? 15.084  7.942   2.148   1.00 24.27 ? 282 PHE A CA    1 
ATOM   2129 C  C     . PHE A 1 288 ? 13.885  7.001   1.969   1.00 23.08 ? 282 PHE A C     1 
ATOM   2130 O  O     . PHE A 1 288 ? 13.137  7.106   0.989   1.00 26.36 ? 282 PHE A O     1 
ATOM   2131 C  CB    . PHE A 1 288 ? 14.696  9.337   2.609   1.00 24.50 ? 282 PHE A CB    1 
ATOM   2132 C  CG    . PHE A 1 288 ? 14.052  9.329   3.975   1.00 27.06 ? 282 PHE A CG    1 
ATOM   2133 C  CD1   . PHE A 1 288 ? 14.765  8.930   5.101   1.00 32.68 ? 282 PHE A CD1   1 
ATOM   2134 C  CD2   . PHE A 1 288 ? 12.719  9.646   4.123   1.00 29.74 ? 282 PHE A CD2   1 
ATOM   2135 C  CE1   . PHE A 1 288 ? 14.159  8.893   6.351   1.00 34.48 ? 282 PHE A CE1   1 
ATOM   2136 C  CE2   . PHE A 1 288 ? 12.118  9.641   5.373   1.00 30.43 ? 282 PHE A CE2   1 
ATOM   2137 C  CZ    . PHE A 1 288 ? 12.826  9.237   6.479   1.00 31.95 ? 282 PHE A CZ    1 
ATOM   2138 N  N     . TRP A 1 289 ? 13.748  6.063   2.881   1.00 21.15 ? 283 TRP A N     1 
ATOM   2139 C  CA    . TRP A 1 289 ? 12.585  5.166   3.002   1.00 20.97 ? 283 TRP A CA    1 
ATOM   2140 C  C     . TRP A 1 289 ? 12.225  5.091   4.488   1.00 22.96 ? 283 TRP A C     1 
ATOM   2141 O  O     . TRP A 1 289 ? 13.053  4.578   5.258   1.00 23.59 ? 283 TRP A O     1 
ATOM   2142 C  CB    . TRP A 1 289 ? 12.876  3.791   2.431   1.00 19.94 ? 283 TRP A CB    1 
ATOM   2143 C  CG    . TRP A 1 289 ? 11.691  2.899   2.530   1.00 20.96 ? 283 TRP A CG    1 
ATOM   2144 C  CD1   . TRP A 1 289 ? 10.384  3.198   2.300   1.00 21.37 ? 283 TRP A CD1   1 
ATOM   2145 C  CD2   . TRP A 1 289 ? 11.740  1.511   2.881   1.00 21.69 ? 283 TRP A CD2   1 
ATOM   2146 N  NE1   . TRP A 1 289 ? 9.618   2.074   2.492   1.00 21.92 ? 283 TRP A NE1   1 
ATOM   2147 C  CE2   . TRP A 1 289 ? 10.425  1.023   2.826   1.00 19.89 ? 283 TRP A CE2   1 
ATOM   2148 C  CE3   . TRP A 1 289 ? 12.782  0.659   3.242   1.00 22.21 ? 283 TRP A CE3   1 
ATOM   2149 C  CZ2   . TRP A 1 289 ? 10.116  -0.291  3.149   1.00 24.00 ? 283 TRP A CZ2   1 
ATOM   2150 C  CZ3   . TRP A 1 289 ? 12.483  -0.653  3.532   1.00 23.47 ? 283 TRP A CZ3   1 
ATOM   2151 C  CH2   . TRP A 1 289 ? 11.168  -1.118  3.500   1.00 22.93 ? 283 TRP A CH2   1 
ATOM   2152 N  N     . ASP A 1 290 ? 11.088  5.674   4.860   1.00 21.77 ? 284 ASP A N     1 
ATOM   2153 C  CA    . ASP A 1 290 ? 10.631  5.748   6.275   1.00 22.87 ? 284 ASP A CA    1 
ATOM   2154 C  C     . ASP A 1 290 ? 9.966   4.425   6.654   1.00 20.94 ? 284 ASP A C     1 
ATOM   2155 O  O     . ASP A 1 290 ? 8.742   4.221   6.422   1.00 22.05 ? 284 ASP A O     1 
ATOM   2156 C  CB    . ASP A 1 290 ? 9.752   6.980   6.482   1.00 23.77 ? 284 ASP A CB    1 
ATOM   2157 C  CG    . ASP A 1 290 ? 9.361   7.274   7.925   1.00 23.67 ? 284 ASP A CG    1 
ATOM   2158 O  OD1   . ASP A 1 290 ? 9.527   6.369   8.809   1.00 23.43 ? 284 ASP A OD1   1 
ATOM   2159 O  OD2   . ASP A 1 290 ? 8.807   8.388   8.143   1.00 27.31 ? 284 ASP A OD2   1 
ATOM   2160 N  N     . GLU A 1 291 ? 10.742  3.543   7.248   1.00 20.60 ? 285 GLU A N     1 
ATOM   2161 C  CA    . GLU A 1 291 ? 10.250  2.199   7.580   1.00 22.13 ? 285 GLU A CA    1 
ATOM   2162 C  C     . GLU A 1 291 ? 9.215   2.265   8.700   1.00 21.21 ? 285 GLU A C     1 
ATOM   2163 O  O     . GLU A 1 291 ? 8.278   1.464   8.670   1.00 21.01 ? 285 GLU A O     1 
ATOM   2164 C  CB    . GLU A 1 291 ? 11.425  1.311   7.926   1.00 26.15 ? 285 GLU A CB    1 
ATOM   2165 C  CG    . GLU A 1 291 ? 12.206  0.933   6.708   1.00 28.94 ? 285 GLU A CG    1 
ATOM   2166 C  CD    . GLU A 1 291 ? 13.190  -0.192  6.953   1.00 33.78 ? 285 GLU A CD    1 
ATOM   2167 O  OE1   . GLU A 1 291 ? 12.738  -1.290  7.283   1.00 37.19 ? 285 GLU A OE1   1 
ATOM   2168 O  OE2   . GLU A 1 291 ? 14.387  0.049   6.818   1.00 34.40 ? 285 GLU A OE2   1 
ATOM   2169 N  N     . GLU A 1 292 ? 9.320   3.209   9.626   1.00 18.97 ? 286 GLU A N     1 
ATOM   2170 C  CA    . GLU A 1 292 ? 8.271   3.319   10.675  1.00 20.51 ? 286 GLU A CA    1 
ATOM   2171 C  C     . GLU A 1 292 ? 6.952   3.727   9.998   1.00 21.02 ? 286 GLU A C     1 
ATOM   2172 O  O     . GLU A 1 292 ? 5.896   3.150   10.313  1.00 21.85 ? 286 GLU A O     1 
ATOM   2173 C  CB    . GLU A 1 292 ? 8.680   4.311   11.762  1.00 26.00 ? 286 GLU A CB    1 
ATOM   2174 C  CG    . GLU A 1 292 ? 9.949   3.959   12.554  1.00 27.68 ? 286 GLU A CG    1 
ATOM   2175 C  CD    . GLU A 1 292 ? 10.205  4.966   13.681  1.00 32.33 ? 286 GLU A CD    1 
ATOM   2176 O  OE1   . GLU A 1 292 ? 9.769   6.169   13.529  1.00 29.53 ? 286 GLU A OE1   1 
ATOM   2177 O  OE2   . GLU A 1 292 ? 10.791  4.556   14.726  1.00 33.40 ? 286 GLU A OE2   1 
ATOM   2178 N  N     . ALA A 1 293 ? 6.971   4.697   9.088   1.00 19.02 ? 287 ALA A N     1 
ATOM   2179 C  CA    . ALA A 1 293 ? 5.751   5.093   8.330   1.00 19.33 ? 287 ALA A CA    1 
ATOM   2180 C  C     . ALA A 1 293 ? 5.234   3.886   7.538   1.00 18.33 ? 287 ALA A C     1 
ATOM   2181 O  O     . ALA A 1 293 ? 4.012   3.679   7.479   1.00 18.72 ? 287 ALA A O     1 
ATOM   2182 C  CB    . ALA A 1 293 ? 6.014   6.243   7.404   1.00 22.81 ? 287 ALA A CB    1 
ATOM   2183 N  N     . PHE A 1 294 ? 6.126   3.133   6.914   1.00 17.49 ? 288 PHE A N     1 
ATOM   2184 C  CA    . PHE A 1 294 ? 5.755   1.960   6.076   1.00 17.79 ? 288 PHE A CA    1 
ATOM   2185 C  C     . PHE A 1 294 ? 5.010   0.929   6.938   1.00 18.56 ? 288 PHE A C     1 
ATOM   2186 O  O     . PHE A 1 294 ? 3.898   0.464   6.593   1.00 19.14 ? 288 PHE A O     1 
ATOM   2187 C  CB    . PHE A 1 294 ? 7.024   1.377   5.477   1.00 17.88 ? 288 PHE A CB    1 
ATOM   2188 C  CG    . PHE A 1 294 ? 6.827   0.049   4.790   1.00 19.03 ? 288 PHE A CG    1 
ATOM   2189 C  CD1   . PHE A 1 294 ? 6.317   -0.015  3.499   1.00 19.71 ? 288 PHE A CD1   1 
ATOM   2190 C  CD2   . PHE A 1 294 ? 7.175   -1.124  5.421   1.00 19.11 ? 288 PHE A CD2   1 
ATOM   2191 C  CE1   . PHE A 1 294 ? 6.177   -1.226  2.845   1.00 20.02 ? 288 PHE A CE1   1 
ATOM   2192 C  CE2   . PHE A 1 294 ? 7.022   -2.337  4.779   1.00 20.03 ? 288 PHE A CE2   1 
ATOM   2193 C  CZ    . PHE A 1 294 ? 6.482   -2.391  3.505   1.00 20.80 ? 288 PHE A CZ    1 
ATOM   2194 N  N     . VAL A 1 295 ? 5.560   0.599   8.098   1.00 19.01 ? 289 VAL A N     1 
ATOM   2195 C  CA    . VAL A 1 295 ? 4.877   -0.334  9.036   1.00 20.29 ? 289 VAL A CA    1 
ATOM   2196 C  C     . VAL A 1 295 ? 3.545   0.297   9.502   1.00 19.30 ? 289 VAL A C     1 
ATOM   2197 O  O     . VAL A 1 295 ? 2.520   -0.383  9.448   1.00 20.05 ? 289 VAL A O     1 
ATOM   2198 C  CB    . VAL A 1 295 ? 5.800   -0.766  10.194  1.00 20.75 ? 289 VAL A CB    1 
ATOM   2199 C  CG1   . VAL A 1 295 ? 5.022   -1.550  11.227  1.00 22.79 ? 289 VAL A CG1   1 
ATOM   2200 C  CG2   . VAL A 1 295 ? 7.003   -1.566  9.682   1.00 24.23 ? 289 VAL A CG2   1 
ATOM   2201 N  N     . GLU A 1 296 ? 3.534   1.577   9.875   1.00 18.65 ? 290 GLU A N     1 
ATOM   2202 C  CA    . GLU A 1 296 ? 2.341   2.232   10.452  1.00 19.32 ? 290 GLU A CA    1 
ATOM   2203 C  C     . GLU A 1 296 ? 1.195   2.215   9.453   1.00 19.74 ? 290 GLU A C     1 
ATOM   2204 O  O     . GLU A 1 296 ? 0.073   1.962   9.886   1.00 20.11 ? 290 GLU A O     1 
ATOM   2205 C  CB    . GLU A 1 296 ? 2.618   3.664   10.900  1.00 20.75 ? 290 GLU A CB    1 
ATOM   2206 C  CG    . GLU A 1 296 ? 1.411   4.370   11.489  1.00 21.95 ? 290 GLU A CG    1 
ATOM   2207 C  CD    . GLU A 1 296 ? 1.791   5.461   12.499  1.00 24.57 ? 290 GLU A CD    1 
ATOM   2208 O  OE1   . GLU A 1 296 ? 2.772   5.244   13.290  1.00 25.86 ? 290 GLU A OE1   1 
ATOM   2209 O  OE2   . GLU A 1 296 ? 1.144   6.537   12.498  1.00 27.26 ? 290 GLU A OE2   1 
ATOM   2210 N  N     . ARG A 1 297 ? 1.441   2.450   8.153   1.00 19.30 ? 291 ARG A N     1 
ATOM   2211 C  CA    . ARG A 1 297 ? 0.334   2.443   7.169   1.00 20.42 ? 291 ARG A CA    1 
ATOM   2212 C  C     . ARG A 1 297 ? -0.145  1.023   6.863   1.00 22.11 ? 291 ARG A C     1 
ATOM   2213 O  O     . ARG A 1 297 ? -1.134  0.896   6.128   1.00 25.42 ? 291 ARG A O     1 
ATOM   2214 C  CB    . ARG A 1 297 ? 0.701   3.182   5.877   1.00 20.12 ? 291 ARG A CB    1 
ATOM   2215 C  CG    . ARG A 1 297 ? 1.832   2.569   5.062   1.00 19.82 ? 291 ARG A CG    1 
ATOM   2216 C  CD    . ARG A 1 297 ? 1.915   3.286   3.726   1.00 18.95 ? 291 ARG A CD    1 
ATOM   2217 N  NE    . ARG A 1 297 ? 3.077   2.904   2.913   1.00 18.60 ? 291 ARG A NE    1 
ATOM   2218 C  CZ    . ARG A 1 297 ? 3.117   1.840   2.137   1.00 17.36 ? 291 ARG A CZ    1 
ATOM   2219 N  NH1   . ARG A 1 297 ? 2.089   1.008   2.097   1.00 19.91 ? 291 ARG A NH1   1 
ATOM   2220 N  NH2   . ARG A 1 297 ? 4.194   1.573   1.448   1.00 19.57 ? 291 ARG A NH2   1 
ATOM   2221 N  N     . GLY A 1 298 ? 0.532   -0.017  7.338   1.00 21.07 ? 292 GLY A N     1 
ATOM   2222 C  CA    . GLY A 1 298 ? 0.161   -1.410  7.051   1.00 22.67 ? 292 GLY A CA    1 
ATOM   2223 C  C     . GLY A 1 298 ? 0.846   -1.985  5.812   1.00 22.54 ? 292 GLY A C     1 
ATOM   2224 O  O     . GLY A 1 298 ? 0.226   -2.825  5.132   1.00 21.97 ? 292 GLY A O     1 
ATOM   2225 N  N     . GLY A 1 299 ? 2.099   -1.620  5.557   1.00 21.78 ? 293 GLY A N     1 
ATOM   2226 C  CA    . GLY A 1 299 ? 2.869   -2.098  4.402   1.00 23.87 ? 293 GLY A CA    1 
ATOM   2227 C  C     . GLY A 1 299 ? 3.137   -3.594  4.422   1.00 23.36 ? 293 GLY A C     1 
ATOM   2228 O  O     . GLY A 1 299 ? 3.355   -4.166  3.346   1.00 22.36 ? 293 GLY A O     1 
ATOM   2229 N  N     . ILE A 1 300 ? 3.199   -4.202  5.620   1.00 25.23 ? 294 ILE A N     1 
ATOM   2230 C  CA    . ILE A 1 300 ? 3.335   -5.674  5.814   1.00 26.55 ? 294 ILE A CA    1 
ATOM   2231 C  C     . ILE A 1 300 ? 1.968   -6.212  6.198   1.00 24.94 ? 294 ILE A C     1 
ATOM   2232 O  O     . ILE A 1 300 ? 1.408   -5.765  7.216   1.00 26.72 ? 294 ILE A O     1 
ATOM   2233 C  CB    . ILE A 1 300 ? 4.383   -6.069  6.871   1.00 27.84 ? 294 ILE A CB    1 
ATOM   2234 C  CG1   . ILE A 1 300 ? 5.746   -5.430  6.622   1.00 28.74 ? 294 ILE A CG1   1 
ATOM   2235 C  CG2   . ILE A 1 300 ? 4.470   -7.591  6.951   1.00 30.34 ? 294 ILE A CG2   1 
ATOM   2236 C  CD1   . ILE A 1 300 ? 6.434   -5.908  5.369   1.00 29.88 ? 294 ILE A CD1   1 
ATOM   2237 N  N     . TYR A 1 301 ? 1.420   -7.081  5.357   1.00 24.30 ? 295 TYR A N     1 
ATOM   2238 C  CA    . TYR A 1 301 ? 0.079   -7.650  5.572   1.00 24.03 ? 295 TYR A CA    1 
ATOM   2239 C  C     . TYR A 1 301 ? 0.010   -9.038  4.955   1.00 25.77 ? 295 TYR A C     1 
ATOM   2240 O  O     . TYR A 1 301 ? 1.011   -9.473  4.378   1.00 24.55 ? 295 TYR A O     1 
ATOM   2241 C  CB    . TYR A 1 301 ? -0.975  -6.705  5.016   1.00 23.54 ? 295 TYR A CB    1 
ATOM   2242 C  CG    . TYR A 1 301 ? -0.990  -6.433  3.530   1.00 21.19 ? 295 TYR A CG    1 
ATOM   2243 C  CD1   . TYR A 1 301 ? -0.165  -5.468  2.959   1.00 21.13 ? 295 TYR A CD1   1 
ATOM   2244 C  CD2   . TYR A 1 301 ? -1.924  -7.035  2.713   1.00 19.56 ? 295 TYR A CD2   1 
ATOM   2245 C  CE1   . TYR A 1 301 ? -0.240  -5.163  1.608   1.00 21.55 ? 295 TYR A CE1   1 
ATOM   2246 C  CE2   . TYR A 1 301 ? -2.042  -6.716  1.374   1.00 23.12 ? 295 TYR A CE2   1 
ATOM   2247 C  CZ    . TYR A 1 301 ? -1.196  -5.777  0.811   1.00 21.48 ? 295 TYR A CZ    1 
ATOM   2248 O  OH    . TYR A 1 301 ? -1.377  -5.467  -0.513  1.00 22.16 ? 295 TYR A OH    1 
ATOM   2249 N  N     . ASP A 1 302 ? -1.156  -9.669  5.089   1.00 27.35 ? 296 ASP A N     1 
ATOM   2250 C  CA    . ASP A 1 302 ? -1.490  -10.981 4.466   1.00 31.02 ? 296 ASP A CA    1 
ATOM   2251 C  C     . ASP A 1 302 ? -1.720  -10.759 2.958   1.00 24.94 ? 296 ASP A C     1 
ATOM   2252 O  O     . ASP A 1 302 ? -2.866  -10.567 2.528   1.00 28.70 ? 296 ASP A O     1 
ATOM   2253 C  CB    . ASP A 1 302 ? -2.674  -11.643 5.191   1.00 37.91 ? 296 ASP A CB    1 
ATOM   2254 C  CG    . ASP A 1 302 ? -2.371  -12.080 6.631   1.00 49.71 ? 296 ASP A CG    1 
ATOM   2255 O  OD1   . ASP A 1 302 ? -1.164  -12.286 6.957   1.00 52.16 ? 296 ASP A OD1   1 
ATOM   2256 O  OD2   . ASP A 1 302 ? -3.349  -12.212 7.437   1.00 60.10 ? 296 ASP A OD2   1 
ATOM   2257 N  N     . TRP A 1 303 ? -0.635  -10.762 2.202   1.00 25.90 ? 297 TRP A N     1 
ATOM   2258 C  CA    . TRP A 1 303 ? -0.592  -10.268 0.804   1.00 26.49 ? 297 TRP A CA    1 
ATOM   2259 C  C     . TRP A 1 303 ? -0.618  -11.414 -0.211  1.00 28.64 ? 297 TRP A C     1 
ATOM   2260 O  O     . TRP A 1 303 ? -0.352  -11.167 -1.395  1.00 25.02 ? 297 TRP A O     1 
ATOM   2261 C  CB    . TRP A 1 303 ? 0.607   -9.354  0.622   1.00 24.18 ? 297 TRP A CB    1 
ATOM   2262 C  CG    . TRP A 1 303 ? 1.941   -9.839  1.084   1.00 23.77 ? 297 TRP A CG    1 
ATOM   2263 C  CD1   . TRP A 1 303 ? 2.426   -11.113 1.082   1.00 23.76 ? 297 TRP A CD1   1 
ATOM   2264 C  CD2   . TRP A 1 303 ? 3.012   -8.996  1.550   1.00 23.11 ? 297 TRP A CD2   1 
ATOM   2265 N  NE1   . TRP A 1 303 ? 3.726   -11.113 1.507   1.00 23.80 ? 297 TRP A NE1   1 
ATOM   2266 C  CE2   . TRP A 1 303 ? 4.108   -9.836  1.825   1.00 23.73 ? 297 TRP A CE2   1 
ATOM   2267 C  CE3   . TRP A 1 303 ? 3.160   -7.621  1.764   1.00 24.47 ? 297 TRP A CE3   1 
ATOM   2268 C  CZ2   . TRP A 1 303 ? 5.324   -9.354  2.301   1.00 24.10 ? 297 TRP A CZ2   1 
ATOM   2269 C  CZ3   . TRP A 1 303 ? 4.365   -7.139  2.233   1.00 22.84 ? 297 TRP A CZ3   1 
ATOM   2270 C  CH2   . TRP A 1 303 ? 5.437   -8.001  2.489   1.00 25.22 ? 297 TRP A CH2   1 
ATOM   2271 N  N     . ASN A 1 304 ? -1.014  -12.611 0.213   1.00 30.12 ? 298 ASN A N     1 
ATOM   2272 C  CA    . ASN A 1 304 ? -1.352  -13.705 -0.738  1.00 33.93 ? 298 ASN A CA    1 
ATOM   2273 C  C     . ASN A 1 304 ? -2.437  -14.598 -0.135  1.00 39.61 ? 298 ASN A C     1 
ATOM   2274 O  O     . ASN A 1 304 ? -2.835  -14.351 1.025   1.00 37.37 ? 298 ASN A O     1 
ATOM   2275 C  CB    . ASN A 1 304 ? -0.084  -14.441 -1.162  1.00 34.42 ? 298 ASN A CB    1 
ATOM   2276 C  CG    . ASN A 1 304 ? 0.691   -14.991 0.012   1.00 34.80 ? 298 ASN A CG    1 
ATOM   2277 O  OD1   . ASN A 1 304 ? 0.086   -15.419 0.988   1.00 43.26 ? 298 ASN A OD1   1 
ATOM   2278 N  ND2   . ASN A 1 304 ? 2.014   -14.956 -0.052  1.00 32.29 ? 298 ASN A ND2   1 
ATOM   2279 N  N     . LYS A 1 305 ? -2.892  -15.606 -0.882  1.00 46.40 ? 299 LYS A N     1 
ATOM   2280 C  CA    . LYS A 1 305 ? -4.087  -16.416 -0.513  1.00 55.31 ? 299 LYS A CA    1 
ATOM   2281 C  C     . LYS A 1 305 ? -3.783  -17.375 0.653   1.00 64.07 ? 299 LYS A C     1 
ATOM   2282 O  O     . LYS A 1 305 ? -4.704  -17.625 1.440   1.00 73.77 ? 299 LYS A O     1 
ATOM   2283 C  CB    . LYS A 1 305 ? -4.646  -17.166 -1.722  1.00 57.62 ? 299 LYS A CB    1 
ATOM   2284 C  CG    . LYS A 1 305 ? -6.165  -17.127 -1.810  1.00 68.18 ? 299 LYS A CG    1 
ATOM   2285 C  CD    . LYS A 1 305 ? -6.709  -15.830 -2.392  1.00 71.71 ? 299 LYS A CD    1 
ATOM   2286 C  CE    . LYS A 1 305 ? -8.166  -15.580 -2.059  1.00 73.09 ? 299 LYS A CE    1 
ATOM   2287 N  NZ    . LYS A 1 305 ? -8.863  -14.908 -3.182  1.00 75.98 ? 299 LYS A NZ    1 
ATOM   2288 N  N     . SER A 1 306 ? -2.563  -17.898 0.786   1.00 69.29 ? 300 SER A N     1 
ATOM   2289 C  CA    . SER A 1 306 ? -2.207  -18.851 1.872   1.00 78.45 ? 300 SER A CA    1 
ATOM   2290 C  C     . SER A 1 306 ? -2.037  -18.102 3.209   1.00 89.11 ? 300 SER A C     1 
ATOM   2291 O  O     . SER A 1 306 ? -2.121  -18.767 4.265   1.00 95.49 ? 300 SER A O     1 
ATOM   2292 C  CB    . SER A 1 306 ? -0.991  -19.674 1.514   1.00 78.78 ? 300 SER A CB    1 
ATOM   2293 O  OG    . SER A 1 306 ? 0.192   -18.892 1.566   1.00 74.14 ? 300 SER A OG    1 
ATOM   2294 N  N     . SER A 1 307 ? -1.825  -16.778 3.178   1.00 85.56 ? 301 SER A N     1 
ATOM   2295 C  CA    . SER A 1 307 ? -1.687  -15.912 4.382   1.00 86.41 ? 301 SER A CA    1 
ATOM   2296 C  C     . SER A 1 307 ? -2.963  -16.007 5.227   1.00 84.21 ? 301 SER A C     1 
ATOM   2297 O  O     . SER A 1 307 ? -2.954  -16.659 6.267   1.00 88.60 ? 301 SER A O     1 
ATOM   2298 C  CB    . SER A 1 307 ? -1.388  -14.467 4.019   1.00 85.78 ? 301 SER A CB    1 
ATOM   2299 O  OG    . SER A 1 307 ? -0.128  -14.320 3.372   1.00 76.49 ? 301 SER A OG    1 
ATOM   2300 N  N     . GLY B 1 24  ? -62.999 31.694  13.288  1.00 46.74 ? 18  GLY B N     1 
ATOM   2301 C  CA    . GLY B 1 24  ? -62.305 31.211  12.047  1.00 41.01 ? 18  GLY B CA    1 
ATOM   2302 C  C     . GLY B 1 24  ? -60.792 31.287  12.191  1.00 37.89 ? 18  GLY B C     1 
ATOM   2303 O  O     . GLY B 1 24  ? -60.321 32.264  12.763  1.00 33.68 ? 18  GLY B O     1 
ATOM   2304 N  N     . GLN B 1 25  ? -60.052 30.284  11.692  1.00 35.59 ? 19  GLN B N     1 
ATOM   2305 C  CA    . GLN B 1 25  ? -58.571 30.196  11.822  1.00 33.00 ? 19  GLN B CA    1 
ATOM   2306 C  C     . GLN B 1 25  ? -57.945 31.255  10.904  1.00 33.98 ? 19  GLN B C     1 
ATOM   2307 O  O     . GLN B 1 25  ? -58.534 31.537  9.824   1.00 33.97 ? 19  GLN B O     1 
ATOM   2308 C  CB    . GLN B 1 25  ? -58.117 28.767  11.502  1.00 32.36 ? 19  GLN B CB    1 
ATOM   2309 C  CG    . GLN B 1 25  ? -58.619 27.754  12.519  1.00 32.29 ? 19  GLN B CG    1 
ATOM   2310 C  CD    . GLN B 1 25  ? -58.190 26.336  12.239  1.00 35.14 ? 19  GLN B CD    1 
ATOM   2311 O  OE1   . GLN B 1 25  ? -58.793 25.623  11.428  1.00 36.16 ? 19  GLN B OE1   1 
ATOM   2312 N  NE2   . GLN B 1 25  ? -57.209 25.867  13.001  1.00 26.97 ? 19  GLN B NE2   1 
ATOM   2313 N  N     . VAL B 1 26  ? -56.841 31.872  11.338  1.00 28.51 ? 20  VAL B N     1 
ATOM   2314 C  CA    . VAL B 1 26  ? -56.080 32.881  10.552  1.00 25.89 ? 20  VAL B CA    1 
ATOM   2315 C  C     . VAL B 1 26  ? -55.007 32.141  9.743   1.00 27.40 ? 20  VAL B C     1 
ATOM   2316 O  O     . VAL B 1 26  ? -54.102 31.552  10.328  1.00 26.28 ? 20  VAL B O     1 
ATOM   2317 C  CB    . VAL B 1 26  ? -55.460 33.948  11.469  1.00 29.41 ? 20  VAL B CB    1 
ATOM   2318 C  CG1   . VAL B 1 26  ? -54.620 34.930  10.688  1.00 28.00 ? 20  VAL B CG1   1 
ATOM   2319 C  CG2   . VAL B 1 26  ? -56.529 34.683  12.284  1.00 31.14 ? 20  VAL B CG2   1 
ATOM   2320 N  N     . PRO B 1 27  ? -55.051 32.199  8.393   1.00 26.12 ? 21  PRO B N     1 
ATOM   2321 C  CA    . PRO B 1 27  ? -54.168 31.386  7.547   1.00 25.63 ? 21  PRO B CA    1 
ATOM   2322 C  C     . PRO B 1 27  ? -52.787 32.030  7.408   1.00 24.41 ? 21  PRO B C     1 
ATOM   2323 O  O     . PRO B 1 27  ? -52.470 32.591  6.357   1.00 25.76 ? 21  PRO B O     1 
ATOM   2324 C  CB    . PRO B 1 27  ? -54.948 31.329  6.221   1.00 26.54 ? 21  PRO B CB    1 
ATOM   2325 C  CG    . PRO B 1 27  ? -55.660 32.679  6.156   1.00 27.58 ? 21  PRO B CG    1 
ATOM   2326 C  CD    . PRO B 1 27  ? -56.026 32.977  7.592   1.00 26.30 ? 21  PRO B CD    1 
ATOM   2327 N  N     . VAL B 1 28  ? -51.983 31.970  8.481   1.00 22.96 ? 22  VAL B N     1 
ATOM   2328 C  CA    . VAL B 1 28  ? -50.756 32.804  8.574   1.00 22.35 ? 22  VAL B CA    1 
ATOM   2329 C  C     . VAL B 1 28  ? -49.709 32.332  7.547   1.00 20.39 ? 22  VAL B C     1 
ATOM   2330 O  O     . VAL B 1 28  ? -48.916 33.177  7.107   1.00 21.59 ? 22  VAL B O     1 
ATOM   2331 C  CB    . VAL B 1 28  ? -50.162 32.802  10.001  1.00 24.66 ? 22  VAL B CB    1 
ATOM   2332 C  CG1   . VAL B 1 28  ? -49.682 31.429  10.428  1.00 25.98 ? 22  VAL B CG1   1 
ATOM   2333 C  CG2   . VAL B 1 28  ? -49.052 33.805  10.140  1.00 27.28 ? 22  VAL B CG2   1 
ATOM   2334 N  N     . SER B 1 29  ? -49.655 31.035  7.241   1.00 22.29 ? 23  SER B N     1 
ATOM   2335 C  CA    . SER B 1 29  ? -48.590 30.445  6.387   1.00 22.24 ? 23  SER B CA    1 
ATOM   2336 C  C     . SER B 1 29  ? -49.244 29.419  5.470   1.00 19.90 ? 23  SER B C     1 
ATOM   2337 O  O     . SER B 1 29  ? -49.777 28.432  5.983   1.00 20.92 ? 23  SER B O     1 
ATOM   2338 C  CB    . SER B 1 29  ? -47.491 29.831  7.251   1.00 23.21 ? 23  SER B CB    1 
ATOM   2339 O  OG    . SER B 1 29  ? -46.411 29.399  6.452   1.00 21.77 ? 23  SER B OG    1 
ATOM   2340 N  N     . VAL B 1 30  ? -49.245 29.687  4.164   1.00 20.66 ? 24  VAL B N     1 
ATOM   2341 C  CA    . VAL B 1 30  ? -50.030 28.895  3.179   1.00 20.18 ? 24  VAL B CA    1 
ATOM   2342 C  C     . VAL B 1 30  ? -49.108 28.338  2.088   1.00 18.04 ? 24  VAL B C     1 
ATOM   2343 O  O     . VAL B 1 30  ? -48.261 29.085  1.576   1.00 20.79 ? 24  VAL B O     1 
ATOM   2344 C  CB    . VAL B 1 30  ? -51.117 29.808  2.588   1.00 20.40 ? 24  VAL B CB    1 
ATOM   2345 C  CG1   . VAL B 1 30  ? -51.960 29.094  1.527   1.00 21.40 ? 24  VAL B CG1   1 
ATOM   2346 C  CG2   . VAL B 1 30  ? -51.977 30.368  3.713   1.00 21.08 ? 24  VAL B CG2   1 
ATOM   2347 N  N     . ASN B 1 31  ? -49.383 27.096  1.698   1.00 20.30 ? 25  ASN B N     1 
ATOM   2348 C  CA    . ASN B 1 31  ? -48.774 26.387  0.555   1.00 20.34 ? 25  ASN B CA    1 
ATOM   2349 C  C     . ASN B 1 31  ? -49.736 26.450  -0.626  1.00 20.97 ? 25  ASN B C     1 
ATOM   2350 O  O     . ASN B 1 31  ? -50.852 25.940  -0.499  1.00 21.72 ? 25  ASN B O     1 
ATOM   2351 C  CB    . ASN B 1 31  ? -48.433 24.945  0.911   1.00 21.37 ? 25  ASN B CB    1 
ATOM   2352 C  CG    . ASN B 1 31  ? -47.113 24.883  1.645   1.00 22.32 ? 25  ASN B CG    1 
ATOM   2353 O  OD1   . ASN B 1 31  ? -46.082 24.597  1.033   1.00 23.88 ? 25  ASN B OD1   1 
ATOM   2354 N  ND2   . ASN B 1 31  ? -47.132 25.223  2.922   1.00 20.68 ? 25  ASN B ND2   1 
ATOM   2355 N  N     . TYR B 1 32  ? -49.310 27.109  -1.691  1.00 20.74 ? 26  TYR B N     1 
ATOM   2356 C  CA    . TYR B 1 32  ? -50.064 27.154  -2.963  1.00 19.30 ? 26  TYR B CA    1 
ATOM   2357 C  C     . TYR B 1 32  ? -49.390 26.187  -3.929  1.00 18.28 ? 26  TYR B C     1 
ATOM   2358 O  O     . TYR B 1 32  ? -48.374 26.500  -4.544  1.00 18.18 ? 26  TYR B O     1 
ATOM   2359 C  CB    . TYR B 1 32  ? -50.154 28.582  -3.464  1.00 19.02 ? 26  TYR B CB    1 
ATOM   2360 C  CG    . TYR B 1 32  ? -50.902 28.817  -4.740  1.00 18.20 ? 26  TYR B CG    1 
ATOM   2361 C  CD1   . TYR B 1 32  ? -51.877 27.960  -5.218  1.00 18.49 ? 26  TYR B CD1   1 
ATOM   2362 C  CD2   . TYR B 1 32  ? -50.637 29.957  -5.470  1.00 19.87 ? 26  TYR B CD2   1 
ATOM   2363 C  CE1   . TYR B 1 32  ? -52.569 28.238  -6.394  1.00 19.40 ? 26  TYR B CE1   1 
ATOM   2364 C  CE2   . TYR B 1 32  ? -51.279 30.222  -6.662  1.00 20.09 ? 26  TYR B CE2   1 
ATOM   2365 C  CZ    . TYR B 1 32  ? -52.264 29.370  -7.126  1.00 18.92 ? 26  TYR B CZ    1 
ATOM   2366 O  OH    . TYR B 1 32  ? -52.886 29.616  -8.319  1.00 20.99 ? 26  TYR B OH    1 
ATOM   2367 N  N     . HIS B 1 33  ? -49.976 25.008  -4.058  1.00 20.26 ? 27  HIS B N     1 
ATOM   2368 C  CA    . HIS B 1 33  ? -49.578 24.015  -5.077  1.00 20.19 ? 27  HIS B CA    1 
ATOM   2369 C  C     . HIS B 1 33  ? -50.277 24.411  -6.381  1.00 21.77 ? 27  HIS B C     1 
ATOM   2370 O  O     . HIS B 1 33  ? -51.371 23.918  -6.679  1.00 22.32 ? 27  HIS B O     1 
ATOM   2371 C  CB    . HIS B 1 33  ? -49.896 22.594  -4.599  1.00 21.24 ? 27  HIS B CB    1 
ATOM   2372 C  CG    . HIS B 1 33  ? -49.222 22.201  -3.332  1.00 23.32 ? 27  HIS B CG    1 
ATOM   2373 N  ND1   . HIS B 1 33  ? -48.368 21.114  -3.257  1.00 28.34 ? 27  HIS B ND1   1 
ATOM   2374 C  CD2   . HIS B 1 33  ? -49.257 22.737  -2.088  1.00 23.66 ? 27  HIS B CD2   1 
ATOM   2375 C  CE1   . HIS B 1 33  ? -47.921 21.001  -2.015  1.00 28.77 ? 27  HIS B CE1   1 
ATOM   2376 N  NE2   . HIS B 1 33  ? -48.464 21.974  -1.275  1.00 23.31 ? 27  HIS B NE2   1 
ATOM   2377 N  N     . PHE B 1 34  ? -49.728 25.401  -7.071  1.00 20.69 ? 28  PHE B N     1 
ATOM   2378 C  CA    . PHE B 1 34  ? -50.418 26.090  -8.175  1.00 20.84 ? 28  PHE B CA    1 
ATOM   2379 C  C     . PHE B 1 34  ? -50.515 25.241  -9.460  1.00 22.04 ? 28  PHE B C     1 
ATOM   2380 O  O     . PHE B 1 34  ? -51.311 25.579  -10.349 1.00 21.75 ? 28  PHE B O     1 
ATOM   2381 C  CB    . PHE B 1 34  ? -49.766 27.447  -8.421  1.00 21.46 ? 28  PHE B CB    1 
ATOM   2382 C  CG    . PHE B 1 34  ? -48.372 27.408  -8.981  1.00 21.79 ? 28  PHE B CG    1 
ATOM   2383 C  CD1   . PHE B 1 34  ? -48.180 27.366  -10.342 1.00 20.05 ? 28  PHE B CD1   1 
ATOM   2384 C  CD2   . PHE B 1 34  ? -47.258 27.537  -8.158  1.00 21.71 ? 28  PHE B CD2   1 
ATOM   2385 C  CE1   . PHE B 1 34  ? -46.906 27.370  -10.884 1.00 21.64 ? 28  PHE B CE1   1 
ATOM   2386 C  CE2   . PHE B 1 34  ? -45.982 27.521  -8.696  1.00 21.09 ? 28  PHE B CE2   1 
ATOM   2387 C  CZ    . PHE B 1 34  ? -45.812 27.476  -10.067 1.00 22.09 ? 28  PHE B CZ    1 
ATOM   2388 N  N     A SER B 1 35  ? -49.740 24.162  -9.548  0.69 19.84 ? 29  SER B N     1 
ATOM   2389 N  N     B SER B 1 35  ? -49.706 24.189  -9.559  0.31 21.09 ? 29  SER B N     1 
ATOM   2390 C  CA    A SER B 1 35  ? -49.588 23.303  -10.752 0.69 21.06 ? 29  SER B CA    1 
ATOM   2391 C  CA    B SER B 1 35  ? -49.617 23.286  -10.733 0.31 21.72 ? 29  SER B CA    1 
ATOM   2392 C  C     A SER B 1 35  ? -49.150 21.907  -10.300 0.69 21.88 ? 29  SER B C     1 
ATOM   2393 C  C     B SER B 1 35  ? -49.249 21.889  -10.240 0.31 22.12 ? 29  SER B C     1 
ATOM   2394 O  O     A SER B 1 35  ? -48.536 21.812  -9.218  0.69 20.41 ? 29  SER B O     1 
ATOM   2395 O  O     B SER B 1 35  ? -48.734 21.785  -9.102  0.31 20.83 ? 29  SER B O     1 
ATOM   2396 C  CB    A SER B 1 35  ? -48.614 23.918  -11.750 0.69 21.64 ? 29  SER B CB    1 
ATOM   2397 C  CB    B SER B 1 35  ? -48.615 23.796  -11.734 0.31 22.14 ? 29  SER B CB    1 
ATOM   2398 O  OG    A SER B 1 35  ? -47.255 23.832  -11.324 0.69 20.46 ? 29  SER B OG    1 
ATOM   2399 O  OG    B SER B 1 35  ? -48.322 22.803  -12.705 0.31 21.82 ? 29  SER B OG    1 
ATOM   2400 N  N     . ARG B 1 36  ? -49.559 20.860  -11.036 1.00 22.49 ? 30  ARG B N     1 
ATOM   2401 C  CA    . ARG B 1 36  ? -49.276 19.464  -10.668 1.00 21.68 ? 30  ARG B CA    1 
ATOM   2402 C  C     . ARG B 1 36  ? -48.258 18.834  -11.620 1.00 22.85 ? 30  ARG B C     1 
ATOM   2403 O  O     . ARG B 1 36  ? -47.851 17.708  -11.322 1.00 22.07 ? 30  ARG B O     1 
ATOM   2404 C  CB    . ARG B 1 36  ? -50.561 18.668  -10.584 1.00 21.87 ? 30  ARG B CB    1 
ATOM   2405 C  CG    . ARG B 1 36  ? -51.365 18.982  -9.335  1.00 22.80 ? 30  ARG B CG    1 
ATOM   2406 C  CD    . ARG B 1 36  ? -52.610 18.138  -9.291  1.00 24.17 ? 30  ARG B CD    1 
ATOM   2407 N  NE    . ARG B 1 36  ? -53.328 18.244  -8.041  1.00 24.79 ? 30  ARG B NE    1 
ATOM   2408 C  CZ    . ARG B 1 36  ? -53.249 17.406  -7.025  1.00 22.67 ? 30  ARG B CZ    1 
ATOM   2409 N  NH1   . ARG B 1 36  ? -52.439 16.349  -7.049  1.00 24.41 ? 30  ARG B NH1   1 
ATOM   2410 N  NH2   . ARG B 1 36  ? -53.960 17.668  -5.948  1.00 26.12 ? 30  ARG B NH2   1 
ATOM   2411 N  N     . LYS B 1 37  ? -47.842 19.529  -12.670 1.00 23.61 ? 31  LYS B N     1 
ATOM   2412 C  CA    . LYS B 1 37  ? -46.869 18.980  -13.639 1.00 22.97 ? 31  LYS B CA    1 
ATOM   2413 C  C     . LYS B 1 37  ? -45.529 18.822  -12.915 1.00 22.43 ? 31  LYS B C     1 
ATOM   2414 O  O     . LYS B 1 37  ? -45.186 19.700  -12.068 1.00 20.58 ? 31  LYS B O     1 
ATOM   2415 C  CB    . LYS B 1 37  ? -46.733 19.932  -14.836 1.00 24.56 ? 31  LYS B CB    1 
ATOM   2416 C  CG    . LYS B 1 37  ? -46.104 19.351  -16.093 1.00 34.85 ? 31  LYS B CG    1 
ATOM   2417 C  CD    . LYS B 1 37  ? -46.103 20.352  -17.270 1.00 40.75 ? 31  LYS B CD    1 
ATOM   2418 C  CE    . LYS B 1 37  ? -45.735 19.726  -18.599 1.00 51.17 ? 31  LYS B CE    1 
ATOM   2419 N  NZ    . LYS B 1 37  ? -44.339 19.215  -18.616 1.00 58.83 ? 31  LYS B NZ    1 
ATOM   2420 N  N     . CYS B 1 38  ? -44.740 17.824  -13.299 1.00 19.04 ? 32  CYS B N     1 
ATOM   2421 C  CA    . CYS B 1 38  ? -43.370 17.677  -12.754 1.00 18.76 ? 32  CYS B CA    1 
ATOM   2422 C  C     . CYS B 1 38  ? -42.472 16.936  -13.756 1.00 21.08 ? 32  CYS B C     1 
ATOM   2423 O  O     . CYS B 1 38  ? -42.994 16.129  -14.525 1.00 22.64 ? 32  CYS B O     1 
ATOM   2424 C  CB    . CYS B 1 38  ? -43.410 16.926  -11.427 1.00 19.76 ? 32  CYS B CB    1 
ATOM   2425 S  SG    . CYS B 1 38  ? -41.767 16.886  -10.674 1.00 21.62 ? 32  CYS B SG    1 
ATOM   2426 N  N     . ASN B 1 39  ? -41.181 17.217  -13.714 1.00 21.24 ? 33  ASN B N     1 
ATOM   2427 C  CA    . ASN B 1 39  ? -40.173 16.628  -14.628 1.00 23.18 ? 33  ASN B CA    1 
ATOM   2428 C  C     . ASN B 1 39  ? -39.505 15.417  -13.971 1.00 24.17 ? 33  ASN B C     1 
ATOM   2429 O  O     . ASN B 1 39  ? -38.735 14.740  -14.647 1.00 25.07 ? 33  ASN B O     1 
ATOM   2430 C  CB    . ASN B 1 39  ? -39.179 17.699  -15.057 1.00 24.03 ? 33  ASN B CB    1 
ATOM   2431 C  CG    . ASN B 1 39  ? -38.432 18.329  -13.907 1.00 26.30 ? 33  ASN B CG    1 
ATOM   2432 O  OD1   . ASN B 1 39  ? -39.016 18.632  -12.872 1.00 25.05 ? 33  ASN B OD1   1 
ATOM   2433 N  ND2   . ASN B 1 39  ? -37.133 18.510  -14.079 1.00 30.67 ? 33  ASN B ND2   1 
ATOM   2434 N  N     . LYS B 1 40  ? -39.828 15.105  -12.718 1.00 22.80 ? 34  LYS B N     1 
ATOM   2435 C  CA    . LYS B 1 40  ? -39.175 13.999  -11.993 1.00 21.84 ? 34  LYS B CA    1 
ATOM   2436 C  C     . LYS B 1 40  ? -40.213 12.937  -11.672 1.00 22.50 ? 34  LYS B C     1 
ATOM   2437 O  O     . LYS B 1 40  ? -41.359 13.094  -12.116 1.00 23.45 ? 34  LYS B O     1 
ATOM   2438 C  CB    . LYS B 1 40  ? -38.407 14.533  -10.771 1.00 22.12 ? 34  LYS B CB    1 
ATOM   2439 C  CG    . LYS B 1 40  ? -37.148 15.317  -11.119 1.00 24.83 ? 34  LYS B CG    1 
ATOM   2440 C  CD    . LYS B 1 40  ? -36.297 15.611  -9.903  1.00 25.96 ? 34  LYS B CD    1 
ATOM   2441 C  CE    . LYS B 1 40  ? -35.086 16.460  -10.219 1.00 29.41 ? 34  LYS B CE    1 
ATOM   2442 N  NZ    . LYS B 1 40  ? -34.152 15.728  -11.118 1.00 29.21 ? 34  LYS B NZ    1 
ATOM   2443 N  N     . GLU B 1 41  ? -39.795 11.819  -11.074 1.00 20.04 ? 35  GLU B N     1 
ATOM   2444 C  CA    . GLU B 1 41  ? -40.656 10.618  -10.895 1.00 23.11 ? 35  GLU B CA    1 
ATOM   2445 C  C     . GLU B 1 41  ? -40.476 9.999   -9.514  1.00 20.75 ? 35  GLU B C     1 
ATOM   2446 O  O     . GLU B 1 41  ? -40.504 8.751   -9.392  1.00 20.70 ? 35  GLU B O     1 
ATOM   2447 C  CB    . GLU B 1 41  ? -40.356 9.587   -11.995 1.00 29.88 ? 35  GLU B CB    1 
ATOM   2448 C  CG    . GLU B 1 41  ? -40.807 10.033  -13.388 1.00 36.86 ? 35  GLU B CG    1 
ATOM   2449 C  CD    . GLU B 1 41  ? -40.481 9.063   -14.520 1.00 49.46 ? 35  GLU B CD    1 
ATOM   2450 O  OE1   . GLU B 1 41  ? -39.594 8.187   -14.319 1.00 51.97 ? 35  GLU B OE1   1 
ATOM   2451 O  OE2   . GLU B 1 41  ? -41.098 9.185   -15.607 1.00 60.09 ? 35  GLU B OE2   1 
ATOM   2452 N  N     . CYS B 1 42  ? -40.378 10.811  -8.462  1.00 21.73 ? 36  CYS B N     1 
ATOM   2453 C  CA    . CYS B 1 42  ? -40.131 10.320  -7.087  1.00 21.14 ? 36  CYS B CA    1 
ATOM   2454 C  C     . CYS B 1 42  ? -41.230 9.310   -6.722  1.00 21.73 ? 36  CYS B C     1 
ATOM   2455 O  O     . CYS B 1 42  ? -42.445 9.643   -6.843  1.00 22.17 ? 36  CYS B O     1 
ATOM   2456 C  CB    . CYS B 1 42  ? -40.077 11.457  -6.059  1.00 21.19 ? 36  CYS B CB    1 
ATOM   2457 S  SG    . CYS B 1 42  ? -39.079 12.872  -6.582  1.00 21.39 ? 36  CYS B SG    1 
ATOM   2458 N  N     . LEU B 1 43  ? -40.847 8.110   -6.300  1.00 21.22 ? 37  LEU B N     1 
ATOM   2459 C  CA    . LEU B 1 43  ? -41.775 6.974   -6.082  1.00 21.86 ? 37  LEU B CA    1 
ATOM   2460 C  C     . LEU B 1 43  ? -42.769 7.263   -4.957  1.00 20.58 ? 37  LEU B C     1 
ATOM   2461 O  O     . LEU B 1 43  ? -43.816 6.632   -4.929  1.00 21.22 ? 37  LEU B O     1 
ATOM   2462 C  CB    . LEU B 1 43  ? -40.968 5.706   -5.788  1.00 23.38 ? 37  LEU B CB    1 
ATOM   2463 C  CG    . LEU B 1 43  ? -40.261 5.091   -7.000  1.00 29.34 ? 37  LEU B CG    1 
ATOM   2464 C  CD1   . LEU B 1 43  ? -39.526 3.829   -6.567  1.00 28.64 ? 37  LEU B CD1   1 
ATOM   2465 C  CD2   . LEU B 1 43  ? -41.232 4.775   -8.126  1.00 31.66 ? 37  LEU B CD2   1 
ATOM   2466 N  N     . PHE B 1 44  ? -42.485 8.217   -4.075  1.00 20.81 ? 38  PHE B N     1 
ATOM   2467 C  CA    . PHE B 1 44  ? -43.321 8.478   -2.880  1.00 21.50 ? 38  PHE B CA    1 
ATOM   2468 C  C     . PHE B 1 44  ? -44.191 9.719   -3.068  1.00 19.30 ? 38  PHE B C     1 
ATOM   2469 O  O     . PHE B 1 44  ? -44.975 9.953   -2.154  1.00 20.33 ? 38  PHE B O     1 
ATOM   2470 C  CB    . PHE B 1 44  ? -42.469 8.617   -1.616  1.00 21.33 ? 38  PHE B CB    1 
ATOM   2471 C  CG    . PHE B 1 44  ? -41.348 9.600   -1.768  1.00 20.45 ? 38  PHE B CG    1 
ATOM   2472 C  CD1   . PHE B 1 44  ? -41.602 10.940  -2.015  1.00 21.19 ? 38  PHE B CD1   1 
ATOM   2473 C  CD2   . PHE B 1 44  ? -40.026 9.186   -1.676  1.00 24.07 ? 38  PHE B CD2   1 
ATOM   2474 C  CE1   . PHE B 1 44  ? -40.575 11.811  -2.276  1.00 21.36 ? 38  PHE B CE1   1 
ATOM   2475 C  CE2   . PHE B 1 44  ? -38.992 10.087  -1.883  1.00 22.27 ? 38  PHE B CE2   1 
ATOM   2476 C  CZ    . PHE B 1 44  ? -39.271 11.393  -2.173  1.00 21.63 ? 38  PHE B CZ    1 
ATOM   2477 N  N     . CYS B 1 45  ? -44.098 10.431  -4.192  1.00 18.17 ? 39  CYS B N     1 
ATOM   2478 C  CA    . CYS B 1 45  ? -44.659 11.782  -4.360  1.00 19.38 ? 39  CYS B CA    1 
ATOM   2479 C  C     . CYS B 1 45  ? -46.104 11.797  -3.851  1.00 20.34 ? 39  CYS B C     1 
ATOM   2480 O  O     . CYS B 1 45  ? -46.922 10.991  -4.365  1.00 19.63 ? 39  CYS B O     1 
ATOM   2481 C  CB    . CYS B 1 45  ? -44.651 12.182  -5.830  1.00 20.87 ? 39  CYS B CB    1 
ATOM   2482 S  SG    . CYS B 1 45  ? -45.239 13.866  -6.076  1.00 21.06 ? 39  CYS B SG    1 
ATOM   2483 N  N     . PHE B 1 46  ? -46.459 12.733  -2.972  1.00 20.52 ? 40  PHE B N     1 
ATOM   2484 C  CA    . PHE B 1 46  ? -47.844 12.807  -2.416  1.00 20.00 ? 40  PHE B CA    1 
ATOM   2485 C  C     . PHE B 1 46  ? -48.639 13.949  -3.053  1.00 19.66 ? 40  PHE B C     1 
ATOM   2486 O  O     . PHE B 1 46  ? -49.701 14.333  -2.520  1.00 21.25 ? 40  PHE B O     1 
ATOM   2487 C  CB    . PHE B 1 46  ? -47.853 12.893  -0.883  1.00 21.74 ? 40  PHE B CB    1 
ATOM   2488 C  CG    . PHE B 1 46  ? -47.165 14.052  -0.208  1.00 18.51 ? 40  PHE B CG    1 
ATOM   2489 C  CD1   . PHE B 1 46  ? -46.641 15.135  -0.896  1.00 19.10 ? 40  PHE B CD1   1 
ATOM   2490 C  CD2   . PHE B 1 46  ? -47.029 14.015  1.181   1.00 20.81 ? 40  PHE B CD2   1 
ATOM   2491 C  CE1   . PHE B 1 46  ? -46.012 16.173  -0.205  1.00 21.09 ? 40  PHE B CE1   1 
ATOM   2492 C  CE2   . PHE B 1 46  ? -46.405 15.054  1.858   1.00 20.50 ? 40  PHE B CE2   1 
ATOM   2493 C  CZ    . PHE B 1 46  ? -45.899 16.124  1.167   1.00 18.53 ? 40  PHE B CZ    1 
ATOM   2494 N  N     . HIS B 1 47  ? -48.147 14.532  -4.138  1.00 19.34 ? 41  HIS B N     1 
ATOM   2495 C  CA    . HIS B 1 47  ? -48.872 15.615  -4.831  1.00 20.92 ? 41  HIS B CA    1 
ATOM   2496 C  C     . HIS B 1 47  ? -48.631 15.482  -6.339  1.00 23.06 ? 41  HIS B C     1 
ATOM   2497 O  O     . HIS B 1 47  ? -47.838 16.257  -6.889  1.00 24.21 ? 41  HIS B O     1 
ATOM   2498 C  CB    . HIS B 1 47  ? -48.504 16.989  -4.254  1.00 19.46 ? 41  HIS B CB    1 
ATOM   2499 C  CG    . HIS B 1 47  ? -49.581 17.969  -4.501  1.00 21.21 ? 41  HIS B CG    1 
ATOM   2500 N  ND1   . HIS B 1 47  ? -50.647 18.080  -3.654  1.00 22.85 ? 41  HIS B ND1   1 
ATOM   2501 C  CD2   . HIS B 1 47  ? -49.815 18.786  -5.549  1.00 22.32 ? 41  HIS B CD2   1 
ATOM   2502 C  CE1   . HIS B 1 47  ? -51.516 18.955  -4.157  1.00 24.06 ? 41  HIS B CE1   1 
ATOM   2503 N  NE2   . HIS B 1 47  ? -51.012 19.423  -5.315  1.00 24.56 ? 41  HIS B NE2   1 
ATOM   2504 N  N     . THR B 1 48  ? -49.365 14.546  -6.948  1.00 21.87 ? 42  THR B N     1 
ATOM   2505 C  CA    . THR B 1 48  ? -49.082 13.878  -8.232  1.00 24.54 ? 42  THR B CA    1 
ATOM   2506 C  C     . THR B 1 48  ? -49.752 14.628  -9.405  1.00 24.17 ? 42  THR B C     1 
ATOM   2507 O  O     . THR B 1 48  ? -50.611 15.516  -9.172  1.00 23.99 ? 42  THR B O     1 
ATOM   2508 C  CB    . THR B 1 48  ? -49.541 12.408  -8.126  1.00 24.31 ? 42  THR B CB    1 
ATOM   2509 O  OG1   . THR B 1 48  ? -50.958 12.315  -7.912  1.00 22.42 ? 42  THR B OG1   1 
ATOM   2510 C  CG2   . THR B 1 48  ? -48.840 11.669  -7.004  1.00 25.68 ? 42  THR B CG2   1 
ATOM   2511 N  N     . ALA B 1 49  ? -49.360 14.269  -10.626 1.00 23.49 ? 43  ALA B N     1 
ATOM   2512 C  CA    . ALA B 1 49  ? -49.632 14.997  -11.883 1.00 25.27 ? 43  ALA B CA    1 
ATOM   2513 C  C     . ALA B 1 49  ? -51.012 14.601  -12.433 1.00 25.78 ? 43  ALA B C     1 
ATOM   2514 O  O     . ALA B 1 49  ? -51.049 14.097  -13.572 1.00 26.94 ? 43  ALA B O     1 
ATOM   2515 C  CB    . ALA B 1 49  ? -48.534 14.703  -12.890 1.00 27.64 ? 43  ALA B CB    1 
ATOM   2516 N  N     . THR B 1 50  ? -52.078 14.816  -11.660 1.00 26.98 ? 44  THR B N     1 
ATOM   2517 C  CA    . THR B 1 50  ? -53.471 14.375  -11.972 1.00 28.06 ? 44  THR B CA    1 
ATOM   2518 C  C     . THR B 1 50  ? -54.198 15.385  -12.874 1.00 30.99 ? 44  THR B C     1 
ATOM   2519 O  O     . THR B 1 50  ? -55.196 14.976  -13.495 1.00 32.79 ? 44  THR B O     1 
ATOM   2520 C  CB    . THR B 1 50  ? -54.303 14.174  -10.704 1.00 29.11 ? 44  THR B CB    1 
ATOM   2521 O  OG1   . THR B 1 50  ? -54.241 15.355  -9.895  1.00 27.76 ? 44  THR B OG1   1 
ATOM   2522 C  CG2   . THR B 1 50  ? -53.842 12.998  -9.884  1.00 29.58 ? 44  THR B CG2   1 
ATOM   2523 N  N     . THR B 1 51  ? -53.773 16.652  -12.936 1.00 27.89 ? 45  THR B N     1 
ATOM   2524 C  CA    . THR B 1 51  ? -54.376 17.698  -13.816 1.00 29.11 ? 45  THR B CA    1 
ATOM   2525 C  C     . THR B 1 51  ? -53.261 18.581  -14.367 1.00 30.44 ? 45  THR B C     1 
ATOM   2526 O  O     . THR B 1 51  ? -52.176 18.621  -13.771 1.00 30.37 ? 45  THR B O     1 
ATOM   2527 C  CB    . THR B 1 51  ? -55.401 18.571  -13.076 1.00 28.85 ? 45  THR B CB    1 
ATOM   2528 O  OG1   . THR B 1 51  ? -54.634 19.555  -12.371 1.00 33.61 ? 45  THR B OG1   1 
ATOM   2529 C  CG2   . THR B 1 51  ? -56.283 17.792  -12.124 1.00 29.09 ? 45  THR B CG2   1 
ATOM   2530 N  N     . SER B 1 52  ? -53.533 19.306  -15.447 1.00 27.89 ? 46  SER B N     1 
ATOM   2531 C  CA    . SER B 1 52  ? -52.604 20.320  -15.989 1.00 28.97 ? 46  SER B CA    1 
ATOM   2532 C  C     . SER B 1 52  ? -53.175 21.723  -15.734 1.00 26.10 ? 46  SER B C     1 
ATOM   2533 O  O     . SER B 1 52  ? -52.583 22.687  -16.222 1.00 26.86 ? 46  SER B O     1 
ATOM   2534 C  CB    . SER B 1 52  ? -52.346 20.055  -17.464 1.00 32.44 ? 46  SER B CB    1 
ATOM   2535 O  OG    . SER B 1 52  ? -53.589 20.071  -18.149 1.00 34.33 ? 46  SER B OG    1 
ATOM   2536 N  N     . HIS B 1 53  ? -54.263 21.839  -14.968 1.00 24.75 ? 47  HIS B N     1 
ATOM   2537 C  CA    . HIS B 1 53  ? -54.936 23.145  -14.756 1.00 24.59 ? 47  HIS B CA    1 
ATOM   2538 C  C     . HIS B 1 53  ? -53.995 24.060  -13.959 1.00 23.21 ? 47  HIS B C     1 
ATOM   2539 O  O     . HIS B 1 53  ? -53.444 23.602  -12.919 1.00 23.33 ? 47  HIS B O     1 
ATOM   2540 C  CB    . HIS B 1 53  ? -56.294 23.008  -14.074 1.00 24.45 ? 47  HIS B CB    1 
ATOM   2541 C  CG    . HIS B 1 53  ? -56.853 24.326  -13.657 1.00 27.73 ? 47  HIS B CG    1 
ATOM   2542 N  ND1   . HIS B 1 53  ? -57.604 25.118  -14.513 1.00 29.69 ? 47  HIS B ND1   1 
ATOM   2543 C  CD2   . HIS B 1 53  ? -56.693 25.034  -12.506 1.00 26.65 ? 47  HIS B CD2   1 
ATOM   2544 C  CE1   . HIS B 1 53  ? -57.909 26.257  -13.889 1.00 31.92 ? 47  HIS B CE1   1 
ATOM   2545 N  NE2   . HIS B 1 53  ? -57.382 26.213  -12.634 1.00 29.34 ? 47  HIS B NE2   1 
ATOM   2546 N  N     . VAL B 1 54  ? -53.862 25.318  -14.394 1.00 22.76 ? 48  VAL B N     1 
ATOM   2547 C  CA    . VAL B 1 54  ? -53.225 26.412  -13.601 1.00 23.00 ? 48  VAL B CA    1 
ATOM   2548 C  C     . VAL B 1 54  ? -54.127 27.627  -13.685 1.00 26.26 ? 48  VAL B C     1 
ATOM   2549 O  O     . VAL B 1 54  ? -54.723 27.844  -14.777 1.00 25.65 ? 48  VAL B O     1 
ATOM   2550 C  CB    . VAL B 1 54  ? -51.805 26.719  -14.083 1.00 23.71 ? 48  VAL B CB    1 
ATOM   2551 C  CG1   . VAL B 1 54  ? -51.140 27.780  -13.214 1.00 23.01 ? 48  VAL B CG1   1 
ATOM   2552 C  CG2   . VAL B 1 54  ? -50.970 25.447  -14.118 1.00 27.99 ? 48  VAL B CG2   1 
ATOM   2553 N  N     . GLU B 1 55  ? -54.307 28.343  -12.583 1.00 25.67 ? 49  GLU B N     1 
ATOM   2554 C  CA    . GLU B 1 55  ? -55.170 29.551  -12.574 1.00 25.29 ? 49  GLU B CA    1 
ATOM   2555 C  C     . GLU B 1 55  ? -54.557 30.558  -13.534 1.00 25.72 ? 49  GLU B C     1 
ATOM   2556 O  O     . GLU B 1 55  ? -53.326 30.575  -13.684 1.00 26.43 ? 49  GLU B O     1 
ATOM   2557 C  CB    . GLU B 1 55  ? -55.335 30.122  -11.163 1.00 27.11 ? 49  GLU B CB    1 
ATOM   2558 C  CG    . GLU B 1 55  ? -56.349 29.367  -10.312 1.00 27.61 ? 49  GLU B CG    1 
ATOM   2559 C  CD    . GLU B 1 55  ? -57.774 29.312  -10.861 1.00 31.74 ? 49  GLU B CD    1 
ATOM   2560 O  OE1   . GLU B 1 55  ? -58.327 30.389  -11.147 1.00 30.15 ? 49  GLU B OE1   1 
ATOM   2561 O  OE2   . GLU B 1 55  ? -58.335 28.189  -11.022 1.00 32.32 ? 49  GLU B OE2   1 
ATOM   2562 N  N     . LYS B 1 56  ? -55.384 31.350  -14.203 1.00 26.08 ? 50  LYS B N     1 
ATOM   2563 C  CA    . LYS B 1 56  ? -54.898 32.526  -14.956 1.00 30.52 ? 50  LYS B CA    1 
ATOM   2564 C  C     . LYS B 1 56  ? -54.255 33.486  -13.963 1.00 28.70 ? 50  LYS B C     1 
ATOM   2565 O  O     . LYS B 1 56  ? -54.785 33.672  -12.864 1.00 27.33 ? 50  LYS B O     1 
ATOM   2566 C  CB    . LYS B 1 56  ? -56.078 33.157  -15.691 1.00 34.31 ? 50  LYS B CB    1 
ATOM   2567 C  CG    . LYS B 1 56  ? -56.609 32.290  -16.823 1.00 39.07 ? 50  LYS B CG    1 
ATOM   2568 C  CD    . LYS B 1 56  ? -57.610 33.005  -17.696 1.00 46.49 ? 50  LYS B CD    1 
ATOM   2569 C  CE    . LYS B 1 56  ? -57.842 32.256  -18.990 1.00 52.36 ? 50  LYS B CE    1 
ATOM   2570 N  NZ    . LYS B 1 56  ? -58.705 31.083  -18.744 1.00 53.66 ? 50  LYS B NZ    1 
ATOM   2571 N  N     . PRO B 1 57  ? -53.144 34.169  -14.315 1.00 29.21 ? 51  PRO B N     1 
ATOM   2572 C  CA    . PRO B 1 57  ? -52.480 35.054  -13.357 1.00 30.76 ? 51  PRO B CA    1 
ATOM   2573 C  C     . PRO B 1 57  ? -53.421 36.052  -12.643 1.00 28.93 ? 51  PRO B C     1 
ATOM   2574 O  O     . PRO B 1 57  ? -53.242 36.282  -11.471 1.00 28.89 ? 51  PRO B O     1 
ATOM   2575 C  CB    . PRO B 1 57  ? -51.399 35.773  -14.183 1.00 30.29 ? 51  PRO B CB    1 
ATOM   2576 C  CG    . PRO B 1 57  ? -51.156 34.870  -15.376 1.00 31.90 ? 51  PRO B CG    1 
ATOM   2577 C  CD    . PRO B 1 57  ? -52.469 34.131  -15.621 1.00 30.46 ? 51  PRO B CD    1 
ATOM   2578 N  N     . GLU B 1 58  ? -54.401 36.629  -13.345 1.00 31.13 ? 52  GLU B N     1 
ATOM   2579 C  CA    . GLU B 1 58  ? -55.344 37.615  -12.756 1.00 32.68 ? 52  GLU B CA    1 
ATOM   2580 C  C     . GLU B 1 58  ? -56.147 36.955  -11.627 1.00 30.80 ? 52  GLU B C     1 
ATOM   2581 O  O     . GLU B 1 58  ? -56.427 37.614  -10.621 1.00 32.08 ? 52  GLU B O     1 
ATOM   2582 C  CB    . GLU B 1 58  ? -56.248 38.221  -13.836 1.00 37.48 ? 52  GLU B CB    1 
ATOM   2583 C  CG    . GLU B 1 58  ? -56.661 37.251  -14.951 1.00 49.22 ? 52  GLU B CG    1 
ATOM   2584 C  CD    . GLU B 1 58  ? -55.774 37.215  -16.209 1.00 55.18 ? 52  GLU B CD    1 
ATOM   2585 O  OE1   . GLU B 1 58  ? -54.717 36.516  -16.222 1.00 45.57 ? 52  GLU B OE1   1 
ATOM   2586 O  OE2   . GLU B 1 58  ? -56.144 37.894  -17.200 1.00 69.39 ? 52  GLU B OE2   1 
ATOM   2587 N  N     . ASN B 1 59  ? -56.530 35.695  -11.804 1.00 30.17 ? 53  ASN B N     1 
ATOM   2588 C  CA    . ASN B 1 59  ? -57.318 34.919  -10.817 1.00 27.66 ? 53  ASN B CA    1 
ATOM   2589 C  C     . ASN B 1 59  ? -56.406 34.554  -9.629  1.00 27.40 ? 53  ASN B C     1 
ATOM   2590 O  O     . ASN B 1 59  ? -56.825 34.783  -8.480  1.00 24.22 ? 53  ASN B O     1 
ATOM   2591 C  CB    . ASN B 1 59  ? -58.023 33.750  -11.500 1.00 30.85 ? 53  ASN B CB    1 
ATOM   2592 C  CG    . ASN B 1 59  ? -59.085 34.232  -12.473 1.00 33.65 ? 53  ASN B CG    1 
ATOM   2593 O  OD1   . ASN B 1 59  ? -59.564 35.362  -12.357 1.00 35.41 ? 53  ASN B OD1   1 
ATOM   2594 N  ND2   . ASN B 1 59  ? -59.433 33.406  -13.446 1.00 34.07 ? 53  ASN B ND2   1 
ATOM   2595 N  N     . ALA B 1 60  ? -55.170 34.111  -9.875  1.00 25.25 ? 54  ALA B N     1 
ATOM   2596 C  CA    . ALA B 1 60  ? -54.208 33.809  -8.794  1.00 24.54 ? 54  ALA B CA    1 
ATOM   2597 C  C     . ALA B 1 60  ? -53.959 35.065  -7.952  1.00 25.59 ? 54  ALA B C     1 
ATOM   2598 O  O     . ALA B 1 60  ? -54.026 34.970  -6.695  1.00 26.98 ? 54  ALA B O     1 
ATOM   2599 C  CB    . ALA B 1 60  ? -52.923 33.225  -9.334  1.00 24.61 ? 54  ALA B CB    1 
ATOM   2600 N  N     . LYS B 1 61  ? -53.748 36.212  -8.595  1.00 27.40 ? 55  LYS B N     1 
ATOM   2601 C  CA    . LYS B 1 61  ? -53.523 37.502  -7.890  1.00 29.19 ? 55  LYS B CA    1 
ATOM   2602 C  C     . LYS B 1 61  ? -54.722 37.867  -7.014  1.00 29.57 ? 55  LYS B C     1 
ATOM   2603 O  O     . LYS B 1 61  ? -54.504 38.332  -5.884  1.00 27.32 ? 55  LYS B O     1 
ATOM   2604 C  CB    . LYS B 1 61  ? -53.214 38.616  -8.886  1.00 31.02 ? 55  LYS B CB    1 
ATOM   2605 C  CG    . LYS B 1 61  ? -51.811 38.595  -9.461  1.00 31.86 ? 55  LYS B CG    1 
ATOM   2606 C  CD    . LYS B 1 61  ? -51.657 39.742  -10.431 1.00 34.26 ? 55  LYS B CD    1 
ATOM   2607 C  CE    . LYS B 1 61  ? -50.520 39.574  -11.400 1.00 39.33 ? 55  LYS B CE    1 
ATOM   2608 N  NZ    . LYS B 1 61  ? -50.470 40.759  -12.281 1.00 41.80 ? 55  LYS B NZ    1 
ATOM   2609 N  N     A ARG B 1 62  ? -55.964 37.686  -7.473  0.47 31.19 ? 56  ARG B N     1 
ATOM   2610 N  N     B ARG B 1 62  ? -55.937 37.688  -7.537  0.53 29.84 ? 56  ARG B N     1 
ATOM   2611 C  CA    A ARG B 1 62  ? -57.129 38.007  -6.604  0.47 31.97 ? 56  ARG B CA    1 
ATOM   2612 C  CA    B ARG B 1 62  ? -57.219 37.868  -6.803  0.53 29.45 ? 56  ARG B CA    1 
ATOM   2613 C  C     A ARG B 1 62  ? -57.133 37.044  -5.412  0.47 29.24 ? 56  ARG B C     1 
ATOM   2614 C  C     B ARG B 1 62  ? -57.153 37.048  -5.506  0.53 28.17 ? 56  ARG B C     1 
ATOM   2615 O  O     A ARG B 1 62  ? -57.398 37.510  -4.289  0.47 28.56 ? 56  ARG B O     1 
ATOM   2616 O  O     B ARG B 1 62  ? -57.346 37.625  -4.429  0.53 28.59 ? 56  ARG B O     1 
ATOM   2617 C  CB    A ARG B 1 62  ? -58.486 37.992  -7.317  0.47 35.70 ? 56  ARG B CB    1 
ATOM   2618 C  CB    B ARG B 1 62  ? -58.385 37.476  -7.723  0.53 30.39 ? 56  ARG B CB    1 
ATOM   2619 C  CG    A ARG B 1 62  ? -59.560 38.703  -6.497  0.47 40.79 ? 56  ARG B CG    1 
ATOM   2620 C  CG    B ARG B 1 62  ? -59.778 37.635  -7.128  0.53 33.24 ? 56  ARG B CG    1 
ATOM   2621 C  CD    A ARG B 1 62  ? -60.953 38.756  -7.102  0.47 44.97 ? 56  ARG B CD    1 
ATOM   2622 C  CD    B ARG B 1 62  ? -60.856 37.957  -8.168  0.53 33.52 ? 56  ARG B CD    1 
ATOM   2623 N  NE    A ARG B 1 62  ? -61.766 37.592  -6.769  0.47 47.62 ? 56  ARG B NE    1 
ATOM   2624 N  NE    B ARG B 1 62  ? -60.863 37.040  -9.306  0.53 35.25 ? 56  ARG B NE    1 
ATOM   2625 C  CZ    A ARG B 1 62  ? -62.315 36.780  -7.665  0.47 51.11 ? 56  ARG B CZ    1 
ATOM   2626 C  CZ    B ARG B 1 62  ? -61.493 35.860  -9.348  0.53 36.65 ? 56  ARG B CZ    1 
ATOM   2627 N  NH1   A ARG B 1 62  ? -62.145 37.015  -8.955  0.47 54.59 ? 56  ARG B NH1   1 
ATOM   2628 N  NH1   B ARG B 1 62  ? -62.203 35.418  -8.321  0.53 37.94 ? 56  ARG B NH1   1 
ATOM   2629 N  NH2   A ARG B 1 62  ? -63.047 35.751  -7.273  0.47 49.89 ? 56  ARG B NH2   1 
ATOM   2630 N  NH2   B ARG B 1 62  ? -61.414 35.118  -10.437 0.53 37.25 ? 56  ARG B NH2   1 
ATOM   2631 N  N     . GLY B 1 63  ? -56.835 35.758  -5.620  1.00 26.79 ? 57  GLY B N     1 
ATOM   2632 C  CA    . GLY B 1 63  ? -56.837 34.800  -4.502  1.00 23.76 ? 57  GLY B CA    1 
ATOM   2633 C  C     . GLY B 1 63  ? -55.770 35.148  -3.485  1.00 23.45 ? 57  GLY B C     1 
ATOM   2634 O  O     . GLY B 1 63  ? -56.042 35.044  -2.275  1.00 23.99 ? 57  GLY B O     1 
ATOM   2635 N  N     . LEU B 1 64  ? -54.582 35.512  -3.948  1.00 23.49 ? 58  LEU B N     1 
ATOM   2636 C  CA    . LEU B 1 64  ? -53.472 35.887  -3.045  1.00 25.50 ? 58  LEU B CA    1 
ATOM   2637 C  C     . LEU B 1 64  ? -53.857 37.152  -2.264  1.00 26.66 ? 58  LEU B C     1 
ATOM   2638 O  O     . LEU B 1 64  ? -53.577 37.176  -1.071  1.00 22.89 ? 58  LEU B O     1 
ATOM   2639 C  CB    . LEU B 1 64  ? -52.174 36.027  -3.843  1.00 26.09 ? 58  LEU B CB    1 
ATOM   2640 C  CG    . LEU B 1 64  ? -51.696 34.714  -4.474  1.00 26.82 ? 58  LEU B CG    1 
ATOM   2641 C  CD1   . LEU B 1 64  ? -50.570 34.951  -5.445  1.00 30.38 ? 58  LEU B CD1   1 
ATOM   2642 C  CD2   . LEU B 1 64  ? -51.244 33.747  -3.390  1.00 31.16 ? 58  LEU B CD2   1 
ATOM   2643 N  N     . THR B 1 65  ? -54.514 38.123  -2.916  1.00 26.83 ? 59  THR B N     1 
ATOM   2644 C  CA    . THR B 1 65  ? -55.062 39.356  -2.285  1.00 28.41 ? 59  THR B CA    1 
ATOM   2645 C  C     . THR B 1 65  ? -56.014 38.946  -1.154  1.00 25.90 ? 59  THR B C     1 
ATOM   2646 O  O     . THR B 1 65  ? -55.868 39.488  -0.049  1.00 27.53 ? 59  THR B O     1 
ATOM   2647 C  CB    . THR B 1 65  ? -55.685 40.301  -3.327  1.00 27.85 ? 59  THR B CB    1 
ATOM   2648 O  OG1   . THR B 1 65  ? -54.692 40.624  -4.299  1.00 28.24 ? 59  THR B OG1   1 
ATOM   2649 C  CG2   . THR B 1 65  ? -56.260 41.574  -2.739  1.00 29.34 ? 59  THR B CG2   1 
ATOM   2650 N  N     . LEU B 1 66  ? -56.956 38.037  -1.389  1.00 25.64 ? 60  LEU B N     1 
ATOM   2651 C  CA    . LEU B 1 66  ? -57.927 37.588  -0.360  1.00 25.41 ? 60  LEU B CA    1 
ATOM   2652 C  C     . LEU B 1 66  ? -57.194 36.903  0.811   1.00 27.44 ? 60  LEU B C     1 
ATOM   2653 O  O     . LEU B 1 66  ? -57.668 37.009  1.961   1.00 29.18 ? 60  LEU B O     1 
ATOM   2654 C  CB    . LEU B 1 66  ? -58.944 36.611  -0.963  1.00 27.34 ? 60  LEU B CB    1 
ATOM   2655 C  CG    . LEU B 1 66  ? -59.832 37.131  -2.094  1.00 28.59 ? 60  LEU B CG    1 
ATOM   2656 C  CD1   . LEU B 1 66  ? -60.773 36.034  -2.532  1.00 29.41 ? 60  LEU B CD1   1 
ATOM   2657 C  CD2   . LEU B 1 66  ? -60.607 38.381  -1.687  1.00 31.16 ? 60  LEU B CD2   1 
ATOM   2658 N  N     . LEU B 1 67  ? -56.089 36.200  0.556   1.00 24.55 ? 61  LEU B N     1 
ATOM   2659 C  CA    . LEU B 1 67  ? -55.347 35.522  1.631   1.00 24.67 ? 61  LEU B CA    1 
ATOM   2660 C  C     . LEU B 1 67  ? -54.637 36.551  2.515   1.00 24.13 ? 61  LEU B C     1 
ATOM   2661 O  O     . LEU B 1 67  ? -54.684 36.400  3.775   1.00 24.32 ? 61  LEU B O     1 
ATOM   2662 C  CB    . LEU B 1 67  ? -54.378 34.510  1.016   1.00 25.32 ? 61  LEU B CB    1 
ATOM   2663 C  CG    . LEU B 1 67  ? -55.012 33.228  0.487   1.00 24.92 ? 61  LEU B CG    1 
ATOM   2664 C  CD1   . LEU B 1 67  ? -54.003 32.472  -0.358  1.00 27.55 ? 61  LEU B CD1   1 
ATOM   2665 C  CD2   . LEU B 1 67  ? -55.543 32.315  1.586   1.00 26.35 ? 61  LEU B CD2   1 
ATOM   2666 N  N     . LYS B 1 68  ? -53.975 37.523  1.889   1.00 23.75 ? 62  LYS B N     1 
ATOM   2667 C  CA    . LYS B 1 68  ? -53.355 38.688  2.563   1.00 26.50 ? 62  LYS B CA    1 
ATOM   2668 C  C     . LYS B 1 68  ? -54.393 39.344  3.481   1.00 30.69 ? 62  LYS B C     1 
ATOM   2669 O  O     . LYS B 1 68  ? -54.090 39.586  4.659   1.00 28.05 ? 62  LYS B O     1 
ATOM   2670 C  CB    . LYS B 1 68  ? -52.861 39.707  1.550   1.00 29.38 ? 62  LYS B CB    1 
ATOM   2671 C  CG    . LYS B 1 68  ? -52.437 41.045  2.136   1.00 33.87 ? 62  LYS B CG    1 
ATOM   2672 C  CD    . LYS B 1 68  ? -51.167 40.964  2.975   1.00 37.20 ? 62  LYS B CD    1 
ATOM   2673 C  CE    . LYS B 1 68  ? -50.844 42.286  3.653   1.00 38.95 ? 62  LYS B CE    1 
ATOM   2674 N  NZ    . LYS B 1 68  ? -49.419 42.361  4.050   1.00 39.92 ? 62  LYS B NZ    1 
ATOM   2675 N  N     . GLN B 1 69  ? -55.593 39.586  2.964   1.00 32.28 ? 63  GLN B N     1 
ATOM   2676 C  CA    . GLN B 1 69  ? -56.649 40.308  3.714   1.00 31.98 ? 63  GLN B CA    1 
ATOM   2677 C  C     . GLN B 1 69  ? -57.097 39.439  4.893   1.00 29.97 ? 63  GLN B C     1 
ATOM   2678 O  O     . GLN B 1 69  ? -57.509 40.024  5.924   1.00 31.20 ? 63  GLN B O     1 
ATOM   2679 C  CB    . GLN B 1 69  ? -57.776 40.730  2.764   1.00 33.84 ? 63  GLN B CB    1 
ATOM   2680 C  CG    . GLN B 1 69  ? -57.367 41.837  1.794   1.00 34.25 ? 63  GLN B CG    1 
ATOM   2681 C  CD    . GLN B 1 69  ? -58.407 42.058  0.719   1.00 42.20 ? 63  GLN B CD    1 
ATOM   2682 O  OE1   . GLN B 1 69  ? -59.371 41.310  0.589   1.00 48.24 ? 63  GLN B OE1   1 
ATOM   2683 N  NE2   . GLN B 1 69  ? -58.214 43.100  -0.068  1.00 49.46 ? 63  GLN B NE2   1 
ATOM   2684 N  N     . ALA B 1 70  ? -56.970 38.107  4.804   1.00 28.39 ? 64  ALA B N     1 
ATOM   2685 C  CA    . ALA B 1 70  ? -57.366 37.161  5.869   1.00 27.72 ? 64  ALA B CA    1 
ATOM   2686 C  C     . ALA B 1 70  ? -56.245 37.008  6.915   1.00 27.88 ? 64  ALA B C     1 
ATOM   2687 O  O     . ALA B 1 70  ? -56.483 36.323  7.923   1.00 27.72 ? 64  ALA B O     1 
ATOM   2688 C  CB    . ALA B 1 70  ? -57.782 35.837  5.266   1.00 24.93 ? 64  ALA B CB    1 
ATOM   2689 N  N     . GLY B 1 71  ? -55.082 37.625  6.700   1.00 26.01 ? 65  GLY B N     1 
ATOM   2690 C  CA    . GLY B 1 71  ? -53.969 37.634  7.671   1.00 28.26 ? 65  GLY B CA    1 
ATOM   2691 C  C     . GLY B 1 71  ? -52.799 36.741  7.275   1.00 28.38 ? 65  GLY B C     1 
ATOM   2692 O  O     . GLY B 1 71  ? -51.937 36.474  8.135   1.00 27.87 ? 65  GLY B O     1 
ATOM   2693 N  N     . MET B 1 72  ? -52.703 36.328  6.008   1.00 27.48 ? 66  MET B N     1 
ATOM   2694 C  CA    . MET B 1 72  ? -51.513 35.566  5.530   1.00 25.69 ? 66  MET B CA    1 
ATOM   2695 C  C     . MET B 1 72  ? -50.257 36.427  5.683   1.00 23.85 ? 66  MET B C     1 
ATOM   2696 O  O     . MET B 1 72  ? -50.277 37.601  5.227   1.00 27.22 ? 66  MET B O     1 
ATOM   2697 C  CB    . MET B 1 72  ? -51.654 35.144  4.067   1.00 22.40 ? 66  MET B CB    1 
ATOM   2698 C  CG    . MET B 1 72  ? -50.513 34.268  3.600   1.00 24.24 ? 66  MET B CG    1 
ATOM   2699 S  SD    . MET B 1 72  ? -50.808 33.534  1.957   1.00 24.90 ? 66  MET B SD    1 
ATOM   2700 C  CE    . MET B 1 72  ? -50.735 34.999  0.936   1.00 26.04 ? 66  MET B CE    1 
ATOM   2701 N  N     . LYS B 1 73  ? -49.178 35.838  6.190   1.00 23.02 ? 67  LYS B N     1 
ATOM   2702 C  CA    . LYS B 1 73  ? -47.849 36.480  6.291   1.00 24.90 ? 67  LYS B CA    1 
ATOM   2703 C  C     . LYS B 1 73  ? -46.830 35.798  5.373   1.00 23.29 ? 67  LYS B C     1 
ATOM   2704 O  O     . LYS B 1 73  ? -45.909 36.495  4.866   1.00 24.36 ? 67  LYS B O     1 
ATOM   2705 C  CB    . LYS B 1 73  ? -47.351 36.435  7.738   1.00 27.56 ? 67  LYS B CB    1 
ATOM   2706 C  CG    . LYS B 1 73  ? -48.205 37.242  8.714   1.00 29.53 ? 67  LYS B CG    1 
ATOM   2707 C  CD    . LYS B 1 73  ? -47.711 37.173  10.148  1.00 35.31 ? 67  LYS B CD    1 
ATOM   2708 C  CE    . LYS B 1 73  ? -48.550 38.035  11.074  1.00 42.69 ? 67  LYS B CE    1 
ATOM   2709 N  NZ    . LYS B 1 73  ? -48.542 37.507  12.455  1.00 47.19 ? 67  LYS B NZ    1 
ATOM   2710 N  N     . LYS B 1 74  ? -46.958 34.493  5.192   1.00 21.94 ? 68  LYS B N     1 
ATOM   2711 C  CA    . LYS B 1 74  ? -45.989 33.689  4.418   1.00 20.61 ? 68  LYS B CA    1 
ATOM   2712 C  C     . LYS B 1 74  ? -46.755 32.911  3.343   1.00 19.73 ? 68  LYS B C     1 
ATOM   2713 O  O     . LYS B 1 74  ? -47.698 32.223  3.674   1.00 19.17 ? 68  LYS B O     1 
ATOM   2714 C  CB    . LYS B 1 74  ? -45.218 32.714  5.321   1.00 20.35 ? 68  LYS B CB    1 
ATOM   2715 C  CG    . LYS B 1 74  ? -44.195 31.847  4.608   1.00 20.66 ? 68  LYS B CG    1 
ATOM   2716 C  CD    . LYS B 1 74  ? -43.209 31.179  5.530   1.00 22.46 ? 68  LYS B CD    1 
ATOM   2717 C  CE    . LYS B 1 74  ? -42.190 30.322  4.796   1.00 22.64 ? 68  LYS B CE    1 
ATOM   2718 N  NZ    . LYS B 1 74  ? -42.753 29.012  4.382   1.00 21.77 ? 68  LYS B NZ    1 
ATOM   2719 N  N     . ILE B 1 75  ? -46.256 32.943  2.122   1.00 21.49 ? 69  ILE B N     1 
ATOM   2720 C  CA    . ILE B 1 75  ? -46.760 32.072  1.024   1.00 21.46 ? 69  ILE B CA    1 
ATOM   2721 C  C     . ILE B 1 75  ? -45.590 31.212  0.573   1.00 21.21 ? 69  ILE B C     1 
ATOM   2722 O  O     . ILE B 1 75  ? -44.474 31.747  0.437   1.00 22.06 ? 69  ILE B O     1 
ATOM   2723 C  CB    . ILE B 1 75  ? -47.311 32.916  -0.139  1.00 22.75 ? 69  ILE B CB    1 
ATOM   2724 C  CG1   . ILE B 1 75  ? -47.872 32.031  -1.255  1.00 25.34 ? 69  ILE B CG1   1 
ATOM   2725 C  CG2   . ILE B 1 75  ? -46.283 33.873  -0.690  1.00 23.80 ? 69  ILE B CG2   1 
ATOM   2726 C  CD1   . ILE B 1 75  ? -49.204 31.469  -0.898  1.00 24.43 ? 69  ILE B CD1   1 
ATOM   2727 N  N     . ASN B 1 76  ? -45.831 29.941  0.349   1.00 18.67 ? 70  ASN B N     1 
ATOM   2728 C  CA    . ASN B 1 76  ? -44.847 29.010  -0.243  1.00 18.55 ? 70  ASN B CA    1 
ATOM   2729 C  C     . ASN B 1 76  ? -45.454 28.501  -1.547  1.00 18.20 ? 70  ASN B C     1 
ATOM   2730 O  O     . ASN B 1 76  ? -46.547 27.913  -1.492  1.00 19.02 ? 70  ASN B O     1 
ATOM   2731 C  CB    . ASN B 1 76  ? -44.550 27.841  0.694   1.00 17.45 ? 70  ASN B CB    1 
ATOM   2732 C  CG    . ASN B 1 76  ? -43.430 26.934  0.236   1.00 19.73 ? 70  ASN B CG    1 
ATOM   2733 O  OD1   . ASN B 1 76  ? -42.345 27.428  -0.075  1.00 20.12 ? 70  ASN B OD1   1 
ATOM   2734 N  ND2   . ASN B 1 76  ? -43.664 25.623  0.290   1.00 20.70 ? 70  ASN B ND2   1 
ATOM   2735 N  N     . PHE B 1 77  ? -44.712 28.654  -2.628  1.00 18.95 ? 71  PHE B N     1 
ATOM   2736 C  CA    . PHE B 1 77  ? -45.075 28.195  -3.987  1.00 20.88 ? 71  PHE B CA    1 
ATOM   2737 C  C     . PHE B 1 77  ? -44.533 26.785  -4.113  1.00 19.25 ? 71  PHE B C     1 
ATOM   2738 O  O     . PHE B 1 77  ? -43.340 26.564  -3.913  1.00 22.46 ? 71  PHE B O     1 
ATOM   2739 C  CB    . PHE B 1 77  ? -44.565 29.173  -5.045  1.00 22.55 ? 71  PHE B CB    1 
ATOM   2740 C  CG    . PHE B 1 77  ? -45.307 30.484  -4.999  1.00 22.70 ? 71  PHE B CG    1 
ATOM   2741 C  CD1   . PHE B 1 77  ? -46.587 30.586  -5.522  1.00 23.26 ? 71  PHE B CD1   1 
ATOM   2742 C  CD2   . PHE B 1 77  ? -44.747 31.603  -4.409  1.00 23.12 ? 71  PHE B CD2   1 
ATOM   2743 C  CE1   . PHE B 1 77  ? -47.292 31.788  -5.429  1.00 26.77 ? 71  PHE B CE1   1 
ATOM   2744 C  CE2   . PHE B 1 77  ? -45.438 32.804  -4.338  1.00 23.53 ? 71  PHE B CE2   1 
ATOM   2745 C  CZ    . PHE B 1 77  ? -46.716 32.900  -4.838  1.00 25.80 ? 71  PHE B CZ    1 
ATOM   2746 N  N     . ALA B 1 78  ? -45.415 25.857  -4.401  1.00 19.11 ? 72  ALA B N     1 
ATOM   2747 C  CA    . ALA B 1 78  ? -45.164 24.416  -4.403  1.00 21.38 ? 72  ALA B CA    1 
ATOM   2748 C  C     . ALA B 1 78  ? -45.903 23.807  -5.586  1.00 19.04 ? 72  ALA B C     1 
ATOM   2749 O  O     . ALA B 1 78  ? -46.421 24.567  -6.404  1.00 20.73 ? 72  ALA B O     1 
ATOM   2750 C  CB    . ALA B 1 78  ? -45.591 23.802  -3.088  1.00 22.08 ? 72  ALA B CB    1 
ATOM   2751 N  N     . GLY B 1 79  ? -45.973 22.485  -5.622  1.00 21.46 ? 73  GLY B N     1 
ATOM   2752 C  CA    . GLY B 1 79  ? -46.662 21.752  -6.696  1.00 20.08 ? 73  GLY B CA    1 
ATOM   2753 C  C     . GLY B 1 79  ? -46.521 20.268  -6.447  1.00 19.82 ? 73  GLY B C     1 
ATOM   2754 O  O     . GLY B 1 79  ? -46.680 19.855  -5.308  1.00 21.44 ? 73  GLY B O     1 
ATOM   2755 N  N     . GLY B 1 80  ? -46.259 19.475  -7.502  1.00 20.21 ? 74  GLY B N     1 
ATOM   2756 C  CA    . GLY B 1 80  ? -45.723 19.928  -8.763  1.00 22.51 ? 74  GLY B CA    1 
ATOM   2757 C  C     . GLY B 1 80  ? -44.344 20.553  -8.650  1.00 22.20 ? 74  GLY B C     1 
ATOM   2758 O  O     . GLY B 1 80  ? -43.909 20.852  -7.518  1.00 21.85 ? 74  GLY B O     1 
ATOM   2759 N  N     . GLU B 1 81  ? -43.713 20.815  -9.793  1.00 21.89 ? 75  GLU B N     1 
ATOM   2760 C  CA    . GLU B 1 81  ? -42.436 21.549  -9.878  1.00 20.39 ? 75  GLU B CA    1 
ATOM   2761 C  C     . GLU B 1 81  ? -42.682 22.995  -10.277 1.00 20.13 ? 75  GLU B C     1 
ATOM   2762 O  O     . GLU B 1 81  ? -42.977 23.282  -11.446 1.00 20.58 ? 75  GLU B O     1 
ATOM   2763 C  CB    . GLU B 1 81  ? -41.467 20.884  -10.856 1.00 21.04 ? 75  GLU B CB    1 
ATOM   2764 C  CG    . GLU B 1 81  ? -40.203 21.693  -11.015 1.00 19.69 ? 75  GLU B CG    1 
ATOM   2765 C  CD    . GLU B 1 81  ? -39.590 22.187  -9.703  1.00 20.36 ? 75  GLU B CD    1 
ATOM   2766 O  OE1   . GLU B 1 81  ? -39.541 21.376  -8.738  1.00 18.01 ? 75  GLU B OE1   1 
ATOM   2767 O  OE2   . GLU B 1 81  ? -39.131 23.366  -9.659  1.00 21.44 ? 75  GLU B OE2   1 
ATOM   2768 N  N     . PRO B 1 82  ? -42.534 23.982  -9.355  1.00 18.17 ? 76  PRO B N     1 
ATOM   2769 C  CA    . PRO B 1 82  ? -42.823 25.375  -9.705  1.00 18.94 ? 76  PRO B CA    1 
ATOM   2770 C  C     . PRO B 1 82  ? -42.051 25.922  -10.911 1.00 19.06 ? 76  PRO B C     1 
ATOM   2771 O  O     . PRO B 1 82  ? -42.558 26.782  -11.592 1.00 21.60 ? 76  PRO B O     1 
ATOM   2772 C  CB    . PRO B 1 82  ? -42.439 26.135  -8.428  1.00 19.14 ? 76  PRO B CB    1 
ATOM   2773 C  CG    . PRO B 1 82  ? -42.721 25.131  -7.357  1.00 20.46 ? 76  PRO B CG    1 
ATOM   2774 C  CD    . PRO B 1 82  ? -42.201 23.835  -7.924  1.00 19.36 ? 76  PRO B CD    1 
ATOM   2775 N  N     . PHE B 1 83  ? -40.806 25.501  -11.100 1.00 22.00 ? 77  PHE B N     1 
ATOM   2776 C  CA    . PHE B 1 83  ? -39.930 26.082  -12.149 1.00 20.87 ? 77  PHE B CA    1 
ATOM   2777 C  C     . PHE B 1 83  ? -40.278 25.529  -13.543 1.00 20.85 ? 77  PHE B C     1 
ATOM   2778 O  O     . PHE B 1 83  ? -39.646 25.990  -14.489 1.00 20.29 ? 77  PHE B O     1 
ATOM   2779 C  CB    . PHE B 1 83  ? -38.466 25.929  -11.754 1.00 21.36 ? 77  PHE B CB    1 
ATOM   2780 C  CG    . PHE B 1 83  ? -38.020 26.985  -10.777 1.00 21.38 ? 77  PHE B CG    1 
ATOM   2781 C  CD1   . PHE B 1 83  ? -38.165 26.803  -9.414  1.00 22.76 ? 77  PHE B CD1   1 
ATOM   2782 C  CD2   . PHE B 1 83  ? -37.508 28.191  -11.225 1.00 22.63 ? 77  PHE B CD2   1 
ATOM   2783 C  CE1   . PHE B 1 83  ? -37.803 27.801  -8.520  1.00 22.02 ? 77  PHE B CE1   1 
ATOM   2784 C  CE2   . PHE B 1 83  ? -37.146 29.187  -10.326 1.00 24.95 ? 77  PHE B CE2   1 
ATOM   2785 C  CZ    . PHE B 1 83  ? -37.264 28.981  -8.970  1.00 22.34 ? 77  PHE B CZ    1 
ATOM   2786 N  N     . LEU B 1 84  ? -41.301 24.679  -13.683 1.00 22.93 ? 78  LEU B N     1 
ATOM   2787 C  CA    . LEU B 1 84  ? -41.918 24.395  -15.011 1.00 22.56 ? 78  LEU B CA    1 
ATOM   2788 C  C     . LEU B 1 84  ? -42.768 25.581  -15.464 1.00 23.54 ? 78  LEU B C     1 
ATOM   2789 O  O     . LEU B 1 84  ? -43.048 25.650  -16.661 1.00 22.10 ? 78  LEU B O     1 
ATOM   2790 C  CB    . LEU B 1 84  ? -42.774 23.137  -14.912 1.00 22.69 ? 78  LEU B CB    1 
ATOM   2791 C  CG    . LEU B 1 84  ? -41.987 21.831  -14.989 1.00 22.47 ? 78  LEU B CG    1 
ATOM   2792 C  CD1   . LEU B 1 84  ? -42.874 20.618  -14.758 1.00 24.10 ? 78  LEU B CD1   1 
ATOM   2793 C  CD2   . LEU B 1 84  ? -41.231 21.710  -16.305 1.00 25.32 ? 78  LEU B CD2   1 
ATOM   2794 N  N     . TYR B 1 85  ? -43.135 26.488  -14.557 1.00 20.19 ? 79  TYR B N     1 
ATOM   2795 C  CA    . TYR B 1 85  ? -43.971 27.677  -14.854 1.00 21.85 ? 79  TYR B CA    1 
ATOM   2796 C  C     . TYR B 1 85  ? -43.279 28.940  -14.367 1.00 21.80 ? 79  TYR B C     1 
ATOM   2797 O  O     . TYR B 1 85  ? -43.843 29.629  -13.530 1.00 22.02 ? 79  TYR B O     1 
ATOM   2798 C  CB    . TYR B 1 85  ? -45.368 27.530  -14.237 1.00 22.75 ? 79  TYR B CB    1 
ATOM   2799 C  CG    . TYR B 1 85  ? -46.196 26.398  -14.792 1.00 21.25 ? 79  TYR B CG    1 
ATOM   2800 C  CD1   . TYR B 1 85  ? -46.032 25.103  -14.344 1.00 22.40 ? 79  TYR B CD1   1 
ATOM   2801 C  CD2   . TYR B 1 85  ? -47.189 26.622  -15.738 1.00 22.92 ? 79  TYR B CD2   1 
ATOM   2802 C  CE1   . TYR B 1 85  ? -46.792 24.056  -14.852 1.00 22.72 ? 79  TYR B CE1   1 
ATOM   2803 C  CE2   . TYR B 1 85  ? -47.970 25.589  -16.243 1.00 26.21 ? 79  TYR B CE2   1 
ATOM   2804 C  CZ    . TYR B 1 85  ? -47.763 24.291  -15.807 1.00 27.49 ? 79  TYR B CZ    1 
ATOM   2805 O  OH    . TYR B 1 85  ? -48.538 23.242  -16.258 1.00 28.06 ? 79  TYR B OH    1 
ATOM   2806 N  N     . PRO B 1 86  ? -42.085 29.299  -14.897 1.00 20.89 ? 80  PRO B N     1 
ATOM   2807 C  CA    . PRO B 1 86  ? -41.329 30.438  -14.404 1.00 22.24 ? 80  PRO B CA    1 
ATOM   2808 C  C     . PRO B 1 86  ? -42.052 31.744  -14.704 1.00 24.48 ? 80  PRO B C     1 
ATOM   2809 O  O     . PRO B 1 86  ? -41.868 32.693  -13.941 1.00 24.78 ? 80  PRO B O     1 
ATOM   2810 C  CB    . PRO B 1 86  ? -39.981 30.416  -15.143 1.00 21.32 ? 80  PRO B CB    1 
ATOM   2811 C  CG    . PRO B 1 86  ? -40.225 29.542  -16.337 1.00 21.41 ? 80  PRO B CG    1 
ATOM   2812 C  CD    . PRO B 1 86  ? -41.334 28.576  -15.948 1.00 22.45 ? 80  PRO B CD    1 
ATOM   2813 N  N     . LYS B 1 87  ? -42.879 31.792  -15.750 1.00 21.57 ? 81  LYS B N     1 
ATOM   2814 C  CA    . LYS B 1 87  ? -43.557 33.089  -16.058 1.00 23.37 ? 81  LYS B CA    1 
ATOM   2815 C  C     . LYS B 1 87  ? -44.615 33.347  -14.981 1.00 22.58 ? 81  LYS B C     1 
ATOM   2816 O  O     . LYS B 1 87  ? -44.640 34.466  -14.392 1.00 23.26 ? 81  LYS B O     1 
ATOM   2817 C  CB    . LYS B 1 87  ? -44.149 33.124  -17.466 1.00 24.48 ? 81  LYS B CB    1 
ATOM   2818 C  CG    . LYS B 1 87  ? -44.746 34.479  -17.806 1.00 25.69 ? 81  LYS B CG    1 
ATOM   2819 C  CD    . LYS B 1 87  ? -45.057 34.660  -19.274 1.00 27.69 ? 81  LYS B CD    1 
ATOM   2820 C  CE    . LYS B 1 87  ? -45.720 35.987  -19.587 1.00 31.97 ? 81  LYS B CE    1 
ATOM   2821 N  NZ    . LYS B 1 87  ? -44.754 37.107  -19.472 1.00 33.64 ? 81  LYS B NZ    1 
ATOM   2822 N  N     . PHE B 1 88  ? -45.483 32.363  -14.730 1.00 21.17 ? 82  PHE B N     1 
ATOM   2823 C  CA    . PHE B 1 88  ? -46.489 32.419  -13.645 1.00 22.82 ? 82  PHE B CA    1 
ATOM   2824 C  C     . PHE B 1 88  ? -45.781 32.697  -12.300 1.00 20.34 ? 82  PHE B C     1 
ATOM   2825 O  O     . PHE B 1 88  ? -46.181 33.616  -11.559 1.00 20.35 ? 82  PHE B O     1 
ATOM   2826 C  CB    . PHE B 1 88  ? -47.279 31.110  -13.578 1.00 23.63 ? 82  PHE B CB    1 
ATOM   2827 C  CG    . PHE B 1 88  ? -48.380 31.117  -12.551 1.00 25.39 ? 82  PHE B CG    1 
ATOM   2828 C  CD1   . PHE B 1 88  ? -49.659 31.540  -12.876 1.00 26.30 ? 82  PHE B CD1   1 
ATOM   2829 C  CD2   . PHE B 1 88  ? -48.131 30.709  -11.246 1.00 25.40 ? 82  PHE B CD2   1 
ATOM   2830 C  CE1   . PHE B 1 88  ? -50.656 31.559  -11.906 1.00 25.06 ? 82  PHE B CE1   1 
ATOM   2831 C  CE2   . PHE B 1 88  ? -49.122 30.739  -10.283 1.00 24.05 ? 82  PHE B CE2   1 
ATOM   2832 C  CZ    . PHE B 1 88  ? -50.384 31.167  -10.620 1.00 23.72 ? 82  PHE B CZ    1 
ATOM   2833 N  N     . LEU B 1 89  ? -44.775 31.906  -11.982 1.00 21.38 ? 83  LEU B N     1 
ATOM   2834 C  CA    . LEU B 1 89  ? -44.053 31.957  -10.674 1.00 22.06 ? 83  LEU B CA    1 
ATOM   2835 C  C     . LEU B 1 89  ? -43.426 33.353  -10.476 1.00 24.24 ? 83  LEU B C     1 
ATOM   2836 O  O     . LEU B 1 89  ? -43.630 33.934  -9.394  1.00 23.43 ? 83  LEU B O     1 
ATOM   2837 C  CB    . LEU B 1 89  ? -43.003 30.845  -10.636 1.00 22.95 ? 83  LEU B CB    1 
ATOM   2838 C  CG    . LEU B 1 89  ? -42.253 30.698  -9.307  1.00 24.06 ? 83  LEU B CG    1 
ATOM   2839 C  CD1   . LEU B 1 89  ? -43.210 30.389  -8.156  1.00 24.56 ? 83  LEU B CD1   1 
ATOM   2840 C  CD2   . LEU B 1 89  ? -41.168 29.653  -9.412  1.00 23.62 ? 83  LEU B CD2   1 
ATOM   2841 N  N     . GLY B 1 90  ? -42.760 33.904  -11.495 1.00 23.58 ? 84  GLY B N     1 
ATOM   2842 C  CA    . GLY B 1 90  ? -42.161 35.255  -11.445 1.00 25.36 ? 84  GLY B CA    1 
ATOM   2843 C  C     . GLY B 1 90  ? -43.207 36.328  -11.199 1.00 27.00 ? 84  GLY B C     1 
ATOM   2844 O  O     . GLY B 1 90  ? -42.967 37.224  -10.354 1.00 24.56 ? 84  GLY B O     1 
ATOM   2845 N  N     . GLU B 1 91  ? -44.364 36.232  -11.862 1.00 25.03 ? 85  GLU B N     1 
ATOM   2846 C  CA    . GLU B 1 91  ? -45.459 37.230  -11.743 1.00 26.61 ? 85  GLU B CA    1 
ATOM   2847 C  C     . GLU B 1 91  ? -46.041 37.189  -10.328 1.00 27.00 ? 85  GLU B C     1 
ATOM   2848 O  O     . GLU B 1 91  ? -46.369 38.265  -9.797  1.00 24.36 ? 85  GLU B O     1 
ATOM   2849 C  CB    . GLU B 1 91  ? -46.593 36.987  -12.746 1.00 31.57 ? 85  GLU B CB    1 
ATOM   2850 C  CG    . GLU B 1 91  ? -46.299 37.480  -14.141 1.00 39.99 ? 85  GLU B CG    1 
ATOM   2851 C  CD    . GLU B 1 91  ? -47.292 37.016  -15.206 1.00 48.56 ? 85  GLU B CD    1 
ATOM   2852 O  OE1   . GLU B 1 91  ? -47.739 37.874  -15.987 1.00 53.16 ? 85  GLU B OE1   1 
ATOM   2853 O  OE2   . GLU B 1 91  ? -47.585 35.774  -15.283 1.00 51.21 ? 85  GLU B OE2   1 
ATOM   2854 N  N     . MET B 1 92  ? -46.203 35.993  -9.755  1.00 23.82 ? 86  MET B N     1 
ATOM   2855 C  CA    . MET B 1 92  ? -46.835 35.810  -8.427  1.00 24.90 ? 86  MET B CA    1 
ATOM   2856 C  C     . MET B 1 92  ? -45.851 36.236  -7.339  1.00 25.99 ? 86  MET B C     1 
ATOM   2857 O  O     . MET B 1 92  ? -46.307 36.903  -6.391  1.00 25.73 ? 86  MET B O     1 
ATOM   2858 C  CB    . MET B 1 92  ? -47.269 34.370  -8.159  1.00 27.19 ? 86  MET B CB    1 
ATOM   2859 C  CG    . MET B 1 92  ? -48.442 33.896  -9.025  1.00 30.26 ? 86  MET B CG    1 
ATOM   2860 S  SD    . MET B 1 92  ? -49.818 35.074  -9.184  1.00 36.03 ? 86  MET B SD    1 
ATOM   2861 C  CE    . MET B 1 92  ? -49.549 35.696  -10.841 1.00 39.78 ? 86  MET B CE    1 
ATOM   2862 N  N     . ILE B 1 93  ? -44.564 35.923  -7.488  1.00 25.57 ? 87  ILE B N     1 
ATOM   2863 C  CA    . ILE B 1 93  ? -43.525 36.338  -6.495  1.00 25.74 ? 87  ILE B CA    1 
ATOM   2864 C  C     . ILE B 1 93  ? -43.450 37.867  -6.453  1.00 26.43 ? 87  ILE B C     1 
ATOM   2865 O  O     . ILE B 1 93  ? -43.469 38.447  -5.337  1.00 25.24 ? 87  ILE B O     1 
ATOM   2866 C  CB    . ILE B 1 93  ? -42.173 35.714  -6.823  1.00 28.62 ? 87  ILE B CB    1 
ATOM   2867 C  CG1   . ILE B 1 93  ? -42.157 34.219  -6.481  1.00 30.84 ? 87  ILE B CG1   1 
ATOM   2868 C  CG2   . ILE B 1 93  ? -41.042 36.471  -6.149  1.00 31.03 ? 87  ILE B CG2   1 
ATOM   2869 C  CD1   . ILE B 1 93  ? -41.025 33.494  -7.189  1.00 34.74 ? 87  ILE B CD1   1 
ATOM   2870 N  N     . ASP B 1 94  ? -43.346 38.520  -7.608  1.00 25.85 ? 88  ASP B N     1 
ATOM   2871 C  CA    . ASP B 1 94  ? -43.255 40.003  -7.638  1.00 27.80 ? 88  ASP B CA    1 
ATOM   2872 C  C     . ASP B 1 94  ? -44.516 40.636  -7.039  1.00 26.14 ? 88  ASP B C     1 
ATOM   2873 O  O     . ASP B 1 94  ? -44.388 41.597  -6.256  1.00 25.72 ? 88  ASP B O     1 
ATOM   2874 C  CB    . ASP B 1 94  ? -43.026 40.527  -9.050  1.00 30.64 ? 88  ASP B CB    1 
ATOM   2875 C  CG    . ASP B 1 94  ? -41.749 40.029  -9.686  1.00 32.39 ? 88  ASP B CG    1 
ATOM   2876 O  OD1   . ASP B 1 94  ? -40.865 39.491  -8.953  1.00 31.62 ? 88  ASP B OD1   1 
ATOM   2877 O  OD2   . ASP B 1 94  ? -41.663 40.175  -10.919 1.00 33.36 ? 88  ASP B OD2   1 
ATOM   2878 N  N     . PHE B 1 95  ? -45.698 40.128  -7.377  1.00 25.61 ? 89  PHE B N     1 
ATOM   2879 C  CA    . PHE B 1 95  ? -46.981 40.648  -6.848  1.00 26.90 ? 89  PHE B CA    1 
ATOM   2880 C  C     . PHE B 1 95  ? -47.055 40.506  -5.320  1.00 28.94 ? 89  PHE B C     1 
ATOM   2881 O  O     . PHE B 1 95  ? -47.467 41.457  -4.618  1.00 26.79 ? 89  PHE B O     1 
ATOM   2882 C  CB    . PHE B 1 95  ? -48.138 39.883  -7.462  1.00 25.47 ? 89  PHE B CB    1 
ATOM   2883 C  CG    . PHE B 1 95  ? -49.489 40.416  -7.082  1.00 26.11 ? 89  PHE B CG    1 
ATOM   2884 C  CD1   . PHE B 1 95  ? -49.944 41.618  -7.606  1.00 27.80 ? 89  PHE B CD1   1 
ATOM   2885 C  CD2   . PHE B 1 95  ? -50.292 39.725  -6.190  1.00 25.52 ? 89  PHE B CD2   1 
ATOM   2886 C  CE1   . PHE B 1 95  ? -51.211 42.080  -7.289  1.00 26.97 ? 89  PHE B CE1   1 
ATOM   2887 C  CE2   . PHE B 1 95  ? -51.536 40.214  -5.838  1.00 29.58 ? 89  PHE B CE2   1 
ATOM   2888 C  CZ    . PHE B 1 95  ? -51.997 41.391  -6.400  1.00 28.53 ? 89  PHE B CZ    1 
ATOM   2889 N  N     . CYS B 1 96  ? -46.695 39.338  -4.806  1.00 25.19 ? 90  CYS B N     1 
ATOM   2890 C  CA    . CYS B 1 96  ? -46.742 39.020  -3.363  1.00 27.84 ? 90  CYS B CA    1 
ATOM   2891 C  C     . CYS B 1 96  ? -45.819 39.941  -2.551  1.00 27.37 ? 90  CYS B C     1 
ATOM   2892 O  O     . CYS B 1 96  ? -46.266 40.408  -1.467  1.00 32.16 ? 90  CYS B O     1 
ATOM   2893 C  CB    . CYS B 1 96  ? -46.391 37.567  -3.117  1.00 26.04 ? 90  CYS B CB    1 
ATOM   2894 S  SG    . CYS B 1 96  ? -47.814 36.505  -3.452  1.00 27.50 ? 90  CYS B SG    1 
ATOM   2895 N  N     . LYS B 1 97  ? -44.603 40.190  -3.010  1.00 29.72 ? 91  LYS B N     1 
ATOM   2896 C  CA    . LYS B 1 97  ? -43.661 41.073  -2.269  1.00 31.39 ? 91  LYS B CA    1 
ATOM   2897 C  C     . LYS B 1 97  ? -43.987 42.546  -2.531  1.00 33.34 ? 91  LYS B C     1 
ATOM   2898 O  O     . LYS B 1 97  ? -44.132 43.273  -1.552  1.00 35.39 ? 91  LYS B O     1 
ATOM   2899 C  CB    . LYS B 1 97  ? -42.204 40.811  -2.639  1.00 33.32 ? 91  LYS B CB    1 
ATOM   2900 C  CG    . LYS B 1 97  ? -41.190 41.488  -1.724  1.00 34.98 ? 91  LYS B CG    1 
ATOM   2901 C  CD    . LYS B 1 97  ? -41.383 41.223  -0.248  1.00 36.90 ? 91  LYS B CD    1 
ATOM   2902 C  CE    . LYS B 1 97  ? -41.169 39.769  0.117   1.00 38.09 ? 91  LYS B CE    1 
ATOM   2903 N  NZ    . LYS B 1 97  ? -40.918 39.605  1.576   1.00 40.54 ? 91  LYS B NZ    1 
ATOM   2904 N  N     . GLU B 1 98  ? -44.100 42.974  -3.791  1.00 33.81 ? 92  GLU B N     1 
ATOM   2905 C  CA    . GLU B 1 98  ? -44.161 44.413  -4.170  1.00 32.38 ? 92  GLU B CA    1 
ATOM   2906 C  C     . GLU B 1 98  ? -45.547 44.999  -3.902  1.00 37.30 ? 92  GLU B C     1 
ATOM   2907 O  O     . GLU B 1 98  ? -45.596 46.177  -3.536  1.00 39.07 ? 92  GLU B O     1 
ATOM   2908 C  CB    . GLU B 1 98  ? -43.784 44.637  -5.629  1.00 36.77 ? 92  GLU B CB    1 
ATOM   2909 C  CG    . GLU B 1 98  ? -42.372 44.201  -5.944  1.00 42.74 ? 92  GLU B CG    1 
ATOM   2910 C  CD    . GLU B 1 98  ? -41.960 44.314  -7.402  1.00 50.21 ? 92  GLU B CD    1 
ATOM   2911 O  OE1   . GLU B 1 98  ? -42.799 44.750  -8.241  1.00 57.18 ? 92  GLU B OE1   1 
ATOM   2912 O  OE2   . GLU B 1 98  ? -40.803 43.954  -7.700  1.00 48.60 ? 92  GLU B OE2   1 
ATOM   2913 N  N     . THR B 1 99  ? -46.630 44.251  -4.106  1.00 36.15 ? 93  THR B N     1 
ATOM   2914 C  CA    . THR B 1 99  ? -48.017 44.782  -3.990  1.00 35.13 ? 93  THR B CA    1 
ATOM   2915 C  C     . THR B 1 99  ? -48.624 44.337  -2.662  1.00 32.75 ? 93  THR B C     1 
ATOM   2916 O  O     . THR B 1 99  ? -49.239 45.164  -1.998  1.00 36.25 ? 93  THR B O     1 
ATOM   2917 C  CB    . THR B 1 99  ? -48.928 44.367  -5.162  1.00 33.31 ? 93  THR B CB    1 
ATOM   2918 O  OG1   . THR B 1 99  ? -48.477 44.935  -6.390  1.00 32.12 ? 93  THR B OG1   1 
ATOM   2919 C  CG2   . THR B 1 99  ? -50.360 44.803  -4.974  1.00 34.28 ? 93  THR B CG2   1 
ATOM   2920 N  N     . LEU B 1 100 ? -48.520 43.063  -2.308  1.00 30.88 ? 94  LEU B N     1 
ATOM   2921 C  CA    . LEU B 1 100 ? -49.170 42.552  -1.089  1.00 28.82 ? 94  LEU B CA    1 
ATOM   2922 C  C     . LEU B 1 100 ? -48.260 42.808  0.113   1.00 29.78 ? 94  LEU B C     1 
ATOM   2923 O  O     . LEU B 1 100 ? -48.777 42.748  1.231   1.00 32.74 ? 94  LEU B O     1 
ATOM   2924 C  CB    . LEU B 1 100 ? -49.507 41.067  -1.235  1.00 29.07 ? 94  LEU B CB    1 
ATOM   2925 C  CG    . LEU B 1 100 ? -50.539 40.722  -2.314  1.00 28.68 ? 94  LEU B CG    1 
ATOM   2926 C  CD1   . LEU B 1 100 ? -50.903 39.252  -2.256  1.00 27.04 ? 94  LEU B CD1   1 
ATOM   2927 C  CD2   . LEU B 1 100 ? -51.803 41.567  -2.191  1.00 30.50 ? 94  LEU B CD2   1 
ATOM   2928 N  N     . GLN B 1 101 ? -46.960 42.975  -0.098  1.00 31.51 ? 95  GLN B N     1 
ATOM   2929 C  CA    . GLN B 1 101 ? -45.973 43.235  0.989   1.00 34.40 ? 95  GLN B CA    1 
ATOM   2930 C  C     . GLN B 1 101 ? -46.052 42.094  1.999   1.00 34.73 ? 95  GLN B C     1 
ATOM   2931 O  O     . GLN B 1 101 ? -46.091 42.368  3.207   1.00 34.45 ? 95  GLN B O     1 
ATOM   2932 C  CB    . GLN B 1 101 ? -46.243 44.599  1.637   1.00 35.19 ? 95  GLN B CB    1 
ATOM   2933 C  CG    . GLN B 1 101 ? -46.088 45.741  0.643   1.00 38.91 ? 95  GLN B CG    1 
ATOM   2934 C  CD    . GLN B 1 101 ? -46.188 47.093  1.302   1.00 44.92 ? 95  GLN B CD    1 
ATOM   2935 O  OE1   . GLN B 1 101 ? -47.229 47.741  1.276   1.00 49.87 ? 95  GLN B OE1   1 
ATOM   2936 N  NE2   . GLN B 1 101 ? -45.109 47.505  1.947   1.00 49.52 ? 95  GLN B NE2   1 
ATOM   2937 N  N     . LEU B 1 102 ? -46.066 40.846  1.521   1.00 30.16 ? 96  LEU B N     1 
ATOM   2938 C  CA    . LEU B 1 102 ? -46.062 39.665  2.418   1.00 29.61 ? 96  LEU B CA    1 
ATOM   2939 C  C     . LEU B 1 102 ? -44.749 39.663  3.182   1.00 27.27 ? 96  LEU B C     1 
ATOM   2940 O  O     . LEU B 1 102 ? -43.768 40.176  2.625   1.00 25.32 ? 96  LEU B O     1 
ATOM   2941 C  CB    . LEU B 1 102 ? -46.253 38.405  1.578   1.00 30.11 ? 96  LEU B CB    1 
ATOM   2942 C  CG    . LEU B 1 102 ? -47.665 38.219  1.037   1.00 33.40 ? 96  LEU B CG    1 
ATOM   2943 C  CD1   . LEU B 1 102 ? -47.743 36.942  0.221   1.00 35.94 ? 96  LEU B CD1   1 
ATOM   2944 C  CD2   . LEU B 1 102 ? -48.684 38.174  2.166   1.00 31.44 ? 96  LEU B CD2   1 
ATOM   2945 N  N     . GLU B 1 103 ? -44.747 39.152  4.414   1.00 28.73 ? 97  GLU B N     1 
ATOM   2946 C  CA    . GLU B 1 103 ? -43.516 39.049  5.240   1.00 29.07 ? 97  GLU B CA    1 
ATOM   2947 C  C     . GLU B 1 103 ? -42.569 38.060  4.574   1.00 27.46 ? 97  GLU B C     1 
ATOM   2948 O  O     . GLU B 1 103 ? -41.354 38.288  4.602   1.00 27.99 ? 97  GLU B O     1 
ATOM   2949 C  CB    . GLU B 1 103 ? -43.799 38.577  6.666   1.00 31.99 ? 97  GLU B CB    1 
ATOM   2950 C  CG    . GLU B 1 103 ? -44.469 39.630  7.532   1.00 37.70 ? 97  GLU B CG    1 
ATOM   2951 C  CD    . GLU B 1 103 ? -44.815 39.161  8.938   1.00 38.77 ? 97  GLU B CD    1 
ATOM   2952 O  OE1   . GLU B 1 103 ? -44.113 38.252  9.473   1.00 41.73 ? 97  GLU B OE1   1 
ATOM   2953 O  OE2   . GLU B 1 103 ? -45.812 39.684  9.499   1.00 46.98 ? 97  GLU B OE2   1 
ATOM   2954 N  N     . SER B 1 104 ? -43.084 36.974  3.989   1.00 23.90 ? 98  SER B N     1 
ATOM   2955 C  CA    . SER B 1 104 ? -42.183 35.897  3.497   1.00 21.88 ? 98  SER B CA    1 
ATOM   2956 C  C     . SER B 1 104 ? -42.735 35.283  2.218   1.00 21.15 ? 98  SER B C     1 
ATOM   2957 O  O     . SER B 1 104 ? -43.902 34.862  2.203   1.00 22.47 ? 98  SER B O     1 
ATOM   2958 C  CB    . SER B 1 104 ? -41.996 34.853  4.533   1.00 22.26 ? 98  SER B CB    1 
ATOM   2959 O  OG    . SER B 1 104 ? -41.071 33.872  4.109   1.00 24.08 ? 98  SER B OG    1 
ATOM   2960 N  N     . VAL B 1 105 ? -41.919 35.265  1.193   1.00 21.38 ? 99  VAL B N     1 
ATOM   2961 C  CA    . VAL B 1 105 ? -42.246 34.597  -0.086  1.00 22.10 ? 99  VAL B CA    1 
ATOM   2962 C  C     . VAL B 1 105 ? -41.233 33.466  -0.217  1.00 21.42 ? 99  VAL B C     1 
ATOM   2963 O  O     . VAL B 1 105 ? -40.033 33.745  -0.260  1.00 24.01 ? 99  VAL B O     1 
ATOM   2964 C  CB    . VAL B 1 105 ? -42.210 35.570  -1.270  1.00 24.79 ? 99  VAL B CB    1 
ATOM   2965 C  CG1   . VAL B 1 105 ? -42.293 34.825  -2.590  1.00 25.17 ? 99  VAL B CG1   1 
ATOM   2966 C  CG2   . VAL B 1 105 ? -43.306 36.620  -1.155  1.00 28.13 ? 99  VAL B CG2   1 
ATOM   2967 N  N     . SER B 1 106 ? -41.712 32.234  -0.201  1.00 22.41 ? 100 SER B N     1 
ATOM   2968 C  CA    . SER B 1 106 ? -40.832 31.056  -0.310  1.00 22.67 ? 100 SER B CA    1 
ATOM   2969 C  C     . SER B 1 106 ? -41.252 30.229  -1.533  1.00 21.46 ? 100 SER B C     1 
ATOM   2970 O  O     . SER B 1 106 ? -42.409 30.364  -2.020  1.00 20.10 ? 100 SER B O     1 
ATOM   2971 C  CB    . SER B 1 106 ? -40.762 30.238  0.974   1.00 22.66 ? 100 SER B CB    1 
ATOM   2972 O  OG    . SER B 1 106 ? -42.019 29.737  1.428   1.00 26.63 ? 100 SER B OG    1 
ATOM   2973 N  N     . ILE B 1 107 ? -40.310 29.453  -2.018  1.00 22.12 ? 101 ILE B N     1 
ATOM   2974 C  CA    . ILE B 1 107 ? -40.508 28.448  -3.105  1.00 22.45 ? 101 ILE B CA    1 
ATOM   2975 C  C     . ILE B 1 107 ? -39.856 27.142  -2.670  1.00 22.67 ? 101 ILE B C     1 
ATOM   2976 O  O     . ILE B 1 107 ? -38.750 27.185  -2.055  1.00 24.84 ? 101 ILE B O     1 
ATOM   2977 C  CB    . ILE B 1 107 ? -39.888 28.930  -4.429  1.00 23.91 ? 101 ILE B CB    1 
ATOM   2978 C  CG1   . ILE B 1 107 ? -40.247 30.372  -4.758  1.00 27.31 ? 101 ILE B CG1   1 
ATOM   2979 C  CG2   . ILE B 1 107 ? -40.259 28.008  -5.583  1.00 23.33 ? 101 ILE B CG2   1 
ATOM   2980 C  CD1   . ILE B 1 107 ? -39.239 31.030  -5.680  1.00 31.55 ? 101 ILE B CD1   1 
ATOM   2981 N  N     . VAL B 1 108 ? -40.500 26.022  -2.954  1.00 20.33 ? 102 VAL B N     1 
ATOM   2982 C  CA    . VAL B 1 108 ? -39.876 24.684  -2.799  1.00 18.86 ? 102 VAL B CA    1 
ATOM   2983 C  C     . VAL B 1 108 ? -39.763 24.064  -4.200  1.00 22.00 ? 102 VAL B C     1 
ATOM   2984 O  O     . VAL B 1 108 ? -40.748 24.078  -4.970  1.00 20.18 ? 102 VAL B O     1 
ATOM   2985 C  CB    . VAL B 1 108 ? -40.607 23.777  -1.799  1.00 20.60 ? 102 VAL B CB    1 
ATOM   2986 C  CG1   . VAL B 1 108 ? -42.065 23.612  -2.146  1.00 24.68 ? 102 VAL B CG1   1 
ATOM   2987 C  CG2   . VAL B 1 108 ? -39.917 22.441  -1.633  1.00 18.50 ? 102 VAL B CG2   1 
ATOM   2988 N  N     . THR B 1 109 ? -38.570 23.594  -4.535  1.00 19.38 ? 103 THR B N     1 
ATOM   2989 C  CA    . THR B 1 109 ? -38.212 23.171  -5.899  1.00 19.11 ? 103 THR B CA    1 
ATOM   2990 C  C     . THR B 1 109 ? -37.353 21.913  -5.822  1.00 20.78 ? 103 THR B C     1 
ATOM   2991 O  O     . THR B 1 109 ? -36.487 21.796  -4.884  1.00 18.71 ? 103 THR B O     1 
ATOM   2992 C  CB    . THR B 1 109 ? -37.525 24.314  -6.682  1.00 20.83 ? 103 THR B CB    1 
ATOM   2993 O  OG1   . THR B 1 109 ? -37.144 23.790  -7.952  1.00 19.66 ? 103 THR B OG1   1 
ATOM   2994 C  CG2   . THR B 1 109 ? -36.320 24.949  -6.015  1.00 20.32 ? 103 THR B CG2   1 
ATOM   2995 N  N     . ASN B 1 110 ? -37.411 21.090  -6.878  1.00 18.10 ? 104 ASN B N     1 
ATOM   2996 C  CA    . ASN B 1 110 ? -36.437 19.980  -7.072  1.00 18.79 ? 104 ASN B CA    1 
ATOM   2997 C  C     . ASN B 1 110 ? -35.093 20.526  -7.592  1.00 19.53 ? 104 ASN B C     1 
ATOM   2998 O  O     . ASN B 1 110 ? -34.139 19.707  -7.697  1.00 22.07 ? 104 ASN B O     1 
ATOM   2999 C  CB    . ASN B 1 110 ? -37.028 18.853  -7.922  1.00 18.30 ? 104 ASN B CB    1 
ATOM   3000 C  CG    . ASN B 1 110 ? -37.301 19.196  -9.380  1.00 18.98 ? 104 ASN B CG    1 
ATOM   3001 O  OD1   . ASN B 1 110 ? -36.572 19.997  -9.979  1.00 18.65 ? 104 ASN B OD1   1 
ATOM   3002 N  ND2   . ASN B 1 110 ? -38.315 18.554  -9.978  1.00 18.32 ? 104 ASN B ND2   1 
ATOM   3003 N  N     . GLY B 1 111 ? -35.015 21.814  -7.915  1.00 20.12 ? 105 GLY B N     1 
ATOM   3004 C  CA    . GLY B 1 111 ? -33.778 22.540  -8.302  1.00 22.15 ? 105 GLY B CA    1 
ATOM   3005 C  C     . GLY B 1 111 ? -33.286 22.344  -9.750  1.00 22.67 ? 105 GLY B C     1 
ATOM   3006 O  O     . GLY B 1 111 ? -32.451 23.140  -10.206 1.00 25.05 ? 105 GLY B O     1 
ATOM   3007 N  N     A SER B 1 112 ? -33.811 21.354  -10.471 0.72 23.59 ? 106 SER B N     1 
ATOM   3008 N  N     B SER B 1 112 ? -33.754 21.325  -10.466 0.28 23.35 ? 106 SER B N     1 
ATOM   3009 C  CA    A SER B 1 112 ? -33.324 20.950  -11.827 0.72 24.34 ? 106 SER B CA    1 
ATOM   3010 C  CA    B SER B 1 112 ? -33.262 21.011  -11.837 0.28 23.62 ? 106 SER B CA    1 
ATOM   3011 C  C     A SER B 1 112 ? -33.490 22.078  -12.847 0.72 24.12 ? 106 SER B C     1 
ATOM   3012 C  C     B SER B 1 112 ? -33.377 22.235  -12.745 0.28 23.71 ? 106 SER B C     1 
ATOM   3013 O  O     A SER B 1 112 ? -32.628 22.184  -13.750 0.72 22.43 ? 106 SER B O     1 
ATOM   3014 O  O     B SER B 1 112 ? -32.385 22.557  -13.432 0.28 22.75 ? 106 SER B O     1 
ATOM   3015 C  CB    A SER B 1 112 ? -33.965 19.684  -12.300 0.72 25.10 ? 106 SER B CB    1 
ATOM   3016 C  CB    B SER B 1 112 ? -33.977 19.852  -12.420 0.28 23.90 ? 106 SER B CB    1 
ATOM   3017 O  OG    A SER B 1 112 ? -35.386 19.808  -12.377 0.72 26.29 ? 106 SER B OG    1 
ATOM   3018 O  OG    B SER B 1 112 ? -33.583 18.672  -11.754 0.28 24.19 ? 106 SER B OG    1 
ATOM   3019 N  N     . LEU B 1 113 ? -34.522 22.916  -12.721 1.00 23.35 ? 107 LEU B N     1 
ATOM   3020 C  CA    . LEU B 1 113 ? -34.838 23.940  -13.736 1.00 24.83 ? 107 LEU B CA    1 
ATOM   3021 C  C     . LEU B 1 113 ? -34.570 25.358  -13.229 1.00 25.33 ? 107 LEU B C     1 
ATOM   3022 O  O     . LEU B 1 113 ? -34.952 26.321  -13.934 1.00 27.27 ? 107 LEU B O     1 
ATOM   3023 C  CB    . LEU B 1 113 ? -36.291 23.758  -14.180 1.00 23.96 ? 107 LEU B CB    1 
ATOM   3024 C  CG    . LEU B 1 113 ? -36.727 22.324  -14.478 1.00 27.16 ? 107 LEU B CG    1 
ATOM   3025 C  CD1   . LEU B 1 113 ? -38.217 22.297  -14.786 1.00 28.99 ? 107 LEU B CD1   1 
ATOM   3026 C  CD2   . LEU B 1 113 ? -35.971 21.686  -15.645 1.00 29.44 ? 107 LEU B CD2   1 
ATOM   3027 N  N     . VAL B 1 114 ? -33.888 25.519  -12.095 1.00 23.24 ? 108 VAL B N     1 
ATOM   3028 C  CA    . VAL B 1 114 ? -33.576 26.860  -11.530 1.00 24.89 ? 108 VAL B CA    1 
ATOM   3029 C  C     . VAL B 1 114 ? -32.370 27.389  -12.296 1.00 25.65 ? 108 VAL B C     1 
ATOM   3030 O  O     . VAL B 1 114 ? -31.376 26.664  -12.372 1.00 24.07 ? 108 VAL B O     1 
ATOM   3031 C  CB    . VAL B 1 114 ? -33.256 26.812  -10.020 1.00 23.45 ? 108 VAL B CB    1 
ATOM   3032 C  CG1   . VAL B 1 114 ? -32.891 28.182  -9.497  1.00 23.79 ? 108 VAL B CG1   1 
ATOM   3033 C  CG2   . VAL B 1 114 ? -34.428 26.269  -9.238  1.00 24.91 ? 108 VAL B CG2   1 
ATOM   3034 N  N     . LYS B 1 115 ? -32.447 28.623  -12.787 1.00 30.20 ? 109 LYS B N     1 
ATOM   3035 C  CA    . LYS B 1 115 ? -31.332 29.266  -13.527 1.00 32.75 ? 109 LYS B CA    1 
ATOM   3036 C  C     . LYS B 1 115 ? -31.011 30.562  -12.803 1.00 29.73 ? 109 LYS B C     1 
ATOM   3037 O  O     . LYS B 1 115 ? -31.936 31.168  -12.242 1.00 28.37 ? 109 LYS B O     1 
ATOM   3038 C  CB    . LYS B 1 115 ? -31.725 29.607  -14.971 1.00 38.99 ? 109 LYS B CB    1 
ATOM   3039 C  CG    . LYS B 1 115 ? -32.352 28.472  -15.764 1.00 46.10 ? 109 LYS B CG    1 
ATOM   3040 C  CD    . LYS B 1 115 ? -33.125 28.941  -16.980 1.00 52.54 ? 109 LYS B CD    1 
ATOM   3041 C  CE    . LYS B 1 115 ? -32.580 28.383  -18.279 1.00 58.94 ? 109 LYS B CE    1 
ATOM   3042 N  NZ    . LYS B 1 115 ? -31.197 28.840  -18.544 1.00 57.12 ? 109 LYS B NZ    1 
ATOM   3043 N  N     . GLU B 1 116 ? -29.777 31.029  -12.914 1.00 29.35 ? 110 GLU B N     1 
ATOM   3044 C  CA    . GLU B 1 116 ? -29.337 32.254  -12.221 1.00 32.96 ? 110 GLU B CA    1 
ATOM   3045 C  C     . GLU B 1 116 ? -30.210 33.412  -12.688 1.00 30.22 ? 110 GLU B C     1 
ATOM   3046 O  O     . GLU B 1 116 ? -30.578 34.265  -11.837 1.00 30.63 ? 110 GLU B O     1 
ATOM   3047 C  CB    . GLU B 1 116 ? -27.839 32.511  -12.417 1.00 36.04 ? 110 GLU B CB    1 
ATOM   3048 C  CG    . GLU B 1 116 ? -27.383 33.626  -11.506 1.00 40.63 ? 110 GLU B CG    1 
ATOM   3049 C  CD    . GLU B 1 116 ? -25.915 34.008  -11.532 1.00 46.47 ? 110 GLU B CD    1 
ATOM   3050 O  OE1   . GLU B 1 116 ? -25.127 33.215  -12.071 1.00 46.17 ? 110 GLU B OE1   1 
ATOM   3051 O  OE2   . GLU B 1 116 ? -25.587 35.103  -10.996 1.00 46.18 ? 110 GLU B OE2   1 
ATOM   3052 N  N     . GLN B 1 117 ? -30.560 33.437  -13.979 1.00 29.86 ? 111 GLN B N     1 
ATOM   3053 C  CA    . GLN B 1 117 ? -31.325 34.566  -14.587 1.00 29.44 ? 111 GLN B CA    1 
ATOM   3054 C  C     . GLN B 1 117 ? -32.606 34.807  -13.798 1.00 26.13 ? 111 GLN B C     1 
ATOM   3055 O  O     . GLN B 1 117 ? -32.983 35.974  -13.627 1.00 25.50 ? 111 GLN B O     1 
ATOM   3056 C  CB    . GLN B 1 117 ? -31.635 34.300  -16.065 1.00 33.54 ? 111 GLN B CB    1 
ATOM   3057 C  CG    . GLN B 1 117 ? -30.397 34.297  -16.954 1.00 44.12 ? 111 GLN B CG    1 
ATOM   3058 C  CD    . GLN B 1 117 ? -29.697 32.973  -17.212 1.00 53.43 ? 111 GLN B CD    1 
ATOM   3059 O  OE1   . GLN B 1 117 ? -29.343 32.196  -16.300 1.00 45.40 ? 111 GLN B OE1   1 
ATOM   3060 N  NE2   . GLN B 1 117 ? -29.403 32.753  -18.494 1.00 42.20 ? 111 GLN B NE2   1 
ATOM   3061 N  N     . PHE B 1 118 ? -33.275 33.763  -13.308 1.00 27.45 ? 112 PHE B N     1 
ATOM   3062 C  CA    . PHE B 1 118 ? -34.546 33.913  -12.544 1.00 25.51 ? 112 PHE B CA    1 
ATOM   3063 C  C     . PHE B 1 118 ? -34.283 34.648  -11.224 1.00 26.26 ? 112 PHE B C     1 
ATOM   3064 O  O     . PHE B 1 118 ? -35.074 35.528  -10.853 1.00 28.35 ? 112 PHE B O     1 
ATOM   3065 C  CB    . PHE B 1 118 ? -35.186 32.545  -12.286 1.00 24.86 ? 112 PHE B CB    1 
ATOM   3066 C  CG    . PHE B 1 118 ? -36.588 32.619  -11.740 1.00 24.57 ? 112 PHE B CG    1 
ATOM   3067 C  CD1   . PHE B 1 118 ? -36.815 32.715  -10.381 1.00 25.33 ? 112 PHE B CD1   1 
ATOM   3068 C  CD2   . PHE B 1 118 ? -37.688 32.656  -12.587 1.00 25.73 ? 112 PHE B CD2   1 
ATOM   3069 C  CE1   . PHE B 1 118 ? -38.106 32.800  -9.872  1.00 23.71 ? 112 PHE B CE1   1 
ATOM   3070 C  CE2   . PHE B 1 118 ? -38.970 32.763  -12.086 1.00 24.36 ? 112 PHE B CE2   1 
ATOM   3071 C  CZ    . PHE B 1 118 ? -39.186 32.810  -10.724 1.00 24.02 ? 112 PHE B CZ    1 
ATOM   3072 N  N     . LEU B 1 119 ? -33.193 34.309  -10.535 1.00 29.13 ? 113 LEU B N     1 
ATOM   3073 C  CA    . LEU B 1 119 ? -32.855 34.910  -9.206  1.00 31.54 ? 113 LEU B CA    1 
ATOM   3074 C  C     . LEU B 1 119 ? -32.329 36.331  -9.392  1.00 29.75 ? 113 LEU B C     1 
ATOM   3075 O  O     . LEU B 1 119 ? -32.687 37.139  -8.574  1.00 29.84 ? 113 LEU B O     1 
ATOM   3076 C  CB    . LEU B 1 119 ? -31.868 34.021  -8.461  1.00 30.61 ? 113 LEU B CB    1 
ATOM   3077 C  CG    . LEU B 1 119 ? -32.380 32.616  -8.204  1.00 34.39 ? 113 LEU B CG    1 
ATOM   3078 C  CD1   . LEU B 1 119 ? -31.377 31.836  -7.378  1.00 38.76 ? 113 LEU B CD1   1 
ATOM   3079 C  CD2   . LEU B 1 119 ? -33.752 32.667  -7.526  1.00 34.54 ? 113 LEU B CD2   1 
ATOM   3080 N  N     . GLN B 1 120 ? -31.682 36.646  -10.512 1.00 32.34 ? 114 GLN B N     1 
ATOM   3081 C  CA    . GLN B 1 120 ? -31.337 38.042  -10.852 1.00 33.74 ? 114 GLN B CA    1 
ATOM   3082 C  C     . GLN B 1 120 ? -32.617 38.840  -11.042 1.00 33.82 ? 114 GLN B C     1 
ATOM   3083 O  O     . GLN B 1 120 ? -32.687 39.963  -10.544 1.00 33.03 ? 114 GLN B O     1 
ATOM   3084 C  CB    . GLN B 1 120 ? -30.560 38.180  -12.160 1.00 41.19 ? 114 GLN B CB    1 
ATOM   3085 C  CG    . GLN B 1 120 ? -29.333 37.292  -12.283 1.00 47.59 ? 114 GLN B CG    1 
ATOM   3086 C  CD    . GLN B 1 120 ? -28.585 37.598  -13.565 1.00 58.20 ? 114 GLN B CD    1 
ATOM   3087 O  OE1   . GLN B 1 120 ? -28.175 36.691  -14.315 1.00 53.41 ? 114 GLN B OE1   1 
ATOM   3088 N  NE2   . GLN B 1 120 ? -28.441 38.896  -13.833 1.00 53.15 ? 114 GLN B NE2   1 
ATOM   3089 N  N     . LYS B 1 121 ? -33.584 38.304  -11.793 1.00 28.77 ? 115 LYS B N     1 
ATOM   3090 C  CA    . LYS B 1 121 ? -34.823 39.058  -12.085 1.00 29.36 ? 115 LYS B CA    1 
ATOM   3091 C  C     . LYS B 1 121 ? -35.680 39.197  -10.824 1.00 27.29 ? 115 LYS B C     1 
ATOM   3092 O  O     . LYS B 1 121 ? -36.268 40.265  -10.639 1.00 29.18 ? 115 LYS B O     1 
ATOM   3093 C  CB    . LYS B 1 121 ? -35.607 38.393  -13.218 1.00 31.00 ? 115 LYS B CB    1 
ATOM   3094 C  CG    . LYS B 1 121 ? -36.738 39.224  -13.793 1.00 36.49 ? 115 LYS B CG    1 
ATOM   3095 C  CD    . LYS B 1 121 ? -36.278 40.537  -14.411 1.00 45.11 ? 115 LYS B CD    1 
ATOM   3096 C  CE    . LYS B 1 121 ? -37.381 41.293  -15.144 1.00 53.82 ? 115 LYS B CE    1 
ATOM   3097 N  NZ    . LYS B 1 121 ? -38.690 41.222  -14.441 1.00 57.60 ? 115 LYS B NZ    1 
ATOM   3098 N  N     . HIS B 1 122 ? -35.886 38.126  -10.063 1.00 25.09 ? 116 HIS B N     1 
ATOM   3099 C  CA    . HIS B 1 122 ? -36.943 38.072  -9.020  1.00 24.97 ? 116 HIS B CA    1 
ATOM   3100 C  C     . HIS B 1 122 ? -36.375 37.921  -7.597  1.00 26.48 ? 116 HIS B C     1 
ATOM   3101 O  O     . HIS B 1 122 ? -37.192 37.904  -6.673  1.00 25.38 ? 116 HIS B O     1 
ATOM   3102 C  CB    . HIS B 1 122 ? -37.920 36.913  -9.300  1.00 25.23 ? 116 HIS B CB    1 
ATOM   3103 C  CG    . HIS B 1 122 ? -38.583 37.000  -10.629 1.00 24.28 ? 116 HIS B CG    1 
ATOM   3104 N  ND1   . HIS B 1 122 ? -39.516 37.962  -10.900 1.00 25.06 ? 116 HIS B ND1   1 
ATOM   3105 C  CD2   . HIS B 1 122 ? -38.419 36.275  -11.763 1.00 25.65 ? 116 HIS B CD2   1 
ATOM   3106 C  CE1   . HIS B 1 122 ? -39.925 37.820  -12.148 1.00 28.26 ? 116 HIS B CE1   1 
ATOM   3107 N  NE2   . HIS B 1 122 ? -39.263 36.776  -12.702 1.00 26.71 ? 116 HIS B NE2   1 
ATOM   3108 N  N     . GLY B 1 123 ? -35.063 37.746  -7.446  1.00 26.08 ? 117 GLY B N     1 
ATOM   3109 C  CA    . GLY B 1 123 ? -34.402 37.426  -6.167  1.00 29.13 ? 117 GLY B CA    1 
ATOM   3110 C  C     . GLY B 1 123 ? -34.685 38.453  -5.087  1.00 28.97 ? 117 GLY B C     1 
ATOM   3111 O  O     . GLY B 1 123 ? -34.869 38.068  -3.937  1.00 27.31 ? 117 GLY B O     1 
ATOM   3112 N  N     . ARG B 1 124 ? -34.765 39.729  -5.415  1.00 30.65 ? 118 ARG B N     1 
ATOM   3113 C  CA    . ARG B 1 124 ? -35.059 40.743  -4.370  1.00 36.30 ? 118 ARG B CA    1 
ATOM   3114 C  C     . ARG B 1 124 ? -36.417 40.415  -3.709  1.00 35.90 ? 118 ARG B C     1 
ATOM   3115 O  O     . ARG B 1 124 ? -36.623 40.803  -2.561  1.00 34.72 ? 118 ARG B O     1 
ATOM   3116 C  CB    . ARG B 1 124 ? -34.963 42.160  -4.961  1.00 41.83 ? 118 ARG B CB    1 
ATOM   3117 C  CG    . ARG B 1 124 ? -36.197 42.598  -5.731  1.00 46.65 ? 118 ARG B CG    1 
ATOM   3118 C  CD    . ARG B 1 124 ? -35.935 43.783  -6.652  1.00 53.48 ? 118 ARG B CD    1 
ATOM   3119 N  NE    . ARG B 1 124 ? -37.127 44.054  -7.441  1.00 55.81 ? 118 ARG B NE    1 
ATOM   3120 C  CZ    . ARG B 1 124 ? -37.509 43.343  -8.500  1.00 57.63 ? 118 ARG B CZ    1 
ATOM   3121 N  NH1   . ARG B 1 124 ? -36.781 42.316  -8.912  1.00 56.68 ? 118 ARG B NH1   1 
ATOM   3122 N  NH2   . ARG B 1 124 ? -38.625 43.659  -9.140  1.00 58.81 ? 118 ARG B NH2   1 
ATOM   3123 N  N     . ASN B 1 125 ? -37.321 39.709  -4.393  1.00 29.27 ? 119 ASN B N     1 
ATOM   3124 C  CA    . ASN B 1 125 ? -38.706 39.482  -3.927  1.00 27.42 ? 119 ASN B CA    1 
ATOM   3125 C  C     . ASN B 1 125 ? -38.841 38.114  -3.242  1.00 24.44 ? 119 ASN B C     1 
ATOM   3126 O  O     . ASN B 1 125 ? -39.964 37.819  -2.800  1.00 25.70 ? 119 ASN B O     1 
ATOM   3127 C  CB    . ASN B 1 125 ? -39.705 39.608  -5.083  1.00 28.03 ? 119 ASN B CB    1 
ATOM   3128 C  CG    . ASN B 1 125 ? -39.832 41.040  -5.547  1.00 32.26 ? 119 ASN B CG    1 
ATOM   3129 O  OD1   . ASN B 1 125 ? -39.685 41.959  -4.738  1.00 31.57 ? 119 ASN B OD1   1 
ATOM   3130 N  ND2   . ASN B 1 125 ? -40.058 41.240  -6.837  1.00 29.78 ? 119 ASN B ND2   1 
ATOM   3131 N  N     . ILE B 1 126 ? -37.783 37.300  -3.238  1.00 24.87 ? 120 ILE B N     1 
ATOM   3132 C  CA    . ILE B 1 126 ? -37.794 35.931  -2.666  1.00 23.47 ? 120 ILE B CA    1 
ATOM   3133 C  C     . ILE B 1 126 ? -37.098 35.978  -1.312  1.00 23.61 ? 120 ILE B C     1 
ATOM   3134 O  O     . ILE B 1 126 ? -35.915 36.348  -1.289  1.00 26.10 ? 120 ILE B O     1 
ATOM   3135 C  CB    . ILE B 1 126 ? -37.090 34.933  -3.611  1.00 22.85 ? 120 ILE B CB    1 
ATOM   3136 C  CG1   . ILE B 1 126 ? -37.712 34.958  -5.018  1.00 25.18 ? 120 ILE B CG1   1 
ATOM   3137 C  CG2   . ILE B 1 126 ? -37.102 33.538  -3.016  1.00 21.31 ? 120 ILE B CG2   1 
ATOM   3138 C  CD1   . ILE B 1 126 ? -36.951 34.137  -6.033  1.00 24.19 ? 120 ILE B CD1   1 
ATOM   3139 N  N     . ASP B 1 127 ? -37.744 35.481  -0.260  1.00 23.74 ? 121 ASP B N     1 
ATOM   3140 C  CA    . ASP B 1 127 ? -37.126 35.426  1.086   1.00 24.26 ? 121 ASP B CA    1 
ATOM   3141 C  C     . ASP B 1 127 ? -36.379 34.104  1.264   1.00 22.35 ? 121 ASP B C     1 
ATOM   3142 O  O     . ASP B 1 127 ? -35.329 34.079  1.939   1.00 22.81 ? 121 ASP B O     1 
ATOM   3143 C  CB    . ASP B 1 127 ? -38.215 35.653  2.130   1.00 25.29 ? 121 ASP B CB    1 
ATOM   3144 C  CG    . ASP B 1 127 ? -38.790 37.062  2.092   1.00 30.90 ? 121 ASP B CG    1 
ATOM   3145 O  OD1   . ASP B 1 127 ? -38.041 38.001  2.500   1.00 34.49 ? 121 ASP B OD1   1 
ATOM   3146 O  OD2   . ASP B 1 127 ? -39.959 37.232  1.602   1.00 29.37 ? 121 ASP B OD2   1 
ATOM   3147 N  N     . ILE B 1 128 ? -36.976 33.008  0.809   1.00 21.96 ? 122 ILE B N     1 
ATOM   3148 C  CA    . ILE B 1 128 ? -36.524 31.623  1.103   1.00 21.97 ? 122 ILE B CA    1 
ATOM   3149 C  C     . ILE B 1 128 ? -36.633 30.784  -0.170  1.00 21.74 ? 122 ILE B C     1 
ATOM   3150 O  O     . ILE B 1 128 ? -37.702 30.761  -0.790  1.00 20.55 ? 122 ILE B O     1 
ATOM   3151 C  CB    . ILE B 1 128 ? -37.359 31.006  2.239   1.00 24.53 ? 122 ILE B CB    1 
ATOM   3152 C  CG1   . ILE B 1 128 ? -37.199 31.723  3.585   1.00 25.60 ? 122 ILE B CG1   1 
ATOM   3153 C  CG2   . ILE B 1 128 ? -37.031 29.543  2.375   1.00 22.84 ? 122 ILE B CG2   1 
ATOM   3154 C  CD1   . ILE B 1 128 ? -38.339 31.445  4.534   1.00 25.82 ? 122 ILE B CD1   1 
ATOM   3155 N  N     . LEU B 1 129 ? -35.565 30.092  -0.520  1.00 19.77 ? 123 LEU B N     1 
ATOM   3156 C  CA    . LEU B 1 129 ? -35.609 29.103  -1.613  1.00 21.57 ? 123 LEU B CA    1 
ATOM   3157 C  C     . LEU B 1 129 ? -35.261 27.772  -0.988  1.00 21.39 ? 123 LEU B C     1 
ATOM   3158 O  O     . LEU B 1 129 ? -34.166 27.657  -0.435  1.00 22.67 ? 123 LEU B O     1 
ATOM   3159 C  CB    . LEU B 1 129 ? -34.633 29.494  -2.721  1.00 23.48 ? 123 LEU B CB    1 
ATOM   3160 C  CG    . LEU B 1 129 ? -34.652 28.576  -3.936  1.00 26.69 ? 123 LEU B CG    1 
ATOM   3161 C  CD1   . LEU B 1 129 ? -36.071 28.434  -4.492  1.00 27.78 ? 123 LEU B CD1   1 
ATOM   3162 C  CD2   . LEU B 1 129 ? -33.719 29.098  -4.997  1.00 28.21 ? 123 LEU B CD2   1 
ATOM   3163 N  N     . ALA B 1 130 ? -36.170 26.808  -1.036  1.00 19.37 ? 124 ALA B N     1 
ATOM   3164 C  CA    . ALA B 1 130 ? -35.961 25.443  -0.510  1.00 19.56 ? 124 ALA B CA    1 
ATOM   3165 C  C     . ALA B 1 130 ? -35.712 24.506  -1.691  1.00 20.30 ? 124 ALA B C     1 
ATOM   3166 O  O     . ALA B 1 130 ? -36.499 24.519  -2.643  1.00 20.89 ? 124 ALA B O     1 
ATOM   3167 C  CB    . ALA B 1 130 ? -37.135 25.013  0.325   1.00 19.39 ? 124 ALA B CB    1 
ATOM   3168 N  N     . VAL B 1 131 ? -34.640 23.727  -1.628  1.00 19.06 ? 125 VAL B N     1 
ATOM   3169 C  CA    . VAL B 1 131 ? -34.325 22.706  -2.642  1.00 19.52 ? 125 VAL B CA    1 
ATOM   3170 C  C     . VAL B 1 131 ? -34.497 21.347  -2.009  1.00 20.64 ? 125 VAL B C     1 
ATOM   3171 O  O     . VAL B 1 131 ? -33.994 21.094  -0.885  1.00 19.51 ? 125 VAL B O     1 
ATOM   3172 C  CB    . VAL B 1 131 ? -32.932 22.848  -3.266  1.00 21.44 ? 125 VAL B CB    1 
ATOM   3173 C  CG1   . VAL B 1 131 ? -32.763 21.831  -4.387  1.00 21.30 ? 125 VAL B CG1   1 
ATOM   3174 C  CG2   . VAL B 1 131 ? -32.670 24.280  -3.737  1.00 23.03 ? 125 VAL B CG2   1 
ATOM   3175 N  N     . SER B 1 132 ? -35.240 20.490  -2.701  1.00 19.91 ? 126 SER B N     1 
ATOM   3176 C  CA    . SER B 1 132 ? -35.372 19.076  -2.294  1.00 20.27 ? 126 SER B CA    1 
ATOM   3177 C  C     . SER B 1 132 ? -34.085 18.326  -2.628  1.00 23.83 ? 126 SER B C     1 
ATOM   3178 O  O     . SER B 1 132 ? -33.641 18.394  -3.783  1.00 23.70 ? 126 SER B O     1 
ATOM   3179 C  CB    . SER B 1 132 ? -36.561 18.433  -2.908  1.00 19.78 ? 126 SER B CB    1 
ATOM   3180 O  OG    . SER B 1 132 ? -37.700 18.966  -2.273  1.00 20.93 ? 126 SER B OG    1 
ATOM   3181 N  N     . CYS B 1 133 ? -33.520 17.628  -1.645  1.00 23.86 ? 127 CYS B N     1 
ATOM   3182 C  CA    . CYS B 1 133 ? -32.315 16.775  -1.823  1.00 24.23 ? 127 CYS B CA    1 
ATOM   3183 C  C     . CYS B 1 133 ? -32.488 15.566  -0.933  1.00 24.74 ? 127 CYS B C     1 
ATOM   3184 O  O     . CYS B 1 133 ? -32.319 15.690  0.294   1.00 23.57 ? 127 CYS B O     1 
ATOM   3185 C  CB    . CYS B 1 133 ? -31.034 17.502  -1.465  1.00 26.99 ? 127 CYS B CB    1 
ATOM   3186 S  SG    . CYS B 1 133 ? -29.561 16.490  -1.807  1.00 32.43 ? 127 CYS B SG    1 
ATOM   3187 N  N     . ASP B 1 134 ? -32.823 14.438  -1.538  1.00 22.74 ? 128 ASP B N     1 
ATOM   3188 C  CA    . ASP B 1 134 ? -33.007 13.176  -0.800  1.00 22.33 ? 128 ASP B CA    1 
ATOM   3189 C  C     . ASP B 1 134 ? -31.681 12.429  -0.668  1.00 23.12 ? 128 ASP B C     1 
ATOM   3190 O  O     . ASP B 1 134 ? -31.625 11.549  0.162   1.00 23.61 ? 128 ASP B O     1 
ATOM   3191 C  CB    . ASP B 1 134 ? -34.082 12.316  -1.422  1.00 24.62 ? 128 ASP B CB    1 
ATOM   3192 C  CG    . ASP B 1 134 ? -35.429 13.023  -1.368  1.00 29.07 ? 128 ASP B CG    1 
ATOM   3193 O  OD1   . ASP B 1 134 ? -35.598 13.904  -0.448  1.00 25.66 ? 128 ASP B OD1   1 
ATOM   3194 O  OD2   . ASP B 1 134 ? -36.256 12.776  -2.304  1.00 28.12 ? 128 ASP B OD2   1 
ATOM   3195 N  N     . SER B 1 135 ? -30.682 12.721  -1.491  1.00 22.01 ? 129 SER B N     1 
ATOM   3196 C  CA    . SER B 1 135 ? -29.409 11.971  -1.464  1.00 23.25 ? 129 SER B CA    1 
ATOM   3197 C  C     . SER B 1 135 ? -28.346 12.760  -2.182  1.00 22.45 ? 129 SER B C     1 
ATOM   3198 O  O     . SER B 1 135 ? -28.687 13.459  -3.162  1.00 20.92 ? 129 SER B O     1 
ATOM   3199 C  CB    . SER B 1 135 ? -29.532 10.620  -2.090  1.00 23.63 ? 129 SER B CB    1 
ATOM   3200 O  OG    . SER B 1 135 ? -28.304 9.904   -1.995  1.00 23.49 ? 129 SER B OG    1 
ATOM   3201 N  N     . PHE B 1 136 ? -27.108 12.592  -1.714  1.00 23.79 ? 130 PHE B N     1 
ATOM   3202 C  CA    . PHE B 1 136 ? -25.893 13.135  -2.369  1.00 23.15 ? 130 PHE B CA    1 
ATOM   3203 C  C     . PHE B 1 136 ? -25.280 12.047  -3.261  1.00 23.39 ? 130 PHE B C     1 
ATOM   3204 O  O     . PHE B 1 136 ? -24.261 12.362  -3.884  1.00 26.69 ? 130 PHE B O     1 
ATOM   3205 C  CB    . PHE B 1 136 ? -24.938 13.698  -1.305  1.00 22.75 ? 130 PHE B CB    1 
ATOM   3206 C  CG    . PHE B 1 136 ? -25.489 14.915  -0.617  1.00 24.42 ? 130 PHE B CG    1 
ATOM   3207 C  CD1   . PHE B 1 136 ? -26.307 14.790  0.501   1.00 23.73 ? 130 PHE B CD1   1 
ATOM   3208 C  CD2   . PHE B 1 136 ? -25.222 16.180  -1.101  1.00 25.43 ? 130 PHE B CD2   1 
ATOM   3209 C  CE1   . PHE B 1 136 ? -26.823 15.903  1.131   1.00 21.52 ? 130 PHE B CE1   1 
ATOM   3210 C  CE2   . PHE B 1 136 ? -25.755 17.286  -0.479  1.00 25.58 ? 130 PHE B CE2   1 
ATOM   3211 C  CZ    . PHE B 1 136 ? -26.568 17.139  0.618   1.00 24.24 ? 130 PHE B CZ    1 
ATOM   3212 N  N     . ASN B 1 137 ? -25.904 10.865  -3.361  1.00 24.39 ? 131 ASN B N     1 
ATOM   3213 C  CA    . ASN B 1 137 ? -25.416 9.707   -4.154  1.00 24.48 ? 131 ASN B CA    1 
ATOM   3214 C  C     . ASN B 1 137 ? -26.318 9.461   -5.371  1.00 25.60 ? 131 ASN B C     1 
ATOM   3215 O  O     . ASN B 1 137 ? -27.552 9.243   -5.212  1.00 22.10 ? 131 ASN B O     1 
ATOM   3216 C  CB    . ASN B 1 137 ? -25.276 8.463   -3.280  1.00 23.73 ? 131 ASN B CB    1 
ATOM   3217 C  CG    . ASN B 1 137 ? -24.161 8.621   -2.265  1.00 27.45 ? 131 ASN B CG    1 
ATOM   3218 O  OD1   . ASN B 1 137 ? -23.228 9.392   -2.469  1.00 27.40 ? 131 ASN B OD1   1 
ATOM   3219 N  ND2   . ASN B 1 137 ? -24.230 7.878   -1.186  1.00 26.72 ? 131 ASN B ND2   1 
ATOM   3220 N  N     . GLU B 1 138 ? -25.706 9.436   -6.560  1.00 25.63 ? 132 GLU B N     1 
ATOM   3221 C  CA    . GLU B 1 138 ? -26.412 9.174   -7.851  1.00 28.12 ? 132 GLU B CA    1 
ATOM   3222 C  C     . GLU B 1 138 ? -27.241 7.907   -7.767  1.00 24.95 ? 132 GLU B C     1 
ATOM   3223 O  O     . GLU B 1 138 ? -28.427 7.949   -8.159  1.00 28.28 ? 132 GLU B O     1 
ATOM   3224 C  CB    . GLU B 1 138 ? -25.445 9.022   -9.036  1.00 30.79 ? 132 GLU B CB    1 
ATOM   3225 C  CG    . GLU B 1 138 ? -24.896 10.356  -9.482  1.00 36.24 ? 132 GLU B CG    1 
ATOM   3226 C  CD    . GLU B 1 138 ? -23.803 10.326  -10.551 1.00 39.08 ? 132 GLU B CD    1 
ATOM   3227 O  OE1   . GLU B 1 138 ? -23.542 9.209   -11.099 1.00 33.47 ? 132 GLU B OE1   1 
ATOM   3228 O  OE2   . GLU B 1 138 ? -23.185 11.418  -10.791 1.00 29.81 ? 132 GLU B OE2   1 
ATOM   3229 N  N     . ALA B 1 139 ? -26.670 6.789   -7.329  1.00 25.39 ? 133 ALA B N     1 
ATOM   3230 C  CA    . ALA B 1 139 ? -27.372 5.489   -7.348  1.00 26.44 ? 133 ALA B CA    1 
ATOM   3231 C  C     . ALA B 1 139 ? -28.666 5.587   -6.520  1.00 26.92 ? 133 ALA B C     1 
ATOM   3232 O  O     . ALA B 1 139 ? -29.685 5.011   -6.892  1.00 26.04 ? 133 ALA B O     1 
ATOM   3233 C  CB    . ALA B 1 139 ? -26.483 4.396   -6.812  1.00 30.13 ? 133 ALA B CB    1 
ATOM   3234 N  N     . THR B 1 140 ? -28.622 6.325   -5.424  1.00 24.00 ? 134 THR B N     1 
ATOM   3235 C  CA    . THR B 1 140 ? -29.768 6.447   -4.491  1.00 22.80 ? 134 THR B CA    1 
ATOM   3236 C  C     . THR B 1 140 ? -30.843 7.315   -5.163  1.00 19.95 ? 134 THR B C     1 
ATOM   3237 O  O     . THR B 1 140 ? -32.040 6.934   -5.128  1.00 24.23 ? 134 THR B O     1 
ATOM   3238 C  CB    . THR B 1 140 ? -29.291 6.999   -3.141  1.00 23.51 ? 134 THR B CB    1 
ATOM   3239 O  OG1   . THR B 1 140 ? -28.287 6.144   -2.582  1.00 25.83 ? 134 THR B OG1   1 
ATOM   3240 C  CG2   . THR B 1 140 ? -30.428 7.123   -2.161  1.00 23.76 ? 134 THR B CG2   1 
ATOM   3241 N  N     . ASN B 1 141 ? -30.443 8.443   -5.720  1.00 21.25 ? 135 ASN B N     1 
ATOM   3242 C  CA    . ASN B 1 141 ? -31.352 9.325   -6.491  1.00 22.48 ? 135 ASN B CA    1 
ATOM   3243 C  C     . ASN B 1 141 ? -32.014 8.518   -7.603  1.00 23.51 ? 135 ASN B C     1 
ATOM   3244 O  O     . ASN B 1 141 ? -33.207 8.731   -7.849  1.00 21.78 ? 135 ASN B O     1 
ATOM   3245 C  CB    . ASN B 1 141 ? -30.664 10.590  -6.975  1.00 21.65 ? 135 ASN B CB    1 
ATOM   3246 C  CG    . ASN B 1 141 ? -30.510 11.561  -5.833  1.00 23.89 ? 135 ASN B CG    1 
ATOM   3247 O  OD1   . ASN B 1 141 ? -31.366 11.609  -4.941  1.00 22.86 ? 135 ASN B OD1   1 
ATOM   3248 N  ND2   . ASN B 1 141 ? -29.422 12.308  -5.824  1.00 25.04 ? 135 ASN B ND2   1 
ATOM   3249 N  N     . ILE B 1 142 ? -31.267 7.668   -8.294  1.00 23.69 ? 136 ILE B N     1 
ATOM   3250 C  CA    . ILE B 1 142 ? -31.852 6.867   -9.400  1.00 23.45 ? 136 ILE B CA    1 
ATOM   3251 C  C     . ILE B 1 142 ? -32.947 5.970   -8.838  1.00 22.40 ? 136 ILE B C     1 
ATOM   3252 O  O     . ILE B 1 142 ? -34.061 5.966   -9.432  1.00 23.22 ? 136 ILE B O     1 
ATOM   3253 C  CB    . ILE B 1 142 ? -30.776 6.098   -10.183 1.00 24.65 ? 136 ILE B CB    1 
ATOM   3254 C  CG1   . ILE B 1 142 ? -29.934 7.091   -10.972 1.00 27.30 ? 136 ILE B CG1   1 
ATOM   3255 C  CG2   . ILE B 1 142 ? -31.456 5.042   -11.055 1.00 27.63 ? 136 ILE B CG2   1 
ATOM   3256 C  CD1   . ILE B 1 142 ? -28.660 6.502   -11.557 1.00 30.11 ? 136 ILE B CD1   1 
ATOM   3257 N  N     . LYS B 1 143 ? -32.720 5.302   -7.720  1.00 21.61 ? 137 LYS B N     1 
ATOM   3258 C  CA    . LYS B 1 143 ? -33.725 4.357   -7.161  1.00 23.93 ? 137 LYS B CA    1 
ATOM   3259 C  C     . LYS B 1 143 ? -34.952 5.117   -6.676  1.00 24.09 ? 137 LYS B C     1 
ATOM   3260 O  O     . LYS B 1 143 ? -36.057 4.602   -6.841  1.00 24.50 ? 137 LYS B O     1 
ATOM   3261 C  CB    . LYS B 1 143 ? -33.155 3.533   -6.018  1.00 26.59 ? 137 LYS B CB    1 
ATOM   3262 C  CG    . LYS B 1 143 ? -32.238 2.415   -6.505  1.00 34.65 ? 137 LYS B CG    1 
ATOM   3263 C  CD    . LYS B 1 143 ? -31.716 1.559   -5.392  1.00 36.91 ? 137 LYS B CD    1 
ATOM   3264 C  CE    . LYS B 1 143 ? -30.382 2.024   -4.864  1.00 45.12 ? 137 LYS B CE    1 
ATOM   3265 N  NZ    . LYS B 1 143 ? -29.583 0.846   -4.451  1.00 51.57 ? 137 LYS B NZ    1 
ATOM   3266 N  N     . ILE B 1 144 ? -34.756 6.303   -6.121  1.00 21.17 ? 138 ILE B N     1 
ATOM   3267 C  CA    . ILE B 1 144 ? -35.901 7.091   -5.574  1.00 22.29 ? 138 ILE B CA    1 
ATOM   3268 C  C     . ILE B 1 144 ? -36.786 7.589   -6.729  1.00 21.96 ? 138 ILE B C     1 
ATOM   3269 O  O     . ILE B 1 144 ? -38.011 7.734   -6.498  1.00 22.26 ? 138 ILE B O     1 
ATOM   3270 C  CB    . ILE B 1 144 ? -35.358 8.215   -4.686  1.00 21.92 ? 138 ILE B CB    1 
ATOM   3271 C  CG1   . ILE B 1 144 ? -34.789 7.668   -3.375  1.00 24.35 ? 138 ILE B CG1   1 
ATOM   3272 C  CG2   . ILE B 1 144 ? -36.395 9.304   -4.442  1.00 22.54 ? 138 ILE B CG2   1 
ATOM   3273 C  CD1   . ILE B 1 144 ? -33.902 8.689   -2.666  1.00 25.28 ? 138 ILE B CD1   1 
ATOM   3274 N  N     . GLY B 1 145 ? -36.214 7.918   -7.883  1.00 23.22 ? 139 GLY B N     1 
ATOM   3275 C  CA    . GLY B 1 145 ? -36.937 8.586   -8.992  1.00 25.19 ? 139 GLY B CA    1 
ATOM   3276 C  C     . GLY B 1 145 ? -36.580 10.046  -9.145  1.00 21.68 ? 139 GLY B C     1 
ATOM   3277 O  O     . GLY B 1 145 ? -37.217 10.720  -9.974  1.00 21.68 ? 139 GLY B O     1 
ATOM   3278 N  N     . ARG B 1 146 ? -35.516 10.519  -8.473  1.00 22.14 ? 140 ARG B N     1 
ATOM   3279 C  CA    . ARG B 1 146 ? -35.030 11.913  -8.601  1.00 22.08 ? 140 ARG B CA    1 
ATOM   3280 C  C     . ARG B 1 146 ? -34.108 12.041  -9.822  1.00 23.52 ? 140 ARG B C     1 
ATOM   3281 O  O     . ARG B 1 146 ? -33.792 13.182  -10.183 1.00 26.42 ? 140 ARG B O     1 
ATOM   3282 C  CB    . ARG B 1 146 ? -34.292 12.374  -7.336  1.00 22.90 ? 140 ARG B CB    1 
ATOM   3283 C  CG    . ARG B 1 146 ? -35.141 12.512  -6.075  1.00 24.18 ? 140 ARG B CG    1 
ATOM   3284 C  CD    . ARG B 1 146 ? -35.686 13.919  -5.996  1.00 25.67 ? 140 ARG B CD    1 
ATOM   3285 N  NE    . ARG B 1 146 ? -36.418 14.088  -4.747  1.00 26.64 ? 140 ARG B NE    1 
ATOM   3286 C  CZ    . ARG B 1 146 ? -37.301 15.038  -4.482  1.00 26.98 ? 140 ARG B CZ    1 
ATOM   3287 N  NH1   . ARG B 1 146 ? -37.519 16.018  -5.338  1.00 28.01 ? 140 ARG B NH1   1 
ATOM   3288 N  NH2   . ARG B 1 146 ? -37.934 15.019  -3.320  1.00 26.82 ? 140 ARG B NH2   1 
ATOM   3289 N  N     . GLY B 1 147 ? -33.655 10.927  -10.399 1.00 25.85 ? 141 GLY B N     1 
ATOM   3290 C  CA    . GLY B 1 147 ? -32.888 10.907  -11.661 1.00 27.55 ? 141 GLY B CA    1 
ATOM   3291 C  C     . GLY B 1 147 ? -31.385 10.788  -11.459 1.00 27.99 ? 141 GLY B C     1 
ATOM   3292 O  O     . GLY B 1 147 ? -30.938 10.779  -10.308 1.00 26.58 ? 141 GLY B O     1 
ATOM   3293 N  N     . SER B 1 148 ? -30.612 10.760  -12.556 1.00 27.90 ? 142 SER B N     1 
ATOM   3294 C  CA    . SER B 1 148 ? -29.153 10.446  -12.561 1.00 30.87 ? 142 SER B CA    1 
ATOM   3295 C  C     . SER B 1 148 ? -28.295 11.709  -12.741 1.00 31.71 ? 142 SER B C     1 
ATOM   3296 O  O     . SER B 1 148 ? -27.065 11.579  -12.849 1.00 37.85 ? 142 SER B O     1 
ATOM   3297 C  CB    . SER B 1 148 ? -28.880 9.473   -13.667 1.00 34.75 ? 142 SER B CB    1 
ATOM   3298 O  OG    . SER B 1 148 ? -29.278 10.058  -14.898 1.00 32.14 ? 142 SER B OG    1 
ATOM   3299 N  N     . GLY B 1 149 ? -28.915 12.884  -12.809 1.00 31.86 ? 143 GLY B N     1 
ATOM   3300 C  CA    . GLY B 1 149 ? -28.232 14.171  -13.045 1.00 32.19 ? 143 GLY B CA    1 
ATOM   3301 C  C     . GLY B 1 149 ? -27.343 14.584  -11.883 1.00 30.38 ? 143 GLY B C     1 
ATOM   3302 O  O     . GLY B 1 149 ? -27.395 13.956  -10.804 1.00 28.26 ? 143 GLY B O     1 
ATOM   3303 N  N     . ASP B 1 150 ? -26.538 15.623  -12.103 1.00 32.99 ? 144 ASP B N     1 
ATOM   3304 C  CA    . ASP B 1 150 ? -25.575 16.144  -11.100 1.00 32.06 ? 144 ASP B CA    1 
ATOM   3305 C  C     . ASP B 1 150 ? -26.347 17.110  -10.173 1.00 28.70 ? 144 ASP B C     1 
ATOM   3306 O  O     . ASP B 1 150 ? -26.124 18.322  -10.268 1.00 24.55 ? 144 ASP B O     1 
ATOM   3307 C  CB    . ASP B 1 150 ? -24.355 16.772  -11.793 1.00 33.78 ? 144 ASP B CB    1 
ATOM   3308 C  CG    . ASP B 1 150 ? -23.225 17.086  -10.819 1.00 43.50 ? 144 ASP B CG    1 
ATOM   3309 O  OD1   . ASP B 1 150 ? -23.418 16.859  -9.577  1.00 39.52 ? 144 ASP B OD1   1 
ATOM   3310 O  OD2   . ASP B 1 150 ? -22.162 17.563  -11.290 1.00 43.16 ? 144 ASP B OD2   1 
ATOM   3311 N  N     . ASN B 1 151 ? -27.225 16.576  -9.317  1.00 28.97 ? 145 ASN B N     1 
ATOM   3312 C  CA    . ASN B 1 151 ? -28.056 17.384  -8.376  1.00 30.12 ? 145 ASN B CA    1 
ATOM   3313 C  C     . ASN B 1 151 ? -27.150 18.095  -7.358  1.00 28.55 ? 145 ASN B C     1 
ATOM   3314 O  O     . ASN B 1 151 ? -27.431 19.255  -7.003  1.00 28.60 ? 145 ASN B O     1 
ATOM   3315 C  CB    . ASN B 1 151 ? -29.122 16.518  -7.698  1.00 29.86 ? 145 ASN B CB    1 
ATOM   3316 C  CG    . ASN B 1 151 ? -28.554 15.676  -6.582  1.00 34.94 ? 145 ASN B CG    1 
ATOM   3317 O  OD1   . ASN B 1 151 ? -27.773 14.763  -6.847  1.00 32.80 ? 145 ASN B OD1   1 
ATOM   3318 N  ND2   . ASN B 1 151 ? -28.892 16.013  -5.344  1.00 28.68 ? 145 ASN B ND2   1 
ATOM   3319 N  N     . VAL B 1 152 ? -26.029 17.485  -6.974  1.00 28.45 ? 146 VAL B N     1 
ATOM   3320 C  CA    . VAL B 1 152 ? -25.153 18.064  -5.920  1.00 27.54 ? 146 VAL B CA    1 
ATOM   3321 C  C     . VAL B 1 152 ? -24.487 19.318  -6.480  1.00 27.21 ? 146 VAL B C     1 
ATOM   3322 O  O     . VAL B 1 152 ? -24.499 20.352  -5.811  1.00 24.25 ? 146 VAL B O     1 
ATOM   3323 C  CB    . VAL B 1 152 ? -24.151 17.027  -5.380  1.00 29.75 ? 146 VAL B CB    1 
ATOM   3324 C  CG1   . VAL B 1 152 ? -23.194 17.631  -4.360  1.00 31.28 ? 146 VAL B CG1   1 
ATOM   3325 C  CG2   . VAL B 1 152 ? -24.888 15.836  -4.791  1.00 32.43 ? 146 VAL B CG2   1 
ATOM   3326 N  N     . GLN B 1 153 ? -23.952 19.279  -7.704  1.00 26.83 ? 147 GLN B N     1 
ATOM   3327 C  CA    . GLN B 1 153 ? -23.368 20.517  -8.275  1.00 24.12 ? 147 GLN B CA    1 
ATOM   3328 C  C     . GLN B 1 153 ? -24.425 21.618  -8.314  1.00 22.92 ? 147 GLN B C     1 
ATOM   3329 O  O     . GLN B 1 153 ? -24.075 22.777  -8.016  1.00 22.33 ? 147 GLN B O     1 
ATOM   3330 C  CB    . GLN B 1 153 ? -22.821 20.245  -9.663  1.00 28.08 ? 147 GLN B CB    1 
ATOM   3331 C  CG    . GLN B 1 153 ? -22.344 21.481  -10.381 1.00 32.37 ? 147 GLN B CG    1 
ATOM   3332 C  CD    . GLN B 1 153 ? -21.756 21.053  -11.701 1.00 38.44 ? 147 GLN B CD    1 
ATOM   3333 O  OE1   . GLN B 1 153 ? -20.551 21.083  -11.894 1.00 46.70 ? 147 GLN B OE1   1 
ATOM   3334 N  NE2   . GLN B 1 153 ? -22.617 20.629  -12.610 1.00 46.53 ? 147 GLN B NE2   1 
ATOM   3335 N  N     . LYS B 1 154 ? -25.669 21.280  -8.691  1.00 23.87 ? 148 LYS B N     1 
ATOM   3336 C  CA    . LYS B 1 154 ? -26.771 22.277  -8.822  1.00 25.32 ? 148 LYS B CA    1 
ATOM   3337 C  C     . LYS B 1 154 ? -27.127 22.849  -7.438  1.00 22.28 ? 148 LYS B C     1 
ATOM   3338 O  O     . LYS B 1 154 ? -27.382 24.037  -7.314  1.00 23.09 ? 148 LYS B O     1 
ATOM   3339 C  CB    . LYS B 1 154 ? -27.998 21.642  -9.495  1.00 26.01 ? 148 LYS B CB    1 
ATOM   3340 C  CG    . LYS B 1 154 ? -29.208 22.552  -9.509  1.00 29.40 ? 148 LYS B CG    1 
ATOM   3341 C  CD    . LYS B 1 154 ? -28.922 23.869  -10.141 1.00 29.70 ? 148 LYS B CD    1 
ATOM   3342 C  CE    . LYS B 1 154 ? -29.056 23.828  -11.635 1.00 34.98 ? 148 LYS B CE    1 
ATOM   3343 N  NZ    . LYS B 1 154 ? -30.433 24.207  -12.024 1.00 34.37 ? 148 LYS B NZ    1 
ATOM   3344 N  N     . LEU B 1 155 ? -27.057 22.016  -6.413  1.00 24.57 ? 149 LEU B N     1 
ATOM   3345 C  CA    . LEU B 1 155 ? -27.367 22.409  -5.029  1.00 27.66 ? 149 LEU B CA    1 
ATOM   3346 C  C     . LEU B 1 155 ? -26.335 23.432  -4.535  1.00 24.77 ? 149 LEU B C     1 
ATOM   3347 O  O     . LEU B 1 155 ? -26.739 24.492  -4.029  1.00 26.22 ? 149 LEU B O     1 
ATOM   3348 C  CB    . LEU B 1 155 ? -27.404 21.105  -4.228  1.00 30.81 ? 149 LEU B CB    1 
ATOM   3349 C  CG    . LEU B 1 155 ? -28.085 21.191  -2.879  1.00 35.14 ? 149 LEU B CG    1 
ATOM   3350 C  CD1   . LEU B 1 155 ? -29.525 21.678  -3.035  1.00 33.88 ? 149 LEU B CD1   1 
ATOM   3351 C  CD2   . LEU B 1 155 ? -28.024 19.837  -2.180  1.00 35.14 ? 149 LEU B CD2   1 
ATOM   3352 N  N     . TYR B 1 156 ? -25.026 23.197  -4.734  1.00 29.67 ? 150 TYR B N     1 
ATOM   3353 C  CA    . TYR B 1 156 ? -23.960 24.167  -4.349  1.00 28.74 ? 150 TYR B CA    1 
ATOM   3354 C  C     . TYR B 1 156 ? -24.159 25.443  -5.169  1.00 29.10 ? 150 TYR B C     1 
ATOM   3355 O  O     . TYR B 1 156 ? -24.036 26.544  -4.608  1.00 28.71 ? 150 TYR B O     1 
ATOM   3356 C  CB    . TYR B 1 156 ? -22.576 23.504  -4.390  1.00 31.81 ? 150 TYR B CB    1 
ATOM   3357 C  CG    . TYR B 1 156 ? -22.291 22.590  -3.212  1.00 31.50 ? 150 TYR B CG    1 
ATOM   3358 C  CD1   . TYR B 1 156 ? -22.745 21.286  -3.187  1.00 30.39 ? 150 TYR B CD1   1 
ATOM   3359 C  CD2   . TYR B 1 156 ? -21.617 23.041  -2.080  1.00 35.27 ? 150 TYR B CD2   1 
ATOM   3360 C  CE1   . TYR B 1 156 ? -22.525 20.443  -2.107  1.00 33.93 ? 150 TYR B CE1   1 
ATOM   3361 C  CE2   . TYR B 1 156 ? -21.388 22.211  -0.984  1.00 33.51 ? 150 TYR B CE2   1 
ATOM   3362 C  CZ    . TYR B 1 156 ? -21.846 20.906  -0.997  1.00 33.84 ? 150 TYR B CZ    1 
ATOM   3363 O  OH    . TYR B 1 156 ? -21.640 20.038  0.045   1.00 33.04 ? 150 TYR B OH    1 
ATOM   3364 N  N     . GLU B 1 157 ? -24.572 25.339  -6.445  1.00 29.02 ? 151 GLU B N     1 
ATOM   3365 C  CA    . GLU B 1 157 ? -24.771 26.540  -7.283  1.00 27.91 ? 151 GLU B CA    1 
ATOM   3366 C  C     . GLU B 1 157 ? -25.922 27.369  -6.723  1.00 24.27 ? 151 GLU B C     1 
ATOM   3367 O  O     . GLU B 1 157 ? -25.780 28.594  -6.649  1.00 26.18 ? 151 GLU B O     1 
ATOM   3368 C  CB    . GLU B 1 157 ? -25.080 26.193  -8.735  1.00 32.11 ? 151 GLU B CB    1 
ATOM   3369 C  CG    . GLU B 1 157 ? -23.876 25.703  -9.531  1.00 39.48 ? 151 GLU B CG    1 
ATOM   3370 C  CD    . GLU B 1 157 ? -24.236 25.151  -10.914 1.00 46.19 ? 151 GLU B CD    1 
ATOM   3371 O  OE1   . GLU B 1 157 ? -25.442 25.107  -11.246 1.00 46.13 ? 151 GLU B OE1   1 
ATOM   3372 O  OE2   . GLU B 1 157 ? -23.305 24.742  -11.657 1.00 50.63 ? 151 GLU B OE2   1 
ATOM   3373 N  N     . ILE B 1 158 ? -27.079 26.740  -6.465  1.00 24.03 ? 152 ILE B N     1 
ATOM   3374 C  CA    . ILE B 1 158 ? -28.227 27.485  -5.900  1.00 23.76 ? 152 ILE B CA    1 
ATOM   3375 C  C     . ILE B 1 158 ? -27.845 28.178  -4.576  1.00 22.59 ? 152 ILE B C     1 
ATOM   3376 O  O     . ILE B 1 158 ? -28.236 29.354  -4.357  1.00 26.42 ? 152 ILE B O     1 
ATOM   3377 C  CB    . ILE B 1 158 ? -29.440 26.554  -5.782  1.00 23.23 ? 152 ILE B CB    1 
ATOM   3378 C  CG1   . ILE B 1 158 ? -29.929 26.124  -7.170  1.00 24.83 ? 152 ILE B CG1   1 
ATOM   3379 C  CG2   . ILE B 1 158 ? -30.519 27.253  -4.949  1.00 23.23 ? 152 ILE B CG2   1 
ATOM   3380 C  CD1   . ILE B 1 158 ? -30.914 24.955  -7.169  1.00 26.31 ? 152 ILE B CD1   1 
ATOM   3381 N  N     . GLY B 1 159 ? -27.145 27.473  -3.692  1.00 26.49 ? 153 GLY B N     1 
ATOM   3382 C  CA    . GLY B 1 159 ? -26.690 27.989  -2.385  1.00 30.17 ? 153 GLY B CA    1 
ATOM   3383 C  C     . GLY B 1 159 ? -25.860 29.244  -2.573  1.00 27.81 ? 153 GLY B C     1 
ATOM   3384 O  O     . GLY B 1 159 ? -26.138 30.246  -1.897  1.00 29.49 ? 153 GLY B O     1 
ATOM   3385 N  N     . SER B 1 160 ? -24.952 29.240  -3.549  1.00 28.76 ? 154 SER B N     1 
ATOM   3386 C  CA    . SER B 1 160 ? -24.141 30.426  -3.923  1.00 29.82 ? 154 SER B CA    1 
ATOM   3387 C  C     . SER B 1 160 ? -25.033 31.554  -4.450  1.00 29.02 ? 154 SER B C     1 
ATOM   3388 O  O     . SER B 1 160 ? -24.869 32.675  -3.984  1.00 28.59 ? 154 SER B O     1 
ATOM   3389 C  CB    . SER B 1 160 ? -23.058 30.099  -4.896  1.00 34.58 ? 154 SER B CB    1 
ATOM   3390 O  OG    . SER B 1 160 ? -22.328 31.294  -5.177  1.00 39.83 ? 154 SER B OG    1 
ATOM   3391 N  N     . TRP B 1 161 ? -25.987 31.284  -5.354  1.00 26.27 ? 155 TRP B N     1 
ATOM   3392 C  CA    . TRP B 1 161 ? -26.922 32.329  -5.845  1.00 27.56 ? 155 TRP B CA    1 
ATOM   3393 C  C     . TRP B 1 161 ? -27.732 32.924  -4.686  1.00 25.05 ? 155 TRP B C     1 
ATOM   3394 O  O     . TRP B 1 161 ? -27.978 34.137  -4.698  1.00 25.21 ? 155 TRP B O     1 
ATOM   3395 C  CB    . TRP B 1 161 ? -27.843 31.786  -6.947  1.00 28.67 ? 155 TRP B CB    1 
ATOM   3396 C  CG    . TRP B 1 161 ? -27.109 31.256  -8.135  1.00 33.49 ? 155 TRP B CG    1 
ATOM   3397 C  CD1   . TRP B 1 161 ? -25.887 31.665  -8.586  1.00 34.46 ? 155 TRP B CD1   1 
ATOM   3398 C  CD2   . TRP B 1 161 ? -27.556 30.236  -9.048  1.00 32.25 ? 155 TRP B CD2   1 
ATOM   3399 N  NE1   . TRP B 1 161 ? -25.532 30.952  -9.697  1.00 35.92 ? 155 TRP B NE1   1 
ATOM   3400 C  CE2   . TRP B 1 161 ? -26.535 30.068  -10.006 1.00 36.84 ? 155 TRP B CE2   1 
ATOM   3401 C  CE3   . TRP B 1 161 ? -28.719 29.457  -9.157  1.00 33.26 ? 155 TRP B CE3   1 
ATOM   3402 C  CZ2   . TRP B 1 161 ? -26.641 29.141  -11.046 1.00 34.88 ? 155 TRP B CZ2   1 
ATOM   3403 C  CZ3   . TRP B 1 161 ? -28.809 28.525  -10.168 1.00 31.83 ? 155 TRP B CZ3   1 
ATOM   3404 C  CH2   . TRP B 1 161 ? -27.781 28.367  -11.094 1.00 32.31 ? 155 TRP B CH2   1 
ATOM   3405 N  N     . CYS B 1 162 ? -28.203 32.118  -3.728  1.00 26.05 ? 156 CYS B N     1 
ATOM   3406 C  CA    . CYS B 1 162 ? -28.990 32.634  -2.582  1.00 24.18 ? 156 CYS B CA    1 
ATOM   3407 C  C     . CYS B 1 162 ? -28.162 33.688  -1.821  1.00 25.14 ? 156 CYS B C     1 
ATOM   3408 O  O     . CYS B 1 162 ? -28.705 34.717  -1.387  1.00 28.73 ? 156 CYS B O     1 
ATOM   3409 C  CB    . CYS B 1 162 ? -29.379 31.479  -1.671  1.00 28.07 ? 156 CYS B CB    1 
ATOM   3410 S  SG    . CYS B 1 162 ? -30.708 30.484  -2.411  1.00 29.41 ? 156 CYS B SG    1 
ATOM   3411 N  N     . GLN B 1 163 ? -26.865 33.447  -1.667  1.00 26.56 ? 157 GLN B N     1 
ATOM   3412 C  CA    . GLN B 1 163 ? -25.970 34.396  -0.964  1.00 29.91 ? 157 GLN B CA    1 
ATOM   3413 C  C     . GLN B 1 163 ? -25.935 35.718  -1.739  1.00 30.41 ? 157 GLN B C     1 
ATOM   3414 O  O     . GLN B 1 163 ? -26.128 36.784  -1.125  1.00 38.14 ? 157 GLN B O     1 
ATOM   3415 C  CB    . GLN B 1 163 ? -24.592 33.763  -0.817  1.00 29.78 ? 157 GLN B CB    1 
ATOM   3416 C  CG    . GLN B 1 163 ? -24.582 32.557  0.105   1.00 31.35 ? 157 GLN B CG    1 
ATOM   3417 C  CD    . GLN B 1 163 ? -23.260 31.836  0.021   1.00 35.15 ? 157 GLN B CD    1 
ATOM   3418 O  OE1   . GLN B 1 163 ? -22.337 32.271  -0.671  1.00 38.22 ? 157 GLN B OE1   1 
ATOM   3419 N  NE2   . GLN B 1 163 ? -23.163 30.711  0.710   1.00 37.63 ? 157 GLN B NE2   1 
ATOM   3420 N  N     . LYS B 1 164 ? -25.813 35.644  -3.061  1.00 32.22 ? 158 LYS B N     1 
ATOM   3421 C  CA    . LYS B 1 164 ? -25.653 36.817  -3.935  1.00 31.88 ? 158 LYS B CA    1 
ATOM   3422 C  C     . LYS B 1 164 ? -26.929 37.656  -3.934  1.00 34.70 ? 158 LYS B C     1 
ATOM   3423 O  O     . LYS B 1 164 ? -26.806 38.914  -3.950  1.00 32.32 ? 158 LYS B O     1 
ATOM   3424 C  CB    . LYS B 1 164 ? -25.274 36.353  -5.337  1.00 34.52 ? 158 LYS B CB    1 
ATOM   3425 C  CG    . LYS B 1 164 ? -25.112 37.491  -6.335  1.00 36.25 ? 158 LYS B CG    1 
ATOM   3426 C  CD    . LYS B 1 164 ? -24.615 36.994  -7.671  1.00 37.00 ? 158 LYS B CD    1 
ATOM   3427 C  CE    . LYS B 1 164 ? -24.257 38.113  -8.622  1.00 41.77 ? 158 LYS B CE    1 
ATOM   3428 N  NZ    . LYS B 1 164 ? -23.521 37.563  -9.787  1.00 44.52 ? 158 LYS B NZ    1 
ATOM   3429 N  N     . TYR B 1 165 ? -28.107 37.014  -3.918  1.00 30.42 ? 159 TYR B N     1 
ATOM   3430 C  CA    . TYR B 1 165 ? -29.402 37.710  -4.127  1.00 32.68 ? 159 TYR B CA    1 
ATOM   3431 C  C     . TYR B 1 165 ? -30.094 37.851  -2.771  1.00 31.10 ? 159 TYR B C     1 
ATOM   3432 O  O     . TYR B 1 165 ? -31.242 38.292  -2.762  1.00 34.52 ? 159 TYR B O     1 
ATOM   3433 C  CB    . TYR B 1 165 ? -30.222 37.061  -5.258  1.00 30.94 ? 159 TYR B CB    1 
ATOM   3434 C  CG    . TYR B 1 165 ? -29.505 37.062  -6.586  1.00 32.83 ? 159 TYR B CG    1 
ATOM   3435 C  CD1   . TYR B 1 165 ? -29.267 38.244  -7.293  1.00 36.93 ? 159 TYR B CD1   1 
ATOM   3436 C  CD2   . TYR B 1 165 ? -28.948 35.897  -7.072  1.00 33.09 ? 159 TYR B CD2   1 
ATOM   3437 C  CE1   . TYR B 1 165 ? -28.537 38.243  -8.477  1.00 36.91 ? 159 TYR B CE1   1 
ATOM   3438 C  CE2   . TYR B 1 165 ? -28.200 35.883  -8.233  1.00 37.81 ? 159 TYR B CE2   1 
ATOM   3439 C  CZ    . TYR B 1 165 ? -28.012 37.051  -8.947  1.00 35.71 ? 159 TYR B CZ    1 
ATOM   3440 O  OH    . TYR B 1 165 ? -27.264 36.964  -10.085 1.00 43.18 ? 159 TYR B OH    1 
ATOM   3441 N  N     . ASP B 1 166 ? -29.376 37.582  -1.679  1.00 32.16 ? 160 ASP B N     1 
ATOM   3442 C  CA    . ASP B 1 166 ? -29.863 37.756  -0.292  1.00 31.84 ? 160 ASP B CA    1 
ATOM   3443 C  C     . ASP B 1 166 ? -31.156 36.931  -0.119  1.00 30.46 ? 160 ASP B C     1 
ATOM   3444 O  O     . ASP B 1 166 ? -32.193 37.520  0.284   1.00 30.29 ? 160 ASP B O     1 
ATOM   3445 C  CB    . ASP B 1 166 ? -30.063 39.254  0.012   1.00 40.56 ? 160 ASP B CB    1 
ATOM   3446 C  CG    . ASP B 1 166 ? -30.436 39.558  1.458   1.00 46.17 ? 160 ASP B CG    1 
ATOM   3447 O  OD1   . ASP B 1 166 ? -29.956 38.819  2.346   1.00 50.18 ? 160 ASP B OD1   1 
ATOM   3448 O  OD2   . ASP B 1 166 ? -31.226 40.519  1.689   1.00 53.52 ? 160 ASP B OD2   1 
ATOM   3449 N  N     . ILE B 1 167 ? -31.083 35.619  -0.382  1.00 26.87 ? 161 ILE B N     1 
ATOM   3450 C  CA    . ILE B 1 167 ? -32.186 34.643  -0.177  1.00 26.47 ? 161 ILE B CA    1 
ATOM   3451 C  C     . ILE B 1 167 ? -31.739 33.652  0.891   1.00 24.67 ? 161 ILE B C     1 
ATOM   3452 O  O     . ILE B 1 167 ? -30.587 33.222  0.870   1.00 24.99 ? 161 ILE B O     1 
ATOM   3453 C  CB    . ILE B 1 167 ? -32.547 33.925  -1.499  1.00 26.24 ? 161 ILE B CB    1 
ATOM   3454 C  CG1   . ILE B 1 167 ? -32.894 34.943  -2.594  1.00 27.82 ? 161 ILE B CG1   1 
ATOM   3455 C  CG2   . ILE B 1 167 ? -33.668 32.909  -1.286  1.00 25.78 ? 161 ILE B CG2   1 
ATOM   3456 C  CD1   . ILE B 1 167 ? -32.984 34.341  -3.983  1.00 29.49 ? 161 ILE B CD1   1 
ATOM   3457 N  N     . LYS B 1 168 ? -32.617 33.307  1.812   1.00 26.15 ? 162 LYS B N     1 
ATOM   3458 C  CA    . LYS B 1 168 ? -32.349 32.230  2.795   1.00 24.28 ? 162 LYS B CA    1 
ATOM   3459 C  C     . LYS B 1 168 ? -32.434 30.870  2.092   1.00 25.06 ? 162 LYS B C     1 
ATOM   3460 O  O     . LYS B 1 168 ? -33.435 30.591  1.399   1.00 23.43 ? 162 LYS B O     1 
ATOM   3461 C  CB    . LYS B 1 168 ? -33.302 32.353  3.968   1.00 24.81 ? 162 LYS B CB    1 
ATOM   3462 C  CG    . LYS B 1 168 ? -33.160 33.649  4.752   1.00 29.03 ? 162 LYS B CG    1 
ATOM   3463 C  CD    . LYS B 1 168 ? -34.066 33.690  5.934   1.00 31.87 ? 162 LYS B CD    1 
ATOM   3464 C  CE    . LYS B 1 168 ? -33.328 33.582  7.243   1.00 38.44 ? 162 LYS B CE    1 
ATOM   3465 N  NZ    . LYS B 1 168 ? -33.872 34.548  8.223   1.00 38.18 ? 162 LYS B NZ    1 
ATOM   3466 N  N     . PHE B 1 169 ? -31.411 30.054  2.287   1.00 22.07 ? 163 PHE B N     1 
ATOM   3467 C  CA    . PHE B 1 169 ? -31.248 28.742  1.611   1.00 22.45 ? 163 PHE B CA    1 
ATOM   3468 C  C     . PHE B 1 169 ? -31.691 27.611  2.531   1.00 21.10 ? 163 PHE B C     1 
ATOM   3469 O  O     . PHE B 1 169 ? -31.191 27.449  3.683   1.00 21.47 ? 163 PHE B O     1 
ATOM   3470 C  CB    . PHE B 1 169 ? -29.812 28.600  1.136   1.00 26.49 ? 163 PHE B CB    1 
ATOM   3471 C  CG    . PHE B 1 169 ? -29.484 27.287  0.476   1.00 26.51 ? 163 PHE B CG    1 
ATOM   3472 C  CD1   . PHE B 1 169 ? -30.197 26.840  -0.622  1.00 28.63 ? 163 PHE B CD1   1 
ATOM   3473 C  CD2   . PHE B 1 169 ? -28.402 26.536  0.904   1.00 30.30 ? 163 PHE B CD2   1 
ATOM   3474 C  CE1   . PHE B 1 169 ? -29.861 25.655  -1.257  1.00 28.20 ? 163 PHE B CE1   1 
ATOM   3475 C  CE2   . PHE B 1 169 ? -28.055 25.359  0.251   1.00 31.34 ? 163 PHE B CE2   1 
ATOM   3476 C  CZ    . PHE B 1 169 ? -28.789 24.915  -0.822  1.00 31.25 ? 163 PHE B CZ    1 
ATOM   3477 N  N     . LYS B 1 170 ? -32.671 26.840  2.062   1.00 20.61 ? 164 LYS B N     1 
ATOM   3478 C  CA    . LYS B 1 170 ? -33.306 25.724  2.827   1.00 18.97 ? 164 LYS B CA    1 
ATOM   3479 C  C     . LYS B 1 170 ? -33.201 24.405  2.063   1.00 18.85 ? 164 LYS B C     1 
ATOM   3480 O  O     . LYS B 1 170 ? -33.200 24.398  0.828   1.00 19.29 ? 164 LYS B O     1 
ATOM   3481 C  CB    . LYS B 1 170 ? -34.748 26.163  3.116   1.00 19.65 ? 164 LYS B CB    1 
ATOM   3482 C  CG    . LYS B 1 170 ? -35.717 25.137  3.676   1.00 19.52 ? 164 LYS B CG    1 
ATOM   3483 C  CD    . LYS B 1 170 ? -37.101 25.731  3.856   1.00 18.91 ? 164 LYS B CD    1 
ATOM   3484 C  CE    . LYS B 1 170 ? -38.146 24.650  4.046   1.00 21.02 ? 164 LYS B CE    1 
ATOM   3485 N  NZ    . LYS B 1 170 ? -39.499 25.162  3.789   1.00 23.62 ? 164 LYS B NZ    1 
ATOM   3486 N  N     . LEU B 1 171 ? -33.098 23.296  2.783   1.00 19.69 ? 165 LEU B N     1 
ATOM   3487 C  CA    . LEU B 1 171 ? -33.018 21.948  2.197   1.00 20.45 ? 165 LEU B CA    1 
ATOM   3488 C  C     . LEU B 1 171 ? -34.171 21.144  2.755   1.00 19.97 ? 165 LEU B C     1 
ATOM   3489 O  O     . LEU B 1 171 ? -34.418 21.244  3.959   1.00 19.85 ? 165 LEU B O     1 
ATOM   3490 C  CB    . LEU B 1 171 ? -31.685 21.268  2.531   1.00 25.63 ? 165 LEU B CB    1 
ATOM   3491 C  CG    . LEU B 1 171 ? -30.491 21.639  1.671   1.00 34.53 ? 165 LEU B CG    1 
ATOM   3492 C  CD1   . LEU B 1 171 ? -29.265 20.833  2.110   1.00 36.22 ? 165 LEU B CD1   1 
ATOM   3493 C  CD2   . LEU B 1 171 ? -30.773 21.394  0.196   1.00 33.44 ? 165 LEU B CD2   1 
ATOM   3494 N  N     . ASN B 1 172 ? -34.794 20.338  1.892   1.00 17.95 ? 166 ASN B N     1 
ATOM   3495 C  CA    . ASN B 1 172 ? -35.865 19.391  2.256   1.00 18.34 ? 166 ASN B CA    1 
ATOM   3496 C  C     . ASN B 1 172 ? -35.417 17.982  1.872   1.00 19.83 ? 166 ASN B C     1 
ATOM   3497 O  O     . ASN B 1 172 ? -35.021 17.769  0.698   1.00 21.53 ? 166 ASN B O     1 
ATOM   3498 C  CB    . ASN B 1 172 ? -37.165 19.721  1.527   1.00 19.62 ? 166 ASN B CB    1 
ATOM   3499 C  CG    . ASN B 1 172 ? -37.925 20.914  2.070   1.00 22.32 ? 166 ASN B CG    1 
ATOM   3500 O  OD1   . ASN B 1 172 ? -37.404 21.655  2.903   1.00 23.77 ? 166 ASN B OD1   1 
ATOM   3501 N  ND2   . ASN B 1 172 ? -39.123 21.144  1.536   1.00 19.83 ? 166 ASN B ND2   1 
ATOM   3502 N  N     . THR B 1 173 ? -35.516 17.040  2.789   1.00 18.19 ? 167 THR B N     1 
ATOM   3503 C  CA    . THR B 1 173 ? -35.135 15.628  2.582   1.00 19.19 ? 167 THR B CA    1 
ATOM   3504 C  C     . THR B 1 173 ? -36.316 14.761  3.007   1.00 19.95 ? 167 THR B C     1 
ATOM   3505 O  O     . THR B 1 173 ? -36.789 14.967  4.144   1.00 19.46 ? 167 THR B O     1 
ATOM   3506 C  CB    . THR B 1 173 ? -33.878 15.285  3.391   1.00 19.02 ? 167 THR B CB    1 
ATOM   3507 O  OG1   . THR B 1 173 ? -32.824 16.129  2.944   1.00 20.36 ? 167 THR B OG1   1 
ATOM   3508 C  CG2   . THR B 1 173 ? -33.493 13.831  3.313   1.00 20.08 ? 167 THR B CG2   1 
ATOM   3509 N  N     . VAL B 1 174 ? -36.710 13.798  2.166   1.00 19.10 ? 168 VAL B N     1 
ATOM   3510 C  CA    . VAL B 1 174 ? -37.643 12.697  2.532   1.00 20.17 ? 168 VAL B CA    1 
ATOM   3511 C  C     . VAL B 1 174 ? -36.818 11.481  2.945   1.00 19.86 ? 168 VAL B C     1 
ATOM   3512 O  O     . VAL B 1 174 ? -36.107 10.919  2.091   1.00 18.86 ? 168 VAL B O     1 
ATOM   3513 C  CB    . VAL B 1 174 ? -38.620 12.367  1.392   1.00 19.99 ? 168 VAL B CB    1 
ATOM   3514 C  CG1   . VAL B 1 174 ? -39.526 11.228  1.786   1.00 20.97 ? 168 VAL B CG1   1 
ATOM   3515 C  CG2   . VAL B 1 174 ? -39.449 13.566  1.009   1.00 21.46 ? 168 VAL B CG2   1 
ATOM   3516 N  N     . VAL B 1 175 ? -36.981 11.042  4.188   1.00 20.43 ? 169 VAL B N     1 
ATOM   3517 C  CA    . VAL B 1 175 ? -36.206 9.898   4.743   1.00 20.64 ? 169 VAL B CA    1 
ATOM   3518 C  C     . VAL B 1 175 ? -36.962 8.640   4.350   1.00 23.03 ? 169 VAL B C     1 
ATOM   3519 O  O     . VAL B 1 175 ? -38.120 8.480   4.781   1.00 24.34 ? 169 VAL B O     1 
ATOM   3520 C  CB    . VAL B 1 175 ? -36.001 10.018  6.268   1.00 22.82 ? 169 VAL B CB    1 
ATOM   3521 C  CG1   . VAL B 1 175 ? -35.154 8.875   6.805   1.00 22.14 ? 169 VAL B CG1   1 
ATOM   3522 C  CG2   . VAL B 1 175 ? -35.408 11.379  6.616   1.00 23.19 ? 169 VAL B CG2   1 
ATOM   3523 N  N     . ASN B 1 176 ? -36.326 7.755   3.586   1.00 21.35 ? 170 ASN B N     1 
ATOM   3524 C  CA    . ASN B 1 176 ? -37.056 6.661   2.904   1.00 21.56 ? 170 ASN B CA    1 
ATOM   3525 C  C     . ASN B 1 176 ? -36.176 5.418   2.853   1.00 22.83 ? 170 ASN B C     1 
ATOM   3526 O  O     . ASN B 1 176 ? -35.035 5.459   3.351   1.00 20.99 ? 170 ASN B O     1 
ATOM   3527 C  CB    . ASN B 1 176 ? -37.527 7.116   1.514   1.00 21.49 ? 170 ASN B CB    1 
ATOM   3528 C  CG    . ASN B 1 176 ? -36.388 7.410   0.567   1.00 21.31 ? 170 ASN B CG    1 
ATOM   3529 O  OD1   . ASN B 1 176 ? -35.772 6.489   0.050   1.00 22.92 ? 170 ASN B OD1   1 
ATOM   3530 N  ND2   . ASN B 1 176 ? -36.119 8.678   0.299   1.00 21.27 ? 170 ASN B ND2   1 
ATOM   3531 N  N     . LYS B 1 177 ? -36.720 4.343   2.298   1.00 23.38 ? 171 LYS B N     1 
ATOM   3532 C  CA    . LYS B 1 177 ? -36.067 3.014   2.230   1.00 26.03 ? 171 LYS B CA    1 
ATOM   3533 C  C     . LYS B 1 177 ? -34.659 3.143   1.645   1.00 23.52 ? 171 LYS B C     1 
ATOM   3534 O  O     . LYS B 1 177 ? -33.778 2.446   2.140   1.00 23.76 ? 171 LYS B O     1 
ATOM   3535 C  CB    . LYS B 1 177 ? -36.902 2.030   1.404   1.00 30.37 ? 171 LYS B CB    1 
ATOM   3536 C  CG    . LYS B 1 177 ? -36.364 0.600   1.364   1.00 34.74 ? 171 LYS B CG    1 
ATOM   3537 C  CD    . LYS B 1 177 ? -36.425 -0.080  0.002   1.00 38.26 ? 171 LYS B CD    1 
ATOM   3538 C  CE    . LYS B 1 177 ? -37.812 -0.110  -0.585  1.00 41.70 ? 171 LYS B CE    1 
ATOM   3539 N  NZ    . LYS B 1 177 ? -37.932 -0.998  -1.774  1.00 44.62 ? 171 LYS B NZ    1 
ATOM   3540 N  N     . PHE B 1 178 ? -34.453 3.984   0.638   1.00 23.99 ? 172 PHE B N     1 
ATOM   3541 C  CA    . PHE B 1 178 ? -33.169 4.048   -0.097  1.00 23.45 ? 172 PHE B CA    1 
ATOM   3542 C  C     . PHE B 1 178 ? -32.139 4.940   0.616   1.00 24.16 ? 172 PHE B C     1 
ATOM   3543 O  O     . PHE B 1 178 ? -30.961 4.683   0.365   1.00 25.50 ? 172 PHE B O     1 
ATOM   3544 C  CB    . PHE B 1 178 ? -33.383 4.489   -1.550  1.00 25.39 ? 172 PHE B CB    1 
ATOM   3545 C  CG    . PHE B 1 178 ? -34.205 3.505   -2.337  1.00 24.31 ? 172 PHE B CG    1 
ATOM   3546 C  CD1   . PHE B 1 178 ? -33.750 2.206   -2.504  1.00 25.73 ? 172 PHE B CD1   1 
ATOM   3547 C  CD2   . PHE B 1 178 ? -35.487 3.808   -2.746  1.00 25.50 ? 172 PHE B CD2   1 
ATOM   3548 C  CE1   . PHE B 1 178 ? -34.512 1.259   -3.167  1.00 24.72 ? 172 PHE B CE1   1 
ATOM   3549 C  CE2   . PHE B 1 178 ? -36.250 2.866   -3.423  1.00 27.92 ? 172 PHE B CE2   1 
ATOM   3550 C  CZ    . PHE B 1 178 ? -35.758 1.599   -3.637  1.00 27.52 ? 172 PHE B CZ    1 
ATOM   3551 N  N     . ASN B 1 179 ? -32.504 5.982   1.386   1.00 20.75 ? 173 ASN B N     1 
ATOM   3552 C  CA    . ASN B 1 179 ? -31.498 6.965   1.899   1.00 19.95 ? 173 ASN B CA    1 
ATOM   3553 C  C     . ASN B 1 179 ? -31.334 6.922   3.437   1.00 21.09 ? 173 ASN B C     1 
ATOM   3554 O  O     . ASN B 1 179 ? -30.521 7.705   3.951   1.00 22.97 ? 173 ASN B O     1 
ATOM   3555 C  CB    . ASN B 1 179 ? -31.798 8.387   1.441   1.00 20.90 ? 173 ASN B CB    1 
ATOM   3556 C  CG    . ASN B 1 179 ? -33.133 8.915   1.949   1.00 20.04 ? 173 ASN B CG    1 
ATOM   3557 O  OD1   . ASN B 1 179 ? -33.819 8.197   2.653   1.00 21.57 ? 173 ASN B OD1   1 
ATOM   3558 N  ND2   . ASN B 1 179 ? -33.469 10.169  1.640   1.00 18.52 ? 173 ASN B ND2   1 
ATOM   3559 N  N     . HIS B 1 180 ? -32.085 6.099   4.177   1.00 20.85 ? 174 HIS B N     1 
ATOM   3560 C  CA    . HIS B 1 180 ? -32.194 6.228   5.658   1.00 21.75 ? 174 HIS B CA    1 
ATOM   3561 C  C     . HIS B 1 180 ? -30.868 5.867   6.355   1.00 23.03 ? 174 HIS B C     1 
ATOM   3562 O  O     . HIS B 1 180 ? -30.690 6.340   7.492   1.00 21.30 ? 174 HIS B O     1 
ATOM   3563 C  CB    . HIS B 1 180 ? -33.403 5.457   6.201   1.00 23.17 ? 174 HIS B CB    1 
ATOM   3564 C  CG    . HIS B 1 180 ? -33.207 3.994   6.295   1.00 22.90 ? 174 HIS B CG    1 
ATOM   3565 N  ND1   . HIS B 1 180 ? -32.785 3.396   7.445   1.00 24.59 ? 174 HIS B ND1   1 
ATOM   3566 C  CD2   . HIS B 1 180 ? -33.403 3.006   5.391   1.00 27.06 ? 174 HIS B CD2   1 
ATOM   3567 C  CE1   . HIS B 1 180 ? -32.677 2.098   7.246   1.00 26.55 ? 174 HIS B CE1   1 
ATOM   3568 N  NE2   . HIS B 1 180 ? -33.075 1.838   5.999   1.00 27.22 ? 174 HIS B NE2   1 
ATOM   3569 N  N     . LEU B 1 181 ? -29.939 5.163   5.682   1.00 22.91 ? 175 LEU B N     1 
ATOM   3570 C  CA    . LEU B 1 181 ? -28.611 4.835   6.250   1.00 23.41 ? 175 LEU B CA    1 
ATOM   3571 C  C     . LEU B 1 181 ? -27.553 5.873   5.851   1.00 24.46 ? 175 LEU B C     1 
ATOM   3572 O  O     . LEU B 1 181 ? -26.432 5.764   6.372   1.00 24.67 ? 175 LEU B O     1 
ATOM   3573 C  CB    . LEU B 1 181 ? -28.169 3.426   5.818   1.00 26.54 ? 175 LEU B CB    1 
ATOM   3574 C  CG    . LEU B 1 181 ? -28.998 2.258   6.354   1.00 26.74 ? 175 LEU B CG    1 
ATOM   3575 C  CD1   . LEU B 1 181 ? -28.440 0.929   5.847   1.00 32.43 ? 175 LEU B CD1   1 
ATOM   3576 C  CD2   . LEU B 1 181 ? -29.090 2.255   7.869   1.00 27.90 ? 175 LEU B CD2   1 
ATOM   3577 N  N     . GLU B 1 182 ? -27.849 6.816   4.960   1.00 24.09 ? 176 GLU B N     1 
ATOM   3578 C  CA    . GLU B 1 182 ? -26.860 7.788   4.438   1.00 25.50 ? 176 GLU B CA    1 
ATOM   3579 C  C     . GLU B 1 182 ? -26.417 8.729   5.561   1.00 24.47 ? 176 GLU B C     1 
ATOM   3580 O  O     . GLU B 1 182 ? -27.217 9.075   6.473   1.00 24.64 ? 176 GLU B O     1 
ATOM   3581 C  CB    . GLU B 1 182 ? -27.460 8.605   3.287   1.00 27.15 ? 176 GLU B CB    1 
ATOM   3582 C  CG    . GLU B 1 182 ? -26.449 9.445   2.525   1.00 27.42 ? 176 GLU B CG    1 
ATOM   3583 C  CD    . GLU B 1 182 ? -26.980 9.969   1.195   1.00 28.73 ? 176 GLU B CD    1 
ATOM   3584 O  OE1   . GLU B 1 182 ? -27.859 9.252   0.610   1.00 28.77 ? 176 GLU B OE1   1 
ATOM   3585 O  OE2   . GLU B 1 182 ? -26.575 11.104  0.769   1.00 26.21 ? 176 GLU B OE2   1 
ATOM   3586 N  N     . ASP B 1 183 ? -25.157 9.144   5.475   1.00 24.24 ? 177 ASP B N     1 
ATOM   3587 C  CA    . ASP B 1 183 ? -24.530 10.155  6.338   1.00 23.13 ? 177 ASP B CA    1 
ATOM   3588 C  C     . ASP B 1 183 ? -24.305 11.404  5.498   1.00 24.41 ? 177 ASP B C     1 
ATOM   3589 O  O     . ASP B 1 183 ? -23.406 11.404  4.605   1.00 24.90 ? 177 ASP B O     1 
ATOM   3590 C  CB    . ASP B 1 183 ? -23.235 9.589   6.923   1.00 26.27 ? 177 ASP B CB    1 
ATOM   3591 C  CG    . ASP B 1 183 ? -22.599 10.491  7.952   1.00 25.45 ? 177 ASP B CG    1 
ATOM   3592 O  OD1   . ASP B 1 183 ? -22.873 11.716  7.920   1.00 22.63 ? 177 ASP B OD1   1 
ATOM   3593 O  OD2   . ASP B 1 183 ? -21.784 9.957   8.741   1.00 29.14 ? 177 ASP B OD2   1 
ATOM   3594 N  N     . MET B 1 184 ? -25.108 12.428  5.772   1.00 22.56 ? 178 MET B N     1 
ATOM   3595 C  CA    . MET B 1 184 ? -25.176 13.708  5.044   1.00 23.88 ? 178 MET B CA    1 
ATOM   3596 C  C     . MET B 1 184 ? -24.493 14.835  5.834   1.00 20.67 ? 178 MET B C     1 
ATOM   3597 O  O     . MET B 1 184 ? -24.485 15.967  5.357   1.00 23.47 ? 178 MET B O     1 
ATOM   3598 C  CB    . MET B 1 184 ? -26.664 14.041  4.853   1.00 24.26 ? 178 MET B CB    1 
ATOM   3599 C  CG    . MET B 1 184 ? -27.380 13.067  4.003   1.00 27.13 ? 178 MET B CG    1 
ATOM   3600 S  SD    . MET B 1 184 ? -29.057 13.699  3.607   1.00 27.27 ? 178 MET B SD    1 
ATOM   3601 C  CE    . MET B 1 184 ? -29.719 12.220  2.835   1.00 30.48 ? 178 MET B CE    1 
ATOM   3602 N  N     . ASN B 1 185 ? -23.990 14.554  7.044   1.00 22.48 ? 179 ASN B N     1 
ATOM   3603 C  CA    . ASN B 1 185 ? -23.514 15.580  8.008   1.00 22.91 ? 179 ASN B CA    1 
ATOM   3604 C  C     . ASN B 1 185 ? -22.522 16.529  7.319   1.00 22.57 ? 179 ASN B C     1 
ATOM   3605 O  O     . ASN B 1 185 ? -22.672 17.744  7.465   1.00 23.32 ? 179 ASN B O     1 
ATOM   3606 C  CB    . ASN B 1 185 ? -22.893 14.934  9.256   1.00 24.37 ? 179 ASN B CB    1 
ATOM   3607 C  CG    . ASN B 1 185 ? -23.937 14.428  10.230  1.00 24.38 ? 179 ASN B CG    1 
ATOM   3608 O  OD1   . ASN B 1 185 ? -24.659 15.236  10.798  1.00 22.19 ? 179 ASN B OD1   1 
ATOM   3609 N  ND2   . ASN B 1 185 ? -24.034 13.116  10.394  1.00 23.11 ? 179 ASN B ND2   1 
ATOM   3610 N  N     . ASP B 1 186 ? -21.472 15.991  6.674   1.00 23.77 ? 180 ASP B N     1 
ATOM   3611 C  CA    . ASP B 1 186 ? -20.378 16.849  6.169   1.00 24.00 ? 180 ASP B CA    1 
ATOM   3612 C  C     . ASP B 1 186 ? -20.866 17.679  4.969   1.00 21.22 ? 180 ASP B C     1 
ATOM   3613 O  O     . ASP B 1 186 ? -20.474 18.860  4.872   1.00 22.95 ? 180 ASP B O     1 
ATOM   3614 C  CB    . ASP B 1 186 ? -19.085 16.032  6.018   1.00 24.93 ? 180 ASP B CB    1 
ATOM   3615 C  CG    . ASP B 1 186 ? -18.590 15.486  7.357   1.00 25.92 ? 180 ASP B CG    1 
ATOM   3616 O  OD1   . ASP B 1 186 ? -18.641 16.263  8.387   1.00 28.37 ? 180 ASP B OD1   1 
ATOM   3617 O  OD2   . ASP B 1 186 ? -18.189 14.289  7.383   1.00 28.47 ? 180 ASP B OD2   1 
ATOM   3618 N  N     . HIS B 1 187 ? -21.747 17.142  4.126   1.00 23.33 ? 181 HIS B N     1 
ATOM   3619 C  CA    . HIS B 1 187 ? -22.415 17.942  3.078   1.00 22.68 ? 181 HIS B CA    1 
ATOM   3620 C  C     . HIS B 1 187 ? -23.241 19.064  3.725   1.00 21.70 ? 181 HIS B C     1 
ATOM   3621 O  O     . HIS B 1 187 ? -23.143 20.214  3.270   1.00 23.84 ? 181 HIS B O     1 
ATOM   3622 C  CB    . HIS B 1 187 ? -23.276 17.067  2.170   1.00 22.47 ? 181 HIS B CB    1 
ATOM   3623 C  CG    . HIS B 1 187 ? -22.555 16.450  1.022   1.00 22.43 ? 181 HIS B CG    1 
ATOM   3624 N  ND1   . HIS B 1 187 ? -22.002 17.205  0.007   1.00 24.17 ? 181 HIS B ND1   1 
ATOM   3625 C  CD2   . HIS B 1 187 ? -22.356 15.161  0.698   1.00 23.51 ? 181 HIS B CD2   1 
ATOM   3626 C  CE1   . HIS B 1 187 ? -21.478 16.385  -0.886  1.00 21.97 ? 181 HIS B CE1   1 
ATOM   3627 N  NE2   . HIS B 1 187 ? -21.695 15.139  -0.485  1.00 25.15 ? 181 HIS B NE2   1 
ATOM   3628 N  N     . LEU B 1 188 ? -24.071 18.745  4.710   1.00 25.96 ? 182 LEU B N     1 
ATOM   3629 C  CA    . LEU B 1 188 ? -24.902 19.782  5.383   1.00 26.75 ? 182 LEU B CA    1 
ATOM   3630 C  C     . LEU B 1 188 ? -24.005 20.858  6.010   1.00 24.77 ? 182 LEU B C     1 
ATOM   3631 O  O     . LEU B 1 188 ? -24.368 22.041  5.928   1.00 28.79 ? 182 LEU B O     1 
ATOM   3632 C  CB    . LEU B 1 188 ? -25.839 19.138  6.414   1.00 30.54 ? 182 LEU B CB    1 
ATOM   3633 C  CG    . LEU B 1 188 ? -27.240 18.816  5.887   1.00 34.68 ? 182 LEU B CG    1 
ATOM   3634 C  CD1   . LEU B 1 188 ? -28.050 20.084  5.671   1.00 36.99 ? 182 LEU B CD1   1 
ATOM   3635 C  CD2   . LEU B 1 188 ? -27.176 18.054  4.598   1.00 35.90 ? 182 LEU B CD2   1 
ATOM   3636 N  N     . ASN B 1 189 ? -22.869 20.490  6.609   1.00 25.40 ? 183 ASN B N     1 
ATOM   3637 C  CA    . ASN B 1 189 ? -21.923 21.481  7.204   1.00 26.96 ? 183 ASN B CA    1 
ATOM   3638 C  C     . ASN B 1 189 ? -21.384 22.406  6.109   1.00 26.73 ? 183 ASN B C     1 
ATOM   3639 O  O     . ASN B 1 189 ? -21.261 23.622  6.398   1.00 27.31 ? 183 ASN B O     1 
ATOM   3640 C  CB    . ASN B 1 189 ? -20.818 20.830  8.041   1.00 28.46 ? 183 ASN B CB    1 
ATOM   3641 C  CG    . ASN B 1 189 ? -21.394 20.147  9.272   1.00 34.29 ? 183 ASN B CG    1 
ATOM   3642 O  OD1   . ASN B 1 189 ? -22.474 20.532  9.722   1.00 35.53 ? 183 ASN B OD1   1 
ATOM   3643 N  ND2   . ASN B 1 189 ? -20.752 19.094  9.780   1.00 32.65 ? 183 ASN B ND2   1 
ATOM   3644 N  N     . ALA B 1 190 ? -21.110 21.866  4.908   1.00 27.70 ? 184 ALA B N     1 
ATOM   3645 C  CA    . ALA B 1 190 ? -20.617 22.611  3.727   1.00 27.22 ? 184 ALA B CA    1 
ATOM   3646 C  C     . ALA B 1 190 ? -21.712 23.544  3.185   1.00 28.70 ? 184 ALA B C     1 
ATOM   3647 O  O     . ALA B 1 190 ? -21.463 24.746  3.030   1.00 29.01 ? 184 ALA B O     1 
ATOM   3648 C  CB    . ALA B 1 190 ? -20.094 21.628  2.699   1.00 26.41 ? 184 ALA B CB    1 
ATOM   3649 N  N     . LEU B 1 191 ? -22.927 23.035  2.974   1.00 29.98 ? 185 LEU B N     1 
ATOM   3650 C  CA    . LEU B 1 191 ? -24.060 23.825  2.410   1.00 28.07 ? 185 LEU B CA    1 
ATOM   3651 C  C     . LEU B 1 191 ? -24.608 24.862  3.401   1.00 26.10 ? 185 LEU B C     1 
ATOM   3652 O  O     . LEU B 1 191 ? -25.109 25.902  2.946   1.00 27.51 ? 185 LEU B O     1 
ATOM   3653 C  CB    . LEU B 1 191 ? -25.149 22.831  2.024   1.00 28.21 ? 185 LEU B CB    1 
ATOM   3654 C  CG    . LEU B 1 191 ? -24.807 22.004  0.805   1.00 30.45 ? 185 LEU B CG    1 
ATOM   3655 C  CD1   . LEU B 1 191 ? -25.712 20.795  0.724   1.00 33.52 ? 185 LEU B CD1   1 
ATOM   3656 C  CD2   . LEU B 1 191 ? -24.861 22.850  -0.461  1.00 32.96 ? 185 LEU B CD2   1 
ATOM   3657 N  N     . GLN B 1 192 ? -24.620 24.565  4.703   1.00 27.48 ? 186 GLN B N     1 
ATOM   3658 C  CA    . GLN B 1 192 ? -25.036 25.534  5.749   1.00 30.98 ? 186 GLN B CA    1 
ATOM   3659 C  C     . GLN B 1 192 ? -26.451 26.060  5.495   1.00 26.70 ? 186 GLN B C     1 
ATOM   3660 O  O     . GLN B 1 192 ? -26.700 27.252  5.636   1.00 28.51 ? 186 GLN B O     1 
ATOM   3661 C  CB    . GLN B 1 192 ? -24.080 26.742  5.766   1.00 35.12 ? 186 GLN B CB    1 
ATOM   3662 C  CG    . GLN B 1 192 ? -22.918 26.619  6.724   1.00 43.90 ? 186 GLN B CG    1 
ATOM   3663 C  CD    . GLN B 1 192 ? -22.063 27.868  6.774   1.00 48.90 ? 186 GLN B CD    1 
ATOM   3664 O  OE1   . GLN B 1 192 ? -21.043 27.878  7.448   1.00 55.88 ? 186 GLN B OE1   1 
ATOM   3665 N  NE2   . GLN B 1 192 ? -22.451 28.927  6.067   1.00 46.33 ? 186 GLN B NE2   1 
ATOM   3666 N  N     . PRO B 1 193 ? -27.462 25.229  5.172   1.00 25.32 ? 187 PRO B N     1 
ATOM   3667 C  CA    . PRO B 1 193 ? -28.823 25.754  5.098   1.00 23.49 ? 187 PRO B CA    1 
ATOM   3668 C  C     . PRO B 1 193 ? -29.267 26.253  6.477   1.00 22.56 ? 187 PRO B C     1 
ATOM   3669 O  O     . PRO B 1 193 ? -28.865 25.680  7.475   1.00 24.84 ? 187 PRO B O     1 
ATOM   3670 C  CB    . PRO B 1 193 ? -29.672 24.525  4.707   1.00 23.17 ? 187 PRO B CB    1 
ATOM   3671 C  CG    . PRO B 1 193 ? -28.881 23.368  5.250   1.00 22.84 ? 187 PRO B CG    1 
ATOM   3672 C  CD    . PRO B 1 193 ? -27.416 23.762  5.071   1.00 22.78 ? 187 PRO B CD    1 
ATOM   3673 N  N     . PHE B 1 194 ? -30.157 27.238  6.541   1.00 23.68 ? 188 PHE B N     1 
ATOM   3674 C  CA    . PHE B 1 194 ? -30.640 27.794  7.825   1.00 22.19 ? 188 PHE B CA    1 
ATOM   3675 C  C     . PHE B 1 194 ? -31.734 26.877  8.382   1.00 23.41 ? 188 PHE B C     1 
ATOM   3676 O  O     . PHE B 1 194 ? -32.151 27.006  9.550   1.00 23.37 ? 188 PHE B O     1 
ATOM   3677 C  CB    . PHE B 1 194 ? -31.092 29.241  7.602   1.00 24.40 ? 188 PHE B CB    1 
ATOM   3678 C  CG    . PHE B 1 194 ? -32.525 29.406  7.177   1.00 22.64 ? 188 PHE B CG    1 
ATOM   3679 C  CD1   . PHE B 1 194 ? -32.896 29.196  5.862   1.00 24.42 ? 188 PHE B CD1   1 
ATOM   3680 C  CD2   . PHE B 1 194 ? -33.503 29.731  8.100   1.00 22.00 ? 188 PHE B CD2   1 
ATOM   3681 C  CE1   . PHE B 1 194 ? -34.220 29.311  5.472   1.00 22.19 ? 188 PHE B CE1   1 
ATOM   3682 C  CE2   . PHE B 1 194 ? -34.823 29.893  7.706   1.00 22.67 ? 188 PHE B CE2   1 
ATOM   3683 C  CZ    . PHE B 1 194 ? -35.184 29.659  6.394   1.00 22.51 ? 188 PHE B CZ    1 
ATOM   3684 N  N     . ARG B 1 195 ? -32.226 25.970  7.543   1.00 20.79 ? 189 ARG B N     1 
ATOM   3685 C  CA    . ARG B 1 195 ? -33.439 25.159  7.812   1.00 18.82 ? 189 ARG B CA    1 
ATOM   3686 C  C     . ARG B 1 195 ? -33.331 23.911  6.939   1.00 18.04 ? 189 ARG B C     1 
ATOM   3687 O  O     . ARG B 1 195 ? -33.133 24.056  5.724   1.00 19.93 ? 189 ARG B O     1 
ATOM   3688 C  CB    . ARG B 1 195 ? -34.705 25.954  7.478   1.00 17.84 ? 189 ARG B CB    1 
ATOM   3689 C  CG    . ARG B 1 195 ? -36.024 25.313  7.880   1.00 18.23 ? 189 ARG B CG    1 
ATOM   3690 C  CD    . ARG B 1 195 ? -37.103 26.390  7.831   1.00 21.07 ? 189 ARG B CD    1 
ATOM   3691 N  NE    . ARG B 1 195 ? -38.432 25.977  8.291   1.00 21.63 ? 189 ARG B NE    1 
ATOM   3692 C  CZ    . ARG B 1 195 ? -38.824 25.881  9.551   1.00 22.54 ? 189 ARG B CZ    1 
ATOM   3693 N  NH1   . ARG B 1 195 ? -37.981 26.145  10.536  1.00 21.61 ? 189 ARG B NH1   1 
ATOM   3694 N  NH2   . ARG B 1 195 ? -40.071 25.519  9.820   1.00 23.54 ? 189 ARG B NH2   1 
ATOM   3695 N  N     . TRP B 1 196 ? -33.406 22.748  7.567   1.00 19.02 ? 190 TRP B N     1 
ATOM   3696 C  CA    . TRP B 1 196 ? -33.287 21.437  6.910   1.00 18.70 ? 190 TRP B CA    1 
ATOM   3697 C  C     . TRP B 1 196 ? -34.447 20.553  7.335   1.00 19.40 ? 190 TRP B C     1 
ATOM   3698 O  O     . TRP B 1 196 ? -34.397 20.024  8.452   1.00 19.90 ? 190 TRP B O     1 
ATOM   3699 C  CB    . TRP B 1 196 ? -31.956 20.772  7.225   1.00 19.18 ? 190 TRP B CB    1 
ATOM   3700 C  CG    . TRP B 1 196 ? -31.817 19.409  6.611   1.00 19.50 ? 190 TRP B CG    1 
ATOM   3701 C  CD1   . TRP B 1 196 ? -32.287 18.997  5.396   1.00 18.50 ? 190 TRP B CD1   1 
ATOM   3702 C  CD2   . TRP B 1 196 ? -31.078 18.299  7.146   1.00 20.17 ? 190 TRP B CD2   1 
ATOM   3703 N  NE1   . TRP B 1 196 ? -31.918 17.692  5.168   1.00 20.54 ? 190 TRP B NE1   1 
ATOM   3704 C  CE2   . TRP B 1 196 ? -31.143 17.256  6.203   1.00 21.43 ? 190 TRP B CE2   1 
ATOM   3705 C  CE3   . TRP B 1 196 ? -30.366 18.086  8.332   1.00 21.86 ? 190 TRP B CE3   1 
ATOM   3706 C  CZ2   . TRP B 1 196 ? -30.556 16.012  6.423   1.00 22.81 ? 190 TRP B CZ2   1 
ATOM   3707 C  CZ3   . TRP B 1 196 ? -29.752 16.876  8.526   1.00 24.19 ? 190 TRP B CZ3   1 
ATOM   3708 C  CH2   . TRP B 1 196 ? -29.846 15.851  7.586   1.00 26.22 ? 190 TRP B CH2   1 
ATOM   3709 N  N     . LYS B 1 197 ? -35.498 20.472  6.518   1.00 18.47 ? 191 LYS B N     1 
ATOM   3710 C  CA    . LYS B 1 197 ? -36.663 19.628  6.834   1.00 19.21 ? 191 LYS B CA    1 
ATOM   3711 C  C     . LYS B 1 197 ? -36.303 18.178  6.571   1.00 19.14 ? 191 LYS B C     1 
ATOM   3712 O  O     . LYS B 1 197 ? -35.830 17.879  5.460   1.00 21.17 ? 191 LYS B O     1 
ATOM   3713 C  CB    . LYS B 1 197 ? -37.876 19.995  5.978   1.00 20.83 ? 191 LYS B CB    1 
ATOM   3714 C  CG    . LYS B 1 197 ? -38.400 21.421  6.112   1.00 24.00 ? 191 LYS B CG    1 
ATOM   3715 C  CD    . LYS B 1 197 ? -38.933 21.745  7.455   1.00 28.43 ? 191 LYS B CD    1 
ATOM   3716 C  CE    . LYS B 1 197 ? -39.885 22.921  7.485   1.00 23.85 ? 191 LYS B CE    1 
ATOM   3717 N  NZ    . LYS B 1 197 ? -41.284 22.501  7.284   1.00 26.06 ? 191 LYS B NZ    1 
ATOM   3718 N  N     . CYS B 1 198 ? -36.588 17.274  7.512   1.00 19.85 ? 192 CYS B N     1 
ATOM   3719 C  CA    . CYS B 1 198 ? -36.481 15.803  7.321   1.00 19.12 ? 192 CYS B CA    1 
ATOM   3720 C  C     . CYS B 1 198 ? -37.859 15.194  7.556   1.00 19.02 ? 192 CYS B C     1 
ATOM   3721 O  O     . CYS B 1 198 ? -38.250 15.011  8.710   1.00 19.84 ? 192 CYS B O     1 
ATOM   3722 C  CB    . CYS B 1 198 ? -35.451 15.154  8.232   1.00 22.29 ? 192 CYS B CB    1 
ATOM   3723 S  SG    . CYS B 1 198 ? -33.781 15.664  7.740   1.00 26.91 ? 192 CYS B SG    1 
ATOM   3724 N  N     . PHE B 1 199 ? -38.515 14.859  6.463   1.00 19.93 ? 193 PHE B N     1 
ATOM   3725 C  CA    . PHE B 1 199 ? -39.898 14.352  6.430   1.00 18.73 ? 193 PHE B CA    1 
ATOM   3726 C  C     . PHE B 1 199 ? -39.891 12.840  6.458   1.00 20.66 ? 193 PHE B C     1 
ATOM   3727 O  O     . PHE B 1 199 ? -39.127 12.193  5.686   1.00 20.23 ? 193 PHE B O     1 
ATOM   3728 C  CB    . PHE B 1 199 ? -40.616 14.793  5.164   1.00 18.62 ? 193 PHE B CB    1 
ATOM   3729 C  CG    . PHE B 1 199 ? -40.605 16.266  4.860   1.00 18.80 ? 193 PHE B CG    1 
ATOM   3730 C  CD1   . PHE B 1 199 ? -41.208 17.171  5.719   1.00 19.48 ? 193 PHE B CD1   1 
ATOM   3731 C  CD2   . PHE B 1 199 ? -40.070 16.727  3.676   1.00 20.10 ? 193 PHE B CD2   1 
ATOM   3732 C  CE1   . PHE B 1 199 ? -41.268 18.514  5.382   1.00 21.88 ? 193 PHE B CE1   1 
ATOM   3733 C  CE2   . PHE B 1 199 ? -40.140 18.062  3.329   1.00 20.23 ? 193 PHE B CE2   1 
ATOM   3734 C  CZ    . PHE B 1 199 ? -40.707 18.966  4.203   1.00 21.31 ? 193 PHE B CZ    1 
ATOM   3735 N  N     . GLN B 1 200 ? -40.721 12.280  7.325   1.00 19.22 ? 194 GLN B N     1 
ATOM   3736 C  CA    . GLN B 1 200 ? -41.114 10.865  7.217   1.00 21.54 ? 194 GLN B CA    1 
ATOM   3737 C  C     . GLN B 1 200 ? -42.031 10.734  5.997   1.00 21.92 ? 194 GLN B C     1 
ATOM   3738 O  O     . GLN B 1 200 ? -42.831 11.657  5.747   1.00 20.03 ? 194 GLN B O     1 
ATOM   3739 C  CB    . GLN B 1 200 ? -41.769 10.391  8.507   1.00 22.89 ? 194 GLN B CB    1 
ATOM   3740 C  CG    . GLN B 1 200 ? -42.195 8.939   8.473   1.00 25.64 ? 194 GLN B CG    1 
ATOM   3741 C  CD    . GLN B 1 200 ? -42.656 8.483   9.842   1.00 29.58 ? 194 GLN B CD    1 
ATOM   3742 O  OE1   . GLN B 1 200 ? -43.272 9.227   10.608  1.00 28.15 ? 194 GLN B OE1   1 
ATOM   3743 N  NE2   . GLN B 1 200 ? -42.321 7.242   10.161  1.00 38.62 ? 194 GLN B NE2   1 
ATOM   3744 N  N     . VAL B 1 201 ? -41.879 9.668   5.216   1.00 21.84 ? 195 VAL B N     1 
ATOM   3745 C  CA    . VAL B 1 201 ? -42.791 9.417   4.067   1.00 21.38 ? 195 VAL B CA    1 
ATOM   3746 C  C     . VAL B 1 201 ? -44.243 9.451   4.566   1.00 21.34 ? 195 VAL B C     1 
ATOM   3747 O  O     . VAL B 1 201 ? -44.602 8.728   5.553   1.00 22.19 ? 195 VAL B O     1 
ATOM   3748 C  CB    . VAL B 1 201 ? -42.465 8.085   3.375   1.00 23.80 ? 195 VAL B CB    1 
ATOM   3749 C  CG1   . VAL B 1 201 ? -43.544 7.760   2.367   1.00 23.44 ? 195 VAL B CG1   1 
ATOM   3750 C  CG2   . VAL B 1 201 ? -41.114 8.103   2.700   1.00 22.88 ? 195 VAL B CG2   1 
ATOM   3751 N  N     . LEU B 1 202 ? -45.063 10.293  3.950   1.00 21.75 ? 196 LEU B N     1 
ATOM   3752 C  CA    . LEU B 1 202 ? -46.504 10.409  4.287   1.00 21.36 ? 196 LEU B CA    1 
ATOM   3753 C  C     . LEU B 1 202 ? -47.339 9.741   3.186   1.00 22.26 ? 196 LEU B C     1 
ATOM   3754 O  O     . LEU B 1 202 ? -47.171 10.098  1.976   1.00 22.65 ? 196 LEU B O     1 
ATOM   3755 C  CB    . LEU B 1 202 ? -46.866 11.890  4.480   1.00 22.13 ? 196 LEU B CB    1 
ATOM   3756 C  CG    . LEU B 1 202 ? -48.306 12.145  4.914   1.00 23.71 ? 196 LEU B CG    1 
ATOM   3757 C  CD1   . LEU B 1 202 ? -48.590 11.564  6.285   1.00 24.67 ? 196 LEU B CD1   1 
ATOM   3758 C  CD2   . LEU B 1 202 ? -48.607 13.626  4.881   1.00 25.31 ? 196 LEU B CD2   1 
ATOM   3759 N  N     . ILE B 1 203 ? -48.228 8.828   3.588   1.00 23.51 ? 197 ILE B N     1 
ATOM   3760 C  CA    . ILE B 1 203 ? -49.215 8.186   2.663   1.00 25.23 ? 197 ILE B CA    1 
ATOM   3761 C  C     . ILE B 1 203 ? -50.504 9.020   2.653   1.00 25.10 ? 197 ILE B C     1 
ATOM   3762 O  O     . ILE B 1 203 ? -51.002 9.379   3.736   1.00 25.39 ? 197 ILE B O     1 
ATOM   3763 C  CB    . ILE B 1 203 ? -49.512 6.724   3.041   1.00 27.96 ? 197 ILE B CB    1 
ATOM   3764 C  CG1   . ILE B 1 203 ? -48.249 5.875   3.155   1.00 28.85 ? 197 ILE B CG1   1 
ATOM   3765 C  CG2   . ILE B 1 203 ? -50.511 6.130   2.053   1.00 28.98 ? 197 ILE B CG2   1 
ATOM   3766 C  CD1   . ILE B 1 203 ? -47.459 5.773   1.904   1.00 30.05 ? 197 ILE B CD1   1 
ATOM   3767 N  N     . ILE B 1 204 ? -50.966 9.391   1.472   1.00 25.26 ? 198 ILE B N     1 
ATOM   3768 C  CA    . ILE B 1 204 ? -52.209 10.178  1.258   1.00 26.63 ? 198 ILE B CA    1 
ATOM   3769 C  C     . ILE B 1 204 ? -53.076 9.376   0.285   1.00 27.29 ? 198 ILE B C     1 
ATOM   3770 O  O     . ILE B 1 204 ? -52.631 9.105   -0.866  1.00 26.71 ? 198 ILE B O     1 
ATOM   3771 C  CB    . ILE B 1 204 ? -51.878 11.596  0.750   1.00 26.40 ? 198 ILE B CB    1 
ATOM   3772 C  CG1   . ILE B 1 204 ? -51.068 12.381  1.795   1.00 26.76 ? 198 ILE B CG1   1 
ATOM   3773 C  CG2   . ILE B 1 204 ? -53.155 12.326  0.336   1.00 27.12 ? 198 ILE B CG2   1 
ATOM   3774 C  CD1   . ILE B 1 204 ? -50.700 13.785  1.363   1.00 29.06 ? 198 ILE B CD1   1 
ATOM   3775 N  N     . GLU B 1 205 ? -54.268 9.005   0.738   1.00 30.96 ? 199 GLU B N     1 
ATOM   3776 C  CA    . GLU B 1 205 ? -55.250 8.245   -0.072  1.00 34.54 ? 199 GLU B CA    1 
ATOM   3777 C  C     . GLU B 1 205 ? -55.667 9.064   -1.287  1.00 32.37 ? 199 GLU B C     1 
ATOM   3778 O  O     . GLU B 1 205 ? -55.974 10.236  -1.121  1.00 31.90 ? 199 GLU B O     1 
ATOM   3779 C  CB    . GLU B 1 205 ? -56.456 7.875   0.778   1.00 43.53 ? 199 GLU B CB    1 
ATOM   3780 C  CG    . GLU B 1 205 ? -56.131 6.830   1.825   1.00 49.83 ? 199 GLU B CG    1 
ATOM   3781 C  CD    . GLU B 1 205 ? -57.356 6.271   2.534   1.00 61.51 ? 199 GLU B CD    1 
ATOM   3782 O  OE1   . GLU B 1 205 ? -58.505 6.529   2.043   1.00 54.91 ? 199 GLU B OE1   1 
ATOM   3783 O  OE2   . GLU B 1 205 ? -57.157 5.574   3.566   1.00 68.33 ? 199 GLU B OE2   1 
ATOM   3784 N  N     . GLY B 1 206 ? -55.597 8.458   -2.478  1.00 31.47 ? 200 GLY B N     1 
ATOM   3785 C  CA    . GLY B 1 206 ? -55.906 9.089   -3.766  1.00 28.31 ? 200 GLY B CA    1 
ATOM   3786 C  C     . GLY B 1 206 ? -54.692 9.729   -4.393  1.00 30.90 ? 200 GLY B C     1 
ATOM   3787 O  O     . GLY B 1 206 ? -54.807 10.156  -5.539  1.00 32.98 ? 200 GLY B O     1 
ATOM   3788 N  N     . GLU B 1 207 ? -53.549 9.792   -3.691  1.00 28.66 ? 201 GLU B N     1 
ATOM   3789 C  CA    . GLU B 1 207 ? -52.292 10.335  -4.272  1.00 26.94 ? 201 GLU B CA    1 
ATOM   3790 C  C     . GLU B 1 207 ? -51.258 9.222   -4.454  1.00 24.45 ? 201 GLU B C     1 
ATOM   3791 O  O     . GLU B 1 207 ? -50.739 9.085   -5.537  1.00 22.54 ? 201 GLU B O     1 
ATOM   3792 C  CB    . GLU B 1 207 ? -51.731 11.462  -3.400  1.00 27.08 ? 201 GLU B CB    1 
ATOM   3793 C  CG    . GLU B 1 207 ? -52.572 12.739  -3.437  1.00 29.39 ? 201 GLU B CG    1 
ATOM   3794 C  CD    . GLU B 1 207 ? -52.440 13.623  -4.678  1.00 33.59 ? 201 GLU B CD    1 
ATOM   3795 O  OE1   . GLU B 1 207 ? -51.578 13.344  -5.506  1.00 31.25 ? 201 GLU B OE1   1 
ATOM   3796 O  OE2   . GLU B 1 207 ? -53.172 14.635  -4.796  1.00 38.51 ? 201 GLU B OE2   1 
ATOM   3797 N  N     . ASN B 1 208 ? -50.903 8.527   -3.388  1.00 22.44 ? 202 ASN B N     1 
ATOM   3798 C  CA    . ASN B 1 208 ? -49.697 7.663   -3.410  1.00 23.55 ? 202 ASN B CA    1 
ATOM   3799 C  C     . ASN B 1 208 ? -49.944 6.377   -2.629  1.00 24.39 ? 202 ASN B C     1 
ATOM   3800 O  O     . ASN B 1 208 ? -48.965 5.808   -2.119  1.00 24.16 ? 202 ASN B O     1 
ATOM   3801 C  CB    . ASN B 1 208 ? -48.482 8.451   -2.913  1.00 21.23 ? 202 ASN B CB    1 
ATOM   3802 C  CG    . ASN B 1 208 ? -48.574 8.836   -1.462  1.00 22.55 ? 202 ASN B CG    1 
ATOM   3803 O  OD1   . ASN B 1 208 ? -49.591 8.593   -0.799  1.00 22.46 ? 202 ASN B OD1   1 
ATOM   3804 N  ND2   . ASN B 1 208 ? -47.495 9.411   -0.951  1.00 23.01 ? 202 ASN B ND2   1 
ATOM   3805 N  N     . ASP B 1 209 ? -51.187 5.889   -2.557  1.00 24.53 ? 203 ASP B N     1 
ATOM   3806 C  CA    . ASP B 1 209 ? -51.498 4.798   -1.593  1.00 28.86 ? 203 ASP B CA    1 
ATOM   3807 C  C     . ASP B 1 209 ? -51.748 3.437   -2.253  1.00 28.77 ? 203 ASP B C     1 
ATOM   3808 O  O     . ASP B 1 209 ? -51.926 2.490   -1.459  1.00 28.45 ? 203 ASP B O     1 
ATOM   3809 C  CB    . ASP B 1 209 ? -52.708 5.150   -0.731  1.00 29.96 ? 203 ASP B CB    1 
ATOM   3810 C  CG    . ASP B 1 209 ? -53.989 5.236   -1.545  1.00 34.96 ? 203 ASP B CG    1 
ATOM   3811 O  OD1   . ASP B 1 209 ? -53.973 5.859   -2.629  1.00 39.33 ? 203 ASP B OD1   1 
ATOM   3812 O  OD2   . ASP B 1 209 ? -54.986 4.665   -1.099  1.00 39.00 ? 203 ASP B OD2   1 
ATOM   3813 N  N     . SER B 1 210 ? -51.779 3.310   -3.586  1.00 28.59 ? 204 SER B N     1 
ATOM   3814 C  CA    . SER B 1 210 ? -52.093 2.012   -4.262  1.00 31.05 ? 204 SER B CA    1 
ATOM   3815 C  C     . SER B 1 210 ? -51.434 1.860   -5.644  1.00 29.53 ? 204 SER B C     1 
ATOM   3816 O  O     . SER B 1 210 ? -50.765 2.791   -6.127  1.00 26.64 ? 204 SER B O     1 
ATOM   3817 C  CB    . SER B 1 210 ? -53.603 1.847   -4.376  1.00 31.28 ? 204 SER B CB    1 
ATOM   3818 O  OG    . SER B 1 210 ? -54.112 2.664   -5.416  1.00 30.82 ? 204 SER B OG    1 
ATOM   3819 N  N     . ASP B 1 211 ? -51.706 0.733   -6.327  1.00 29.54 ? 205 ASP B N     1 
ATOM   3820 C  CA    . ASP B 1 211 ? -51.308 0.500   -7.739  1.00 30.24 ? 205 ASP B CA    1 
ATOM   3821 C  C     . ASP B 1 211 ? -52.150 1.368   -8.688  1.00 29.62 ? 205 ASP B C     1 
ATOM   3822 O  O     . ASP B 1 211 ? -51.716 1.543   -9.828  1.00 30.55 ? 205 ASP B O     1 
ATOM   3823 C  CB    . ASP B 1 211 ? -51.460 -0.967  -8.152  1.00 33.62 ? 205 ASP B CB    1 
ATOM   3824 C  CG    . ASP B 1 211 ? -52.877 -1.497  -7.953  1.00 38.06 ? 205 ASP B CG    1 
ATOM   3825 O  OD1   . ASP B 1 211 ? -53.447 -1.231  -6.860  1.00 41.38 ? 205 ASP B OD1   1 
ATOM   3826 O  OD2   . ASP B 1 211 ? -53.405 -2.192  -8.886  1.00 41.90 ? 205 ASP B OD2   1 
ATOM   3827 N  N     . LYS B 1 212 ? -53.293 1.899   -8.236  1.00 28.48 ? 206 LYS B N     1 
ATOM   3828 C  CA    . LYS B 1 212 ? -54.249 2.660   -9.073  1.00 30.86 ? 206 LYS B CA    1 
ATOM   3829 C  C     . LYS B 1 212 ? -53.937 4.154   -9.082  1.00 32.32 ? 206 LYS B C     1 
ATOM   3830 O  O     . LYS B 1 212 ? -54.405 4.807   -10.000 1.00 32.41 ? 206 LYS B O     1 
ATOM   3831 C  CB    . LYS B 1 212 ? -55.664 2.378   -8.569  1.00 35.40 ? 206 LYS B CB    1 
ATOM   3832 C  CG    . LYS B 1 212 ? -56.043 0.923   -8.772  1.00 36.03 ? 206 LYS B CG    1 
ATOM   3833 C  CD    . LYS B 1 212 ? -56.065 0.551   -10.243 1.00 42.40 ? 206 LYS B CD    1 
ATOM   3834 C  CE    . LYS B 1 212 ? -55.756 -0.901  -10.488 1.00 45.26 ? 206 LYS B CE    1 
ATOM   3835 N  NZ    . LYS B 1 212 ? -56.268 -1.343  -11.803 1.00 45.13 ? 206 LYS B NZ    1 
ATOM   3836 N  N     . THR B 1 213 ? -53.172 4.665   -8.116  1.00 29.16 ? 207 THR B N     1 
ATOM   3837 C  CA    . THR B 1 213 ? -52.722 6.084   -8.103  1.00 27.23 ? 207 THR B CA    1 
ATOM   3838 C  C     . THR B 1 213 ? -51.473 6.228   -8.968  1.00 26.79 ? 207 THR B C     1 
ATOM   3839 O  O     . THR B 1 213 ? -50.950 5.216   -9.444  1.00 26.96 ? 207 THR B O     1 
ATOM   3840 C  CB    . THR B 1 213 ? -52.507 6.544   -6.667  1.00 26.93 ? 207 THR B CB    1 
ATOM   3841 O  OG1   . THR B 1 213 ? -51.819 5.508   -5.958  1.00 25.27 ? 207 THR B OG1   1 
ATOM   3842 C  CG2   . THR B 1 213 ? -53.809 6.863   -5.965  1.00 27.72 ? 207 THR B CG2   1 
ATOM   3843 N  N     . LEU B 1 214 ? -51.041 7.453   -9.239  1.00 26.83 ? 208 LEU B N     1 
ATOM   3844 C  CA    . LEU B 1 214 ? -49.882 7.680   -10.123 1.00 26.38 ? 208 LEU B CA    1 
ATOM   3845 C  C     . LEU B 1 214 ? -48.617 7.179   -9.422  1.00 24.80 ? 208 LEU B C     1 
ATOM   3846 O  O     . LEU B 1 214 ? -47.647 6.916   -10.141 1.00 26.64 ? 208 LEU B O     1 
ATOM   3847 C  CB    . LEU B 1 214 ? -49.789 9.167   -10.465 1.00 27.25 ? 208 LEU B CB    1 
ATOM   3848 C  CG    . LEU B 1 214 ? -50.874 9.663   -11.419 1.00 28.90 ? 208 LEU B CG    1 
ATOM   3849 C  CD1   . LEU B 1 214 ? -50.726 11.150  -11.666 1.00 29.30 ? 208 LEU B CD1   1 
ATOM   3850 C  CD2   . LEU B 1 214 ? -50.796 8.903   -12.744 1.00 30.02 ? 208 LEU B CD2   1 
ATOM   3851 N  N     . ARG B 1 215 ? -48.619 7.132   -8.087  1.00 26.37 ? 209 ARG B N     1 
ATOM   3852 C  CA    . ARG B 1 215 ? -47.470 6.615   -7.295  1.00 24.71 ? 209 ARG B CA    1 
ATOM   3853 C  C     . ARG B 1 215 ? -47.966 5.688   -6.208  1.00 23.51 ? 209 ARG B C     1 
ATOM   3854 O  O     . ARG B 1 215 ? -49.133 5.740   -5.841  1.00 23.86 ? 209 ARG B O     1 
ATOM   3855 C  CB    . ARG B 1 215 ? -46.676 7.769   -6.670  1.00 24.56 ? 209 ARG B CB    1 
ATOM   3856 C  CG    . ARG B 1 215 ? -46.131 8.740   -7.692  1.00 25.42 ? 209 ARG B CG    1 
ATOM   3857 C  CD    . ARG B 1 215 ? -44.933 8.237   -8.460  1.00 25.23 ? 209 ARG B CD    1 
ATOM   3858 N  NE    . ARG B 1 215 ? -44.848 8.817   -9.790  1.00 28.06 ? 209 ARG B NE    1 
ATOM   3859 C  CZ    . ARG B 1 215 ? -44.386 10.015  -10.101 1.00 28.91 ? 209 ARG B CZ    1 
ATOM   3860 N  NH1   . ARG B 1 215 ? -43.899 10.812  -9.164  1.00 24.64 ? 209 ARG B NH1   1 
ATOM   3861 N  NH2   . ARG B 1 215 ? -44.408 10.417  -11.364 1.00 30.94 ? 209 ARG B NH2   1 
ATOM   3862 N  N     . ASN B 1 216 ? -47.094 4.798   -5.751  1.00 27.24 ? 210 ASN B N     1 
ATOM   3863 C  CA    . ASN B 1 216 ? -47.332 3.925   -4.594  1.00 24.89 ? 210 ASN B CA    1 
ATOM   3864 C  C     . ASN B 1 216 ? -46.130 4.055   -3.641  1.00 26.36 ? 210 ASN B C     1 
ATOM   3865 O  O     . ASN B 1 216 ? -45.090 3.381   -3.863  1.00 24.89 ? 210 ASN B O     1 
ATOM   3866 C  CB    . ASN B 1 216 ? -47.561 2.474   -5.014  1.00 27.20 ? 210 ASN B CB    1 
ATOM   3867 C  CG    . ASN B 1 216 ? -48.050 1.681   -3.839  1.00 27.91 ? 210 ASN B CG    1 
ATOM   3868 O  OD1   . ASN B 1 216 ? -47.894 2.097   -2.695  1.00 30.18 ? 210 ASN B OD1   1 
ATOM   3869 N  ND2   . ASN B 1 216 ? -48.682 0.560   -4.111  1.00 32.49 ? 210 ASN B ND2   1 
ATOM   3870 N  N     . ALA B 1 217 ? -46.296 4.848   -2.588  1.00 24.31 ? 211 ALA B N     1 
ATOM   3871 C  CA    . ALA B 1 217 ? -45.206 5.163   -1.633  1.00 24.41 ? 211 ALA B CA    1 
ATOM   3872 C  C     . ALA B 1 217 ? -44.994 4.007   -0.655  1.00 25.39 ? 211 ALA B C     1 
ATOM   3873 O  O     . ALA B 1 217 ? -44.033 4.079   0.114   1.00 23.96 ? 211 ALA B O     1 
ATOM   3874 C  CB    . ALA B 1 217 ? -45.487 6.442   -0.897  1.00 26.10 ? 211 ALA B CB    1 
ATOM   3875 N  N     . HIS B 1 218 ? -45.833 2.970   -0.649  1.00 27.01 ? 212 HIS B N     1 
ATOM   3876 C  CA    . HIS B 1 218 ? -45.797 1.960   0.454   1.00 29.53 ? 212 HIS B CA    1 
ATOM   3877 C  C     . HIS B 1 218 ? -44.434 1.267   0.544   1.00 29.72 ? 212 HIS B C     1 
ATOM   3878 O  O     . HIS B 1 218 ? -43.941 1.063   1.676   1.00 34.64 ? 212 HIS B O     1 
ATOM   3879 C  CB    . HIS B 1 218 ? -46.906 0.922   0.337   1.00 29.20 ? 212 HIS B CB    1 
ATOM   3880 C  CG    . HIS B 1 218 ? -48.201 1.437   0.848   1.00 33.46 ? 212 HIS B CG    1 
ATOM   3881 N  ND1   . HIS B 1 218 ? -48.450 1.584   2.198   1.00 35.72 ? 212 HIS B ND1   1 
ATOM   3882 C  CD2   . HIS B 1 218 ? -49.305 1.863   0.198   1.00 30.73 ? 212 HIS B CD2   1 
ATOM   3883 C  CE1   . HIS B 1 218 ? -49.661 2.061   2.364   1.00 34.53 ? 212 HIS B CE1   1 
ATOM   3884 N  NE2   . HIS B 1 218 ? -50.208 2.231   1.150   1.00 31.38 ? 212 HIS B NE2   1 
ATOM   3885 N  N     . SER B 1 219 ? -43.812 0.964   -0.580  1.00 32.59 ? 213 SER B N     1 
ATOM   3886 C  CA    . SER B 1 219 ? -42.490 0.285   -0.591  1.00 36.99 ? 213 SER B CA    1 
ATOM   3887 C  C     . SER B 1 219 ? -41.345 1.238   -0.178  1.00 35.68 ? 213 SER B C     1 
ATOM   3888 O  O     . SER B 1 219 ? -40.243 0.741   0.006   1.00 38.77 ? 213 SER B O     1 
ATOM   3889 C  CB    . SER B 1 219 ? -42.230 -0.338  -1.913  1.00 35.62 ? 213 SER B CB    1 
ATOM   3890 O  OG    . SER B 1 219 ? -42.018 0.654   -2.887  1.00 41.69 ? 213 SER B OG    1 
ATOM   3891 N  N     . LEU B 1 220 ? -41.543 2.553   -0.072  1.00 32.52 ? 214 LEU B N     1 
ATOM   3892 C  CA    . LEU B 1 220 ? -40.423 3.473   0.290   1.00 31.31 ? 214 LEU B CA    1 
ATOM   3893 C  C     . LEU B 1 220 ? -40.473 3.846   1.778   1.00 31.06 ? 214 LEU B C     1 
ATOM   3894 O  O     . LEU B 1 220 ? -39.533 4.542   2.215   1.00 29.35 ? 214 LEU B O     1 
ATOM   3895 C  CB    . LEU B 1 220 ? -40.441 4.714   -0.610  1.00 34.93 ? 214 LEU B CB    1 
ATOM   3896 C  CG    . LEU B 1 220 ? -39.731 4.477   -1.937  1.00 36.84 ? 214 LEU B CG    1 
ATOM   3897 C  CD1   . LEU B 1 220 ? -40.713 3.931   -2.955  1.00 42.11 ? 214 LEU B CD1   1 
ATOM   3898 C  CD2   . LEU B 1 220 ? -39.037 5.716   -2.440  1.00 37.47 ? 214 LEU B CD2   1 
ATOM   3899 N  N     . THR B 1 221 ? -41.528 3.437   2.505   1.00 28.77 ? 215 THR B N     1 
ATOM   3900 C  CA    . THR B 1 221 ? -41.686 3.703   3.952   1.00 29.75 ? 215 THR B CA    1 
ATOM   3901 C  C     . THR B 1 221 ? -40.666 2.874   4.740   1.00 29.41 ? 215 THR B C     1 
ATOM   3902 O  O     . THR B 1 221 ? -40.183 1.849   4.234   1.00 31.24 ? 215 THR B O     1 
ATOM   3903 C  CB    . THR B 1 221 ? -43.107 3.427   4.440   1.00 33.01 ? 215 THR B CB    1 
ATOM   3904 O  OG1   . THR B 1 221 ? -43.309 2.033   4.231   1.00 32.40 ? 215 THR B OG1   1 
ATOM   3905 C  CG2   . THR B 1 221 ? -44.159 4.261   3.727   1.00 30.24 ? 215 THR B CG2   1 
ATOM   3906 N  N     . ILE B 1 222 ? -40.357 3.348   5.934   1.00 28.39 ? 216 ILE B N     1 
ATOM   3907 C  CA    . ILE B 1 222 ? -39.426 2.702   6.893   1.00 28.27 ? 216 ILE B CA    1 
ATOM   3908 C  C     . ILE B 1 222 ? -40.118 2.640   8.256   1.00 29.33 ? 216 ILE B C     1 
ATOM   3909 O  O     . ILE B 1 222 ? -41.145 3.308   8.476   1.00 28.35 ? 216 ILE B O     1 
ATOM   3910 C  CB    . ILE B 1 222 ? -38.095 3.484   6.952   1.00 28.55 ? 216 ILE B CB    1 
ATOM   3911 C  CG1   . ILE B 1 222 ? -38.323 4.923   7.419   1.00 29.63 ? 216 ILE B CG1   1 
ATOM   3912 C  CG2   . ILE B 1 222 ? -37.370 3.445   5.615   1.00 30.23 ? 216 ILE B CG2   1 
ATOM   3913 C  CD1   . ILE B 1 222 ? -37.090 5.757   7.515   1.00 30.23 ? 216 ILE B CD1   1 
ATOM   3914 N  N     . SER B 1 223 ? -39.508 1.938   9.198   1.00 30.27 ? 217 SER B N     1 
ATOM   3915 C  CA    . SER B 1 223 ? -40.006 1.887   10.589  1.00 32.74 ? 217 SER B CA    1 
ATOM   3916 C  C     . SER B 1 223 ? -39.788 3.242   11.268  1.00 32.49 ? 217 SER B C     1 
ATOM   3917 O  O     . SER B 1 223 ? -38.921 4.063   10.814  1.00 26.96 ? 217 SER B O     1 
ATOM   3918 C  CB    . SER B 1 223 ? -39.361 0.776   11.329  1.00 32.42 ? 217 SER B CB    1 
ATOM   3919 O  OG    . SER B 1 223 ? -38.028 1.108   11.652  1.00 31.11 ? 217 SER B OG    1 
ATOM   3920 N  N     . ASP B 1 224 ? -40.569 3.499   12.308  1.00 31.58 ? 218 ASP B N     1 
ATOM   3921 C  CA    . ASP B 1 224 ? -40.437 4.735   13.114  1.00 35.03 ? 218 ASP B CA    1 
ATOM   3922 C  C     . ASP B 1 224 ? -39.020 4.757   13.709  1.00 32.22 ? 218 ASP B C     1 
ATOM   3923 O  O     . ASP B 1 224 ? -38.417 5.840   13.786  1.00 30.33 ? 218 ASP B O     1 
ATOM   3924 C  CB    . ASP B 1 224 ? -41.536 4.845   14.177  1.00 35.19 ? 218 ASP B CB    1 
ATOM   3925 C  CG    . ASP B 1 224 ? -42.939 5.096   13.638  1.00 41.93 ? 218 ASP B CG    1 
ATOM   3926 O  OD1   . ASP B 1 224 ? -43.097 5.520   12.441  1.00 36.75 ? 218 ASP B OD1   1 
ATOM   3927 O  OD2   . ASP B 1 224 ? -43.885 4.849   14.413  1.00 48.52 ? 218 ASP B OD2   1 
ATOM   3928 N  N     . ASP B 1 225 ? -38.504 3.601   14.109  1.00 30.06 ? 219 ASP B N     1 
ATOM   3929 C  CA    . ASP B 1 225 ? -37.141 3.473   14.686  1.00 31.90 ? 219 ASP B CA    1 
ATOM   3930 C  C     . ASP B 1 225 ? -36.088 3.840   13.635  1.00 28.70 ? 219 ASP B C     1 
ATOM   3931 O  O     . ASP B 1 225 ? -35.096 4.486   14.001  1.00 29.68 ? 219 ASP B O     1 
ATOM   3932 C  CB    . ASP B 1 225 ? -36.906 2.061   15.212  1.00 35.84 ? 219 ASP B CB    1 
ATOM   3933 C  CG    . ASP B 1 225 ? -37.504 1.829   16.593  1.00 45.22 ? 219 ASP B CG    1 
ATOM   3934 O  OD1   . ASP B 1 225 ? -38.313 2.683   17.057  1.00 46.04 ? 219 ASP B OD1   1 
ATOM   3935 O  OD2   . ASP B 1 225 ? -37.131 0.804   17.217  1.00 55.11 ? 219 ASP B OD2   1 
ATOM   3936 N  N     . GLU B 1 226 ? -36.257 3.417   12.392  1.00 25.29 ? 220 GLU B N     1 
ATOM   3937 C  CA    . GLU B 1 226 ? -35.309 3.762   11.294  1.00 25.90 ? 220 GLU B CA    1 
ATOM   3938 C  C     . GLU B 1 226 ? -35.339 5.271   11.037  1.00 24.81 ? 220 GLU B C     1 
ATOM   3939 O  O     . GLU B 1 226 ? -34.259 5.874   10.831  1.00 24.13 ? 220 GLU B O     1 
ATOM   3940 C  CB    . GLU B 1 226 ? -35.585 2.953   10.023  1.00 28.70 ? 220 GLU B CB    1 
ATOM   3941 C  CG    . GLU B 1 226 ? -35.226 1.497   10.163  1.00 32.10 ? 220 GLU B CG    1 
ATOM   3942 C  CD    . GLU B 1 226 ? -35.731 0.550   9.070   1.00 36.87 ? 220 GLU B CD    1 
ATOM   3943 O  OE1   . GLU B 1 226 ? -36.871 0.756   8.514   1.00 34.12 ? 220 GLU B OE1   1 
ATOM   3944 O  OE2   . GLU B 1 226 ? -34.972 -0.409  8.761   1.00 43.93 ? 220 GLU B OE2   1 
ATOM   3945 N  N     . PHE B 1 227 ? -36.515 5.890   11.086  1.00 25.09 ? 221 PHE B N     1 
ATOM   3946 C  CA    . PHE B 1 227 ? -36.634 7.362   10.914  1.00 24.80 ? 221 PHE B CA    1 
ATOM   3947 C  C     . PHE B 1 227 ? -35.884 8.039   12.063  1.00 26.73 ? 221 PHE B C     1 
ATOM   3948 O  O     . PHE B 1 227 ? -35.068 8.965   11.817  1.00 24.06 ? 221 PHE B O     1 
ATOM   3949 C  CB    . PHE B 1 227 ? -38.102 7.802   10.813  1.00 25.98 ? 221 PHE B CB    1 
ATOM   3950 C  CG    . PHE B 1 227 ? -38.263 9.286   10.636  1.00 21.85 ? 221 PHE B CG    1 
ATOM   3951 C  CD1   . PHE B 1 227 ? -37.991 9.886   9.424   1.00 22.69 ? 221 PHE B CD1   1 
ATOM   3952 C  CD2   . PHE B 1 227 ? -38.589 10.090  11.712  1.00 25.26 ? 221 PHE B CD2   1 
ATOM   3953 C  CE1   . PHE B 1 227 ? -38.047 11.256  9.281   1.00 23.34 ? 221 PHE B CE1   1 
ATOM   3954 C  CE2   . PHE B 1 227 ? -38.678 11.462  11.563  1.00 25.21 ? 221 PHE B CE2   1 
ATOM   3955 C  CZ    . PHE B 1 227 ? -38.417 12.043  10.344  1.00 23.29 ? 221 PHE B CZ    1 
ATOM   3956 N  N     . ASP B 1 228 ? -36.119 7.576   13.290  1.00 26.80 ? 222 ASP B N     1 
ATOM   3957 C  CA    . ASP B 1 228 ? -35.491 8.197   14.489  1.00 28.96 ? 222 ASP B CA    1 
ATOM   3958 C  C     . ASP B 1 228 ? -33.978 8.061   14.378  1.00 26.40 ? 222 ASP B C     1 
ATOM   3959 O  O     . ASP B 1 228 ? -33.272 9.027   14.716  1.00 26.83 ? 222 ASP B O     1 
ATOM   3960 C  CB    . ASP B 1 228 ? -36.044 7.598   15.782  1.00 31.42 ? 222 ASP B CB    1 
ATOM   3961 C  CG    . ASP B 1 228 ? -37.464 8.055   16.045  1.00 39.39 ? 222 ASP B CG    1 
ATOM   3962 O  OD1   . ASP B 1 228 ? -37.849 9.123   15.506  1.00 40.66 ? 222 ASP B OD1   1 
ATOM   3963 O  OD2   . ASP B 1 228 ? -38.191 7.319   16.736  1.00 41.21 ? 222 ASP B OD2   1 
ATOM   3964 N  N     . ARG B 1 229 ? -33.488 6.908   13.910  1.00 26.84 ? 223 ARG B N     1 
ATOM   3965 C  CA    . ARG B 1 229 ? -32.027 6.678   13.842  1.00 26.53 ? 223 ARG B CA    1 
ATOM   3966 C  C     . ARG B 1 229 ? -31.401 7.611   12.803  1.00 24.58 ? 223 ARG B C     1 
ATOM   3967 O  O     . ARG B 1 229 ? -30.274 8.063   13.058  1.00 25.10 ? 223 ARG B O     1 
ATOM   3968 C  CB    . ARG B 1 229 ? -31.704 5.209   13.565  1.00 30.23 ? 223 ARG B CB    1 
ATOM   3969 C  CG    . ARG B 1 229 ? -31.887 4.329   14.794  1.00 38.87 ? 223 ARG B CG    1 
ATOM   3970 C  CD    . ARG B 1 229 ? -31.312 2.942   14.604  1.00 48.43 ? 223 ARG B CD    1 
ATOM   3971 N  NE    . ARG B 1 229 ? -32.317 1.957   14.202  1.00 57.13 ? 223 ARG B NE    1 
ATOM   3972 C  CZ    . ARG B 1 229 ? -32.508 1.466   12.972  1.00 57.25 ? 223 ARG B CZ    1 
ATOM   3973 N  NH1   . ARG B 1 229 ? -33.453 0.557   12.812  1.00 55.59 ? 223 ARG B NH1   1 
ATOM   3974 N  NH2   . ARG B 1 229 ? -31.786 1.868   11.920  1.00 55.29 ? 223 ARG B NH2   1 
ATOM   3975 N  N     . PHE B 1 230 ? -32.073 7.881   11.668  1.00 23.49 ? 224 PHE B N     1 
ATOM   3976 C  CA    . PHE B 1 230 ? -31.594 8.898   10.698  1.00 21.82 ? 224 PHE B CA    1 
ATOM   3977 C  C     . PHE B 1 230 ? -31.448 10.227  11.434  1.00 21.73 ? 224 PHE B C     1 
ATOM   3978 O  O     . PHE B 1 230 ? -30.412 10.879  11.315  1.00 21.96 ? 224 PHE B O     1 
ATOM   3979 C  CB    . PHE B 1 230 ? -32.518 9.058   9.489   1.00 22.53 ? 224 PHE B CB    1 
ATOM   3980 C  CG    . PHE B 1 230 ? -32.027 10.080  8.504   1.00 21.02 ? 224 PHE B CG    1 
ATOM   3981 C  CD1   . PHE B 1 230 ? -32.355 11.412  8.657   1.00 22.40 ? 224 PHE B CD1   1 
ATOM   3982 C  CD2   . PHE B 1 230 ? -31.237 9.710   7.430   1.00 23.35 ? 224 PHE B CD2   1 
ATOM   3983 C  CE1   . PHE B 1 230 ? -31.919 12.355  7.747   1.00 23.71 ? 224 PHE B CE1   1 
ATOM   3984 C  CE2   . PHE B 1 230 ? -30.765 10.664  6.541   1.00 24.77 ? 224 PHE B CE2   1 
ATOM   3985 C  CZ    . PHE B 1 230 ? -31.111 11.981  6.703   1.00 24.82 ? 224 PHE B CZ    1 
ATOM   3986 N  N     . CYS B 1 231 ? -32.480 10.662  12.166  1.00 24.63 ? 225 CYS B N     1 
ATOM   3987 C  CA    . CYS B 1 231 ? -32.452 11.993  12.828  1.00 25.80 ? 225 CYS B CA    1 
ATOM   3988 C  C     . CYS B 1 231 ? -31.306 12.032  13.861  1.00 25.22 ? 225 CYS B C     1 
ATOM   3989 O  O     . CYS B 1 231 ? -30.575 13.037  13.882  1.00 24.29 ? 225 CYS B O     1 
ATOM   3990 C  CB    . CYS B 1 231 ? -33.811 12.387  13.403  1.00 29.95 ? 225 CYS B CB    1 
ATOM   3991 S  SG    . CYS B 1 231 ? -35.043 12.558  12.078  1.00 32.17 ? 225 CYS B SG    1 
ATOM   3992 N  N     . GLU B 1 232 ? -31.145 10.970  14.651  1.00 27.22 ? 226 GLU B N     1 
ATOM   3993 C  CA    . GLU B 1 232 ? -30.103 10.843  15.711  1.00 29.24 ? 226 GLU B CA    1 
ATOM   3994 C  C     . GLU B 1 232 ? -28.705 10.933  15.085  1.00 29.80 ? 226 GLU B C     1 
ATOM   3995 O  O     . GLU B 1 232 ? -27.877 11.661  15.639  1.00 26.74 ? 226 GLU B O     1 
ATOM   3996 C  CB    . GLU B 1 232 ? -30.319 9.552   16.508  1.00 34.31 ? 226 GLU B CB    1 
ATOM   3997 C  CG    . GLU B 1 232 ? -31.556 9.681   17.414  1.00 44.96 ? 226 GLU B CG    1 
ATOM   3998 C  CD    . GLU B 1 232 ? -32.322 8.439   17.864  1.00 50.21 ? 226 GLU B CD    1 
ATOM   3999 O  OE1   . GLU B 1 232 ? -31.827 7.284   17.686  1.00 52.85 ? 226 GLU B OE1   1 
ATOM   4000 O  OE2   . GLU B 1 232 ? -33.438 8.635   18.397  1.00 54.15 ? 226 GLU B OE2   1 
ATOM   4001 N  N     . ARG B 1 233 ? -28.467 10.304  13.926  1.00 26.80 ? 227 ARG B N     1 
ATOM   4002 C  CA    A ARG B 1 233 ? -27.123 10.306  13.285  0.50 27.19 ? 227 ARG B CA    1 
ATOM   4003 C  CA    B ARG B 1 233 ? -27.133 10.302  13.263  0.50 27.22 ? 227 ARG B CA    1 
ATOM   4004 C  C     . ARG B 1 233 ? -26.799 11.729  12.785  1.00 27.00 ? 227 ARG B C     1 
ATOM   4005 O  O     . ARG B 1 233 ? -25.605 12.012  12.521  1.00 25.85 ? 227 ARG B O     1 
ATOM   4006 C  CB    A ARG B 1 233 ? -27.024 9.229   12.194  0.50 28.41 ? 227 ARG B CB    1 
ATOM   4007 C  CB    B ARG B 1 233 ? -27.082 9.260   12.135  0.50 28.45 ? 227 ARG B CB    1 
ATOM   4008 C  CG    A ARG B 1 233 ? -26.676 7.836   12.721  0.50 31.78 ? 227 ARG B CG    1 
ATOM   4009 C  CG    B ARG B 1 233 ? -27.001 7.812   12.619  0.50 31.96 ? 227 ARG B CG    1 
ATOM   4010 C  CD    A ARG B 1 233 ? -26.393 6.798   11.627  0.50 31.37 ? 227 ARG B CD    1 
ATOM   4011 C  CD    B ARG B 1 233 ? -26.668 6.779   11.531  0.50 32.55 ? 227 ARG B CD    1 
ATOM   4012 N  NE    A ARG B 1 233 ? -27.388 6.874   10.547  0.50 28.93 ? 227 ARG B NE    1 
ATOM   4013 N  NE    B ARG B 1 233 ? -27.225 7.166   10.233  0.50 28.82 ? 227 ARG B NE    1 
ATOM   4014 C  CZ    A ARG B 1 233 ? -27.258 7.630   9.464   0.50 25.66 ? 227 ARG B CZ    1 
ATOM   4015 C  CZ    B ARG B 1 233 ? -28.334 6.685   9.667   0.50 25.55 ? 227 ARG B CZ    1 
ATOM   4016 N  NH1   A ARG B 1 233 ? -26.163 8.356   9.302   0.50 22.31 ? 227 ARG B NH1   1 
ATOM   4017 N  NH1   B ARG B 1 233 ? -28.711 7.214   8.515   0.50 25.81 ? 227 ARG B NH1   1 
ATOM   4018 N  NH2   A ARG B 1 233 ? -28.238 7.683   8.574   0.50 25.25 ? 227 ARG B NH2   1 
ATOM   4019 N  NH2   B ARG B 1 233 ? -29.062 5.718   10.225  0.50 23.48 ? 227 ARG B NH2   1 
ATOM   4020 N  N     . HIS B 1 234 ? -27.790 12.624  12.702  1.00 21.89 ? 228 HIS B N     1 
ATOM   4021 C  CA    . HIS B 1 234 ? -27.608 14.008  12.190  1.00 22.55 ? 228 HIS B CA    1 
ATOM   4022 C  C     . HIS B 1 234 ? -27.945 15.006  13.313  1.00 24.57 ? 228 HIS B C     1 
ATOM   4023 O  O     . HIS B 1 234 ? -28.231 16.165  13.001  1.00 21.01 ? 228 HIS B O     1 
ATOM   4024 C  CB    . HIS B 1 234 ? -28.448 14.198  10.914  1.00 23.46 ? 228 HIS B CB    1 
ATOM   4025 C  CG    . HIS B 1 234 ? -28.014 13.338  9.778   1.00 22.99 ? 228 HIS B CG    1 
ATOM   4026 N  ND1   . HIS B 1 234 ? -28.593 12.102  9.506   1.00 23.32 ? 228 HIS B ND1   1 
ATOM   4027 C  CD2   . HIS B 1 234 ? -27.073 13.551  8.820   1.00 23.75 ? 228 HIS B CD2   1 
ATOM   4028 C  CE1   . HIS B 1 234 ? -27.979 11.564  8.463   1.00 22.87 ? 228 HIS B CE1   1 
ATOM   4029 N  NE2   . HIS B 1 234 ? -27.057 12.461  7.988   1.00 21.75 ? 228 HIS B NE2   1 
ATOM   4030 N  N     . SER B 1 235 ? -27.858 14.582  14.584  1.00 27.60 ? 229 SER B N     1 
ATOM   4031 C  CA    . SER B 1 235 ? -28.200 15.427  15.760  1.00 30.76 ? 229 SER B CA    1 
ATOM   4032 C  C     . SER B 1 235 ? -27.247 16.625  15.872  1.00 30.19 ? 229 SER B C     1 
ATOM   4033 O  O     . SER B 1 235 ? -27.664 17.614  16.459  1.00 32.29 ? 229 SER B O     1 
ATOM   4034 C  CB    . SER B 1 235 ? -28.231 14.604  17.049  1.00 32.62 ? 229 SER B CB    1 
ATOM   4035 O  OG    . SER B 1 235 ? -26.929 14.143  17.376  1.00 30.64 ? 229 SER B OG    1 
ATOM   4036 N  N     . SER B 1 236 ? -26.058 16.617  15.255  1.00 28.02 ? 230 SER B N     1 
ATOM   4037 C  CA    . SER B 1 236 ? -25.158 17.804  15.285  1.00 29.67 ? 230 SER B CA    1 
ATOM   4038 C  C     . SER B 1 236 ? -25.684 18.944  14.406  1.00 30.23 ? 230 SER B C     1 
ATOM   4039 O  O     . SER B 1 236 ? -25.196 20.092  14.585  1.00 28.90 ? 230 SER B O     1 
ATOM   4040 C  CB    . SER B 1 236 ? -23.742 17.447  14.912  1.00 34.82 ? 230 SER B CB    1 
ATOM   4041 O  OG    . SER B 1 236 ? -23.656 17.021  13.551  1.00 38.18 ? 230 SER B OG    1 
ATOM   4042 N  N     . GLN B 1 237 ? -26.671 18.696  13.525  1.00 28.37 ? 231 GLN B N     1 
ATOM   4043 C  CA    . GLN B 1 237 ? -27.252 19.737  12.619  1.00 27.07 ? 231 GLN B CA    1 
ATOM   4044 C  C     . GLN B 1 237 ? -28.294 20.541  13.393  1.00 26.43 ? 231 GLN B C     1 
ATOM   4045 O  O     . GLN B 1 237 ? -29.424 20.036  13.633  1.00 28.19 ? 231 GLN B O     1 
ATOM   4046 C  CB    . GLN B 1 237 ? -27.876 19.108  11.373  1.00 27.38 ? 231 GLN B CB    1 
ATOM   4047 C  CG    . GLN B 1 237 ? -26.906 18.217  10.605  1.00 28.62 ? 231 GLN B CG    1 
ATOM   4048 C  CD    . GLN B 1 237 ? -25.703 19.019  10.211  1.00 30.03 ? 231 GLN B CD    1 
ATOM   4049 O  OE1   . GLN B 1 237 ? -25.853 20.203  9.926   1.00 32.87 ? 231 GLN B OE1   1 
ATOM   4050 N  NE2   . GLN B 1 237 ? -24.531 18.393  10.214  1.00 27.34 ? 231 GLN B NE2   1 
ATOM   4051 N  N     . THR B 1 238 ? -27.961 21.761  13.764  1.00 29.68 ? 232 THR B N     1 
ATOM   4052 C  CA    . THR B 1 238 ? -28.868 22.654  14.526  1.00 31.05 ? 232 THR B CA    1 
ATOM   4053 C  C     . THR B 1 238 ? -30.027 23.098  13.622  1.00 29.82 ? 232 THR B C     1 
ATOM   4054 O  O     . THR B 1 238 ? -31.086 23.418  14.178  1.00 31.11 ? 232 THR B O     1 
ATOM   4055 C  CB    . THR B 1 238 ? -28.086 23.833  15.113  1.00 34.64 ? 232 THR B CB    1 
ATOM   4056 O  OG1   . THR B 1 238 ? -27.571 24.609  14.027  1.00 40.69 ? 232 THR B OG1   1 
ATOM   4057 C  CG2   . THR B 1 238 ? -26.936 23.363  15.982  1.00 35.74 ? 232 THR B CG2   1 
ATOM   4058 N  N     . CYS B 1 239 ? -29.854 23.043  12.293  1.00 28.74 ? 233 CYS B N     1 
ATOM   4059 C  CA    . CYS B 1 239 ? -30.893 23.412  11.278  1.00 27.85 ? 233 CYS B CA    1 
ATOM   4060 C  C     . CYS B 1 239 ? -31.969 22.315  11.120  1.00 25.87 ? 233 CYS B C     1 
ATOM   4061 O  O     . CYS B 1 239 ? -32.981 22.570  10.383  1.00 23.48 ? 233 CYS B O     1 
ATOM   4062 C  CB    . CYS B 1 239 ? -30.240 23.670  9.921   1.00 29.40 ? 233 CYS B CB    1 
ATOM   4063 S  SG    . CYS B 1 239 ? -29.291 22.263  9.261   1.00 32.97 ? 233 CYS B SG    1 
ATOM   4064 N  N     . LEU B 1 240 ? -31.773 21.126  11.695  1.00 23.34 ? 234 LEU B N     1 
ATOM   4065 C  CA    . LEU B 1 240 ? -32.621 19.928  11.422  1.00 22.72 ? 234 LEU B CA    1 
ATOM   4066 C  C     . LEU B 1 240 ? -34.011 20.147  12.002  1.00 25.16 ? 234 LEU B C     1 
ATOM   4067 O  O     . LEU B 1 240 ? -34.113 20.475  13.185  1.00 23.47 ? 234 LEU B O     1 
ATOM   4068 C  CB    . LEU B 1 240 ? -31.943 18.706  12.024  1.00 25.33 ? 234 LEU B CB    1 
ATOM   4069 C  CG    . LEU B 1 240 ? -32.686 17.373  12.010  1.00 30.32 ? 234 LEU B CG    1 
ATOM   4070 C  CD1   . LEU B 1 240 ? -33.317 17.041  10.691  1.00 32.49 ? 234 LEU B CD1   1 
ATOM   4071 C  CD2   . LEU B 1 240 ? -31.738 16.252  12.401  1.00 32.32 ? 234 LEU B CD2   1 
ATOM   4072 N  N     . VAL B 1 241 ? -35.043 20.021  11.169  1.00 24.23 ? 235 VAL B N     1 
ATOM   4073 C  CA    . VAL B 1 241 ? -36.471 20.112  11.554  1.00 22.45 ? 235 VAL B CA    1 
ATOM   4074 C  C     . VAL B 1 241 ? -37.118 18.781  11.187  1.00 21.51 ? 235 VAL B C     1 
ATOM   4075 O  O     . VAL B 1 241 ? -37.458 18.544  10.028  1.00 21.57 ? 235 VAL B O     1 
ATOM   4076 C  CB    . VAL B 1 241 ? -37.140 21.291  10.852  1.00 22.29 ? 235 VAL B CB    1 
ATOM   4077 C  CG1   . VAL B 1 241 ? -38.601 21.432  11.245  1.00 23.22 ? 235 VAL B CG1   1 
ATOM   4078 C  CG2   . VAL B 1 241 ? -36.369 22.574  11.075  1.00 22.18 ? 235 VAL B CG2   1 
ATOM   4079 N  N     . PRO B 1 242 ? -37.245 17.839  12.135  1.00 21.27 ? 236 PRO B N     1 
ATOM   4080 C  CA    . PRO B 1 242 ? -37.822 16.523  11.840  1.00 23.40 ? 236 PRO B CA    1 
ATOM   4081 C  C     . PRO B 1 242 ? -39.349 16.597  11.810  1.00 23.72 ? 236 PRO B C     1 
ATOM   4082 O  O     . PRO B 1 242 ? -39.921 17.297  12.628  1.00 23.05 ? 236 PRO B O     1 
ATOM   4083 C  CB    . PRO B 1 242 ? -37.422 15.619  13.008  1.00 25.51 ? 236 PRO B CB    1 
ATOM   4084 C  CG    . PRO B 1 242 ? -36.526 16.508  13.901  1.00 29.20 ? 236 PRO B CG    1 
ATOM   4085 C  CD    . PRO B 1 242 ? -36.835 17.957  13.546  1.00 25.56 ? 236 PRO B CD    1 
ATOM   4086 N  N     . GLU B 1 243 ? -39.964 15.893  10.876  1.00 21.85 ? 237 GLU B N     1 
ATOM   4087 C  CA    . GLU B 1 243 ? -41.437 15.878  10.683  1.00 21.38 ? 237 GLU B CA    1 
ATOM   4088 C  C     . GLU B 1 243 ? -41.909 14.456  10.485  1.00 21.67 ? 237 GLU B C     1 
ATOM   4089 O  O     . GLU B 1 243 ? -42.120 14.015  9.352   1.00 22.53 ? 237 GLU B O     1 
ATOM   4090 C  CB    . GLU B 1 243 ? -41.850 16.761  9.522   1.00 21.64 ? 237 GLU B CB    1 
ATOM   4091 C  CG    . GLU B 1 243 ? -41.534 18.208  9.757   1.00 23.00 ? 237 GLU B CG    1 
ATOM   4092 C  CD    . GLU B 1 243 ? -42.271 19.176  8.864   1.00 25.64 ? 237 GLU B CD    1 
ATOM   4093 O  OE1   . GLU B 1 243 ? -43.375 18.818  8.355   1.00 22.99 ? 237 GLU B OE1   1 
ATOM   4094 O  OE2   . GLU B 1 243 ? -41.759 20.282  8.707   1.00 23.58 ? 237 GLU B OE2   1 
ATOM   4095 N  N     . PRO B 1 244 ? -42.096 13.720  11.594  1.00 22.85 ? 238 PRO B N     1 
ATOM   4096 C  CA    . PRO B 1 244 ? -42.810 12.455  11.554  1.00 22.99 ? 238 PRO B CA    1 
ATOM   4097 C  C     . PRO B 1 244 ? -44.249 12.685  11.062  1.00 21.31 ? 238 PRO B C     1 
ATOM   4098 O  O     . PRO B 1 244 ? -44.716 13.806  11.084  1.00 20.89 ? 238 PRO B O     1 
ATOM   4099 C  CB    . PRO B 1 244 ? -42.865 11.956  13.005  1.00 24.64 ? 238 PRO B CB    1 
ATOM   4100 C  CG    . PRO B 1 244 ? -41.946 12.879  13.784  1.00 26.87 ? 238 PRO B CG    1 
ATOM   4101 C  CD    . PRO B 1 244 ? -41.775 14.146  12.968  1.00 23.75 ? 238 PRO B CD    1 
ATOM   4102 N  N     . ASN B 1 245 ? -44.934 11.631  10.653  1.00 22.73 ? 239 ASN B N     1 
ATOM   4103 C  CA    . ASN B 1 245 ? -46.347 11.734  10.169  1.00 23.07 ? 239 ASN B CA    1 
ATOM   4104 C  C     . ASN B 1 245 ? -47.240 12.490  11.171  1.00 23.05 ? 239 ASN B C     1 
ATOM   4105 O  O     . ASN B 1 245 ? -48.080 13.323  10.747  1.00 22.83 ? 239 ASN B O     1 
ATOM   4106 C  CB    . ASN B 1 245 ? -46.953 10.362  9.876   1.00 24.49 ? 239 ASN B CB    1 
ATOM   4107 C  CG    . ASN B 1 245 ? -46.325 9.621   8.708   1.00 25.00 ? 239 ASN B CG    1 
ATOM   4108 O  OD1   . ASN B 1 245 ? -45.523 10.166  7.931   1.00 27.56 ? 239 ASN B OD1   1 
ATOM   4109 N  ND2   . ASN B 1 245 ? -46.729 8.376   8.546   1.00 22.06 ? 239 ASN B ND2   1 
ATOM   4110 N  N     . ARG B 1 246 ? -47.035 12.282  12.467  1.00 22.48 ? 240 ARG B N     1 
ATOM   4111 C  CA    . ARG B 1 246 ? -47.891 12.883  13.523  1.00 25.31 ? 240 ARG B CA    1 
ATOM   4112 C  C     . ARG B 1 246 ? -47.863 14.399  13.357  1.00 23.95 ? 240 ARG B C     1 
ATOM   4113 O  O     . ARG B 1 246 ? -48.905 15.048  13.577  1.00 25.71 ? 240 ARG B O     1 
ATOM   4114 C  CB    . ARG B 1 246 ? -47.409 12.394  14.891  1.00 29.96 ? 240 ARG B CB    1 
ATOM   4115 C  CG    . ARG B 1 246 ? -47.833 13.273  16.054  1.00 36.15 ? 240 ARG B CG    1 
ATOM   4116 C  CD    . ARG B 1 246 ? -47.281 12.763  17.375  1.00 35.88 ? 240 ARG B CD    1 
ATOM   4117 N  NE    . ARG B 1 246 ? -47.628 13.692  18.446  1.00 33.31 ? 240 ARG B NE    1 
ATOM   4118 C  CZ    . ARG B 1 246 ? -46.876 14.723  18.819  1.00 35.42 ? 240 ARG B CZ    1 
ATOM   4119 N  NH1   . ARG B 1 246 ? -45.723 14.964  18.208  1.00 34.71 ? 240 ARG B NH1   1 
ATOM   4120 N  NH2   . ARG B 1 246 ? -47.258 15.496  19.825  1.00 31.12 ? 240 ARG B NH2   1 
ATOM   4121 N  N     . LEU B 1 247 ? -46.709 14.981  13.049  1.00 23.08 ? 241 LEU B N     1 
ATOM   4122 C  CA    . LEU B 1 247 ? -46.597 16.463  12.922  1.00 21.59 ? 241 LEU B CA    1 
ATOM   4123 C  C     . LEU B 1 247 ? -46.845 16.935  11.482  1.00 22.14 ? 241 LEU B C     1 
ATOM   4124 O  O     . LEU B 1 247 ? -47.178 18.136  11.301  1.00 27.26 ? 241 LEU B O     1 
ATOM   4125 C  CB    . LEU B 1 247 ? -45.214 16.915  13.393  1.00 22.19 ? 241 LEU B CB    1 
ATOM   4126 C  CG    . LEU B 1 247 ? -44.965 16.886  14.898  1.00 25.83 ? 241 LEU B CG    1 
ATOM   4127 C  CD1   . LEU B 1 247 ? -43.586 17.434  15.249  1.00 28.35 ? 241 LEU B CD1   1 
ATOM   4128 C  CD2   . LEU B 1 247 ? -46.052 17.635  15.668  1.00 28.64 ? 241 LEU B CD2   1 
ATOM   4129 N  N     . MET B 1 248 ? -46.607 16.103  10.464  1.00 20.88 ? 242 MET B N     1 
ATOM   4130 C  CA    . MET B 1 248 ? -46.675 16.596  9.067   1.00 20.97 ? 242 MET B CA    1 
ATOM   4131 C  C     . MET B 1 248 ? -48.133 16.560  8.548   1.00 21.40 ? 242 MET B C     1 
ATOM   4132 O  O     . MET B 1 248 ? -48.508 17.460  7.789   1.00 21.26 ? 242 MET B O     1 
ATOM   4133 C  CB    . MET B 1 248 ? -45.777 15.765  8.159   1.00 20.86 ? 242 MET B CB    1 
ATOM   4134 C  CG    . MET B 1 248 ? -45.518 16.440  6.840   1.00 23.12 ? 242 MET B CG    1 
ATOM   4135 S  SD    . MET B 1 248 ? -44.548 15.456  5.670   1.00 22.68 ? 242 MET B SD    1 
ATOM   4136 C  CE    . MET B 1 248 ? -44.282 16.719  4.432   1.00 22.73 ? 242 MET B CE    1 
ATOM   4137 N  N     . ALA B 1 249 ? -48.918 15.557  8.920   1.00 21.11 ? 243 ALA B N     1 
ATOM   4138 C  CA    . ALA B 1 249 ? -50.108 15.166  8.137   1.00 22.84 ? 243 ALA B CA    1 
ATOM   4139 C  C     . ALA B 1 249 ? -51.109 16.339  8.065   1.00 24.51 ? 243 ALA B C     1 
ATOM   4140 O  O     . ALA B 1 249 ? -51.616 16.610  6.936   1.00 23.11 ? 243 ALA B O     1 
ATOM   4141 C  CB    . ALA B 1 249 ? -50.695 13.884  8.703   1.00 23.84 ? 243 ALA B CB    1 
ATOM   4142 N  N     . LYS B 1 250 ? -51.385 17.044  9.172   1.00 21.27 ? 244 LYS B N     1 
ATOM   4143 C  CA    . LYS B 1 250 ? -52.548 17.979  9.213   1.00 23.44 ? 244 LYS B CA    1 
ATOM   4144 C  C     . LYS B 1 250 ? -52.141 19.383  9.657   1.00 23.15 ? 244 LYS B C     1 
ATOM   4145 O  O     . LYS B 1 250 ? -53.053 20.178  10.003  1.00 22.99 ? 244 LYS B O     1 
ATOM   4146 C  CB    . LYS B 1 250 ? -53.651 17.401  10.107  1.00 27.30 ? 244 LYS B CB    1 
ATOM   4147 C  CG    . LYS B 1 250 ? -54.250 16.096  9.600   1.00 29.46 ? 244 LYS B CG    1 
ATOM   4148 C  CD    . LYS B 1 250 ? -54.799 15.214  10.692  1.00 36.26 ? 244 LYS B CD    1 
ATOM   4149 C  CE    . LYS B 1 250 ? -55.093 13.810  10.223  1.00 45.07 ? 244 LYS B CE    1 
ATOM   4150 N  NZ    . LYS B 1 250 ? -54.706 12.823  11.259  1.00 49.70 ? 244 LYS B NZ    1 
ATOM   4151 N  N     . SER B 1 251 ? -50.846 19.717  9.570   1.00 19.57 ? 245 SER B N     1 
ATOM   4152 C  CA    . SER B 1 251 ? -50.263 20.945  10.136  1.00 20.45 ? 245 SER B CA    1 
ATOM   4153 C  C     . SER B 1 251 ? -50.040 21.986  9.040   1.00 20.38 ? 245 SER B C     1 
ATOM   4154 O  O     . SER B 1 251 ? -49.515 23.048  9.362   1.00 19.59 ? 245 SER B O     1 
ATOM   4155 C  CB    . SER B 1 251 ? -48.988 20.650  10.889  1.00 21.03 ? 245 SER B CB    1 
ATOM   4156 O  OG    . SER B 1 251 ? -48.025 20.061  10.032  1.00 19.29 ? 245 SER B OG    1 
ATOM   4157 N  N     . TYR B 1 252 ? -50.413 21.704  7.797   1.00 18.30 ? 246 TYR B N     1 
ATOM   4158 C  CA    . TYR B 1 252 ? -50.227 22.637  6.670   1.00 18.29 ? 246 TYR B CA    1 
ATOM   4159 C  C     . TYR B 1 252 ? -51.584 23.169  6.206   1.00 19.10 ? 246 TYR B C     1 
ATOM   4160 O  O     . TYR B 1 252 ? -52.567 22.422  6.244   1.00 21.89 ? 246 TYR B O     1 
ATOM   4161 C  CB    . TYR B 1 252 ? -49.471 21.979  5.520   1.00 18.84 ? 246 TYR B CB    1 
ATOM   4162 C  CG    . TYR B 1 252 ? -48.021 21.657  5.839   1.00 17.84 ? 246 TYR B CG    1 
ATOM   4163 C  CD1   . TYR B 1 252 ? -47.676 20.540  6.590   1.00 18.35 ? 246 TYR B CD1   1 
ATOM   4164 C  CD2   . TYR B 1 252 ? -47.000 22.484  5.417   1.00 19.83 ? 246 TYR B CD2   1 
ATOM   4165 C  CE1   . TYR B 1 252 ? -46.354 20.236  6.881   1.00 18.30 ? 246 TYR B CE1   1 
ATOM   4166 C  CE2   . TYR B 1 252 ? -45.674 22.173  5.658   1.00 19.13 ? 246 TYR B CE2   1 
ATOM   4167 C  CZ    . TYR B 1 252 ? -45.353 21.038  6.383   1.00 19.28 ? 246 TYR B CZ    1 
ATOM   4168 O  OH    . TYR B 1 252 ? -44.032 20.748  6.648   1.00 20.90 ? 246 TYR B OH    1 
ATOM   4169 N  N     . LEU B 1 253 ? -51.573 24.417  5.744   1.00 19.24 ? 247 LEU B N     1 
ATOM   4170 C  CA    . LEU B 1 253 ? -52.652 25.039  4.937   1.00 19.80 ? 247 LEU B CA    1 
ATOM   4171 C  C     . LEU B 1 253 ? -52.270 24.882  3.463   1.00 20.48 ? 247 LEU B C     1 
ATOM   4172 O  O     . LEU B 1 253 ? -51.252 25.477  3.037   1.00 20.35 ? 247 LEU B O     1 
ATOM   4173 C  CB    . LEU B 1 253 ? -52.802 26.510  5.321   1.00 21.18 ? 247 LEU B CB    1 
ATOM   4174 C  CG    . LEU B 1 253 ? -53.332 26.749  6.731   1.00 25.13 ? 247 LEU B CG    1 
ATOM   4175 C  CD1   . LEU B 1 253 ? -53.178 28.217  7.123   1.00 28.05 ? 247 LEU B CD1   1 
ATOM   4176 C  CD2   . LEU B 1 253 ? -54.782 26.330  6.858   1.00 25.36 ? 247 LEU B CD2   1 
ATOM   4177 N  N     . ILE B 1 254 ? -53.025 24.044  2.747   1.00 20.88 ? 248 ILE B N     1 
ATOM   4178 C  CA    . ILE B 1 254 ? -52.668 23.568  1.380   1.00 20.13 ? 248 ILE B CA    1 
ATOM   4179 C  C     . ILE B 1 254 ? -53.725 24.039  0.386   1.00 19.77 ? 248 ILE B C     1 
ATOM   4180 O  O     . ILE B 1 254 ? -54.859 23.581  0.494   1.00 22.10 ? 248 ILE B O     1 
ATOM   4181 C  CB    . ILE B 1 254 ? -52.516 22.037  1.364   1.00 20.08 ? 248 ILE B CB    1 
ATOM   4182 C  CG1   . ILE B 1 254 ? -51.503 21.575  2.421   1.00 21.47 ? 248 ILE B CG1   1 
ATOM   4183 C  CG2   . ILE B 1 254 ? -52.131 21.599  -0.037  1.00 23.00 ? 248 ILE B CG2   1 
ATOM   4184 C  CD1   . ILE B 1 254 ? -51.418 20.078  2.597   1.00 23.32 ? 248 ILE B CD1   1 
ATOM   4185 N  N     . LEU B 1 255 ? -53.352 24.904  -0.532  1.00 19.33 ? 249 LEU B N     1 
ATOM   4186 C  CA    . LEU B 1 255 ? -54.219 25.343  -1.647  1.00 21.60 ? 249 LEU B CA    1 
ATOM   4187 C  C     . LEU B 1 255 ? -53.827 24.571  -2.911  1.00 21.63 ? 249 LEU B C     1 
ATOM   4188 O  O     . LEU B 1 255 ? -52.642 24.570  -3.266  1.00 20.89 ? 249 LEU B O     1 
ATOM   4189 C  CB    . LEU B 1 255 ? -54.067 26.834  -1.874  1.00 24.75 ? 249 LEU B CB    1 
ATOM   4190 C  CG    . LEU B 1 255 ? -54.819 27.767  -0.956  1.00 27.16 ? 249 LEU B CG    1 
ATOM   4191 C  CD1   . LEU B 1 255 ? -54.416 29.191  -1.335  1.00 29.60 ? 249 LEU B CD1   1 
ATOM   4192 C  CD2   . LEU B 1 255 ? -56.324 27.582  -1.057  1.00 25.82 ? 249 LEU B CD2   1 
ATOM   4193 N  N     . ASP B 1 256 ? -54.798 23.950  -3.580  1.00 22.08 ? 250 ASP B N     1 
ATOM   4194 C  CA    . ASP B 1 256 ? -54.552 23.196  -4.830  1.00 19.89 ? 250 ASP B CA    1 
ATOM   4195 C  C     . ASP B 1 256 ? -54.576 24.169  -6.019  1.00 21.29 ? 250 ASP B C     1 
ATOM   4196 O  O     . ASP B 1 256 ? -54.613 25.404  -5.806  1.00 19.10 ? 250 ASP B O     1 
ATOM   4197 C  CB    . ASP B 1 256 ? -55.511 22.024  -4.956  1.00 19.79 ? 250 ASP B CB    1 
ATOM   4198 C  CG    . ASP B 1 256 ? -56.951 22.367  -5.327  1.00 21.56 ? 250 ASP B CG    1 
ATOM   4199 O  OD1   . ASP B 1 256 ? -57.282 23.597  -5.501  1.00 21.82 ? 250 ASP B OD1   1 
ATOM   4200 O  OD2   . ASP B 1 256 ? -57.740 21.392  -5.457  1.00 22.88 ? 250 ASP B OD2   1 
ATOM   4201 N  N     . GLU B 1 257 ? -54.604 23.616  -7.235  1.00 19.15 ? 251 GLU B N     1 
ATOM   4202 C  CA    . GLU B 1 257 ? -54.397 24.394  -8.461  1.00 19.10 ? 251 GLU B CA    1 
ATOM   4203 C  C     . GLU B 1 257 ? -55.665 25.191  -8.783  1.00 19.32 ? 251 GLU B C     1 
ATOM   4204 O  O     . GLU B 1 257 ? -55.588 26.058  -9.685  1.00 21.43 ? 251 GLU B O     1 
ATOM   4205 C  CB    . GLU B 1 257 ? -53.959 23.499  -9.631  1.00 19.39 ? 251 GLU B CB    1 
ATOM   4206 C  CG    . GLU B 1 257 ? -54.960 22.425  -10.043 1.00 22.23 ? 251 GLU B CG    1 
ATOM   4207 C  CD    . GLU B 1 257 ? -55.055 21.090  -9.316  1.00 24.19 ? 251 GLU B CD    1 
ATOM   4208 O  OE1   . GLU B 1 257 ? -54.574 20.965  -8.162  1.00 24.28 ? 251 GLU B OE1   1 
ATOM   4209 O  OE2   . GLU B 1 257 ? -55.640 20.128  -9.929  1.00 28.00 ? 251 GLU B OE2   1 
ATOM   4210 N  N     . TYR B 1 258 ? -56.768 24.915  -8.088  1.00 21.26 ? 252 TYR B N     1 
ATOM   4211 C  CA    . TYR B 1 258 ? -58.052 25.648  -8.229  1.00 22.17 ? 252 TYR B CA    1 
ATOM   4212 C  C     . TYR B 1 258 ? -58.254 26.598  -7.037  1.00 22.82 ? 252 TYR B C     1 
ATOM   4213 O  O     . TYR B 1 258 ? -59.351 27.197  -6.897  1.00 26.86 ? 252 TYR B O     1 
ATOM   4214 C  CB    . TYR B 1 258 ? -59.222 24.664  -8.330  1.00 22.34 ? 252 TYR B CB    1 
ATOM   4215 C  CG    . TYR B 1 258 ? -59.209 23.809  -9.564  1.00 24.07 ? 252 TYR B CG    1 
ATOM   4216 C  CD1   . TYR B 1 258 ? -59.729 24.292  -10.762 1.00 27.51 ? 252 TYR B CD1   1 
ATOM   4217 C  CD2   . TYR B 1 258 ? -58.704 22.517  -9.538  1.00 24.27 ? 252 TYR B CD2   1 
ATOM   4218 C  CE1   . TYR B 1 258 ? -59.722 23.528  -11.910 1.00 25.19 ? 252 TYR B CE1   1 
ATOM   4219 C  CE2   . TYR B 1 258 ? -58.716 21.729  -10.679 1.00 27.79 ? 252 TYR B CE2   1 
ATOM   4220 C  CZ    . TYR B 1 258 ? -59.220 22.243  -11.867 1.00 28.57 ? 252 TYR B CZ    1 
ATOM   4221 O  OH    . TYR B 1 258 ? -59.235 21.497  -13.009 1.00 34.81 ? 252 TYR B OH    1 
ATOM   4222 N  N     . MET B 1 259 ? -57.229 26.735  -6.178  1.00 23.92 ? 253 MET B N     1 
ATOM   4223 C  CA    . MET B 1 259 ? -57.210 27.558  -4.939  1.00 23.45 ? 253 MET B CA    1 
ATOM   4224 C  C     . MET B 1 259 ? -58.320 27.081  -3.996  1.00 22.41 ? 253 MET B C     1 
ATOM   4225 O  O     . MET B 1 259 ? -59.001 27.885  -3.360  1.00 22.23 ? 253 MET B O     1 
ATOM   4226 C  CB    . MET B 1 259 ? -57.311 29.046  -5.273  1.00 26.27 ? 253 MET B CB    1 
ATOM   4227 C  CG    . MET B 1 259 ? -56.192 29.518  -6.183  1.00 29.25 ? 253 MET B CG    1 
ATOM   4228 S  SD    . MET B 1 259 ? -55.990 31.309  -6.294  1.00 27.48 ? 253 MET B SD    1 
ATOM   4229 C  CE    . MET B 1 259 ? -54.646 31.622  -5.158  1.00 31.04 ? 253 MET B CE    1 
ATOM   4230 N  N     . ARG B 1 260 ? -58.452 25.767  -3.883  1.00 21.34 ? 254 ARG B N     1 
ATOM   4231 C  CA    . ARG B 1 260 ? -59.244 25.076  -2.852  1.00 20.31 ? 254 ARG B CA    1 
ATOM   4232 C  C     . ARG B 1 260 ? -58.279 24.570  -1.747  1.00 22.72 ? 254 ARG B C     1 
ATOM   4233 O  O     . ARG B 1 260 ? -57.207 24.062  -2.077  1.00 19.80 ? 254 ARG B O     1 
ATOM   4234 C  CB    . ARG B 1 260 ? -59.979 23.906  -3.486  1.00 22.85 ? 254 ARG B CB    1 
ATOM   4235 C  CG    . ARG B 1 260 ? -60.765 24.271  -4.740  1.00 23.63 ? 254 ARG B CG    1 
ATOM   4236 C  CD    . ARG B 1 260 ? -61.466 23.073  -5.343  1.00 24.39 ? 254 ARG B CD    1 
ATOM   4237 N  NE    . ARG B 1 260 ? -60.529 22.106  -5.896  1.00 25.11 ? 254 ARG B NE    1 
ATOM   4238 C  CZ    . ARG B 1 260 ? -60.868 20.970  -6.453  1.00 29.31 ? 254 ARG B CZ    1 
ATOM   4239 N  NH1   . ARG B 1 260 ? -62.149 20.652  -6.596  1.00 30.24 ? 254 ARG B NH1   1 
ATOM   4240 N  NH2   . ARG B 1 260 ? -59.923 20.153  -6.883  1.00 31.00 ? 254 ARG B NH2   1 
ATOM   4241 N  N     . PHE B 1 261 ? -58.677 24.681  -0.480  1.00 22.18 ? 255 PHE B N     1 
ATOM   4242 C  CA    . PHE B 1 261 ? -57.968 24.096  0.679   1.00 22.20 ? 255 PHE B CA    1 
ATOM   4243 C  C     . PHE B 1 261 ? -58.190 22.598  0.649   1.00 21.70 ? 255 PHE B C     1 
ATOM   4244 O  O     . PHE B 1 261 ? -59.323 22.116  0.407   1.00 21.47 ? 255 PHE B O     1 
ATOM   4245 C  CB    . PHE B 1 261 ? -58.430 24.702  1.995   1.00 22.84 ? 255 PHE B CB    1 
ATOM   4246 C  CG    . PHE B 1 261 ? -57.901 26.087  2.195   1.00 22.69 ? 255 PHE B CG    1 
ATOM   4247 C  CD1   . PHE B 1 261 ? -56.555 26.297  2.432   1.00 23.75 ? 255 PHE B CD1   1 
ATOM   4248 C  CD2   . PHE B 1 261 ? -58.753 27.170  2.220   1.00 24.09 ? 255 PHE B CD2   1 
ATOM   4249 C  CE1   . PHE B 1 261 ? -56.061 27.575  2.611   1.00 25.64 ? 255 PHE B CE1   1 
ATOM   4250 C  CE2   . PHE B 1 261 ? -58.255 28.450  2.383   1.00 24.81 ? 255 PHE B CE2   1 
ATOM   4251 C  CZ    . PHE B 1 261 ? -56.915 28.652  2.595   1.00 24.74 ? 255 PHE B CZ    1 
ATOM   4252 N  N     . LEU B 1 262 ? -57.118 21.854  0.879   1.00 22.77 ? 256 LEU B N     1 
ATOM   4253 C  CA    . LEU B 1 262 ? -57.179 20.385  0.931   1.00 23.54 ? 256 LEU B CA    1 
ATOM   4254 C  C     . LEU B 1 262 ? -57.248 19.963  2.404   1.00 24.27 ? 256 LEU B C     1 
ATOM   4255 O  O     . LEU B 1 262 ? -56.400 20.387  3.189   1.00 26.01 ? 256 LEU B O     1 
ATOM   4256 C  CB    . LEU B 1 262 ? -55.966 19.825  0.191   1.00 23.29 ? 256 LEU B CB    1 
ATOM   4257 C  CG    . LEU B 1 262 ? -55.840 20.264  -1.271  1.00 23.88 ? 256 LEU B CG    1 
ATOM   4258 C  CD1   . LEU B 1 262 ? -54.717 19.506  -1.973  1.00 24.49 ? 256 LEU B CD1   1 
ATOM   4259 C  CD2   . LEU B 1 262 ? -57.157 20.039  -2.016  1.00 23.83 ? 256 LEU B CD2   1 
ATOM   4260 N  N     . ASN B 1 263 ? -58.277 19.201  2.748   1.00 24.84 ? 257 ASN B N     1 
ATOM   4261 C  CA    . ASN B 1 263 ? -58.493 18.655  4.109   1.00 27.44 ? 257 ASN B CA    1 
ATOM   4262 C  C     . ASN B 1 263 ? -57.816 17.281  4.203   1.00 28.07 ? 257 ASN B C     1 
ATOM   4263 O  O     . ASN B 1 263 ? -58.165 16.400  3.413   1.00 27.63 ? 257 ASN B O     1 
ATOM   4264 C  CB    . ASN B 1 263 ? -59.983 18.569  4.419   1.00 28.44 ? 257 ASN B CB    1 
ATOM   4265 C  CG    . ASN B 1 263 ? -60.270 18.288  5.867   1.00 29.22 ? 257 ASN B CG    1 
ATOM   4266 O  OD1   . ASN B 1 263 ? -59.372 18.357  6.697   1.00 28.93 ? 257 ASN B OD1   1 
ATOM   4267 N  ND2   . ASN B 1 263 ? -61.520 17.970  6.169   1.00 34.17 ? 257 ASN B ND2   1 
ATOM   4268 N  N     . CYS B 1 264 ? -56.895 17.104  5.142   1.00 28.83 ? 258 CYS B N     1 
ATOM   4269 C  CA    . CYS B 1 264 ? -56.133 15.843  5.306   1.00 29.62 ? 258 CYS B CA    1 
ATOM   4270 C  C     . CYS B 1 264 ? -56.598 15.059  6.542   1.00 31.81 ? 258 CYS B C     1 
ATOM   4271 O  O     . CYS B 1 264 ? -55.906 14.093  6.856   1.00 33.04 ? 258 CYS B O     1 
ATOM   4272 C  CB    . CYS B 1 264 ? -54.635 16.137  5.336   1.00 31.19 ? 258 CYS B CB    1 
ATOM   4273 S  SG    . CYS B 1 264 ? -54.101 16.879  3.772   1.00 32.05 ? 258 CYS B SG    1 
ATOM   4274 N  N     . THR B 1 265 ? -57.744 15.369  7.183   1.00 33.46 ? 259 THR B N     1 
ATOM   4275 C  CA    . THR B 1 265 ? -58.295 14.490  8.264   1.00 38.68 ? 259 THR B CA    1 
ATOM   4276 C  C     . THR B 1 265 ? -58.622 13.126  7.653   1.00 43.33 ? 259 THR B C     1 
ATOM   4277 O  O     . THR B 1 265 ? -59.056 13.089  6.519   1.00 47.56 ? 259 THR B O     1 
ATOM   4278 C  CB    . THR B 1 265 ? -59.533 15.015  9.005   1.00 40.79 ? 259 THR B CB    1 
ATOM   4279 O  OG1   . THR B 1 265 ? -60.542 15.485  8.115   1.00 44.95 ? 259 THR B OG1   1 
ATOM   4280 C  CG2   . THR B 1 265 ? -59.188 16.108  9.980   1.00 43.58 ? 259 THR B CG2   1 
ATOM   4281 N  N     . GLY B 1 266 ? -58.342 12.036  8.360   1.00 47.43 ? 260 GLY B N     1 
ATOM   4282 C  CA    . GLY B 1 266 ? -58.477 10.672  7.802   1.00 52.72 ? 260 GLY B CA    1 
ATOM   4283 C  C     . GLY B 1 266 ? -57.785 10.486  6.446   1.00 50.12 ? 260 GLY B C     1 
ATOM   4284 O  O     . GLY B 1 266 ? -58.348 9.760   5.611   1.00 46.41 ? 260 GLY B O     1 
ATOM   4285 N  N     . GLY B 1 267 ? -56.650 11.161  6.215   1.00 41.43 ? 261 GLY B N     1 
ATOM   4286 C  CA    . GLY B 1 267 ? -55.562 10.723  5.319   1.00 40.61 ? 261 GLY B CA    1 
ATOM   4287 C  C     . GLY B 1 267 ? -55.802 10.959  3.837   1.00 38.04 ? 261 GLY B C     1 
ATOM   4288 O  O     . GLY B 1 267 ? -55.068 10.351  3.033   1.00 32.78 ? 261 GLY B O     1 
ATOM   4289 N  N     . ARG B 1 268 ? -56.758 11.804  3.450   1.00 37.39 ? 262 ARG B N     1 
ATOM   4290 C  CA    . ARG B 1 268 ? -57.009 12.112  2.015   1.00 36.63 ? 262 ARG B CA    1 
ATOM   4291 C  C     . ARG B 1 268 ? -56.586 13.563  1.780   1.00 31.66 ? 262 ARG B C     1 
ATOM   4292 O  O     . ARG B 1 268 ? -56.020 14.163  2.698   1.00 31.72 ? 262 ARG B O     1 
ATOM   4293 C  CB    . ARG B 1 268 ? -58.471 11.877  1.621   1.00 43.48 ? 262 ARG B CB    1 
ATOM   4294 C  CG    . ARG B 1 268 ? -59.204 10.857  2.487   1.00 49.57 ? 262 ARG B CG    1 
ATOM   4295 C  CD    . ARG B 1 268 ? -60.599 10.570  1.940   1.00 54.38 ? 262 ARG B CD    1 
ATOM   4296 N  NE    . ARG B 1 268 ? -60.551 10.456  0.485   1.00 55.33 ? 262 ARG B NE    1 
ATOM   4297 C  CZ    . ARG B 1 268 ? -60.138 9.383   -0.197  1.00 58.22 ? 262 ARG B CZ    1 
ATOM   4298 N  NH1   . ARG B 1 268 ? -59.761 8.270   0.423   1.00 58.88 ? 262 ARG B NH1   1 
ATOM   4299 N  NH2   . ARG B 1 268 ? -60.128 9.427   -1.519  1.00 62.02 ? 262 ARG B NH2   1 
ATOM   4300 N  N     . LYS B 1 269 ? -56.801 14.067  0.577   1.00 28.48 ? 263 LYS B N     1 
ATOM   4301 C  CA    . LYS B 1 269 ? -56.604 15.495  0.214   1.00 28.03 ? 263 LYS B CA    1 
ATOM   4302 C  C     . LYS B 1 269 ? -57.927 16.014  -0.360  1.00 28.87 ? 263 LYS B C     1 
ATOM   4303 O  O     . LYS B 1 269 ? -58.014 16.219  -1.583  1.00 30.72 ? 263 LYS B O     1 
ATOM   4304 C  CB    . LYS B 1 269 ? -55.428 15.627  -0.758  1.00 27.91 ? 263 LYS B CB    1 
ATOM   4305 C  CG    . LYS B 1 269 ? -54.110 15.988  -0.073  1.00 25.07 ? 263 LYS B CG    1 
ATOM   4306 C  CD    . LYS B 1 269 ? -52.972 16.197  -1.042  1.00 25.43 ? 263 LYS B CD    1 
ATOM   4307 C  CE    . LYS B 1 269 ? -51.782 16.841  -0.365  1.00 23.92 ? 263 LYS B CE    1 
ATOM   4308 N  NZ    . LYS B 1 269 ? -50.542 16.645  -1.138  1.00 23.32 ? 263 LYS B NZ    1 
ATOM   4309 N  N     . ASP B 1 270 ? -58.936 16.159  0.491   1.00 27.87 ? 264 ASP B N     1 
ATOM   4310 C  CA    . ASP B 1 270 ? -60.336 16.441  0.057   1.00 30.29 ? 264 ASP B CA    1 
ATOM   4311 C  C     . ASP B 1 270 ? -60.520 17.953  -0.069  1.00 25.84 ? 264 ASP B C     1 
ATOM   4312 O  O     . ASP B 1 270 ? -60.327 18.700  0.902   1.00 25.44 ? 264 ASP B O     1 
ATOM   4313 C  CB    . ASP B 1 270 ? -61.365 15.853  1.026   1.00 36.50 ? 264 ASP B CB    1 
ATOM   4314 C  CG    . ASP B 1 270 ? -61.495 14.346  0.937   1.00 40.92 ? 264 ASP B CG    1 
ATOM   4315 O  OD1   . ASP B 1 270 ? -61.580 13.829  -0.199  1.00 51.46 ? 264 ASP B OD1   1 
ATOM   4316 O  OD2   . ASP B 1 270 ? -61.553 13.706  2.006   1.00 50.69 ? 264 ASP B OD2   1 
ATOM   4317 N  N     . PRO B 1 271 ? -60.886 18.445  -1.272  1.00 24.60 ? 265 PRO B N     1 
ATOM   4318 C  CA    . PRO B 1 271 ? -60.910 19.879  -1.518  1.00 24.00 ? 265 PRO B CA    1 
ATOM   4319 C  C     . PRO B 1 271 ? -62.165 20.579  -0.987  1.00 26.30 ? 265 PRO B C     1 
ATOM   4320 O  O     . PRO B 1 271 ? -63.250 20.057  -1.110  1.00 26.86 ? 265 PRO B O     1 
ATOM   4321 C  CB    . PRO B 1 271 ? -60.820 19.982  -3.041  1.00 26.25 ? 265 PRO B CB    1 
ATOM   4322 C  CG    . PRO B 1 271 ? -61.448 18.687  -3.554  1.00 29.03 ? 265 PRO B CG    1 
ATOM   4323 C  CD    . PRO B 1 271 ? -61.143 17.661  -2.486  1.00 28.10 ? 265 PRO B CD    1 
ATOM   4324 N  N     . SER B 1 272 ? -61.965 21.777  -0.469  1.00 24.43 ? 266 SER B N     1 
ATOM   4325 C  CA    . SER B 1 272 ? -63.031 22.752  -0.145  1.00 24.28 ? 266 SER B CA    1 
ATOM   4326 C  C     . SER B 1 272 ? -63.570 23.306  -1.456  1.00 25.02 ? 266 SER B C     1 
ATOM   4327 O  O     . SER B 1 272 ? -63.045 22.944  -2.519  1.00 23.53 ? 266 SER B O     1 
ATOM   4328 C  CB    . SER B 1 272 ? -62.485 23.842  0.736   1.00 25.89 ? 266 SER B CB    1 
ATOM   4329 O  OG    . SER B 1 272 ? -61.629 24.714  0.001   1.00 23.94 ? 266 SER B OG    1 
ATOM   4330 N  N     . LYS B 1 273 ? -64.532 24.215  -1.402  1.00 27.10 ? 267 LYS B N     1 
ATOM   4331 C  CA    . LYS B 1 273 ? -64.799 25.083  -2.569  1.00 27.07 ? 267 LYS B CA    1 
ATOM   4332 C  C     . LYS B 1 273 ? -63.647 26.079  -2.687  1.00 24.74 ? 267 LYS B C     1 
ATOM   4333 O  O     . LYS B 1 273 ? -62.954 26.295  -1.690  1.00 24.76 ? 267 LYS B O     1 
ATOM   4334 C  CB    . LYS B 1 273 ? -66.164 25.763  -2.464  1.00 30.91 ? 267 LYS B CB    1 
ATOM   4335 C  CG    . LYS B 1 273 ? -67.286 24.762  -2.240  1.00 34.66 ? 267 LYS B CG    1 
ATOM   4336 C  CD    . LYS B 1 273 ? -68.426 24.865  -3.186  1.00 43.55 ? 267 LYS B CD    1 
ATOM   4337 C  CE    . LYS B 1 273 ? -69.604 24.021  -2.730  1.00 46.70 ? 267 LYS B CE    1 
ATOM   4338 N  NZ    . LYS B 1 273 ? -70.061 23.133  -3.818  1.00 48.34 ? 267 LYS B NZ    1 
ATOM   4339 N  N     . SER B 1 274 ? -63.435 26.624  -3.881  1.00 22.84 ? 268 SER B N     1 
ATOM   4340 C  CA    . SER B 1 274 ? -62.322 27.553  -4.174  1.00 23.14 ? 268 SER B CA    1 
ATOM   4341 C  C     . SER B 1 274 ? -62.503 28.805  -3.324  1.00 25.54 ? 268 SER B C     1 
ATOM   4342 O  O     . SER B 1 274 ? -63.663 29.293  -3.191  1.00 27.36 ? 268 SER B O     1 
ATOM   4343 C  CB    . SER B 1 274 ? -62.240 27.868  -5.626  1.00 21.59 ? 268 SER B CB    1 
ATOM   4344 O  OG    . SER B 1 274 ? -61.258 28.858  -5.867  1.00 22.10 ? 268 SER B OG    1 
ATOM   4345 N  N     . ILE B 1 275 ? -61.404 29.349  -2.811  1.00 23.33 ? 269 ILE B N     1 
ATOM   4346 C  CA    . ILE B 1 275 ? -61.441 30.707  -2.214  1.00 24.12 ? 269 ILE B CA    1 
ATOM   4347 C  C     . ILE B 1 275 ? -61.933 31.718  -3.252  1.00 24.19 ? 269 ILE B C     1 
ATOM   4348 O  O     . ILE B 1 275 ? -62.396 32.762  -2.839  1.00 23.71 ? 269 ILE B O     1 
ATOM   4349 C  CB    . ILE B 1 275 ? -60.080 31.107  -1.620  1.00 23.22 ? 269 ILE B CB    1 
ATOM   4350 C  CG1   . ILE B 1 275 ? -59.044 31.336  -2.722  1.00 23.76 ? 269 ILE B CG1   1 
ATOM   4351 C  CG2   . ILE B 1 275 ? -59.645 30.080  -0.576  1.00 24.39 ? 269 ILE B CG2   1 
ATOM   4352 C  CD1   . ILE B 1 275 ? -57.702 31.837  -2.233  1.00 26.16 ? 269 ILE B CD1   1 
ATOM   4353 N  N     . LEU B 1 276 ? -61.754 31.474  -4.551  1.00 23.42 ? 270 LEU B N     1 
ATOM   4354 C  CA    . LEU B 1 276 ? -62.194 32.418  -5.606  1.00 24.99 ? 270 LEU B CA    1 
ATOM   4355 C  C     . LEU B 1 276 ? -63.730 32.396  -5.745  1.00 27.23 ? 270 LEU B C     1 
ATOM   4356 O  O     . LEU B 1 276 ? -64.224 33.333  -6.356  1.00 30.20 ? 270 LEU B O     1 
ATOM   4357 C  CB    . LEU B 1 276 ? -61.531 32.028  -6.929  1.00 27.78 ? 270 LEU B CB    1 
ATOM   4358 C  CG    . LEU B 1 276 ? -60.005 32.134  -6.926  1.00 27.06 ? 270 LEU B CG    1 
ATOM   4359 C  CD1   . LEU B 1 276 ? -59.411 31.533  -8.192  1.00 29.47 ? 270 LEU B CD1   1 
ATOM   4360 C  CD2   . LEU B 1 276 ? -59.573 33.554  -6.742  1.00 30.27 ? 270 LEU B CD2   1 
ATOM   4361 N  N     . GLU B 1 277 ? -64.423 31.382  -5.217  1.00 26.97 ? 271 GLU B N     1 
ATOM   4362 C  CA    . GLU B 1 277 ? -65.904 31.238  -5.261  1.00 28.53 ? 271 GLU B CA    1 
ATOM   4363 C  C     . GLU B 1 277 ? -66.542 31.697  -3.949  1.00 27.20 ? 271 GLU B C     1 
ATOM   4364 O  O     . GLU B 1 277 ? -67.617 32.324  -4.022  1.00 25.18 ? 271 GLU B O     1 
ATOM   4365 C  CB    . GLU B 1 277 ? -66.342 29.794  -5.499  1.00 32.59 ? 271 GLU B CB    1 
ATOM   4366 C  CG    . GLU B 1 277 ? -65.680 29.142  -6.690  1.00 43.80 ? 271 GLU B CG    1 
ATOM   4367 C  CD    . GLU B 1 277 ? -66.309 29.395  -8.043  1.00 54.50 ? 271 GLU B CD    1 
ATOM   4368 O  OE1   . GLU B 1 277 ? -66.577 30.577  -8.364  1.00 55.13 ? 271 GLU B OE1   1 
ATOM   4369 O  OE2   . GLU B 1 277 ? -66.508 28.393  -8.782  1.00 71.92 ? 271 GLU B OE2   1 
ATOM   4370 N  N     . VAL B 1 278 ? -65.990 31.327  -2.788  1.00 24.73 ? 272 VAL B N     1 
ATOM   4371 C  CA    . VAL B 1 278 ? -66.708 31.487  -1.489  1.00 25.95 ? 272 VAL B CA    1 
ATOM   4372 C  C     . VAL B 1 278 ? -65.909 32.349  -0.506  1.00 24.08 ? 272 VAL B C     1 
ATOM   4373 O  O     . VAL B 1 278 ? -66.423 32.628  0.574   1.00 27.87 ? 272 VAL B O     1 
ATOM   4374 C  CB    . VAL B 1 278 ? -67.072 30.127  -0.878  1.00 25.82 ? 272 VAL B CB    1 
ATOM   4375 C  CG1   . VAL B 1 278 ? -67.940 29.284  -1.804  1.00 27.52 ? 272 VAL B CG1   1 
ATOM   4376 C  CG2   . VAL B 1 278 ? -65.832 29.365  -0.468  1.00 25.33 ? 272 VAL B CG2   1 
ATOM   4377 N  N     . GLY B 1 279 ? -64.706 32.756  -0.866  1.00 23.37 ? 273 GLY B N     1 
ATOM   4378 C  CA    . GLY B 1 279 ? -63.829 33.540  0.013   1.00 23.66 ? 273 GLY B CA    1 
ATOM   4379 C  C     . GLY B 1 279 ? -63.012 32.630  0.924   1.00 24.32 ? 273 GLY B C     1 
ATOM   4380 O  O     . GLY B 1 279 ? -63.330 31.429  1.047   1.00 23.19 ? 273 GLY B O     1 
ATOM   4381 N  N     . VAL B 1 280 ? -61.998 33.192  1.563   1.00 25.83 ? 274 VAL B N     1 
ATOM   4382 C  CA    . VAL B 1 280 ? -61.026 32.430  2.406   1.00 24.25 ? 274 VAL B CA    1 
ATOM   4383 C  C     . VAL B 1 280 ? -61.732 31.830  3.628   1.00 25.80 ? 274 VAL B C     1 
ATOM   4384 O  O     . VAL B 1 280 ? -61.603 30.610  3.882   1.00 25.62 ? 274 VAL B O     1 
ATOM   4385 C  CB    . VAL B 1 280 ? -59.859 33.331  2.792   1.00 25.46 ? 274 VAL B CB    1 
ATOM   4386 C  CG1   . VAL B 1 280 ? -58.963 32.646  3.829   1.00 28.04 ? 274 VAL B CG1   1 
ATOM   4387 C  CG2   . VAL B 1 280 ? -59.063 33.760  1.579   1.00 29.13 ? 274 VAL B CG2   1 
ATOM   4388 N  N     . GLN B 1 281 ? -62.529 32.620  4.349   1.00 29.86 ? 275 GLN B N     1 
ATOM   4389 C  CA    . GLN B 1 281 ? -63.122 32.167  5.646   1.00 32.82 ? 275 GLN B CA    1 
ATOM   4390 C  C     . GLN B 1 281 ? -64.024 30.954  5.415   1.00 29.39 ? 275 GLN B C     1 
ATOM   4391 O  O     . GLN B 1 281 ? -63.884 29.940  6.119   1.00 28.89 ? 275 GLN B O     1 
ATOM   4392 C  CB    . GLN B 1 281 ? -63.899 33.298  6.336   1.00 38.65 ? 275 GLN B CB    1 
ATOM   4393 C  CG    . GLN B 1 281 ? -64.808 32.809  7.457   1.00 43.29 ? 275 GLN B CG    1 
ATOM   4394 C  CD    . GLN B 1 281 ? -65.857 33.825  7.859   1.00 51.22 ? 275 GLN B CD    1 
ATOM   4395 O  OE1   . GLN B 1 281 ? -65.543 34.925  8.304   1.00 45.20 ? 275 GLN B OE1   1 
ATOM   4396 N  NE2   . GLN B 1 281 ? -67.118 33.464  7.668   1.00 48.83 ? 275 GLN B NE2   1 
ATOM   4397 N  N     . GLN B 1 282 ? -64.898 31.001  4.408   1.00 30.02 ? 276 GLN B N     1 
ATOM   4398 C  CA    . GLN B 1 282 ? -65.812 29.876  4.143   1.00 27.07 ? 276 GLN B CA    1 
ATOM   4399 C  C     . GLN B 1 282 ? -65.027 28.639  3.675   1.00 27.06 ? 276 GLN B C     1 
ATOM   4400 O  O     . GLN B 1 282 ? -65.369 27.505  4.103   1.00 27.07 ? 276 GLN B O     1 
ATOM   4401 C  CB    . GLN B 1 282 ? -66.856 30.269  3.104   1.00 30.58 ? 276 GLN B CB    1 
ATOM   4402 C  CG    . GLN B 1 282 ? -67.817 29.138  2.768   1.00 32.37 ? 276 GLN B CG    1 
ATOM   4403 C  CD    . GLN B 1 282 ? -68.760 28.825  3.904   1.00 32.93 ? 276 GLN B CD    1 
ATOM   4404 O  OE1   . GLN B 1 282 ? -68.963 29.634  4.801   1.00 34.42 ? 276 GLN B OE1   1 
ATOM   4405 N  NE2   . GLN B 1 282 ? -69.358 27.646  3.852   1.00 33.98 ? 276 GLN B NE2   1 
ATOM   4406 N  N     . ALA B 1 283 ? -64.066 28.809  2.767   1.00 25.02 ? 277 ALA B N     1 
ATOM   4407 C  CA    . ALA B 1 283 ? -63.260 27.658  2.282   1.00 25.76 ? 277 ALA B CA    1 
ATOM   4408 C  C     . ALA B 1 283 ? -62.513 27.014  3.465   1.00 25.35 ? 277 ALA B C     1 
ATOM   4409 O  O     . ALA B 1 283 ? -62.524 25.785  3.582   1.00 28.02 ? 277 ALA B O     1 
ATOM   4410 C  CB    . ALA B 1 283 ? -62.309 28.087  1.204   1.00 24.25 ? 277 ALA B CB    1 
ATOM   4411 N  N     . LEU B 1 284 ? -61.938 27.817  4.345   1.00 25.83 ? 278 LEU B N     1 
ATOM   4412 C  CA    . LEU B 1 284 ? -61.118 27.319  5.484   1.00 29.22 ? 278 LEU B CA    1 
ATOM   4413 C  C     . LEU B 1 284 ? -61.988 26.667  6.568   1.00 32.93 ? 278 LEU B C     1 
ATOM   4414 O  O     . LEU B 1 284 ? -61.515 25.728  7.249   1.00 31.56 ? 278 LEU B O     1 
ATOM   4415 C  CB    . LEU B 1 284 ? -60.313 28.498  6.024   1.00 31.79 ? 278 LEU B CB    1 
ATOM   4416 C  CG    . LEU B 1 284 ? -59.133 28.122  6.907   1.00 37.85 ? 278 LEU B CG    1 
ATOM   4417 C  CD1   . LEU B 1 284 ? -58.186 27.178  6.176   1.00 38.66 ? 278 LEU B CD1   1 
ATOM   4418 C  CD2   . LEU B 1 284 ? -58.415 29.379  7.356   1.00 40.06 ? 278 LEU B CD2   1 
ATOM   4419 N  N     . GLN B 1 285 ? -63.251 27.065  6.715   1.00 35.18 ? 279 GLN B N     1 
ATOM   4420 C  CA    . GLN B 1 285 ? -64.085 26.549  7.831   1.00 39.68 ? 279 GLN B CA    1 
ATOM   4421 C  C     . GLN B 1 285 ? -64.309 25.053  7.590   1.00 40.77 ? 279 GLN B C     1 
ATOM   4422 O  O     . GLN B 1 285 ? -64.516 24.320  8.545   1.00 43.54 ? 279 GLN B O     1 
ATOM   4423 C  CB    . GLN B 1 285 ? -65.360 27.390  7.974   1.00 42.59 ? 279 GLN B CB    1 
ATOM   4424 C  CG    . GLN B 1 285 ? -66.642 26.657  7.634   1.00 48.88 ? 279 GLN B CG    1 
ATOM   4425 C  CD    . GLN B 1 285 ? -67.831 27.520  7.978   1.00 62.16 ? 279 GLN B CD    1 
ATOM   4426 O  OE1   . GLN B 1 285 ? -67.726 28.496  8.728   1.00 63.58 ? 279 GLN B OE1   1 
ATOM   4427 N  NE2   . GLN B 1 285 ? -68.978 27.171  7.414   1.00 60.73 ? 279 GLN B NE2   1 
ATOM   4428 N  N     . ALA B 1 286 ? -64.166 24.646  6.335   1.00 42.07 ? 280 ALA B N     1 
ATOM   4429 C  CA    . ALA B 1 286 ? -64.393 23.296  5.779   1.00 45.81 ? 280 ALA B CA    1 
ATOM   4430 C  C     . ALA B 1 286 ? -63.279 22.315  6.202   1.00 43.51 ? 280 ALA B C     1 
ATOM   4431 O  O     . ALA B 1 286 ? -63.492 21.110  6.059   1.00 41.63 ? 280 ALA B O     1 
ATOM   4432 C  CB    . ALA B 1 286 ? -64.462 23.452  4.266   1.00 39.73 ? 280 ALA B CB    1 
ATOM   4433 N  N     . VAL B 1 287 ? -62.112 22.807  6.633   1.00 36.23 ? 281 VAL B N     1 
ATOM   4434 C  CA    . VAL B 1 287 ? -60.871 21.979  6.645   1.00 34.32 ? 281 VAL B CA    1 
ATOM   4435 C  C     . VAL B 1 287 ? -60.314 21.976  8.053   1.00 30.74 ? 281 VAL B C     1 
ATOM   4436 O  O     . VAL B 1 287 ? -60.413 22.992  8.767   1.00 28.42 ? 281 VAL B O     1 
ATOM   4437 C  CB    . VAL B 1 287 ? -59.804 22.420  5.611   1.00 39.60 ? 281 VAL B CB    1 
ATOM   4438 C  CG1   . VAL B 1 287 ? -60.379 22.543  4.208   1.00 39.55 ? 281 VAL B CG1   1 
ATOM   4439 C  CG2   . VAL B 1 287 ? -59.091 23.698  5.989   1.00 42.02 ? 281 VAL B CG2   1 
ATOM   4440 N  N     . PHE B 1 288 ? -59.683 20.870  8.399   1.00 25.84 ? 282 PHE B N     1 
ATOM   4441 C  CA    . PHE B 1 288 ? -58.935 20.749  9.661   1.00 26.06 ? 282 PHE B CA    1 
ATOM   4442 C  C     . PHE B 1 288 ? -57.530 21.307  9.456   1.00 22.75 ? 282 PHE B C     1 
ATOM   4443 O  O     . PHE B 1 288 ? -56.831 20.876  8.538   1.00 25.60 ? 282 PHE B O     1 
ATOM   4444 C  CB    . PHE B 1 288 ? -58.863 19.288  10.110  1.00 27.44 ? 282 PHE B CB    1 
ATOM   4445 C  CG    . PHE B 1 288 ? -58.188 19.126  11.447  1.00 28.85 ? 282 PHE B CG    1 
ATOM   4446 C  CD1   . PHE B 1 288 ? -58.608 19.870  12.538  1.00 33.25 ? 282 PHE B CD1   1 
ATOM   4447 C  CD2   . PHE B 1 288 ? -57.133 18.240  11.603  1.00 32.22 ? 282 PHE B CD2   1 
ATOM   4448 C  CE1   . PHE B 1 288 ? -58.007 19.719  13.779  1.00 35.13 ? 282 PHE B CE1   1 
ATOM   4449 C  CE2   . PHE B 1 288 ? -56.512 18.108  12.837  1.00 33.86 ? 282 PHE B CE2   1 
ATOM   4450 C  CZ    . PHE B 1 288 ? -56.963 18.834  13.921  1.00 35.03 ? 282 PHE B CZ    1 
ATOM   4451 N  N     . TRP B 1 289 ? -57.120 22.242  10.285  1.00 23.28 ? 283 TRP B N     1 
ATOM   4452 C  CA    . TRP B 1 289 ? -55.700 22.672  10.371  1.00 22.72 ? 283 TRP B CA    1 
ATOM   4453 C  C     . TRP B 1 289 ? -55.271 22.574  11.830  1.00 24.32 ? 283 TRP B C     1 
ATOM   4454 O  O     . TRP B 1 289 ? -55.784 23.341  12.691  1.00 22.96 ? 283 TRP B O     1 
ATOM   4455 C  CB    . TRP B 1 289 ? -55.538 24.074  9.822   1.00 23.22 ? 283 TRP B CB    1 
ATOM   4456 C  CG    . TRP B 1 289 ? -54.149 24.611  9.958   1.00 23.09 ? 283 TRP B CG    1 
ATOM   4457 C  CD1   . TRP B 1 289 ? -52.975 23.954  9.718   1.00 23.66 ? 283 TRP B CD1   1 
ATOM   4458 C  CD2   . TRP B 1 289 ? -53.798 25.948  10.333  1.00 24.31 ? 283 TRP B CD2   1 
ATOM   4459 N  NE1   . TRP B 1 289 ? -51.921 24.801  9.923   1.00 23.94 ? 283 TRP B NE1   1 
ATOM   4460 C  CE2   . TRP B 1 289 ? -52.390 26.031  10.303  1.00 23.75 ? 283 TRP B CE2   1 
ATOM   4461 C  CE3   . TRP B 1 289 ? -54.537 27.080  10.703  1.00 25.37 ? 283 TRP B CE3   1 
ATOM   4462 C  CZ2   . TRP B 1 289 ? -51.708 27.212  10.605  1.00 26.90 ? 283 TRP B CZ2   1 
ATOM   4463 C  CZ3   . TRP B 1 289 ? -53.861 28.244  10.998  1.00 25.60 ? 283 TRP B CZ3   1 
ATOM   4464 C  CH2   . TRP B 1 289 ? -52.467 28.311  10.959  1.00 27.28 ? 283 TRP B CH2   1 
ATOM   4465 N  N     . ASP B 1 290 ? -54.375 21.648  12.116  1.00 22.21 ? 284 ASP B N     1 
ATOM   4466 C  CA    . ASP B 1 290 ? -53.901 21.407  13.495  1.00 22.93 ? 284 ASP B CA    1 
ATOM   4467 C  C     . ASP B 1 290 ? -52.850 22.464  13.834  1.00 22.64 ? 284 ASP B C     1 
ATOM   4468 O  O     . ASP B 1 290 ? -51.661 22.263  13.504  1.00 21.72 ? 284 ASP B O     1 
ATOM   4469 C  CB    . ASP B 1 290 ? -53.426 19.970  13.612  1.00 25.32 ? 284 ASP B CB    1 
ATOM   4470 C  CG    . ASP B 1 290 ? -53.030 19.555  15.017  1.00 25.81 ? 284 ASP B CG    1 
ATOM   4471 O  OD1   . ASP B 1 290 ? -52.831 20.464  15.864  1.00 24.17 ? 284 ASP B OD1   1 
ATOM   4472 O  OD2   . ASP B 1 290 ? -52.924 18.324  15.213  1.00 25.11 ? 284 ASP B OD2   1 
ATOM   4473 N  N     . GLU B 1 291 ? -53.278 23.565  14.472  1.00 22.35 ? 285 GLU B N     1 
ATOM   4474 C  CA    . GLU B 1 291 ? -52.368 24.695  14.744  1.00 23.78 ? 285 GLU B CA    1 
ATOM   4475 C  C     . GLU B 1 291 ? -51.372 24.314  15.828  1.00 20.19 ? 285 GLU B C     1 
ATOM   4476 O  O     . GLU B 1 291 ? -50.275 24.885  15.817  1.00 22.70 ? 285 GLU B O     1 
ATOM   4477 C  CB    . GLU B 1 291 ? -53.121 25.955  15.166  1.00 27.63 ? 285 GLU B CB    1 
ATOM   4478 C  CG    . GLU B 1 291 ? -54.031 26.479  14.097  1.00 28.01 ? 285 GLU B CG    1 
ATOM   4479 C  CD    . GLU B 1 291 ? -54.582 27.852  14.445  1.00 31.69 ? 285 GLU B CD    1 
ATOM   4480 O  OE1   . GLU B 1 291 ? -53.781 28.754  14.729  1.00 33.52 ? 285 GLU B OE1   1 
ATOM   4481 O  OE2   . GLU B 1 291 ? -55.810 27.999  14.427  1.00 36.37 ? 285 GLU B OE2   1 
ATOM   4482 N  N     . GLU B 1 292 ? -51.751 23.457  16.783  1.00 20.36 ? 286 GLU B N     1 
ATOM   4483 C  CA    . GLU B 1 292 ? -50.805 22.929  17.796  1.00 22.07 ? 286 GLU B CA    1 
ATOM   4484 C  C     . GLU B 1 292 ? -49.657 22.184  17.078  1.00 21.29 ? 286 GLU B C     1 
ATOM   4485 O  O     . GLU B 1 292 ? -48.482 22.437  17.406  1.00 18.87 ? 286 GLU B O     1 
ATOM   4486 C  CB    . GLU B 1 292 ? -51.559 22.029  18.786  1.00 25.15 ? 286 GLU B CB    1 
ATOM   4487 C  CG    . GLU B 1 292 ? -52.506 22.792  19.715  1.00 27.28 ? 286 GLU B CG    1 
ATOM   4488 C  CD    . GLU B 1 292 ? -53.132 21.908  20.779  1.00 30.43 ? 286 GLU B CD    1 
ATOM   4489 O  OE1   . GLU B 1 292 ? -53.145 20.649  20.595  1.00 29.85 ? 286 GLU B OE1   1 
ATOM   4490 O  OE2   . GLU B 1 292 ? -53.615 22.463  21.790  1.00 31.78 ? 286 GLU B OE2   1 
ATOM   4491 N  N     . ALA B 1 293 ? -49.954 21.284  16.151  1.00 19.79 ? 287 ALA B N     1 
ATOM   4492 C  CA    . ALA B 1 293 ? -48.928 20.575  15.355  1.00 18.98 ? 287 ALA B CA    1 
ATOM   4493 C  C     . ALA B 1 293 ? -48.097 21.574  14.546  1.00 21.10 ? 287 ALA B C     1 
ATOM   4494 O  O     . ALA B 1 293 ? -46.856 21.404  14.464  1.00 23.97 ? 287 ALA B O     1 
ATOM   4495 C  CB    . ALA B 1 293 ? -49.570 19.562  14.474  1.00 21.01 ? 287 ALA B CB    1 
ATOM   4496 N  N     . PHE B 1 294 ? -48.725 22.626  14.015  1.00 19.55 ? 288 PHE B N     1 
ATOM   4497 C  CA    . PHE B 1 294 ? -48.080 23.663  13.184  1.00 20.08 ? 288 PHE B CA    1 
ATOM   4498 C  C     . PHE B 1 294 ? -46.995 24.333  14.022  1.00 21.32 ? 288 PHE B C     1 
ATOM   4499 O  O     . PHE B 1 294 ? -45.847 24.471  13.586  1.00 20.13 ? 288 PHE B O     1 
ATOM   4500 C  CB    . PHE B 1 294 ? -49.102 24.704  12.708  1.00 21.09 ? 288 PHE B CB    1 
ATOM   4501 C  CG    . PHE B 1 294 ? -48.512 25.919  12.051  1.00 19.72 ? 288 PHE B CG    1 
ATOM   4502 C  CD1   . PHE B 1 294 ? -48.008 25.834  10.754  1.00 21.03 ? 288 PHE B CD1   1 
ATOM   4503 C  CD2   . PHE B 1 294 ? -48.550 27.160  12.668  1.00 21.46 ? 288 PHE B CD2   1 
ATOM   4504 C  CE1   . PHE B 1 294 ? -47.485 26.933  10.105  1.00 20.89 ? 288 PHE B CE1   1 
ATOM   4505 C  CE2   . PHE B 1 294 ? -48.009 28.263  12.033  1.00 22.03 ? 288 PHE B CE2   1 
ATOM   4506 C  CZ    . PHE B 1 294 ? -47.471 28.155  10.755  1.00 22.13 ? 288 PHE B CZ    1 
ATOM   4507 N  N     . VAL B 1 295 ? -47.342 24.737  15.244  1.00 19.29 ? 289 VAL B N     1 
ATOM   4508 C  CA    . VAL B 1 295 ? -46.338 25.395  16.132  1.00 19.71 ? 289 VAL B CA    1 
ATOM   4509 C  C     . VAL B 1 295 ? -45.258 24.374  16.512  1.00 18.99 ? 289 VAL B C     1 
ATOM   4510 O  O     . VAL B 1 295 ? -44.052 24.740  16.470  1.00 22.34 ? 289 VAL B O     1 
ATOM   4511 C  CB    . VAL B 1 295 ? -47.007 26.048  17.355  1.00 20.39 ? 289 VAL B CB    1 
ATOM   4512 C  CG1   . VAL B 1 295 ? -45.986 26.462  18.403  1.00 20.31 ? 289 VAL B CG1   1 
ATOM   4513 C  CG2   . VAL B 1 295 ? -47.887 27.233  16.929  1.00 21.09 ? 289 VAL B CG2   1 
ATOM   4514 N  N     . GLU B 1 296 ? -45.652 23.175  16.911  1.00 20.51 ? 290 GLU B N     1 
ATOM   4515 C  CA    . GLU B 1 296 ? -44.727 22.154  17.459  1.00 19.81 ? 290 GLU B CA    1 
ATOM   4516 C  C     . GLU B 1 296 ? -43.664 21.785  16.416  1.00 21.17 ? 290 GLU B C     1 
ATOM   4517 O  O     . GLU B 1 296 ? -42.538 21.513  16.824  1.00 21.20 ? 290 GLU B O     1 
ATOM   4518 C  CB    . GLU B 1 296 ? -45.469 20.905  17.902  1.00 21.30 ? 290 GLU B CB    1 
ATOM   4519 C  CG    . GLU B 1 296 ? -44.585 19.862  18.575  1.00 21.82 ? 290 GLU B CG    1 
ATOM   4520 C  CD    . GLU B 1 296 ? -45.360 19.027  19.575  1.00 24.00 ? 290 GLU B CD    1 
ATOM   4521 O  OE1   . GLU B 1 296 ? -46.171 19.653  20.331  1.00 23.06 ? 290 GLU B OE1   1 
ATOM   4522 O  OE2   . GLU B 1 296 ? -45.186 17.770  19.607  1.00 26.13 ? 290 GLU B OE2   1 
ATOM   4523 N  N     . ARG B 1 297 ? -44.010 21.712  15.138  1.00 21.76 ? 291 ARG B N     1 
ATOM   4524 C  CA    . ARG B 1 297 ? -43.031 21.325  14.075  1.00 22.52 ? 291 ARG B CA    1 
ATOM   4525 C  C     . ARG B 1 297 ? -42.124 22.508  13.722  1.00 22.81 ? 291 ARG B C     1 
ATOM   4526 O  O     . ARG B 1 297 ? -41.164 22.294  12.968  1.00 25.37 ? 291 ARG B O     1 
ATOM   4527 C  CB    . ARG B 1 297 ? -43.719 20.771  12.827  1.00 22.74 ? 291 ARG B CB    1 
ATOM   4528 C  CG    . ARG B 1 297 ? -44.500 21.809  12.036  1.00 21.42 ? 291 ARG B CG    1 
ATOM   4529 C  CD    . ARG B 1 297 ? -44.902 21.212  10.707  1.00 21.43 ? 291 ARG B CD    1 
ATOM   4530 N  NE    . ARG B 1 297 ? -45.880 21.992  9.940   1.00 22.10 ? 291 ARG B NE    1 
ATOM   4531 C  CZ    . ARG B 1 297 ? -45.598 23.038  9.203   1.00 21.82 ? 291 ARG B CZ    1 
ATOM   4532 N  NH1   . ARG B 1 297 ? -44.370 23.510  9.167   1.00 22.84 ? 291 ARG B NH1   1 
ATOM   4533 N  NH2   . ARG B 1 297 ? -46.545 23.636  8.505   1.00 23.43 ? 291 ARG B NH2   1 
ATOM   4534 N  N     . GLY B 1 298 ? -42.393 23.715  14.231  1.00 24.05 ? 292 GLY B N     1 
ATOM   4535 C  CA    . GLY B 1 298 ? -41.588 24.923  13.977  1.00 24.05 ? 292 GLY B CA    1 
ATOM   4536 C  C     . GLY B 1 298 ? -42.133 25.768  12.836  1.00 23.87 ? 292 GLY B C     1 
ATOM   4537 O  O     . GLY B 1 298 ? -41.342 26.433  12.164  1.00 24.10 ? 292 GLY B O     1 
ATOM   4538 N  N     . GLY B 1 299 ? -43.446 25.734  12.610  1.00 21.80 ? 293 GLY B N     1 
ATOM   4539 C  CA    . GLY B 1 299 ? -44.122 26.467  11.519  1.00 24.30 ? 293 GLY B CA    1 
ATOM   4540 C  C     . GLY B 1 299 ? -43.947 27.984  11.604  1.00 25.16 ? 293 GLY B C     1 
ATOM   4541 O  O     . GLY B 1 299 ? -44.006 28.657  10.521  1.00 24.98 ? 293 GLY B O     1 
ATOM   4542 N  N     . ILE B 1 300 ? -43.745 28.542  12.810  1.00 22.96 ? 294 ILE B N     1 
ATOM   4543 C  CA    . ILE B 1 300 ? -43.446 29.991  12.974  1.00 24.11 ? 294 ILE B CA    1 
ATOM   4544 C  C     . ILE B 1 300 ? -41.951 30.158  13.225  1.00 24.79 ? 294 ILE B C     1 
ATOM   4545 O  O     . ILE B 1 300 ? -41.457 29.604  14.217  1.00 24.98 ? 294 ILE B O     1 
ATOM   4546 C  CB    . ILE B 1 300 ? -44.244 30.650  14.127  1.00 25.87 ? 294 ILE B CB    1 
ATOM   4547 C  CG1   . ILE B 1 300 ? -45.753 30.496  13.976  1.00 26.11 ? 294 ILE B CG1   1 
ATOM   4548 C  CG2   . ILE B 1 300 ? -43.831 32.113  14.242  1.00 26.66 ? 294 ILE B CG2   1 
ATOM   4549 C  CD1   . ILE B 1 300 ? -46.328 31.164  12.786  1.00 29.26 ? 294 ILE B CD1   1 
ATOM   4550 N  N     . TYR B 1 301 ? -41.258 30.906  12.364  1.00 24.49 ? 295 TYR B N     1 
ATOM   4551 C  CA    . TYR B 1 301 ? -39.808 31.134  12.498  1.00 23.44 ? 295 TYR B CA    1 
ATOM   4552 C  C     . TYR B 1 301 ? -39.406 32.452  11.850  1.00 24.03 ? 295 TYR B C     1 
ATOM   4553 O  O     . TYR B 1 301 ? -40.293 33.160  11.400  1.00 24.13 ? 295 TYR B O     1 
ATOM   4554 C  CB    . TYR B 1 301 ? -39.053 29.953  11.896  1.00 25.43 ? 295 TYR B CB    1 
ATOM   4555 C  CG    . TYR B 1 301 ? -39.262 29.701  10.422  1.00 22.23 ? 295 TYR B CG    1 
ATOM   4556 C  CD1   . TYR B 1 301 ? -40.349 28.964  9.962   1.00 21.16 ? 295 TYR B CD1   1 
ATOM   4557 C  CD2   . TYR B 1 301 ? -38.348 30.147  9.492   1.00 23.35 ? 295 TYR B CD2   1 
ATOM   4558 C  CE1   . TYR B 1 301 ? -40.523 28.694  8.613   1.00 20.20 ? 295 TYR B CE1   1 
ATOM   4559 C  CE2   . TYR B 1 301 ? -38.481 29.851  8.146   1.00 22.55 ? 295 TYR B CE2   1 
ATOM   4560 C  CZ    . TYR B 1 301 ? -39.574 29.114  7.701   1.00 23.39 ? 295 TYR B CZ    1 
ATOM   4561 O  OH    . TYR B 1 301 ? -39.655 28.794  6.366   1.00 22.52 ? 295 TYR B OH    1 
ATOM   4562 N  N     . ASP B 1 302 ? -38.096 32.743  11.831  1.00 25.07 ? 296 ASP B N     1 
ATOM   4563 C  CA    . ASP B 1 302 ? -37.476 33.943  11.207  1.00 28.19 ? 296 ASP B CA    1 
ATOM   4564 C  C     . ASP B 1 302 ? -37.586 33.815  9.672   1.00 26.47 ? 296 ASP B C     1 
ATOM   4565 O  O     . ASP B 1 302 ? -36.647 33.373  9.037   1.00 25.09 ? 296 ASP B O     1 
ATOM   4566 C  CB    . ASP B 1 302 ? -36.016 34.054  11.678  1.00 33.42 ? 296 ASP B CB    1 
ATOM   4567 C  CG    . ASP B 1 302 ? -35.188 32.787  11.402  1.00 40.26 ? 296 ASP B CG    1 
ATOM   4568 O  OD1   . ASP B 1 302 ? -35.581 31.684  11.915  1.00 45.04 ? 296 ASP B OD1   1 
ATOM   4569 O  OD2   . ASP B 1 302 ? -34.181 32.872  10.631  1.00 43.32 ? 296 ASP B OD2   1 
ATOM   4570 N  N     . TRP B 1 303 ? -38.726 34.120  9.079   1.00 26.17 ? 297 TRP B N     1 
ATOM   4571 C  CA    . TRP B 1 303 ? -38.993 33.706  7.678   1.00 25.25 ? 297 TRP B CA    1 
ATOM   4572 C  C     . TRP B 1 303 ? -38.768 34.868  6.698   1.00 28.45 ? 297 TRP B C     1 
ATOM   4573 O  O     . TRP B 1 303 ? -38.975 34.705  5.492   1.00 24.81 ? 297 TRP B O     1 
ATOM   4574 C  CB    . TRP B 1 303 ? -40.375 33.098  7.591   1.00 25.54 ? 297 TRP B CB    1 
ATOM   4575 C  CG    . TRP B 1 303 ? -41.487 33.924  8.164   1.00 25.68 ? 297 TRP B CG    1 
ATOM   4576 C  CD1   . TRP B 1 303 ? -41.629 35.288  8.170   1.00 27.15 ? 297 TRP B CD1   1 
ATOM   4577 C  CD2   . TRP B 1 303 ? -42.705 33.387  8.686   1.00 21.83 ? 297 TRP B CD2   1 
ATOM   4578 N  NE1   . TRP B 1 303 ? -42.842 35.628  8.707   1.00 25.68 ? 297 TRP B NE1   1 
ATOM   4579 C  CE2   . TRP B 1 303 ? -43.526 34.479  9.025   1.00 25.58 ? 297 TRP B CE2   1 
ATOM   4580 C  CE3   . TRP B 1 303 ? -43.158 32.090  8.917   1.00 24.96 ? 297 TRP B CE3   1 
ATOM   4581 C  CZ2   . TRP B 1 303 ? -44.794 34.303  9.560   1.00 24.22 ? 297 TRP B CZ2   1 
ATOM   4582 C  CZ3   . TRP B 1 303 ? -44.408 31.915  9.449   1.00 26.41 ? 297 TRP B CZ3   1 
ATOM   4583 C  CH2   . TRP B 1 303 ? -45.207 33.014  9.784   1.00 28.37 ? 297 TRP B CH2   1 
ATOM   4584 N  N     . ASN B 1 304 ? -38.426 36.046  7.216   1.00 31.65 ? 298 ASN B N     1 
ATOM   4585 C  CA    . ASN B 1 304 ? -38.155 37.242  6.383   1.00 32.78 ? 298 ASN B CA    1 
ATOM   4586 C  C     . ASN B 1 304 ? -36.666 37.207  6.105   1.00 34.29 ? 298 ASN B C     1 
ATOM   4587 O  O     . ASN B 1 304 ? -35.911 36.897  7.068   1.00 35.81 ? 298 ASN B O     1 
ATOM   4588 C  CB    . ASN B 1 304 ? -38.614 38.523  7.087   1.00 35.92 ? 298 ASN B CB    1 
ATOM   4589 C  CG    . ASN B 1 304 ? -38.514 39.709  6.164   1.00 43.56 ? 298 ASN B CG    1 
ATOM   4590 O  OD1   . ASN B 1 304 ? -37.416 40.214  5.921   1.00 45.39 ? 298 ASN B OD1   1 
ATOM   4591 N  ND2   . ASN B 1 304 ? -39.641 40.104  5.592   1.00 41.80 ? 298 ASN B ND2   1 
ATOM   4592 N  N     . LYS B 1 305 ? -36.234 37.598  4.896   1.00 39.64 ? 299 LYS B N     1 
ATOM   4593 C  CA    . LYS B 1 305 ? -34.795 37.555  4.507   1.00 44.48 ? 299 LYS B CA    1 
ATOM   4594 C  C     . LYS B 1 305 ? -33.926 38.384  5.490   1.00 46.38 ? 299 LYS B C     1 
ATOM   4595 O  O     . LYS B 1 305 ? -32.725 38.086  5.596   1.00 44.83 ? 299 LYS B O     1 
ATOM   4596 C  CB    . LYS B 1 305 ? -34.590 37.878  3.015   1.00 42.21 ? 299 LYS B CB    1 
ATOM   4597 C  CG    . LYS B 1 305 ? -34.987 39.259  2.499   1.00 40.00 ? 299 LYS B CG    1 
ATOM   4598 C  CD    . LYS B 1 305 ? -34.358 39.596  1.086   1.00 37.50 ? 299 LYS B CD    1 
ATOM   4599 C  CE    . LYS B 1 305 ? -35.025 38.935  -0.133  1.00 32.03 ? 299 LYS B CE    1 
ATOM   4600 N  NZ    . LYS B 1 305 ? -34.138 38.569  -1.285  1.00 19.74 ? 299 LYS B NZ    1 
ATOM   4601 N  N     . SER B 1 306 ? -34.478 39.353  6.219   1.00 48.62 ? 300 SER B N     1 
ATOM   4602 C  CA    . SER B 1 306 ? -33.688 40.227  7.130   1.00 54.67 ? 300 SER B CA    1 
ATOM   4603 C  C     . SER B 1 306 ? -33.683 39.675  8.568   1.00 58.51 ? 300 SER B C     1 
ATOM   4604 O  O     . SER B 1 306 ? -32.697 39.957  9.281   1.00 66.42 ? 300 SER B O     1 
ATOM   4605 C  CB    . SER B 1 306 ? -34.174 41.654  7.065   1.00 58.14 ? 300 SER B CB    1 
ATOM   4606 O  OG    . SER B 1 306 ? -35.505 41.756  7.541   1.00 61.46 ? 300 SER B OG    1 
ATOM   4607 N  N     . SER B 1 307 ? -34.705 38.899  8.969   1.00 55.95 ? 301 SER B N     1 
ATOM   4608 C  CA    . SER B 1 307 ? -34.900 38.307  10.330  1.00 56.60 ? 301 SER B CA    1 
ATOM   4609 C  C     . SER B 1 307 ? -33.735 37.382  10.737  1.00 54.02 ? 301 SER B C     1 
ATOM   4610 O  O     . SER B 1 307 ? -33.296 36.578  9.892   1.00 55.95 ? 301 SER B O     1 
ATOM   4611 C  CB    . SER B 1 307 ? -36.210 37.527  10.412  1.00 57.06 ? 301 SER B CB    1 
ATOM   4612 O  OG    . SER B 1 307 ? -37.333 38.386  10.292  1.00 63.23 ? 301 SER B OG    1 
ATOM   4613 N  N     . CYS B 1 308 ? -33.326 37.415  12.013  1.00 52.73 ? 302 CYS B N     1 
ATOM   4614 C  CA    . CYS B 1 308 ? -32.332 36.487  12.639  1.00 57.44 ? 302 CYS B CA    1 
ATOM   4615 C  C     . CYS B 1 308 ? -33.038 35.488  13.580  1.00 49.74 ? 302 CYS B C     1 
ATOM   4616 O  O     . CYS B 1 308 ? -33.996 35.905  14.248  1.00 43.73 ? 302 CYS B O     1 
ATOM   4617 C  CB    . CYS B 1 308 ? -31.283 37.286  13.408  1.00 61.76 ? 302 CYS B CB    1 
ATOM   4618 S  SG    . CYS B 1 308 ? -30.434 38.508  12.374  1.00 79.38 ? 302 CYS B SG    1 
ATOM   4619 N  N     . SER B 1 309 ? -32.572 34.234  13.673  1.00 48.36 ? 303 SER B N     1 
ATOM   4620 C  CA    . SER B 1 309 ? -33.075 33.238  14.668  1.00 55.40 ? 303 SER B CA    1 
ATOM   4621 C  C     . SER B 1 309 ? -32.738 33.689  16.111  1.00 55.37 ? 303 SER B C     1 
ATOM   4622 O  O     . SER B 1 309 ? -33.486 33.296  17.042  1.00 48.50 ? 303 SER B O     1 
ATOM   4623 C  CB    . SER B 1 309 ? -32.585 31.826  14.367  1.00 55.38 ? 303 SER B CB    1 
ATOM   4624 O  OG    . SER B 1 309 ? -31.209 31.656  14.688  1.00 56.16 ? 303 SER B OG    1 
ATOM   4625 N  N     . SER B 1 310 ? -31.690 34.517  16.290  1.00 57.84 ? 304 SER B N     1 
ATOM   4626 C  CA    . SER B 1 310 ? -31.201 35.064  17.591  1.00 62.64 ? 304 SER B CA    1 
ATOM   4627 C  C     . SER B 1 310 ? -32.195 36.076  18.178  1.00 59.57 ? 304 SER B C     1 
ATOM   4628 O  O     . SER B 1 310 ? -32.045 36.408  19.385  1.00 58.39 ? 304 SER B O     1 
ATOM   4629 C  CB    . SER B 1 310 ? -29.847 35.725  17.450  1.00 63.59 ? 304 SER B CB    1 
ATOM   4630 O  OG    . SER B 1 310 ? -28.903 34.832  16.898  1.00 67.01 ? 304 SER B OG    1 
ATOM   4631 N  N     . ASP B 1 311 ? -33.142 36.558  17.360  1.00 52.06 ? 305 ASP B N     1 
ATOM   4632 C  CA    . ASP B 1 311 ? -34.163 37.559  17.760  1.00 55.62 ? 305 ASP B CA    1 
ATOM   4633 C  C     . ASP B 1 311 ? -35.451 36.839  18.200  1.00 48.86 ? 305 ASP B C     1 
ATOM   4634 O  O     . ASP B 1 311 ? -36.408 37.554  18.550  1.00 44.61 ? 305 ASP B O     1 
ATOM   4635 C  CB    . ASP B 1 311 ? -34.332 38.631  16.670  1.00 59.73 ? 305 ASP B CB    1 
ATOM   4636 C  CG    . ASP B 1 311 ? -35.379 38.377  15.594  1.00 67.54 ? 305 ASP B CG    1 
ATOM   4637 O  OD1   . ASP B 1 311 ? -36.135 37.407  15.719  1.00 80.42 ? 305 ASP B OD1   1 
ATOM   4638 O  OD2   . ASP B 1 311 ? -35.430 39.169  14.625  1.00 81.96 ? 305 ASP B OD2   1 
ATOM   4639 N  N     . SER B 1 312 ? -35.496 35.492  18.232  1.00 43.53 ? 306 SER B N     1 
ATOM   4640 C  CA    . SER B 1 312 ? -36.695 34.755  18.739  1.00 39.29 ? 306 SER B CA    1 
ATOM   4641 C  C     . SER B 1 312 ? -36.984 35.204  20.188  1.00 35.64 ? 306 SER B C     1 
ATOM   4642 O  O     . SER B 1 312 ? -38.173 35.153  20.619  1.00 34.42 ? 306 SER B O     1 
ATOM   4643 C  CB    . SER B 1 312 ? -36.567 33.240  18.634  1.00 38.02 ? 306 SER B CB    1 
ATOM   4644 O  OG    . SER B 1 312 ? -35.488 32.742  19.416  1.00 35.62 ? 306 SER B OG    1 
ATOM   4645 N  N     . LYS B 1 313 ? -35.952 35.645  20.923  1.00 33.15 ? 307 LYS B N     1 
ATOM   4646 C  CA    . LYS B 1 313 ? -36.102 36.093  22.339  1.00 34.36 ? 307 LYS B CA    1 
ATOM   4647 C  C     . LYS B 1 313 ? -36.943 37.374  22.415  1.00 35.35 ? 307 LYS B C     1 
ATOM   4648 O  O     . LYS B 1 313 ? -37.530 37.621  23.510  1.00 31.40 ? 307 LYS B O     1 
ATOM   4649 C  CB    . LYS B 1 313 ? -34.751 36.272  23.033  1.00 35.43 ? 307 LYS B CB    1 
ATOM   4650 C  CG    . LYS B 1 313 ? -33.798 37.285  22.431  1.00 35.77 ? 307 LYS B CG    1 
ATOM   4651 C  CD    . LYS B 1 313 ? -32.480 37.275  23.162  1.00 37.41 ? 307 LYS B CD    1 
ATOM   4652 C  CE    . LYS B 1 313 ? -31.529 38.366  22.733  1.00 43.59 ? 307 LYS B CE    1 
ATOM   4653 N  NZ    . LYS B 1 313 ? -30.419 38.502  23.711  1.00 50.89 ? 307 LYS B NZ    1 
ATOM   4654 N  N     . ASP B 1 314 ? -37.016 38.148  21.319  1.00 34.81 ? 308 ASP B N     1 
ATOM   4655 C  CA    . ASP B 1 314 ? -37.670 39.488  21.288  1.00 41.65 ? 308 ASP B CA    1 
ATOM   4656 C  C     . ASP B 1 314 ? -39.165 39.381  20.928  1.00 42.09 ? 308 ASP B C     1 
ATOM   4657 O  O     . ASP B 1 314 ? -39.833 40.437  20.957  1.00 41.68 ? 308 ASP B O     1 
ATOM   4658 C  CB    . ASP B 1 314 ? -36.924 40.445  20.341  1.00 44.24 ? 308 ASP B CB    1 
ATOM   4659 C  CG    . ASP B 1 314 ? -35.437 40.647  20.656  1.00 50.23 ? 308 ASP B CG    1 
ATOM   4660 O  OD1   . ASP B 1 314 ? -35.044 40.614  21.873  1.00 39.25 ? 308 ASP B OD1   1 
ATOM   4661 O  OD2   . ASP B 1 314 ? -34.660 40.824  19.683  1.00 56.86 ? 308 ASP B OD2   1 
ATOM   4662 N  N     . LEU B 1 315 ? -39.690 38.184  20.616  1.00 45.78 ? 309 LEU B N     1 
ATOM   4663 C  CA    . LEU B 1 315 ? -41.102 37.984  20.157  1.00 48.44 ? 309 LEU B CA    1 
ATOM   4664 C  C     . LEU B 1 315 ? -42.021 37.655  21.345  1.00 46.68 ? 309 LEU B C     1 
ATOM   4665 O  O     . LEU B 1 315 ? -41.629 36.816  22.166  1.00 43.70 ? 309 LEU B O     1 
ATOM   4666 C  CB    . LEU B 1 315 ? -41.133 36.856  19.113  1.00 54.58 ? 309 LEU B CB    1 
ATOM   4667 C  CG    . LEU B 1 315 ? -40.313 37.111  17.839  1.00 58.71 ? 309 LEU B CG    1 
ATOM   4668 C  CD1   . LEU B 1 315 ? -40.428 35.951  16.853  1.00 56.49 ? 309 LEU B CD1   1 
ATOM   4669 C  CD2   . LEU B 1 315 ? -40.730 38.416  17.168  1.00 56.16 ? 309 LEU B CD2   1 
ATOM   4670 N  N     . GLU B 1 316 ? -43.187 38.309  21.441  1.00 46.95 ? 310 GLU B N     1 
ATOM   4671 C  CA    . GLU B 1 316 ? -44.299 37.936  22.371  1.00 49.14 ? 310 GLU B CA    1 
ATOM   4672 C  C     . GLU B 1 316 ? -45.573 37.849  21.518  1.00 44.82 ? 310 GLU B C     1 
ATOM   4673 O  O     . GLU B 1 316 ? -45.869 38.832  20.849  1.00 50.56 ? 310 GLU B O     1 
ATOM   4674 C  CB    . GLU B 1 316 ? -44.437 38.923  23.543  1.00 48.75 ? 310 GLU B CB    1 
ATOM   4675 C  CG    . GLU B 1 316 ? -43.122 39.237  24.270  1.00 54.93 ? 310 GLU B CG    1 
ATOM   4676 C  CD    . GLU B 1 316 ? -42.699 38.304  25.410  1.00 60.48 ? 310 GLU B CD    1 
ATOM   4677 O  OE1   . GLU B 1 316 ? -43.593 37.598  25.955  1.00 57.28 ? 310 GLU B OE1   1 
ATOM   4678 O  OE2   . GLU B 1 316 ? -41.473 38.282  25.772  1.00 49.69 ? 310 GLU B OE2   1 
ATOM   4679 N  N     . TRP B 1 317 ? -46.246 36.696  21.479  1.00 38.84 ? 311 TRP B N     1 
ATOM   4680 C  CA    . TRP B 1 317 ? -47.429 36.442  20.597  1.00 43.28 ? 311 TRP B CA    1 
ATOM   4681 C  C     . TRP B 1 317 ? -48.693 37.118  21.150  1.00 43.99 ? 311 TRP B C     1 
ATOM   4682 O  O     . TRP B 1 317 ? -49.104 36.700  22.219  1.00 52.52 ? 311 TRP B O     1 
ATOM   4683 C  CB    . TRP B 1 317 ? -47.654 34.939  20.374  1.00 40.22 ? 311 TRP B CB    1 
ATOM   4684 C  CG    . TRP B 1 317 ? -46.655 34.287  19.454  1.00 41.20 ? 311 TRP B CG    1 
ATOM   4685 C  CD1   . TRP B 1 317 ? -45.664 34.882  18.717  1.00 42.51 ? 311 TRP B CD1   1 
ATOM   4686 C  CD2   . TRP B 1 317 ? -46.576 32.884  19.151  1.00 41.73 ? 311 TRP B CD2   1 
ATOM   4687 N  NE1   . TRP B 1 317 ? -44.967 33.946  17.991  1.00 37.51 ? 311 TRP B NE1   1 
ATOM   4688 C  CE2   . TRP B 1 317 ? -45.508 32.713  18.234  1.00 37.86 ? 311 TRP B CE2   1 
ATOM   4689 C  CE3   . TRP B 1 317 ? -47.291 31.754  19.581  1.00 42.95 ? 311 TRP B CE3   1 
ATOM   4690 C  CZ2   . TRP B 1 317 ? -45.137 31.452  17.757  1.00 41.15 ? 311 TRP B CZ2   1 
ATOM   4691 C  CZ3   . TRP B 1 317 ? -46.939 30.514  19.083  1.00 41.83 ? 311 TRP B CZ3   1 
ATOM   4692 C  CH2   . TRP B 1 317 ? -45.880 30.371  18.177  1.00 41.84 ? 311 TRP B CH2   1 
ATOM   4693 N  N     . GLY C 1 24  ? 13.403  32.123  -16.338 1.00 60.63 ? 18  GLY C N     1 
ATOM   4694 C  CA    . GLY C 1 24  ? 12.049  32.366  -16.961 1.00 58.64 ? 18  GLY C CA    1 
ATOM   4695 C  C     . GLY C 1 24  ? 11.680  33.844  -17.030 1.00 57.38 ? 18  GLY C C     1 
ATOM   4696 O  O     . GLY C 1 24  ? 12.412  34.605  -17.681 1.00 59.50 ? 18  GLY C O     1 
ATOM   4697 N  N     . GLN C 1 25  ? 10.565  34.265  -16.415 1.00 49.03 ? 19  GLN C N     1 
ATOM   4698 C  CA    . GLN C 1 25  ? 10.098  35.682  -16.509 1.00 40.50 ? 19  GLN C CA    1 
ATOM   4699 C  C     . GLN C 1 25  ? 11.003  36.566  -15.624 1.00 38.08 ? 19  GLN C C     1 
ATOM   4700 O  O     . GLN C 1 25  ? 11.631  36.026  -14.698 1.00 39.53 ? 19  GLN C O     1 
ATOM   4701 C  CB    . GLN C 1 25  ? 8.625   35.754  -16.123 1.00 36.15 ? 19  GLN C CB    1 
ATOM   4702 C  CG    . GLN C 1 25  ? 7.750   34.826  -16.949 1.00 42.09 ? 19  GLN C CG    1 
ATOM   4703 C  CD    . GLN C 1 25  ? 6.306   34.832  -16.516 1.00 33.60 ? 19  GLN C CD    1 
ATOM   4704 O  OE1   . GLN C 1 25  ? 5.940   34.292  -15.481 1.00 47.58 ? 19  GLN C OE1   1 
ATOM   4705 N  NE2   . GLN C 1 25  ? 5.451   35.395  -17.340 1.00 35.52 ? 19  GLN C NE2   1 
ATOM   4706 N  N     . VAL C 1 26  ? 11.074  37.874  -15.871 1.00 32.86 ? 20  VAL C N     1 
ATOM   4707 C  CA    . VAL C 1 26  ? 11.759  38.829  -14.942 1.00 31.97 ? 20  VAL C CA    1 
ATOM   4708 C  C     . VAL C 1 26  ? 10.685  39.500  -14.070 1.00 29.68 ? 20  VAL C C     1 
ATOM   4709 O  O     . VAL C 1 26  ? 9.777   40.170  -14.592 1.00 27.43 ? 20  VAL C O     1 
ATOM   4710 C  CB    . VAL C 1 26  ? 12.583  39.882  -15.703 1.00 33.16 ? 20  VAL C CB    1 
ATOM   4711 C  CG1   . VAL C 1 26  ? 13.125  40.931  -14.763 1.00 34.36 ? 20  VAL C CG1   1 
ATOM   4712 C  CG2   . VAL C 1 26  ? 13.706  39.269  -16.534 1.00 37.09 ? 20  VAL C CG2   1 
ATOM   4713 N  N     . PRO C 1 27  ? 10.752  39.369  -12.728 1.00 23.84 ? 21  PRO C N     1 
ATOM   4714 C  CA    . PRO C 1 27  ? 9.723   39.933  -11.851 1.00 22.56 ? 21  PRO C CA    1 
ATOM   4715 C  C     . PRO C 1 27  ? 9.956   41.424  -11.600 1.00 22.59 ? 21  PRO C C     1 
ATOM   4716 O  O     . PRO C 1 27  ? 10.441  41.818  -10.534 1.00 25.03 ? 21  PRO C O     1 
ATOM   4717 C  CB    . PRO C 1 27  ? 9.873   39.090  -10.571 1.00 22.67 ? 21  PRO C CB    1 
ATOM   4718 C  CG    . PRO C 1 27  ? 11.374  38.841  -10.504 1.00 24.13 ? 21  PRO C CG    1 
ATOM   4719 C  CD    . PRO C 1 27  ? 11.781  38.651  -11.958 1.00 24.33 ? 21  PRO C CD    1 
ATOM   4720 N  N     . VAL C 1 28  ? 9.581   42.246  -12.572 1.00 21.61 ? 22  VAL C N     1 
ATOM   4721 C  CA    . VAL C 1 28  ? 10.021  43.656  -12.642 1.00 21.71 ? 22  VAL C CA    1 
ATOM   4722 C  C     . VAL C 1 28  ? 9.269   44.504  -11.611 1.00 21.33 ? 22  VAL C C     1 
ATOM   4723 O  O     . VAL C 1 28  ? 9.831   45.465  -11.108 1.00 22.41 ? 22  VAL C O     1 
ATOM   4724 C  CB    . VAL C 1 28  ? 9.857   44.193  -14.071 1.00 23.90 ? 22  VAL C CB    1 
ATOM   4725 C  CG1   . VAL C 1 28  ? 8.398   44.297  -14.481 1.00 25.08 ? 22  VAL C CG1   1 
ATOM   4726 C  CG2   . VAL C 1 28  ? 10.549  45.514  -14.222 1.00 29.70 ? 22  VAL C CG2   1 
ATOM   4727 N  N     . SER C 1 29  ? 8.014   44.173  -11.306 1.00 21.46 ? 23  SER C N     1 
ATOM   4728 C  CA    . SER C 1 29  ? 7.169   44.989  -10.396 1.00 18.73 ? 23  SER C CA    1 
ATOM   4729 C  C     . SER C 1 29  ? 6.397   44.042  -9.479  1.00 18.86 ? 23  SER C C     1 
ATOM   4730 O  O     . SER C 1 29  ? 5.669   43.200  -10.020 1.00 20.46 ? 23  SER C O     1 
ATOM   4731 C  CB    . SER C 1 29  ? 6.281   45.851  -11.184 1.00 20.24 ? 23  SER C CB    1 
ATOM   4732 O  OG    . SER C 1 29  ? 5.515   46.661  -10.327 1.00 19.65 ? 23  SER C OG    1 
ATOM   4733 N  N     . VAL C 1 30  ? 6.666   44.094  -8.175  1.00 18.24 ? 24  VAL C N     1 
ATOM   4734 C  CA    . VAL C 1 30  ? 6.166   43.074  -7.217  1.00 17.29 ? 24  VAL C CA    1 
ATOM   4735 C  C     . VAL C 1 30  ? 5.344   43.729  -6.111  1.00 18.34 ? 24  VAL C C     1 
ATOM   4736 O  O     . VAL C 1 30  ? 5.743   44.789  -5.575  1.00 18.50 ? 24  VAL C O     1 
ATOM   4737 C  CB    . VAL C 1 30  ? 7.326   42.269  -6.640  1.00 18.97 ? 24  VAL C CB    1 
ATOM   4738 C  CG1   . VAL C 1 30  ? 6.864   41.246  -5.599  1.00 20.74 ? 24  VAL C CG1   1 
ATOM   4739 C  CG2   . VAL C 1 30  ? 8.097   41.605  -7.780  1.00 18.84 ? 24  VAL C CG2   1 
ATOM   4740 N  N     . ASN C 1 31  ? 4.245   43.081  -5.755  1.00 18.45 ? 25  ASN C N     1 
ATOM   4741 C  CA    . ASN C 1 31  ? 3.405   43.487  -4.614  1.00 17.00 ? 25  ASN C CA    1 
ATOM   4742 C  C     . ASN C 1 31  ? 3.730   42.603  -3.412  1.00 17.66 ? 25  ASN C C     1 
ATOM   4743 O  O     . ASN C 1 31  ? 3.613   41.378  -3.529  1.00 19.03 ? 25  ASN C O     1 
ATOM   4744 C  CB    . ASN C 1 31  ? 1.921   43.389  -4.965  1.00 18.98 ? 25  ASN C CB    1 
ATOM   4745 C  CG    . ASN C 1 31  ? 1.481   44.646  -5.645  1.00 20.65 ? 25  ASN C CG    1 
ATOM   4746 O  OD1   . ASN C 1 31  ? 0.894   45.532  -5.005  1.00 25.91 ? 25  ASN C OD1   1 
ATOM   4747 N  ND2   . ASN C 1 31  ? 1.785   44.729  -6.924  1.00 18.74 ? 25  ASN C ND2   1 
ATOM   4748 N  N     . TYR C 1 32  ? 4.228   43.197  -2.353  1.00 17.45 ? 26  TYR C N     1 
ATOM   4749 C  CA    . TYR C 1 32  ? 4.511   42.462  -1.103  1.00 17.46 ? 26  TYR C CA    1 
ATOM   4750 C  C     . TYR C 1 32  ? 3.409   42.760  -0.101  1.00 17.05 ? 26  TYR C C     1 
ATOM   4751 O  O     . TYR C 1 32  ? 3.458   43.843  0.522   1.00 18.30 ? 26  TYR C O     1 
ATOM   4752 C  CB    . TYR C 1 32  ? 5.912   42.794  -0.587  1.00 18.51 ? 26  TYR C CB    1 
ATOM   4753 C  CG    . TYR C 1 32  ? 6.335   42.120  0.689   1.00 16.70 ? 26  TYR C CG    1 
ATOM   4754 C  CD1   . TYR C 1 32  ? 5.771   40.928  1.139   1.00 17.41 ? 26  TYR C CD1   1 
ATOM   4755 C  CD2   . TYR C 1 32  ? 7.379   42.650  1.437   1.00 18.94 ? 26  TYR C CD2   1 
ATOM   4756 C  CE1   . TYR C 1 32  ? 6.208   40.326  2.317   1.00 19.10 ? 26  TYR C CE1   1 
ATOM   4757 C  CE2   . TYR C 1 32  ? 7.803   42.085  2.624   1.00 18.42 ? 26  TYR C CE2   1 
ATOM   4758 C  CZ    . TYR C 1 32  ? 7.244   40.892  3.056   1.00 18.39 ? 26  TYR C CZ    1 
ATOM   4759 O  OH    . TYR C 1 32  ? 7.664   40.343  4.246   1.00 18.59 ? 26  TYR C OH    1 
ATOM   4760 N  N     . HIS C 1 33  ? 2.460   41.807  0.037   1.00 18.14 ? 27  HIS C N     1 
ATOM   4761 C  CA    . HIS C 1 33  ? 1.353   41.852  1.029   1.00 18.48 ? 27  HIS C CA    1 
ATOM   4762 C  C     . HIS C 1 33  ? 1.943   41.332  2.355   1.00 18.21 ? 27  HIS C C     1 
ATOM   4763 O  O     . HIS C 1 33  ? 1.800   40.128  2.690   1.00 19.22 ? 27  HIS C O     1 
ATOM   4764 C  CB    . HIS C 1 33  ? 0.134   41.084  0.506   1.00 19.60 ? 27  HIS C CB    1 
ATOM   4765 C  CG    . HIS C 1 33  ? -0.460  41.652  -0.742  1.00 22.29 ? 27  HIS C CG    1 
ATOM   4766 N  ND1   . HIS C 1 33  ? -1.713  42.240  -0.761  1.00 25.28 ? 27  HIS C ND1   1 
ATOM   4767 C  CD2   . HIS C 1 33  ? 0.031   41.772  -1.987  1.00 21.54 ? 27  HIS C CD2   1 
ATOM   4768 C  CE1   . HIS C 1 33  ? -1.989  42.605  -2.007  1.00 25.79 ? 27  HIS C CE1   1 
ATOM   4769 N  NE2   . HIS C 1 33  ? -0.926  42.323  -2.768  1.00 23.09 ? 27  HIS C NE2   1 
ATOM   4770 N  N     . PHE C 1 34  ? 2.708   42.174  3.049   1.00 18.72 ? 28  PHE C N     1 
ATOM   4771 C  CA    . PHE C 1 34  ? 3.616   41.676  4.115   1.00 19.67 ? 28  PHE C CA    1 
ATOM   4772 C  C     . PHE C 1 34  ? 2.811   41.290  5.366   1.00 19.61 ? 28  PHE C C     1 
ATOM   4773 O  O     . PHE C 1 34  ? 3.353   40.563  6.227   1.00 19.69 ? 28  PHE C O     1 
ATOM   4774 C  CB    . PHE C 1 34  ? 4.690   42.709  4.415   1.00 18.64 ? 28  PHE C CB    1 
ATOM   4775 C  CG    . PHE C 1 34  ? 4.204   44.018  4.980   1.00 18.27 ? 28  PHE C CG    1 
ATOM   4776 C  CD1   . PHE C 1 34  ? 4.091   44.196  6.349   1.00 17.84 ? 28  PHE C CD1   1 
ATOM   4777 C  CD2   . PHE C 1 34  ? 4.006   45.100  4.151   1.00 18.48 ? 28  PHE C CD2   1 
ATOM   4778 C  CE1   . PHE C 1 34  ? 3.701   45.419  6.872   1.00 17.02 ? 28  PHE C CE1   1 
ATOM   4779 C  CE2   . PHE C 1 34  ? 3.580   46.313  4.679   1.00 19.83 ? 28  PHE C CE2   1 
ATOM   4780 C  CZ    . PHE C 1 34  ? 3.512   46.491  6.037   1.00 18.44 ? 28  PHE C CZ    1 
ATOM   4781 N  N     . SER C 1 35  ? 1.570   41.771  5.483   1.00 20.10 ? 29  SER C N     1 
ATOM   4782 C  CA    A SER C 1 35  ? 0.667   41.380  6.592   0.50 20.88 ? 29  SER C CA    1 
ATOM   4783 C  CA    B SER C 1 35  ? 0.664   41.460  6.616   0.50 21.57 ? 29  SER C CA    1 
ATOM   4784 C  C     . SER C 1 35  ? -0.783  41.399  6.116   1.00 20.67 ? 29  SER C C     1 
ATOM   4785 O  O     . SER C 1 35  ? -1.092  42.119  5.161   1.00 19.87 ? 29  SER C O     1 
ATOM   4786 C  CB    A SER C 1 35  ? 0.848   42.280  7.793   0.50 21.58 ? 29  SER C CB    1 
ATOM   4787 C  CB    B SER C 1 35  ? 0.831   42.493  7.727   0.50 22.83 ? 29  SER C CB    1 
ATOM   4788 O  OG    A SER C 1 35  ? -0.158  42.040  8.774   0.50 20.73 ? 29  SER C OG    1 
ATOM   4789 O  OG    B SER C 1 35  ? 0.291   43.765  7.365   0.50 23.68 ? 29  SER C OG    1 
ATOM   4790 N  N     . ARG C 1 36  ? -1.622  40.581  6.746   1.00 21.35 ? 30  ARG C N     1 
ATOM   4791 C  CA    . ARG C 1 36  ? -3.064  40.509  6.387   1.00 21.68 ? 30  ARG C CA    1 
ATOM   4792 C  C     . ARG C 1 36  ? -3.923  41.266  7.394   1.00 21.60 ? 30  ARG C C     1 
ATOM   4793 O  O     . ARG C 1 36  ? -5.131  41.378  7.154   1.00 22.70 ? 30  ARG C O     1 
ATOM   4794 C  CB    . ARG C 1 36  ? -3.471  39.043  6.264   1.00 22.04 ? 30  ARG C CB    1 
ATOM   4795 C  CG    . ARG C 1 36  ? -2.969  38.370  5.002   1.00 21.14 ? 30  ARG C CG    1 
ATOM   4796 C  CD    . ARG C 1 36  ? -3.325  36.922  4.948   1.00 20.46 ? 30  ARG C CD    1 
ATOM   4797 N  NE    . ARG C 1 36  ? -3.047  36.318  3.664   1.00 21.62 ? 30  ARG C NE    1 
ATOM   4798 C  CZ    . ARG C 1 36  ? -3.904  36.205  2.663   1.00 23.03 ? 30  ARG C CZ    1 
ATOM   4799 N  NH1   . ARG C 1 36  ? -5.136  36.674  2.769   1.00 21.40 ? 30  ARG C NH1   1 
ATOM   4800 N  NH2   . ARG C 1 36  ? -3.513  35.591  1.554   1.00 26.73 ? 30  ARG C NH2   1 
ATOM   4801 N  N     . LYS C 1 37  ? -3.354  41.823  8.465   1.00 23.82 ? 31  LYS C N     1 
ATOM   4802 C  CA    . LYS C 1 37  ? -4.135  42.590  9.476   1.00 24.68 ? 31  LYS C CA    1 
ATOM   4803 C  C     . LYS C 1 37  ? -4.672  43.875  8.859   1.00 21.34 ? 31  LYS C C     1 
ATOM   4804 O  O     . LYS C 1 37  ? -3.945  44.543  8.063   1.00 20.21 ? 31  LYS C O     1 
ATOM   4805 C  CB    . LYS C 1 37  ? -3.295  42.911  10.723  1.00 27.35 ? 31  LYS C CB    1 
ATOM   4806 C  CG    . LYS C 1 37  ? -4.117  43.190  11.982  1.00 39.84 ? 31  LYS C CG    1 
ATOM   4807 C  CD    . LYS C 1 37  ? -3.290  43.458  13.263  1.00 46.76 ? 31  LYS C CD    1 
ATOM   4808 C  CE    . LYS C 1 37  ? -2.510  42.245  13.748  1.00 53.29 ? 31  LYS C CE    1 
ATOM   4809 N  NZ    . LYS C 1 37  ? -3.292  41.394  14.680  1.00 55.80 ? 31  LYS C NZ    1 
ATOM   4810 N  N     . CYS C 1 38  ? -5.914  44.223  9.183   1.00 20.87 ? 32  CYS C N     1 
ATOM   4811 C  CA    . CYS C 1 38  ? -6.517  45.489  8.749   1.00 22.52 ? 32  CYS C CA    1 
ATOM   4812 C  C     . CYS C 1 38  ? -7.501  46.079  9.765   1.00 23.52 ? 32  CYS C C     1 
ATOM   4813 O  O     . CYS C 1 38  ? -8.132  45.312  10.496  1.00 26.10 ? 32  CYS C O     1 
ATOM   4814 C  CB    . CYS C 1 38  ? -7.231  45.275  7.425   1.00 20.88 ? 32  CYS C CB    1 
ATOM   4815 S  SG    . CYS C 1 38  ? -7.739  46.866  6.778   1.00 23.92 ? 32  CYS C SG    1 
ATOM   4816 N  N     . ASN C 1 39  ? -7.638  47.399  9.749   1.00 27.57 ? 33  ASN C N     1 
ATOM   4817 C  CA    . ASN C 1 39  ? -8.495  48.153  10.695  1.00 32.90 ? 33  ASN C CA    1 
ATOM   4818 C  C     . ASN C 1 39  ? -9.855  48.458  10.072  1.00 31.60 ? 33  ASN C C     1 
ATOM   4819 O  O     . ASN C 1 39  ? -10.655 49.117  10.746  1.00 33.73 ? 33  ASN C O     1 
ATOM   4820 C  CB    . ASN C 1 39  ? -7.837  49.456  11.144  1.00 29.69 ? 33  ASN C CB    1 
ATOM   4821 C  CG    . ASN C 1 39  ? -7.529  50.436  10.032  1.00 31.18 ? 33  ASN C CG    1 
ATOM   4822 O  OD1   . ASN C 1 39  ? -7.084  50.069  8.952   1.00 28.69 ? 33  ASN C OD1   1 
ATOM   4823 N  ND2   . ASN C 1 39  ? -7.667  51.710  10.325  1.00 30.02 ? 33  ASN C ND2   1 
ATOM   4824 N  N     . LYS C 1 40  ? -10.138 48.008  8.849   1.00 26.93 ? 34  LYS C N     1 
ATOM   4825 C  CA    . LYS C 1 40  ? -11.419 48.340  8.168   1.00 27.03 ? 34  LYS C CA    1 
ATOM   4826 C  C     . LYS C 1 40  ? -12.161 47.048  7.827   1.00 24.02 ? 34  LYS C C     1 
ATOM   4827 O  O     . LYS C 1 40  ? -11.681 46.014  8.187   1.00 27.64 ? 34  LYS C O     1 
ATOM   4828 C  CB    . LYS C 1 40  ? -11.144 49.281  6.996   1.00 29.43 ? 34  LYS C CB    1 
ATOM   4829 C  CG    . LYS C 1 40  ? -10.755 50.682  7.427   1.00 36.25 ? 34  LYS C CG    1 
ATOM   4830 C  CD    . LYS C 1 40  ? -10.840 51.715  6.320   1.00 45.30 ? 34  LYS C CD    1 
ATOM   4831 C  CE    . LYS C 1 40  ? -10.820 53.144  6.845   1.00 53.66 ? 34  LYS C CE    1 
ATOM   4832 N  NZ    . LYS C 1 40  ? -10.778 54.139  5.740   1.00 61.39 ? 34  LYS C NZ    1 
ATOM   4833 N  N     . GLU C 1 41  ? -13.316 47.149  7.163   1.00 26.09 ? 35  GLU C N     1 
ATOM   4834 C  CA    . GLU C 1 41  ? -14.302 46.042  7.005   1.00 26.97 ? 35  GLU C CA    1 
ATOM   4835 C  C     . GLU C 1 41  ? -14.852 45.995  5.580   1.00 27.24 ? 35  GLU C C     1 
ATOM   4836 O  O     . GLU C 1 41  ? -16.005 45.547  5.414   1.00 26.50 ? 35  GLU C O     1 
ATOM   4837 C  CB    . GLU C 1 41  ? -15.465 46.251  7.971   1.00 30.89 ? 35  GLU C CB    1 
ATOM   4838 C  CG    . GLU C 1 41  ? -15.005 46.404  9.406   1.00 39.33 ? 35  GLU C CG    1 
ATOM   4839 C  CD    . GLU C 1 41  ? -16.100 46.390  10.468  1.00 47.35 ? 35  GLU C CD    1 
ATOM   4840 O  OE1   . GLU C 1 41  ? -17.238 45.948  10.173  1.00 51.37 ? 35  GLU C OE1   1 
ATOM   4841 O  OE2   . GLU C 1 41  ? -15.808 46.824  11.596  1.00 60.76 ? 35  GLU C OE2   1 
ATOM   4842 N  N     . CYS C 1 42  ? -14.072 46.399  4.573   1.00 23.92 ? 36  CYS C N     1 
ATOM   4843 C  CA    . CYS C 1 42  ? -14.590 46.556  3.203   1.00 23.64 ? 36  CYS C CA    1 
ATOM   4844 C  C     . CYS C 1 42  ? -15.275 45.243  2.814   1.00 23.26 ? 36  CYS C C     1 
ATOM   4845 O  O     . CYS C 1 42  ? -14.611 44.164  2.863   1.00 21.25 ? 36  CYS C O     1 
ATOM   4846 C  CB    . CYS C 1 42  ? -13.499 46.940  2.197   1.00 26.05 ? 36  CYS C CB    1 
ATOM   4847 S  SG    . CYS C 1 42  ? -12.497 48.344  2.741   1.00 25.18 ? 36  CYS C SG    1 
ATOM   4848 N  N     . LEU C 1 43  ? -16.548 45.322  2.387   1.00 23.02 ? 37  LEU C N     1 
ATOM   4849 C  CA    . LEU C 1 43  ? -17.373 44.114  2.089   1.00 23.62 ? 37  LEU C CA    1 
ATOM   4850 C  C     . LEU C 1 43  ? -16.752 43.297  0.948   1.00 22.64 ? 37  LEU C C     1 
ATOM   4851 O  O     . LEU C 1 43  ? -16.975 42.087  0.919   1.00 23.41 ? 37  LEU C O     1 
ATOM   4852 C  CB    . LEU C 1 43  ? -18.815 44.520  1.753   1.00 26.70 ? 37  LEU C CB    1 
ATOM   4853 C  CG    . LEU C 1 43  ? -19.614 45.078  2.934   1.00 32.15 ? 37  LEU C CG    1 
ATOM   4854 C  CD1   . LEU C 1 43  ? -21.044 45.444  2.561   1.00 33.13 ? 37  LEU C CD1   1 
ATOM   4855 C  CD2   . LEU C 1 43  ? -19.619 44.092  4.087   1.00 32.31 ? 37  LEU C CD2   1 
ATOM   4856 N  N     . PHE C 1 44  ? -15.980 43.895  0.055   1.00 19.96 ? 38  PHE C N     1 
ATOM   4857 C  CA    . PHE C 1 44  ? -15.458 43.156  -1.126  1.00 21.25 ? 38  PHE C CA    1 
ATOM   4858 C  C     . PHE C 1 44  ? -14.029 42.636  -0.921  1.00 20.12 ? 38  PHE C C     1 
ATOM   4859 O  O     . PHE C 1 44  ? -13.510 42.005  -1.856  1.00 20.50 ? 38  PHE C O     1 
ATOM   4860 C  CB    . PHE C 1 44  ? -15.514 44.020  -2.387  1.00 19.82 ? 38  PHE C CB    1 
ATOM   4861 C  CG    . PHE C 1 44  ? -14.969 45.399  -2.191  1.00 21.43 ? 38  PHE C CG    1 
ATOM   4862 C  CD1   . PHE C 1 44  ? -13.617 45.600  -1.954  1.00 22.26 ? 38  PHE C CD1   1 
ATOM   4863 C  CD2   . PHE C 1 44  ? -15.809 46.503  -2.242  1.00 24.69 ? 38  PHE C CD2   1 
ATOM   4864 C  CE1   . PHE C 1 44  ? -13.130 46.863  -1.693  1.00 23.41 ? 38  PHE C CE1   1 
ATOM   4865 C  CE2   . PHE C 1 44  ? -15.301 47.769  -2.024  1.00 26.38 ? 38  PHE C CE2   1 
ATOM   4866 C  CZ    . PHE C 1 44  ? -13.970 47.941  -1.755  1.00 27.09 ? 38  PHE C CZ    1 
ATOM   4867 N  N     . CYS C 1 45  ? -13.408 42.883  0.231   1.00 21.24 ? 39  CYS C N     1 
ATOM   4868 C  CA    . CYS C 1 45  ? -11.932 42.716  0.390   1.00 21.27 ? 39  CYS C CA    1 
ATOM   4869 C  C     . CYS C 1 45  ? -11.483 41.375  -0.182  1.00 19.84 ? 39  CYS C C     1 
ATOM   4870 O  O     . CYS C 1 45  ? -11.956 40.307  0.313   1.00 20.77 ? 39  CYS C O     1 
ATOM   4871 C  CB    . CYS C 1 45  ? -11.515 42.823  1.844   1.00 20.88 ? 39  CYS C CB    1 
ATOM   4872 S  SG    . CYS C 1 45  ? -9.709  42.792  2.026   1.00 21.34 ? 39  CYS C SG    1 
ATOM   4873 N  N     . PHE C 1 46  ? -10.550 41.378  -1.139  1.00 18.22 ? 40  PHE C N     1 
ATOM   4874 C  CA    . PHE C 1 46  ? -9.965  40.123  -1.700  1.00 16.74 ? 40  PHE C CA    1 
ATOM   4875 C  C     . PHE C 1 46  ? -8.614  39.706  -1.114  1.00 16.99 ? 40  PHE C C     1 
ATOM   4876 O  O     . PHE C 1 46  ? -7.948  38.804  -1.704  1.00 19.00 ? 40  PHE C O     1 
ATOM   4877 C  CB    . PHE C 1 46  ? -9.914  40.157  -3.227  1.00 18.15 ? 40  PHE C CB    1 
ATOM   4878 C  CG    . PHE C 1 46  ? -9.016  41.151  -3.901  1.00 17.39 ? 40  PHE C CG    1 
ATOM   4879 C  CD1   . PHE C 1 46  ? -8.117  41.913  -3.188  1.00 16.68 ? 40  PHE C CD1   1 
ATOM   4880 C  CD2   . PHE C 1 46  ? -9.068  41.309  -5.287  1.00 18.27 ? 40  PHE C CD2   1 
ATOM   4881 C  CE1   . PHE C 1 46  ? -7.325  42.849  -3.844  1.00 18.25 ? 40  PHE C CE1   1 
ATOM   4882 C  CE2   . PHE C 1 46  ? -8.233  42.211  -5.934  1.00 18.40 ? 40  PHE C CE2   1 
ATOM   4883 C  CZ    . PHE C 1 46  ? -7.378  43.000  -5.193  1.00 18.50 ? 40  PHE C CZ    1 
ATOM   4884 N  N     . HIS C 1 47  ? -8.194  40.301  -0.014  1.00 18.52 ? 41  HIS C N     1 
ATOM   4885 C  CA    . HIS C 1 47  ? -6.923  39.905  0.644   1.00 18.89 ? 41  HIS C CA    1 
ATOM   4886 C  C     . HIS C 1 47  ? -7.130  40.038  2.149   1.00 20.10 ? 41  HIS C C     1 
ATOM   4887 O  O     . HIS C 1 47  ? -6.738  41.067  2.735   1.00 22.05 ? 41  HIS C O     1 
ATOM   4888 C  CB    . HIS C 1 47  ? -5.747  40.699  0.086   1.00 18.62 ? 41  HIS C CB    1 
ATOM   4889 C  CG    . HIS C 1 47  ? -4.472  39.984  0.362   1.00 17.83 ? 41  HIS C CG    1 
ATOM   4890 N  ND1   . HIS C 1 47  ? -3.987  39.010  -0.482  1.00 20.19 ? 41  HIS C ND1   1 
ATOM   4891 C  CD2   . HIS C 1 47  ? -3.654  40.021  1.430   1.00 19.12 ? 41  HIS C CD2   1 
ATOM   4892 C  CE1   . HIS C 1 47  ? -2.861  38.518  0.028   1.00 19.42 ? 41  HIS C CE1   1 
ATOM   4893 N  NE2   . HIS C 1 47  ? -2.637  39.117  1.211   1.00 19.34 ? 41  HIS C NE2   1 
ATOM   4894 N  N     . THR C 1 48  ? -7.813  39.049  2.706   1.00 18.82 ? 42  THR C N     1 
ATOM   4895 C  CA    . THR C 1 48  ? -8.497  39.129  4.021   1.00 19.81 ? 42  THR C CA    1 
ATOM   4896 C  C     . THR C 1 48  ? -7.563  38.728  5.174   1.00 20.81 ? 42  THR C C     1 
ATOM   4897 O  O     . THR C 1 48  ? -6.457  38.153  4.950   1.00 20.41 ? 42  THR C O     1 
ATOM   4898 C  CB    . THR C 1 48  ? -9.781  38.286  4.016   1.00 20.37 ? 42  THR C CB    1 
ATOM   4899 O  OG1   . THR C 1 48  ? -9.480  36.915  3.793   1.00 21.58 ? 42  THR C OG1   1 
ATOM   4900 C  CG2   . THR C 1 48  ? -10.781 38.783  2.991   1.00 22.19 ? 42  THR C CG2   1 
ATOM   4901 N  N     . ALA C 1 49  ? -8.004  39.034  6.390   1.00 21.46 ? 43  ALA C N     1 
ATOM   4902 C  CA    . ALA C 1 49  ? -7.210  38.892  7.638   1.00 22.76 ? 43  ALA C CA    1 
ATOM   4903 C  C     . ALA C 1 49  ? -7.250  37.438  8.117   1.00 23.99 ? 43  ALA C C     1 
ATOM   4904 O  O     . ALA C 1 49  ? -7.773  37.173  9.228   1.00 27.46 ? 43  ALA C O     1 
ATOM   4905 C  CB    . ALA C 1 49  ? -7.758  39.857  8.642   1.00 22.93 ? 43  ALA C CB    1 
ATOM   4906 N  N     . THR C 1 50  ? -6.684  36.515  7.345   1.00 24.04 ? 44  THR C N     1 
ATOM   4907 C  CA    . THR C 1 50  ? -6.711  35.067  7.669   1.00 27.51 ? 44  THR C CA    1 
ATOM   4908 C  C     . THR C 1 50  ? -5.536  34.671  8.587   1.00 29.61 ? 44  THR C C     1 
ATOM   4909 O  O     . THR C 1 50  ? -5.569  33.569  9.145   1.00 27.70 ? 44  THR C O     1 
ATOM   4910 C  CB    . THR C 1 50  ? -6.674  34.220  6.403   1.00 28.31 ? 44  THR C CB    1 
ATOM   4911 O  OG1   . THR C 1 50  ? -5.532  34.659  5.662   1.00 27.41 ? 44  THR C OG1   1 
ATOM   4912 C  CG2   . THR C 1 50  ? -7.942  34.338  5.583   1.00 29.53 ? 44  THR C CG2   1 
ATOM   4913 N  N     . THR C 1 51  ? -4.510  35.506  8.719   1.00 25.96 ? 45  THR C N     1 
ATOM   4914 C  CA    . THR C 1 51  ? -3.330  35.232  9.586   1.00 27.14 ? 45  THR C CA    1 
ATOM   4915 C  C     . THR C 1 51  ? -2.827  36.559  10.130  1.00 27.11 ? 45  THR C C     1 
ATOM   4916 O  O     . THR C 1 51  ? -3.141  37.590  9.531   1.00 29.41 ? 45  THR C O     1 
ATOM   4917 C  CB    . THR C 1 51  ? -2.166  34.492  8.887   1.00 27.57 ? 45  THR C CB    1 
ATOM   4918 O  OG1   . THR C 1 51  ? -1.421  35.472  8.150   1.00 32.33 ? 45  THR C OG1   1 
ATOM   4919 C  CG2   . THR C 1 51  ? -2.593  33.373  7.959   1.00 27.42 ? 45  THR C CG2   1 
ATOM   4920 N  N     . SER C 1 52  ? -2.062  36.521  11.221  1.00 26.52 ? 46  SER C N     1 
ATOM   4921 C  CA    . SER C 1 52  ? -1.338  37.693  11.764  1.00 28.09 ? 46  SER C CA    1 
ATOM   4922 C  C     . SER C 1 52  ? 0.183   37.553  11.544  1.00 26.01 ? 46  SER C C     1 
ATOM   4923 O  O     . SER C 1 52  ? 0.905   38.420  12.019  1.00 28.64 ? 46  SER C O     1 
ATOM   4924 C  CB    . SER C 1 52  ? -1.688  37.838  13.223  1.00 33.56 ? 46  SER C CB    1 
ATOM   4925 O  OG    . SER C 1 52  ? -1.431  36.597  13.859  1.00 33.58 ? 46  SER C OG    1 
ATOM   4926 N  N     . HIS C 1 53  ? 0.662   36.531  10.831  1.00 23.78 ? 47  HIS C N     1 
ATOM   4927 C  CA    . HIS C 1 53  ? 2.102   36.327  10.560  1.00 22.70 ? 47  HIS C CA    1 
ATOM   4928 C  C     . HIS C 1 53  ? 2.679   37.494  9.762   1.00 24.41 ? 47  HIS C C     1 
ATOM   4929 O  O     . HIS C 1 53  ? 2.108   37.900  8.715   1.00 22.25 ? 47  HIS C O     1 
ATOM   4930 C  CB    . HIS C 1 53  ? 2.391   35.029  9.837   1.00 24.61 ? 47  HIS C CB    1 
ATOM   4931 C  CG    . HIS C 1 53  ? 3.830   34.889  9.455   1.00 27.53 ? 47  HIS C CG    1 
ATOM   4932 N  ND1   . HIS C 1 53  ? 4.792   34.457  10.353  1.00 27.92 ? 47  HIS C ND1   1 
ATOM   4933 C  CD2   . HIS C 1 53  ? 4.488   35.166  8.297   1.00 26.26 ? 47  HIS C CD2   1 
ATOM   4934 C  CE1   . HIS C 1 53  ? 5.968   34.421  9.739   1.00 28.81 ? 47  HIS C CE1   1 
ATOM   4935 N  NE2   . HIS C 1 53  ? 5.810   34.847  8.474   1.00 28.20 ? 47  HIS C NE2   1 
ATOM   4936 N  N     . VAL C 1 54  ? 3.834   37.964  10.203  1.00 21.60 ? 48  VAL C N     1 
ATOM   4937 C  CA    . VAL C 1 54  ? 4.650   38.965  9.469   1.00 21.73 ? 48  VAL C CA    1 
ATOM   4938 C  C     . VAL C 1 54  ? 6.103   38.501  9.592   1.00 22.81 ? 48  VAL C C     1 
ATOM   4939 O  O     . VAL C 1 54  ? 6.526   38.152  10.716  1.00 22.52 ? 48  VAL C O     1 
ATOM   4940 C  CB    . VAL C 1 54  ? 4.465   40.395  10.004  1.00 23.06 ? 48  VAL C CB    1 
ATOM   4941 C  CG1   . VAL C 1 54  ? 5.277   41.373  9.166   1.00 26.01 ? 48  VAL C CG1   1 
ATOM   4942 C  CG2   . VAL C 1 54  ? 3.007   40.832  10.090  1.00 23.48 ? 48  VAL C CG2   1 
ATOM   4943 N  N     . GLU C 1 55  ? 6.842   38.524  8.497   1.00 23.66 ? 49  GLU C N     1 
ATOM   4944 C  CA    . GLU C 1 55  ? 8.267   38.136  8.496   1.00 24.20 ? 49  GLU C CA    1 
ATOM   4945 C  C     . GLU C 1 55  ? 9.010   39.052  9.472   1.00 26.99 ? 49  GLU C C     1 
ATOM   4946 O  O     . GLU C 1 55  ? 8.722   40.264  9.496   1.00 24.44 ? 49  GLU C O     1 
ATOM   4947 C  CB    . GLU C 1 55  ? 8.853   38.185  7.086   1.00 26.19 ? 49  GLU C CB    1 
ATOM   4948 C  CG    . GLU C 1 55  ? 8.379   37.040  6.181   1.00 29.72 ? 49  GLU C CG    1 
ATOM   4949 C  CD    . GLU C 1 55  ? 8.845   35.673  6.638   1.00 35.27 ? 49  GLU C CD    1 
ATOM   4950 O  OE1   . GLU C 1 55  ? 10.050  35.558  6.940   1.00 31.70 ? 49  GLU C OE1   1 
ATOM   4951 O  OE2   . GLU C 1 55  ? 8.003   34.744  6.754   1.00 35.21 ? 49  GLU C OE2   1 
ATOM   4952 N  N     . LYS C 1 56  ? 10.010  38.501  10.161  1.00 26.69 ? 50  LYS C N     1 
ATOM   4953 C  CA    . LYS C 1 56  ? 11.042  39.334  10.838  1.00 33.61 ? 50  LYS C CA    1 
ATOM   4954 C  C     . LYS C 1 56  ? 11.709  40.249  9.817   1.00 29.15 ? 50  LYS C C     1 
ATOM   4955 O  O     . LYS C 1 56  ? 12.009  39.839  8.694   1.00 26.34 ? 50  LYS C O     1 
ATOM   4956 C  CB    . LYS C 1 56  ? 12.147  38.469  11.439  1.00 37.15 ? 50  LYS C CB    1 
ATOM   4957 C  CG    . LYS C 1 56  ? 11.688  37.387  12.398  1.00 45.93 ? 50  LYS C CG    1 
ATOM   4958 C  CD    . LYS C 1 56  ? 12.854  36.619  12.988  1.00 50.83 ? 50  LYS C CD    1 
ATOM   4959 C  CE    . LYS C 1 56  ? 12.437  35.710  14.127  1.00 57.43 ? 50  LYS C CE    1 
ATOM   4960 N  NZ    . LYS C 1 56  ? 11.488  36.386  15.053  1.00 57.80 ? 50  LYS C NZ    1 
ATOM   4961 N  N     . PRO C 1 57  ? 12.024  41.500  10.178  1.00 29.43 ? 51  PRO C N     1 
ATOM   4962 C  CA    . PRO C 1 57  ? 12.641  42.421  9.225   1.00 32.14 ? 51  PRO C CA    1 
ATOM   4963 C  C     . PRO C 1 57  ? 13.892  41.838  8.539   1.00 28.74 ? 51  PRO C C     1 
ATOM   4964 O  O     . PRO C 1 57  ? 14.021  42.010  7.360   1.00 25.25 ? 51  PRO C O     1 
ATOM   4965 C  CB    . PRO C 1 57  ? 12.991  43.685  10.032  1.00 33.53 ? 51  PRO C CB    1 
ATOM   4966 C  CG    . PRO C 1 57  ? 12.423  43.459  11.433  1.00 34.88 ? 51  PRO C CG    1 
ATOM   4967 C  CD    . PRO C 1 57  ? 11.729  42.114  11.477  1.00 33.11 ? 51  PRO C CD    1 
ATOM   4968 N  N     . GLU C 1 58  ? 14.794  41.175  9.271   1.00 29.52 ? 52  GLU C N     1 
ATOM   4969 C  CA    . GLU C 1 58  ? 16.009  40.560  8.673   1.00 28.40 ? 52  GLU C CA    1 
ATOM   4970 C  C     . GLU C 1 58  ? 15.588  39.593  7.554   1.00 27.86 ? 52  GLU C C     1 
ATOM   4971 O  O     . GLU C 1 58  ? 16.279  39.516  6.506   1.00 26.68 ? 52  GLU C O     1 
ATOM   4972 C  CB    . GLU C 1 58  ? 16.898  39.843  9.704   1.00 33.29 ? 52  GLU C CB    1 
ATOM   4973 C  CG    . GLU C 1 58  ? 16.155  38.945  10.680  1.00 41.11 ? 52  GLU C CG    1 
ATOM   4974 C  CD    . GLU C 1 58  ? 15.769  39.558  12.036  1.00 50.27 ? 52  GLU C CD    1 
ATOM   4975 O  OE1   . GLU C 1 58  ? 15.102  40.651  12.084  1.00 42.66 ? 52  GLU C OE1   1 
ATOM   4976 O  OE2   . GLU C 1 58  ? 16.150  38.948  13.066  1.00 56.25 ? 52  GLU C OE2   1 
ATOM   4977 N  N     . ASN C 1 59  ? 14.507  38.853  7.730   1.00 27.38 ? 53  ASN C N     1 
ATOM   4978 C  CA    . ASN C 1 59  ? 14.095  37.830  6.735   1.00 25.81 ? 53  ASN C CA    1 
ATOM   4979 C  C     . ASN C 1 59  ? 13.414  38.525  5.549   1.00 23.52 ? 53  ASN C C     1 
ATOM   4980 O  O     . ASN C 1 59  ? 13.645  38.123  4.370   1.00 23.87 ? 53  ASN C O     1 
ATOM   4981 C  CB    . ASN C 1 59  ? 13.238  36.749  7.381   1.00 29.74 ? 53  ASN C CB    1 
ATOM   4982 C  CG    . ASN C 1 59  ? 14.036  35.902  8.359   1.00 33.51 ? 53  ASN C CG    1 
ATOM   4983 O  OD1   . ASN C 1 59  ? 15.260  35.850  8.286   1.00 35.90 ? 53  ASN C OD1   1 
ATOM   4984 N  ND2   . ASN C 1 59  ? 13.357  35.270  9.290   1.00 36.09 ? 53  ASN C ND2   1 
ATOM   4985 N  N     . ALA C 1 60  ? 12.565  39.502  5.808   1.00 22.33 ? 54  ALA C N     1 
ATOM   4986 C  CA    . ALA C 1 60  ? 11.973  40.304  4.723   1.00 22.62 ? 54  ALA C CA    1 
ATOM   4987 C  C     . ALA C 1 60  ? 13.113  40.924  3.894   1.00 23.41 ? 54  ALA C C     1 
ATOM   4988 O  O     . ALA C 1 60  ? 13.038  40.919  2.651   1.00 21.09 ? 54  ALA C O     1 
ATOM   4989 C  CB    . ALA C 1 60  ? 11.042  41.341  5.291   1.00 22.65 ? 54  ALA C CB    1 
ATOM   4990 N  N     . LYS C 1 61  ? 14.157  41.440  4.549   1.00 23.14 ? 55  LYS C N     1 
ATOM   4991 C  CA    . LYS C 1 61  ? 15.311  42.032  3.826   1.00 25.30 ? 55  LYS C CA    1 
ATOM   4992 C  C     . LYS C 1 61  ? 15.982  40.965  2.944   1.00 22.67 ? 55  LYS C C     1 
ATOM   4993 O  O     . LYS C 1 61  ? 16.389  41.302  1.798   1.00 24.95 ? 55  LYS C O     1 
ATOM   4994 C  CB    . LYS C 1 61  ? 16.322  42.655  4.802   1.00 25.87 ? 55  LYS C CB    1 
ATOM   4995 C  CG    . LYS C 1 61  ? 15.924  43.999  5.356   1.00 29.13 ? 55  LYS C CG    1 
ATOM   4996 C  CD    . LYS C 1 61  ? 16.915  44.498  6.381   1.00 36.90 ? 55  LYS C CD    1 
ATOM   4997 C  CE    . LYS C 1 61  ? 16.622  45.927  6.769   1.00 44.42 ? 55  LYS C CE    1 
ATOM   4998 N  NZ    . LYS C 1 61  ? 17.000  46.207  8.175   1.00 47.99 ? 55  LYS C NZ    1 
ATOM   4999 N  N     . ARG C 1 62  ? 16.136  39.742  3.436   1.00 24.54 ? 56  ARG C N     1 
ATOM   5000 C  CA    . ARG C 1 62  ? 16.735  38.630  2.664   1.00 23.22 ? 56  ARG C CA    1 
ATOM   5001 C  C     . ARG C 1 62  ? 15.908  38.463  1.386   1.00 22.59 ? 56  ARG C C     1 
ATOM   5002 O  O     . ARG C 1 62  ? 16.484  38.368  0.284   1.00 24.31 ? 56  ARG C O     1 
ATOM   5003 C  CB    . ARG C 1 62  ? 16.794  37.345  3.498   1.00 26.18 ? 56  ARG C CB    1 
ATOM   5004 C  CG    . ARG C 1 62  ? 17.958  37.273  4.476   1.00 29.95 ? 56  ARG C CG    1 
ATOM   5005 C  CD    . ARG C 1 62  ? 17.918  36.028  5.385   1.00 33.68 ? 56  ARG C CD    1 
ATOM   5006 N  NE    . ARG C 1 62  ? 17.421  34.843  4.666   1.00 40.80 ? 56  ARG C NE    1 
ATOM   5007 C  CZ    . ARG C 1 62  ? 16.375  34.078  5.029   1.00 45.27 ? 56  ARG C CZ    1 
ATOM   5008 N  NH1   . ARG C 1 62  ? 15.695  34.330  6.141   1.00 50.27 ? 56  ARG C NH1   1 
ATOM   5009 N  NH2   . ARG C 1 62  ? 16.025  33.040  4.292   1.00 38.29 ? 56  ARG C NH2   1 
ATOM   5010 N  N     . GLY C 1 63  ? 14.580  38.434  1.510   1.00 20.96 ? 57  GLY C N     1 
ATOM   5011 C  CA    . GLY C 1 63  ? 13.705  38.196  0.359   1.00 21.53 ? 57  GLY C CA    1 
ATOM   5012 C  C     . GLY C 1 63  ? 13.776  39.322  -0.667  1.00 21.50 ? 57  GLY C C     1 
ATOM   5013 O  O     . GLY C 1 63  ? 13.830  39.016  -1.876  1.00 22.68 ? 57  GLY C O     1 
ATOM   5014 N  N     . LEU C 1 64  ? 13.690  40.572  -0.213  1.00 20.85 ? 58  LEU C N     1 
ATOM   5015 C  CA    . LEU C 1 64  ? 13.710  41.749  -1.094  1.00 21.35 ? 58  LEU C CA    1 
ATOM   5016 C  C     . LEU C 1 64  ? 15.066  41.778  -1.819  1.00 22.14 ? 58  LEU C C     1 
ATOM   5017 O  O     . LEU C 1 64  ? 15.091  42.075  -3.004  1.00 23.77 ? 58  LEU C O     1 
ATOM   5018 C  CB    . LEU C 1 64  ? 13.430  43.012  -0.274  1.00 24.10 ? 58  LEU C CB    1 
ATOM   5019 C  CG    . LEU C 1 64  ? 12.023  43.140  0.324   1.00 24.57 ? 58  LEU C CG    1 
ATOM   5020 C  CD1   . LEU C 1 64  ? 11.991  44.216  1.392   1.00 23.70 ? 58  LEU C CD1   1 
ATOM   5021 C  CD2   . LEU C 1 64  ? 10.987  43.446  -0.727  1.00 27.83 ? 58  LEU C CD2   1 
ATOM   5022 N  N     . THR C 1 65  ? 16.146  41.362  -1.156  1.00 23.66 ? 59  THR C N     1 
ATOM   5023 C  CA    . THR C 1 65  ? 17.475  41.263  -1.793  1.00 26.52 ? 59  THR C CA    1 
ATOM   5024 C  C     . THR C 1 65  ? 17.408  40.247  -2.937  1.00 23.17 ? 59  THR C C     1 
ATOM   5025 O  O     . THR C 1 65  ? 17.917  40.567  -4.009  1.00 22.67 ? 59  THR C O     1 
ATOM   5026 C  CB    . THR C 1 65  ? 18.571  40.942  -0.771  1.00 26.93 ? 59  THR C CB    1 
ATOM   5027 O  OG1   . THR C 1 65  ? 18.581  42.033  0.146   1.00 26.23 ? 59  THR C OG1   1 
ATOM   5028 C  CG2   . THR C 1 65  ? 19.950  40.804  -1.390  1.00 29.52 ? 59  THR C CG2   1 
ATOM   5029 N  N     . LEU C 1 66  ? 16.808  39.076  -2.717  1.00 22.37 ? 60  LEU C N     1 
ATOM   5030 C  CA    . LEU C 1 66  ? 16.713  38.045  -3.792  1.00 21.65 ? 60  LEU C CA    1 
ATOM   5031 C  C     . LEU C 1 66  ? 15.935  38.621  -4.993  1.00 23.72 ? 60  LEU C C     1 
ATOM   5032 O  O     . LEU C 1 66  ? 16.297  38.356  -6.125  1.00 22.46 ? 60  LEU C O     1 
ATOM   5033 C  CB    . LEU C 1 66  ? 16.003  36.798  -3.269  1.00 22.22 ? 60  LEU C CB    1 
ATOM   5034 C  CG    . LEU C 1 66  ? 16.667  36.037  -2.128  1.00 23.16 ? 60  LEU C CG    1 
ATOM   5035 C  CD1   . LEU C 1 66  ? 15.834  34.812  -1.764  1.00 23.81 ? 60  LEU C CD1   1 
ATOM   5036 C  CD2   . LEU C 1 66  ? 18.102  35.622  -2.455  1.00 23.28 ? 60  LEU C CD2   1 
ATOM   5037 N  N     . LEU C 1 67  ? 14.880  39.400  -4.743  1.00 22.75 ? 61  LEU C N     1 
ATOM   5038 C  CA    . LEU C 1 67  ? 14.034  39.959  -5.807  1.00 23.33 ? 61  LEU C CA    1 
ATOM   5039 C  C     . LEU C 1 67  ? 14.835  41.002  -6.597  1.00 23.52 ? 61  LEU C C     1 
ATOM   5040 O  O     . LEU C 1 67  ? 14.742  40.981  -7.838  1.00 23.21 ? 61  LEU C O     1 
ATOM   5041 C  CB    . LEU C 1 67  ? 12.757  40.569  -5.210  1.00 21.95 ? 61  LEU C CB    1 
ATOM   5042 C  CG    . LEU C 1 67  ? 11.758  39.556  -4.644  1.00 22.29 ? 61  LEU C CG    1 
ATOM   5043 C  CD1   . LEU C 1 67  ? 10.783  40.259  -3.725  1.00 24.49 ? 61  LEU C CD1   1 
ATOM   5044 C  CD2   . LEU C 1 67  ? 11.023  38.844  -5.759  1.00 24.09 ? 61  LEU C CD2   1 
ATOM   5045 N  N     . LYS C 1 68  ? 15.560  41.892  -5.918  1.00 22.21 ? 62  LYS C N     1 
ATOM   5046 C  CA    . LYS C 1 68  ? 16.435  42.865  -6.582  1.00 23.49 ? 62  LYS C CA    1 
ATOM   5047 C  C     . LYS C 1 68  ? 17.402  42.104  -7.517  1.00 23.62 ? 62  LYS C C     1 
ATOM   5048 O  O     . LYS C 1 68  ? 17.537  42.521  -8.675  1.00 24.71 ? 62  LYS C O     1 
ATOM   5049 C  CB    . LYS C 1 68  ? 17.209  43.695  -5.562  1.00 27.36 ? 62  LYS C CB    1 
ATOM   5050 C  CG    . LYS C 1 68  ? 18.379  44.468  -6.181  1.00 28.81 ? 62  LYS C CG    1 
ATOM   5051 C  CD    . LYS C 1 68  ? 17.945  45.569  -7.119  1.00 29.75 ? 62  LYS C CD    1 
ATOM   5052 C  CE    . LYS C 1 68  ? 19.130  46.311  -7.722  1.00 30.47 ? 62  LYS C CE    1 
ATOM   5053 N  NZ    . LYS C 1 68  ? 18.766  47.741  -7.930  1.00 32.40 ? 62  LYS C NZ    1 
ATOM   5054 N  N     . GLN C 1 69  ? 18.067  41.054  -7.025  1.00 24.82 ? 63  GLN C N     1 
ATOM   5055 C  CA    . GLN C 1 69  ? 19.038  40.222  -7.806  1.00 28.20 ? 63  GLN C CA    1 
ATOM   5056 C  C     . GLN C 1 69  ? 18.323  39.664  -9.044  1.00 30.41 ? 63  GLN C C     1 
ATOM   5057 O  O     . GLN C 1 69  ? 18.967  39.589  -10.114 1.00 29.45 ? 63  GLN C O     1 
ATOM   5058 C  CB    . GLN C 1 69  ? 19.607  39.054  -6.990  1.00 31.32 ? 63  GLN C CB    1 
ATOM   5059 C  CG    . GLN C 1 69  ? 20.525  39.392  -5.808  1.00 38.97 ? 63  GLN C CG    1 
ATOM   5060 C  CD    . GLN C 1 69  ? 20.874  38.199  -4.915  1.00 46.30 ? 63  GLN C CD    1 
ATOM   5061 O  OE1   . GLN C 1 69  ? 20.741  37.006  -5.285  1.00 44.59 ? 63  GLN C OE1   1 
ATOM   5062 N  NE2   . GLN C 1 69  ? 21.348  38.502  -3.705  1.00 40.25 ? 63  GLN C NE2   1 
ATOM   5063 N  N     . ALA C 1 70  ? 17.038  39.280  -8.921  1.00 24.97 ? 64  ALA C N     1 
ATOM   5064 C  CA    . ALA C 1 70  ? 16.242  38.656  -9.995  1.00 25.03 ? 64  ALA C CA    1 
ATOM   5065 C  C     . ALA C 1 70  ? 15.723  39.682  -11.001 1.00 23.85 ? 64  ALA C C     1 
ATOM   5066 O  O     . ALA C 1 70  ? 15.210  39.236  -12.057 1.00 28.19 ? 64  ALA C O     1 
ATOM   5067 C  CB    . ALA C 1 70  ? 15.119  37.833  -9.435  1.00 23.15 ? 64  ALA C CB    1 
ATOM   5068 N  N     . GLY C 1 71  ? 15.889  40.981  -10.749 1.00 24.42 ? 65  GLY C N     1 
ATOM   5069 C  CA    . GLY C 1 71  ? 15.566  42.029  -11.740 1.00 24.79 ? 65  GLY C CA    1 
ATOM   5070 C  C     . GLY C 1 71  ? 14.398  42.920  -11.332 1.00 23.74 ? 65  GLY C C     1 
ATOM   5071 O  O     . GLY C 1 71  ? 13.911  43.707  -12.170 1.00 23.55 ? 65  GLY C O     1 
ATOM   5072 N  N     . MET C 1 72  ? 13.951  42.849  -10.082 1.00 24.10 ? 66  MET C N     1 
ATOM   5073 C  CA    . MET C 1 72  ? 12.862  43.734  -9.610  1.00 20.51 ? 66  MET C CA    1 
ATOM   5074 C  C     . MET C 1 72  ? 13.326  45.174  -9.710  1.00 21.26 ? 66  MET C C     1 
ATOM   5075 O  O     . MET C 1 72  ? 14.470  45.482  -9.256  1.00 20.66 ? 66  MET C O     1 
ATOM   5076 C  CB    . MET C 1 72  ? 12.490  43.441  -8.164  1.00 22.90 ? 66  MET C CB    1 
ATOM   5077 C  CG    . MET C 1 72  ? 11.280  44.190  -7.696  1.00 24.05 ? 66  MET C CG    1 
ATOM   5078 S  SD    . MET C 1 72  ? 10.807  43.724  -5.989  1.00 24.05 ? 66  MET C SD    1 
ATOM   5079 C  CE    . MET C 1 72  ? 12.266  44.203  -5.053  1.00 23.29 ? 66  MET C CE    1 
ATOM   5080 N  N     . LYS C 1 73  ? 12.454  46.027  -10.243 1.00 20.49 ? 67  LYS C N     1 
ATOM   5081 C  CA    . LYS C 1 73  ? 12.671  47.482  -10.313 1.00 21.14 ? 67  LYS C CA    1 
ATOM   5082 C  C     . LYS C 1 73  ? 11.702  48.238  -9.414  1.00 21.50 ? 67  LYS C C     1 
ATOM   5083 O  O     . LYS C 1 73  ? 12.077  49.296  -8.940  1.00 19.25 ? 67  LYS C O     1 
ATOM   5084 C  CB    . LYS C 1 73  ? 12.502  47.928  -11.758 1.00 26.16 ? 67  LYS C CB    1 
ATOM   5085 C  CG    . LYS C 1 73  ? 13.618  47.456  -12.675 1.00 29.39 ? 67  LYS C CG    1 
ATOM   5086 C  CD    . LYS C 1 73  ? 13.433  47.935  -14.092 1.00 33.63 ? 67  LYS C CD    1 
ATOM   5087 C  CE    . LYS C 1 73  ? 14.461  47.310  -15.010 1.00 41.26 ? 67  LYS C CE    1 
ATOM   5088 N  NZ    . LYS C 1 73  ? 14.990  48.305  -15.963 1.00 48.13 ? 67  LYS C NZ    1 
ATOM   5089 N  N     . LYS C 1 74  ? 10.467  47.753  -9.242  1.00 18.19 ? 68  LYS C N     1 
ATOM   5090 C  CA    . LYS C 1 74  ? 9.466   48.416  -8.400  1.00 17.70 ? 68  LYS C CA    1 
ATOM   5091 C  C     . LYS C 1 74  ? 8.928   47.425  -7.365  1.00 17.65 ? 68  LYS C C     1 
ATOM   5092 O  O     . LYS C 1 74  ? 8.658   46.262  -7.740  1.00 18.58 ? 68  LYS C O     1 
ATOM   5093 C  CB    . LYS C 1 74  ? 8.303   48.909  -9.254  1.00 18.84 ? 68  LYS C CB    1 
ATOM   5094 C  CG    . LYS C 1 74  ? 7.137   49.527  -8.492  1.00 18.38 ? 68  LYS C CG    1 
ATOM   5095 C  CD    . LYS C 1 74  ? 6.209   50.302  -9.390  1.00 19.73 ? 68  LYS C CD    1 
ATOM   5096 C  CE    . LYS C 1 74  ? 5.130   51.007  -8.586  1.00 21.12 ? 68  LYS C CE    1 
ATOM   5097 N  NZ    . LYS C 1 74  ? 4.089   50.047  -8.144  1.00 21.37 ? 68  LYS C NZ    1 
ATOM   5098 N  N     . ILE C 1 75  ? 8.774   47.897  -6.136  1.00 18.39 ? 69  ILE C N     1 
ATOM   5099 C  CA    . ILE C 1 75  ? 8.126   47.155  -5.011  1.00 18.53 ? 69  ILE C CA    1 
ATOM   5100 C  C     . ILE C 1 75  ? 6.944   47.994  -4.536  1.00 19.33 ? 69  ILE C C     1 
ATOM   5101 O  O     . ILE C 1 75  ? 7.115   49.211  -4.314  1.00 18.96 ? 69  ILE C O     1 
ATOM   5102 C  CB    . ILE C 1 75  ? 9.113   46.829  -3.862  1.00 19.73 ? 69  ILE C CB    1 
ATOM   5103 C  CG1   . ILE C 1 75  ? 8.453   46.017  -2.743  1.00 23.03 ? 69  ILE C CG1   1 
ATOM   5104 C  CG2   . ILE C 1 75  ? 9.761   48.077  -3.289  1.00 22.27 ? 69  ILE C CG2   1 
ATOM   5105 C  CD1   . ILE C 1 75  ? 8.377   44.566  -3.053  1.00 25.95 ? 69  ILE C CD1   1 
ATOM   5106 N  N     . ASN C 1 76  ? 5.781   47.362  -4.373  1.00 16.80 ? 70  ASN C N     1 
ATOM   5107 C  CA    . ASN C 1 76  ? 4.587   47.965  -3.772  1.00 17.42 ? 70  ASN C CA    1 
ATOM   5108 C  C     . ASN C 1 76  ? 4.330   47.242  -2.449  1.00 17.90 ? 70  ASN C C     1 
ATOM   5109 O  O     . ASN C 1 76  ? 4.176   45.994  -2.463  1.00 18.60 ? 70  ASN C O     1 
ATOM   5110 C  CB    . ASN C 1 76  ? 3.392   47.885  -4.727  1.00 19.11 ? 70  ASN C CB    1 
ATOM   5111 C  CG    . ASN C 1 76  ? 2.221   48.680  -4.195  1.00 23.33 ? 70  ASN C CG    1 
ATOM   5112 O  OD1   . ASN C 1 76  ? 2.372   49.854  -3.853  1.00 22.95 ? 70  ASN C OD1   1 
ATOM   5113 N  ND2   . ASN C 1 76  ? 1.058   48.044  -4.143  1.00 21.94 ? 70  ASN C ND2   1 
ATOM   5114 N  N     . PHE C 1 77  ? 4.307   47.987  -1.338  1.00 18.58 ? 71  PHE C N     1 
ATOM   5115 C  CA    . PHE C 1 77  ? 3.922   47.459  -0.013  1.00 17.97 ? 71  PHE C CA    1 
ATOM   5116 C  C     . PHE C 1 77  ? 2.414   47.542  0.101   1.00 19.29 ? 71  PHE C C     1 
ATOM   5117 O  O     . PHE C 1 77  ? 1.855   48.627  0.021   1.00 20.05 ? 71  PHE C O     1 
ATOM   5118 C  CB    . PHE C 1 77  ? 4.686   48.197  1.084   1.00 20.56 ? 71  PHE C CB    1 
ATOM   5119 C  CG    . PHE C 1 77  ? 6.165   47.918  1.032   1.00 19.82 ? 71  PHE C CG    1 
ATOM   5120 C  CD1   . PHE C 1 77  ? 6.689   46.789  1.642   1.00 22.73 ? 71  PHE C CD1   1 
ATOM   5121 C  CD2   . PHE C 1 77  ? 7.035   48.780  0.389   1.00 22.78 ? 71  PHE C CD2   1 
ATOM   5122 C  CE1   . PHE C 1 77  ? 8.043   46.509  1.566   1.00 23.43 ? 71  PHE C CE1   1 
ATOM   5123 C  CE2   . PHE C 1 77  ? 8.396   48.525  0.358   1.00 20.48 ? 71  PHE C CE2   1 
ATOM   5124 C  CZ    . PHE C 1 77  ? 8.890   47.385  0.925   1.00 24.97 ? 71  PHE C CZ    1 
ATOM   5125 N  N     . ALA C 1 78  ? 1.797   46.400  0.352   1.00 19.92 ? 72  ALA C N     1 
ATOM   5126 C  CA    . ALA C 1 78  ? 0.345   46.220  0.406   1.00 20.91 ? 72  ALA C CA    1 
ATOM   5127 C  C     . ALA C 1 78  ? 0.009   45.307  1.586   1.00 20.53 ? 72  ALA C C     1 
ATOM   5128 O  O     . ALA C 1 78  ? 0.866   45.061  2.402   1.00 20.98 ? 72  ALA C O     1 
ATOM   5129 C  CB    . ALA C 1 78  ? -0.134  45.687  -0.920  1.00 21.98 ? 72  ALA C CB    1 
ATOM   5130 N  N     . GLY C 1 79  ? -1.223  44.820  1.646   1.00 20.33 ? 73  GLY C N     1 
ATOM   5131 C  CA    . GLY C 1 79  ? -1.692  43.923  2.695   1.00 19.22 ? 73  GLY C CA    1 
ATOM   5132 C  C     . GLY C 1 79  ? -3.145  43.559  2.425   1.00 18.02 ? 73  GLY C C     1 
ATOM   5133 O  O     . GLY C 1 79  ? -3.489  43.303  1.275   1.00 18.12 ? 73  GLY C O     1 
ATOM   5134 N  N     . GLY C 1 80  ? -3.980  43.608  3.468   1.00 19.65 ? 74  GLY C N     1 
ATOM   5135 C  CA    . GLY C 1 80  ? -3.697  44.205  4.758   1.00 18.69 ? 74  GLY C CA    1 
ATOM   5136 C  C     . GLY C 1 80  ? -3.489  45.699  4.687   1.00 18.59 ? 74  GLY C C     1 
ATOM   5137 O  O     . GLY C 1 80  ? -3.450  46.253  3.581   1.00 20.23 ? 74  GLY C O     1 
ATOM   5138 N  N     . GLU C 1 81  ? -3.411  46.352  5.854   1.00 20.07 ? 75  GLU C N     1 
ATOM   5139 C  CA    . GLU C 1 81  ? -3.147  47.799  5.936   1.00 18.89 ? 75  GLU C CA    1 
ATOM   5140 C  C     . GLU C 1 81  ? -1.696  47.988  6.362   1.00 19.91 ? 75  GLU C C     1 
ATOM   5141 O  O     . GLU C 1 81  ? -1.342  47.695  7.524   1.00 19.18 ? 75  GLU C O     1 
ATOM   5142 C  CB    . GLU C 1 81  ? -4.113  48.492  6.897   1.00 19.94 ? 75  GLU C CB    1 
ATOM   5143 C  CG    . GLU C 1 81  ? -3.813  49.960  7.050   1.00 20.45 ? 75  GLU C CG    1 
ATOM   5144 C  CD    . GLU C 1 81  ? -3.568  50.728  5.764   1.00 21.75 ? 75  GLU C CD    1 
ATOM   5145 O  OE1   . GLU C 1 81  ? -4.395  50.593  4.806   1.00 24.85 ? 75  GLU C OE1   1 
ATOM   5146 O  OE2   . GLU C 1 81  ? -2.602  51.548  5.727   1.00 23.64 ? 75  GLU C OE2   1 
ATOM   5147 N  N     . PRO C 1 82  ? -0.835  48.465  5.439   1.00 20.34 ? 76  PRO C N     1 
ATOM   5148 C  CA    . PRO C 1 82  ? 0.589   48.606  5.725   1.00 20.70 ? 76  PRO C CA    1 
ATOM   5149 C  C     . PRO C 1 82  ? 0.889   49.523  6.918   1.00 20.42 ? 76  PRO C C     1 
ATOM   5150 O  O     . PRO C 1 82  ? 1.828   49.269  7.648   1.00 22.05 ? 76  PRO C O     1 
ATOM   5151 C  CB    . PRO C 1 82  ? 1.162   49.181  4.434   1.00 21.09 ? 76  PRO C CB    1 
ATOM   5152 C  CG    . PRO C 1 82  ? 0.234   48.641  3.367   1.00 24.30 ? 76  PRO C CG    1 
ATOM   5153 C  CD    . PRO C 1 82  ? -1.135  48.752  4.011   1.00 20.40 ? 76  PRO C CD    1 
ATOM   5154 N  N     . PHE C 1 83  ? 0.089   50.564  7.114   1.00 21.79 ? 77  PHE C N     1 
ATOM   5155 C  CA    . PHE C 1 83  ? 0.363   51.574  8.162   1.00 21.63 ? 77  PHE C CA    1 
ATOM   5156 C  C     . PHE C 1 83  ? -0.046  51.069  9.548   1.00 23.82 ? 77  PHE C C     1 
ATOM   5157 O  O     . PHE C 1 83  ? 0.167   51.845  10.527  1.00 24.16 ? 77  PHE C O     1 
ATOM   5158 C  CB    . PHE C 1 83  ? -0.287  52.908  7.768   1.00 22.44 ? 77  PHE C CB    1 
ATOM   5159 C  CG    . PHE C 1 83  ? 0.546   53.683  6.780   1.00 24.90 ? 77  PHE C CG    1 
ATOM   5160 C  CD1   . PHE C 1 83  ? 0.422   53.487  5.408   1.00 22.00 ? 77  PHE C CD1   1 
ATOM   5161 C  CD2   . PHE C 1 83  ? 1.538   54.547  7.243   1.00 24.70 ? 77  PHE C CD2   1 
ATOM   5162 C  CE1   . PHE C 1 83  ? 1.221   54.189  4.530   1.00 24.27 ? 77  PHE C CE1   1 
ATOM   5163 C  CE2   . PHE C 1 83  ? 2.322   55.262  6.351   1.00 28.39 ? 77  PHE C CE2   1 
ATOM   5164 C  CZ    . PHE C 1 83  ? 2.178   55.064  4.998   1.00 25.12 ? 77  PHE C CZ    1 
ATOM   5165 N  N     . LEU C 1 84  ? -0.531  49.822  9.693   1.00 21.59 ? 78  LEU C N     1 
ATOM   5166 C  CA    . LEU C 1 84  ? -0.554  49.145  11.013  1.00 22.45 ? 78  LEU C CA    1 
ATOM   5167 C  C     . LEU C 1 84  ? 0.868   48.806  11.485  1.00 23.01 ? 78  LEU C C     1 
ATOM   5168 O  O     . LEU C 1 84  ? 1.026   48.465  12.673  1.00 21.12 ? 78  LEU C O     1 
ATOM   5169 C  CB    . LEU C 1 84  ? -1.414  47.894  10.960  1.00 23.59 ? 78  LEU C CB    1 
ATOM   5170 C  CG    . LEU C 1 84  ? -2.905  48.209  10.999  1.00 25.81 ? 78  LEU C CG    1 
ATOM   5171 C  CD1   . LEU C 1 84  ? -3.701  46.965  10.648  1.00 28.48 ? 78  LEU C CD1   1 
ATOM   5172 C  CD2   . LEU C 1 84  ? -3.314  48.731  12.371  1.00 28.85 ? 78  LEU C CD2   1 
ATOM   5173 N  N     . TYR C 1 85  ? 1.863   48.868  10.596  1.00 21.50 ? 79  TYR C N     1 
ATOM   5174 C  CA    . TYR C 1 85  ? 3.254   48.435  10.897  1.00 21.31 ? 79  TYR C CA    1 
ATOM   5175 C  C     . TYR C 1 85  ? 4.256   49.476  10.432  1.00 21.38 ? 79  TYR C C     1 
ATOM   5176 O  O     . TYR C 1 85  ? 5.101   49.161  9.592   1.00 19.90 ? 79  TYR C O     1 
ATOM   5177 C  CB    . TYR C 1 85  ? 3.561   47.120  10.196  1.00 22.27 ? 79  TYR C CB    1 
ATOM   5178 C  CG    . TYR C 1 85  ? 2.728   45.951  10.641  1.00 24.07 ? 79  TYR C CG    1 
ATOM   5179 C  CD1   . TYR C 1 85  ? 1.482   45.693  10.081  1.00 24.75 ? 79  TYR C CD1   1 
ATOM   5180 C  CD2   . TYR C 1 85  ? 3.201   45.082  11.600  1.00 24.30 ? 79  TYR C CD2   1 
ATOM   5181 C  CE1   . TYR C 1 85  ? 0.730   44.603  10.493  1.00 26.98 ? 79  TYR C CE1   1 
ATOM   5182 C  CE2   . TYR C 1 85  ? 2.468   43.979  12.017  1.00 30.46 ? 79  TYR C CE2   1 
ATOM   5183 C  CZ    . TYR C 1 85  ? 1.220   43.742  11.457  1.00 31.39 ? 79  TYR C CZ    1 
ATOM   5184 O  OH    . TYR C 1 85  ? 0.471   42.664  11.843  1.00 32.61 ? 79  TYR C OH    1 
ATOM   5185 N  N     . PRO C 1 86  ? 4.220   50.715  10.958  1.00 20.66 ? 80  PRO C N     1 
ATOM   5186 C  CA    . PRO C 1 86  ? 5.114   51.767  10.476  1.00 22.39 ? 80  PRO C CA    1 
ATOM   5187 C  C     . PRO C 1 86  ? 6.603   51.554  10.780  1.00 22.93 ? 80  PRO C C     1 
ATOM   5188 O  O     . PRO C 1 86  ? 7.408   52.071  10.022  1.00 22.52 ? 80  PRO C O     1 
ATOM   5189 C  CB    . PRO C 1 86  ? 4.632   53.051  11.163  1.00 21.16 ? 80  PRO C CB    1 
ATOM   5190 C  CG    . PRO C 1 86  ? 3.880   52.569  12.363  1.00 21.49 ? 80  PRO C CG    1 
ATOM   5191 C  CD    . PRO C 1 86  ? 3.296   51.222  11.995  1.00 21.00 ? 80  PRO C CD    1 
ATOM   5192 N  N     . LYS C 1 87  ? 6.954   50.769  11.805  1.00 22.27 ? 81  LYS C N     1 
ATOM   5193 C  CA    . LYS C 1 87  ? 8.390   50.463  12.062  1.00 22.78 ? 81  LYS C CA    1 
ATOM   5194 C  C     . LYS C 1 87  ? 8.873   49.491  10.966  1.00 22.87 ? 81  LYS C C     1 
ATOM   5195 O  O     . LYS C 1 87  ? 9.897   49.763  10.327  1.00 22.40 ? 81  LYS C O     1 
ATOM   5196 C  CB    . LYS C 1 87  ? 8.636   49.903  13.463  1.00 22.86 ? 81  LYS C CB    1 
ATOM   5197 C  CG    . LYS C 1 87  ? 10.110  49.856  13.813  1.00 26.41 ? 81  LYS C CG    1 
ATOM   5198 C  CD    . LYS C 1 87  ? 10.393  49.405  15.209  1.00 30.01 ? 81  LYS C CD    1 
ATOM   5199 C  CE    . LYS C 1 87  ? 11.879  49.384  15.514  1.00 30.88 ? 81  LYS C CE    1 
ATOM   5200 N  NZ    . LYS C 1 87  ? 12.517  50.690  15.183  1.00 33.49 ? 81  LYS C NZ    1 
ATOM   5201 N  N     . PHE C 1 88  ? 8.154   48.398  10.729  1.00 21.04 ? 82  PHE C N     1 
ATOM   5202 C  CA    . PHE C 1 88  ? 8.523   47.413  9.675   1.00 22.09 ? 82  PHE C CA    1 
ATOM   5203 C  C     . PHE C 1 88  ? 8.541   48.148  8.337   1.00 20.18 ? 82  PHE C C     1 
ATOM   5204 O  O     . PHE C 1 88  ? 9.494   47.983  7.523   1.00 20.09 ? 82  PHE C O     1 
ATOM   5205 C  CB    . PHE C 1 88  ? 7.524   46.249  9.626   1.00 21.97 ? 82  PHE C CB    1 
ATOM   5206 C  CG    . PHE C 1 88  ? 7.791   45.218  8.548   1.00 21.94 ? 82  PHE C CG    1 
ATOM   5207 C  CD1   . PHE C 1 88  ? 7.252   45.361  7.276   1.00 24.04 ? 82  PHE C CD1   1 
ATOM   5208 C  CD2   . PHE C 1 88  ? 8.552   44.089  8.813   1.00 26.27 ? 82  PHE C CD2   1 
ATOM   5209 C  CE1   . PHE C 1 88  ? 7.489   44.427  6.288   1.00 24.67 ? 82  PHE C CE1   1 
ATOM   5210 C  CE2   . PHE C 1 88  ? 8.778   43.142  7.817   1.00 25.93 ? 82  PHE C CE2   1 
ATOM   5211 C  CZ    . PHE C 1 88  ? 8.229   43.305  6.565   1.00 23.86 ? 82  PHE C CZ    1 
ATOM   5212 N  N     . LEU C 1 89  ? 7.482   48.917  8.071   1.00 21.25 ? 83  LEU C N     1 
ATOM   5213 C  CA    . LEU C 1 89  ? 7.279   49.574  6.749   1.00 22.54 ? 83  LEU C CA    1 
ATOM   5214 C  C     . LEU C 1 89  ? 8.395   50.592  6.486   1.00 23.37 ? 83  LEU C C     1 
ATOM   5215 O  O     . LEU C 1 89  ? 9.052   50.508  5.410   1.00 23.13 ? 83  LEU C O     1 
ATOM   5216 C  CB    . LEU C 1 89  ? 5.921   50.262  6.731   1.00 22.04 ? 83  LEU C CB    1 
ATOM   5217 C  CG    . LEU C 1 89  ? 5.525   50.884  5.399   1.00 20.66 ? 83  LEU C CG    1 
ATOM   5218 C  CD1   . LEU C 1 89  ? 5.560   49.820  4.293   1.00 22.48 ? 83  LEU C CD1   1 
ATOM   5219 C  CD2   . LEU C 1 89  ? 4.168   51.545  5.569   1.00 20.95 ? 83  LEU C CD2   1 
ATOM   5220 N  N     . GLY C 1 90  ? 8.672   51.438  7.464   1.00 22.40 ? 84  GLY C N     1 
ATOM   5221 C  CA    . GLY C 1 90  ? 9.786   52.400  7.408   1.00 22.81 ? 84  GLY C CA    1 
ATOM   5222 C  C     . GLY C 1 90  ? 11.111  51.739  7.145   1.00 24.41 ? 84  GLY C C     1 
ATOM   5223 O  O     . GLY C 1 90  ? 11.839  52.246  6.284   1.00 23.61 ? 84  GLY C O     1 
ATOM   5224 N  N     . GLU C 1 91  ? 11.416  50.637  7.834   1.00 25.55 ? 85  GLU C N     1 
ATOM   5225 C  CA    . GLU C 1 91  ? 12.697  49.900  7.662   1.00 26.81 ? 85  GLU C CA    1 
ATOM   5226 C  C     . GLU C 1 91  ? 12.789  49.332  6.241   1.00 26.13 ? 85  GLU C C     1 
ATOM   5227 O  O     . GLU C 1 91  ? 13.849  49.451  5.636   1.00 23.67 ? 85  GLU C O     1 
ATOM   5228 C  CB    . GLU C 1 91  ? 12.832  48.752  8.663   1.00 32.49 ? 85  GLU C CB    1 
ATOM   5229 C  CG    . GLU C 1 91  ? 13.031  49.195  10.079  1.00 41.35 ? 85  GLU C CG    1 
ATOM   5230 C  CD    . GLU C 1 91  ? 13.117  48.044  11.076  1.00 49.67 ? 85  GLU C CD    1 
ATOM   5231 O  OE1   . GLU C 1 91  ? 14.243  47.752  11.482  1.00 54.73 ? 85  GLU C OE1   1 
ATOM   5232 O  OE2   . GLU C 1 91  ? 12.043  47.449  11.453  1.00 55.25 ? 85  GLU C OE2   1 
ATOM   5233 N  N     . MET C 1 92  ? 11.732  48.699  5.724   1.00 22.45 ? 86  MET C N     1 
ATOM   5234 C  CA    . MET C 1 92  ? 11.766  48.066  4.379   1.00 23.04 ? 86  MET C CA    1 
ATOM   5235 C  C     . MET C 1 92  ? 11.861  49.143  3.273   1.00 23.06 ? 86  MET C C     1 
ATOM   5236 O  O     . MET C 1 92  ? 12.566  48.931  2.322   1.00 22.90 ? 86  MET C O     1 
ATOM   5237 C  CB    . MET C 1 92  ? 10.530  47.188  4.157   1.00 27.22 ? 86  MET C CB    1 
ATOM   5238 C  CG    . MET C 1 92  ? 10.451  46.015  5.092   1.00 30.58 ? 86  MET C CG    1 
ATOM   5239 S  SD    . MET C 1 92  ? 12.038  45.147  5.309   1.00 35.35 ? 86  MET C SD    1 
ATOM   5240 C  CE    . MET C 1 92  ? 12.097  44.992  7.092   1.00 42.53 ? 86  MET C CE    1 
ATOM   5241 N  N     . ILE C 1 93  ? 11.189  50.280  3.410   1.00 22.35 ? 87  ILE C N     1 
ATOM   5242 C  CA    . ILE C 1 93  ? 11.215  51.395  2.430   1.00 24.14 ? 87  ILE C CA    1 
ATOM   5243 C  C     . ILE C 1 93  ? 12.637  51.971  2.383   1.00 26.39 ? 87  ILE C C     1 
ATOM   5244 O  O     . ILE C 1 93  ? 13.202  52.075  1.273   1.00 23.12 ? 87  ILE C O     1 
ATOM   5245 C  CB    . ILE C 1 93  ? 10.185  52.455  2.822   1.00 24.39 ? 87  ILE C CB    1 
ATOM   5246 C  CG1   . ILE C 1 93  ? 8.773   52.024  2.423   1.00 24.48 ? 87  ILE C CG1   1 
ATOM   5247 C  CG2   . ILE C 1 93  ? 10.546  53.805  2.220   1.00 30.68 ? 87  ILE C CG2   1 
ATOM   5248 C  CD1   . ILE C 1 93  ? 7.723   52.947  2.990   1.00 28.29 ? 87  ILE C CD1   1 
ATOM   5249 N  N     . ASP C 1 94  ? 13.221  52.266  3.545   1.00 25.13 ? 88  ASP C N     1 
ATOM   5250 C  CA    . ASP C 1 94  ? 14.606  52.800  3.576   1.00 26.64 ? 88  ASP C CA    1 
ATOM   5251 C  C     . ASP C 1 94  ? 15.571  51.755  2.986   1.00 25.06 ? 88  ASP C C     1 
ATOM   5252 O  O     . ASP C 1 94  ? 16.437  52.152  2.188   1.00 25.23 ? 88  ASP C O     1 
ATOM   5253 C  CB    . ASP C 1 94  ? 15.011  53.257  4.972   1.00 26.64 ? 88  ASP C CB    1 
ATOM   5254 C  CG    . ASP C 1 94  ? 14.141  54.353  5.572   1.00 30.43 ? 88  ASP C CG    1 
ATOM   5255 O  OD1   . ASP C 1 94  ? 13.336  54.994  4.837   1.00 31.55 ? 88  ASP C OD1   1 
ATOM   5256 O  OD2   . ASP C 1 94  ? 14.262  54.553  6.801   1.00 32.91 ? 88  ASP C OD2   1 
ATOM   5257 N  N     . PHE C 1 95  ? 15.472  50.475  3.352   1.00 22.47 ? 89  PHE C N     1 
ATOM   5258 C  CA    . PHE C 1 95  ? 16.344  49.409  2.790   1.00 23.58 ? 89  PHE C CA    1 
ATOM   5259 C  C     . PHE C 1 95  ? 16.226  49.365  1.252   1.00 24.48 ? 89  PHE C C     1 
ATOM   5260 O  O     . PHE C 1 95  ? 17.247  49.291  0.555   1.00 23.51 ? 89  PHE C O     1 
ATOM   5261 C  CB    . PHE C 1 95  ? 16.016  48.081  3.469   1.00 23.81 ? 89  PHE C CB    1 
ATOM   5262 C  CG    . PHE C 1 95  ? 16.840  46.907  3.026   1.00 23.68 ? 89  PHE C CG    1 
ATOM   5263 C  CD1   . PHE C 1 95  ? 18.131  46.726  3.491   1.00 25.60 ? 89  PHE C CD1   1 
ATOM   5264 C  CD2   . PHE C 1 95  ? 16.315  45.972  2.145   1.00 26.14 ? 89  PHE C CD2   1 
ATOM   5265 C  CE1   . PHE C 1 95  ? 18.866  45.613  3.108   1.00 25.34 ? 89  PHE C CE1   1 
ATOM   5266 C  CE2   . PHE C 1 95  ? 17.066  44.893  1.729   1.00 24.10 ? 89  PHE C CE2   1 
ATOM   5267 C  CZ    . PHE C 1 95  ? 18.348  44.720  2.202   1.00 24.89 ? 89  PHE C CZ    1 
ATOM   5268 N  N     . CYS C 1 96  ? 14.986  49.388  0.727   1.00 23.17 ? 90  CYS C N     1 
ATOM   5269 C  CA    . CYS C 1 96  ? 14.687  49.202  -0.701  1.00 23.07 ? 90  CYS C CA    1 
ATOM   5270 C  C     . CYS C 1 96  ? 15.276  50.348  -1.505  1.00 23.31 ? 90  CYS C C     1 
ATOM   5271 O  O     . CYS C 1 96  ? 15.876  50.076  -2.555  1.00 24.17 ? 90  CYS C O     1 
ATOM   5272 C  CB    . CYS C 1 96  ? 13.187  49.062  -0.972  1.00 23.48 ? 90  CYS C CB    1 
ATOM   5273 S  SG    . CYS C 1 96  ? 12.609  47.404  -0.528  1.00 25.94 ? 90  CYS C SG    1 
ATOM   5274 N  N     . LYS C 1 97  ? 15.116  51.566  -1.021  1.00 25.15 ? 91  LYS C N     1 
ATOM   5275 C  CA    . LYS C 1 97  ? 15.614  52.736  -1.764  1.00 26.86 ? 91  LYS C CA    1 
ATOM   5276 C  C     . LYS C 1 97  ? 17.122  52.883  -1.542  1.00 27.80 ? 91  LYS C C     1 
ATOM   5277 O  O     . LYS C 1 97  ? 17.806  53.066  -2.539  1.00 31.88 ? 91  LYS C O     1 
ATOM   5278 C  CB    . LYS C 1 97  ? 14.882  54.014  -1.388  1.00 28.74 ? 91  LYS C CB    1 
ATOM   5279 C  CG    . LYS C 1 97  ? 14.957  55.058  -2.488  1.00 33.89 ? 91  LYS C CG    1 
ATOM   5280 C  CD    . LYS C 1 97  ? 14.073  54.732  -3.679  1.00 34.27 ? 91  LYS C CD    1 
ATOM   5281 C  CE    . LYS C 1 97  ? 14.417  55.568  -4.881  1.00 39.06 ? 91  LYS C CE    1 
ATOM   5282 N  NZ    . LYS C 1 97  ? 13.712  55.057  -6.068  1.00 36.59 ? 91  LYS C NZ    1 
ATOM   5283 N  N     . GLU C 1 98  ? 17.617  52.802  -0.305  1.00 32.55 ? 92  GLU C N     1 
ATOM   5284 C  CA    . GLU C 1 98  ? 19.018  53.176  0.035   1.00 34.58 ? 92  GLU C CA    1 
ATOM   5285 C  C     . GLU C 1 98  ? 19.973  52.012  -0.223  1.00 36.21 ? 92  GLU C C     1 
ATOM   5286 O  O     . GLU C 1 98  ? 21.026  52.288  -0.778  1.00 36.89 ? 92  GLU C O     1 
ATOM   5287 C  CB    . GLU C 1 98  ? 19.149  53.679  1.470   1.00 37.01 ? 92  GLU C CB    1 
ATOM   5288 C  CG    . GLU C 1 98  ? 18.579  55.077  1.690   1.00 37.74 ? 92  GLU C CG    1 
ATOM   5289 C  CD    . GLU C 1 98  ? 18.401  55.406  3.164   1.00 44.22 ? 92  GLU C CD    1 
ATOM   5290 O  OE1   . GLU C 1 98  ? 18.897  54.621  4.021   1.00 55.74 ? 92  GLU C OE1   1 
ATOM   5291 O  OE2   . GLU C 1 98  ? 17.760  56.408  3.464   1.00 45.58 ? 92  GLU C OE2   1 
ATOM   5292 N  N     . THR C 1 99  ? 19.661  50.770  0.171   1.00 31.90 ? 93  THR C N     1 
ATOM   5293 C  CA    . THR C 1 99  ? 20.590  49.633  0.001   1.00 28.89 ? 93  THR C CA    1 
ATOM   5294 C  C     . THR C 1 99  ? 20.330  48.968  -1.347  1.00 29.13 ? 93  THR C C     1 
ATOM   5295 O  O     . THR C 1 99  ? 21.276  48.735  -2.082  1.00 28.97 ? 93  THR C O     1 
ATOM   5296 C  CB    . THR C 1 99  ? 20.503  48.647  1.167   1.00 29.76 ? 93  THR C CB    1 
ATOM   5297 O  OG1   . THR C 1 99  ? 20.748  49.321  2.403   1.00 29.82 ? 93  THR C OG1   1 
ATOM   5298 C  CG2   . THR C 1 99  ? 21.470  47.503  1.026   1.00 31.23 ? 93  THR C CG2   1 
ATOM   5299 N  N     . LEU C 1 100 ? 19.086  48.627  -1.661  1.00 26.07 ? 94  LEU C N     1 
ATOM   5300 C  CA    . LEU C 1 100 ? 18.800  47.926  -2.935  1.00 25.70 ? 94  LEU C CA    1 
ATOM   5301 C  C     . LEU C 1 100 ? 18.784  48.907  -4.121  1.00 25.86 ? 94  LEU C C     1 
ATOM   5302 O  O     . LEU C 1 100 ? 18.883  48.411  -5.226  1.00 28.40 ? 94  LEU C O     1 
ATOM   5303 C  CB    . LEU C 1 100 ? 17.477  47.159  -2.823  1.00 24.36 ? 94  LEU C CB    1 
ATOM   5304 C  CG    . LEU C 1 100 ? 17.476  46.074  -1.758  1.00 26.99 ? 94  LEU C CG    1 
ATOM   5305 C  CD1   . LEU C 1 100 ? 16.200  45.277  -1.835  1.00 27.28 ? 94  LEU C CD1   1 
ATOM   5306 C  CD2   . LEU C 1 100 ? 18.679  45.153  -1.872  1.00 26.48 ? 94  LEU C CD2   1 
ATOM   5307 N  N     . GLN C 1 101 ? 18.626  50.219  -3.906  1.00 26.51 ? 95  GLN C N     1 
ATOM   5308 C  CA    . GLN C 1 101 ? 18.569  51.224  -5.001  1.00 29.05 ? 95  GLN C CA    1 
ATOM   5309 C  C     . GLN C 1 101 ? 17.487  50.820  -6.018  1.00 30.11 ? 95  GLN C C     1 
ATOM   5310 O  O     . GLN C 1 101 ? 17.734  50.876  -7.215  1.00 27.44 ? 95  GLN C O     1 
ATOM   5311 C  CB    . GLN C 1 101 ? 19.964  51.331  -5.636  1.00 34.72 ? 95  GLN C CB    1 
ATOM   5312 C  CG    . GLN C 1 101 ? 21.024  51.747  -4.625  1.00 38.75 ? 95  GLN C CG    1 
ATOM   5313 C  CD    . GLN C 1 101 ? 22.391  51.892  -5.245  1.00 47.28 ? 95  GLN C CD    1 
ATOM   5314 O  OE1   . GLN C 1 101 ? 23.323  51.170  -4.908  1.00 56.53 ? 95  GLN C OE1   1 
ATOM   5315 N  NE2   . GLN C 1 101 ? 22.513  52.817  -6.181  1.00 52.12 ? 95  GLN C NE2   1 
ATOM   5316 N  N     . LEU C 1 102 ? 16.297  50.435  -5.558  1.00 26.32 ? 96  LEU C N     1 
ATOM   5317 C  CA    . LEU C 1 102 ? 15.184  50.122  -6.468  1.00 26.84 ? 96  LEU C CA    1 
ATOM   5318 C  C     . LEU C 1 102 ? 14.760  51.404  -7.175  1.00 26.54 ? 96  LEU C C     1 
ATOM   5319 O  O     . LEU C 1 102 ? 14.840  52.496  -6.552  1.00 26.12 ? 96  LEU C O     1 
ATOM   5320 C  CB    . LEU C 1 102 ? 14.008  49.557  -5.664  1.00 27.56 ? 96  LEU C CB    1 
ATOM   5321 C  CG    . LEU C 1 102 ? 14.194  48.150  -5.128  1.00 29.84 ? 96  LEU C CG    1 
ATOM   5322 C  CD1   . LEU C 1 102 ? 12.958  47.740  -4.356  1.00 32.47 ? 96  LEU C CD1   1 
ATOM   5323 C  CD2   . LEU C 1 102 ? 14.473  47.164  -6.246  1.00 30.13 ? 96  LEU C CD2   1 
ATOM   5324 N  N     . GLU C 1 103 ? 14.224  51.248  -8.390  1.00 24.31 ? 97  GLU C N     1 
ATOM   5325 C  CA    . GLU C 1 103 ? 13.750  52.393  -9.193  1.00 26.09 ? 97  GLU C CA    1 
ATOM   5326 C  C     . GLU C 1 103 ? 12.503  53.013  -8.575  1.00 25.33 ? 97  GLU C C     1 
ATOM   5327 O  O     . GLU C 1 103 ? 12.325  54.239  -8.692  1.00 24.73 ? 97  GLU C O     1 
ATOM   5328 C  CB    . GLU C 1 103 ? 13.419  51.978  -10.624 1.00 29.27 ? 97  GLU C CB    1 
ATOM   5329 C  CG    . GLU C 1 103 ? 14.616  51.575  -11.447 1.00 33.08 ? 97  GLU C CG    1 
ATOM   5330 C  CD    . GLU C 1 103 ? 14.298  51.383  -12.937 1.00 36.36 ? 97  GLU C CD    1 
ATOM   5331 O  OE1   . GLU C 1 103 ? 13.202  51.838  -13.422 1.00 36.00 ? 97  GLU C OE1   1 
ATOM   5332 O  OE2   . GLU C 1 103 ? 15.148  50.779  -13.639 1.00 36.72 ? 97  GLU C OE2   1 
ATOM   5333 N  N     . SER C 1 104 ? 11.606  52.199  -7.997  1.00 22.74 ? 98  SER C N     1 
ATOM   5334 C  CA    . SER C 1 104 ? 10.314  52.713  -7.495  1.00 20.35 ? 98  SER C CA    1 
ATOM   5335 C  C     . SER C 1 104 ? 9.954   51.965  -6.210  1.00 20.96 ? 98  SER C C     1 
ATOM   5336 O  O     . SER C 1 104 ? 9.962   50.727  -6.214  1.00 20.32 ? 98  SER C O     1 
ATOM   5337 C  CB    . SER C 1 104 ? 9.241   52.582  -8.529  1.00 19.74 ? 98  SER C CB    1 
ATOM   5338 O  OG    . SER C 1 104 ? 8.020   53.169  -8.112  1.00 21.80 ? 98  SER C OG    1 
ATOM   5339 N  N     . VAL C 1 105 ? 9.639   52.720  -5.176  1.00 20.26 ? 99  VAL C N     1 
ATOM   5340 C  CA    . VAL C 1 105 ? 9.086   52.214  -3.893  1.00 20.13 ? 99  VAL C CA    1 
ATOM   5341 C  C     . VAL C 1 105 ? 7.729   52.868  -3.735  1.00 22.30 ? 99  VAL C C     1 
ATOM   5342 O  O     . VAL C 1 105 ? 7.673   54.106  -3.732  1.00 22.28 ? 99  VAL C O     1 
ATOM   5343 C  CB    . VAL C 1 105 ? 10.032  52.497  -2.715  1.00 23.02 ? 99  VAL C CB    1 
ATOM   5344 C  CG1   . VAL C 1 105 ? 9.431   52.084  -1.393  1.00 25.03 ? 99  VAL C CG1   1 
ATOM   5345 C  CG2   . VAL C 1 105 ? 11.372  51.832  -2.962  1.00 22.80 ? 99  VAL C CG2   1 
ATOM   5346 N  N     . SER C 1 106 ? 6.690   52.035  -3.700  1.00 21.70 ? 100 SER C N     1 
ATOM   5347 C  CA    . SER C 1 106 ? 5.280   52.449  -3.599  1.00 21.45 ? 100 SER C CA    1 
ATOM   5348 C  C     . SER C 1 106 ? 4.628   51.742  -2.405  1.00 21.32 ? 100 SER C C     1 
ATOM   5349 O  O     . SER C 1 106 ? 5.165   50.709  -1.932  1.00 20.81 ? 100 SER C O     1 
ATOM   5350 C  CB    . SER C 1 106 ? 4.534   52.252  -4.900  1.00 23.90 ? 100 SER C CB    1 
ATOM   5351 O  OG    . SER C 1 106 ? 4.336   50.895  -5.221  1.00 28.35 ? 100 SER C OG    1 
ATOM   5352 N  N     . ILE C 1 107 ? 3.604   52.399  -1.864  1.00 21.35 ? 101 ILE C N     1 
ATOM   5353 C  CA    . ILE C 1 107 ? 2.717   51.871  -0.798  1.00 20.93 ? 101 ILE C CA    1 
ATOM   5354 C  C     . ILE C 1 107 ? 1.271   52.093  -1.206  1.00 20.34 ? 101 ILE C C     1 
ATOM   5355 O  O     . ILE C 1 107 ? 0.974   53.148  -1.808  1.00 22.99 ? 101 ILE C O     1 
ATOM   5356 C  CB    . ILE C 1 107 ? 2.994   52.590  0.537   1.00 20.48 ? 101 ILE C CB    1 
ATOM   5357 C  CG1   . ILE C 1 107 ? 4.492   52.739  0.803   1.00 23.71 ? 101 ILE C CG1   1 
ATOM   5358 C  CG2   . ILE C 1 107 ? 2.245   51.871  1.650   1.00 20.47 ? 101 ILE C CG2   1 
ATOM   5359 C  CD1   . ILE C 1 107 ? 4.809   53.762  1.857   1.00 27.66 ? 101 ILE C CD1   1 
ATOM   5360 N  N     . VAL C 1 108 ? 0.406   51.125  -0.938  1.00 19.93 ? 102 VAL C N     1 
ATOM   5361 C  CA    . VAL C 1 108 ? -1.053  51.343  -1.105  1.00 19.81 ? 102 VAL C CA    1 
ATOM   5362 C  C     . VAL C 1 108 ? -1.691  51.271  0.292   1.00 18.40 ? 102 VAL C C     1 
ATOM   5363 O  O     . VAL C 1 108 ? -1.413  50.308  1.050   1.00 20.42 ? 102 VAL C O     1 
ATOM   5364 C  CB    . VAL C 1 108 ? -1.657  50.344  -2.110  1.00 21.46 ? 102 VAL C CB    1 
ATOM   5365 C  CG1   . VAL C 1 108 ? -1.360  48.918  -1.738  1.00 23.29 ? 102 VAL C CG1   1 
ATOM   5366 C  CG2   . VAL C 1 108 ? -3.149  50.540  -2.278  1.00 21.51 ? 102 VAL C CG2   1 
ATOM   5367 N  N     . THR C 1 109 ? -2.523  52.247  0.648   1.00 18.35 ? 103 THR C N     1 
ATOM   5368 C  CA    . THR C 1 109 ? -3.069  52.384  2.030   1.00 20.55 ? 103 THR C CA    1 
ATOM   5369 C  C     . THR C 1 109 ? -4.529  52.802  1.999   1.00 19.43 ? 103 THR C C     1 
ATOM   5370 O  O     . THR C 1 109 ? -4.925  53.461  1.023   1.00 20.83 ? 103 THR C O     1 
ATOM   5371 C  CB    . THR C 1 109 ? -2.224  53.379  2.847   1.00 21.06 ? 103 THR C CB    1 
ATOM   5372 O  OG1   . THR C 1 109 ? -2.765  53.508  4.156   1.00 24.87 ? 103 THR C OG1   1 
ATOM   5373 C  CG2   . THR C 1 109 ? -2.159  54.725  2.176   1.00 24.18 ? 103 THR C CG2   1 
ATOM   5374 N  N     . ASN C 1 110 ? -5.284  52.424  3.033   1.00 21.53 ? 104 ASN C N     1 
ATOM   5375 C  CA    . ASN C 1 110 ? -6.672  52.950  3.211   1.00 21.47 ? 104 ASN C CA    1 
ATOM   5376 C  C     . ASN C 1 110 ? -6.598  54.391  3.727   1.00 22.65 ? 104 ASN C C     1 
ATOM   5377 O  O     . ASN C 1 110 ? -7.625  55.035  3.739   1.00 25.46 ? 104 ASN C O     1 
ATOM   5378 C  CB    . ASN C 1 110 ? -7.532  52.038  4.070   1.00 23.28 ? 104 ASN C CB    1 
ATOM   5379 C  CG    . ASN C 1 110 ? -7.081  51.920  5.505   1.00 24.42 ? 104 ASN C CG    1 
ATOM   5380 O  OD1   . ASN C 1 110 ? -6.573  52.893  6.076   1.00 25.62 ? 104 ASN C OD1   1 
ATOM   5381 N  ND2   . ASN C 1 110 ? -7.288  50.745  6.085   1.00 25.20 ? 104 ASN C ND2   1 
ATOM   5382 N  N     . GLY C 1 111 ? -5.403  54.853  4.109   1.00 24.66 ? 105 GLY C N     1 
ATOM   5383 C  CA    . GLY C 1 111 ? -5.103  56.265  4.420   1.00 25.23 ? 105 GLY C CA    1 
ATOM   5384 C  C     . GLY C 1 111 ? -5.435  56.666  5.864   1.00 25.13 ? 105 GLY C C     1 
ATOM   5385 O  O     . GLY C 1 111 ? -4.919  57.751  6.321   1.00 25.47 ? 105 GLY C O     1 
ATOM   5386 N  N     . SER C 1 112 ? -6.187  55.843  6.605   1.00 25.88 ? 106 SER C N     1 
ATOM   5387 C  CA    . SER C 1 112 ? -6.734  56.203  7.945   1.00 27.86 ? 106 SER C CA    1 
ATOM   5388 C  C     . SER C 1 112 ? -5.601  56.414  8.974   1.00 28.16 ? 106 SER C C     1 
ATOM   5389 O  O     . SER C 1 112 ? -5.789  57.233  9.864   1.00 27.59 ? 106 SER C O     1 
ATOM   5390 C  CB    . SER C 1 112 ? -7.788  55.205  8.423   1.00 27.55 ? 106 SER C CB    1 
ATOM   5391 O  OG    . SER C 1 112 ? -7.259  53.889  8.608   1.00 31.13 ? 106 SER C OG    1 
ATOM   5392 N  N     . LEU C 1 113 ? -4.448  55.753  8.847   1.00 24.57 ? 107 LEU C N     1 
ATOM   5393 C  CA    . LEU C 1 113 ? -3.386  55.752  9.887   1.00 26.03 ? 107 LEU C CA    1 
ATOM   5394 C  C     . LEU C 1 113 ? -2.146  56.497  9.414   1.00 26.42 ? 107 LEU C C     1 
ATOM   5395 O  O     . LEU C 1 113 ? -1.179  56.491  10.146  1.00 33.90 ? 107 LEU C O     1 
ATOM   5396 C  CB    . LEU C 1 113 ? -3.020  54.309  10.243  1.00 29.06 ? 107 LEU C CB    1 
ATOM   5397 C  CG    . LEU C 1 113 ? -4.178  53.397  10.631  1.00 31.78 ? 107 LEU C CG    1 
ATOM   5398 C  CD1   . LEU C 1 113 ? -3.686  51.974  10.803  1.00 32.95 ? 107 LEU C CD1   1 
ATOM   5399 C  CD2   . LEU C 1 113 ? -4.861  53.891  11.907  1.00 33.45 ? 107 LEU C CD2   1 
ATOM   5400 N  N     . VAL C 1 114 ? -2.150  57.064  8.215   1.00 26.38 ? 108 VAL C N     1 
ATOM   5401 C  CA    . VAL C 1 114 ? -0.999  57.819  7.644   1.00 29.66 ? 108 VAL C CA    1 
ATOM   5402 C  C     . VAL C 1 114 ? -0.861  59.123  8.449   1.00 29.76 ? 108 VAL C C     1 
ATOM   5403 O  O     . VAL C 1 114 ? -1.849  59.836  8.519   1.00 28.75 ? 108 VAL C O     1 
ATOM   5404 C  CB    . VAL C 1 114 ? -1.248  58.133  6.156   1.00 28.45 ? 108 VAL C CB    1 
ATOM   5405 C  CG1   . VAL C 1 114 ? -0.159  59.005  5.551   1.00 29.06 ? 108 VAL C CG1   1 
ATOM   5406 C  CG2   . VAL C 1 114 ? -1.449  56.848  5.363   1.00 32.46 ? 108 VAL C CG2   1 
ATOM   5407 N  N     . LYS C 1 115 ? 0.326   59.415  8.973   1.00 31.91 ? 109 LYS C N     1 
ATOM   5408 C  CA    . LYS C 1 115 ? 0.639   60.676  9.702   1.00 37.63 ? 109 LYS C CA    1 
ATOM   5409 C  C     . LYS C 1 115 ? 1.746   61.414  8.950   1.00 32.99 ? 109 LYS C C     1 
ATOM   5410 O  O     . LYS C 1 115 ? 2.613   60.729  8.330   1.00 29.85 ? 109 LYS C O     1 
ATOM   5411 C  CB    . LYS C 1 115 ? 1.044   60.355  11.140  1.00 42.99 ? 109 LYS C CB    1 
ATOM   5412 C  CG    . LYS C 1 115 ? -0.080  59.758  11.983  1.00 54.06 ? 109 LYS C CG    1 
ATOM   5413 C  CD    . LYS C 1 115 ? 0.273   59.580  13.456  1.00 65.03 ? 109 LYS C CD    1 
ATOM   5414 C  CE    . LYS C 1 115 ? -0.902  59.102  14.296  1.00 78.75 ? 109 LYS C CE    1 
ATOM   5415 N  NZ    . LYS C 1 115 ? -0.480  58.546  15.611  1.00 79.91 ? 109 LYS C NZ    1 
ATOM   5416 N  N     . GLU C 1 116 ? 1.688   62.743  8.962   1.00 31.22 ? 110 GLU C N     1 
ATOM   5417 C  CA    . GLU C 1 116 ? 2.699   63.597  8.310   1.00 30.57 ? 110 GLU C CA    1 
ATOM   5418 C  C     . GLU C 1 116 ? 4.104   63.177  8.753   1.00 28.09 ? 110 GLU C C     1 
ATOM   5419 O  O     . GLU C 1 116 ? 4.986   63.183  7.894   1.00 29.56 ? 110 GLU C O     1 
ATOM   5420 C  CB    . GLU C 1 116 ? 2.486   65.081  8.593   1.00 32.03 ? 110 GLU C CB    1 
ATOM   5421 C  CG    . GLU C 1 116 ? 3.576   65.899  7.948   1.00 35.50 ? 110 GLU C CG    1 
ATOM   5422 C  CD    . GLU C 1 116 ? 3.301   67.382  7.878   1.00 38.78 ? 110 GLU C CD    1 
ATOM   5423 O  OE1   . GLU C 1 116 ? 2.312   67.803  8.512   1.00 36.32 ? 110 GLU C OE1   1 
ATOM   5424 O  OE2   . GLU C 1 116 ? 4.073   68.088  7.161   1.00 41.65 ? 110 GLU C OE2   1 
ATOM   5425 N  N     . GLN C 1 117 ? 4.318   62.807  10.022  1.00 28.16 ? 111 GLN C N     1 
ATOM   5426 C  CA    . GLN C 1 117 ? 5.687   62.532  10.548  1.00 31.74 ? 111 GLN C CA    1 
ATOM   5427 C  C     . GLN C 1 117 ? 6.304   61.360  9.764   1.00 29.75 ? 111 GLN C C     1 
ATOM   5428 O  O     . GLN C 1 117 ? 7.532   61.348  9.550   1.00 28.94 ? 111 GLN C O     1 
ATOM   5429 C  CB    . GLN C 1 117 ? 5.699   62.292  12.072  1.00 38.66 ? 111 GLN C CB    1 
ATOM   5430 C  CG    . GLN C 1 117 ? 4.980   61.019  12.517  1.00 50.49 ? 111 GLN C CG    1 
ATOM   5431 C  CD    . GLN C 1 117 ? 5.373   60.470  13.877  1.00 61.39 ? 111 GLN C CD    1 
ATOM   5432 O  OE1   . GLN C 1 117 ? 5.643   61.206  14.822  1.00 62.18 ? 111 GLN C OE1   1 
ATOM   5433 N  NE2   . GLN C 1 117 ? 5.386   59.148  13.999  1.00 57.98 ? 111 GLN C NE2   1 
ATOM   5434 N  N     . PHE C 1 118 ? 5.507   60.383  9.330   1.00 26.89 ? 112 PHE C N     1 
ATOM   5435 C  CA    . PHE C 1 118 ? 6.050   59.205  8.597   1.00 26.17 ? 112 PHE C CA    1 
ATOM   5436 C  C     . PHE C 1 118 ? 6.565   59.658  7.228   1.00 27.41 ? 112 PHE C C     1 
ATOM   5437 O  O     . PHE C 1 118 ? 7.642   59.232  6.801   1.00 26.59 ? 112 PHE C O     1 
ATOM   5438 C  CB    . PHE C 1 118 ? 4.995   58.110  8.430   1.00 26.99 ? 112 PHE C CB    1 
ATOM   5439 C  CG    . PHE C 1 118 ? 5.537   56.827  7.844   1.00 22.93 ? 112 PHE C CG    1 
ATOM   5440 C  CD1   . PHE C 1 118 ? 5.609   56.653  6.467   1.00 25.50 ? 112 PHE C CD1   1 
ATOM   5441 C  CD2   . PHE C 1 118 ? 5.971   55.806  8.664   1.00 22.09 ? 112 PHE C CD2   1 
ATOM   5442 C  CE1   . PHE C 1 118 ? 6.131   55.491  5.922   1.00 24.61 ? 112 PHE C CE1   1 
ATOM   5443 C  CE2   . PHE C 1 118 ? 6.502   54.654  8.121   1.00 23.86 ? 112 PHE C CE2   1 
ATOM   5444 C  CZ    . PHE C 1 118 ? 6.550   54.476  6.754   1.00 23.54 ? 112 PHE C CZ    1 
ATOM   5445 N  N     . LEU C 1 119 ? 5.807   60.522  6.550   1.00 29.54 ? 113 LEU C N     1 
ATOM   5446 C  CA    . LEU C 1 119 ? 6.166   60.981  5.192   1.00 31.42 ? 113 LEU C CA    1 
ATOM   5447 C  C     . LEU C 1 119 ? 7.342   61.945  5.317   1.00 33.63 ? 113 LEU C C     1 
ATOM   5448 O  O     . LEU C 1 119 ? 8.207   61.917  4.451   1.00 31.54 ? 113 LEU C O     1 
ATOM   5449 C  CB    . LEU C 1 119 ? 4.939   61.608  4.526   1.00 32.89 ? 113 LEU C CB    1 
ATOM   5450 C  CG    . LEU C 1 119 ? 3.747   60.662  4.411   1.00 31.82 ? 113 LEU C CG    1 
ATOM   5451 C  CD1   . LEU C 1 119 ? 2.594   61.304  3.642   1.00 33.50 ? 113 LEU C CD1   1 
ATOM   5452 C  CD2   . LEU C 1 119 ? 4.159   59.332  3.785   1.00 35.98 ? 113 LEU C CD2   1 
ATOM   5453 N  N     . GLN C 1 120 ? 7.409   62.712  6.404   1.00 34.67 ? 114 GLN C N     1 
ATOM   5454 C  CA    . GLN C 1 120 ? 8.566   63.599  6.662   1.00 34.79 ? 114 GLN C CA    1 
ATOM   5455 C  C     . GLN C 1 120 ? 9.828   62.763  6.877   1.00 32.61 ? 114 GLN C C     1 
ATOM   5456 O  O     . GLN C 1 120 ? 10.880  63.154  6.356   1.00 32.37 ? 114 GLN C O     1 
ATOM   5457 C  CB    . GLN C 1 120 ? 8.330   64.532  7.846   1.00 38.09 ? 114 GLN C CB    1 
ATOM   5458 C  CG    . GLN C 1 120 ? 9.453   65.547  8.005   1.00 44.99 ? 114 GLN C CG    1 
ATOM   5459 C  CD    . GLN C 1 120 ? 9.238   66.485  9.167   1.00 55.56 ? 114 GLN C CD    1 
ATOM   5460 O  OE1   . GLN C 1 120 ? 8.602   66.135  10.165  1.00 62.45 ? 114 GLN C OE1   1 
ATOM   5461 N  NE2   . GLN C 1 120 ? 9.781   67.689  9.045   1.00 59.25 ? 114 GLN C NE2   1 
ATOM   5462 N  N     A LYS C 1 121 ? 9.722   61.665  7.631   0.44 29.01 ? 115 LYS C N     1 
ATOM   5463 N  N     B LYS C 1 121 ? 9.753   61.667  7.646   0.56 29.50 ? 115 LYS C N     1 
ATOM   5464 C  CA    A LYS C 1 121 ? 10.877  60.816  8.019   0.44 29.04 ? 115 LYS C CA    1 
ATOM   5465 C  CA    B LYS C 1 121 ? 10.948  60.844  7.988   0.56 30.45 ? 115 LYS C CA    1 
ATOM   5466 C  C     A LYS C 1 121 ? 11.345  59.972  6.830   0.44 28.63 ? 115 LYS C C     1 
ATOM   5467 C  C     B LYS C 1 121 ? 11.366  60.005  6.778   0.56 29.59 ? 115 LYS C C     1 
ATOM   5468 O  O     A LYS C 1 121 ? 12.575  59.817  6.673   0.44 27.24 ? 115 LYS C O     1 
ATOM   5469 O  O     B LYS C 1 121 ? 12.589  59.885  6.551   0.56 28.00 ? 115 LYS C O     1 
ATOM   5470 C  CB    A LYS C 1 121 ? 10.504  59.882  9.170   0.44 29.14 ? 115 LYS C CB    1 
ATOM   5471 C  CB    B LYS C 1 121 ? 10.705  59.907  9.175   0.56 32.13 ? 115 LYS C CB    1 
ATOM   5472 C  CG    A LYS C 1 121 ? 11.581  58.867  9.523   0.44 30.83 ? 115 LYS C CG    1 
ATOM   5473 C  CG    B LYS C 1 121 ? 11.916  59.073  9.600   0.56 35.15 ? 115 LYS C CG    1 
ATOM   5474 C  CD    A LYS C 1 121 ? 11.346  58.187  10.857  0.44 31.51 ? 115 LYS C CD    1 
ATOM   5475 C  CD    B LYS C 1 121 ? 13.120  59.885  10.076  0.56 37.51 ? 115 LYS C CD    1 
ATOM   5476 C  CE    A LYS C 1 121 ? 12.533  57.374  11.327  0.44 31.22 ? 115 LYS C CE    1 
ATOM   5477 C  CE    B LYS C 1 121 ? 14.064  59.126  10.991  0.56 39.74 ? 115 LYS C CE    1 
ATOM   5478 N  NZ    A LYS C 1 121 ? 12.241  56.753  12.631  0.44 33.28 ? 115 LYS C NZ    1 
ATOM   5479 N  NZ    B LYS C 1 121 ? 14.899  58.154  10.242  0.56 39.12 ? 115 LYS C NZ    1 
ATOM   5480 N  N     . HIS C 1 122 ? 10.406  59.398  6.064   1.00 26.54 ? 116 HIS C N     1 
ATOM   5481 C  CA    . HIS C 1 122 ? 10.719  58.403  4.998   1.00 26.28 ? 116 HIS C CA    1 
ATOM   5482 C  C     . HIS C 1 122 ? 10.455  58.955  3.591   1.00 26.16 ? 116 HIS C C     1 
ATOM   5483 O  O     . HIS C 1 122 ? 10.774  58.224  2.614   1.00 25.82 ? 116 HIS C O     1 
ATOM   5484 C  CB    . HIS C 1 122 ? 9.983   57.076  5.243   1.00 25.83 ? 116 HIS C CB    1 
ATOM   5485 C  CG    . HIS C 1 122 ? 10.299  56.439  6.557   1.00 23.65 ? 116 HIS C CG    1 
ATOM   5486 N  ND1   . HIS C 1 122 ? 11.452  55.746  6.770   1.00 26.78 ? 116 HIS C ND1   1 
ATOM   5487 C  CD2   . HIS C 1 122 ? 9.614   56.410  7.727   1.00 25.24 ? 116 HIS C CD2   1 
ATOM   5488 C  CE1   . HIS C 1 122 ? 11.493  55.316  8.031   1.00 26.43 ? 116 HIS C CE1   1 
ATOM   5489 N  NE2   . HIS C 1 122 ? 10.362  55.716  8.646   1.00 23.56 ? 116 HIS C NE2   1 
ATOM   5490 N  N     . GLY C 1 123 ? 9.943   60.182  3.446   1.00 26.47 ? 117 GLY C N     1 
ATOM   5491 C  CA    . GLY C 1 123 ? 9.506   60.710  2.134   1.00 25.18 ? 117 GLY C CA    1 
ATOM   5492 C  C     . GLY C 1 123 ? 10.588  60.585  1.065   1.00 24.33 ? 117 GLY C C     1 
ATOM   5493 O  O     . GLY C 1 123 ? 10.282  60.251  -0.070  1.00 25.89 ? 117 GLY C O     1 
ATOM   5494 N  N     . ARG C 1 124 ? 11.837  60.867  1.395   1.00 28.97 ? 118 ARG C N     1 
ATOM   5495 C  CA    . ARG C 1 124 ? 12.911  60.872  0.379   1.00 30.67 ? 118 ARG C CA    1 
ATOM   5496 C  C     . ARG C 1 124 ? 12.985  59.480  -0.272  1.00 30.49 ? 118 ARG C C     1 
ATOM   5497 O  O     . ARG C 1 124 ? 13.496  59.385  -1.420  1.00 30.14 ? 118 ARG C O     1 
ATOM   5498 C  CB    . ARG C 1 124 ? 14.232  61.314  1.014   1.00 35.34 ? 118 ARG C CB    1 
ATOM   5499 C  CG    . ARG C 1 124 ? 14.960  60.213  1.778   1.00 37.57 ? 118 ARG C CG    1 
ATOM   5500 C  CD    . ARG C 1 124 ? 16.093  60.710  2.684   1.00 37.55 ? 118 ARG C CD    1 
ATOM   5501 N  NE    . ARG C 1 124 ? 16.637  59.579  3.404   1.00 38.83 ? 118 ARG C NE    1 
ATOM   5502 C  CZ    . ARG C 1 124 ? 16.111  59.039  4.515   1.00 43.28 ? 118 ARG C CZ    1 
ATOM   5503 N  NH1   . ARG C 1 124 ? 15.018  59.530  5.076   1.00 43.24 ? 118 ARG C NH1   1 
ATOM   5504 N  NH2   . ARG C 1 124 ? 16.677  57.975  5.060   1.00 48.36 ? 118 ARG C NH2   1 
ATOM   5505 N  N     . ASN C 1 125 ? 12.472  58.432  0.394   1.00 27.14 ? 119 ASN C N     1 
ATOM   5506 C  CA    . ASN C 1 125 ? 12.606  57.030  -0.066  1.00 25.44 ? 119 ASN C CA    1 
ATOM   5507 C  C     . ASN C 1 125 ? 11.300  56.491  -0.687  1.00 25.73 ? 119 ASN C C     1 
ATOM   5508 O  O     . ASN C 1 125 ? 11.323  55.344  -1.175  1.00 28.85 ? 119 ASN C O     1 
ATOM   5509 C  CB    . ASN C 1 125 ? 13.108  56.155  1.082   1.00 26.38 ? 119 ASN C CB    1 
ATOM   5510 C  CG    . ASN C 1 125 ? 14.564  56.422  1.431   1.00 27.72 ? 119 ASN C CG    1 
ATOM   5511 O  OD1   . ASN C 1 125 ? 15.361  56.687  0.534   1.00 29.80 ? 119 ASN C OD1   1 
ATOM   5512 N  ND2   . ASN C 1 125 ? 14.931  56.321  2.706   1.00 27.68 ? 119 ASN C ND2   1 
ATOM   5513 N  N     . ILE C 1 126 ? 10.214  57.241  -0.639  1.00 24.88 ? 120 ILE C N     1 
ATOM   5514 C  CA    . ILE C 1 126 ? 8.869   56.831  -1.148  1.00 24.51 ? 120 ILE C CA    1 
ATOM   5515 C  C     . ILE C 1 126 ? 8.639   57.523  -2.494  1.00 25.91 ? 120 ILE C C     1 
ATOM   5516 O  O     . ILE C 1 126 ? 8.621   58.752  -2.533  1.00 25.09 ? 120 ILE C O     1 
ATOM   5517 C  CB    . ILE C 1 126 ? 7.750   57.167  -0.154  1.00 24.08 ? 120 ILE C CB    1 
ATOM   5518 C  CG1   . ILE C 1 126 ? 7.990   56.510  1.205   1.00 25.52 ? 120 ILE C CG1   1 
ATOM   5519 C  CG2   . ILE C 1 126 ? 6.380   56.787  -0.735  1.00 25.68 ? 120 ILE C CG2   1 
ATOM   5520 C  CD1   . ILE C 1 126 ? 7.153   57.081  2.304   1.00 22.27 ? 120 ILE C CD1   1 
ATOM   5521 N  N     . ASP C 1 127 ? 8.518   56.766  -3.576  1.00 23.99 ? 121 ASP C N     1 
ATOM   5522 C  CA    . ASP C 1 127 ? 8.292   57.348  -4.922  1.00 22.86 ? 121 ASP C CA    1 
ATOM   5523 C  C     . ASP C 1 127 ? 6.808   57.635  -5.061  1.00 22.51 ? 121 ASP C C     1 
ATOM   5524 O  O     . ASP C 1 127 ? 6.446   58.699  -5.599  1.00 25.80 ? 121 ASP C O     1 
ATOM   5525 C  CB    . ASP C 1 127 ? 8.876   56.452  -6.021  1.00 24.70 ? 121 ASP C CB    1 
ATOM   5526 C  CG    . ASP C 1 127 ? 10.373  56.339  -5.843  1.00 33.73 ? 121 ASP C CG    1 
ATOM   5527 O  OD1   . ASP C 1 127 ? 11.064  57.422  -5.973  1.00 34.04 ? 121 ASP C OD1   1 
ATOM   5528 O  OD2   . ASP C 1 127 ? 10.845  55.217  -5.464  1.00 32.25 ? 121 ASP C OD2   1 
ATOM   5529 N  N     . ILE C 1 128 ? 5.957   56.694  -4.637  1.00 20.57 ? 122 ILE C N     1 
ATOM   5530 C  CA    . ILE C 1 128 ? 4.494   56.751  -4.914  1.00 23.28 ? 122 ILE C CA    1 
ATOM   5531 C  C     . ILE C 1 128 ? 3.737   56.366  -3.645  1.00 22.36 ? 122 ILE C C     1 
ATOM   5532 O  O     . ILE C 1 128 ? 4.078   55.363  -3.022  1.00 21.11 ? 122 ILE C O     1 
ATOM   5533 C  CB    . ILE C 1 128 ? 4.138   55.800  -6.070  1.00 22.16 ? 122 ILE C CB    1 
ATOM   5534 C  CG1   . ILE C 1 128 ? 4.865   56.169  -7.369  1.00 23.85 ? 122 ILE C CG1   1 
ATOM   5535 C  CG2   . ILE C 1 128 ? 2.612   55.710  -6.226  1.00 22.79 ? 122 ILE C CG2   1 
ATOM   5536 C  CD1   . ILE C 1 128 ? 4.931   55.024  -8.381  1.00 24.88 ? 122 ILE C CD1   1 
ATOM   5537 N  N     . LEU C 1 129 ? 2.729   57.146  -3.291  1.00 20.82 ? 123 LEU C N     1 
ATOM   5538 C  CA    . LEU C 1 129 ? 1.786   56.773  -2.228  1.00 22.14 ? 123 LEU C CA    1 
ATOM   5539 C  C     . LEU C 1 129 ? 0.369   56.730  -2.836  1.00 21.67 ? 123 LEU C C     1 
ATOM   5540 O  O     . LEU C 1 129 ? -0.124  57.720  -3.412  1.00 21.59 ? 123 LEU C O     1 
ATOM   5541 C  CB    . LEU C 1 129 ? 1.897   57.752  -1.062  1.00 22.76 ? 123 LEU C CB    1 
ATOM   5542 C  CG    . LEU C 1 129 ? 0.906   57.493  0.066   1.00 24.64 ? 123 LEU C CG    1 
ATOM   5543 C  CD1   . LEU C 1 129 ? 1.178   56.134  0.705   1.00 26.00 ? 123 LEU C CD1   1 
ATOM   5544 C  CD2   . LEU C 1 129 ? 0.971   58.600  1.097   1.00 27.75 ? 123 LEU C CD2   1 
ATOM   5545 N  N     . ALA C 1 130 ? -0.227  55.551  -2.798  1.00 21.57 ? 124 ALA C N     1 
ATOM   5546 C  CA    . ALA C 1 130 ? -1.583  55.288  -3.319  1.00 21.59 ? 124 ALA C CA    1 
ATOM   5547 C  C     . ALA C 1 130 ? -2.523  55.238  -2.132  1.00 20.50 ? 124 ALA C C     1 
ATOM   5548 O  O     . ALA C 1 130 ? -2.239  54.482  -1.166  1.00 19.64 ? 124 ALA C O     1 
ATOM   5549 C  CB    . ALA C 1 130 ? -1.613  54.002  -4.114  1.00 22.51 ? 124 ALA C CB    1 
ATOM   5550 N  N     . VAL C 1 131 ? -3.614  55.979  -2.208  1.00 19.98 ? 125 VAL C N     1 
ATOM   5551 C  CA    . VAL C 1 131 ? -4.700  55.895  -1.189  1.00 20.79 ? 125 VAL C CA    1 
ATOM   5552 C  C     . VAL C 1 131 ? -5.969  55.353  -1.841  1.00 19.78 ? 125 VAL C C     1 
ATOM   5553 O  O     . VAL C 1 131 ? -6.333  55.812  -2.922  1.00 20.28 ? 125 VAL C O     1 
ATOM   5554 C  CB    . VAL C 1 131 ? -4.956  57.244  -0.500  1.00 23.32 ? 125 VAL C CB    1 
ATOM   5555 C  CG1   . VAL C 1 131 ? -5.993  57.112  0.607   1.00 22.12 ? 125 VAL C CG1   1 
ATOM   5556 C  CG2   . VAL C 1 131 ? -3.643  57.790  0.055   1.00 24.89 ? 125 VAL C CG2   1 
ATOM   5557 N  N     . SER C 1 132 ? -6.603  54.365  -1.210  1.00 21.83 ? 126 SER C N     1 
ATOM   5558 C  CA    . SER C 1 132 ? -7.873  53.785  -1.679  1.00 22.91 ? 126 SER C CA    1 
ATOM   5559 C  C     . SER C 1 132 ? -9.022  54.688  -1.272  1.00 28.06 ? 126 SER C C     1 
ATOM   5560 O  O     . SER C 1 132 ? -9.124  55.009  -0.090  1.00 31.10 ? 126 SER C O     1 
ATOM   5561 C  CB    . SER C 1 132 ? -8.040  52.426  -1.150  1.00 24.98 ? 126 SER C CB    1 
ATOM   5562 O  OG    . SER C 1 132 ? -6.967  51.671  -1.668  1.00 25.63 ? 126 SER C OG    1 
ATOM   5563 N  N     . CYS C 1 133 ? -9.814  55.138  -2.234  1.00 28.10 ? 127 CYS C N     1 
ATOM   5564 C  CA    . CYS C 1 133 ? -11.063 55.871  -1.929  1.00 29.32 ? 127 CYS C CA    1 
ATOM   5565 C  C     . CYS C 1 133 ? -12.146 55.432  -2.898  1.00 24.48 ? 127 CYS C C     1 
ATOM   5566 O  O     . CYS C 1 133 ? -11.984 55.673  -4.084  1.00 25.90 ? 127 CYS C O     1 
ATOM   5567 C  CB    . CYS C 1 133 ? -10.870 57.370  -2.046  1.00 36.25 ? 127 CYS C CB    1 
ATOM   5568 S  SG    . CYS C 1 133 ? -12.387 58.235  -1.560  1.00 45.15 ? 127 CYS C SG    1 
ATOM   5569 N  N     . ASP C 1 134 ? -13.167 54.749  -2.400  1.00 25.76 ? 128 ASP C N     1 
ATOM   5570 C  CA    . ASP C 1 134 ? -14.217 54.142  -3.249  1.00 25.05 ? 128 ASP C CA    1 
ATOM   5571 C  C     . ASP C 1 134 ? -15.382 55.118  -3.429  1.00 31.17 ? 128 ASP C C     1 
ATOM   5572 O  O     . ASP C 1 134 ? -16.142 54.976  -4.390  1.00 33.26 ? 128 ASP C O     1 
ATOM   5573 C  CB    . ASP C 1 134 ? -14.628 52.804  -2.664  1.00 29.54 ? 128 ASP C CB    1 
ATOM   5574 C  CG    . ASP C 1 134 ? -13.460 51.831  -2.551  1.00 29.69 ? 128 ASP C CG    1 
ATOM   5575 O  OD1   . ASP C 1 134 ? -12.553 51.858  -3.428  1.00 27.74 ? 128 ASP C OD1   1 
ATOM   5576 O  OD2   . ASP C 1 134 ? -13.432 51.102  -1.552  1.00 29.83 ? 128 ASP C OD2   1 
ATOM   5577 N  N     . SER C 1 135 ? -15.511 56.110  -2.565  1.00 31.16 ? 129 SER C N     1 
ATOM   5578 C  CA    . SER C 1 135 ? -16.626 57.071  -2.664  1.00 32.09 ? 129 SER C CA    1 
ATOM   5579 C  C     . SER C 1 135 ? -16.226 58.356  -1.961  1.00 33.69 ? 129 SER C C     1 
ATOM   5580 O  O     . SER C 1 135 ? -15.413 58.293  -0.992  1.00 33.74 ? 129 SER C O     1 
ATOM   5581 C  CB    . SER C 1 135 ? -17.890 56.492  -2.110  1.00 32.35 ? 129 SER C CB    1 
ATOM   5582 O  OG    . SER C 1 135 ? -18.995 57.320  -2.448  1.00 35.87 ? 129 SER C OG    1 
ATOM   5583 N  N     . PHE C 1 136 ? -16.768 59.466  -2.461  1.00 36.15 ? 130 PHE C N     1 
ATOM   5584 C  CA    . PHE C 1 136 ? -16.679 60.799  -1.816  1.00 38.93 ? 130 PHE C CA    1 
ATOM   5585 C  C     . PHE C 1 136 ? -17.911 61.030  -0.925  1.00 42.45 ? 130 PHE C C     1 
ATOM   5586 O  O     . PHE C 1 136 ? -18.002 62.063  -0.282  1.00 44.39 ? 130 PHE C O     1 
ATOM   5587 C  CB    . PHE C 1 136 ? -16.443 61.824  -2.923  1.00 38.73 ? 130 PHE C CB    1 
ATOM   5588 C  CG    . PHE C 1 136 ? -15.090 61.614  -3.546  1.00 39.03 ? 130 PHE C CG    1 
ATOM   5589 C  CD1   . PHE C 1 136 ? -13.951 62.095  -2.917  1.00 37.53 ? 130 PHE C CD1   1 
ATOM   5590 C  CD2   . PHE C 1 136 ? -14.939 60.861  -4.704  1.00 36.83 ? 130 PHE C CD2   1 
ATOM   5591 C  CE1   . PHE C 1 136 ? -12.697 61.870  -3.461  1.00 38.48 ? 130 PHE C CE1   1 
ATOM   5592 C  CE2   . PHE C 1 136 ? -13.681 60.648  -5.248  1.00 35.92 ? 130 PHE C CE2   1 
ATOM   5593 C  CZ    . PHE C 1 136 ? -12.563 61.150  -4.621  1.00 34.68 ? 130 PHE C CZ    1 
ATOM   5594 N  N     . ASN C 1 137 ? -18.811 60.055  -0.865  1.00 40.60 ? 131 ASN C N     1 
ATOM   5595 C  CA    . ASN C 1 137 ? -20.120 60.169  -0.175  1.00 46.85 ? 131 ASN C CA    1 
ATOM   5596 C  C     . ASN C 1 137 ? -20.032 59.281  1.072   1.00 45.40 ? 131 ASN C C     1 
ATOM   5597 O  O     . ASN C 1 137 ? -19.839 58.065  0.910   1.00 41.68 ? 131 ASN C O     1 
ATOM   5598 C  CB    . ASN C 1 137 ? -21.254 59.819  -1.150  1.00 45.77 ? 131 ASN C CB    1 
ATOM   5599 C  CG    . ASN C 1 137 ? -22.625 59.810  -0.514  1.00 54.78 ? 131 ASN C CG    1 
ATOM   5600 O  OD1   . ASN C 1 137 ? -23.043 58.803  0.049   1.00 54.88 ? 131 ASN C OD1   1 
ATOM   5601 N  ND2   . ASN C 1 137 ? -23.349 60.913  -0.632  1.00 57.57 ? 131 ASN C ND2   1 
ATOM   5602 N  N     . GLU C 1 138 ? -20.156 59.874  2.263   1.00 47.16 ? 132 GLU C N     1 
ATOM   5603 C  CA    . GLU C 1 138 ? -20.044 59.200  3.587   1.00 48.25 ? 132 GLU C CA    1 
ATOM   5604 C  C     . GLU C 1 138 ? -21.018 58.017  3.648   1.00 47.42 ? 132 GLU C C     1 
ATOM   5605 O  O     . GLU C 1 138 ? -20.636 56.948  4.124   1.00 42.42 ? 132 GLU C O     1 
ATOM   5606 C  CB    . GLU C 1 138 ? -20.321 60.227  4.690   1.00 59.15 ? 132 GLU C CB    1 
ATOM   5607 C  CG    . GLU C 1 138 ? -19.741 59.874  6.054   1.00 69.20 ? 132 GLU C CG    1 
ATOM   5608 C  CD    . GLU C 1 138 ? -19.639 61.053  7.021   1.00 77.11 ? 132 GLU C CD    1 
ATOM   5609 O  OE1   . GLU C 1 138 ? -18.670 61.848  6.890   1.00 73.18 ? 132 GLU C OE1   1 
ATOM   5610 O  OE2   . GLU C 1 138 ? -20.533 61.186  7.901   1.00 71.94 ? 132 GLU C OE2   1 
ATOM   5611 N  N     . ALA C 1 139 ? -22.257 58.199  3.207   1.00 45.58 ? 133 ALA C N     1 
ATOM   5612 C  CA    . ALA C 1 139 ? -23.280 57.126  3.211   1.00 48.12 ? 133 ALA C CA    1 
ATOM   5613 C  C     . ALA C 1 139 ? -22.738 55.888  2.472   1.00 42.05 ? 133 ALA C C     1 
ATOM   5614 O  O     . ALA C 1 139 ? -22.777 54.797  3.064   1.00 42.16 ? 133 ALA C O     1 
ATOM   5615 C  CB    . ALA C 1 139 ? -24.573 57.625  2.596   1.00 49.44 ? 133 ALA C CB    1 
ATOM   5616 N  N     . THR C 1 140 ? -22.249 56.055  1.232   1.00 38.11 ? 134 THR C N     1 
ATOM   5617 C  CA    . THR C 1 140 ? -21.686 54.958  0.388   1.00 37.51 ? 134 THR C CA    1 
ATOM   5618 C  C     . THR C 1 140 ? -20.481 54.322  1.103   1.00 33.84 ? 134 THR C C     1 
ATOM   5619 O  O     . THR C 1 140 ? -20.426 53.080  1.169   1.00 36.96 ? 134 THR C O     1 
ATOM   5620 C  CB    . THR C 1 140 ? -21.295 55.446  -1.012  1.00 38.02 ? 134 THR C CB    1 
ATOM   5621 O  OG1   . THR C 1 140 ? -22.407 56.042  -1.681  1.00 39.48 ? 134 THR C OG1   1 
ATOM   5622 C  CG2   . THR C 1 140 ? -20.797 54.318  -1.891  1.00 40.34 ? 134 THR C CG2   1 
ATOM   5623 N  N     . ASN C 1 141 ? -19.572 55.117  1.663   1.00 33.47 ? 135 ASN C N     1 
ATOM   5624 C  CA    . ASN C 1 141 ? -18.386 54.597  2.394   1.00 38.29 ? 135 ASN C CA    1 
ATOM   5625 C  C     . ASN C 1 141 ? -18.836 53.725  3.568   1.00 38.74 ? 135 ASN C C     1 
ATOM   5626 O  O     . ASN C 1 141 ? -18.202 52.697  3.800   1.00 35.37 ? 135 ASN C O     1 
ATOM   5627 C  CB    . ASN C 1 141 ? -17.428 55.697  2.840   1.00 38.08 ? 135 ASN C CB    1 
ATOM   5628 C  CG    . ASN C 1 141 ? -16.469 56.053  1.732   1.00 38.47 ? 135 ASN C CG    1 
ATOM   5629 O  OD1   . ASN C 1 141 ? -16.065 55.166  0.974   1.00 34.84 ? 135 ASN C OD1   1 
ATOM   5630 N  ND2   . ASN C 1 141 ? -16.142 57.327  1.603   1.00 36.38 ? 135 ASN C ND2   1 
ATOM   5631 N  N     . ILE C 1 142 ? -19.905 54.114  4.268   1.00 44.27 ? 136 ILE C N     1 
ATOM   5632 C  CA    . ILE C 1 142 ? -20.448 53.320  5.406   1.00 43.99 ? 136 ILE C CA    1 
ATOM   5633 C  C     . ILE C 1 142 ? -21.003 51.998  4.873   1.00 38.53 ? 136 ILE C C     1 
ATOM   5634 O  O     . ILE C 1 142 ? -20.684 50.988  5.475   1.00 42.01 ? 136 ILE C O     1 
ATOM   5635 C  CB    . ILE C 1 142 ? -21.499 54.108  6.215   1.00 48.01 ? 136 ILE C CB    1 
ATOM   5636 C  CG1   . ILE C 1 142 ? -20.910 55.401  6.785   1.00 48.67 ? 136 ILE C CG1   1 
ATOM   5637 C  CG2   . ILE C 1 142 ? -22.096 53.224  7.305   1.00 44.23 ? 136 ILE C CG2   1 
ATOM   5638 C  CD1   . ILE C 1 142 ? -21.960 56.455  7.066   1.00 53.27 ? 136 ILE C CD1   1 
ATOM   5639 N  N     . LYS C 1 143 ? -21.781 52.015  3.785   1.00 39.86 ? 137 LYS C N     1 
ATOM   5640 C  CA    . LYS C 1 143 ? -22.365 50.804  3.149   1.00 39.17 ? 137 LYS C CA    1 
ATOM   5641 C  C     . LYS C 1 143 ? -21.249 49.853  2.661   1.00 42.16 ? 137 LYS C C     1 
ATOM   5642 O  O     . LYS C 1 143 ? -21.416 48.623  2.812   1.00 41.73 ? 137 LYS C O     1 
ATOM   5643 C  CB    . LYS C 1 143 ? -23.265 51.182  1.966   1.00 46.96 ? 137 LYS C CB    1 
ATOM   5644 C  CG    . LYS C 1 143 ? -24.555 51.917  2.320   1.00 52.50 ? 137 LYS C CG    1 
ATOM   5645 C  CD    . LYS C 1 143 ? -25.251 52.575  1.130   1.00 55.98 ? 137 LYS C CD    1 
ATOM   5646 C  CE    . LYS C 1 143 ? -25.683 51.589  0.060   1.00 65.80 ? 137 LYS C CE    1 
ATOM   5647 N  NZ    . LYS C 1 143 ? -26.572 52.225  -0.946  1.00 69.23 ? 137 LYS C NZ    1 
ATOM   5648 N  N     . ILE C 1 144 ? -20.165 50.381  2.083   1.00 35.31 ? 138 ILE C N     1 
ATOM   5649 C  CA    . ILE C 1 144 ? -19.018 49.566  1.553   1.00 36.07 ? 138 ILE C CA    1 
ATOM   5650 C  C     . ILE C 1 144 ? -18.267 48.885  2.703   1.00 30.99 ? 138 ILE C C     1 
ATOM   5651 O  O     . ILE C 1 144 ? -17.707 47.786  2.505   1.00 31.43 ? 138 ILE C O     1 
ATOM   5652 C  CB    . ILE C 1 144 ? -18.066 50.448  0.724   1.00 36.64 ? 138 ILE C CB    1 
ATOM   5653 C  CG1   . ILE C 1 144 ? -18.660 50.815  -0.632  1.00 41.65 ? 138 ILE C CG1   1 
ATOM   5654 C  CG2   . ILE C 1 144 ? -16.705 49.783  0.535   1.00 41.52 ? 138 ILE C CG2   1 
ATOM   5655 C  CD1   . ILE C 1 144 ? -17.820 51.830  -1.398  1.00 44.81 ? 138 ILE C CD1   1 
ATOM   5656 N  N     . GLY C 1 145 ? -18.156 49.535  3.848   1.00 33.02 ? 139 GLY C N     1 
ATOM   5657 C  CA    . GLY C 1 145 ? -17.368 49.008  4.983   1.00 30.51 ? 139 GLY C CA    1 
ATOM   5658 C  C     . GLY C 1 145 ? -16.077 49.762  5.158   1.00 30.30 ? 139 GLY C C     1 
ATOM   5659 O  O     . GLY C 1 145 ? -15.255 49.323  5.979   1.00 29.13 ? 139 GLY C O     1 
ATOM   5660 N  N     . ARG C 1 146 ? -15.880 50.845  4.394   1.00 30.70 ? 140 ARG C N     1 
ATOM   5661 C  CA    . ARG C 1 146 ? -14.703 51.733  4.558   1.00 37.21 ? 140 ARG C CA    1 
ATOM   5662 C  C     . ARG C 1 146 ? -14.844 52.537  5.860   1.00 41.45 ? 140 ARG C C     1 
ATOM   5663 O  O     . ARG C 1 146 ? -13.850 53.154  6.282   1.00 41.54 ? 140 ARG C O     1 
ATOM   5664 C  CB    . ARG C 1 146 ? -14.551 52.665  3.357   1.00 36.29 ? 140 ARG C CB    1 
ATOM   5665 C  CG    . ARG C 1 146 ? -13.942 51.984  2.139   1.00 33.49 ? 140 ARG C CG    1 
ATOM   5666 C  CD    . ARG C 1 146 ? -12.432 52.124  1.974   1.00 34.07 ? 140 ARG C CD    1 
ATOM   5667 N  NE    . ARG C 1 146 ? -12.128 51.370  0.761   1.00 33.44 ? 140 ARG C NE    1 
ATOM   5668 C  CZ    . ARG C 1 146 ? -11.016 50.706  0.498   1.00 33.22 ? 140 ARG C CZ    1 
ATOM   5669 N  NH1   . ARG C 1 146 ? -10.008 50.706  1.346   1.00 28.00 ? 140 ARG C NH1   1 
ATOM   5670 N  NH2   . ARG C 1 146 ? -10.907 50.054  -0.647  1.00 35.88 ? 140 ARG C NH2   1 
ATOM   5671 N  N     . GLY C 1 147 ? -16.036 52.531  6.468   1.00 49.34 ? 141 GLY C N     1 
ATOM   5672 C  CA    . GLY C 1 147 ? -16.267 53.142  7.789   1.00 48.75 ? 141 GLY C CA    1 
ATOM   5673 C  C     . GLY C 1 147 ? -16.803 54.542  7.645   1.00 50.43 ? 141 GLY C C     1 
ATOM   5674 O  O     . GLY C 1 147 ? -16.645 55.139  6.559   1.00 57.30 ? 141 GLY C O     1 
ATOM   5675 N  N     . SER C 1 148 ? -17.469 55.026  8.691   1.00 61.10 ? 142 SER C N     1 
ATOM   5676 C  CA    . SER C 1 148 ? -17.971 56.418  8.807   1.00 65.28 ? 142 SER C CA    1 
ATOM   5677 C  C     . SER C 1 148 ? -16.790 57.263  9.260   1.00 66.02 ? 142 SER C C     1 
ATOM   5678 O  O     . SER C 1 148 ? -16.165 56.923  10.281  1.00 78.69 ? 142 SER C O     1 
ATOM   5679 C  CB    . SER C 1 148 ? -19.132 56.527  9.762   1.00 68.83 ? 142 SER C CB    1 
ATOM   5680 O  OG    . SER C 1 148 ? -18.678 56.554  11.107  1.00 67.12 ? 142 SER C OG    1 
ATOM   5681 N  N     . GLY C 1 149 ? -16.460 58.288  8.500   1.00 57.34 ? 143 GLY C N     1 
ATOM   5682 C  CA    . GLY C 1 149 ? -15.210 59.022  8.725   1.00 57.34 ? 143 GLY C CA    1 
ATOM   5683 C  C     . GLY C 1 149 ? -15.153 60.203  7.799   1.00 55.67 ? 143 GLY C C     1 
ATOM   5684 O  O     . GLY C 1 149 ? -15.981 60.271  6.859   1.00 56.49 ? 143 GLY C O     1 
ATOM   5685 N  N     . ASP C 1 150 ? -14.226 61.112  8.052   1.00 49.31 ? 144 ASP C N     1 
ATOM   5686 C  CA    . ASP C 1 150 ? -13.888 62.115  7.025   1.00 58.20 ? 144 ASP C CA    1 
ATOM   5687 C  C     . ASP C 1 150 ? -12.697 61.521  6.271   1.00 49.01 ? 144 ASP C C     1 
ATOM   5688 O  O     . ASP C 1 150 ? -11.623 62.151  6.263   1.00 46.65 ? 144 ASP C O     1 
ATOM   5689 C  CB    . ASP C 1 150 ? -13.764 63.521  7.614   1.00 64.83 ? 144 ASP C CB    1 
ATOM   5690 C  CG    . ASP C 1 150 ? -14.347 64.579  6.687   1.00 77.38 ? 144 ASP C CG    1 
ATOM   5691 O  OD1   . ASP C 1 150 ? -14.662 64.230  5.510   1.00 78.66 ? 144 ASP C OD1   1 
ATOM   5692 O  OD2   . ASP C 1 150 ? -14.491 65.742  7.140   1.00 80.44 ? 144 ASP C OD2   1 
ATOM   5693 N  N     . ASN C 1 151 ? -12.925 60.323  5.702   1.00 53.98 ? 145 ASN C N     1 
ATOM   5694 C  CA    . ASN C 1 151 ? -12.093 59.680  4.647   1.00 53.22 ? 145 ASN C CA    1 
ATOM   5695 C  C     . ASN C 1 151 ? -11.662 60.795  3.700   1.00 45.55 ? 145 ASN C C     1 
ATOM   5696 O  O     . ASN C 1 151 ? -10.456 60.957  3.455   1.00 44.31 ? 145 ASN C O     1 
ATOM   5697 C  CB    . ASN C 1 151 ? -12.850 58.593  3.866   1.00 56.75 ? 145 ASN C CB    1 
ATOM   5698 C  CG    . ASN C 1 151 ? -13.064 57.279  4.603   1.00 64.44 ? 145 ASN C CG    1 
ATOM   5699 O  OD1   . ASN C 1 151 ? -12.897 57.170  5.816   1.00 70.72 ? 145 ASN C OD1   1 
ATOM   5700 N  ND2   . ASN C 1 151 ? -13.473 56.257  3.872   1.00 69.30 ? 145 ASN C ND2   1 
ATOM   5701 N  N     . VAL C 1 152 ? -12.632 61.569  3.218   1.00 42.79 ? 146 VAL C N     1 
ATOM   5702 C  CA    . VAL C 1 152 ? -12.398 62.568  2.141   1.00 43.45 ? 146 VAL C CA    1 
ATOM   5703 C  C     . VAL C 1 152 ? -11.472 63.678  2.654   1.00 44.34 ? 146 VAL C C     1 
ATOM   5704 O  O     . VAL C 1 152 ? -10.601 64.080  1.876   1.00 36.55 ? 146 VAL C O     1 
ATOM   5705 C  CB    . VAL C 1 152 ? -13.708 63.117  1.542   1.00 41.10 ? 146 VAL C CB    1 
ATOM   5706 C  CG1   . VAL C 1 152 ? -13.412 64.169  0.487   1.00 42.65 ? 146 VAL C CG1   1 
ATOM   5707 C  CG2   . VAL C 1 152 ? -14.576 61.999  0.977   1.00 43.57 ? 146 VAL C CG2   1 
ATOM   5708 N  N     . GLN C 1 153 ? -11.628 64.181  3.892   1.00 46.05 ? 147 GLN C N     1 
ATOM   5709 C  CA    . GLN C 1 153 ? -10.692 65.215  4.421   1.00 45.25 ? 147 GLN C CA    1 
ATOM   5710 C  C     . GLN C 1 153 ? -9.281  64.624  4.566   1.00 37.72 ? 147 GLN C C     1 
ATOM   5711 O  O     . GLN C 1 153 ? -8.314  65.335  4.284   1.00 34.29 ? 147 GLN C O     1 
ATOM   5712 C  CB    . GLN C 1 153 ? -11.144 65.761  5.778   1.00 56.88 ? 147 GLN C CB    1 
ATOM   5713 C  CG    . GLN C 1 153 ? -11.948 67.053  5.676   1.00 69.64 ? 147 GLN C CG    1 
ATOM   5714 C  CD    . GLN C 1 153 ? -11.908 67.885  6.939   1.00 81.30 ? 147 GLN C CD    1 
ATOM   5715 O  OE1   . GLN C 1 153 ? -11.375 67.473  7.973   1.00 86.48 ? 147 GLN C OE1   1 
ATOM   5716 N  NE2   . GLN C 1 153 ? -12.469 69.084  6.859   1.00 81.98 ? 147 GLN C NE2   1 
ATOM   5717 N  N     . LYS C 1 154 ? -9.174  63.382  5.029   1.00 36.10 ? 148 LYS C N     1 
ATOM   5718 C  CA    . LYS C 1 154 ? -7.866  62.688  5.190   1.00 37.19 ? 148 LYS C CA    1 
ATOM   5719 C  C     . LYS C 1 154 ? -7.180  62.588  3.827   1.00 35.16 ? 148 LYS C C     1 
ATOM   5720 O  O     . LYS C 1 154 ? -5.962  62.734  3.743   1.00 35.71 ? 148 LYS C O     1 
ATOM   5721 C  CB    . LYS C 1 154 ? -8.051  61.289  5.780   1.00 36.40 ? 148 LYS C CB    1 
ATOM   5722 C  CG    . LYS C 1 154 ? -6.776  60.600  6.250   1.00 36.91 ? 148 LYS C CG    1 
ATOM   5723 C  CD    . LYS C 1 154 ? -5.891  61.492  7.121   1.00 39.48 ? 148 LYS C CD    1 
ATOM   5724 C  CE    . LYS C 1 154 ? -4.556  60.862  7.475   1.00 39.94 ? 148 LYS C CE    1 
ATOM   5725 N  NZ    . LYS C 1 154 ? -4.715  59.688  8.364   1.00 38.45 ? 148 LYS C NZ    1 
ATOM   5726 N  N     . LEU C 1 155 ? -7.964  62.329  2.781   1.00 39.71 ? 149 LEU C N     1 
ATOM   5727 C  CA    . LEU C 1 155 ? -7.456  62.124  1.401   1.00 34.77 ? 149 LEU C CA    1 
ATOM   5728 C  C     . LEU C 1 155 ? -6.820  63.416  0.899   1.00 33.33 ? 149 LEU C C     1 
ATOM   5729 O  O     . LEU C 1 155 ? -5.700  63.343  0.384   1.00 34.74 ? 149 LEU C O     1 
ATOM   5730 C  CB    . LEU C 1 155 ? -8.635  61.668  0.532   1.00 35.10 ? 149 LEU C CB    1 
ATOM   5731 C  CG    . LEU C 1 155 ? -8.316  61.358  -0.923  1.00 36.80 ? 149 LEU C CG    1 
ATOM   5732 C  CD1   . LEU C 1 155 ? -7.242  60.278  -1.006  1.00 37.54 ? 149 LEU C CD1   1 
ATOM   5733 C  CD2   . LEU C 1 155 ? -9.582  60.948  -1.665  1.00 37.35 ? 149 LEU C CD2   1 
ATOM   5734 N  N     . TYR C 1 156 ? -7.494  64.573  1.052   1.00 34.28 ? 150 TYR C N     1 
ATOM   5735 C  CA    . TYR C 1 156 ? -6.945  65.900  0.653   1.00 33.26 ? 150 TYR C CA    1 
ATOM   5736 C  C     . TYR C 1 156 ? -5.696  66.193  1.506   1.00 33.28 ? 150 TYR C C     1 
ATOM   5737 O  O     . TYR C 1 156 ? -4.686  66.684  0.979   1.00 34.10 ? 150 TYR C O     1 
ATOM   5738 C  CB    . TYR C 1 156 ? -8.028  66.994  0.712   1.00 37.21 ? 150 TYR C CB    1 
ATOM   5739 C  CG    . TYR C 1 156 ? -8.995  67.024  -0.458  1.00 34.05 ? 150 TYR C CG    1 
ATOM   5740 C  CD1   . TYR C 1 156 ? -10.132 66.240  -0.463  1.00 37.72 ? 150 TYR C CD1   1 
ATOM   5741 C  CD2   . TYR C 1 156 ? -8.799  67.859  -1.547  1.00 39.90 ? 150 TYR C CD2   1 
ATOM   5742 C  CE1   . TYR C 1 156 ? -11.016 66.240  -1.534  1.00 38.09 ? 150 TYR C CE1   1 
ATOM   5743 C  CE2   . TYR C 1 156 ? -9.673  67.877  -2.627  1.00 39.17 ? 150 TYR C CE2   1 
ATOM   5744 C  CZ    . TYR C 1 156 ? -10.796 67.065  -2.624  1.00 42.69 ? 150 TYR C CZ    1 
ATOM   5745 O  OH    . TYR C 1 156 ? -11.701 67.051  -3.666  1.00 42.52 ? 150 TYR C OH    1 
ATOM   5746 N  N     . GLU C 1 157 ? -5.731  65.861  2.794   1.00 36.64 ? 151 GLU C N     1 
ATOM   5747 C  CA    . GLU C 1 157 ? -4.550  66.060  3.687   1.00 39.81 ? 151 GLU C CA    1 
ATOM   5748 C  C     . GLU C 1 157 ? -3.362  65.247  3.145   1.00 34.67 ? 151 GLU C C     1 
ATOM   5749 O  O     . GLU C 1 157 ? -2.265  65.809  2.964   1.00 29.96 ? 151 GLU C O     1 
ATOM   5750 C  CB    . GLU C 1 157 ? -4.916  65.661  5.113   1.00 44.30 ? 151 GLU C CB    1 
ATOM   5751 C  CG    . GLU C 1 157 ? -4.169  66.455  6.161   1.00 55.96 ? 151 GLU C CG    1 
ATOM   5752 C  CD    . GLU C 1 157 ? -4.589  66.133  7.583   1.00 58.43 ? 151 GLU C CD    1 
ATOM   5753 O  OE1   . GLU C 1 157 ? -5.281  65.113  7.777   1.00 56.12 ? 151 GLU C OE1   1 
ATOM   5754 O  OE2   . GLU C 1 157 ? -4.219  66.902  8.485   1.00 62.74 ? 151 GLU C OE2   1 
ATOM   5755 N  N     . ILE C 1 158 ? -3.589  63.968  2.804   1.00 31.61 ? 152 ILE C N     1 
ATOM   5756 C  CA    . ILE C 1 158 ? -2.491  63.098  2.283   1.00 29.95 ? 152 ILE C CA    1 
ATOM   5757 C  C     . ILE C 1 158 ? -1.985  63.673  0.961   1.00 28.28 ? 152 ILE C C     1 
ATOM   5758 O  O     . ILE C 1 158 ? -0.765  63.753  0.768   1.00 24.99 ? 152 ILE C O     1 
ATOM   5759 C  CB    . ILE C 1 158 ? -2.949  61.633  2.174   1.00 28.82 ? 152 ILE C CB    1 
ATOM   5760 C  CG1   . ILE C 1 158 ? -3.186  61.039  3.561   1.00 29.00 ? 152 ILE C CG1   1 
ATOM   5761 C  CG2   . ILE C 1 158 ? -1.951  60.837  1.357   1.00 30.36 ? 152 ILE C CG2   1 
ATOM   5762 C  CD1   . ILE C 1 158 ? -3.900  59.709  3.553   1.00 28.90 ? 152 ILE C CD1   1 
ATOM   5763 N  N     . GLY C 1 159 ? -2.887  64.105  0.081   1.00 30.77 ? 153 GLY C N     1 
ATOM   5764 C  CA    . GLY C 1 159 ? -2.480  64.707  -1.198  1.00 33.63 ? 153 GLY C CA    1 
ATOM   5765 C  C     . GLY C 1 159 ? -1.544  65.885  -0.974  1.00 34.12 ? 153 GLY C C     1 
ATOM   5766 O  O     . GLY C 1 159 ? -0.537  65.992  -1.657  1.00 33.63 ? 153 GLY C O     1 
ATOM   5767 N  N     . SER C 1 160 ? -1.869  66.747  -0.018  1.00 38.11 ? 154 SER C N     1 
ATOM   5768 C  CA    . SER C 1 160 ? -1.061  67.945  0.332   1.00 39.75 ? 154 SER C CA    1 
ATOM   5769 C  C     . SER C 1 160 ? 0.306   67.513  0.871   1.00 33.07 ? 154 SER C C     1 
ATOM   5770 O  O     . SER C 1 160 ? 1.312   68.054  0.423   1.00 31.87 ? 154 SER C O     1 
ATOM   5771 C  CB    . SER C 1 160 ? -1.821  68.795  1.331   1.00 43.78 ? 154 SER C CB    1 
ATOM   5772 O  OG    . SER C 1 160 ? -1.061  69.935  1.675   1.00 52.59 ? 154 SER C OG    1 
ATOM   5773 N  N     . TRP C 1 161 ? 0.347   66.485  1.725   1.00 33.32 ? 155 TRP C N     1 
ATOM   5774 C  CA    . TRP C 1 161 ? 1.621   65.959  2.288   1.00 32.39 ? 155 TRP C CA    1 
ATOM   5775 C  C     . TRP C 1 161 ? 2.490   65.387  1.176   1.00 33.71 ? 155 TRP C C     1 
ATOM   5776 O  O     . TRP C 1 161 ? 3.706   65.542  1.242   1.00 32.02 ? 155 TRP C O     1 
ATOM   5777 C  CB    . TRP C 1 161 ? 1.368   64.902  3.357   1.00 34.93 ? 155 TRP C CB    1 
ATOM   5778 C  CG    . TRP C 1 161 ? 0.678   65.398  4.583   1.00 35.37 ? 155 TRP C CG    1 
ATOM   5779 C  CD1   . TRP C 1 161 ? 0.632   66.682  5.044   1.00 37.70 ? 155 TRP C CD1   1 
ATOM   5780 C  CD2   . TRP C 1 161 ? -0.024  64.597  5.542   1.00 35.45 ? 155 TRP C CD2   1 
ATOM   5781 N  NE1   . TRP C 1 161 ? -0.088  66.735  6.201   1.00 36.55 ? 155 TRP C NE1   1 
ATOM   5782 C  CE2   . TRP C 1 161 ? -0.512  65.478  6.525   1.00 35.47 ? 155 TRP C CE2   1 
ATOM   5783 C  CE3   . TRP C 1 161 ? -0.349  63.239  5.629   1.00 31.70 ? 155 TRP C CE3   1 
ATOM   5784 C  CZ2   . TRP C 1 161 ? -1.271  65.035  7.598   1.00 32.86 ? 155 TRP C CZ2   1 
ATOM   5785 C  CZ3   . TRP C 1 161 ? -1.083  62.797  6.702   1.00 33.67 ? 155 TRP C CZ3   1 
ATOM   5786 C  CH2   . TRP C 1 161 ? -1.556  63.691  7.665   1.00 33.18 ? 155 TRP C CH2   1 
ATOM   5787 N  N     . CYS C 1 162 ? 1.898   64.708  0.192   1.00 32.36 ? 156 CYS C N     1 
ATOM   5788 C  CA    . CYS C 1 162 ? 2.685   64.140  -0.943  1.00 31.94 ? 156 CYS C CA    1 
ATOM   5789 C  C     . CYS C 1 162 ? 3.362   65.270  -1.709  1.00 32.70 ? 156 CYS C C     1 
ATOM   5790 O  O     . CYS C 1 162 ? 4.550   65.130  -2.063  1.00 28.30 ? 156 CYS C O     1 
ATOM   5791 C  CB    . CYS C 1 162 ? 1.810   63.298  -1.860  1.00 32.38 ? 156 CYS C CB    1 
ATOM   5792 S  SG    . CYS C 1 162 ? 1.383   61.714  -1.084  1.00 31.04 ? 156 CYS C SG    1 
ATOM   5793 N  N     . GLN C 1 163 ? 2.629   66.363  -1.948  1.00 36.19 ? 157 GLN C N     1 
ATOM   5794 C  CA    . GLN C 1 163 ? 3.207   67.553  -2.625  1.00 41.05 ? 157 GLN C CA    1 
ATOM   5795 C  C     . GLN C 1 163 ? 4.324   68.149  -1.749  1.00 39.43 ? 157 GLN C C     1 
ATOM   5796 O  O     . GLN C 1 163 ? 5.439   68.334  -2.276  1.00 37.11 ? 157 GLN C O     1 
ATOM   5797 C  CB    . GLN C 1 163 ? 2.089   68.541  -2.918  1.00 42.77 ? 157 GLN C CB    1 
ATOM   5798 C  CG    . GLN C 1 163 ? 2.590   69.776  -3.634  1.00 51.90 ? 157 GLN C CG    1 
ATOM   5799 C  CD    . GLN C 1 163 ? 1.425   70.679  -3.931  1.00 56.14 ? 157 GLN C CD    1 
ATOM   5800 O  OE1   . GLN C 1 163 ? 1.576   71.692  -4.602  1.00 64.48 ? 157 GLN C OE1   1 
ATOM   5801 N  NE2   . GLN C 1 163 ? 0.249   70.303  -3.443  1.00 56.26 ? 157 GLN C NE2   1 
ATOM   5802 N  N     . LYS C 1 164 ? 4.058   68.342  -0.450  1.00 41.17 ? 158 LYS C N     1 
ATOM   5803 C  CA    . LYS C 1 164 ? 5.049   68.895  0.527   1.00 42.88 ? 158 LYS C CA    1 
ATOM   5804 C  C     . LYS C 1 164 ? 6.322   68.032  0.568   1.00 42.08 ? 158 LYS C C     1 
ATOM   5805 O  O     . LYS C 1 164 ? 7.382   68.632  0.627   1.00 35.24 ? 158 LYS C O     1 
ATOM   5806 C  CB    . LYS C 1 164 ? 4.470   69.052  1.943   1.00 47.40 ? 158 LYS C CB    1 
ATOM   5807 C  CG    . LYS C 1 164 ? 5.406   69.748  2.939   1.00 52.50 ? 158 LYS C CG    1 
ATOM   5808 C  CD    . LYS C 1 164 ? 5.018   69.658  4.413   1.00 57.37 ? 158 LYS C CD    1 
ATOM   5809 C  CE    . LYS C 1 164 ? 3.728   70.357  4.782   1.00 65.19 ? 158 LYS C CE    1 
ATOM   5810 N  NZ    . LYS C 1 164 ? 3.780   71.813  4.505   1.00 72.99 ? 158 LYS C NZ    1 
ATOM   5811 N  N     . TYR C 1 165 ? 6.256   66.686  0.561   1.00 40.38 ? 159 TYR C N     1 
ATOM   5812 C  CA    . TYR C 1 165 ? 7.472   65.830  0.688   1.00 37.00 ? 159 TYR C CA    1 
ATOM   5813 C  C     . TYR C 1 165 ? 7.869   65.166  -0.633  1.00 36.50 ? 159 TYR C C     1 
ATOM   5814 O  O     . TYR C 1 165 ? 8.699   64.265  -0.587  1.00 35.68 ? 159 TYR C O     1 
ATOM   5815 C  CB    . TYR C 1 165 ? 7.305   64.796  1.804   1.00 37.06 ? 159 TYR C CB    1 
ATOM   5816 C  CG    . TYR C 1 165 ? 7.064   65.451  3.127   1.00 37.35 ? 159 TYR C CG    1 
ATOM   5817 C  CD1   . TYR C 1 165 ? 8.090   66.133  3.771   1.00 39.48 ? 159 TYR C CD1   1 
ATOM   5818 C  CD2   . TYR C 1 165 ? 5.794   65.512  3.663   1.00 34.59 ? 159 TYR C CD2   1 
ATOM   5819 C  CE1   . TYR C 1 165 ? 7.859   66.819  4.949   1.00 39.01 ? 159 TYR C CE1   1 
ATOM   5820 C  CE2   . TYR C 1 165 ? 5.546   66.187  4.843   1.00 41.68 ? 159 TYR C CE2   1 
ATOM   5821 C  CZ    . TYR C 1 165 ? 6.585   66.844  5.487   1.00 40.21 ? 159 TYR C CZ    1 
ATOM   5822 O  OH    . TYR C 1 165 ? 6.336   67.484  6.657   1.00 43.61 ? 159 TYR C OH    1 
ATOM   5823 N  N     . ASP C 1 166 ? 7.350   65.621  -1.775  1.00 33.04 ? 160 ASP C N     1 
ATOM   5824 C  CA    . ASP C 1 166 ? 7.878   65.220  -3.105  1.00 37.49 ? 160 ASP C CA    1 
ATOM   5825 C  C     . ASP C 1 166 ? 7.527   63.748  -3.390  1.00 32.87 ? 160 ASP C C     1 
ATOM   5826 O  O     . ASP C 1 166 ? 8.370   62.981  -3.854  1.00 31.21 ? 160 ASP C O     1 
ATOM   5827 C  CB    . ASP C 1 166 ? 9.388   65.454  -3.151  1.00 40.54 ? 160 ASP C CB    1 
ATOM   5828 C  CG    . ASP C 1 166 ? 9.978   65.306  -4.534  1.00 49.29 ? 160 ASP C CG    1 
ATOM   5829 O  OD1   . ASP C 1 166 ? 9.253   65.617  -5.510  1.00 57.56 ? 160 ASP C OD1   1 
ATOM   5830 O  OD2   . ASP C 1 166 ? 11.148  64.868  -4.628  1.00 58.06 ? 160 ASP C OD2   1 
ATOM   5831 N  N     . ILE C 1 167 ? 6.320   63.337  -3.055  1.00 32.37 ? 161 ILE C N     1 
ATOM   5832 C  CA    . ILE C 1 167 ? 5.872   61.938  -3.308  1.00 29.36 ? 161 ILE C CA    1 
ATOM   5833 C  C     . ILE C 1 167 ? 4.791   62.018  -4.392  1.00 28.27 ? 161 ILE C C     1 
ATOM   5834 O  O     . ILE C 1 167 ? 3.911   62.868  -4.296  1.00 27.05 ? 161 ILE C O     1 
ATOM   5835 C  CB    . ILE C 1 167 ? 5.386   61.276  -2.015  1.00 31.09 ? 161 ILE C CB    1 
ATOM   5836 C  CG1   . ILE C 1 167 ? 6.482   61.212  -0.944  1.00 30.46 ? 161 ILE C CG1   1 
ATOM   5837 C  CG2   . ILE C 1 167 ? 4.768   59.904  -2.293  1.00 26.97 ? 161 ILE C CG2   1 
ATOM   5838 C  CD1   . ILE C 1 167 ? 5.893   61.128  0.452   1.00 29.88 ? 161 ILE C CD1   1 
ATOM   5839 N  N     . LYS C 1 168 ? 4.822   61.110  -5.356  1.00 25.71 ? 162 LYS C N     1 
ATOM   5840 C  CA    . LYS C 1 168 ? 3.766   61.043  -6.394  1.00 27.76 ? 162 LYS C CA    1 
ATOM   5841 C  C     . LYS C 1 168 ? 2.498   60.478  -5.769  1.00 25.11 ? 162 LYS C C     1 
ATOM   5842 O  O     . LYS C 1 168 ? 2.569   59.442  -5.110  1.00 25.74 ? 162 LYS C O     1 
ATOM   5843 C  CB    . LYS C 1 168 ? 4.262   60.237  -7.585  1.00 28.90 ? 162 LYS C CB    1 
ATOM   5844 C  CG    . LYS C 1 168 ? 5.524   60.824  -8.196  1.00 31.96 ? 162 LYS C CG    1 
ATOM   5845 C  CD    . LYS C 1 168 ? 6.238   59.858  -9.073  1.00 36.32 ? 162 LYS C CD    1 
ATOM   5846 C  CE    . LYS C 1 168 ? 5.434   59.475  -10.285 1.00 39.07 ? 162 LYS C CE    1 
ATOM   5847 N  NZ    . LYS C 1 168 ? 5.091   60.663  -11.080 1.00 43.04 ? 162 LYS C NZ    1 
ATOM   5848 N  N     . PHE C 1 169 ? 1.378   61.159  -5.981  1.00 24.55 ? 163 PHE C N     1 
ATOM   5849 C  CA    . PHE C 1 169 ? 0.087   60.865  -5.324  1.00 24.03 ? 163 PHE C CA    1 
ATOM   5850 C  C     . PHE C 1 169 ? -0.809  60.087  -6.288  1.00 22.48 ? 163 PHE C C     1 
ATOM   5851 O  O     . PHE C 1 169 ? -1.080  60.539  -7.424  1.00 22.12 ? 163 PHE C O     1 
ATOM   5852 C  CB    . PHE C 1 169 ? -0.553  62.181  -4.895  1.00 24.67 ? 163 PHE C CB    1 
ATOM   5853 C  CG    . PHE C 1 169 ? -1.904  62.055  -4.253  1.00 27.49 ? 163 PHE C CG    1 
ATOM   5854 C  CD1   . PHE C 1 169 ? -2.090  61.253  -3.138  1.00 27.50 ? 163 PHE C CD1   1 
ATOM   5855 C  CD2   . PHE C 1 169 ? -2.971  62.794  -4.720  1.00 30.75 ? 163 PHE C CD2   1 
ATOM   5856 C  CE1   . PHE C 1 169 ? -3.326  61.154  -2.522  1.00 29.92 ? 163 PHE C CE1   1 
ATOM   5857 C  CE2   . PHE C 1 169 ? -4.212  62.688  -4.105  1.00 32.02 ? 163 PHE C CE2   1 
ATOM   5858 C  CZ    . PHE C 1 169 ? -4.392  61.862  -3.017  1.00 31.73 ? 163 PHE C CZ    1 
ATOM   5859 N  N     . LYS C 1 170 ? -1.264  58.915  -5.849  1.00 21.98 ? 164 LYS C N     1 
ATOM   5860 C  CA    . LYS C 1 170 ? -2.077  57.999  -6.675  1.00 20.59 ? 164 LYS C CA    1 
ATOM   5861 C  C     . LYS C 1 170 ? -3.351  57.658  -5.905  1.00 19.72 ? 164 LYS C C     1 
ATOM   5862 O  O     . LYS C 1 170 ? -3.296  57.538  -4.681  1.00 20.57 ? 164 LYS C O     1 
ATOM   5863 C  CB    . LYS C 1 170 ? -1.209  56.778  -7.007  1.00 21.32 ? 164 LYS C CB    1 
ATOM   5864 C  CG    . LYS C 1 170 ? -1.944  55.511  -7.421  1.00 21.50 ? 164 LYS C CG    1 
ATOM   5865 C  CD    . LYS C 1 170 ? -0.961  54.399  -7.756  1.00 21.05 ? 164 LYS C CD    1 
ATOM   5866 C  CE    . LYS C 1 170 ? -1.597  53.027  -7.924  1.00 22.99 ? 164 LYS C CE    1 
ATOM   5867 N  NZ    . LYS C 1 170 ? -0.626  51.943  -7.620  1.00 23.92 ? 164 LYS C NZ    1 
ATOM   5868 N  N     . LEU C 1 171 ? -4.450  57.459  -6.615  1.00 20.22 ? 165 LEU C N     1 
ATOM   5869 C  CA    . LEU C 1 171 ? -5.770  57.100  -6.040  1.00 22.39 ? 165 LEU C CA    1 
ATOM   5870 C  C     . LEU C 1 171 ? -6.215  55.750  -6.618  1.00 19.98 ? 165 LEU C C     1 
ATOM   5871 O  O     . LEU C 1 171 ? -6.051  55.537  -7.821  1.00 21.04 ? 165 LEU C O     1 
ATOM   5872 C  CB    . LEU C 1 171 ? -6.713  58.248  -6.414  1.00 25.16 ? 165 LEU C CB    1 
ATOM   5873 C  CG    . LEU C 1 171 ? -8.122  58.218  -5.853  1.00 31.46 ? 165 LEU C CG    1 
ATOM   5874 C  CD1   . LEU C 1 171 ? -8.129  58.407  -4.337  1.00 39.60 ? 165 LEU C CD1   1 
ATOM   5875 C  CD2   . LEU C 1 171 ? -8.978  59.288  -6.531  1.00 34.43 ? 165 LEU C CD2   1 
ATOM   5876 N  N     . ASN C 1 172 ? -6.756  54.887  -5.775  1.00 21.73 ? 166 ASN C N     1 
ATOM   5877 C  CA    . ASN C 1 172 ? -7.291  53.547  -6.121  1.00 20.86 ? 166 ASN C CA    1 
ATOM   5878 C  C     . ASN C 1 172 ? -8.779  53.548  -5.773  1.00 21.66 ? 166 ASN C C     1 
ATOM   5879 O  O     . ASN C 1 172 ? -9.104  53.821  -4.604  1.00 21.27 ? 166 ASN C O     1 
ATOM   5880 C  CB    . ASN C 1 172 ? -6.567  52.445  -5.354  1.00 20.66 ? 166 ASN C CB    1 
ATOM   5881 C  CG    . ASN C 1 172 ? -5.184  52.138  -5.902  1.00 22.81 ? 166 ASN C CG    1 
ATOM   5882 O  OD1   . ASN C 1 172 ? -4.652  52.897  -6.712  1.00 24.70 ? 166 ASN C OD1   1 
ATOM   5883 N  ND2   . ASN C 1 172 ? -4.608  51.016  -5.513  1.00 20.88 ? 166 ASN C ND2   1 
ATOM   5884 N  N     . THR C 1 173 ? -9.624  53.197  -6.740  1.00 20.11 ? 167 THR C N     1 
ATOM   5885 C  CA    . THR C 1 173 ? -11.088 53.075  -6.567  1.00 21.09 ? 167 THR C CA    1 
ATOM   5886 C  C     . THR C 1 173 ? -11.553 51.684  -6.991  1.00 21.00 ? 167 THR C C     1 
ATOM   5887 O  O     . THR C 1 173 ? -11.238 51.251  -8.113  1.00 25.34 ? 167 THR C O     1 
ATOM   5888 C  CB    . THR C 1 173 ? -11.801 54.163  -7.361  1.00 21.91 ? 167 THR C CB    1 
ATOM   5889 O  OG1   . THR C 1 173 ? -11.334 55.387  -6.811  1.00 22.88 ? 167 THR C OG1   1 
ATOM   5890 C  CG2   . THR C 1 173 ? -13.299 54.084  -7.283  1.00 22.03 ? 167 THR C CG2   1 
ATOM   5891 N  N     . VAL C 1 174 ? -12.287 51.000  -6.126  1.00 20.90 ? 168 VAL C N     1 
ATOM   5892 C  CA    . VAL C 1 174 ? -12.995 49.756  -6.489  1.00 20.90 ? 168 VAL C CA    1 
ATOM   5893 C  C     . VAL C 1 174 ? -14.400 50.137  -6.972  1.00 23.34 ? 168 VAL C C     1 
ATOM   5894 O  O     . VAL C 1 174 ? -15.183 50.659  -6.174  1.00 23.84 ? 168 VAL C O     1 
ATOM   5895 C  CB    . VAL C 1 174 ? -13.063 48.773  -5.315  1.00 20.88 ? 168 VAL C CB    1 
ATOM   5896 C  CG1   . VAL C 1 174 ? -13.903 47.581  -5.712  1.00 22.96 ? 168 VAL C CG1   1 
ATOM   5897 C  CG2   . VAL C 1 174 ? -11.675 48.338  -4.841  1.00 21.78 ? 168 VAL C CG2   1 
ATOM   5898 N  N     . VAL C 1 175 ? -14.705 49.833  -8.222  1.00 22.34 ? 169 VAL C N     1 
ATOM   5899 C  CA    . VAL C 1 175 ? -16.044 50.089  -8.809  1.00 23.31 ? 169 VAL C CA    1 
ATOM   5900 C  C     . VAL C 1 175 ? -16.915 48.873  -8.522  1.00 23.55 ? 169 VAL C C     1 
ATOM   5901 O  O     . VAL C 1 175 ? -16.555 47.757  -8.924  1.00 24.76 ? 169 VAL C O     1 
ATOM   5902 C  CB    . VAL C 1 175 ? -15.918 50.395  -10.305 1.00 23.99 ? 169 VAL C CB    1 
ATOM   5903 C  CG1   . VAL C 1 175 ? -17.282 50.841  -10.828 1.00 25.83 ? 169 VAL C CG1   1 
ATOM   5904 C  CG2   . VAL C 1 175 ? -14.837 51.454  -10.578 1.00 23.22 ? 169 VAL C CG2   1 
ATOM   5905 N  N     . ASN C 1 176 ? -17.992 49.096  -7.779  1.00 24.81 ? 170 ASN C N     1 
ATOM   5906 C  CA    . ASN C 1 176 ? -18.844 48.028  -7.230  1.00 26.81 ? 170 ASN C CA    1 
ATOM   5907 C  C     . ASN C 1 176 ? -20.293 48.496  -7.345  1.00 27.72 ? 170 ASN C C     1 
ATOM   5908 O  O     . ASN C 1 176 ? -20.516 49.639  -7.790  1.00 29.33 ? 170 ASN C O     1 
ATOM   5909 C  CB    . ASN C 1 176 ? -18.408 47.718  -5.795  1.00 25.48 ? 170 ASN C CB    1 
ATOM   5910 C  CG    . ASN C 1 176 ? -18.546 48.915  -4.882  1.00 28.29 ? 170 ASN C CG    1 
ATOM   5911 O  OD1   . ASN C 1 176 ? -19.636 49.153  -4.378  1.00 36.37 ? 170 ASN C OD1   1 
ATOM   5912 N  ND2   . ASN C 1 176 ? -17.477 49.668  -4.633  1.00 25.84 ? 170 ASN C ND2   1 
ATOM   5913 N  N     . LYS C 1 177 ? -21.213 47.665  -6.862  1.00 32.16 ? 171 LYS C N     1 
ATOM   5914 C  CA    . LYS C 1 177 ? -22.688 47.863  -6.963  1.00 36.13 ? 171 LYS C CA    1 
ATOM   5915 C  C     . LYS C 1 177 ? -23.077 49.208  -6.354  1.00 36.92 ? 171 LYS C C     1 
ATOM   5916 O  O     . LYS C 1 177 ? -24.074 49.797  -6.820  1.00 37.37 ? 171 LYS C O     1 
ATOM   5917 C  CB    . LYS C 1 177 ? -23.443 46.756  -6.212  1.00 42.45 ? 171 LYS C CB    1 
ATOM   5918 C  CG    . LYS C 1 177 ? -24.947 46.676  -6.472  1.00 50.16 ? 171 LYS C CG    1 
ATOM   5919 C  CD    . LYS C 1 177 ? -25.315 46.031  -7.810  1.00 57.64 ? 171 LYS C CD    1 
ATOM   5920 C  CE    . LYS C 1 177 ? -25.880 47.008  -8.830  1.00 64.36 ? 171 LYS C CE    1 
ATOM   5921 N  NZ    . LYS C 1 177 ? -26.290 46.344  -10.097 1.00 62.87 ? 171 LYS C NZ    1 
ATOM   5922 N  N     . PHE C 1 178 ? -22.349 49.667  -5.334  1.00 35.60 ? 172 PHE C N     1 
ATOM   5923 C  CA    . PHE C 1 178 ? -22.770 50.823  -4.497  1.00 37.30 ? 172 PHE C CA    1 
ATOM   5924 C  C     . PHE C 1 178 ? -22.216 52.141  -5.016  1.00 37.76 ? 172 PHE C C     1 
ATOM   5925 O  O     . PHE C 1 178 ? -22.762 53.194  -4.601  1.00 34.39 ? 172 PHE C O     1 
ATOM   5926 C  CB    . PHE C 1 178 ? -22.380 50.631  -3.030  1.00 41.74 ? 172 PHE C CB    1 
ATOM   5927 C  CG    . PHE C 1 178 ? -23.139 49.532  -2.333  1.00 45.18 ? 172 PHE C CG    1 
ATOM   5928 C  CD1   . PHE C 1 178 ? -24.488 49.311  -2.604  1.00 49.80 ? 172 PHE C CD1   1 
ATOM   5929 C  CD2   . PHE C 1 178 ? -22.509 48.717  -1.409  1.00 44.66 ? 172 PHE C CD2   1 
ATOM   5930 C  CE1   . PHE C 1 178 ? -25.184 48.288  -1.972  1.00 52.84 ? 172 PHE C CE1   1 
ATOM   5931 C  CE2   . PHE C 1 178 ? -23.207 47.692  -0.782  1.00 48.01 ? 172 PHE C CE2   1 
ATOM   5932 C  CZ    . PHE C 1 178 ? -24.541 47.482  -1.062  1.00 51.09 ? 172 PHE C CZ    1 
ATOM   5933 N  N     . ASN C 1 179 ? -21.185 52.131  -5.873  1.00 31.21 ? 173 ASN C N     1 
ATOM   5934 C  CA    . ASN C 1 179 ? -20.634 53.409  -6.380  1.00 29.68 ? 173 ASN C CA    1 
ATOM   5935 C  C     . ASN C 1 179 ? -20.661 53.478  -7.908  1.00 29.41 ? 173 ASN C C     1 
ATOM   5936 O  O     . ASN C 1 179 ? -20.165 54.462  -8.397  1.00 30.48 ? 173 ASN C O     1 
ATOM   5937 C  CB    . ASN C 1 179 ? -19.233 53.639  -5.800  1.00 29.09 ? 173 ASN C CB    1 
ATOM   5938 C  CG    . ASN C 1 179 ? -18.229 52.606  -6.269  1.00 30.09 ? 173 ASN C CG    1 
ATOM   5939 O  OD1   . ASN C 1 179 ? -18.577 51.635  -6.951  1.00 28.03 ? 173 ASN C OD1   1 
ATOM   5940 N  ND2   . ASN C 1 179 ? -16.975 52.803  -5.892  1.00 27.99 ? 173 ASN C ND2   1 
ATOM   5941 N  N     . HIS C 1 180 ? -21.117 52.447  -8.647  1.00 31.97 ? 174 HIS C N     1 
ATOM   5942 C  CA    . HIS C 1 180 ? -20.921 52.352  -10.127 1.00 31.89 ? 174 HIS C CA    1 
ATOM   5943 C  C     . HIS C 1 180 ? -21.613 53.517  -10.844 1.00 33.59 ? 174 HIS C C     1 
ATOM   5944 O  O     . HIS C 1 180 ? -21.179 53.827  -11.974 1.00 30.09 ? 174 HIS C O     1 
ATOM   5945 C  CB    . HIS C 1 180 ? -21.329 50.992  -10.723 1.00 30.64 ? 174 HIS C CB    1 
ATOM   5946 C  CG    . HIS C 1 180 ? -22.792 50.707  -10.825 1.00 33.36 ? 174 HIS C CG    1 
ATOM   5947 N  ND1   . HIS C 1 180 ? -23.511 50.914  -11.994 1.00 32.19 ? 174 HIS C ND1   1 
ATOM   5948 C  CD2   . HIS C 1 180 ? -23.660 50.170  -9.945  1.00 34.94 ? 174 HIS C CD2   1 
ATOM   5949 C  CE1   . HIS C 1 180 ? -24.761 50.540  -11.812 1.00 35.63 ? 174 HIS C CE1   1 
ATOM   5950 N  NE2   . HIS C 1 180 ? -24.887 50.085  -10.565 1.00 34.53 ? 174 HIS C NE2   1 
ATOM   5951 N  N     . LEU C 1 181 ? -22.627 54.141  -10.230 1.00 33.13 ? 175 LEU C N     1 
ATOM   5952 C  CA    . LEU C 1 181 ? -23.339 55.294  -10.849 1.00 35.39 ? 175 LEU C CA    1 
ATOM   5953 C  C     . LEU C 1 181 ? -22.727 56.609  -10.369 1.00 32.88 ? 175 LEU C C     1 
ATOM   5954 O  O     . LEU C 1 181 ? -23.120 57.653  -10.896 1.00 36.23 ? 175 LEU C O     1 
ATOM   5955 C  CB    . LEU C 1 181 ? -24.841 55.228  -10.539 1.00 35.55 ? 175 LEU C CB    1 
ATOM   5956 C  CG    . LEU C 1 181 ? -25.548 54.020  -11.134 1.00 37.19 ? 175 LEU C CG    1 
ATOM   5957 C  CD1   . LEU C 1 181 ? -26.969 53.909  -10.593 1.00 42.78 ? 175 LEU C CD1   1 
ATOM   5958 C  CD2   . LEU C 1 181 ? -25.543 54.071  -12.651 1.00 34.43 ? 175 LEU C CD2   1 
ATOM   5959 N  N     . GLU C 1 182 ? -21.685 56.570  -9.533  1.00 32.99 ? 176 GLU C N     1 
ATOM   5960 C  CA    . GLU C 1 182 ? -21.129 57.805  -8.912  1.00 31.23 ? 176 GLU C CA    1 
ATOM   5961 C  C     . GLU C 1 182 ? -20.352 58.619  -9.954  1.00 32.64 ? 176 GLU C C     1 
ATOM   5962 O  O     . GLU C 1 182 ? -19.682 58.044  -10.830 1.00 31.99 ? 176 GLU C O     1 
ATOM   5963 C  CB    . GLU C 1 182 ? -20.267 57.463  -7.694  1.00 32.81 ? 176 GLU C CB    1 
ATOM   5964 C  CG    . GLU C 1 182 ? -19.827 58.676  -6.900  1.00 33.51 ? 176 GLU C CG    1 
ATOM   5965 C  CD    . GLU C 1 182 ? -19.205 58.421  -5.535  1.00 35.01 ? 176 GLU C CD    1 
ATOM   5966 O  OE1   . GLU C 1 182 ? -19.649 57.438  -4.857  1.00 32.41 ? 176 GLU C OE1   1 
ATOM   5967 O  OE2   . GLU C 1 182 ? -18.300 59.236  -5.126  1.00 34.95 ? 176 GLU C OE2   1 
ATOM   5968 N  N     . ASP C 1 183 ? -20.395 59.937  -9.818  1.00 31.08 ? 177 ASP C N     1 
ATOM   5969 C  CA    . ASP C 1 183 ? -19.631 60.904  -10.653 1.00 32.76 ? 177 ASP C CA    1 
ATOM   5970 C  C     . ASP C 1 183 ? -18.586 61.559  -9.751  1.00 33.29 ? 177 ASP C C     1 
ATOM   5971 O  O     . ASP C 1 183 ? -18.977 62.356  -8.882  1.00 34.69 ? 177 ASP C O     1 
ATOM   5972 C  CB    . ASP C 1 183 ? -20.552 61.944  -11.310 1.00 32.47 ? 177 ASP C CB    1 
ATOM   5973 C  CG    . ASP C 1 183 ? -19.790 62.928  -12.188 1.00 32.85 ? 177 ASP C CG    1 
ATOM   5974 O  OD1   . ASP C 1 183 ? -18.820 63.545  -11.683 1.00 34.34 ? 177 ASP C OD1   1 
ATOM   5975 O  OD2   . ASP C 1 183 ? -20.166 63.051  -13.378 1.00 35.18 ? 177 ASP C OD2   1 
ATOM   5976 N  N     . MET C 1 184 ? -17.298 61.266  -9.967  1.00 29.58 ? 178 MET C N     1 
ATOM   5977 C  CA    . MET C 1 184 ? -16.208 61.714  -9.070  1.00 30.34 ? 178 MET C CA    1 
ATOM   5978 C  C     . MET C 1 184 ? -15.350 62.784  -9.733  1.00 27.01 ? 178 MET C C     1 
ATOM   5979 O  O     . MET C 1 184 ? -14.311 63.118  -9.142  1.00 29.34 ? 178 MET C O     1 
ATOM   5980 C  CB    . MET C 1 184 ? -15.306 60.536  -8.680  1.00 33.82 ? 178 MET C CB    1 
ATOM   5981 C  CG    . MET C 1 184 ? -16.060 59.348  -8.142  1.00 36.21 ? 178 MET C CG    1 
ATOM   5982 S  SD    . MET C 1 184 ? -14.884 58.063  -7.614  1.00 34.96 ? 178 MET C SD    1 
ATOM   5983 C  CE    . MET C 1 184 ? -16.035 56.788  -7.117  1.00 33.90 ? 178 MET C CE    1 
ATOM   5984 N  N     . ASN C 1 185 ? -15.714 63.277  -10.920 1.00 27.15 ? 179 ASN C N     1 
ATOM   5985 C  CA    . ASN C 1 185 ? -14.846 64.224  -11.681 1.00 28.99 ? 179 ASN C CA    1 
ATOM   5986 C  C     . ASN C 1 185 ? -14.414 65.450  -10.842 1.00 31.63 ? 179 ASN C C     1 
ATOM   5987 O  O     . ASN C 1 185 ? -13.241 65.894  -10.990 1.00 27.67 ? 179 ASN C O     1 
ATOM   5988 C  CB    . ASN C 1 185 ? -15.520 64.696  -12.975 1.00 28.49 ? 179 ASN C CB    1 
ATOM   5989 C  CG    . ASN C 1 185 ? -15.643 63.567  -13.975 1.00 27.64 ? 179 ASN C CG    1 
ATOM   5990 O  OD1   . ASN C 1 185 ? -14.636 63.159  -14.547 1.00 24.61 ? 179 ASN C OD1   1 
ATOM   5991 N  ND2   . ASN C 1 185 ? -16.845 63.029  -14.138 1.00 25.16 ? 179 ASN C ND2   1 
ATOM   5992 N  N     . ASP C 1 186 ? -15.294 66.057  -10.044 1.00 35.46 ? 180 ASP C N     1 
ATOM   5993 C  CA    . ASP C 1 186 ? -14.937 67.330  -9.339  1.00 39.86 ? 180 ASP C CA    1 
ATOM   5994 C  C     . ASP C 1 186 ? -13.795 67.085  -8.341  1.00 37.83 ? 180 ASP C C     1 
ATOM   5995 O  O     . ASP C 1 186 ? -12.874 67.902  -8.257  1.00 32.41 ? 180 ASP C O     1 
ATOM   5996 C  CB    . ASP C 1 186 ? -16.121 67.896  -8.558  1.00 45.19 ? 180 ASP C CB    1 
ATOM   5997 C  CG    . ASP C 1 186 ? -17.260 68.368  -9.441  1.00 49.66 ? 180 ASP C CG    1 
ATOM   5998 O  OD1   . ASP C 1 186 ? -16.968 69.030  -10.454 1.00 49.89 ? 180 ASP C OD1   1 
ATOM   5999 O  OD2   . ASP C 1 186 ? -18.419 68.053  -9.107  1.00 53.25 ? 180 ASP C OD2   1 
ATOM   6000 N  N     . HIS C 1 187 ? -13.867 65.980  -7.609  1.00 37.15 ? 181 HIS C N     1 
ATOM   6001 C  CA    . HIS C 1 187 ? -12.830 65.590  -6.622  1.00 39.72 ? 181 HIS C CA    1 
ATOM   6002 C  C     . HIS C 1 187 ? -11.528 65.211  -7.329  1.00 33.62 ? 181 HIS C C     1 
ATOM   6003 O  O     . HIS C 1 187 ? -10.444 65.600  -6.843  1.00 33.71 ? 181 HIS C O     1 
ATOM   6004 C  CB    . HIS C 1 187 ? -13.386 64.476  -5.751  1.00 41.20 ? 181 HIS C CB    1 
ATOM   6005 C  CG    . HIS C 1 187 ? -14.388 64.977  -4.778  1.00 40.09 ? 181 HIS C CG    1 
ATOM   6006 N  ND1   . HIS C 1 187 ? -14.030 65.830  -3.768  1.00 40.29 ? 181 HIS C ND1   1 
ATOM   6007 C  CD2   . HIS C 1 187 ? -15.717 64.756  -4.657  1.00 44.75 ? 181 HIS C CD2   1 
ATOM   6008 C  CE1   . HIS C 1 187 ? -15.086 66.088  -3.025  1.00 41.22 ? 181 HIS C CE1   1 
ATOM   6009 N  NE2   . HIS C 1 187 ? -16.138 65.452  -3.553  1.00 40.13 ? 181 HIS C NE2   1 
ATOM   6010 N  N     . LEU C 1 188 ? -11.615 64.461  -8.429  1.00 34.02 ? 182 LEU C N     1 
ATOM   6011 C  CA    . LEU C 1 188 ? -10.411 64.098  -9.232  1.00 31.90 ? 182 LEU C CA    1 
ATOM   6012 C  C     . LEU C 1 188 ? -9.749  65.376  -9.774  1.00 31.52 ? 182 LEU C C     1 
ATOM   6013 O  O     . LEU C 1 188 ? -8.495  65.474  -9.720  1.00 29.86 ? 182 LEU C O     1 
ATOM   6014 C  CB    . LEU C 1 188 ? -10.800 63.112  -10.342 1.00 31.90 ? 182 LEU C CB    1 
ATOM   6015 C  CG    . LEU C 1 188 ? -10.705 61.633  -9.937  1.00 32.43 ? 182 LEU C CG    1 
ATOM   6016 C  CD1   . LEU C 1 188 ? -9.250  61.232  -9.717  1.00 31.12 ? 182 LEU C CD1   1 
ATOM   6017 C  CD2   . LEU C 1 188 ? -11.509 61.360  -8.676  1.00 32.01 ? 182 LEU C CD2   1 
ATOM   6018 N  N     . ASN C 1 189 ? -10.541 66.354  -10.231 1.00 31.62 ? 183 ASN C N     1 
ATOM   6019 C  CA    . ASN C 1 189 ? -9.995  67.634  -10.769 1.00 32.66 ? 183 ASN C CA    1 
ATOM   6020 C  C     . ASN C 1 189 ? -9.276  68.391  -9.637  1.00 33.75 ? 183 ASN C C     1 
ATOM   6021 O  O     . ASN C 1 189 ? -8.300  69.052  -9.933  1.00 35.09 ? 183 ASN C O     1 
ATOM   6022 C  CB    . ASN C 1 189 ? -11.066 68.493  -11.463 1.00 33.36 ? 183 ASN C CB    1 
ATOM   6023 C  CG    . ASN C 1 189 ? -11.687 67.834  -12.692 1.00 34.10 ? 183 ASN C CG    1 
ATOM   6024 O  OD1   . ASN C 1 189 ? -11.080 66.980  -13.319 1.00 34.56 ? 183 ASN C OD1   1 
ATOM   6025 N  ND2   . ASN C 1 189 ? -12.895 68.229  -13.071 1.00 32.14 ? 183 ASN C ND2   1 
ATOM   6026 N  N     . ALA C 1 190 ? -9.741  68.289  -8.387  1.00 35.52 ? 184 ALA C N     1 
ATOM   6027 C  CA    . ALA C 1 190 ? -9.125  68.957  -7.211  1.00 36.28 ? 184 ALA C CA    1 
ATOM   6028 C  C     . ALA C 1 190 ? -7.898  68.158  -6.734  1.00 37.94 ? 184 ALA C C     1 
ATOM   6029 O  O     . ALA C 1 190 ? -6.828  68.756  -6.509  1.00 35.97 ? 184 ALA C O     1 
ATOM   6030 C  CB    . ALA C 1 190 ? -10.153 69.113  -6.116  1.00 36.57 ? 184 ALA C CB    1 
ATOM   6031 N  N     . LEU C 1 191 ? -8.027  66.837  -6.601  1.00 34.95 ? 185 LEU C N     1 
ATOM   6032 C  CA    . LEU C 1 191 ? -6.947  65.984  -6.033  1.00 35.66 ? 185 LEU C CA    1 
ATOM   6033 C  C     . LEU C 1 191 ? -5.781  65.854  -7.006  1.00 32.67 ? 185 LEU C C     1 
ATOM   6034 O  O     . LEU C 1 191 ? -4.621  65.850  -6.522  1.00 31.54 ? 185 LEU C O     1 
ATOM   6035 C  CB    . LEU C 1 191 ? -7.531  64.628  -5.660  1.00 35.62 ? 185 LEU C CB    1 
ATOM   6036 C  CG    . LEU C 1 191 ? -8.283  64.636  -4.346  1.00 37.47 ? 185 LEU C CG    1 
ATOM   6037 C  CD1   . LEU C 1 191 ? -9.132  63.392  -4.209  1.00 42.49 ? 185 LEU C CD1   1 
ATOM   6038 C  CD2   . LEU C 1 191 ? -7.306  64.788  -3.188  1.00 40.13 ? 185 LEU C CD2   1 
ATOM   6039 N  N     . GLN C 1 192 ? -6.060  65.734  -8.307  1.00 30.36 ? 186 GLN C N     1 
ATOM   6040 C  CA    . GLN C 1 192 ? -5.027  65.694  -9.379  1.00 34.40 ? 186 GLN C CA    1 
ATOM   6041 C  C     . GLN C 1 192 ? -4.015  64.586  -9.104  1.00 34.00 ? 186 GLN C C     1 
ATOM   6042 O  O     . GLN C 1 192 ? -2.807  64.789  -9.190  1.00 31.26 ? 186 GLN C O     1 
ATOM   6043 C  CB    . GLN C 1 192 ? -4.363  67.059  -9.551  1.00 40.48 ? 186 GLN C CB    1 
ATOM   6044 C  CG    . GLN C 1 192 ? -5.222  67.982  -10.410 1.00 46.84 ? 186 GLN C CG    1 
ATOM   6045 C  CD    . GLN C 1 192 ? -4.802  69.430  -10.404 1.00 49.67 ? 186 GLN C CD    1 
ATOM   6046 O  OE1   . GLN C 1 192 ? -3.646  69.754  -10.639 1.00 52.99 ? 186 GLN C OE1   1 
ATOM   6047 N  NE2   . GLN C 1 192 ? -5.758  70.315  -10.145 1.00 53.43 ? 186 GLN C NE2   1 
ATOM   6048 N  N     . PRO C 1 193 ? -4.460  63.336  -8.875  1.00 27.95 ? 187 PRO C N     1 
ATOM   6049 C  CA    . PRO C 1 193 ? -3.503  62.238  -8.788  1.00 27.83 ? 187 PRO C CA    1 
ATOM   6050 C  C     . PRO C 1 193 ? -2.862  62.069  -10.166 1.00 27.10 ? 187 PRO C C     1 
ATOM   6051 O  O     . PRO C 1 193 ? -3.532  62.261  -11.185 1.00 25.76 ? 187 PRO C O     1 
ATOM   6052 C  CB    . PRO C 1 193 ? -4.372  61.055  -8.369  1.00 26.08 ? 187 PRO C CB    1 
ATOM   6053 C  CG    . PRO C 1 193 ? -5.692  61.347  -9.000  1.00 27.26 ? 187 PRO C CG    1 
ATOM   6054 C  CD    . PRO C 1 193 ? -5.843  62.861  -8.864  1.00 29.32 ? 187 PRO C CD    1 
ATOM   6055 N  N     . PHE C 1 194 ? -1.594  61.656  -10.221 1.00 24.35 ? 188 PHE C N     1 
ATOM   6056 C  CA    . PHE C 1 194 ? -0.968  61.340  -11.524 1.00 26.82 ? 188 PHE C CA    1 
ATOM   6057 C  C     . PHE C 1 194 ? -1.475  59.989  -12.079 1.00 27.07 ? 188 PHE C C     1 
ATOM   6058 O  O     . PHE C 1 194 ? -1.248  59.719  -13.254 1.00 26.71 ? 188 PHE C O     1 
ATOM   6059 C  CB    . PHE C 1 194 ? 0.545   61.336  -11.419 1.00 28.58 ? 188 PHE C CB    1 
ATOM   6060 C  CG    . PHE C 1 194 ? 1.096   60.010  -10.979 1.00 27.07 ? 188 PHE C CG    1 
ATOM   6061 C  CD1   . PHE C 1 194 ? 1.044   59.630  -9.647  1.00 27.22 ? 188 PHE C CD1   1 
ATOM   6062 C  CD2   . PHE C 1 194 ? 1.667   59.158  -11.899 1.00 25.57 ? 188 PHE C CD2   1 
ATOM   6063 C  CE1   . PHE C 1 194 ? 1.593   58.428  -9.231  1.00 25.85 ? 188 PHE C CE1   1 
ATOM   6064 C  CE2   . PHE C 1 194 ? 2.178   57.943  -11.492 1.00 26.76 ? 188 PHE C CE2   1 
ATOM   6065 C  CZ    . PHE C 1 194 ? 2.141   57.580  -10.159 1.00 24.27 ? 188 PHE C CZ    1 
ATOM   6066 N  N     . ARG C 1 195 ? -2.146  59.175  -11.256 1.00 25.39 ? 189 ARG C N     1 
ATOM   6067 C  CA    . ARG C 1 195 ? -2.533  57.782  -11.577 1.00 22.16 ? 189 ARG C CA    1 
ATOM   6068 C  C     . ARG C 1 195 ? -3.755  57.467  -10.738 1.00 22.01 ? 189 ARG C C     1 
ATOM   6069 O  O     . ARG C 1 195 ? -3.693  57.699  -9.511  1.00 20.66 ? 189 ARG C O     1 
ATOM   6070 C  CB    . ARG C 1 195 ? -1.372  56.838  -11.228 1.00 22.94 ? 189 ARG C CB    1 
ATOM   6071 C  CG    . ARG C 1 195 ? -1.488  55.434  -11.803 1.00 23.13 ? 189 ARG C CG    1 
ATOM   6072 C  CD    . ARG C 1 195 ? -0.160  54.738  -11.664 1.00 22.25 ? 189 ARG C CD    1 
ATOM   6073 N  NE    . ARG C 1 195 ? -0.145  53.353  -12.113 1.00 23.29 ? 189 ARG C NE    1 
ATOM   6074 C  CZ    . ARG C 1 195 ? -0.053  52.958  -13.377 1.00 22.96 ? 189 ARG C CZ    1 
ATOM   6075 N  NH1   . ARG C 1 195 ? -0.054  53.847  -14.366 1.00 21.77 ? 189 ARG C NH1   1 
ATOM   6076 N  NH2   . ARG C 1 195 ? 0.006   51.660  -13.643 1.00 20.62 ? 189 ARG C NH2   1 
ATOM   6077 N  N     . TRP C 1 196 ? -4.826  57.032  -11.393 1.00 18.91 ? 190 TRP C N     1 
ATOM   6078 C  CA    . TRP C 1 196 ? -6.122  56.730  -10.771 1.00 20.68 ? 190 TRP C CA    1 
ATOM   6079 C  C     . TRP C 1 196 ? -6.558  55.338  -11.221 1.00 21.03 ? 190 TRP C C     1 
ATOM   6080 O  O     . TRP C 1 196 ? -7.062  55.232  -12.309 1.00 19.96 ? 190 TRP C O     1 
ATOM   6081 C  CB    . TRP C 1 196 ? -7.177  57.781  -11.136 1.00 20.61 ? 190 TRP C CB    1 
ATOM   6082 C  CG    . TRP C 1 196 ? -8.501  57.494  -10.502 1.00 21.10 ? 190 TRP C CG    1 
ATOM   6083 C  CD1   . TRP C 1 196 ? -8.758  56.855  -9.319  1.00 22.08 ? 190 TRP C CD1   1 
ATOM   6084 C  CD2   . TRP C 1 196 ? -9.780  57.856  -11.045 1.00 24.22 ? 190 TRP C CD2   1 
ATOM   6085 N  NE1   . TRP C 1 196 ? -10.113 56.805  -9.086  1.00 22.19 ? 190 TRP C NE1   1 
ATOM   6086 C  CE2   . TRP C 1 196 ? -10.763 57.405  -10.137 1.00 22.83 ? 190 TRP C CE2   1 
ATOM   6087 C  CE3   . TRP C 1 196 ? -10.179 58.498  -12.223 1.00 28.11 ? 190 TRP C CE3   1 
ATOM   6088 C  CZ2   . TRP C 1 196 ? -12.123 57.588  -10.375 1.00 25.21 ? 190 TRP C CZ2   1 
ATOM   6089 C  CZ3   . TRP C 1 196 ? -11.526 58.711  -12.429 1.00 27.09 ? 190 TRP C CZ3   1 
ATOM   6090 C  CH2   . TRP C 1 196 ? -12.474 58.255  -11.518 1.00 24.52 ? 190 TRP C CH2   1 
ATOM   6091 N  N     . LYS C 1 197 ? -6.280  54.316  -10.431 1.00 19.96 ? 191 LYS C N     1 
ATOM   6092 C  CA    . LYS C 1 197 ? -6.712  52.946  -10.761 1.00 20.17 ? 191 LYS C CA    1 
ATOM   6093 C  C     . LYS C 1 197 ? -8.193  52.824  -10.478 1.00 20.52 ? 191 LYS C C     1 
ATOM   6094 O  O     . LYS C 1 197 ? -8.594  53.101  -9.351  1.00 22.17 ? 191 LYS C O     1 
ATOM   6095 C  CB    . LYS C 1 197 ? -5.977  51.898  -9.919  1.00 22.45 ? 191 LYS C CB    1 
ATOM   6096 C  CG    . LYS C 1 197 ? -4.475  51.937  -10.073 1.00 23.65 ? 191 LYS C CG    1 
ATOM   6097 C  CD    . LYS C 1 197 ? -3.978  51.500  -11.394 1.00 26.31 ? 191 LYS C CD    1 
ATOM   6098 C  CE    . LYS C 1 197 ? -2.577  50.929  -11.322 1.00 27.17 ? 191 LYS C CE    1 
ATOM   6099 N  NZ    . LYS C 1 197 ? -2.560  49.471  -11.094 1.00 26.46 ? 191 LYS C NZ    1 
ATOM   6100 N  N     . CYS C 1 198 ? -8.958  52.346  -11.452 1.00 20.54 ? 192 CYS C N     1 
ATOM   6101 C  CA    . CYS C 1 198 ? -10.372 51.968  -11.288 1.00 22.04 ? 192 CYS C CA    1 
ATOM   6102 C  C     . CYS C 1 198 ? -10.480 50.452  -11.499 1.00 21.49 ? 192 CYS C C     1 
ATOM   6103 O  O     . CYS C 1 198 ? -10.371 50.012  -12.654 1.00 21.64 ? 192 CYS C O     1 
ATOM   6104 C  CB    . CYS C 1 198 ? -11.251 52.739  -12.259 1.00 25.51 ? 192 CYS C CB    1 
ATOM   6105 S  SG    . CYS C 1 198 ? -11.361 54.483  -11.749 1.00 29.79 ? 192 CYS C SG    1 
ATOM   6106 N  N     . PHE C 1 199 ? -10.619 49.703  -10.411 1.00 18.68 ? 193 PHE C N     1 
ATOM   6107 C  CA    . PHE C 1 199 ? -10.699 48.224  -10.428 1.00 21.74 ? 193 PHE C CA    1 
ATOM   6108 C  C     . PHE C 1 199 ? -12.150 47.804  -10.525 1.00 20.59 ? 193 PHE C C     1 
ATOM   6109 O  O     . PHE C 1 199 ? -12.933 48.253  -9.704  1.00 24.31 ? 193 PHE C O     1 
ATOM   6110 C  CB    . PHE C 1 199 ? -10.112 47.621  -9.165  1.00 19.34 ? 193 PHE C CB    1 
ATOM   6111 C  CG    . PHE C 1 199 ? -8.726  48.095  -8.838  1.00 19.83 ? 193 PHE C CG    1 
ATOM   6112 C  CD1   . PHE C 1 199 ? -7.666  47.836  -9.680  1.00 22.33 ? 193 PHE C CD1   1 
ATOM   6113 C  CD2   . PHE C 1 199 ? -8.477  48.726  -7.642  1.00 22.36 ? 193 PHE C CD2   1 
ATOM   6114 C  CE1   . PHE C 1 199 ? -6.397  48.276  -9.361  1.00 18.74 ? 193 PHE C CE1   1 
ATOM   6115 C  CE2   . PHE C 1 199 ? -7.194  49.123  -7.297  1.00 21.85 ? 193 PHE C CE2   1 
ATOM   6116 C  CZ    . PHE C 1 199 ? -6.159  48.896  -8.170  1.00 18.93 ? 193 PHE C CZ    1 
ATOM   6117 N  N     . GLN C 1 200 ? -12.476 46.903  -11.441 1.00 20.37 ? 194 GLN C N     1 
ATOM   6118 C  CA    . GLN C 1 200 ? -13.769 46.184  -11.327 1.00 22.78 ? 194 GLN C CA    1 
ATOM   6119 C  C     . GLN C 1 200 ? -13.628 45.288  -10.095 1.00 21.17 ? 194 GLN C C     1 
ATOM   6120 O  O     . GLN C 1 200 ? -12.564 44.644  -9.927  1.00 22.02 ? 194 GLN C O     1 
ATOM   6121 C  CB    . GLN C 1 200 ? -14.055 45.406  -12.607 1.00 24.67 ? 194 GLN C CB    1 
ATOM   6122 C  CG    . GLN C 1 200 ? -15.383 44.670  -12.575 1.00 24.11 ? 194 GLN C CG    1 
ATOM   6123 C  CD    . GLN C 1 200 ? -15.622 43.866  -13.832 1.00 24.41 ? 194 GLN C CD    1 
ATOM   6124 O  OE1   . GLN C 1 200 ? -14.728 43.655  -14.672 1.00 22.70 ? 194 GLN C OE1   1 
ATOM   6125 N  NE2   . GLN C 1 200 ? -16.868 43.440  -13.979 1.00 27.15 ? 194 GLN C NE2   1 
ATOM   6126 N  N     A VAL C 1 201 ? -14.636 45.238  -9.232  0.55 20.23 ? 195 VAL C N     1 
ATOM   6127 N  N     B VAL C 1 201 ? -14.652 45.237  -9.238  0.45 20.04 ? 195 VAL C N     1 
ATOM   6128 C  CA    A VAL C 1 201 ? -14.559 44.334  -8.053  0.55 20.97 ? 195 VAL C CA    1 
ATOM   6129 C  CA    B VAL C 1 201 ? -14.724 44.237  -8.132  0.45 20.21 ? 195 VAL C CA    1 
ATOM   6130 C  C     A VAL C 1 201 ? -14.342 42.898  -8.561  0.55 21.25 ? 195 VAL C C     1 
ATOM   6131 C  C     B VAL C 1 201 ? -14.267 42.888  -8.690  0.45 20.67 ? 195 VAL C C     1 
ATOM   6132 O  O     A VAL C 1 201 ? -15.088 42.437  -9.466  0.55 21.75 ? 195 VAL C O     1 
ATOM   6133 O  O     B VAL C 1 201 ? -14.810 42.460  -9.750  0.45 20.64 ? 195 VAL C O     1 
ATOM   6134 C  CB    A VAL C 1 201 ? -15.750 44.513  -7.099  0.55 20.34 ? 195 VAL C CB    1 
ATOM   6135 C  CB    B VAL C 1 201 ? -16.133 44.128  -7.530  0.45 19.71 ? 195 VAL C CB    1 
ATOM   6136 C  CG1   A VAL C 1 201 ? -17.089 44.220  -7.749  0.55 21.01 ? 195 VAL C CG1   1 
ATOM   6137 C  CG1   B VAL C 1 201 ? -16.303 42.849  -6.728  0.45 19.30 ? 195 VAL C CG1   1 
ATOM   6138 C  CG2   A VAL C 1 201 ? -15.551 43.709  -5.832  0.55 20.93 ? 195 VAL C CG2   1 
ATOM   6139 C  CG2   B VAL C 1 201 ? -16.476 45.346  -6.697  0.45 19.58 ? 195 VAL C CG2   1 
ATOM   6140 N  N     . LEU C 1 202 ? -13.314 42.238  -8.012  1.00 20.17 ? 196 LEU C N     1 
ATOM   6141 C  CA    . LEU C 1 202 ? -12.837 40.892  -8.384  1.00 21.02 ? 196 LEU C CA    1 
ATOM   6142 C  C     . LEU C 1 202 ? -13.186 39.873  -7.306  1.00 21.99 ? 196 LEU C C     1 
ATOM   6143 O  O     . LEU C 1 202 ? -12.910 40.139  -6.103  1.00 21.20 ? 196 LEU C O     1 
ATOM   6144 C  CB    . LEU C 1 202 ? -11.331 40.973  -8.609  1.00 23.16 ? 196 LEU C CB    1 
ATOM   6145 C  CG    . LEU C 1 202 ? -10.672 39.688  -9.113  1.00 24.40 ? 196 LEU C CG    1 
ATOM   6146 C  CD1   . LEU C 1 202 ? -11.127 39.326  -10.525 1.00 24.05 ? 196 LEU C CD1   1 
ATOM   6147 C  CD2   . LEU C 1 202 ? -9.170  39.825  -9.048  1.00 22.05 ? 196 LEU C CD2   1 
ATOM   6148 N  N     . ILE C 1 203 ? -13.728 38.725  -7.711  1.00 24.77 ? 197 ILE C N     1 
ATOM   6149 C  CA    . ILE C 1 203 ? -14.003 37.568  -6.801  1.00 23.17 ? 197 ILE C CA    1 
ATOM   6150 C  C     . ILE C 1 203 ? -12.778 36.629  -6.751  1.00 23.83 ? 197 ILE C C     1 
ATOM   6151 O  O     . ILE C 1 203 ? -12.255 36.222  -7.809  1.00 22.79 ? 197 ILE C O     1 
ATOM   6152 C  CB    . ILE C 1 203 ? -15.293 36.826  -7.221  1.00 25.04 ? 197 ILE C CB    1 
ATOM   6153 C  CG1   . ILE C 1 203 ? -16.510 37.746  -7.233  1.00 27.56 ? 197 ILE C CG1   1 
ATOM   6154 C  CG2   . ILE C 1 203 ? -15.519 35.619  -6.322  1.00 25.89 ? 197 ILE C CG2   1 
ATOM   6155 C  CD1   . ILE C 1 203 ? -16.781 38.476  -5.910  1.00 27.93 ? 197 ILE C CD1   1 
ATOM   6156 N  N     . ILE C 1 204 ? -12.297 36.296  -5.560  1.00 21.17 ? 198 ILE C N     1 
ATOM   6157 C  CA    . ILE C 1 204 ? -11.163 35.356  -5.404  1.00 24.23 ? 198 ILE C CA    1 
ATOM   6158 C  C     . ILE C 1 204 ? -11.579 34.244  -4.436  1.00 23.67 ? 198 ILE C C     1 
ATOM   6159 O  O     . ILE C 1 204 ? -11.916 34.570  -3.263  1.00 23.32 ? 198 ILE C O     1 
ATOM   6160 C  CB    . ILE C 1 204 ? -9.892  36.070  -4.904  1.00 23.93 ? 198 ILE C CB    1 
ATOM   6161 C  CG1   . ILE C 1 204 ? -9.413  37.141  -5.877  1.00 24.51 ? 198 ILE C CG1   1 
ATOM   6162 C  CG2   . ILE C 1 204 ? -8.791  35.051  -4.664  1.00 26.82 ? 198 ILE C CG2   1 
ATOM   6163 C  CD1   . ILE C 1 204 ? -8.135  37.794  -5.469  1.00 25.99 ? 198 ILE C CD1   1 
ATOM   6164 N  N     . GLU C 1 205 ? -11.474 32.988  -4.880  1.00 27.13 ? 199 GLU C N     1 
ATOM   6165 C  CA    . GLU C 1 205 ? -11.737 31.780  -4.035  1.00 30.97 ? 199 GLU C CA    1 
ATOM   6166 C  C     . GLU C 1 205 ? -10.879 31.818  -2.758  1.00 30.32 ? 199 GLU C C     1 
ATOM   6167 O  O     . GLU C 1 205 ? -9.672  32.090  -2.834  1.00 30.72 ? 199 GLU C O     1 
ATOM   6168 C  CB    . GLU C 1 205 ? -11.487 30.467  -4.789  1.00 36.22 ? 199 GLU C CB    1 
ATOM   6169 C  CG    . GLU C 1 205 ? -11.861 29.209  -3.993  1.00 39.42 ? 199 GLU C CG    1 
ATOM   6170 C  CD    . GLU C 1 205 ? -10.923 28.729  -2.871  1.00 49.03 ? 199 GLU C CD    1 
ATOM   6171 O  OE1   . GLU C 1 205 ? -9.680  28.874  -2.999  1.00 48.19 ? 199 GLU C OE1   1 
ATOM   6172 O  OE2   . GLU C 1 205 ? -11.435 28.166  -1.852  1.00 55.87 ? 199 GLU C OE2   1 
ATOM   6173 N  N     . GLY C 1 206 ? -11.495 31.539  -1.612  1.00 28.93 ? 200 GLY C N     1 
ATOM   6174 C  CA    . GLY C 1 206 ? -10.853 31.542  -0.286  1.00 30.65 ? 200 GLY C CA    1 
ATOM   6175 C  C     . GLY C 1 206 ? -10.774 32.919  0.355   1.00 30.33 ? 200 GLY C C     1 
ATOM   6176 O  O     . GLY C 1 206 ? -10.326 32.977  1.526   1.00 31.40 ? 200 GLY C O     1 
ATOM   6177 N  N     . GLU C 1 207 ? -11.148 33.999  -0.353  1.00 25.78 ? 201 GLU C N     1 
ATOM   6178 C  CA    . GLU C 1 207 ? -11.053 35.372  0.193   1.00 25.46 ? 201 GLU C CA    1 
ATOM   6179 C  C     . GLU C 1 207 ? -12.463 35.955  0.327   1.00 24.25 ? 201 GLU C C     1 
ATOM   6180 O  O     . GLU C 1 207 ? -12.866 36.384  1.447   1.00 23.70 ? 201 GLU C O     1 
ATOM   6181 C  CB    . GLU C 1 207 ? -10.164 36.241  -0.709  1.00 25.07 ? 201 GLU C CB    1 
ATOM   6182 C  CG    . GLU C 1 207 ? -8.730  35.752  -0.830  1.00 27.13 ? 201 GLU C CG    1 
ATOM   6183 C  CD    . GLU C 1 207 ? -7.879  35.996  0.407   1.00 28.70 ? 201 GLU C CD    1 
ATOM   6184 O  OE1   . GLU C 1 207 ? -8.376  36.651  1.336   1.00 27.47 ? 201 GLU C OE1   1 
ATOM   6185 O  OE2   . GLU C 1 207 ? -6.722  35.517  0.441   1.00 32.33 ? 201 GLU C OE2   1 
ATOM   6186 N  N     . ASN C 1 208 ? -13.192 36.069  -0.781  1.00 23.37 ? 202 ASN C N     1 
ATOM   6187 C  CA    . ASN C 1 208 ? -14.414 36.892  -0.767  1.00 21.57 ? 202 ASN C CA    1 
ATOM   6188 C  C     . ASN C 1 208 ? -15.532 36.179  -1.546  1.00 22.59 ? 202 ASN C C     1 
ATOM   6189 O  O     . ASN C 1 208 ? -16.399 36.884  -2.022  1.00 21.20 ? 202 ASN C O     1 
ATOM   6190 C  CB    . ASN C 1 208 ? -14.118 38.306  -1.281  1.00 19.30 ? 202 ASN C CB    1 
ATOM   6191 C  CG    . ASN C 1 208 ? -13.709 38.330  -2.738  1.00 19.67 ? 202 ASN C CG    1 
ATOM   6192 O  OD1   . ASN C 1 208 ? -13.593 37.273  -3.375  1.00 21.76 ? 202 ASN C OD1   1 
ATOM   6193 N  ND2   . ASN C 1 208 ? -13.487 39.529  -3.282  1.00 19.38 ? 202 ASN C ND2   1 
ATOM   6194 N  N     . ASP C 1 209 ? -15.526 34.843  -1.628  1.00 23.87 ? 203 ASP C N     1 
ATOM   6195 C  CA    . ASP C 1 209 ? -16.372 34.137  -2.636  1.00 26.96 ? 203 ASP C CA    1 
ATOM   6196 C  C     . ASP C 1 209 ? -17.582 33.446  -2.006  1.00 26.67 ? 203 ASP C C     1 
ATOM   6197 O  O     . ASP C 1 209 ? -18.455 33.001  -2.776  1.00 28.09 ? 203 ASP C O     1 
ATOM   6198 C  CB    . ASP C 1 209 ? -15.572 33.155  -3.475  1.00 29.50 ? 203 ASP C CB    1 
ATOM   6199 C  CG    . ASP C 1 209 ? -15.034 31.935  -2.750  1.00 34.11 ? 203 ASP C CG    1 
ATOM   6200 O  OD1   . ASP C 1 209 ? -14.587 32.063  -1.584  1.00 32.84 ? 203 ASP C OD1   1 
ATOM   6201 O  OD2   . ASP C 1 209 ? -15.052 30.863  -3.368  1.00 36.88 ? 203 ASP C OD2   1 
ATOM   6202 N  N     . SER C 1 210 ? -17.669 33.337  -0.685  1.00 27.62 ? 204 SER C N     1 
ATOM   6203 C  CA    . SER C 1 210 ? -18.730 32.511  -0.043  1.00 29.18 ? 204 SER C CA    1 
ATOM   6204 C  C     . SER C 1 210 ? -18.988 32.976  1.378   1.00 31.39 ? 204 SER C C     1 
ATOM   6205 O  O     . SER C 1 210 ? -18.412 33.985  1.792   1.00 31.44 ? 204 SER C O     1 
ATOM   6206 C  CB    . SER C 1 210 ? -18.389 31.046  -0.114  1.00 31.10 ? 204 SER C CB    1 
ATOM   6207 O  OG    . SER C 1 210 ? -17.552 30.623  0.961   1.00 33.23 ? 204 SER C OG    1 
ATOM   6208 N  N     . ASP C 1 211 ? -19.880 32.272  2.078   1.00 32.67 ? 205 ASP C N     1 
ATOM   6209 C  CA    . ASP C 1 211 ? -20.250 32.585  3.474   1.00 33.65 ? 205 ASP C CA    1 
ATOM   6210 C  C     . ASP C 1 211 ? -19.232 31.914  4.398   1.00 30.62 ? 205 ASP C C     1 
ATOM   6211 O  O     . ASP C 1 211 ? -19.288 32.224  5.597   1.00 33.95 ? 205 ASP C O     1 
ATOM   6212 C  CB    . ASP C 1 211 ? -21.725 32.223  3.750   1.00 35.89 ? 205 ASP C CB    1 
ATOM   6213 C  CG    . ASP C 1 211 ? -22.727 33.294  3.291   1.00 41.16 ? 205 ASP C CG    1 
ATOM   6214 O  OD1   . ASP C 1 211 ? -22.283 34.386  2.810   1.00 38.41 ? 205 ASP C OD1   1 
ATOM   6215 O  OD2   . ASP C 1 211 ? -23.970 33.049  3.419   1.00 41.58 ? 205 ASP C OD2   1 
ATOM   6216 N  N     . LYS C 1 212 ? -18.361 31.047  3.872   1.00 29.19 ? 206 LYS C N     1 
ATOM   6217 C  CA    . LYS C 1 212 ? -17.269 30.348  4.622   1.00 32.31 ? 206 LYS C CA    1 
ATOM   6218 C  C     . LYS C 1 212 ? -16.029 31.261  4.777   1.00 31.61 ? 206 LYS C C     1 
ATOM   6219 O  O     . LYS C 1 212 ? -15.240 31.032  5.698   1.00 34.36 ? 206 LYS C O     1 
ATOM   6220 C  CB    . LYS C 1 212 ? -16.820 29.073  3.895   1.00 37.81 ? 206 LYS C CB    1 
ATOM   6221 C  CG    . LYS C 1 212 ? -17.891 28.013  3.689   1.00 43.69 ? 206 LYS C CG    1 
ATOM   6222 C  CD    . LYS C 1 212 ? -18.542 27.630  4.987   1.00 50.66 ? 206 LYS C CD    1 
ATOM   6223 C  CE    . LYS C 1 212 ? -19.267 26.305  4.940   1.00 49.67 ? 206 LYS C CE    1 
ATOM   6224 N  NZ    . LYS C 1 212 ? -19.415 25.768  6.312   1.00 50.80 ? 206 LYS C NZ    1 
ATOM   6225 N  N     . THR C 1 213 ? -15.845 32.233  3.877   1.00 28.88 ? 207 THR C N     1 
ATOM   6226 C  CA    . THR C 1 213 ? -14.673 33.155  3.854   1.00 27.20 ? 207 THR C CA    1 
ATOM   6227 C  C     . THR C 1 213 ? -14.950 34.340  4.781   1.00 24.92 ? 207 THR C C     1 
ATOM   6228 O  O     . THR C 1 213 ? -16.073 34.487  5.248   1.00 25.87 ? 207 THR C O     1 
ATOM   6229 C  CB    . THR C 1 213 ? -14.375 33.531  2.394   1.00 24.89 ? 207 THR C CB    1 
ATOM   6230 O  OG1   . THR C 1 213 ? -15.573 33.961  1.727   1.00 25.07 ? 207 THR C OG1   1 
ATOM   6231 C  CG2   . THR C 1 213 ? -13.791 32.365  1.646   1.00 25.24 ? 207 THR C CG2   1 
ATOM   6232 N  N     . LEU C 1 214 ? -13.974 35.218  5.015   1.00 25.58 ? 208 LEU C N     1 
ATOM   6233 C  CA    . LEU C 1 214 ? -14.187 36.405  5.900   1.00 25.90 ? 208 LEU C CA    1 
ATOM   6234 C  C     . LEU C 1 214 ? -15.043 37.472  5.210   1.00 25.07 ? 208 LEU C C     1 
ATOM   6235 O  O     . LEU C 1 214 ? -15.515 38.396  5.904   1.00 27.00 ? 208 LEU C O     1 
ATOM   6236 C  CB    . LEU C 1 214 ? -12.817 36.973  6.315   1.00 25.92 ? 208 LEU C CB    1 
ATOM   6237 C  CG    . LEU C 1 214 ? -12.040 36.088  7.277   1.00 29.34 ? 208 LEU C CG    1 
ATOM   6238 C  CD1   . LEU C 1 214 ? -10.603 36.589  7.469   1.00 29.45 ? 208 LEU C CD1   1 
ATOM   6239 C  CD2   . LEU C 1 214 ? -12.763 35.978  8.612   1.00 30.47 ? 208 LEU C CD2   1 
ATOM   6240 N  N     . ARG C 1 215 ? -15.177 37.427  3.887   1.00 23.45 ? 209 ARG C N     1 
ATOM   6241 C  CA    . ARG C 1 215 ? -16.045 38.355  3.138   1.00 23.36 ? 209 ARG C CA    1 
ATOM   6242 C  C     . ARG C 1 215 ? -16.796 37.557  2.073   1.00 21.82 ? 209 ARG C C     1 
ATOM   6243 O  O     . ARG C 1 215 ? -16.318 36.496  1.664   1.00 22.79 ? 209 ARG C O     1 
ATOM   6244 C  CB    . ARG C 1 215 ? -15.248 39.503  2.495   1.00 25.11 ? 209 ARG C CB    1 
ATOM   6245 C  CG    . ARG C 1 215 ? -14.376 40.290  3.467   1.00 26.78 ? 209 ARG C CG    1 
ATOM   6246 C  CD    . ARG C 1 215 ? -15.163 41.230  4.372   1.00 28.32 ? 209 ARG C CD    1 
ATOM   6247 N  NE    . ARG C 1 215 ? -14.566 41.407  5.707   1.00 34.54 ? 209 ARG C NE    1 
ATOM   6248 C  CZ    . ARG C 1 215 ? -13.558 42.218  6.012   1.00 35.08 ? 209 ARG C CZ    1 
ATOM   6249 N  NH1   . ARG C 1 215 ? -12.997 42.984  5.103   1.00 33.15 ? 209 ARG C NH1   1 
ATOM   6250 N  NH2   . ARG C 1 215 ? -13.127 42.308  7.253   1.00 37.70 ? 209 ARG C NH2   1 
ATOM   6251 N  N     . ASN C 1 216 ? -17.908 38.125  1.634   1.00 23.44 ? 210 ASN C N     1 
ATOM   6252 C  CA    . ASN C 1 216 ? -18.696 37.643  0.466   1.00 24.12 ? 210 ASN C CA    1 
ATOM   6253 C  C     . ASN C 1 216 ? -18.972 38.823  -0.454  1.00 24.05 ? 210 ASN C C     1 
ATOM   6254 O  O     . ASN C 1 216 ? -19.821 39.643  -0.122  1.00 23.61 ? 210 ASN C O     1 
ATOM   6255 C  CB    . ASN C 1 216 ? -20.020 36.989  0.866   1.00 26.00 ? 210 ASN C CB    1 
ATOM   6256 C  CG    . ASN C 1 216 ? -20.611 36.233  -0.308  1.00 28.67 ? 210 ASN C CG    1 
ATOM   6257 O  OD1   . ASN C 1 216 ? -20.466 36.657  -1.455  1.00 28.98 ? 210 ASN C OD1   1 
ATOM   6258 N  ND2   . ASN C 1 216 ? -21.222 35.094  -0.043  1.00 29.19 ? 210 ASN C ND2   1 
ATOM   6259 N  N     . ALA C 1 217 ? -18.212 38.944  -1.541  1.00 23.20 ? 211 ALA C N     1 
ATOM   6260 C  CA    . ALA C 1 217 ? -18.310 40.119  -2.432  1.00 24.70 ? 211 ALA C CA    1 
ATOM   6261 C  C     . ALA C 1 217 ? -19.381 39.898  -3.500  1.00 24.55 ? 211 ALA C C     1 
ATOM   6262 O  O     . ALA C 1 217 ? -19.561 40.791  -4.306  1.00 26.37 ? 211 ALA C O     1 
ATOM   6263 C  CB    . ALA C 1 217 ? -16.970 40.395  -3.076  1.00 21.92 ? 211 ALA C CB    1 
ATOM   6264 N  N     . HIS C 1 218 ? -20.022 38.731  -3.561  1.00 27.03 ? 212 HIS C N     1 
ATOM   6265 C  CA    . HIS C 1 218 ? -20.966 38.392  -4.681  1.00 27.99 ? 212 HIS C CA    1 
ATOM   6266 C  C     . HIS C 1 218 ? -22.046 39.454  -4.875  1.00 28.75 ? 212 HIS C C     1 
ATOM   6267 O  O     . HIS C 1 218 ? -22.352 39.749  -6.042  1.00 28.98 ? 212 HIS C O     1 
ATOM   6268 C  CB    . HIS C 1 218 ? -21.537 37.011  -4.490  1.00 27.42 ? 212 HIS C CB    1 
ATOM   6269 C  CG    . HIS C 1 218 ? -20.593 35.976  -4.963  1.00 27.42 ? 212 HIS C CG    1 
ATOM   6270 N  ND1   . HIS C 1 218 ? -20.257 35.858  -6.295  1.00 30.88 ? 212 HIS C ND1   1 
ATOM   6271 C  CD2   . HIS C 1 218 ? -19.971 34.975  -4.323  1.00 29.80 ? 212 HIS C CD2   1 
ATOM   6272 C  CE1   . HIS C 1 218 ? -19.440 34.838  -6.449  1.00 29.92 ? 212 HIS C CE1   1 
ATOM   6273 N  NE2   . HIS C 1 218 ? -19.233 34.284  -5.251  1.00 27.72 ? 212 HIS C NE2   1 
ATOM   6274 N  N     A SER C 1 219 ? -22.575 40.042  -3.796  0.65 29.88 ? 213 SER C N     1 
ATOM   6275 N  N     B SER C 1 219 ? -22.560 40.043  -3.789  0.35 29.70 ? 213 SER C N     1 
ATOM   6276 C  CA    A SER C 1 219 ? -23.647 41.073  -3.868  0.65 31.48 ? 213 SER C CA    1 
ATOM   6277 C  CA    B SER C 1 219 ? -23.633 41.075  -3.819  0.35 30.84 ? 213 SER C CA    1 
ATOM   6278 C  C     A SER C 1 219 ? -23.108 42.388  -4.436  0.65 31.65 ? 213 SER C C     1 
ATOM   6279 C  C     B SER C 1 219 ? -23.060 42.472  -4.068  0.35 31.57 ? 213 SER C C     1 
ATOM   6280 O  O     A SER C 1 219 ? -23.918 43.215  -4.901  0.65 28.62 ? 213 SER C O     1 
ATOM   6281 O  O     B SER C 1 219 ? -23.803 43.459  -3.863  0.35 30.93 ? 213 SER C O     1 
ATOM   6282 C  CB    A SER C 1 219 ? -24.324 41.289  -2.535  0.65 35.75 ? 213 SER C CB    1 
ATOM   6283 C  CB    B SER C 1 219 ? -24.448 41.053  -2.555  0.35 32.81 ? 213 SER C CB    1 
ATOM   6284 O  OG    A SER C 1 219 ? -23.370 41.536  -1.523  0.65 35.26 ? 213 SER C OG    1 
ATOM   6285 O  OG    B SER C 1 219 ? -25.020 39.773  -2.367  0.35 31.80 ? 213 SER C OG    1 
ATOM   6286 N  N     . LEU C 1 220 ? -21.790 42.573  -4.461  1.00 32.12 ? 214 LEU C N     1 
ATOM   6287 C  CA    . LEU C 1 220 ? -21.196 43.879  -4.852  1.00 33.56 ? 214 LEU C CA    1 
ATOM   6288 C  C     . LEU C 1 220 ? -20.672 43.842  -6.290  1.00 28.19 ? 214 LEU C C     1 
ATOM   6289 O  O     . LEU C 1 220 ? -20.259 44.912  -6.750  1.00 29.06 ? 214 LEU C O     1 
ATOM   6290 C  CB    . LEU C 1 220 ? -20.125 44.253  -3.824  1.00 36.38 ? 214 LEU C CB    1 
ATOM   6291 C  CG    . LEU C 1 220 ? -20.704 44.747  -2.492  1.00 39.75 ? 214 LEU C CG    1 
ATOM   6292 C  CD1   . LEU C 1 220 ? -20.748 43.622  -1.479  1.00 42.26 ? 214 LEU C CD1   1 
ATOM   6293 C  CD2   . LEU C 1 220 ? -19.907 45.908  -1.932  1.00 43.11 ? 214 LEU C CD2   1 
ATOM   6294 N  N     . THR C 1 221 ? -20.729 42.699  -6.991  1.00 30.70 ? 215 THR C N     1 
ATOM   6295 C  CA    . THR C 1 221 ? -20.204 42.582  -8.381  1.00 29.06 ? 215 THR C CA    1 
ATOM   6296 C  C     . THR C 1 221 ? -21.050 43.385  -9.377  1.00 32.49 ? 215 THR C C     1 
ATOM   6297 O  O     . THR C 1 221 ? -22.247 43.667  -9.111  1.00 30.81 ? 215 THR C O     1 
ATOM   6298 C  CB    . THR C 1 221 ? -20.012 41.125  -8.825  1.00 32.86 ? 215 THR C CB    1 
ATOM   6299 O  OG1   . THR C 1 221 ? -21.214 40.358  -8.701  1.00 30.57 ? 215 THR C OG1   1 
ATOM   6300 C  CG2   . THR C 1 221 ? -18.926 40.471  -8.006  1.00 30.96 ? 215 THR C CG2   1 
ATOM   6301 N  N     . ILE C 1 222 ? -20.412 43.784  -10.471 1.00 32.97 ? 216 ILE C N     1 
ATOM   6302 C  CA    . ILE C 1 222 ? -21.061 44.551  -11.566 1.00 32.65 ? 216 ILE C CA    1 
ATOM   6303 C  C     . ILE C 1 222 ? -20.765 43.872  -12.893 1.00 30.66 ? 216 ILE C C     1 
ATOM   6304 O  O     . ILE C 1 222 ? -19.803 43.061  -13.002 1.00 28.46 ? 216 ILE C O     1 
ATOM   6305 C  CB    . ILE C 1 222 ? -20.634 46.034  -11.541 1.00 30.28 ? 216 ILE C CB    1 
ATOM   6306 C  CG1   . ILE C 1 222 ? -19.116 46.229  -11.647 1.00 31.12 ? 216 ILE C CG1   1 
ATOM   6307 C  CG2   . ILE C 1 222 ? -21.237 46.704  -10.316 1.00 33.07 ? 216 ILE C CG2   1 
ATOM   6308 C  CD1   . ILE C 1 222 ? -18.675 47.680  -11.868 1.00 31.74 ? 216 ILE C CD1   1 
ATOM   6309 N  N     . SER C 1 223 ? -21.601 44.178  -13.874 1.00 35.19 ? 217 SER C N     1 
ATOM   6310 C  CA    . SER C 1 223 ? -21.465 43.722  -15.284 1.00 34.07 ? 217 SER C CA    1 
ATOM   6311 C  C     . SER C 1 223 ? -20.370 44.531  -15.968 1.00 34.27 ? 217 SER C C     1 
ATOM   6312 O  O     . SER C 1 223 ? -20.120 45.692  -15.536 1.00 32.48 ? 217 SER C O     1 
ATOM   6313 C  CB    . SER C 1 223 ? -22.768 43.914  -16.016 1.00 36.38 ? 217 SER C CB    1 
ATOM   6314 O  OG    . SER C 1 223 ? -23.025 45.304  -16.108 1.00 38.62 ? 217 SER C OG    1 
ATOM   6315 N  N     . ASP C 1 224 ? -19.815 43.965  -17.041 1.00 35.69 ? 218 ASP C N     1 
ATOM   6316 C  CA    . ASP C 1 224 ? -18.924 44.656  -17.999 1.00 38.82 ? 218 ASP C CA    1 
ATOM   6317 C  C     . ASP C 1 224 ? -19.524 46.021  -18.339 1.00 40.95 ? 218 ASP C C     1 
ATOM   6318 O  O     . ASP C 1 224 ? -18.776 46.996  -18.273 1.00 42.03 ? 218 ASP C O     1 
ATOM   6319 C  CB    . ASP C 1 224 ? -18.744 43.845  -19.286 1.00 47.49 ? 218 ASP C CB    1 
ATOM   6320 C  CG    . ASP C 1 224 ? -17.988 42.526  -19.162 1.00 53.86 ? 218 ASP C CG    1 
ATOM   6321 O  OD1   . ASP C 1 224 ? -17.799 42.052  -18.024 1.00 57.50 ? 218 ASP C OD1   1 
ATOM   6322 O  OD2   . ASP C 1 224 ? -17.604 41.978  -20.222 1.00 57.32 ? 218 ASP C OD2   1 
ATOM   6323 N  N     . ASP C 1 225 ? -20.809 46.061  -18.721 1.00 38.28 ? 219 ASP C N     1 
ATOM   6324 C  CA    . ASP C 1 225 ? -21.555 47.292  -19.117 1.00 44.92 ? 219 ASP C CA    1 
ATOM   6325 C  C     . ASP C 1 225 ? -21.517 48.364  -18.010 1.00 37.18 ? 219 ASP C C     1 
ATOM   6326 O  O     . ASP C 1 225 ? -21.289 49.532  -18.330 1.00 36.88 ? 219 ASP C O     1 
ATOM   6327 C  CB    . ASP C 1 225 ? -23.022 46.980  -19.441 1.00 49.47 ? 219 ASP C CB    1 
ATOM   6328 C  CG    . ASP C 1 225 ? -23.309 46.698  -20.909 1.00 57.62 ? 219 ASP C CG    1 
ATOM   6329 O  OD1   . ASP C 1 225 ? -22.382 46.249  -21.625 1.00 59.18 ? 219 ASP C OD1   1 
ATOM   6330 O  OD2   . ASP C 1 225 ? -24.467 46.943  -21.331 1.00 66.72 ? 219 ASP C OD2   1 
ATOM   6331 N  N     . GLU C 1 226 ? -21.819 47.992  -16.770 1.00 33.95 ? 220 GLU C N     1 
ATOM   6332 C  CA    . GLU C 1 226 ? -21.833 48.898  -15.590 1.00 31.37 ? 220 GLU C CA    1 
ATOM   6333 C  C     . GLU C 1 226 ? -20.428 49.495  -15.371 1.00 29.74 ? 220 GLU C C     1 
ATOM   6334 O  O     . GLU C 1 226 ? -20.305 50.719  -15.161 1.00 28.83 ? 220 GLU C O     1 
ATOM   6335 C  CB    . GLU C 1 226 ? -22.313 48.129  -14.355 1.00 34.68 ? 220 GLU C CB    1 
ATOM   6336 C  CG    . GLU C 1 226 ? -23.824 47.943  -14.278 1.00 36.81 ? 220 GLU C CG    1 
ATOM   6337 C  CD    . GLU C 1 226 ? -24.315 46.872  -13.310 1.00 41.53 ? 220 GLU C CD    1 
ATOM   6338 O  OE1   . GLU C 1 226 ? -23.572 45.868  -13.052 1.00 42.60 ? 220 GLU C OE1   1 
ATOM   6339 O  OE2   . GLU C 1 226 ? -25.442 47.027  -12.817 1.00 46.81 ? 220 GLU C OE2   1 
ATOM   6340 N  N     . PHE C 1 227 ? -19.387 48.671  -15.473 1.00 28.52 ? 221 PHE C N     1 
ATOM   6341 C  CA    . PHE C 1 227 ? -17.975 49.101  -15.269 1.00 29.50 ? 221 PHE C CA    1 
ATOM   6342 C  C     . PHE C 1 227 ? -17.596 50.058  -16.403 1.00 29.94 ? 221 PHE C C     1 
ATOM   6343 O  O     . PHE C 1 227 ? -17.012 51.110  -16.167 1.00 27.94 ? 221 PHE C O     1 
ATOM   6344 C  CB    . PHE C 1 227 ? -17.030 47.899  -15.190 1.00 26.72 ? 221 PHE C CB    1 
ATOM   6345 C  CG    . PHE C 1 227 ? -15.604 48.315  -14.997 1.00 26.68 ? 221 PHE C CG    1 
ATOM   6346 C  CD1   . PHE C 1 227 ? -15.184 48.820  -13.774 1.00 25.80 ? 221 PHE C CD1   1 
ATOM   6347 C  CD2   . PHE C 1 227 ? -14.712 48.286  -16.040 1.00 26.37 ? 221 PHE C CD2   1 
ATOM   6348 C  CE1   . PHE C 1 227 ? -13.886 49.264  -13.605 1.00 22.50 ? 221 PHE C CE1   1 
ATOM   6349 C  CE2   . PHE C 1 227 ? -13.406 48.718  -15.871 1.00 28.35 ? 221 PHE C CE2   1 
ATOM   6350 C  CZ    . PHE C 1 227 ? -12.992 49.186  -14.646 1.00 28.12 ? 221 PHE C CZ    1 
ATOM   6351 N  N     . ASP C 1 228 ? -17.992 49.715  -17.626 1.00 30.26 ? 222 ASP C N     1 
ATOM   6352 C  CA    . ASP C 1 228 ? -17.646 50.530  -18.821 1.00 34.24 ? 222 ASP C CA    1 
ATOM   6353 C  C     . ASP C 1 228 ? -18.316 51.894  -18.732 1.00 31.69 ? 222 ASP C C     1 
ATOM   6354 O  O     . ASP C 1 228 ? -17.672 52.885  -19.100 1.00 32.59 ? 222 ASP C O     1 
ATOM   6355 C  CB    . ASP C 1 228 ? -17.992 49.817  -20.125 1.00 35.27 ? 222 ASP C CB    1 
ATOM   6356 C  CG    . ASP C 1 228 ? -17.157 48.566  -20.328 1.00 43.54 ? 222 ASP C CG    1 
ATOM   6357 O  OD1   . ASP C 1 228 ? -16.124 48.393  -19.601 1.00 46.28 ? 222 ASP C OD1   1 
ATOM   6358 O  OD2   . ASP C 1 228 ? -17.539 47.770  -21.209 1.00 51.65 ? 222 ASP C OD2   1 
ATOM   6359 N  N     A ARG C 1 229 ? -19.566 51.935  -18.265 0.46 32.77 ? 223 ARG C N     1 
ATOM   6360 N  N     B ARG C 1 229 ? -19.546 51.969  -18.211 0.54 33.57 ? 223 ARG C N     1 
ATOM   6361 C  CA    A ARG C 1 229 ? -20.307 53.209  -18.090 0.46 30.78 ? 223 ARG C CA    1 
ATOM   6362 C  CA    B ARG C 1 229 ? -20.280 53.262  -18.125 0.54 31.78 ? 223 ARG C CA    1 
ATOM   6363 C  C     A ARG C 1 229 ? -19.554 54.078  -17.077 0.46 28.71 ? 223 ARG C C     1 
ATOM   6364 C  C     B ARG C 1 229 ? -19.720 54.109  -16.973 0.54 29.64 ? 223 ARG C C     1 
ATOM   6365 O  O     A ARG C 1 229 ? -19.310 55.262  -17.373 0.46 25.59 ? 223 ARG C O     1 
ATOM   6366 O  O     B ARG C 1 229 ? -19.813 55.340  -17.037 0.54 28.08 ? 223 ARG C O     1 
ATOM   6367 C  CB    A ARG C 1 229 ? -21.767 52.924  -17.733 0.46 33.32 ? 223 ARG C CB    1 
ATOM   6368 C  CB    B ARG C 1 229 ? -21.794 53.025  -18.104 0.54 34.40 ? 223 ARG C CB    1 
ATOM   6369 C  CG    A ARG C 1 229 ? -22.622 52.635  -18.956 0.46 35.60 ? 223 ARG C CG    1 
ATOM   6370 C  CG    B ARG C 1 229 ? -22.352 52.845  -19.509 0.54 38.16 ? 223 ARG C CG    1 
ATOM   6371 C  CD    A ARG C 1 229 ? -24.111 52.644  -18.669 0.46 39.42 ? 223 ARG C CD    1 
ATOM   6372 C  CD    B ARG C 1 229 ? -23.862 52.913  -19.653 0.54 42.10 ? 223 ARG C CD    1 
ATOM   6373 N  NE    A ARG C 1 229 ? -24.580 51.309  -18.341 0.46 43.21 ? 223 ARG C NE    1 
ATOM   6374 N  NE    B ARG C 1 229 ? -24.487 51.599  -19.615 0.54 44.18 ? 223 ARG C NE    1 
ATOM   6375 C  CZ    A ARG C 1 229 ? -24.836 50.878  -17.113 0.46 41.52 ? 223 ARG C CZ    1 
ATOM   6376 C  CZ    B ARG C 1 229 ? -24.298 50.636  -20.508 0.54 46.19 ? 223 ARG C CZ    1 
ATOM   6377 N  NH1   A ARG C 1 229 ? -24.688 51.684  -16.066 0.46 38.66 ? 223 ARG C NH1   1 
ATOM   6378 N  NH1   B ARG C 1 229 ? -23.481 50.813  -21.533 0.54 50.37 ? 223 ARG C NH1   1 
ATOM   6379 N  NH2   A ARG C 1 229 ? -25.260 49.641  -16.956 0.46 39.45 ? 223 ARG C NH2   1 
ATOM   6380 N  NH2   B ARG C 1 229 ? -24.925 49.486  -20.364 0.54 46.98 ? 223 ARG C NH2   1 
ATOM   6381 N  N     . PHE C 1 230 ? -19.111 53.497  -15.963 1.00 28.09 ? 224 PHE C N     1 
ATOM   6382 C  CA    . PHE C 1 230 ? -18.360 54.251  -14.933 1.00 28.69 ? 224 PHE C CA    1 
ATOM   6383 C  C     . PHE C 1 230 ? -17.139 54.903  -15.597 1.00 25.35 ? 224 PHE C C     1 
ATOM   6384 O  O     . PHE C 1 230 ? -16.928 56.126  -15.425 1.00 27.92 ? 224 PHE C O     1 
ATOM   6385 C  CB    . PHE C 1 230 ? -18.033 53.373  -13.723 1.00 25.63 ? 224 PHE C CB    1 
ATOM   6386 C  CG    . PHE C 1 230 ? -17.222 54.117  -12.699 1.00 25.02 ? 224 PHE C CG    1 
ATOM   6387 C  CD1   . PHE C 1 230 ? -15.861 54.286  -12.886 1.00 27.51 ? 224 PHE C CD1   1 
ATOM   6388 C  CD2   . PHE C 1 230 ? -17.819 54.671  -11.587 1.00 26.29 ? 224 PHE C CD2   1 
ATOM   6389 C  CE1   . PHE C 1 230 ? -15.110 54.994  -11.964 1.00 27.52 ? 224 PHE C CE1   1 
ATOM   6390 C  CE2   . PHE C 1 230 ? -17.066 55.378  -10.656 1.00 28.75 ? 224 PHE C CE2   1 
ATOM   6391 C  CZ    . PHE C 1 230 ? -15.714 55.554  -10.860 1.00 28.86 ? 224 PHE C CZ    1 
ATOM   6392 N  N     . CYS C 1 231 ? -16.319 54.140  -16.321 1.00 27.08 ? 225 CYS C N     1 
ATOM   6393 C  CA    . CYS C 1 231 ? -15.067 54.686  -16.910 1.00 27.69 ? 225 CYS C CA    1 
ATOM   6394 C  C     . CYS C 1 231 ? -15.421 55.815  -17.898 1.00 29.53 ? 225 CYS C C     1 
ATOM   6395 O  O     . CYS C 1 231 ? -14.701 56.852  -17.896 1.00 30.38 ? 225 CYS C O     1 
ATOM   6396 C  CB    . CYS C 1 231 ? -14.215 53.602  -17.542 1.00 29.59 ? 225 CYS C CB    1 
ATOM   6397 S  SG    . CYS C 1 231 ? -13.746 52.332  -16.335 1.00 33.60 ? 225 CYS C SG    1 
ATOM   6398 N  N     . GLU C 1 232 ? -16.492 55.637  -18.676 1.00 30.04 ? 226 GLU C N     1 
ATOM   6399 C  CA    . GLU C 1 232 ? -16.925 56.571  -19.764 1.00 33.87 ? 226 GLU C CA    1 
ATOM   6400 C  C     . GLU C 1 232 ? -17.389 57.897  -19.150 1.00 29.31 ? 226 GLU C C     1 
ATOM   6401 O  O     . GLU C 1 232 ? -17.078 58.950  -19.703 1.00 28.47 ? 226 GLU C O     1 
ATOM   6402 C  CB    . GLU C 1 232 ? -18.055 55.933  -20.581 1.00 36.01 ? 226 GLU C CB    1 
ATOM   6403 C  CG    . GLU C 1 232 ? -17.560 54.917  -21.599 1.00 42.95 ? 226 GLU C CG    1 
ATOM   6404 C  CD    . GLU C 1 232 ? -18.565 53.850  -22.047 1.00 53.20 ? 226 GLU C CD    1 
ATOM   6405 O  OE1   . GLU C 1 232 ? -19.801 54.088  -21.968 1.00 51.28 ? 226 GLU C OE1   1 
ATOM   6406 O  OE2   . GLU C 1 232 ? -18.109 52.767  -22.478 1.00 60.59 ? 226 GLU C OE2   1 
ATOM   6407 N  N     . ARG C 1 233 ? -18.038 57.838  -17.994 1.00 29.47 ? 227 ARG C N     1 
ATOM   6408 C  CA    . ARG C 1 233 ? -18.490 59.029  -17.227 1.00 31.54 ? 227 ARG C CA    1 
ATOM   6409 C  C     . ARG C 1 233 ? -17.256 59.825  -16.766 1.00 31.39 ? 227 ARG C C     1 
ATOM   6410 O  O     . ARG C 1 233 ? -17.404 61.029  -16.499 1.00 31.23 ? 227 ARG C O     1 
ATOM   6411 C  CB    . ARG C 1 233 ? -19.416 58.521  -16.108 1.00 35.32 ? 227 ARG C CB    1 
ATOM   6412 C  CG    . ARG C 1 233 ? -20.231 59.552  -15.336 1.00 38.35 ? 227 ARG C CG    1 
ATOM   6413 C  CD    . ARG C 1 233 ? -21.067 58.963  -14.191 1.00 35.30 ? 227 ARG C CD    1 
ATOM   6414 N  NE    . ARG C 1 233 ? -21.766 57.753  -14.602 1.00 33.77 ? 227 ARG C NE    1 
ATOM   6415 C  CZ    . ARG C 1 233 ? -21.539 56.526  -14.119 1.00 35.53 ? 227 ARG C CZ    1 
ATOM   6416 N  NH1   . ARG C 1 233 ? -20.642 56.317  -13.167 1.00 32.63 ? 227 ARG C NH1   1 
ATOM   6417 N  NH2   . ARG C 1 233 ? -22.233 55.499  -14.583 1.00 39.21 ? 227 ARG C NH2   1 
ATOM   6418 N  N     . HIS C 1 234 ? -16.059 59.215  -16.711 1.00 25.65 ? 228 HIS C N     1 
ATOM   6419 C  CA    . HIS C 1 234 ? -14.804 59.879  -16.261 1.00 26.24 ? 228 HIS C CA    1 
ATOM   6420 C  C     . HIS C 1 234 ? -13.775 59.968  -17.404 1.00 30.30 ? 228 HIS C C     1 
ATOM   6421 O  O     . HIS C 1 234 ? -12.556 60.006  -17.108 1.00 26.32 ? 228 HIS C O     1 
ATOM   6422 C  CB    . HIS C 1 234 ? -14.278 59.127  -15.035 1.00 25.31 ? 228 HIS C CB    1 
ATOM   6423 C  CG    . HIS C 1 234 ? -15.217 59.156  -13.885 1.00 22.28 ? 228 HIS C CG    1 
ATOM   6424 N  ND1   . HIS C 1 234 ? -16.142 58.157  -13.674 1.00 23.39 ? 228 HIS C ND1   1 
ATOM   6425 C  CD2   . HIS C 1 234 ? -15.417 60.089  -12.919 1.00 23.77 ? 228 HIS C CD2   1 
ATOM   6426 C  CE1   . HIS C 1 234 ? -16.880 58.457  -12.616 1.00 25.53 ? 228 HIS C CE1   1 
ATOM   6427 N  NE2   . HIS C 1 234 ? -16.417 59.623  -12.095 1.00 22.62 ? 228 HIS C NE2   1 
ATOM   6428 N  N     . SER C 1 235 ? -14.241 60.021  -18.660 1.00 29.50 ? 229 SER C N     1 
ATOM   6429 C  CA    . SER C 1 235 ? -13.378 60.033  -19.876 1.00 34.65 ? 229 SER C CA    1 
ATOM   6430 C  C     . SER C 1 235 ? -12.491 61.298  -19.935 1.00 31.58 ? 229 SER C C     1 
ATOM   6431 O  O     . SER C 1 235 ? -11.467 61.259  -20.628 1.00 31.15 ? 229 SER C O     1 
ATOM   6432 C  CB    . SER C 1 235 ? -14.232 59.871  -21.121 1.00 35.43 ? 229 SER C CB    1 
ATOM   6433 O  OG    . SER C 1 235 ? -15.004 61.045  -21.350 1.00 38.19 ? 229 SER C OG    1 
ATOM   6434 N  N     . SER C 1 236 ? -12.806 62.365  -19.198 1.00 30.86 ? 230 SER C N     1 
ATOM   6435 C  CA    . SER C 1 236 ? -11.968 63.597  -19.136 1.00 32.58 ? 230 SER C CA    1 
ATOM   6436 C  C     . SER C 1 236 ? -10.728 63.380  -18.261 1.00 34.27 ? 230 SER C C     1 
ATOM   6437 O  O     . SER C 1 236 ? -9.807  64.217  -18.303 1.00 37.24 ? 230 SER C O     1 
ATOM   6438 C  CB    . SER C 1 236 ? -12.768 64.786  -18.614 1.00 37.44 ? 230 SER C CB    1 
ATOM   6439 O  OG    . SER C 1 236 ? -13.050 64.662  -17.214 1.00 37.71 ? 230 SER C OG    1 
ATOM   6440 N  N     . GLN C 1 237 ? -10.705 62.326  -17.453 1.00 28.08 ? 231 GLN C N     1 
ATOM   6441 C  CA    . GLN C 1 237 ? -9.593  62.100  -16.495 1.00 29.05 ? 231 GLN C CA    1 
ATOM   6442 C  C     . GLN C 1 237 ? -8.510  61.338  -17.239 1.00 30.72 ? 231 GLN C C     1 
ATOM   6443 O  O     . GLN C 1 237 ? -8.665  60.095  -17.420 1.00 31.63 ? 231 GLN C O     1 
ATOM   6444 C  CB    . GLN C 1 237 ? -10.091 61.342  -15.266 1.00 27.39 ? 231 GLN C CB    1 
ATOM   6445 C  CG    . GLN C 1 237 ? -11.251 62.028  -14.568 1.00 30.27 ? 231 GLN C CG    1 
ATOM   6446 C  CD    . GLN C 1 237 ? -10.852 63.372  -14.010 1.00 32.69 ? 231 GLN C CD    1 
ATOM   6447 O  OE1   . GLN C 1 237 ? -9.677  63.620  -13.753 1.00 28.77 ? 231 GLN C OE1   1 
ATOM   6448 N  NE2   . GLN C 1 237 ? -11.835 64.248  -13.818 1.00 31.50 ? 231 GLN C NE2   1 
ATOM   6449 N  N     . THR C 1 238 ? -7.434  62.025  -17.586 1.00 27.77 ? 232 THR C N     1 
ATOM   6450 C  CA    . THR C 1 238 ? -6.301  61.418  -18.314 1.00 31.69 ? 232 THR C CA    1 
ATOM   6451 C  C     . THR C 1 238 ? -5.525  60.490  -17.378 1.00 28.87 ? 232 THR C C     1 
ATOM   6452 O  O     . THR C 1 238 ? -4.773  59.664  -17.888 1.00 34.39 ? 232 THR C O     1 
ATOM   6453 C  CB    . THR C 1 238 ? -5.381  62.494  -18.907 1.00 35.80 ? 232 THR C CB    1 
ATOM   6454 O  OG1   . THR C 1 238 ? -4.811  63.135  -17.772 1.00 43.54 ? 232 THR C OG1   1 
ATOM   6455 C  CG2   . THR C 1 238 ? -6.107  63.502  -19.767 1.00 35.92 ? 232 THR C CG2   1 
ATOM   6456 N  N     . CYS C 1 239 ? -5.703  60.600  -16.072 1.00 27.26 ? 233 CYS C N     1 
ATOM   6457 C  CA    . CYS C 1 239 ? -4.997  59.741  -15.092 1.00 27.72 ? 233 CYS C CA    1 
ATOM   6458 C  C     . CYS C 1 239 ? -5.685  58.358  -14.964 1.00 24.41 ? 233 CYS C C     1 
ATOM   6459 O  O     . CYS C 1 239 ? -5.129  57.507  -14.225 1.00 21.41 ? 233 CYS C O     1 
ATOM   6460 C  CB    . CYS C 1 239 ? -4.902  60.477  -13.763 1.00 30.87 ? 233 CYS C CB    1 
ATOM   6461 S  SG    . CYS C 1 239 ? -6.525  60.852  -13.060 1.00 32.97 ? 233 CYS C SG    1 
ATOM   6462 N  N     . LEU C 1 240 ? -6.871  58.151  -15.551 1.00 23.88 ? 234 LEU C N     1 
ATOM   6463 C  CA    . LEU C 1 240 ? -7.724  56.944  -15.348 1.00 24.23 ? 234 LEU C CA    1 
ATOM   6464 C  C     . LEU C 1 240 ? -7.039  55.707  -15.950 1.00 25.94 ? 234 LEU C C     1 
ATOM   6465 O  O     . LEU C 1 240 ? -6.677  55.716  -17.129 1.00 23.60 ? 234 LEU C O     1 
ATOM   6466 C  CB    . LEU C 1 240 ? -9.115  57.150  -15.953 1.00 25.87 ? 234 LEU C CB    1 
ATOM   6467 C  CG    . LEU C 1 240 ? -10.106 55.986  -15.852 1.00 30.94 ? 234 LEU C CG    1 
ATOM   6468 C  CD1   . LEU C 1 240 ? -10.085 55.334  -14.501 1.00 33.60 ? 234 LEU C CD1   1 
ATOM   6469 C  CD2   . LEU C 1 240 ? -11.531 56.445  -16.154 1.00 33.32 ? 234 LEU C CD2   1 
ATOM   6470 N  N     . VAL C 1 241 ? -6.876  54.669  -15.129 1.00 24.67 ? 235 VAL C N     1 
ATOM   6471 C  CA    . VAL C 1 241 ? -6.270  53.363  -15.508 1.00 22.37 ? 235 VAL C CA    1 
ATOM   6472 C  C     . VAL C 1 241 ? -7.327  52.338  -15.174 1.00 24.09 ? 235 VAL C C     1 
ATOM   6473 O  O     . VAL C 1 241 ? -7.444  51.894  -14.029 1.00 22.92 ? 235 VAL C O     1 
ATOM   6474 C  CB    . VAL C 1 241 ? -4.949  53.073  -14.780 1.00 23.36 ? 235 VAL C CB    1 
ATOM   6475 C  CG1   . VAL C 1 241 ? -4.388  51.706  -15.149 1.00 23.86 ? 235 VAL C CG1   1 
ATOM   6476 C  CG2   . VAL C 1 241 ? -3.909  54.163  -15.019 1.00 22.52 ? 235 VAL C CG2   1 
ATOM   6477 N  N     . PRO C 1 242 ? -8.132  51.945  -16.164 1.00 25.08 ? 236 PRO C N     1 
ATOM   6478 C  CA    . PRO C 1 242 ? -9.237  51.020  -15.918 1.00 25.74 ? 236 PRO C CA    1 
ATOM   6479 C  C     . PRO C 1 242 ? -8.693  49.598  -15.806 1.00 23.82 ? 236 PRO C C     1 
ATOM   6480 O  O     . PRO C 1 242 ? -7.817  49.220  -16.619 1.00 23.70 ? 236 PRO C O     1 
ATOM   6481 C  CB    . PRO C 1 242 ? -10.138 51.185  -17.173 1.00 27.44 ? 236 PRO C CB    1 
ATOM   6482 C  CG    . PRO C 1 242 ? -9.177  51.644  -18.262 1.00 30.40 ? 236 PRO C CG    1 
ATOM   6483 C  CD    . PRO C 1 242 ? -8.029  52.368  -17.577 1.00 28.82 ? 236 PRO C CD    1 
ATOM   6484 N  N     . GLU C 1 243 ? -9.210  48.818  -14.858 1.00 22.70 ? 237 GLU C N     1 
ATOM   6485 C  CA    . GLU C 1 243 ? -8.799  47.388  -14.744 1.00 21.03 ? 237 GLU C CA    1 
ATOM   6486 C  C     . GLU C 1 243 ? -10.022 46.506  -14.596 1.00 20.61 ? 237 GLU C C     1 
ATOM   6487 O  O     . GLU C 1 243 ? -10.423 46.188  -13.474 1.00 19.75 ? 237 GLU C O     1 
ATOM   6488 C  CB    . GLU C 1 243 ? -7.840  47.202  -13.576 1.00 23.04 ? 237 GLU C CB    1 
ATOM   6489 C  CG    . GLU C 1 243 ? -6.562  47.945  -13.793 1.00 24.17 ? 237 GLU C CG    1 
ATOM   6490 C  CD    . GLU C 1 243 ? -5.459  47.585  -12.812 1.00 22.98 ? 237 GLU C CD    1 
ATOM   6491 O  OE1   . GLU C 1 243 ? -5.498  46.475  -12.246 1.00 23.39 ? 237 GLU C OE1   1 
ATOM   6492 O  OE2   . GLU C 1 243 ? -4.609  48.434  -12.580 1.00 24.83 ? 237 GLU C OE2   1 
ATOM   6493 N  N     . PRO C 1 244 ? -10.649 46.118  -15.730 1.00 20.43 ? 238 PRO C N     1 
ATOM   6494 C  CA    . PRO C 1 244 ? -11.704 45.111  -15.690 1.00 22.56 ? 238 PRO C CA    1 
ATOM   6495 C  C     . PRO C 1 244 ? -11.090 43.793  -15.204 1.00 20.17 ? 238 PRO C C     1 
ATOM   6496 O  O     . PRO C 1 244 ? -9.895  43.722  -15.199 1.00 18.34 ? 238 PRO C O     1 
ATOM   6497 C  CB    . PRO C 1 244 ? -12.188 45.064  -17.149 1.00 21.73 ? 238 PRO C CB    1 
ATOM   6498 C  CG    . PRO C 1 244 ? -11.056 45.559  -17.963 1.00 23.87 ? 238 PRO C CG    1 
ATOM   6499 C  CD    . PRO C 1 244 ? -10.362 46.585  -17.097 1.00 22.86 ? 238 PRO C CD    1 
ATOM   6500 N  N     . ASN C 1 245 ? -11.901 42.804  -14.818 1.00 21.49 ? 239 ASN C N     1 
ATOM   6501 C  CA    . ASN C 1 245 ? -11.398 41.517  -14.257 1.00 22.85 ? 239 ASN C CA    1 
ATOM   6502 C  C     . ASN C 1 245 ? -10.412 40.883  -15.244 1.00 23.52 ? 239 ASN C C     1 
ATOM   6503 O  O     . ASN C 1 245 ? -9.361  40.392  -14.793 1.00 22.70 ? 239 ASN C O     1 
ATOM   6504 C  CB    . ASN C 1 245 ? -12.532 40.547  -13.970 1.00 23.36 ? 239 ASN C CB    1 
ATOM   6505 C  CG    . ASN C 1 245 ? -13.467 40.977  -12.848 1.00 25.10 ? 239 ASN C CG    1 
ATOM   6506 O  OD1   . ASN C 1 245 ? -13.223 41.928  -12.078 1.00 23.44 ? 239 ASN C OD1   1 
ATOM   6507 N  ND2   . ASN C 1 245 ? -14.570 40.269  -12.766 1.00 21.25 ? 239 ASN C ND2   1 
ATOM   6508 N  N     . ARG C 1 246 ? -10.712 40.945  -16.545 1.00 23.91 ? 240 ARG C N     1 
ATOM   6509 C  CA    . ARG C 1 246 ? -9.828  40.362  -17.599 1.00 25.10 ? 240 ARG C CA    1 
ATOM   6510 C  C     . ARG C 1 246 ? -8.370  40.834  -17.411 1.00 23.95 ? 240 ARG C C     1 
ATOM   6511 O  O     . ARG C 1 246 ? -7.440  40.056  -17.633 1.00 24.35 ? 240 ARG C O     1 
ATOM   6512 C  CB    . ARG C 1 246 ? -10.374 40.766  -18.973 1.00 32.75 ? 240 ARG C CB    1 
ATOM   6513 C  CG    . ARG C 1 246 ? -9.358  40.675  -20.102 1.00 40.01 ? 240 ARG C CG    1 
ATOM   6514 C  CD    . ARG C 1 246 ? -10.004 40.836  -21.469 1.00 48.09 ? 240 ARG C CD    1 
ATOM   6515 N  NE    . ARG C 1 246 ? -8.997  40.892  -22.526 1.00 47.07 ? 240 ARG C NE    1 
ATOM   6516 C  CZ    . ARG C 1 246 ? -8.316  41.977  -22.880 1.00 55.69 ? 240 ARG C CZ    1 
ATOM   6517 N  NH1   . ARG C 1 246 ? -8.534  43.128  -22.265 1.00 58.80 ? 240 ARG C NH1   1 
ATOM   6518 N  NH2   . ARG C 1 246 ? -7.430  41.917  -23.866 1.00 58.67 ? 240 ARG C NH2   1 
ATOM   6519 N  N     . LEU C 1 247 ? -8.152  42.110  -17.128 1.00 19.20 ? 241 LEU C N     1 
ATOM   6520 C  CA    . LEU C 1 247 ? -6.791  42.687  -17.024 1.00 20.37 ? 241 LEU C CA    1 
ATOM   6521 C  C     . LEU C 1 247 ? -6.224  42.568  -15.598 1.00 20.88 ? 241 LEU C C     1 
ATOM   6522 O  O     . LEU C 1 247 ? -4.998  42.545  -15.458 1.00 21.95 ? 241 LEU C O     1 
ATOM   6523 C  CB    . LEU C 1 247 ? -6.826  44.157  -17.448 1.00 21.85 ? 241 LEU C CB    1 
ATOM   6524 C  CG    . LEU C 1 247 ? -6.884  44.412  -18.952 1.00 23.69 ? 241 LEU C CG    1 
ATOM   6525 C  CD1   . LEU C 1 247 ? -6.761  45.905  -19.224 1.00 24.68 ? 241 LEU C CD1   1 
ATOM   6526 C  CD2   . LEU C 1 247 ? -5.790  43.628  -19.691 1.00 22.52 ? 241 LEU C CD2   1 
ATOM   6527 N  N     . MET C 1 248 ? -7.052  42.578  -14.568 1.00 18.74 ? 242 MET C N     1 
ATOM   6528 C  CA    . MET C 1 248 ? -6.560  42.621  -13.162 1.00 20.26 ? 242 MET C CA    1 
ATOM   6529 C  C     . MET C 1 248 ? -6.164  41.222  -12.665 1.00 19.61 ? 242 MET C C     1 
ATOM   6530 O  O     . MET C 1 248 ? -5.227  41.133  -11.869 1.00 20.09 ? 242 MET C O     1 
ATOM   6531 C  CB    . MET C 1 248 ? -7.618  43.193  -12.220 1.00 20.08 ? 242 MET C CB    1 
ATOM   6532 C  CG    . MET C 1 248 ? -7.121  43.454  -10.812 1.00 20.17 ? 242 MET C CG    1 
ATOM   6533 S  SD    . MET C 1 248 ? -8.347  44.209  -9.722  1.00 21.06 ? 242 MET C SD    1 
ATOM   6534 C  CE    . MET C 1 248 ? -7.230  44.730  -8.407  1.00 18.08 ? 242 MET C CE    1 
ATOM   6535 N  N     . ALA C 1 249 ? -6.919  40.185  -13.006 1.00 19.72 ? 243 ALA C N     1 
ATOM   6536 C  CA    . ALA C 1 249 ? -6.933  38.938  -12.194 1.00 21.98 ? 243 ALA C CA    1 
ATOM   6537 C  C     . ALA C 1 249 ? -5.542  38.323  -12.102 1.00 20.94 ? 243 ALA C C     1 
ATOM   6538 O  O     . ALA C 1 249 ? -5.142  37.928  -10.964 1.00 20.16 ? 243 ALA C O     1 
ATOM   6539 C  CB    . ALA C 1 249 ? -7.904  37.940  -12.761 1.00 23.06 ? 243 ALA C CB    1 
ATOM   6540 N  N     . LYS C 1 250 ? -4.854  38.181  -13.239 1.00 19.47 ? 244 LYS C N     1 
ATOM   6541 C  CA    . LYS C 1 250 ? -3.580  37.425  -13.263 1.00 20.50 ? 244 LYS C CA    1 
ATOM   6542 C  C     . LYS C 1 250 ? -2.385  38.273  -13.719 1.00 18.86 ? 244 LYS C C     1 
ATOM   6543 O  O     . LYS C 1 250 ? -1.360  37.657  -14.071 1.00 19.46 ? 244 LYS C O     1 
ATOM   6544 C  CB    . LYS C 1 250 ? -3.771  36.189  -14.147 1.00 23.77 ? 244 LYS C CB    1 
ATOM   6545 C  CG    . LYS C 1 250 ? -4.761  35.195  -13.545 1.00 26.63 ? 244 LYS C CG    1 
ATOM   6546 C  CD    . LYS C 1 250 ? -5.408  34.249  -14.526 1.00 31.19 ? 244 LYS C CD    1 
ATOM   6547 C  CE    . LYS C 1 250 ? -6.552  34.878  -15.277 1.00 35.00 ? 244 LYS C CE    1 
ATOM   6548 N  NZ    . LYS C 1 250 ? -7.519  33.855  -15.747 1.00 35.38 ? 244 LYS C NZ    1 
ATOM   6549 N  N     . SER C 1 251 ? -2.445  39.599  -13.653 1.00 17.35 ? 245 SER C N     1 
ATOM   6550 C  CA    . SER C 1 251 ? -1.419  40.508  -14.219 1.00 17.71 ? 245 SER C CA    1 
ATOM   6551 C  C     . SER C 1 251 ? -0.484  41.019  -13.106 1.00 17.83 ? 245 SER C C     1 
ATOM   6552 O  O     . SER C 1 251 ? 0.360   41.848  -13.415 1.00 18.32 ? 245 SER C O     1 
ATOM   6553 C  CB    . SER C 1 251 ? -2.089  41.654  -14.927 1.00 18.42 ? 245 SER C CB    1 
ATOM   6554 O  OG    . SER C 1 251 ? -2.894  42.404  -14.024 1.00 18.38 ? 245 SER C OG    1 
ATOM   6555 N  N     . TYR C 1 252 ? -0.626  40.544  -11.861 1.00 16.77 ? 246 TYR C N     1 
ATOM   6556 C  CA    . TYR C 1 252 ? 0.197   40.983  -10.711 1.00 17.76 ? 246 TYR C CA    1 
ATOM   6557 C  C     . TYR C 1 252 ? 1.125   39.845  -10.294 1.00 20.16 ? 246 TYR C C     1 
ATOM   6558 O  O     . TYR C 1 252 ? 0.774   38.648  -10.402 1.00 18.90 ? 246 TYR C O     1 
ATOM   6559 C  CB    . TYR C 1 252 ? -0.662  41.478  -9.550  1.00 17.69 ? 246 TYR C CB    1 
ATOM   6560 C  CG    . TYR C 1 252 ? -1.381  42.780  -9.835  1.00 16.56 ? 246 TYR C CG    1 
ATOM   6561 C  CD1   . TYR C 1 252 ? -2.565  42.799  -10.562 1.00 18.44 ? 246 TYR C CD1   1 
ATOM   6562 C  CD2   . TYR C 1 252 ? -0.906  43.988  -9.352  1.00 17.54 ? 246 TYR C CD2   1 
ATOM   6563 C  CE1   . TYR C 1 252 ? -3.225  43.985  -10.852 1.00 18.00 ? 246 TYR C CE1   1 
ATOM   6564 C  CE2   . TYR C 1 252 ? -1.587  45.177  -9.590  1.00 17.61 ? 246 TYR C CE2   1 
ATOM   6565 C  CZ    . TYR C 1 252 ? -2.745  45.174  -10.336 1.00 18.65 ? 246 TYR C CZ    1 
ATOM   6566 O  OH    . TYR C 1 252 ? -3.430  46.321  -10.581 1.00 20.21 ? 246 TYR C OH    1 
ATOM   6567 N  N     . LEU C 1 253 ? 2.308   40.252  -9.839  1.00 19.90 ? 247 LEU C N     1 
ATOM   6568 C  CA    . LEU C 1 253 ? 3.224   39.404  -9.047  1.00 20.24 ? 247 LEU C CA    1 
ATOM   6569 C  C     . LEU C 1 253 ? 2.963   39.690  -7.565  1.00 20.16 ? 247 LEU C C     1 
ATOM   6570 O  O     . LEU C 1 253 ? 3.252   40.832  -7.083  1.00 18.81 ? 247 LEU C O     1 
ATOM   6571 C  CB    . LEU C 1 253 ? 4.652   39.740  -9.463  1.00 19.27 ? 247 LEU C CB    1 
ATOM   6572 C  CG    . LEU C 1 253 ? 5.059   39.290  -10.858 1.00 21.55 ? 247 LEU C CG    1 
ATOM   6573 C  CD1   . LEU C 1 253 ? 6.345   39.949  -11.307 1.00 25.32 ? 247 LEU C CD1   1 
ATOM   6574 C  CD2   . LEU C 1 253 ? 5.157   37.788  -10.956 1.00 24.90 ? 247 LEU C CD2   1 
ATOM   6575 N  N     . ILE C 1 254 ? 2.352   38.726  -6.882  1.00 17.51 ? 248 ILE C N     1 
ATOM   6576 C  CA    . ILE C 1 254 ? 1.824   38.913  -5.507  1.00 19.04 ? 248 ILE C CA    1 
ATOM   6577 C  C     . ILE C 1 254 ? 2.587   38.014  -4.542  1.00 18.23 ? 248 ILE C C     1 
ATOM   6578 O  O     . ILE C 1 254 ? 2.450   36.795  -4.671  1.00 20.47 ? 248 ILE C O     1 
ATOM   6579 C  CB    . ILE C 1 254 ? 0.319   38.610  -5.457  1.00 19.43 ? 248 ILE C CB    1 
ATOM   6580 C  CG1   . ILE C 1 254 ? -0.401  39.391  -6.557  1.00 20.49 ? 248 ILE C CG1   1 
ATOM   6581 C  CG2   . ILE C 1 254 ? -0.239  38.904  -4.068  1.00 21.70 ? 248 ILE C CG2   1 
ATOM   6582 C  CD1   . ILE C 1 254 ? -1.855  39.046  -6.695  1.00 23.31 ? 248 ILE C CD1   1 
ATOM   6583 N  N     . LEU C 1 255 ? 3.361   38.604  -3.639  1.00 18.64 ? 249 LEU C N     1 
ATOM   6584 C  CA    . LEU C 1 255 ? 4.041   37.872  -2.536  1.00 21.74 ? 249 LEU C CA    1 
ATOM   6585 C  C     . LEU C 1 255 ? 3.158   38.003  -1.296  1.00 20.05 ? 249 LEU C C     1 
ATOM   6586 O  O     . LEU C 1 255 ? 2.792   39.116  -0.923  1.00 19.62 ? 249 LEU C O     1 
ATOM   6587 C  CB    . LEU C 1 255 ? 5.409   38.490  -2.229  1.00 23.50 ? 249 LEU C CB    1 
ATOM   6588 C  CG    . LEU C 1 255 ? 6.591   38.099  -3.099  1.00 27.23 ? 249 LEU C CG    1 
ATOM   6589 C  CD1   . LEU C 1 255 ? 7.842   38.742  -2.496  1.00 28.93 ? 249 LEU C CD1   1 
ATOM   6590 C  CD2   . LEU C 1 255 ? 6.756   36.586  -3.211  1.00 24.90 ? 249 LEU C CD2   1 
ATOM   6591 N  N     . ASP C 1 256 ? 2.907   36.902  -0.625  1.00 19.17 ? 250 ASP C N     1 
ATOM   6592 C  CA    . ASP C 1 256 ? 2.101   36.897  0.610   1.00 18.74 ? 250 ASP C CA    1 
ATOM   6593 C  C     . ASP C 1 256 ? 2.995   37.139  1.826   1.00 19.22 ? 250 ASP C C     1 
ATOM   6594 O  O     . ASP C 1 256 ? 4.192   37.487  1.660   1.00 19.52 ? 250 ASP C O     1 
ATOM   6595 C  CB    . ASP C 1 256 ? 1.262   35.623  0.700   1.00 19.62 ? 250 ASP C CB    1 
ATOM   6596 C  CG    . ASP C 1 256 ? 1.994   34.344  1.052   1.00 22.46 ? 250 ASP C CG    1 
ATOM   6597 O  OD1   . ASP C 1 256 ? 3.225   34.392  1.251   1.00 19.64 ? 250 ASP C OD1   1 
ATOM   6598 O  OD2   . ASP C 1 256 ? 1.272   33.286  1.168   1.00 21.20 ? 250 ASP C OD2   1 
ATOM   6599 N  N     . GLU C 1 257 ? 2.436   36.959  3.015   1.00 18.42 ? 251 GLU C N     1 
ATOM   6600 C  CA    . GLU C 1 257 ? 3.116   37.317  4.281   1.00 19.11 ? 251 GLU C CA    1 
ATOM   6601 C  C     . GLU C 1 257 ? 4.272   36.349  4.575   1.00 20.52 ? 251 GLU C C     1 
ATOM   6602 O  O     . GLU C 1 257 ? 5.112   36.727  5.433   1.00 21.24 ? 251 GLU C O     1 
ATOM   6603 C  CB    . GLU C 1 257 ? 2.117   37.413  5.448   1.00 19.72 ? 251 GLU C CB    1 
ATOM   6604 C  CG    . GLU C 1 257 ? 1.462   36.079  5.815   1.00 21.45 ? 251 GLU C CG    1 
ATOM   6605 C  CD    . GLU C 1 257 ? 0.183   35.677  5.082   1.00 23.06 ? 251 GLU C CD    1 
ATOM   6606 O  OE1   . GLU C 1 257 ? -0.035  36.123  3.926   1.00 21.82 ? 251 GLU C OE1   1 
ATOM   6607 O  OE2   . GLU C 1 257 ? -0.600  34.885  5.666   1.00 27.72 ? 251 GLU C OE2   1 
ATOM   6608 N  N     . TYR C 1 258 ? 4.351   35.194  3.896   1.00 18.97 ? 252 TYR C N     1 
ATOM   6609 C  CA    . TYR C 1 258 ? 5.469   34.218  3.992   1.00 21.30 ? 252 TYR C CA    1 
ATOM   6610 C  C     . TYR C 1 258 ? 6.390   34.343  2.777   1.00 19.30 ? 252 TYR C C     1 
ATOM   6611 O  O     . TYR C 1 258 ? 7.266   33.490  2.615   1.00 21.25 ? 252 TYR C O     1 
ATOM   6612 C  CB    . TYR C 1 258 ? 4.939   32.782  4.084   1.00 23.55 ? 252 TYR C CB    1 
ATOM   6613 C  CG    . TYR C 1 258 ? 4.147   32.487  5.340   1.00 23.80 ? 252 TYR C CG    1 
ATOM   6614 C  CD1   . TYR C 1 258 ? 4.774   32.134  6.525   1.00 29.21 ? 252 TYR C CD1   1 
ATOM   6615 C  CD2   . TYR C 1 258 ? 2.766   32.590  5.352   1.00 26.80 ? 252 TYR C CD2   1 
ATOM   6616 C  CE1   . TYR C 1 258 ? 4.052   31.860  7.679   1.00 27.65 ? 252 TYR C CE1   1 
ATOM   6617 C  CE2   . TYR C 1 258 ? 2.021   32.314  6.489   1.00 27.33 ? 252 TYR C CE2   1 
ATOM   6618 C  CZ    . TYR C 1 258 ? 2.672   31.969  7.659   1.00 30.75 ? 252 TYR C CZ    1 
ATOM   6619 O  OH    . TYR C 1 258 ? 1.953   31.738  8.793   1.00 35.20 ? 252 TYR C OH    1 
ATOM   6620 N  N     . MET C 1 259 ? 6.214   35.372  1.953   1.00 20.02 ? 253 MET C N     1 
ATOM   6621 C  CA    . MET C 1 259 ? 6.997   35.611  0.707   1.00 20.83 ? 253 MET C CA    1 
ATOM   6622 C  C     . MET C 1 259 ? 6.854   34.427  -0.260  1.00 20.50 ? 253 MET C C     1 
ATOM   6623 O  O     . MET C 1 259 ? 7.802   34.018  -0.927  1.00 19.76 ? 253 MET C O     1 
ATOM   6624 C  CB    . MET C 1 259 ? 8.455   35.945  1.059   1.00 20.68 ? 253 MET C CB    1 
ATOM   6625 C  CG    . MET C 1 259 ? 8.543   37.115  2.008   1.00 24.53 ? 253 MET C CG    1 
ATOM   6626 S  SD    . MET C 1 259 ? 10.193  37.873  2.159   1.00 26.31 ? 253 MET C SD    1 
ATOM   6627 C  CE    . MET C 1 259 ? 10.028  39.287  1.066   1.00 26.24 ? 253 MET C CE    1 
ATOM   6628 N  N     . ARG C 1 260 ? 5.630   33.956  -0.420  1.00 21.14 ? 254 ARG C N     1 
ATOM   6629 C  CA    . ARG C 1 260 ? 5.250   32.978  -1.456  1.00 21.22 ? 254 ARG C CA    1 
ATOM   6630 C  C     . ARG C 1 260 ? 4.512   33.740  -2.561  1.00 21.44 ? 254 ARG C C     1 
ATOM   6631 O  O     . ARG C 1 260 ? 3.708   34.606  -2.194  1.00 18.31 ? 254 ARG C O     1 
ATOM   6632 C  CB    . ARG C 1 260 ? 4.321   31.946  -0.819  1.00 21.06 ? 254 ARG C CB    1 
ATOM   6633 C  CG    . ARG C 1 260 ? 4.916   31.263  0.398   1.00 22.42 ? 254 ARG C CG    1 
ATOM   6634 C  CD    . ARG C 1 260 ? 4.020   30.234  1.048   1.00 22.44 ? 254 ARG C CD    1 
ATOM   6635 N  NE    . ARG C 1 260 ? 2.804   30.828  1.571   1.00 24.33 ? 254 ARG C NE    1 
ATOM   6636 C  CZ    . ARG C 1 260 ? 1.849   30.150  2.152   1.00 23.38 ? 254 ARG C CZ    1 
ATOM   6637 N  NH1   . ARG C 1 260 ? 1.988   28.846  2.322   1.00 22.34 ? 254 ARG C NH1   1 
ATOM   6638 N  NH2   . ARG C 1 260 ? 0.790   30.777  2.624   1.00 24.15 ? 254 ARG C NH2   1 
ATOM   6639 N  N     . PHE C 1 261 ? 4.705   33.373  -3.826  1.00 21.07 ? 255 PHE C N     1 
ATOM   6640 C  CA    . PHE C 1 261 ? 3.948   33.977  -4.957  1.00 18.74 ? 255 PHE C CA    1 
ATOM   6641 C  C     . PHE C 1 261 ? 2.556   33.349  -4.938  1.00 19.76 ? 255 PHE C C     1 
ATOM   6642 O  O     . PHE C 1 261 ? 2.447   32.141  -4.685  1.00 19.41 ? 255 PHE C O     1 
ATOM   6643 C  CB    . PHE C 1 261 ? 4.673   33.763  -6.280  1.00 18.30 ? 255 PHE C CB    1 
ATOM   6644 C  CG    . PHE C 1 261 ? 5.795   34.718  -6.525  1.00 18.82 ? 255 PHE C CG    1 
ATOM   6645 C  CD1   . PHE C 1 261 ? 5.542   36.062  -6.711  1.00 19.28 ? 255 PHE C CD1   1 
ATOM   6646 C  CD2   . PHE C 1 261 ? 7.094   34.262  -6.660  1.00 20.39 ? 255 PHE C CD2   1 
ATOM   6647 C  CE1   . PHE C 1 261 ? 6.580   36.947  -6.952  1.00 22.57 ? 255 PHE C CE1   1 
ATOM   6648 C  CE2   . PHE C 1 261 ? 8.130   35.143  -6.913  1.00 21.67 ? 255 PHE C CE2   1 
ATOM   6649 C  CZ    . PHE C 1 261 ? 7.878   36.480  -7.042  1.00 22.99 ? 255 PHE C CZ    1 
ATOM   6650 N  N     . LEU C 1 262 ? 1.510   34.155  -5.089  1.00 17.98 ? 256 LEU C N     1 
ATOM   6651 C  CA    . LEU C 1 262 ? 0.133   33.642  -5.179  1.00 19.25 ? 256 LEU C CA    1 
ATOM   6652 C  C     . LEU C 1 262 ? -0.249  33.502  -6.648  1.00 19.93 ? 256 LEU C C     1 
ATOM   6653 O  O     . LEU C 1 262 ? -0.117  34.433  -7.449  1.00 20.19 ? 256 LEU C O     1 
ATOM   6654 C  CB    . LEU C 1 262 ? -0.799  34.579  -4.408  1.00 19.32 ? 256 LEU C CB    1 
ATOM   6655 C  CG    . LEU C 1 262 ? -0.438  34.771  -2.934  1.00 18.75 ? 256 LEU C CG    1 
ATOM   6656 C  CD1   . LEU C 1 262 ? -1.528  35.579  -2.227  1.00 20.81 ? 256 LEU C CD1   1 
ATOM   6657 C  CD2   . LEU C 1 262 ? -0.256  33.437  -2.219  1.00 18.91 ? 256 LEU C CD2   1 
ATOM   6658 N  N     . ASN C 1 263 ? -0.687  32.304  -6.994  1.00 20.08 ? 257 ASN C N     1 
ATOM   6659 C  CA    . ASN C 1 263 ? -1.170  31.973  -8.339  1.00 20.52 ? 257 ASN C CA    1 
ATOM   6660 C  C     . ASN C 1 263 ? -2.671  32.242  -8.370  1.00 21.68 ? 257 ASN C C     1 
ATOM   6661 O  O     . ASN C 1 263 ? -3.425  31.662  -7.529  1.00 21.33 ? 257 ASN C O     1 
ATOM   6662 C  CB    . ASN C 1 263 ? -0.831  30.529  -8.677  1.00 20.47 ? 257 ASN C CB    1 
ATOM   6663 C  CG    . ASN C 1 263 ? -1.122  30.174  -10.112 1.00 22.50 ? 257 ASN C CG    1 
ATOM   6664 O  OD1   . ASN C 1 263 ? -1.452  31.064  -10.910 1.00 21.80 ? 257 ASN C OD1   1 
ATOM   6665 N  ND2   . ASN C 1 263 ? -0.859  28.917  -10.470 1.00 20.70 ? 257 ASN C ND2   1 
ATOM   6666 N  N     . CYS C 1 264 ? -3.099  33.068  -9.320  1.00 22.48 ? 258 CYS C N     1 
ATOM   6667 C  CA    . CYS C 1 264 ? -4.520  33.487  -9.431  1.00 23.28 ? 258 CYS C CA    1 
ATOM   6668 C  C     . CYS C 1 264 ? -5.196  32.789  -10.621 1.00 25.44 ? 258 CYS C C     1 
ATOM   6669 O  O     . CYS C 1 264 ? -6.351  33.135  -10.937 1.00 25.57 ? 258 CYS C O     1 
ATOM   6670 C  CB    . CYS C 1 264 ? -4.646  35.003  -9.470  1.00 23.86 ? 258 CYS C CB    1 
ATOM   6671 S  SG    . CYS C 1 264 ? -4.144  35.765  -7.901  1.00 25.45 ? 258 CYS C SG    1 
ATOM   6672 N  N     . THR C 1 265 ? -4.554  31.773  -11.188 1.00 24.12 ? 259 THR C N     1 
ATOM   6673 C  CA    . THR C 1 265 ? -5.206  30.838  -12.130 1.00 25.10 ? 259 THR C CA    1 
ATOM   6674 C  C     . THR C 1 265 ? -6.543  30.354  -11.540 1.00 26.98 ? 259 THR C C     1 
ATOM   6675 O  O     . THR C 1 265 ? -6.623  30.120  -10.296 1.00 24.07 ? 259 THR C O     1 
ATOM   6676 C  CB    . THR C 1 265 ? -4.277  29.666  -12.423 1.00 24.89 ? 259 THR C CB    1 
ATOM   6677 O  OG1   . THR C 1 265 ? -3.245  30.207  -13.231 1.00 26.58 ? 259 THR C OG1   1 
ATOM   6678 C  CG2   . THR C 1 265 ? -4.977  28.547  -13.156 1.00 30.17 ? 259 THR C CG2   1 
ATOM   6679 N  N     . GLY C 1 266 ? -7.591  30.302  -12.367 1.00 28.43 ? 260 GLY C N     1 
ATOM   6680 C  CA    . GLY C 1 266 ? -8.883  29.711  -11.955 1.00 28.14 ? 260 GLY C CA    1 
ATOM   6681 C  C     . GLY C 1 266 ? -9.641  30.538  -10.909 1.00 30.92 ? 260 GLY C C     1 
ATOM   6682 O  O     . GLY C 1 266 ? -10.553 29.975  -10.266 1.00 32.37 ? 260 GLY C O     1 
ATOM   6683 N  N     . GLY C 1 267 ? -9.320  31.813  -10.720 1.00 25.61 ? 261 GLY C N     1 
ATOM   6684 C  CA    . GLY C 1 267 ? -10.015 32.671  -9.746  1.00 28.10 ? 261 GLY C CA    1 
ATOM   6685 C  C     . GLY C 1 267 ? -9.646  32.333  -8.301  1.00 26.39 ? 261 GLY C C     1 
ATOM   6686 O  O     . GLY C 1 267 ? -10.446 32.651  -7.408  1.00 24.91 ? 261 GLY C O     1 
ATOM   6687 N  N     . ARG C 1 268 ? -8.439  31.793  -8.076  1.00 25.63 ? 262 ARG C N     1 
ATOM   6688 C  CA    . ARG C 1 268 ? -7.941  31.351  -6.744  1.00 24.80 ? 262 ARG C CA    1 
ATOM   6689 C  C     . ARG C 1 268 ? -6.766  32.224  -6.288  1.00 24.98 ? 262 ARG C C     1 
ATOM   6690 O  O     . ARG C 1 268 ? -6.425  33.180  -7.000  1.00 23.98 ? 262 ARG C O     1 
ATOM   6691 C  CB    . ARG C 1 268 ? -7.531  29.883  -6.848  1.00 27.24 ? 262 ARG C CB    1 
ATOM   6692 C  CG    . ARG C 1 268 ? -8.676  28.964  -7.244  1.00 28.98 ? 262 ARG C CG    1 
ATOM   6693 C  CD    . ARG C 1 268 ? -8.193  27.535  -7.242  1.00 33.81 ? 262 ARG C CD    1 
ATOM   6694 N  NE    . ARG C 1 268 ? -7.732  27.087  -5.932  1.00 30.12 ? 262 ARG C NE    1 
ATOM   6695 C  CZ    . ARG C 1 268 ? -8.494  26.593  -4.964  1.00 35.07 ? 262 ARG C CZ    1 
ATOM   6696 N  NH1   . ARG C 1 268 ? -9.807  26.478  -5.119  1.00 35.33 ? 262 ARG C NH1   1 
ATOM   6697 N  NH2   . ARG C 1 268 ? -7.917  26.202  -3.832  1.00 34.45 ? 262 ARG C NH2   1 
ATOM   6698 N  N     . LYS C 1 269 ? -6.184  31.919  -5.127  1.00 23.22 ? 263 LYS C N     1 
ATOM   6699 C  CA    . LYS C 1 269 ? -4.960  32.597  -4.615  1.00 21.91 ? 263 LYS C CA    1 
ATOM   6700 C  C     . LYS C 1 269 ? -4.084  31.550  -3.936  1.00 24.43 ? 263 LYS C C     1 
ATOM   6701 O  O     . LYS C 1 269 ? -3.976  31.560  -2.702  1.00 27.04 ? 263 LYS C O     1 
ATOM   6702 C  CB    . LYS C 1 269 ? -5.339  33.762  -3.695  1.00 22.04 ? 263 LYS C CB    1 
ATOM   6703 C  CG    . LYS C 1 269 ? -4.887  35.128  -4.185  1.00 22.73 ? 263 LYS C CG    1 
ATOM   6704 C  CD    . LYS C 1 269 ? -5.281  36.249  -3.258  1.00 21.11 ? 263 LYS C CD    1 
ATOM   6705 C  CE    . LYS C 1 269 ? -4.908  37.585  -3.866  1.00 22.05 ? 263 LYS C CE    1 
ATOM   6706 N  NZ    . LYS C 1 269 ? -5.332  38.725  -3.022  1.00 20.18 ? 263 LYS C NZ    1 
ATOM   6707 N  N     . ASP C 1 270 ? -3.539  30.624  -4.722  1.00 22.98 ? 264 ASP C N     1 
ATOM   6708 C  CA    . ASP C 1 270 ? -2.814  29.446  -4.196  1.00 22.31 ? 264 ASP C CA    1 
ATOM   6709 C  C     . ASP C 1 270 ? -1.322  29.742  -4.176  1.00 21.95 ? 264 ASP C C     1 
ATOM   6710 O  O     . ASP C 1 270 ? -0.720  30.124  -5.187  1.00 21.50 ? 264 ASP C O     1 
ATOM   6711 C  CB    . ASP C 1 270 ? -3.104  28.190  -5.006  1.00 23.36 ? 264 ASP C CB    1 
ATOM   6712 C  CG    . ASP C 1 270 ? -4.491  27.578  -4.785  1.00 27.84 ? 264 ASP C CG    1 
ATOM   6713 O  OD1   . ASP C 1 270 ? -5.138  27.840  -3.709  1.00 32.58 ? 264 ASP C OD1   1 
ATOM   6714 O  OD2   . ASP C 1 270 ? -4.936  26.851  -5.694  1.00 32.00 ? 264 ASP C OD2   1 
ATOM   6715 N  N     . PRO C 1 271 ? -0.685  29.596  -3.002  1.00 21.71 ? 265 PRO C N     1 
ATOM   6716 C  CA    . PRO C 1 271 ? 0.731   29.960  -2.878  1.00 20.94 ? 265 PRO C CA    1 
ATOM   6717 C  C     . PRO C 1 271 ? 1.724   28.933  -3.436  1.00 21.61 ? 265 PRO C C     1 
ATOM   6718 O  O     . PRO C 1 271 ? 1.517   27.708  -3.310  1.00 23.17 ? 265 PRO C O     1 
ATOM   6719 C  CB    . PRO C 1 271 ? 0.900   30.093  -1.349  1.00 22.62 ? 265 PRO C CB    1 
ATOM   6720 C  CG    . PRO C 1 271 ? -0.136  29.125  -0.782  1.00 24.59 ? 265 PRO C CG    1 
ATOM   6721 C  CD    . PRO C 1 271 ? -1.308  29.204  -1.731  1.00 21.33 ? 265 PRO C CD    1 
ATOM   6722 N  N     . SER C 1 272 ? 2.815   29.445  -3.967  1.00 20.19 ? 266 SER C N     1 
ATOM   6723 C  CA    . SER C 1 272 ? 4.057   28.695  -4.268  1.00 20.09 ? 266 SER C CA    1 
ATOM   6724 C  C     . SER C 1 272 ? 4.766   28.372  -2.942  1.00 20.43 ? 266 SER C C     1 
ATOM   6725 O  O     . SER C 1 272 ? 4.305   28.760  -1.847  1.00 19.01 ? 266 SER C O     1 
ATOM   6726 C  CB    . SER C 1 272 ? 4.955   29.522  -5.171  1.00 20.13 ? 266 SER C CB    1 
ATOM   6727 O  OG    . SER C 1 272 ? 5.534   30.596  -4.416  1.00 20.60 ? 266 SER C OG    1 
ATOM   6728 N  N     . LYS C 1 273 ? 5.934   27.769  -3.046  1.00 21.45 ? 267 LYS C N     1 
ATOM   6729 C  CA    . LYS C 1 273 ? 6.882   27.737  -1.925  1.00 24.42 ? 267 LYS C CA    1 
ATOM   6730 C  C     . LYS C 1 273 ? 7.449   29.142  -1.721  1.00 22.42 ? 267 LYS C C     1 
ATOM   6731 O  O     . LYS C 1 273 ? 7.493   29.912  -2.668  1.00 22.82 ? 267 LYS C O     1 
ATOM   6732 C  CB    . LYS C 1 273 ? 7.981   26.728  -2.252  1.00 26.70 ? 267 LYS C CB    1 
ATOM   6733 C  CG    . LYS C 1 273 ? 7.530   25.273  -2.200  1.00 30.33 ? 267 LYS C CG    1 
ATOM   6734 C  CD    . LYS C 1 273 ? 6.874   24.886  -0.913  1.00 36.48 ? 267 LYS C CD    1 
ATOM   6735 C  CE    . LYS C 1 273 ? 6.505   23.411  -0.844  1.00 44.44 ? 267 LYS C CE    1 
ATOM   6736 N  NZ    . LYS C 1 273 ? 7.684   22.555  -1.120  1.00 50.45 ? 267 LYS C NZ    1 
ATOM   6737 N  N     . SER C 1 274 ? 7.942   29.417  -0.536  1.00 22.20 ? 268 SER C N     1 
ATOM   6738 C  CA    . SER C 1 274 ? 8.524   30.734  -0.228  1.00 22.04 ? 268 SER C CA    1 
ATOM   6739 C  C     . SER C 1 274 ? 9.763   30.955  -1.097  1.00 25.34 ? 268 SER C C     1 
ATOM   6740 O  O     . SER C 1 274 ? 10.585  29.985  -1.277  1.00 23.80 ? 268 SER C O     1 
ATOM   6741 C  CB    . SER C 1 274 ? 8.838   30.863  1.213   1.00 22.89 ? 268 SER C CB    1 
ATOM   6742 O  OG    . SER C 1 274 ? 9.366   32.163  1.432   1.00 22.60 ? 268 SER C OG    1 
ATOM   6743 N  N     . ILE C 1 275 ? 9.951   32.192  -1.557  1.00 22.34 ? 269 ILE C N     1 
ATOM   6744 C  CA    . ILE C 1 275 ? 11.215  32.580  -2.240  1.00 24.80 ? 269 ILE C CA    1 
ATOM   6745 C  C     . ILE C 1 275 ? 12.381  32.377  -1.261  1.00 26.70 ? 269 ILE C C     1 
ATOM   6746 O  O     . ILE C 1 275 ? 13.517  32.116  -1.750  1.00 24.56 ? 269 ILE C O     1 
ATOM   6747 C  CB    . ILE C 1 275 ? 11.196  34.027  -2.772  1.00 24.28 ? 269 ILE C CB    1 
ATOM   6748 C  CG1   . ILE C 1 275 ? 11.136  35.089  -1.663  1.00 24.28 ? 269 ILE C CG1   1 
ATOM   6749 C  CG2   . ILE C 1 275 ? 10.102  34.164  -3.803  1.00 23.85 ? 269 ILE C CG2   1 
ATOM   6750 C  CD1   . ILE C 1 275 ? 11.211  36.536  -2.158  1.00 23.62 ? 269 ILE C CD1   1 
ATOM   6751 N  N     . LEU C 1 276 ? 12.133  32.499  0.046   1.00 24.08 ? 270 LEU C N     1 
ATOM   6752 C  CA    . LEU C 1 276 ? 13.181  32.305  1.092   1.00 24.40 ? 270 LEU C CA    1 
ATOM   6753 C  C     . LEU C 1 276 ? 13.638  30.843  1.091   1.00 27.97 ? 270 LEU C C     1 
ATOM   6754 O  O     . LEU C 1 276 ? 14.758  30.595  1.545   1.00 28.56 ? 270 LEU C O     1 
ATOM   6755 C  CB    . LEU C 1 276 ? 12.628  32.683  2.472   1.00 26.81 ? 270 LEU C CB    1 
ATOM   6756 C  CG    . LEU C 1 276 ? 12.204  34.144  2.637   1.00 27.94 ? 270 LEU C CG    1 
ATOM   6757 C  CD1   . LEU C 1 276 ? 11.597  34.385  4.004   1.00 29.32 ? 270 LEU C CD1   1 
ATOM   6758 C  CD2   . LEU C 1 276 ? 13.365  35.087  2.397   1.00 29.03 ? 270 LEU C CD2   1 
ATOM   6759 N  N     . GLU C 1 277 ? 12.775  29.909  0.685   1.00 24.22 ? 271 GLU C N     1 
ATOM   6760 C  CA    . GLU C 1 277 ? 13.034  28.435  0.739   1.00 27.83 ? 271 GLU C CA    1 
ATOM   6761 C  C     . GLU C 1 277 ? 13.598  27.929  -0.598  1.00 28.57 ? 271 GLU C C     1 
ATOM   6762 O  O     . GLU C 1 277 ? 14.500  27.068  -0.554  1.00 28.01 ? 271 GLU C O     1 
ATOM   6763 C  CB    . GLU C 1 277 ? 11.767  27.671  1.112   1.00 31.39 ? 271 GLU C CB    1 
ATOM   6764 C  CG    . GLU C 1 277 ? 11.944  26.154  1.153   1.00 39.00 ? 271 GLU C CG    1 
ATOM   6765 C  CD    . GLU C 1 277 ? 10.648  25.358  1.225   1.00 44.55 ? 271 GLU C CD    1 
ATOM   6766 O  OE1   . GLU C 1 277 ? 9.691   25.855  1.858   1.00 55.01 ? 271 GLU C OE1   1 
ATOM   6767 O  OE2   . GLU C 1 277 ? 10.595  24.241  0.658   1.00 50.06 ? 271 GLU C OE2   1 
ATOM   6768 N  N     . VAL C 1 278 ? 13.078  28.396  -1.737  1.00 23.81 ? 272 VAL C N     1 
ATOM   6769 C  CA    . VAL C 1 278 ? 13.418  27.833  -3.083  1.00 25.61 ? 272 VAL C CA    1 
ATOM   6770 C  C     . VAL C 1 278 ? 14.033  28.886  -4.003  1.00 23.66 ? 272 VAL C C     1 
ATOM   6771 O  O     . VAL C 1 278 ? 14.467  28.502  -5.066  1.00 24.19 ? 272 VAL C O     1 
ATOM   6772 C  CB    . VAL C 1 278 ? 12.206  27.184  -3.770  1.00 25.50 ? 272 VAL C CB    1 
ATOM   6773 C  CG1   . VAL C 1 278 ? 11.692  25.973  -3.005  1.00 25.59 ? 272 VAL C CG1   1 
ATOM   6774 C  CG2   . VAL C 1 278 ? 11.107  28.195  -4.083  1.00 24.98 ? 272 VAL C CG2   1 
ATOM   6775 N  N     . GLY C 1 279 ? 14.070  30.165  -3.625  1.00 23.48 ? 273 GLY C N     1 
ATOM   6776 C  CA    . GLY C 1 279 ? 14.542  31.254  -4.496  1.00 23.57 ? 273 GLY C CA    1 
ATOM   6777 C  C     . GLY C 1 279 ? 13.446  31.779  -5.423  1.00 21.80 ? 273 GLY C C     1 
ATOM   6778 O  O     . GLY C 1 279 ? 12.414  31.126  -5.584  1.00 22.56 ? 273 GLY C O     1 
ATOM   6779 N  N     . VAL C 1 280 ? 13.720  32.896  -6.073  1.00 25.45 ? 274 VAL C N     1 
ATOM   6780 C  CA    . VAL C 1 280 ? 12.720  33.640  -6.875  1.00 23.91 ? 274 VAL C CA    1 
ATOM   6781 C  C     . VAL C 1 280 ? 12.365  32.835  -8.127  1.00 26.34 ? 274 VAL C C     1 
ATOM   6782 O  O     . VAL C 1 280 ? 11.158  32.663  -8.436  1.00 22.91 ? 274 VAL C O     1 
ATOM   6783 C  CB    . VAL C 1 280 ? 13.259  35.034  -7.208  1.00 23.43 ? 274 VAL C CB    1 
ATOM   6784 C  CG1   . VAL C 1 280 ? 12.361  35.731  -8.216  1.00 24.40 ? 274 VAL C CG1   1 
ATOM   6785 C  CG2   . VAL C 1 280 ? 13.442  35.879  -5.956  1.00 23.62 ? 274 VAL C CG2   1 
ATOM   6786 N  N     . GLN C 1 281 ? 13.355  32.346  -8.854  1.00 26.30 ? 275 GLN C N     1 
ATOM   6787 C  CA    . GLN C 1 281 ? 13.085  31.692  -10.157 1.00 29.05 ? 275 GLN C CA    1 
ATOM   6788 C  C     . GLN C 1 281 ? 12.197  30.453  -9.971  1.00 26.17 ? 275 GLN C C     1 
ATOM   6789 O  O     . GLN C 1 281 ? 11.240  30.311  -10.750 1.00 25.35 ? 275 GLN C O     1 
ATOM   6790 C  CB    . GLN C 1 281 ? 14.378  31.379  -10.919 1.00 34.96 ? 275 GLN C CB    1 
ATOM   6791 C  CG    . GLN C 1 281 ? 14.341  31.914  -12.356 1.00 45.98 ? 275 GLN C CG    1 
ATOM   6792 C  CD    . GLN C 1 281 ? 13.767  33.321  -12.486 1.00 49.15 ? 275 GLN C CD    1 
ATOM   6793 O  OE1   . GLN C 1 281 ? 14.288  34.299  -11.925 1.00 49.83 ? 275 GLN C OE1   1 
ATOM   6794 N  NE2   . GLN C 1 281 ? 12.662  33.433  -13.215 1.00 38.85 ? 275 GLN C NE2   1 
ATOM   6795 N  N     . GLN C 1 282 ? 12.450  29.596  -8.979  1.00 26.31 ? 276 GLN C N     1 
ATOM   6796 C  CA    . GLN C 1 282 ? 11.650  28.354  -8.777  1.00 26.89 ? 276 GLN C CA    1 
ATOM   6797 C  C     . GLN C 1 282 ? 10.229  28.729  -8.335  1.00 25.83 ? 276 GLN C C     1 
ATOM   6798 O  O     . GLN C 1 282 ? 9.248   28.145  -8.855  1.00 25.17 ? 276 GLN C O     1 
ATOM   6799 C  CB    . GLN C 1 282 ? 12.333  27.409  -7.782  1.00 29.99 ? 276 GLN C CB    1 
ATOM   6800 C  CG    . GLN C 1 282 ? 11.645  26.049  -7.680  1.00 34.30 ? 276 GLN C CG    1 
ATOM   6801 C  CD    . GLN C 1 282 ? 12.439  25.034  -6.878  1.00 39.25 ? 276 GLN C CD    1 
ATOM   6802 O  OE1   . GLN C 1 282 ? 13.649  24.917  -7.020  1.00 47.17 ? 276 GLN C OE1   1 
ATOM   6803 N  NE2   . GLN C 1 282 ? 11.755  24.268  -6.047  1.00 41.91 ? 276 GLN C NE2   1 
ATOM   6804 N  N     . ALA C 1 283 ? 10.086  29.695  -7.428  1.00 23.89 ? 277 ALA C N     1 
ATOM   6805 C  CA    . ALA C 1 283 ? 8.760   30.106  -6.921  1.00 23.19 ? 277 ALA C CA    1 
ATOM   6806 C  C     . ALA C 1 283 ? 7.967   30.779  -8.058  1.00 25.62 ? 277 ALA C C     1 
ATOM   6807 O  O     . ALA C 1 283 ? 6.747   30.476  -8.229  1.00 24.03 ? 277 ALA C O     1 
ATOM   6808 C  CB    . ALA C 1 283 ? 8.922   31.017  -5.734  1.00 22.35 ? 277 ALA C CB    1 
ATOM   6809 N  N     . LEU C 1 284 ? 8.599   31.675  -8.820  1.00 22.68 ? 278 LEU C N     1 
ATOM   6810 C  CA    . LEU C 1 284 ? 7.932   32.397  -9.926  1.00 22.97 ? 278 LEU C CA    1 
ATOM   6811 C  C     . LEU C 1 284 ? 7.513   31.408  -11.015 1.00 24.02 ? 278 LEU C C     1 
ATOM   6812 O  O     . LEU C 1 284 ? 6.393   31.536  -11.513 1.00 21.49 ? 278 LEU C O     1 
ATOM   6813 C  CB    . LEU C 1 284 ? 8.857   33.477  -10.488 1.00 22.91 ? 278 LEU C CB    1 
ATOM   6814 C  CG    . LEU C 1 284 ? 8.324   34.246  -11.694 1.00 26.38 ? 278 LEU C CG    1 
ATOM   6815 C  CD1   . LEU C 1 284 ? 6.993   34.902  -11.375 1.00 28.87 ? 278 LEU C CD1   1 
ATOM   6816 C  CD2   . LEU C 1 284 ? 9.326   35.297  -12.173 1.00 28.03 ? 278 LEU C CD2   1 
ATOM   6817 N  N     . GLN C 1 285 ? 8.372   30.465  -11.386 1.00 22.73 ? 279 GLN C N     1 
ATOM   6818 C  CA    . GLN C 1 285 ? 8.025   29.491  -12.453 1.00 25.48 ? 279 GLN C CA    1 
ATOM   6819 C  C     . GLN C 1 285 ? 6.831   28.628  -12.026 1.00 23.29 ? 279 GLN C C     1 
ATOM   6820 O  O     . GLN C 1 285 ? 6.085   28.184  -12.912 1.00 24.73 ? 279 GLN C O     1 
ATOM   6821 C  CB    . GLN C 1 285 ? 9.285   28.735  -12.895 1.00 29.67 ? 279 GLN C CB    1 
ATOM   6822 C  CG    . GLN C 1 285 ? 10.174  29.654  -13.763 1.00 39.26 ? 279 GLN C CG    1 
ATOM   6823 C  CD    . GLN C 1 285 ? 9.375   30.518  -14.741 1.00 45.33 ? 279 GLN C CD    1 
ATOM   6824 O  OE1   . GLN C 1 285 ? 9.335   31.763  -14.669 1.00 39.35 ? 279 GLN C OE1   1 
ATOM   6825 N  NE2   . GLN C 1 285 ? 8.658   29.857  -15.641 1.00 45.79 ? 279 GLN C NE2   1 
ATOM   6826 N  N     . ALA C 1 286 ? 6.569   28.474  -10.731 1.00 23.38 ? 280 ALA C N     1 
ATOM   6827 C  CA    . ALA C 1 286 ? 5.463   27.625  -10.240 1.00 23.54 ? 280 ALA C CA    1 
ATOM   6828 C  C     . ALA C 1 286 ? 4.118   28.329  -10.426 1.00 23.82 ? 280 ALA C C     1 
ATOM   6829 O  O     . ALA C 1 286 ? 3.092   27.624  -10.382 1.00 23.55 ? 280 ALA C O     1 
ATOM   6830 C  CB    . ALA C 1 286 ? 5.713   27.212  -8.811  1.00 25.28 ? 280 ALA C CB    1 
ATOM   6831 N  N     . VAL C 1 287 ? 4.088   29.654  -10.616 1.00 22.43 ? 281 VAL C N     1 
ATOM   6832 C  CA    . VAL C 1 287 ? 2.808   30.408  -10.742 1.00 20.61 ? 281 VAL C CA    1 
ATOM   6833 C  C     . VAL C 1 287 ? 2.662   30.945  -12.178 1.00 22.21 ? 281 VAL C C     1 
ATOM   6834 O  O     . VAL C 1 287 ? 3.592   30.819  -12.979 1.00 22.09 ? 281 VAL C O     1 
ATOM   6835 C  CB    . VAL C 1 287 ? 2.662   31.523  -9.690  1.00 20.84 ? 281 VAL C CB    1 
ATOM   6836 C  CG1   . VAL C 1 287 ? 2.900   31.016  -8.261  1.00 21.74 ? 281 VAL C CG1   1 
ATOM   6837 C  CG2   . VAL C 1 287 ? 3.557   32.715  -9.990  1.00 21.97 ? 281 VAL C CG2   1 
ATOM   6838 N  N     . PHE C 1 288 ? 1.467   31.443  -12.502 1.00 20.57 ? 282 PHE C N     1 
ATOM   6839 C  CA    . PHE C 1 288 ? 1.131   32.104  -13.775 1.00 20.95 ? 282 PHE C CA    1 
ATOM   6840 C  C     . PHE C 1 288 ? 1.157   33.602  -13.568 1.00 18.67 ? 282 PHE C C     1 
ATOM   6841 O  O     . PHE C 1 288 ? 0.571   34.106  -12.581 1.00 20.77 ? 282 PHE C O     1 
ATOM   6842 C  CB    . PHE C 1 288 ? -0.259  31.715  -14.272 1.00 22.25 ? 282 PHE C CB    1 
ATOM   6843 C  CG    . PHE C 1 288 ? -0.653  32.390  -15.564 1.00 23.66 ? 282 PHE C CG    1 
ATOM   6844 C  CD1   . PHE C 1 288 ? 0.106   32.221  -16.724 1.00 26.54 ? 282 PHE C CD1   1 
ATOM   6845 C  CD2   . PHE C 1 288 ? -1.791  33.182  -15.613 1.00 23.18 ? 282 PHE C CD2   1 
ATOM   6846 C  CE1   . PHE C 1 288 ? -0.247  32.862  -17.913 1.00 28.79 ? 282 PHE C CE1   1 
ATOM   6847 C  CE2   . PHE C 1 288 ? -2.165  33.787  -16.807 1.00 25.84 ? 282 PHE C CE2   1 
ATOM   6848 C  CZ    . PHE C 1 288 ? -1.384  33.646  -17.943 1.00 28.54 ? 282 PHE C CZ    1 
ATOM   6849 N  N     . TRP C 1 289 ? 1.837   34.294  -14.464 1.00 20.42 ? 283 TRP C N     1 
ATOM   6850 C  CA    . TRP C 1 289 ? 1.855   35.784  -14.516 1.00 18.98 ? 283 TRP C CA    1 
ATOM   6851 C  C     . TRP C 1 289 ? 1.578   36.211  -15.958 1.00 19.42 ? 283 TRP C C     1 
ATOM   6852 O  O     . TRP C 1 289 ? 2.367   35.802  -16.855 1.00 20.21 ? 283 TRP C O     1 
ATOM   6853 C  CB    . TRP C 1 289 ? 3.173   36.343  -13.998 1.00 17.60 ? 283 TRP C CB    1 
ATOM   6854 C  CG    . TRP C 1 289 ? 3.247   37.842  -14.086 1.00 18.59 ? 283 TRP C CG    1 
ATOM   6855 C  CD1   . TRP C 1 289 ? 2.265   38.742  -13.793 1.00 19.28 ? 283 TRP C CD1   1 
ATOM   6856 C  CD2   . TRP C 1 289 ? 4.395   38.611  -14.456 1.00 18.91 ? 283 TRP C CD2   1 
ATOM   6857 N  NE1   . TRP C 1 289 ? 2.737   40.017  -13.930 1.00 19.48 ? 283 TRP C NE1   1 
ATOM   6858 C  CE2   . TRP C 1 289 ? 4.033   39.965  -14.358 1.00 20.39 ? 283 TRP C CE2   1 
ATOM   6859 C  CE3   . TRP C 1 289 ? 5.675   38.282  -14.909 1.00 19.76 ? 283 TRP C CE3   1 
ATOM   6860 C  CZ2   . TRP C 1 289 ? 4.930   40.990  -14.652 1.00 21.71 ? 283 TRP C CZ2   1 
ATOM   6861 C  CZ3   . TRP C 1 289 ? 6.566   39.294  -15.189 1.00 22.29 ? 283 TRP C CZ3   1 
ATOM   6862 C  CH2   . TRP C 1 289 ? 6.194   40.632  -15.071 1.00 22.21 ? 283 TRP C CH2   1 
ATOM   6863 N  N     . ASP C 1 290 ? 0.418   36.837  -16.188 1.00 19.70 ? 284 ASP C N     1 
ATOM   6864 C  CA    . ASP C 1 290 ? 0.010   37.290  -17.544 1.00 20.44 ? 284 ASP C CA    1 
ATOM   6865 C  C     . ASP C 1 290 ? 0.720   38.617  -17.844 1.00 18.67 ? 284 ASP C C     1 
ATOM   6866 O  O     . ASP C 1 290 ? 0.199   39.711  -17.488 1.00 19.19 ? 284 ASP C O     1 
ATOM   6867 C  CB    . ASP C 1 290 ? -1.505  37.351  -17.669 1.00 20.29 ? 284 ASP C CB    1 
ATOM   6868 C  CG    . ASP C 1 290 ? -1.953  37.544  -19.114 1.00 21.50 ? 284 ASP C CG    1 
ATOM   6869 O  OD1   . ASP C 1 290 ? -1.118  37.956  -19.956 1.00 22.51 ? 284 ASP C OD1   1 
ATOM   6870 O  OD2   . ASP C 1 290 ? -3.178  37.443  -19.349 1.00 25.01 ? 284 ASP C OD2   1 
ATOM   6871 N  N     . GLU C 1 291 ? 1.901   38.513  -18.408 1.00 19.53 ? 285 GLU C N     1 
ATOM   6872 C  CA    . GLU C 1 291 ? 2.772   39.676  -18.729 1.00 21.74 ? 285 GLU C CA    1 
ATOM   6873 C  C     . GLU C 1 291 ? 2.135   40.572  -19.793 1.00 20.28 ? 285 GLU C C     1 
ATOM   6874 O  O     . GLU C 1 291 ? 2.346   41.772  -19.721 1.00 20.82 ? 285 GLU C O     1 
ATOM   6875 C  CB    . GLU C 1 291 ? 4.134   39.250  -19.248 1.00 27.48 ? 285 GLU C CB    1 
ATOM   6876 C  CG    . GLU C 1 291 ? 5.062   38.850  -18.155 1.00 33.20 ? 285 GLU C CG    1 
ATOM   6877 C  CD    . GLU C 1 291 ? 6.388   38.318  -18.687 1.00 36.83 ? 285 GLU C CD    1 
ATOM   6878 O  OE1   . GLU C 1 291 ? 7.233   39.151  -19.005 1.00 37.89 ? 285 GLU C OE1   1 
ATOM   6879 O  OE2   . GLU C 1 291 ? 6.526   37.084  -18.841 1.00 41.20 ? 285 GLU C OE2   1 
ATOM   6880 N  N     . GLU C 1 292 ? 1.404   40.018  -20.758 1.00 19.63 ? 286 GLU C N     1 
ATOM   6881 C  CA    . GLU C 1 292 ? 0.690   40.848  -21.763 1.00 21.65 ? 286 GLU C CA    1 
ATOM   6882 C  C     . GLU C 1 292 ? -0.407  41.688  -21.081 1.00 19.42 ? 286 GLU C C     1 
ATOM   6883 O  O     . GLU C 1 292 ? -0.530  42.891  -21.403 1.00 18.56 ? 286 GLU C O     1 
ATOM   6884 C  CB    . GLU C 1 292 ? 0.085   39.965  -22.844 1.00 22.00 ? 286 GLU C CB    1 
ATOM   6885 C  CG    . GLU C 1 292 ? 1.092   39.252  -23.723 1.00 23.18 ? 286 GLU C CG    1 
ATOM   6886 C  CD    . GLU C 1 292 ? 0.401   38.398  -24.795 1.00 28.52 ? 286 GLU C CD    1 
ATOM   6887 O  OE1   . GLU C 1 292 ? -0.750  37.905  -24.556 1.00 28.17 ? 286 GLU C OE1   1 
ATOM   6888 O  OE2   . GLU C 1 292 ? 0.990   38.235  -25.878 1.00 32.25 ? 286 GLU C OE2   1 
ATOM   6889 N  N     . ALA C 1 293 ? -1.179  41.120  -20.163 1.00 18.48 ? 287 ALA C N     1 
ATOM   6890 C  CA    . ALA C 1 293 ? -2.162  41.881  -19.362 1.00 18.56 ? 287 ALA C CA    1 
ATOM   6891 C  C     . ALA C 1 293 ? -1.416  42.933  -18.527 1.00 19.81 ? 287 ALA C C     1 
ATOM   6892 O  O     . ALA C 1 293 ? -1.865  44.097  -18.440 1.00 19.01 ? 287 ALA C O     1 
ATOM   6893 C  CB    . ALA C 1 293 ? -2.984  40.956  -18.522 1.00 20.01 ? 287 ALA C CB    1 
ATOM   6894 N  N     . PHE C 1 294 ? -0.272  42.572  -17.978 1.00 18.63 ? 288 PHE C N     1 
ATOM   6895 C  CA    . PHE C 1 294 ? 0.507   43.482  -17.110 1.00 19.38 ? 288 PHE C CA    1 
ATOM   6896 C  C     . PHE C 1 294 ? 0.905   44.711  -17.931 1.00 21.60 ? 288 PHE C C     1 
ATOM   6897 O  O     . PHE C 1 294 ? 0.635   45.856  -17.486 1.00 19.25 ? 288 PHE C O     1 
ATOM   6898 C  CB    . PHE C 1 294 ? 1.706   42.760  -16.501 1.00 20.75 ? 288 PHE C CB    1 
ATOM   6899 C  CG    . PHE C 1 294 ? 2.752   43.639  -15.894 1.00 19.42 ? 288 PHE C CG    1 
ATOM   6900 C  CD1   . PHE C 1 294 ? 2.596   44.152  -14.632 1.00 19.03 ? 288 PHE C CD1   1 
ATOM   6901 C  CD2   . PHE C 1 294 ? 3.902   43.974  -16.598 1.00 20.34 ? 288 PHE C CD2   1 
ATOM   6902 C  CE1   . PHE C 1 294 ? 3.590   44.913  -14.043 1.00 19.04 ? 288 PHE C CE1   1 
ATOM   6903 C  CE2   . PHE C 1 294 ? 4.891   44.764  -16.024 1.00 19.93 ? 288 PHE C CE2   1 
ATOM   6904 C  CZ    . PHE C 1 294 ? 4.720   45.265  -14.751 1.00 21.39 ? 288 PHE C CZ    1 
ATOM   6905 N  N     . VAL C 1 295 ? 1.467   44.513  -19.119 1.00 18.29 ? 289 VAL C N     1 
ATOM   6906 C  CA    . VAL C 1 295 ? 1.827   45.672  -19.999 1.00 19.43 ? 289 VAL C CA    1 
ATOM   6907 C  C     . VAL C 1 295 ? 0.561   46.423  -20.417 1.00 20.71 ? 289 VAL C C     1 
ATOM   6908 O  O     . VAL C 1 295 ? 0.527   47.650  -20.314 1.00 20.58 ? 289 VAL C O     1 
ATOM   6909 C  CB    . VAL C 1 295 ? 2.665   45.207  -21.207 1.00 21.55 ? 289 VAL C CB    1 
ATOM   6910 C  CG1   . VAL C 1 295 ? 2.869   46.327  -22.215 1.00 22.32 ? 289 VAL C CG1   1 
ATOM   6911 C  CG2   . VAL C 1 295 ? 4.022   44.695  -20.752 1.00 24.23 ? 289 VAL C CG2   1 
ATOM   6912 N  N     . GLU C 1 296 ? -0.486  45.723  -20.823 1.00 19.50 ? 290 GLU C N     1 
ATOM   6913 C  CA    . GLU C 1 296 ? -1.713  46.381  -21.348 1.00 20.65 ? 290 GLU C CA    1 
ATOM   6914 C  C     . GLU C 1 296 ? -2.391  47.264  -20.296 1.00 22.75 ? 290 GLU C C     1 
ATOM   6915 O  O     . GLU C 1 296 ? -2.928  48.296  -20.672 1.00 20.25 ? 290 GLU C O     1 
ATOM   6916 C  CB    . GLU C 1 296 ? -2.662  45.327  -21.897 1.00 20.81 ? 290 GLU C CB    1 
ATOM   6917 C  CG    . GLU C 1 296 ? -3.944  45.907  -22.478 1.00 21.20 ? 290 GLU C CG    1 
ATOM   6918 C  CD    . GLU C 1 296 ? -4.624  45.038  -23.535 1.00 26.00 ? 290 GLU C CD    1 
ATOM   6919 O  OE1   . GLU C 1 296 ? -3.905  44.448  -24.409 1.00 22.25 ? 290 GLU C OE1   1 
ATOM   6920 O  OE2   . GLU C 1 296 ? -5.886  44.940  -23.477 1.00 27.04 ? 290 GLU C OE2   1 
ATOM   6921 N  N     . ARG C 1 297 ? -2.407  46.883  -19.014 1.00 22.39 ? 291 ARG C N     1 
ATOM   6922 C  CA    . ARG C 1 297 ? -3.055  47.716  -17.969 1.00 21.47 ? 291 ARG C CA    1 
ATOM   6923 C  C     . ARG C 1 297 ? -2.154  48.901  -17.610 1.00 22.72 ? 291 ARG C C     1 
ATOM   6924 O  O     . ARG C 1 297 ? -2.592  49.748  -16.831 1.00 26.30 ? 291 ARG C O     1 
ATOM   6925 C  CB    . ARG C 1 297 ? -3.438  46.865  -16.749 1.00 21.20 ? 291 ARG C CB    1 
ATOM   6926 C  CG    . ARG C 1 297 ? -2.258  46.306  -15.966 1.00 20.33 ? 291 ARG C CG    1 
ATOM   6927 C  CD    . ARG C 1 297 ? -2.737  45.841  -14.596 1.00 21.33 ? 291 ARG C CD    1 
ATOM   6928 N  NE    . ARG C 1 297 ? -1.753  45.059  -13.841 1.00 19.16 ? 291 ARG C NE    1 
ATOM   6929 C  CZ    . ARG C 1 297 ? -0.776  45.564  -13.090 1.00 20.47 ? 291 ARG C CZ    1 
ATOM   6930 N  NH1   . ARG C 1 297 ? -0.622  46.880  -12.978 1.00 19.70 ? 291 ARG C NH1   1 
ATOM   6931 N  NH2   . ARG C 1 297 ? 0.033   44.747  -12.423 1.00 20.27 ? 291 ARG C NH2   1 
ATOM   6932 N  N     . GLY C 1 298 ? -0.925  48.939  -18.111 1.00 22.60 ? 292 GLY C N     1 
ATOM   6933 C  CA    . GLY C 1 298 ? -0.004  50.047  -17.818 1.00 24.19 ? 292 GLY C CA    1 
ATOM   6934 C  C     . GLY C 1 298 ? 0.937   49.722  -16.678 1.00 23.40 ? 292 GLY C C     1 
ATOM   6935 O  O     . GLY C 1 298 ? 1.390   50.655  -16.017 1.00 23.92 ? 292 GLY C O     1 
ATOM   6936 N  N     . GLY C 1 299 ? 1.338   48.457  -16.499 1.00 21.82 ? 293 GLY C N     1 
ATOM   6937 C  CA    . GLY C 1 299 ? 2.223   48.098  -15.369 1.00 20.78 ? 293 GLY C CA    1 
ATOM   6938 C  C     . GLY C 1 299 ? 3.652   48.638  -15.464 1.00 20.42 ? 293 GLY C C     1 
ATOM   6939 O  O     . GLY C 1 299 ? 4.304   48.749  -14.417 1.00 20.37 ? 293 GLY C O     1 
ATOM   6940 N  N     . ILE C 1 300 ? 4.119   49.031  -16.644 1.00 21.97 ? 294 ILE C N     1 
ATOM   6941 C  CA    . ILE C 1 300 ? 5.420   49.735  -16.791 1.00 24.13 ? 294 ILE C CA    1 
ATOM   6942 C  C     . ILE C 1 300 ? 5.132   51.205  -17.114 1.00 24.34 ? 294 ILE C C     1 
ATOM   6943 O  O     . ILE C 1 300 ? 4.406   51.500  -18.090 1.00 24.05 ? 294 ILE C O     1 
ATOM   6944 C  CB    . ILE C 1 300 ? 6.326   49.053  -17.829 1.00 29.07 ? 294 ILE C CB    1 
ATOM   6945 C  CG1   . ILE C 1 300 ? 6.705   47.632  -17.398 1.00 32.77 ? 294 ILE C CG1   1 
ATOM   6946 C  CG2   . ILE C 1 300 ? 7.576   49.892  -18.064 1.00 27.37 ? 294 ILE C CG2   1 
ATOM   6947 C  CD1   . ILE C 1 300 ? 7.039   46.719  -18.563 1.00 37.91 ? 294 ILE C CD1   1 
ATOM   6948 N  N     . TYR C 1 301 ? 5.537   52.099  -16.221 1.00 23.92 ? 295 TYR C N     1 
ATOM   6949 C  CA    . TYR C 1 301 ? 5.236   53.535  -16.345 1.00 23.41 ? 295 TYR C CA    1 
ATOM   6950 C  C     . TYR C 1 301 ? 6.362   54.347  -15.722 1.00 24.40 ? 295 TYR C C     1 
ATOM   6951 O  O     . TYR C 1 301 ? 7.306   53.790  -15.195 1.00 22.85 ? 295 TYR C O     1 
ATOM   6952 C  CB    . TYR C 1 301 ? 3.847   53.831  -15.773 1.00 24.72 ? 295 TYR C CB    1 
ATOM   6953 C  CG    . TYR C 1 301 ? 3.648   53.614  -14.295 1.00 23.71 ? 295 TYR C CG    1 
ATOM   6954 C  CD1   . TYR C 1 301 ? 3.391   52.352  -13.770 1.00 22.10 ? 295 TYR C CD1   1 
ATOM   6955 C  CD2   . TYR C 1 301 ? 3.688   54.677  -13.401 1.00 23.10 ? 295 TYR C CD2   1 
ATOM   6956 C  CE1   . TYR C 1 301 ? 3.218   52.157  -12.407 1.00 19.87 ? 295 TYR C CE1   1 
ATOM   6957 C  CE2   . TYR C 1 301 ? 3.497   54.501  -12.036 1.00 20.50 ? 295 TYR C CE2   1 
ATOM   6958 C  CZ    . TYR C 1 301 ? 3.226   53.237  -11.541 1.00 19.57 ? 295 TYR C CZ    1 
ATOM   6959 O  OH    . TYR C 1 301 ? 2.944   53.088  -10.225 1.00 24.11 ? 295 TYR C OH    1 
ATOM   6960 N  N     A ASP C 1 302 ? 6.218   55.664  -15.775 0.50 26.57 ? 296 ASP C N     1 
ATOM   6961 N  N     B ASP C 1 302 ? 6.247   55.674  -15.803 0.50 27.85 ? 296 ASP C N     1 
ATOM   6962 C  CA    A ASP C 1 302 ? 7.162   56.627  -15.150 0.50 29.26 ? 296 ASP C CA    1 
ATOM   6963 C  CA    B ASP C 1 302 ? 7.176   56.623  -15.126 0.50 31.49 ? 296 ASP C CA    1 
ATOM   6964 C  C     A ASP C 1 302 ? 6.931   56.585  -13.631 0.50 26.39 ? 296 ASP C C     1 
ATOM   6965 C  C     B ASP C 1 302 ? 6.915   56.569  -13.621 0.50 27.43 ? 296 ASP C C     1 
ATOM   6966 O  O     A ASP C 1 302 ? 6.195   57.435  -13.098 0.50 26.41 ? 296 ASP C O     1 
ATOM   6967 O  O     B ASP C 1 302 ? 6.169   57.412  -13.093 0.50 27.13 ? 296 ASP C O     1 
ATOM   6968 C  CB    A ASP C 1 302 ? 7.015   57.982  -15.851 0.50 33.17 ? 296 ASP C CB    1 
ATOM   6969 C  CB    B ASP C 1 302 ? 7.067   58.053  -15.659 0.50 37.84 ? 296 ASP C CB    1 
ATOM   6970 C  CG    A ASP C 1 302 ? 7.256   57.863  -17.354 0.50 39.14 ? 296 ASP C CG    1 
ATOM   6971 C  CG    B ASP C 1 302 ? 8.333   58.475  -16.392 0.50 47.17 ? 296 ASP C CG    1 
ATOM   6972 O  OD1   A ASP C 1 302 ? 8.180   57.105  -17.739 0.50 38.32 ? 296 ASP C OD1   1 
ATOM   6973 O  OD1   B ASP C 1 302 ? 9.122   57.567  -16.761 0.50 51.34 ? 296 ASP C OD1   1 
ATOM   6974 O  OD2   A ASP C 1 302 ? 6.510   58.511  -18.142 0.50 48.24 ? 296 ASP C OD2   1 
ATOM   6975 O  OD2   B ASP C 1 302 ? 8.530   59.704  -16.583 0.50 56.81 ? 296 ASP C OD2   1 
ATOM   6976 N  N     . TRP C 1 303 ? 7.534   55.597  -12.971 1.00 26.45 ? 297 TRP C N     1 
ATOM   6977 C  CA    . TRP C 1 303 ? 7.238   55.254  -11.563 1.00 26.00 ? 297 TRP C CA    1 
ATOM   6978 C  C     . TRP C 1 303 ? 8.197   55.928  -10.561 1.00 26.50 ? 297 TRP C C     1 
ATOM   6979 O  O     . TRP C 1 303 ? 8.152   55.573  -9.386  1.00 23.90 ? 297 TRP C O     1 
ATOM   6980 C  CB    . TRP C 1 303 ? 7.146   53.735  -11.427 1.00 23.28 ? 297 TRP C CB    1 
ATOM   6981 C  CG    . TRP C 1 303 ? 8.271   52.949  -12.015 1.00 22.04 ? 297 TRP C CG    1 
ATOM   6982 C  CD1   . TRP C 1 303 ? 9.595   53.284  -12.080 1.00 25.44 ? 297 TRP C CD1   1 
ATOM   6983 C  CD2   . TRP C 1 303 ? 8.172   51.628  -12.563 1.00 23.75 ? 297 TRP C CD2   1 
ATOM   6984 N  NE1   . TRP C 1 303 ? 10.314  52.271  -12.662 1.00 23.64 ? 297 TRP C NE1   1 
ATOM   6985 C  CE2   . TRP C 1 303 ? 9.473   51.233  -12.943 1.00 23.23 ? 297 TRP C CE2   1 
ATOM   6986 C  CE3   . TRP C 1 303 ? 7.104   50.760  -12.797 1.00 21.22 ? 297 TRP C CE3   1 
ATOM   6987 C  CZ2   . TRP C 1 303 ? 9.740   50.008  -13.537 1.00 24.04 ? 297 TRP C CZ2   1 
ATOM   6988 C  CZ3   . TRP C 1 303 ? 7.375   49.545  -13.373 1.00 23.89 ? 297 TRP C CZ3   1 
ATOM   6989 C  CH2   . TRP C 1 303 ? 8.667   49.186  -13.764 1.00 25.04 ? 297 TRP C CH2   1 
ATOM   6990 N  N     . ASN C 1 304 ? 8.946   56.962  -10.945 1.00 27.73 ? 298 ASN C N     1 
ATOM   6991 C  CA    . ASN C 1 304 ? 9.678   57.800  -9.951  1.00 33.94 ? 298 ASN C CA    1 
ATOM   6992 C  C     . ASN C 1 304 ? 9.690   59.264  -10.416 1.00 39.16 ? 298 ASN C C     1 
ATOM   6993 O  O     . ASN C 1 304 ? 9.186   59.508  -11.503 1.00 36.02 ? 298 ASN C O     1 
ATOM   6994 C  CB    . ASN C 1 304 ? 11.022  57.152  -9.649  1.00 32.18 ? 298 ASN C CB    1 
ATOM   6995 C  CG    . ASN C 1 304 ? 11.920  56.989  -10.852 1.00 35.84 ? 298 ASN C CG    1 
ATOM   6996 O  OD1   . ASN C 1 304 ? 11.979  57.864  -11.699 1.00 36.41 ? 298 ASN C OD1   1 
ATOM   6997 N  ND2   . ASN C 1 304 ? 12.677  55.908  -10.897 1.00 33.15 ? 298 ASN C ND2   1 
ATOM   6998 N  N     . LYS C 1 305 ? 10.205  60.203  -9.610  1.00 51.15 ? 299 LYS C N     1 
ATOM   6999 C  CA    . LYS C 1 305 ? 10.355  61.636  -10.003 1.00 57.16 ? 299 LYS C CA    1 
ATOM   7000 C  C     . LYS C 1 305 ? 11.423  61.754  -11.099 1.00 62.28 ? 299 LYS C C     1 
ATOM   7001 O  O     . LYS C 1 305 ? 11.240  62.580  -12.010 1.00 60.75 ? 299 LYS C O     1 
ATOM   7002 C  CB    . LYS C 1 305 ? 10.713  62.525  -8.810  1.00 65.67 ? 299 LYS C CB    1 
ATOM   7003 C  CG    . LYS C 1 305 ? 10.948  63.992  -9.169  1.00 78.56 ? 299 LYS C CG    1 
ATOM   7004 C  CD    . LYS C 1 305 ? 10.997  64.958  -7.990  1.00 77.78 ? 299 LYS C CD    1 
ATOM   7005 C  CE    . LYS C 1 305 ? 10.623  66.379  -8.374  1.00 76.62 ? 299 LYS C CE    1 
ATOM   7006 N  NZ    . LYS C 1 305 ? 11.091  67.380  -7.381  1.00 74.68 ? 299 LYS C NZ    1 
ATOM   7007 N  N     . SER C 1 306 ? 12.505  60.976  -11.007 1.00 71.99 ? 300 SER C N     1 
ATOM   7008 C  CA    . SER C 1 306 ? 13.456  60.720  -12.123 1.00 80.27 ? 300 SER C CA    1 
ATOM   7009 C  C     . SER C 1 306 ? 14.520  59.703  -11.692 1.00 80.77 ? 300 SER C C     1 
ATOM   7010 O  O     . SER C 1 306 ? 15.024  58.947  -12.524 1.00 69.23 ? 300 SER C O     1 
ATOM   7011 C  CB    . SER C 1 306 ? 14.093  61.998  -12.617 1.00 89.33 ? 300 SER C CB    1 
ATOM   7012 O  OG    . SER C 1 306 ? 14.332  61.925  -14.015 1.00 93.63 ? 300 SER C OG    1 
HETATM 7013 FE FE1   . SF4 D 2 .   ? -2.290  9.207   -13.152 1.00 20.59 ? 401 SF4 A FE1   1 
HETATM 7014 FE FE2   . SF4 D 2 .   ? -4.994  8.857   -13.408 1.00 18.97 ? 401 SF4 A FE2   1 
HETATM 7015 FE FE3   . SF4 D 2 .   ? -3.420  6.588   -12.879 1.00 20.96 ? 401 SF4 A FE3   1 
HETATM 7016 FE FE4   . SF4 D 2 .   ? -3.310  7.888   -15.271 1.00 19.61 ? 401 SF4 A FE4   1 
HETATM 7017 S  S1    . SF4 D 2 .   ? -5.178  6.868   -14.397 1.00 19.27 ? 401 SF4 A S1    1 
HETATM 7018 S  S2    . SF4 D 2 .   ? -1.451  7.325   -14.061 1.00 19.41 ? 401 SF4 A S2    1 
HETATM 7019 S  S3    . SF4 D 2 .   ? -3.692  10.079  -14.852 1.00 19.99 ? 401 SF4 A S3    1 
HETATM 7020 S  S4    . SF4 D 2 .   ? -3.698  8.443   -11.516 1.00 20.65 ? 401 SF4 A S4    1 
HETATM 7021 N  N     . SAM E 3 .   ? -2.716  4.430   -13.587 1.00 20.81 ? 402 SAM A N     1 
HETATM 7022 C  CA    . SAM E 3 .   ? -2.888  3.477   -12.467 1.00 20.80 ? 402 SAM A CA    1 
HETATM 7023 C  C     . SAM E 3 .   ? -3.994  3.976   -11.535 1.00 21.08 ? 402 SAM A C     1 
HETATM 7024 O  O     . SAM E 3 .   ? -4.445  3.128   -10.723 1.00 22.35 ? 402 SAM A O     1 
HETATM 7025 O  OXT   . SAM E 3 .   ? -4.403  5.174   -11.610 1.00 20.65 ? 402 SAM A OXT   1 
HETATM 7026 C  CB    . SAM E 3 .   ? -1.591  3.261   -11.674 1.00 22.02 ? 402 SAM A CB    1 
HETATM 7027 C  CG    . SAM E 3 .   ? -0.697  4.449   -11.432 1.00 24.39 ? 402 SAM A CG    1 
HETATM 7028 S  SD    . SAM E 3 .   ? -1.460  5.664   -10.296 1.00 27.48 ? 402 SAM A SD    1 
HETATM 7029 C  CE    . SAM E 3 .   ? -0.345  7.079   -10.439 1.00 30.71 ? 402 SAM A CE    1 
HETATM 7030 C  "C5'" . SAM E 3 .   ? -1.100  4.839   -8.672  1.00 27.10 ? 402 SAM A "C5'" 1 
HETATM 7031 C  "C4'" . SAM E 3 .   ? -2.048  5.185   -7.513  1.00 24.18 ? 402 SAM A "C4'" 1 
HETATM 7032 O  "O4'" . SAM E 3 .   ? -1.758  6.527   -7.019  1.00 22.00 ? 402 SAM A "O4'" 1 
HETATM 7033 C  "C3'" . SAM E 3 .   ? -3.541  5.164   -7.876  1.00 20.09 ? 402 SAM A "C3'" 1 
HETATM 7034 O  "O3'" . SAM E 3 .   ? -4.363  4.470   -6.937  1.00 20.12 ? 402 SAM A "O3'" 1 
HETATM 7035 C  "C2'" . SAM E 3 .   ? -3.817  6.667   -7.995  1.00 21.24 ? 402 SAM A "C2'" 1 
HETATM 7036 O  "O2'" . SAM E 3 .   ? -5.167  7.038   -7.925  1.00 24.00 ? 402 SAM A "O2'" 1 
HETATM 7037 C  "C1'" . SAM E 3 .   ? -2.972  7.234   -6.857  1.00 18.65 ? 402 SAM A "C1'" 1 
HETATM 7038 N  N9    . SAM E 3 .   ? -2.670  8.665   -6.944  1.00 17.15 ? 402 SAM A N9    1 
HETATM 7039 C  C8    . SAM E 3 .   ? -2.426  9.374   -8.101  1.00 15.85 ? 402 SAM A C8    1 
HETATM 7040 N  N7    . SAM E 3 .   ? -2.138  10.637  -7.903  1.00 14.29 ? 402 SAM A N7    1 
HETATM 7041 C  C5    . SAM E 3 .   ? -2.177  10.789  -6.527  1.00 16.06 ? 402 SAM A C5    1 
HETATM 7042 C  C6    . SAM E 3 .   ? -1.987  11.920  -5.685  1.00 16.16 ? 402 SAM A C6    1 
HETATM 7043 N  N6    . SAM E 3 .   ? -1.693  13.156  -6.123  1.00 16.49 ? 402 SAM A N6    1 
HETATM 7044 N  N1    . SAM E 3 .   ? -2.085  11.706  -4.350  1.00 15.90 ? 402 SAM A N1    1 
HETATM 7045 C  C2    . SAM E 3 .   ? -2.380  10.470  -3.910  1.00 16.69 ? 402 SAM A C2    1 
HETATM 7046 N  N3    . SAM E 3 .   ? -2.658  9.367   -4.608  1.00 16.66 ? 402 SAM A N3    1 
HETATM 7047 C  C4    . SAM E 3 .   ? -2.503  9.579   -5.923  1.00 16.77 ? 402 SAM A C4    1 
HETATM 7048 N  N1    . CTP F 4 .   ? 3.462   6.692   -4.606  1.00 17.55 ? 403 CTP A N1    1 
HETATM 7049 C  C2    . CTP F 4 .   ? 4.084   7.680   -5.377  1.00 18.60 ? 403 CTP A C2    1 
HETATM 7050 N  N3    . CTP F 4 .   ? 4.719   8.688   -4.742  1.00 17.83 ? 403 CTP A N3    1 
HETATM 7051 C  C4    . CTP F 4 .   ? 4.747   8.736   -3.397  1.00 19.59 ? 403 CTP A C4    1 
HETATM 7052 C  C5    . CTP F 4 .   ? 4.161   7.705   -2.599  1.00 19.14 ? 403 CTP A C5    1 
HETATM 7053 C  C6    . CTP F 4 .   ? 3.516   6.712   -3.248  1.00 17.62 ? 403 CTP A C6    1 
HETATM 7054 O  O2    . CTP F 4 .   ? 4.066   7.576   -6.617  1.00 17.55 ? 403 CTP A O2    1 
HETATM 7055 N  N4    . CTP F 4 .   ? 5.399   9.743   -2.830  1.00 19.82 ? 403 CTP A N4    1 
HETATM 7056 C  "C1'" . CTP F 4 .   ? 2.820   5.571   -5.322  1.00 19.41 ? 403 CTP A "C1'" 1 
HETATM 7057 C  "C2'" . CTP F 4 .   ? 3.391   4.205   -4.966  1.00 19.43 ? 403 CTP A "C2'" 1 
HETATM 7058 O  "O2'" . CTP F 4 .   ? 4.613   3.880   -5.586  1.00 19.57 ? 403 CTP A "O2'" 1 
HETATM 7059 C  "C3'" . CTP F 4 .   ? 2.247   3.307   -5.438  1.00 19.04 ? 403 CTP A "C3'" 1 
HETATM 7060 C  "C4'" . CTP F 4 .   ? 1.002   4.158   -5.171  1.00 20.00 ? 403 CTP A "C4'" 1 
HETATM 7061 O  "O4'" . CTP F 4 .   ? 1.475   5.497   -4.892  1.00 20.08 ? 403 CTP A "O4'" 1 
HETATM 7062 O  "O3'" . CTP F 4 .   ? 2.337   2.925   -6.804  1.00 20.44 ? 403 CTP A "O3'" 1 
HETATM 7063 C  "C5'" . CTP F 4 .   ? 0.187   3.662   -4.007  1.00 20.97 ? 403 CTP A "C5'" 1 
HETATM 7064 O  "O5'" . CTP F 4 .   ? -0.497  2.469   -4.434  1.00 22.53 ? 403 CTP A "O5'" 1 
HETATM 7065 P  PA    . CTP F 4 .   ? -0.711  1.304   -3.337  1.00 24.12 ? 403 CTP A PA    1 
HETATM 7066 O  O1A   . CTP F 4 .   ? -0.672  1.961   -2.002  1.00 26.34 ? 403 CTP A O1A   1 
HETATM 7067 O  O2A   . CTP F 4 .   ? -1.813  0.475   -3.773  1.00 27.44 ? 403 CTP A O2A   1 
HETATM 7068 O  O3A   . CTP F 4 .   ? 0.695   0.501   -3.426  1.00 21.43 ? 403 CTP A O3A   1 
HETATM 7069 P  PB    . CTP F 4 .   ? 1.157   -0.930  -2.862  1.00 21.10 ? 403 CTP A PB    1 
HETATM 7070 O  O1B   . CTP F 4 .   ? 2.618   -0.832  -2.649  1.00 21.78 ? 403 CTP A O1B   1 
HETATM 7071 O  O2B   . CTP F 4 .   ? 0.633   -2.013  -3.686  1.00 20.77 ? 403 CTP A O2B   1 
HETATM 7072 O  O3B   . CTP F 4 .   ? 0.349   -0.941  -1.505  1.00 21.46 ? 403 CTP A O3B   1 
HETATM 7073 P  PG    . CTP F 4 .   ? 0.221   -2.099  -0.384  1.00 19.79 ? 403 CTP A PG    1 
HETATM 7074 O  O1G   . CTP F 4 .   ? -1.105  -2.786  -0.673  1.00 20.77 ? 403 CTP A O1G   1 
HETATM 7075 O  O2G   . CTP F 4 .   ? 1.364   -3.027  -0.515  1.00 20.35 ? 403 CTP A O2G   1 
HETATM 7076 O  O3G   . CTP F 4 .   ? 0.208   -1.326  0.889   1.00 20.71 ? 403 CTP A O3G   1 
HETATM 7077 N  N1    . EPE G 5 .   ? -8.106  -9.867  -25.951 1.00 80.44 ? 404 EPE A N1    1 
HETATM 7078 C  C2    . EPE G 5 .   ? -8.472  -9.021  -27.110 1.00 73.57 ? 404 EPE A C2    1 
HETATM 7079 C  C3    . EPE G 5 .   ? -9.807  -9.418  -27.698 1.00 71.79 ? 404 EPE A C3    1 
HETATM 7080 N  N4    . EPE G 5 .   ? -9.833  -10.854 -28.047 1.00 71.90 ? 404 EPE A N4    1 
HETATM 7081 C  C5    . EPE G 5 .   ? -9.536  -11.649 -26.846 1.00 77.47 ? 404 EPE A C5    1 
HETATM 7082 C  C6    . EPE G 5 .   ? -8.176  -11.295 -26.301 1.00 82.69 ? 404 EPE A C6    1 
HETATM 7083 C  C7    . EPE G 5 .   ? -11.115 -11.268 -28.635 1.00 64.47 ? 404 EPE A C7    1 
HETATM 7084 C  C8    . EPE G 5 .   ? -11.059 -11.733 -30.082 1.00 58.05 ? 404 EPE A C8    1 
HETATM 7085 O  O8    . EPE G 5 .   ? -9.781  -12.132 -30.549 1.00 36.15 ? 404 EPE A O8    1 
HETATM 7086 C  C9    . EPE G 5 .   ? -6.784  -9.526  -25.427 1.00 77.77 ? 404 EPE A C9    1 
HETATM 7087 C  C10   . EPE G 5 .   ? -6.854  -8.310  -24.529 1.00 71.16 ? 404 EPE A C10   1 
HETATM 7088 S  S     . EPE G 5 .   ? -5.297  -8.002  -23.738 1.00 66.49 ? 404 EPE A S     1 
HETATM 7089 O  O1S   . EPE G 5 .   ? -5.383  -6.615  -23.370 1.00 52.98 ? 404 EPE A O1S   1 
HETATM 7090 O  O2S   . EPE G 5 .   ? -4.293  -8.414  -24.683 1.00 62.90 ? 404 EPE A O2S   1 
HETATM 7091 O  O3S   . EPE G 5 .   ? -5.280  -8.963  -22.513 1.00 38.57 ? 404 EPE A O3S   1 
HETATM 7092 N  N1    . EPE H 5 .   ? -3.553  29.138  -17.571 1.00 41.67 ? 405 EPE A N1    1 
HETATM 7093 C  C2    . EPE H 5 .   ? -2.508  30.035  -18.103 1.00 42.40 ? 405 EPE A C2    1 
HETATM 7094 C  C3    . EPE H 5 .   ? -1.404  29.287  -18.814 1.00 40.73 ? 405 EPE A C3    1 
HETATM 7095 N  N4    . EPE H 5 .   ? -0.767  28.331  -17.897 1.00 43.86 ? 405 EPE A N4    1 
HETATM 7096 C  C5    . EPE H 5 .   ? -1.813  27.384  -17.499 1.00 42.36 ? 405 EPE A C5    1 
HETATM 7097 C  C6    . EPE H 5 .   ? -2.912  28.098  -16.753 1.00 40.46 ? 405 EPE A C6    1 
HETATM 7098 C  C7    . EPE H 5 .   ? 0.408   27.630  -18.451 1.00 41.75 ? 405 EPE A C7    1 
HETATM 7099 C  C8    . EPE H 5 .   ? 1.508   28.500  -19.052 1.00 45.90 ? 405 EPE A C8    1 
HETATM 7100 O  O8    . EPE H 5 .   ? 2.101   29.395  -18.127 1.00 39.29 ? 405 EPE A O8    1 
HETATM 7101 C  C9    . EPE H 5 .   ? -4.528  29.878  -16.745 1.00 45.70 ? 405 EPE A C9    1 
HETATM 7102 C  C10   . EPE H 5 .   ? -5.703  30.508  -17.454 1.00 53.33 ? 405 EPE A C10   1 
HETATM 7103 S  S     . EPE H 5 .   ? -7.188  30.488  -16.466 1.00 57.98 ? 405 EPE A S     1 
HETATM 7104 O  O1S   . EPE H 5 .   ? -8.216  31.042  -17.307 1.00 66.03 ? 405 EPE A O1S   1 
HETATM 7105 O  O2S   . EPE H 5 .   ? -6.910  31.132  -15.207 1.00 44.14 ? 405 EPE A O2S   1 
HETATM 7106 O  O3S   . EPE H 5 .   ? -7.476  28.984  -16.190 1.00 57.98 ? 405 EPE A O3S   1 
HETATM 7107 MG MG    . MG  I 6 .   ? -4.154  -15.722 -7.911  1.00 30.44 ? 406 MG  A MG    1 
HETATM 7108 MG MG    . MG  J 6 .   ? -18.358 6.893   11.982  1.00 43.71 ? 407 MG  A MG    1 
HETATM 7109 FE FE1   . SF4 K 2 .   ? -40.588 14.536  -6.855  1.00 19.32 ? 401 SF4 B FE1   1 
HETATM 7110 FE FE2   . SF4 K 2 .   ? -43.305 14.994  -6.510  1.00 22.26 ? 401 SF4 B FE2   1 
HETATM 7111 FE FE3   . SF4 K 2 .   ? -41.997 16.008  -8.640  1.00 20.45 ? 401 SF4 B FE3   1 
HETATM 7112 FE FE4   . SF4 K 2 .   ? -41.420 17.115  -6.237  1.00 21.15 ? 401 SF4 B FE4   1 
HETATM 7113 S  S1    . SF4 K 2 .   ? -43.543 17.057  -7.360  1.00 20.20 ? 401 SF4 B S1    1 
HETATM 7114 S  S2    . SF4 K 2 .   ? -39.885 16.371  -7.772  1.00 20.60 ? 401 SF4 B S2    1 
HETATM 7115 S  S3    . SF4 K 2 .   ? -41.644 15.283  -4.922  1.00 20.84 ? 401 SF4 B S3    1 
HETATM 7116 S  S4    . SF4 K 2 .   ? -42.300 13.854  -8.237  1.00 20.56 ? 401 SF4 B S4    1 
HETATM 7117 N  N     . SAM L 3 .   ? -41.449 19.292  -6.826  1.00 24.51 ? 402 SAM B N     1 
HETATM 7118 C  CA    . SAM L 3 .   ? -40.880 20.159  -5.756  1.00 22.96 ? 402 SAM B CA    1 
HETATM 7119 C  C     . SAM L 3 .   ? -39.936 19.338  -4.877  1.00 24.09 ? 402 SAM B C     1 
HETATM 7120 O  O     . SAM L 3 .   ? -39.821 18.111  -4.985  1.00 20.98 ? 402 SAM B O     1 
HETATM 7121 O  OXT   . SAM L 3 .   ? -39.233 19.960  -4.036  1.00 22.23 ? 402 SAM B OXT   1 
HETATM 7122 C  CB    . SAM L 3 .   ? -41.967 20.798  -4.870  1.00 24.55 ? 402 SAM B CB    1 
HETATM 7123 C  CG    . SAM L 3 .   ? -43.191 19.979  -4.585  1.00 27.82 ? 402 SAM B CG    1 
HETATM 7124 S  SD    . SAM L 3 .   ? -42.835 18.487  -3.625  1.00 30.84 ? 402 SAM B SD    1 
HETATM 7125 C  CE    . SAM L 3 .   ? -44.361 17.546  -3.773  1.00 40.74 ? 402 SAM B CE    1 
HETATM 7126 C  "C5'" . SAM L 3 .   ? -42.962 19.269  -1.922  1.00 33.16 ? 402 SAM B "C5'" 1 
HETATM 7127 C  "C4'" . SAM L 3 .   ? -42.076 18.726  -0.779  1.00 29.45 ? 402 SAM B "C4'" 1 
HETATM 7128 O  "O4'" . SAM L 3 .   ? -42.702 17.568  -0.165  1.00 26.62 ? 402 SAM B "O4'" 1 
HETATM 7129 C  "C3'" . SAM L 3 .   ? -40.673 18.267  -1.201  1.00 27.18 ? 402 SAM B "C3'" 1 
HETATM 7130 O  "O3'" . SAM L 3 .   ? -39.603 18.574  -0.305  1.00 25.84 ? 402 SAM B "O3'" 1 
HETATM 7131 C  "C2'" . SAM L 3 .   ? -40.863 16.756  -1.337  1.00 26.43 ? 402 SAM B "C2'" 1 
HETATM 7132 O  "O2'" . SAM L 3 .   ? -39.662 16.015  -1.357  1.00 25.09 ? 402 SAM B "O2'" 1 
HETATM 7133 C  "C1'" . SAM L 3 .   ? -41.807 16.477  -0.167  1.00 24.50 ? 402 SAM B "C1'" 1 
HETATM 7134 N  N9    . SAM L 3 .   ? -42.569 15.235  -0.324  1.00 21.35 ? 402 SAM B N9    1 
HETATM 7135 C  C8    . SAM L 3 .   ? -43.046 14.690  -1.499  1.00 22.26 ? 402 SAM B C8    1 
HETATM 7136 N  N7    . SAM L 3 .   ? -43.692 13.555  -1.345  1.00 21.28 ? 402 SAM B N7    1 
HETATM 7137 C  C5    . SAM L 3 .   ? -43.658 13.347  0.029   1.00 19.80 ? 402 SAM B C5    1 
HETATM 7138 C  C6    . SAM L 3 .   ? -44.164 12.317  0.846   1.00 20.08 ? 402 SAM B C6    1 
HETATM 7139 N  N6    . SAM L 3 .   ? -44.821 11.242  0.393   1.00 17.66 ? 402 SAM B N6    1 
HETATM 7140 N  N1    . SAM L 3 .   ? -43.951 12.418  2.183   1.00 19.02 ? 402 SAM B N1    1 
HETATM 7141 C  C2    . SAM L 3 .   ? -43.287 13.485  2.640   1.00 17.82 ? 402 SAM B C2    1 
HETATM 7142 N  N3    . SAM L 3 .   ? -42.768 14.513  1.983   1.00 18.52 ? 402 SAM B N3    1 
HETATM 7143 C  C4    . SAM L 3 .   ? -42.966 14.375  0.661   1.00 19.10 ? 402 SAM B C4    1 
HETATM 7144 N  N1    . CTP M 4 .   ? -47.811 18.746  2.293   1.00 19.95 ? 403 CTP B N1    1 
HETATM 7145 C  C2    . CTP M 4 .   ? -48.759 18.033  1.549   1.00 20.46 ? 403 CTP B C2    1 
HETATM 7146 N  N3    . CTP M 4 .   ? -49.658 17.266  2.180   1.00 19.07 ? 403 CTP B N3    1 
HETATM 7147 C  C4    . CTP M 4 .   ? -49.634 17.156  3.510   1.00 20.52 ? 403 CTP B C4    1 
HETATM 7148 C  C5    . CTP M 4 .   ? -48.674 17.862  4.300   1.00 21.03 ? 403 CTP B C5    1 
HETATM 7149 C  C6    . CTP M 4 .   ? -47.819 18.667  3.655   1.00 19.34 ? 403 CTP B C6    1 
HETATM 7150 O  O2    . CTP M 4 .   ? -48.750 18.132  0.328   1.00 22.18 ? 403 CTP B O2    1 
HETATM 7151 N  N4    . CTP M 4 .   ? -50.557 16.398  4.078   1.00 18.09 ? 403 CTP B N4    1 
HETATM 7152 C  "C1'" . CTP M 4 .   ? -46.861 19.642  1.594   1.00 21.10 ? 403 CTP B "C1'" 1 
HETATM 7153 C  "C2'" . CTP M 4 .   ? -46.992 21.119  1.990   1.00 21.03 ? 403 CTP B "C2'" 1 
HETATM 7154 O  "O2'" . CTP M 4 .   ? -48.063 21.842  1.411   1.00 20.34 ? 403 CTP B "O2'" 1 
HETATM 7155 C  "C3'" . CTP M 4 .   ? -45.636 21.642  1.496   1.00 22.35 ? 403 CTP B "C3'" 1 
HETATM 7156 C  "C4'" . CTP M 4 .   ? -44.695 20.450  1.695   1.00 20.96 ? 403 CTP B "C4'" 1 
HETATM 7157 O  "O4'" . CTP M 4 .   ? -45.547 19.319  1.987   1.00 21.15 ? 403 CTP B "O4'" 1 
HETATM 7158 O  "O3'" . CTP M 4 .   ? -45.605 22.014  0.125   1.00 21.50 ? 403 CTP B "O3'" 1 
HETATM 7159 C  "C5'" . CTP M 4 .   ? -43.670 20.616  2.794   1.00 20.21 ? 403 CTP B "C5'" 1 
HETATM 7160 O  "O5'" . CTP M 4 .   ? -42.713 21.610  2.396   1.00 22.40 ? 403 CTP B "O5'" 1 
HETATM 7161 P  PA    . CTP M 4 .   ? -42.091 22.565  3.519   1.00 25.12 ? 403 CTP B PA    1 
HETATM 7162 O  O1A   . CTP M 4 .   ? -42.258 21.881  4.842   1.00 28.09 ? 403 CTP B O1A   1 
HETATM 7163 O  O2A   . CTP M 4 .   ? -40.777 23.045  3.101   1.00 28.61 ? 403 CTP B O2A   1 
HETATM 7164 O  O3A   . CTP M 4 .   ? -43.192 23.739  3.439   1.00 22.77 ? 403 CTP B O3A   1 
HETATM 7165 P  PB    . CTP M 4 .   ? -43.221 25.206  4.063   1.00 22.26 ? 403 CTP B PB    1 
HETATM 7166 O  O1B   . CTP M 4 .   ? -42.398 26.172  3.339   1.00 20.45 ? 403 CTP B O1B   1 
HETATM 7167 O  O2B   . CTP M 4 .   ? -44.618 25.580  4.377   1.00 21.80 ? 403 CTP B O2B   1 
HETATM 7168 O  O3B   . CTP M 4 .   ? -42.515 24.856  5.465   1.00 21.27 ? 403 CTP B O3B   1 
HETATM 7169 P  PG    . CTP M 4 .   ? -41.960 25.932  6.600   1.00 20.82 ? 403 CTP B PG    1 
HETATM 7170 O  O1G   . CTP M 4 .   ? -40.537 26.219  6.242   1.00 20.76 ? 403 CTP B O1G   1 
HETATM 7171 O  O2G   . CTP M 4 .   ? -42.807 27.147  6.498   1.00 20.47 ? 403 CTP B O2G   1 
HETATM 7172 O  O3G   . CTP M 4 .   ? -42.090 25.180  7.861   1.00 20.76 ? 403 CTP B O3G   1 
HETATM 7173 FE FE1   . SF4 N 2 .   ? -8.650  46.490  4.710   1.00 20.81 ? 401 SF4 C FE1   1 
HETATM 7174 FE FE2   . SF4 N 2 .   ? -9.192  44.956  2.525   1.00 22.94 ? 401 SF4 C FE2   1 
HETATM 7175 FE FE3   . SF4 N 2 .   ? -7.735  47.407  2.306   1.00 22.69 ? 401 SF4 C FE3   1 
HETATM 7176 FE FE4   . SF4 N 2 .   ? -10.483 47.327  2.950   1.00 21.50 ? 401 SF4 C FE4   1 
HETATM 7177 S  S1    . SF4 N 2 .   ? -9.497  46.592  1.028   1.00 22.73 ? 401 SF4 C S1    1 
HETATM 7178 S  S2    . SF4 N 2 .   ? -8.857  48.558  3.958   1.00 20.80 ? 401 SF4 C S2    1 
HETATM 7179 S  S3    . SF4 N 2 .   ? -10.692 45.509  4.245   1.00 22.78 ? 401 SF4 C S3    1 
HETATM 7180 S  S4    . SF4 N 2 .   ? -7.147  45.346  3.390   1.00 20.24 ? 401 SF4 C S4    1 
HETATM 7181 N  N     . SAM O 3 .   ? -5.591  48.192  2.977   1.00 22.43 ? 402 SAM C N     1 
HETATM 7182 C  CA    . SAM O 3 .   ? -4.982  48.913  1.853   1.00 22.76 ? 402 SAM C CA    1 
HETATM 7183 C  C     . SAM O 3 .   ? -6.087  49.494  0.967   1.00 24.53 ? 402 SAM C C     1 
HETATM 7184 O  O     . SAM O 3 .   ? -7.276  49.096  1.097   1.00 22.47 ? 402 SAM C O     1 
HETATM 7185 O  OXT   . SAM O 3 .   ? -5.721  50.316  0.138   1.00 23.25 ? 402 SAM C OXT   1 
HETATM 7186 C  CB    . SAM O 3 .   ? -4.075  48.013  1.008   1.00 24.96 ? 402 SAM C CB    1 
HETATM 7187 C  CG    . SAM O 3 .   ? -4.547  46.606  0.699   1.00 27.74 ? 402 SAM C CG    1 
HETATM 7188 S  SD    . SAM O 3 .   ? -6.041  46.518  -0.334  1.00 31.28 ? 402 SAM C SD    1 
HETATM 7189 C  CE    . SAM O 3 .   ? -6.406  44.749  -0.265  1.00 33.48 ? 402 SAM C CE    1 
HETATM 7190 C  "C5'" . SAM O 3 .   ? -5.193  46.730  -1.993  1.00 31.73 ? 402 SAM C "C5'" 1 
HETATM 7191 C  "C4'" . SAM O 3 .   ? -6.000  47.389  -3.139  1.00 27.80 ? 402 SAM C "C4'" 1 
HETATM 7192 O  "O4'" . SAM O 3 .   ? -6.918  46.413  -3.711  1.00 23.21 ? 402 SAM C "O4'" 1 
HETATM 7193 C  "C3'" . SAM O 3 .   ? -6.869  48.576  -2.705  1.00 23.19 ? 402 SAM C "C3'" 1 
HETATM 7194 O  "O3'" . SAM O 3 .   ? -6.876  49.690  -3.594  1.00 22.97 ? 402 SAM C "O3'" 1 
HETATM 7195 C  "C2'" . SAM O 3 .   ? -8.251  47.920  -2.565  1.00 23.65 ? 402 SAM C "C2'" 1 
HETATM 7196 O  "O2'" . SAM O 3 .   ? -9.294  48.872  -2.580  1.00 24.91 ? 402 SAM C "O2'" 1 
HETATM 7197 C  "C1'" . SAM O 3 .   ? -8.229  46.940  -3.742  1.00 22.70 ? 402 SAM C "C1'" 1 
HETATM 7198 N  N9    . SAM O 3 .   ? -9.193  45.853  -3.647  1.00 20.08 ? 402 SAM C N9    1 
HETATM 7199 C  C8    . SAM O 3 .   ? -9.598  45.227  -2.487  1.00 18.35 ? 402 SAM C C8    1 
HETATM 7200 N  N7    . SAM O 3 .   ? -10.471 44.283  -2.683  1.00 18.53 ? 402 SAM C N7    1 
HETATM 7201 C  C5    . SAM O 3 .   ? -10.714 44.296  -4.049  1.00 17.58 ? 402 SAM C C5    1 
HETATM 7202 C  C6    . SAM O 3 .   ? -11.560 43.527  -4.884  1.00 16.86 ? 402 SAM C C6    1 
HETATM 7203 N  N6    . SAM O 3 .   ? -12.378 42.579  -4.436  1.00 16.65 ? 402 SAM C N6    1 
HETATM 7204 N  N1    . SAM O 3 .   ? -11.529 43.794  -6.217  1.00 16.27 ? 402 SAM C N1    1 
HETATM 7205 C  C2    . SAM O 3 .   ? -10.692 44.746  -6.670  1.00 19.33 ? 402 SAM C C2    1 
HETATM 7206 N  N3    . SAM O 3 .   ? -9.882  45.549  -5.971  1.00 17.90 ? 402 SAM C N3    1 
HETATM 7207 C  C4    . SAM O 3 .   ? -9.926  45.261  -4.661  1.00 19.04 ? 402 SAM C C4    1 
HETATM 7208 N  N1    . CTP P 4 .   ? -4.162  42.083  -6.285  1.00 20.27 ? 403 CTP C N1    1 
HETATM 7209 C  C2    . CTP P 4 .   ? -4.627  40.976  -5.560  1.00 18.66 ? 403 CTP C C2    1 
HETATM 7210 N  N3    . CTP P 4 .   ? -5.141  39.910  -6.224  1.00 19.98 ? 403 CTP C N3    1 
HETATM 7211 C  C4    . CTP P 4 .   ? -5.232  39.928  -7.563  1.00 20.16 ? 403 CTP C C4    1 
HETATM 7212 C  C5    . CTP P 4 .   ? -4.817  41.067  -8.322  1.00 20.61 ? 403 CTP C C5    1 
HETATM 7213 C  C6    . CTP P 4 .   ? -4.301  42.116  -7.650  1.00 20.75 ? 403 CTP C C6    1 
HETATM 7214 O  O2    . CTP P 4 .   ? -4.550  40.980  -4.335  1.00 20.82 ? 403 CTP C O2    1 
HETATM 7215 N  N4    . CTP P 4 .   ? -5.710  38.844  -8.166  1.00 20.50 ? 403 CTP C N4    1 
HETATM 7216 C  "C1'" . CTP P 4 .   ? -3.588  43.250  -5.577  1.00 19.86 ? 403 CTP C "C1'" 1 
HETATM 7217 C  "C2'" . CTP P 4 .   ? -2.170  43.613  -6.054  1.00 20.65 ? 403 CTP C "C2'" 1 
HETATM 7218 O  "O2'" . CTP P 4 .   ? -1.149  42.771  -5.557  1.00 20.87 ? 403 CTP C "O2'" 1 
HETATM 7219 C  "C3'" . CTP P 4 .   ? -2.094  45.034  -5.506  1.00 20.24 ? 403 CTP C "C3'" 1 
HETATM 7220 C  "C4'" . CTP P 4 .   ? -3.526  45.539  -5.691  1.00 21.69 ? 403 CTP C "C4'" 1 
HETATM 7221 O  "O4'" . CTP P 4 .   ? -4.349  44.368  -5.940  1.00 22.83 ? 403 CTP C "O4'" 1 
HETATM 7222 O  "O3'" . CTP P 4 .   ? -1.783  45.083  -4.122  1.00 20.72 ? 403 CTP C "O3'" 1 
HETATM 7223 C  "C5'" . CTP P 4 .   ? -3.702  46.571  -6.776  1.00 21.57 ? 403 CTP C "C5'" 1 
HETATM 7224 O  "O5'" . CTP P 4 .   ? -3.028  47.752  -6.326  1.00 24.12 ? 403 CTP C "O5'" 1 
HETATM 7225 P  PA    . CTP P 4 .   ? -2.309  48.658  -7.417  1.00 24.72 ? 403 CTP C PA    1 
HETATM 7226 O  O1A   . CTP P 4 .   ? -2.873  48.360  -8.769  1.00 25.00 ? 403 CTP C O1A   1 
HETATM 7227 O  O2A   . CTP P 4 .   ? -2.203  50.039  -6.965  1.00 26.85 ? 403 CTP C O2A   1 
HETATM 7228 O  O3A   . CTP P 4 .   ? -0.837  47.977  -7.340  1.00 21.97 ? 403 CTP C O3A   1 
HETATM 7229 P  PB    . CTP P 4 .   ? 0.570   48.390  -7.999  1.00 21.73 ? 403 CTP C PB    1 
HETATM 7230 O  O1B   . CTP P 4 .   ? 1.348   47.168  -8.340  1.00 19.85 ? 403 CTP C O1B   1 
HETATM 7231 O  O2B   . CTP P 4 .   ? 1.253   49.383  -7.115  1.00 19.97 ? 403 CTP C O2B   1 
HETATM 7232 O  O3B   . CTP P 4 .   ? 0.065   49.091  -9.328  1.00 19.71 ? 403 CTP C O3B   1 
HETATM 7233 P  PG    . CTP P 4 .   ? 0.962   49.890  -10.462 1.00 19.86 ? 403 CTP C PG    1 
HETATM 7234 O  O1G   . CTP P 4 .   ? 0.328   49.485  -11.755 1.00 19.18 ? 403 CTP C O1G   1 
HETATM 7235 O  O2G   . CTP P 4 .   ? 2.392   49.497  -10.345 1.00 18.76 ? 403 CTP C O2G   1 
HETATM 7236 O  O3G   . CTP P 4 .   ? 0.719   51.337  -10.175 1.00 21.01 ? 403 CTP C O3G   1 
HETATM 7237 C  C1    . GOL Q 7 .   ? 1.902   27.005  -6.632  1.00 32.01 ? 404 GOL C C1    1 
HETATM 7238 O  O1    . GOL Q 7 .   ? 3.088   26.315  -7.014  1.00 36.07 ? 404 GOL C O1    1 
HETATM 7239 C  C2    . GOL Q 7 .   ? 0.847   26.820  -7.695  1.00 33.70 ? 404 GOL C C2    1 
HETATM 7240 O  O2    . GOL Q 7 .   ? 1.069   27.726  -8.775  1.00 33.01 ? 404 GOL C O2    1 
HETATM 7241 C  C3    . GOL Q 7 .   ? -0.556  26.997  -7.178  1.00 32.22 ? 404 GOL C C3    1 
HETATM 7242 O  O3    . GOL Q 7 .   ? -1.470  26.859  -8.256  1.00 29.19 ? 404 GOL C O3    1 
HETATM 7243 MG MG    . MG  R 6 .   ? 10.039  60.995  -2.741  1.00 26.57 ? 405 MG  C MG    1 
HETATM 7244 O  O     . HOH S 8 .   ? -3.258  14.998  6.837   1.00 38.36 ? 501 HOH A O     1 
HETATM 7245 O  O     . HOH S 8 .   ? -9.784  -1.842  -24.501 1.00 53.19 ? 502 HOH A O     1 
HETATM 7246 O  O     . HOH S 8 .   ? 8.194   10.218  6.710   1.00 27.94 ? 503 HOH A O     1 
HETATM 7247 O  O     . HOH S 8 .   ? -16.932 7.528   13.254  1.00 46.47 ? 504 HOH A O     1 
HETATM 7248 O  O     . HOH S 8 .   ? 20.997  6.310   -3.349  1.00 42.97 ? 505 HOH A O     1 
HETATM 7249 O  O     . HOH S 8 .   ? -18.972 12.439  -5.159  1.00 26.62 ? 506 HOH A O     1 
HETATM 7250 O  O     . HOH S 8 .   ? 9.367   13.131  -11.374 1.00 41.85 ? 507 HOH A O     1 
HETATM 7251 O  O     . HOH S 8 .   ? -13.109 13.293  -17.301 1.00 39.52 ? 508 HOH A O     1 
HETATM 7252 O  O     . HOH S 8 .   ? -9.138  7.184   -22.336 1.00 48.25 ? 509 HOH A O     1 
HETATM 7253 O  O     . HOH S 8 .   ? -25.900 2.319   -3.704  1.00 39.06 ? 510 HOH A O     1 
HETATM 7254 O  O     . HOH S 8 .   ? -1.138  7.440   13.024  1.00 52.11 ? 511 HOH A O     1 
HETATM 7255 O  O     . HOH S 8 .   ? 13.090  -9.905  2.915   1.00 31.08 ? 512 HOH A O     1 
HETATM 7256 O  O     . HOH S 8 .   ? -6.442  -18.048 -11.308 1.00 48.19 ? 513 HOH A O     1 
HETATM 7257 O  O     . HOH S 8 .   ? -7.975  15.925  12.266  1.00 37.92 ? 514 HOH A O     1 
HETATM 7258 O  O     . HOH S 8 .   ? 1.586   2.820   -19.181 1.00 39.37 ? 515 HOH A O     1 
HETATM 7259 O  O     . HOH S 8 .   ? 3.137   -10.758 4.945   1.00 50.72 ? 516 HOH A O     1 
HETATM 7260 O  O     . HOH S 8 .   ? 11.280  15.528  4.140   1.00 42.28 ? 517 HOH A O     1 
HETATM 7261 O  O     . HOH S 8 .   ? 11.556  9.905   -15.566 1.00 28.23 ? 518 HOH A O     1 
HETATM 7262 O  O     . HOH S 8 .   ? -1.558  2.310   -26.763 1.00 38.31 ? 519 HOH A O     1 
HETATM 7263 O  O     . HOH S 8 .   ? 9.055   16.761  -13.951 1.00 40.03 ? 520 HOH A O     1 
HETATM 7264 O  O     . HOH S 8 .   ? 16.066  5.678   4.648   1.00 24.36 ? 521 HOH A O     1 
HETATM 7265 O  O     . HOH S 8 .   ? 17.370  -11.033 -17.981 1.00 39.54 ? 522 HOH A O     1 
HETATM 7266 O  O     . HOH S 8 .   ? -7.923  22.750  -2.202  1.00 36.68 ? 523 HOH A O     1 
HETATM 7267 O  O     . HOH S 8 .   ? 11.636  11.830  -11.205 1.00 30.10 ? 524 HOH A O     1 
HETATM 7268 O  O     . HOH S 8 .   ? -20.820 3.141   -14.318 1.00 36.10 ? 525 HOH A O     1 
HETATM 7269 O  O     . HOH S 8 .   ? 12.209  2.402   14.636  1.00 37.26 ? 526 HOH A O     1 
HETATM 7270 O  O     . HOH S 8 .   ? 18.429  12.672  -8.538  1.00 47.29 ? 527 HOH A O     1 
HETATM 7271 O  O     . HOH S 8 .   ? 1.317   8.716   -16.049 1.00 20.16 ? 528 HOH A O     1 
HETATM 7272 O  O     . HOH S 8 .   ? -7.595  6.082   -6.763  1.00 22.52 ? 529 HOH A O     1 
HETATM 7273 O  O     . HOH S 8 .   ? -11.562 3.313   -12.318 1.00 32.23 ? 530 HOH A O     1 
HETATM 7274 O  O     . HOH S 8 .   ? 7.664   -14.415 -18.335 1.00 33.45 ? 531 HOH A O     1 
HETATM 7275 O  O     . HOH S 8 .   ? 10.114  7.557   11.042  1.00 41.45 ? 532 HOH A O     1 
HETATM 7276 O  O     . HOH S 8 .   ? -5.265  23.000  -9.100  1.00 33.80 ? 533 HOH A O     1 
HETATM 7277 O  O     . HOH S 8 .   ? -2.232  11.139  -18.064 1.00 24.78 ? 534 HOH A O     1 
HETATM 7278 O  O     . HOH S 8 .   ? 3.487   31.602  -18.221 1.00 43.68 ? 535 HOH A O     1 
HETATM 7279 O  O     . HOH S 8 .   ? 10.387  12.446  -15.790 1.00 37.96 ? 536 HOH A O     1 
HETATM 7280 O  O     . HOH S 8 .   ? -23.943 5.363   5.407   1.00 29.05 ? 537 HOH A O     1 
HETATM 7281 O  O     . HOH S 8 .   ? -19.101 3.629   8.350   1.00 32.05 ? 538 HOH A O     1 
HETATM 7282 O  O     . HOH S 8 .   ? -4.830  -4.293  -21.843 1.00 37.29 ? 539 HOH A O     1 
HETATM 7283 O  O     . HOH S 8 .   ? -5.341  -10.360 3.352   1.00 40.50 ? 540 HOH A O     1 
HETATM 7284 O  O     . HOH S 8 .   ? -1.399  28.214  -13.251 1.00 25.74 ? 541 HOH A O     1 
HETATM 7285 O  O     . HOH S 8 .   ? -12.204 8.032   -10.183 1.00 40.10 ? 542 HOH A O     1 
HETATM 7286 O  O     . HOH S 8 .   ? 3.578   -3.032  0.896   1.00 19.45 ? 543 HOH A O     1 
HETATM 7287 O  O     . HOH S 8 .   ? -1.352  11.207  1.264   1.00 19.15 ? 544 HOH A O     1 
HETATM 7288 O  O     . HOH S 8 .   ? -16.787 -3.498  2.670   1.00 38.79 ? 545 HOH A O     1 
HETATM 7289 O  O     . HOH S 8 .   ? 18.410  4.046   2.211   1.00 18.09 ? 546 HOH A O     1 
HETATM 7290 O  O     . HOH S 8 .   ? 8.846   8.048   15.124  1.00 33.44 ? 547 HOH A O     1 
HETATM 7291 O  O     . HOH S 8 .   ? 12.430  -20.675 -9.747  1.00 47.10 ? 548 HOH A O     1 
HETATM 7292 O  O     . HOH S 8 .   ? 8.086   5.585   -13.912 1.00 22.83 ? 549 HOH A O     1 
HETATM 7293 O  O     . HOH S 8 .   ? -20.698 -4.159  -13.847 1.00 38.87 ? 550 HOH A O     1 
HETATM 7294 O  O     . HOH S 8 .   ? 24.959  -1.886  -5.195  1.00 33.23 ? 551 HOH A O     1 
HETATM 7295 O  O     . HOH S 8 .   ? 0.188   17.995  8.620   1.00 51.86 ? 552 HOH A O     1 
HETATM 7296 O  O     . HOH S 8 .   ? -12.953 19.240  -13.756 1.00 36.88 ? 553 HOH A O     1 
HETATM 7297 O  O     . HOH S 8 .   ? -3.658  20.173  3.132   1.00 45.10 ? 554 HOH A O     1 
HETATM 7298 O  O     . HOH S 8 .   ? 10.678  0.215   -17.374 1.00 21.84 ? 555 HOH A O     1 
HETATM 7299 O  O     . HOH S 8 .   ? -1.671  -3.162  -5.261  1.00 34.73 ? 556 HOH A O     1 
HETATM 7300 O  O     . HOH S 8 .   ? 11.632  9.293   -12.989 1.00 26.23 ? 557 HOH A O     1 
HETATM 7301 O  O     . HOH S 8 .   ? -17.332 -3.150  10.731  1.00 55.92 ? 558 HOH A O     1 
HETATM 7302 O  O     . HOH S 8 .   ? 8.787   15.504  -20.520 1.00 40.36 ? 559 HOH A O     1 
HETATM 7303 O  O     . HOH S 8 .   ? -12.221 4.897   9.429   1.00 32.31 ? 560 HOH A O     1 
HETATM 7304 O  O     . HOH S 8 .   ? -11.953 8.722   -20.187 1.00 42.83 ? 561 HOH A O     1 
HETATM 7305 O  O     . HOH S 8 .   ? 7.651   24.634  -12.146 1.00 35.12 ? 562 HOH A O     1 
HETATM 7306 O  O     . HOH S 8 .   ? 11.581  5.212   10.073  1.00 42.96 ? 563 HOH A O     1 
HETATM 7307 O  O     . HOH S 8 .   ? -10.516 21.895  7.748   1.00 41.34 ? 564 HOH A O     1 
HETATM 7308 O  O     . HOH S 8 .   ? -2.989  3.178   7.479   1.00 26.07 ? 565 HOH A O     1 
HETATM 7309 O  O     . HOH S 8 .   ? -0.890  -4.656  8.089   1.00 30.85 ? 566 HOH A O     1 
HETATM 7310 O  O     . HOH S 8 .   ? -14.632 -5.181  2.686   1.00 31.68 ? 567 HOH A O     1 
HETATM 7311 O  O     . HOH S 8 .   ? -21.028 7.332   8.525   1.00 27.81 ? 568 HOH A O     1 
HETATM 7312 O  O     . HOH S 8 .   ? -9.346  1.665   9.288   1.00 36.07 ? 569 HOH A O     1 
HETATM 7313 O  O     . HOH S 8 .   ? 6.055   2.746   -24.801 1.00 45.77 ? 570 HOH A O     1 
HETATM 7314 O  O     . HOH S 8 .   ? 4.613   16.792  -14.736 1.00 26.33 ? 571 HOH A O     1 
HETATM 7315 O  O     . HOH S 8 .   ? 6.198   11.972  7.401   1.00 38.70 ? 572 HOH A O     1 
HETATM 7316 O  O     . HOH S 8 .   ? 13.408  14.457  -2.896  1.00 39.24 ? 573 HOH A O     1 
HETATM 7317 O  O     . HOH S 8 .   ? 18.234  -14.811 -8.022  1.00 46.31 ? 574 HOH A O     1 
HETATM 7318 O  O     . HOH S 8 .   ? -2.658  20.087  -17.288 1.00 47.76 ? 575 HOH A O     1 
HETATM 7319 O  O     . HOH S 8 .   ? -18.309 2.650   13.052  1.00 42.16 ? 576 HOH A O     1 
HETATM 7320 O  O     . HOH S 8 .   ? -1.673  1.240   11.858  1.00 41.08 ? 577 HOH A O     1 
HETATM 7321 O  O     . HOH S 8 .   ? -0.604  0.733   3.452   1.00 21.23 ? 578 HOH A O     1 
HETATM 7322 O  O     . HOH S 8 .   ? 4.181   -0.593  -0.419  1.00 19.74 ? 579 HOH A O     1 
HETATM 7323 O  O     . HOH S 8 .   ? -14.462 15.507  4.785   1.00 21.27 ? 580 HOH A O     1 
HETATM 7324 O  O     . HOH S 8 .   ? -1.695  22.637  -1.891  1.00 44.17 ? 581 HOH A O     1 
HETATM 7325 O  O     . HOH S 8 .   ? 21.937  -4.789  -16.693 1.00 41.38 ? 582 HOH A O     1 
HETATM 7326 O  O     . HOH S 8 .   ? 7.747   5.911   -19.465 1.00 23.86 ? 583 HOH A O     1 
HETATM 7327 O  O     . HOH S 8 .   ? 5.469   23.653  -19.266 1.00 47.05 ? 584 HOH A O     1 
HETATM 7328 O  O     . HOH S 8 .   ? 12.159  4.911   -3.497  1.00 21.02 ? 585 HOH A O     1 
HETATM 7329 O  O     . HOH S 8 .   ? -24.268 -1.713  -5.255  1.00 38.44 ? 586 HOH A O     1 
HETATM 7330 O  O     . HOH S 8 .   ? -16.829 18.185  -2.511  1.00 44.89 ? 587 HOH A O     1 
HETATM 7331 O  O     . HOH S 8 .   ? -4.266  19.371  -13.149 1.00 18.63 ? 588 HOH A O     1 
HETATM 7332 O  O     . HOH S 8 .   ? 12.139  5.075   -0.641  1.00 23.22 ? 589 HOH A O     1 
HETATM 7333 O  O     . HOH S 8 .   ? -10.173 22.647  -9.651  1.00 52.13 ? 590 HOH A O     1 
HETATM 7334 O  O     . HOH S 8 .   ? 9.598   -3.271  -23.118 1.00 35.41 ? 591 HOH A O     1 
HETATM 7335 O  O     . HOH S 8 .   ? 7.563   7.245   -0.821  1.00 21.04 ? 592 HOH A O     1 
HETATM 7336 O  O     . HOH S 8 .   ? 21.427  0.183   0.572   1.00 30.52 ? 593 HOH A O     1 
HETATM 7337 O  O     . HOH S 8 .   ? -15.565 17.548  6.071   1.00 25.74 ? 594 HOH A O     1 
HETATM 7338 O  O     . HOH S 8 .   ? 11.291  8.767   -0.256  1.00 28.19 ? 595 HOH A O     1 
HETATM 7339 O  O     . HOH S 8 .   ? -9.894  10.692  -18.986 1.00 41.90 ? 596 HOH A O     1 
HETATM 7340 O  O     . HOH S 8 .   ? -9.181  22.422  2.012   1.00 42.18 ? 597 HOH A O     1 
HETATM 7341 O  O     . HOH S 8 .   ? -14.282 -3.937  5.276   1.00 44.43 ? 598 HOH A O     1 
HETATM 7342 O  O     . HOH S 8 .   ? -6.773  -4.025  -23.152 1.00 40.16 ? 599 HOH A O     1 
HETATM 7343 O  O     . HOH S 8 .   ? 6.793   0.166   -1.632  1.00 20.05 ? 600 HOH A O     1 
HETATM 7344 O  O     . HOH S 8 .   ? -6.698  -0.027  -17.460 1.00 32.60 ? 601 HOH A O     1 
HETATM 7345 O  O     . HOH S 8 .   ? 16.064  -1.323  -22.026 1.00 41.07 ? 602 HOH A O     1 
HETATM 7346 O  O     . HOH S 8 .   ? 13.420  -12.331 -1.537  1.00 34.65 ? 603 HOH A O     1 
HETATM 7347 O  O     . HOH S 8 .   ? -19.259 15.971  -14.374 1.00 31.29 ? 604 HOH A O     1 
HETATM 7348 O  O     . HOH S 8 .   ? 4.118   -3.254  -3.120  1.00 21.74 ? 605 HOH A O     1 
HETATM 7349 O  O     . HOH S 8 .   ? -13.937 -9.954  -5.473  1.00 35.61 ? 606 HOH A O     1 
HETATM 7350 O  O     . HOH S 8 .   ? 0.851   -1.505  11.391  1.00 30.21 ? 607 HOH A O     1 
HETATM 7351 O  O     . HOH S 8 .   ? 25.690  -3.163  -13.773 1.00 32.48 ? 608 HOH A O     1 
HETATM 7352 O  O     . HOH S 8 .   ? -21.677 13.724  3.803   1.00 26.07 ? 609 HOH A O     1 
HETATM 7353 O  O     . HOH S 8 .   ? 20.483  -2.046  0.857   1.00 32.20 ? 610 HOH A O     1 
HETATM 7354 O  O     . HOH S 8 .   ? -12.294 1.565   -15.100 1.00 33.73 ? 611 HOH A O     1 
HETATM 7355 O  O     . HOH S 8 .   ? 0.706   17.730  4.053   1.00 47.52 ? 612 HOH A O     1 
HETATM 7356 O  O     . HOH S 8 .   ? 7.794   21.874  -10.543 1.00 32.27 ? 613 HOH A O     1 
HETATM 7357 O  O     . HOH S 8 .   ? -21.043 6.934   -2.875  1.00 25.82 ? 614 HOH A O     1 
HETATM 7358 O  O     . HOH S 8 .   ? 20.917  -7.399  -5.330  1.00 34.11 ? 615 HOH A O     1 
HETATM 7359 O  O     . HOH S 8 .   ? -25.117 -1.345  2.591   1.00 47.21 ? 616 HOH A O     1 
HETATM 7360 O  O     . HOH S 8 .   ? 21.643  5.312   -14.149 1.00 35.69 ? 617 HOH A O     1 
HETATM 7361 O  O     . HOH S 8 .   ? -15.241 5.875   -18.281 1.00 42.13 ? 618 HOH A O     1 
HETATM 7362 O  O     . HOH S 8 .   ? 0.526   13.111  -17.192 1.00 23.30 ? 619 HOH A O     1 
HETATM 7363 O  O     . HOH S 8 .   ? -0.040  22.516  -14.651 1.00 33.79 ? 620 HOH A O     1 
HETATM 7364 O  O     . HOH S 8 .   ? 10.718  12.749  -22.312 1.00 44.34 ? 621 HOH A O     1 
HETATM 7365 O  O     . HOH S 8 .   ? 12.640  -4.105  5.407   1.00 37.50 ? 622 HOH A O     1 
HETATM 7366 O  O     . HOH S 8 .   ? -4.468  17.189  0.233   1.00 19.61 ? 623 HOH A O     1 
HETATM 7367 O  O     . HOH S 8 .   ? -1.650  -15.815 -7.173  1.00 48.12 ? 624 HOH A O     1 
HETATM 7368 O  O     . HOH S 8 .   ? -4.464  -14.364 -4.716  1.00 38.22 ? 625 HOH A O     1 
HETATM 7369 O  O     . HOH S 8 .   ? 20.598  -5.057  3.341   1.00 46.51 ? 626 HOH A O     1 
HETATM 7370 O  O     . HOH S 8 .   ? 23.680  -4.148  -4.638  1.00 46.54 ? 627 HOH A O     1 
HETATM 7371 O  O     . HOH S 8 .   ? 24.247  -4.156  4.848   1.00 57.43 ? 628 HOH A O     1 
HETATM 7372 O  O     . HOH S 8 .   ? -13.113 0.900   -12.870 1.00 32.09 ? 629 HOH A O     1 
HETATM 7373 O  O     . HOH S 8 .   ? 2.574   1.318   -16.200 1.00 36.41 ? 630 HOH A O     1 
HETATM 7374 O  O     . HOH S 8 .   ? -11.431 -10.854 -22.537 1.00 31.62 ? 631 HOH A O     1 
HETATM 7375 O  O     . HOH S 8 .   ? 10.046  7.211   -2.167  1.00 27.04 ? 632 HOH A O     1 
HETATM 7376 O  O     . HOH S 8 .   ? 18.068  1.825   -17.068 1.00 42.35 ? 633 HOH A O     1 
HETATM 7377 O  O     . HOH S 8 .   ? 13.339  4.028   8.466   1.00 28.65 ? 634 HOH A O     1 
HETATM 7378 O  O     . HOH S 8 .   ? 1.981   -7.058  9.761   1.00 39.19 ? 635 HOH A O     1 
HETATM 7379 O  O     . HOH S 8 .   ? 16.884  12.030  -15.192 1.00 55.40 ? 636 HOH A O     1 
HETATM 7380 O  O     . HOH S 8 .   ? 6.080   9.323   4.984   1.00 28.33 ? 637 HOH A O     1 
HETATM 7381 O  O     . HOH S 8 .   ? 17.950  -13.140 -13.871 1.00 34.28 ? 638 HOH A O     1 
HETATM 7382 O  O     . HOH S 8 .   ? -13.838 -1.440  -20.051 1.00 45.07 ? 639 HOH A O     1 
HETATM 7383 O  O     . HOH S 8 .   ? 0.636   17.486  -0.359  1.00 23.64 ? 640 HOH A O     1 
HETATM 7384 O  O     . HOH S 8 .   ? -12.280 2.245   9.317   1.00 31.77 ? 641 HOH A O     1 
HETATM 7385 O  O     . HOH S 8 .   ? 22.123  -5.556  -6.725  1.00 33.78 ? 642 HOH A O     1 
HETATM 7386 O  O     . HOH S 8 .   ? -19.205 -2.410  6.702   1.00 52.08 ? 643 HOH A O     1 
HETATM 7387 O  O     . HOH S 8 .   ? -8.936  16.159  -16.844 1.00 37.45 ? 644 HOH A O     1 
HETATM 7388 O  O     . HOH S 8 .   ? -15.567 21.258  0.612   1.00 41.94 ? 645 HOH A O     1 
HETATM 7389 O  O     . HOH S 8 .   ? -6.068  24.377  -1.827  1.00 52.70 ? 646 HOH A O     1 
HETATM 7390 O  O     . HOH S 8 .   ? 18.333  12.344  -3.638  1.00 43.47 ? 647 HOH A O     1 
HETATM 7391 O  O     . HOH S 8 .   ? -3.249  -8.697  6.908   1.00 36.57 ? 648 HOH A O     1 
HETATM 7392 O  O     . HOH S 8 .   ? 14.505  -8.097  -23.917 1.00 33.81 ? 649 HOH A O     1 
HETATM 7393 O  O     . HOH S 8 .   ? -2.622  -3.357  6.582   1.00 25.69 ? 650 HOH A O     1 
HETATM 7394 O  O     . HOH S 8 .   ? -0.564  14.368  6.966   1.00 24.95 ? 651 HOH A O     1 
HETATM 7395 O  O     . HOH S 8 .   ? 2.733   -3.133  8.415   1.00 23.65 ? 652 HOH A O     1 
HETATM 7396 O  O     . HOH S 8 .   ? -6.223  -6.802  -20.252 1.00 29.74 ? 653 HOH A O     1 
HETATM 7397 O  O     . HOH S 8 .   ? -21.852 0.404   6.525   1.00 39.89 ? 654 HOH A O     1 
HETATM 7398 O  O     . HOH S 8 .   ? -13.435 17.020  12.491  1.00 43.05 ? 655 HOH A O     1 
HETATM 7399 O  O     . HOH S 8 .   ? 17.761  11.054  1.237   1.00 48.13 ? 656 HOH A O     1 
HETATM 7400 O  O     . HOH S 8 .   ? -1.113  24.520  -15.700 1.00 36.42 ? 657 HOH A O     1 
HETATM 7401 O  O     . HOH S 8 .   ? -15.375 -10.553 -20.684 1.00 41.05 ? 658 HOH A O     1 
HETATM 7402 O  O     . HOH S 8 .   ? 22.715  6.469   -6.891  1.00 33.07 ? 659 HOH A O     1 
HETATM 7403 O  O     . HOH S 8 .   ? 17.841  10.134  -5.006  1.00 40.82 ? 660 HOH A O     1 
HETATM 7404 O  O     . HOH S 8 .   ? -8.808  10.432  -21.644 1.00 45.35 ? 661 HOH A O     1 
HETATM 7405 O  O     . HOH S 8 .   ? 2.493   14.170  -21.658 1.00 46.37 ? 662 HOH A O     1 
HETATM 7406 O  O     . HOH S 8 .   ? -5.529  -5.563  4.058   1.00 29.85 ? 663 HOH A O     1 
HETATM 7407 O  O     . HOH S 8 .   ? -2.014  25.482  -13.349 1.00 30.12 ? 664 HOH A O     1 
HETATM 7408 O  O     . HOH S 8 .   ? 5.551   15.012  -1.141  1.00 43.66 ? 665 HOH A O     1 
HETATM 7409 O  O     . HOH S 8 .   ? 19.890  1.705   2.444   1.00 28.04 ? 666 HOH A O     1 
HETATM 7410 O  O     . HOH S 8 .   ? 4.040   23.382  -4.345  1.00 35.40 ? 667 HOH A O     1 
HETATM 7411 O  O     . HOH S 8 .   ? 0.574   9.200   -21.853 1.00 28.31 ? 668 HOH A O     1 
HETATM 7412 O  O     . HOH S 8 .   ? -5.330  21.866  -12.782 1.00 35.67 ? 669 HOH A O     1 
HETATM 7413 O  O     . HOH S 8 .   ? -1.151  8.246   -23.784 1.00 44.27 ? 670 HOH A O     1 
HETATM 7414 O  O     . HOH S 8 .   ? -10.663 -10.377 -2.200  1.00 31.07 ? 671 HOH A O     1 
HETATM 7415 O  O     . HOH S 8 .   ? -23.477 5.021   1.034   1.00 36.64 ? 672 HOH A O     1 
HETATM 7416 O  O     . HOH S 8 .   ? -7.452  -2.987  7.074   1.00 47.68 ? 673 HOH A O     1 
HETATM 7417 O  O     . HOH S 8 .   ? -22.404 4.564   -1.165  1.00 43.86 ? 674 HOH A O     1 
HETATM 7418 O  O     . HOH S 8 .   ? -6.781  20.275  9.463   1.00 32.58 ? 675 HOH A O     1 
HETATM 7419 O  O     . HOH S 8 .   ? -13.292 -8.949  -21.128 1.00 29.78 ? 676 HOH A O     1 
HETATM 7420 O  O     . HOH S 8 .   ? -6.334  22.463  0.972   1.00 49.57 ? 677 HOH A O     1 
HETATM 7421 O  O     . HOH S 8 .   ? -17.350 15.766  -1.951  1.00 30.10 ? 678 HOH A O     1 
HETATM 7422 O  O     . HOH S 8 .   ? 11.066  8.663   -23.195 1.00 48.33 ? 679 HOH A O     1 
HETATM 7423 O  O     . HOH S 8 .   ? -3.567  -18.341 -15.022 1.00 36.11 ? 680 HOH A O     1 
HETATM 7424 O  O     . HOH S 8 .   ? -18.461 -3.224  -17.425 1.00 50.04 ? 681 HOH A O     1 
HETATM 7425 O  O     . HOH S 8 .   ? -2.383  18.540  1.449   1.00 34.98 ? 682 HOH A O     1 
HETATM 7426 O  O     . HOH S 8 .   ? -13.539 -9.586  1.516   1.00 46.73 ? 683 HOH A O     1 
HETATM 7427 O  O     . HOH S 8 .   ? 8.657   -17.391 -15.872 1.00 54.76 ? 684 HOH A O     1 
HETATM 7428 O  O     . HOH S 8 .   ? -19.937 6.332   10.886  1.00 45.04 ? 685 HOH A O     1 
HETATM 7429 O  O     . HOH S 8 .   ? -20.607 -7.029  -5.736  1.00 52.48 ? 686 HOH A O     1 
HETATM 7430 O  O     . HOH S 8 .   ? -10.951 16.885  -15.737 1.00 38.71 ? 687 HOH A O     1 
HETATM 7431 O  O     . HOH S 8 .   ? 23.600  0.596   2.085   1.00 45.24 ? 688 HOH A O     1 
HETATM 7432 O  O     . HOH S 8 .   ? -2.518  3.852   10.002  1.00 38.13 ? 689 HOH A O     1 
HETATM 7433 O  O     . HOH S 8 .   ? -4.216  20.770  7.259   1.00 36.65 ? 690 HOH A O     1 
HETATM 7434 O  O     . HOH S 8 .   ? 0.586   3.751   -28.815 1.00 37.09 ? 691 HOH A O     1 
HETATM 7435 O  O     . HOH S 8 .   ? -23.102 6.437   -4.576  1.00 38.47 ? 692 HOH A O     1 
HETATM 7436 O  O     . HOH S 8 .   ? 8.996   5.805   -27.669 1.00 41.77 ? 693 HOH A O     1 
HETATM 7437 O  O     . HOH S 8 .   ? 15.482  5.421   7.391   1.00 31.59 ? 694 HOH A O     1 
HETATM 7438 O  O     . HOH S 8 .   ? -7.120  -4.343  5.281   1.00 46.39 ? 695 HOH A O     1 
HETATM 7439 O  O     . HOH S 8 .   ? 13.802  10.874  -16.992 1.00 44.45 ? 696 HOH A O     1 
HETATM 7440 O  O     . HOH S 8 .   ? -16.391 -4.200  6.938   1.00 36.45 ? 697 HOH A O     1 
HETATM 7441 O  O     . HOH S 8 .   ? -3.086  6.463   -23.975 1.00 39.50 ? 698 HOH A O     1 
HETATM 7442 O  O     . HOH S 8 .   ? -1.252  11.407  -20.756 1.00 25.50 ? 699 HOH A O     1 
HETATM 7443 O  O     . HOH S 8 .   ? 18.322  7.327   4.248   1.00 48.21 ? 700 HOH A O     1 
HETATM 7444 O  O     . HOH S 8 .   ? -0.287  14.174  -19.860 1.00 29.46 ? 701 HOH A O     1 
HETATM 7445 O  O     . HOH S 8 .   ? 3.681   15.175  3.960   1.00 48.40 ? 702 HOH A O     1 
HETATM 7446 O  O     . HOH S 8 .   ? -19.448 9.053   11.910  1.00 37.42 ? 703 HOH A O     1 
HETATM 7447 O  O     . HOH S 8 .   ? -16.760 20.079  10.541  1.00 47.68 ? 704 HOH A O     1 
HETATM 7448 O  O     . HOH S 8 .   ? 20.499  8.152   -14.014 1.00 37.48 ? 705 HOH A O     1 
HETATM 7449 O  O     . HOH S 8 .   ? -22.392 5.081   7.964   1.00 41.22 ? 706 HOH A O     1 
HETATM 7450 O  O     . HOH S 8 .   ? -7.678  -2.560  -25.579 1.00 37.58 ? 707 HOH A O     1 
HETATM 7451 O  O     . HOH S 8 .   ? -19.229 14.425  -3.277  1.00 38.57 ? 708 HOH A O     1 
HETATM 7452 O  O     . HOH S 8 .   ? 26.252  -6.331  -15.350 1.00 45.84 ? 709 HOH A O     1 
HETATM 7453 O  O     . HOH S 8 .   ? 18.674  9.291   2.731   1.00 41.92 ? 710 HOH A O     1 
HETATM 7454 O  O     . HOH S 8 .   ? -2.145  21.643  -15.391 1.00 47.09 ? 711 HOH A O     1 
HETATM 7455 O  O     . HOH S 8 .   ? 14.297  -18.819 -15.268 1.00 48.55 ? 712 HOH A O     1 
HETATM 7456 O  O     . HOH S 8 .   ? 12.762  -8.705  5.109   1.00 53.77 ? 713 HOH A O     1 
HETATM 7457 O  O     . HOH S 8 .   ? 10.353  12.515  7.188   1.00 42.15 ? 714 HOH A O     1 
HETATM 7458 O  O     . HOH S 8 .   ? 5.513   10.653  -23.888 1.00 54.81 ? 715 HOH A O     1 
HETATM 7459 O  O     . HOH S 8 .   ? -0.456  10.662  -16.124 1.00 19.52 ? 716 HOH A O     1 
HETATM 7460 O  O     . HOH S 8 .   ? -25.659 0.611   -5.793  1.00 53.36 ? 717 HOH A O     1 
HETATM 7461 O  O     . HOH S 8 .   ? -5.677  25.750  -15.133 1.00 49.84 ? 718 HOH A O     1 
HETATM 7462 O  O     . HOH S 8 .   ? -4.375  24.917  -12.713 1.00 37.36 ? 719 HOH A O     1 
HETATM 7463 O  O     . HOH S 8 .   ? -4.544  19.103  -15.782 1.00 28.89 ? 720 HOH A O     1 
HETATM 7464 O  O     . HOH S 8 .   ? 20.621  -4.332  -0.663  1.00 38.72 ? 721 HOH A O     1 
HETATM 7465 O  O     . HOH S 8 .   ? 6.695   18.184  -16.281 1.00 40.94 ? 722 HOH A O     1 
HETATM 7466 O  O     . HOH S 8 .   ? 21.662  -5.932  -2.458  1.00 40.47 ? 723 HOH A O     1 
HETATM 7467 O  O     . HOH S 8 .   ? 16.477  -12.812 -15.939 1.00 46.29 ? 724 HOH A O     1 
HETATM 7468 O  O     . HOH S 8 .   ? -17.671 17.703  -15.412 1.00 50.61 ? 725 HOH A O     1 
HETATM 7469 O  O     . HOH S 8 .   ? 11.478  14.339  -17.269 1.00 44.96 ? 726 HOH A O     1 
HETATM 7470 O  O     . HOH S 8 .   ? -5.411  25.619  -10.095 1.00 31.33 ? 727 HOH A O     1 
HETATM 7471 O  O     . HOH S 8 .   ? -18.600 0.076   13.120  1.00 45.50 ? 728 HOH A O     1 
HETATM 7472 O  O     . HOH S 8 .   ? 1.461   16.612  6.412   1.00 54.30 ? 729 HOH A O     1 
HETATM 7473 O  O     . HOH S 8 .   ? -6.577  1.855   10.482  1.00 42.07 ? 730 HOH A O     1 
HETATM 7474 O  O     . HOH S 8 .   ? 3.957   -4.777  10.390  1.00 37.65 ? 731 HOH A O     1 
HETATM 7475 O  O     . HOH S 8 .   ? -2.460  -6.875  8.523   1.00 42.61 ? 732 HOH A O     1 
HETATM 7476 O  O     . HOH S 8 .   ? -5.062  -7.670  4.777   1.00 38.19 ? 733 HOH A O     1 
HETATM 7477 O  O     . HOH S 8 .   ? 12.372  -6.426  5.918   1.00 50.14 ? 734 HOH A O     1 
HETATM 7478 O  O     . HOH S 8 .   ? 2.344   -4.044  11.839  1.00 39.30 ? 735 HOH A O     1 
HETATM 7479 O  O     . HOH S 8 .   ? 3.709   25.697  -19.881 1.00 47.44 ? 736 HOH A O     1 
HETATM 7480 O  O     . HOH S 8 .   ? -0.524  20.118  0.046   1.00 40.13 ? 737 HOH A O     1 
HETATM 7481 O  O     . HOH S 8 .   ? -8.167  18.052  -18.183 1.00 48.68 ? 738 HOH A O     1 
HETATM 7482 O  O     . HOH S 8 .   ? 0.759   -6.169  11.916  1.00 37.00 ? 739 HOH A O     1 
HETATM 7483 O  O     . HOH S 8 .   ? 23.117  -6.219  2.557   1.00 47.64 ? 740 HOH A O     1 
HETATM 7484 O  O     . HOH S 8 .   ? 10.063  -6.182  6.791   1.00 53.27 ? 741 HOH A O     1 
HETATM 7485 O  O     . HOH T 8 .   ? -33.616 31.443  18.374  1.00 31.11 ? 501 HOH B O     1 
HETATM 7486 O  O     . HOH T 8 .   ? -50.534 23.624  -17.311 1.00 49.22 ? 502 HOH B O     1 
HETATM 7487 O  O     . HOH T 8 .   ? -49.651 21.539  -14.202 1.00 25.14 ? 503 HOH B O     1 
HETATM 7488 O  O     . HOH T 8 .   ? -39.472 37.325  10.139  1.00 40.82 ? 504 HOH B O     1 
HETATM 7489 O  O     . HOH T 8 .   ? -34.712 29.418  11.779  1.00 34.69 ? 505 HOH B O     1 
HETATM 7490 O  O     . HOH T 8 .   ? -58.888 13.813  4.199   1.00 40.90 ? 506 HOH B O     1 
HETATM 7491 O  O     . HOH T 8 .   ? -44.487 1.086   -3.273  1.00 44.15 ? 507 HOH B O     1 
HETATM 7492 O  O     . HOH T 8 .   ? -56.274 11.309  -7.120  1.00 46.62 ? 508 HOH B O     1 
HETATM 7493 O  O     . HOH T 8 .   ? -42.291 -0.134  3.684   1.00 40.10 ? 509 HOH B O     1 
HETATM 7494 O  O     . HOH T 8 .   ? -46.338 40.375  -11.060 1.00 34.15 ? 510 HOH B O     1 
HETATM 7495 O  O     . HOH T 8 .   ? -49.158 36.971  -17.799 1.00 40.36 ? 511 HOH B O     1 
HETATM 7496 O  O     . HOH T 8 .   ? -24.550 14.715  13.804  1.00 31.79 ? 512 HOH B O     1 
HETATM 7497 O  O     . HOH T 8 .   ? -36.855 -0.877  12.583  1.00 40.43 ? 513 HOH B O     1 
HETATM 7498 O  O     . HOH T 8 .   ? -23.125 13.093  -8.950  1.00 44.37 ? 514 HOH B O     1 
HETATM 7499 O  O     . HOH T 8 .   ? -52.867 18.704  22.154  1.00 32.41 ? 515 HOH B O     1 
HETATM 7500 O  O     . HOH T 8 .   ? -27.290 6.919   -0.114  1.00 30.86 ? 516 HOH B O     1 
HETATM 7501 O  O     . HOH T 8 .   ? -45.499 22.384  -12.382 1.00 24.29 ? 517 HOH B O     1 
HETATM 7502 O  O     . HOH T 8 .   ? -36.413 31.235  14.245  1.00 43.30 ? 518 HOH B O     1 
HETATM 7503 O  O     . HOH T 8 .   ? -56.432 15.834  -8.750  1.00 35.22 ? 519 HOH B O     1 
HETATM 7504 O  O     . HOH T 8 .   ? -52.702 16.459  13.534  1.00 35.90 ? 520 HOH B O     1 
HETATM 7505 O  O     . HOH T 8 .   ? -43.848 36.438  28.192  1.00 42.08 ? 521 HOH B O     1 
HETATM 7506 O  O     . HOH T 8 .   ? -44.271 6.492   6.701   1.00 29.69 ? 522 HOH B O     1 
HETATM 7507 O  O     . HOH T 8 .   ? -59.048 23.186  12.127  1.00 28.21 ? 523 HOH B O     1 
HETATM 7508 O  O     . HOH T 8 .   ? -44.731 27.861  8.014   1.00 21.32 ? 524 HOH B O     1 
HETATM 7509 O  O     . HOH T 8 .   ? -55.725 -3.262  -8.869  1.00 41.08 ? 525 HOH B O     1 
HETATM 7510 O  O     . HOH T 8 .   ? -33.021 41.334  23.258  1.00 32.23 ? 526 HOH B O     1 
HETATM 7511 O  O     . HOH T 8 .   ? -57.380 27.386  16.350  1.00 42.71 ? 527 HOH B O     1 
HETATM 7512 O  O     . HOH T 8 .   ? -49.263 44.603  5.304   1.00 47.73 ? 528 HOH B O     1 
HETATM 7513 O  O     . HOH T 8 .   ? -60.132 37.581  2.451   1.00 24.74 ? 529 HOH B O     1 
HETATM 7514 O  O     . HOH T 8 .   ? -60.883 25.432  9.925   1.00 20.92 ? 530 HOH B O     1 
HETATM 7515 O  O     . HOH T 8 .   ? -51.212 13.933  13.900  1.00 42.58 ? 531 HOH B O     1 
HETATM 7516 O  O     . HOH T 8 .   ? -44.455 37.597  11.954  1.00 41.45 ? 532 HOH B O     1 
HETATM 7517 O  O     . HOH T 8 .   ? -40.136 7.772   6.244   1.00 35.64 ? 533 HOH B O     1 
HETATM 7518 O  O     . HOH T 8 .   ? -58.172 31.160  -13.772 1.00 29.23 ? 534 HOH B O     1 
HETATM 7519 O  O     . HOH T 8 .   ? -32.082 40.527  19.573  1.00 52.63 ? 535 HOH B O     1 
HETATM 7520 O  O     . HOH T 8 .   ? -57.307 16.769  -4.022  1.00 34.60 ? 536 HOH B O     1 
HETATM 7521 O  O     . HOH T 8 .   ? -24.742 12.745  -12.817 1.00 39.90 ? 537 HOH B O     1 
HETATM 7522 O  O     . HOH T 8 .   ? -42.116 25.042  18.181  1.00 32.95 ? 538 HOH B O     1 
HETATM 7523 O  O     . HOH T 8 .   ? -19.786 11.125  9.934   1.00 37.24 ? 539 HOH B O     1 
HETATM 7524 O  O     . HOH T 8 .   ? -18.661 15.656  10.933  1.00 33.34 ? 540 HOH B O     1 
HETATM 7525 O  O     . HOH T 8 .   ? -58.821 35.546  8.824   1.00 42.32 ? 541 HOH B O     1 
HETATM 7526 O  O     . HOH T 8 .   ? -43.036 16.302  19.976  1.00 48.40 ? 542 HOH B O     1 
HETATM 7527 O  O     . HOH T 8 .   ? -44.702 37.939  -16.969 1.00 36.87 ? 543 HOH B O     1 
HETATM 7528 O  O     . HOH T 8 .   ? -51.989 37.688  10.478  1.00 33.00 ? 544 HOH B O     1 
HETATM 7529 O  O     . HOH T 8 .   ? -63.312 18.301  4.250   1.00 42.22 ? 545 HOH B O     1 
HETATM 7530 O  O     . HOH T 8 .   ? -54.402 43.237  -4.603  1.00 43.17 ? 546 HOH B O     1 
HETATM 7531 O  O     . HOH T 8 .   ? -52.352 21.287  -6.759  1.00 23.01 ? 547 HOH B O     1 
HETATM 7532 O  O     . HOH T 8 .   ? -25.392 22.516  8.721   1.00 41.30 ? 548 HOH B O     1 
HETATM 7533 O  O     . HOH T 8 .   ? -52.146 11.192  5.292   1.00 39.50 ? 549 HOH B O     1 
HETATM 7534 O  O     . HOH T 8 .   ? -46.638 16.421  -9.248  1.00 24.37 ? 550 HOH B O     1 
HETATM 7535 O  O     . HOH T 8 .   ? -32.237 14.025  -4.277  1.00 20.33 ? 551 HOH B O     1 
HETATM 7536 O  O     . HOH T 8 .   ? -31.697 28.729  11.516  1.00 37.06 ? 552 HOH B O     1 
HETATM 7537 O  O     . HOH T 8 .   ? -60.912 30.904  -11.455 1.00 50.82 ? 553 HOH B O     1 
HETATM 7538 O  O     . HOH T 8 .   ? -51.990 21.407  -12.579 1.00 26.63 ? 554 HOH B O     1 
HETATM 7539 O  O     . HOH T 8 .   ? -17.435 12.478  9.183   1.00 28.17 ? 555 HOH B O     1 
HETATM 7540 O  O     . HOH T 8 .   ? -57.007 18.434  -8.387  1.00 26.19 ? 556 HOH B O     1 
HETATM 7541 O  O     . HOH T 8 .   ? -54.636 24.910  21.488  1.00 33.63 ? 557 HOH B O     1 
HETATM 7542 O  O     . HOH T 8 .   ? -40.048 19.583  13.999  1.00 28.90 ? 558 HOH B O     1 
HETATM 7543 O  O     . HOH T 8 .   ? -63.910 34.893  -3.389  1.00 35.09 ? 559 HOH B O     1 
HETATM 7544 O  O     . HOH T 8 .   ? -18.164 19.830  5.802   1.00 25.64 ? 560 HOH B O     1 
HETATM 7545 O  O     . HOH T 8 .   ? -37.138 16.083  -0.287  1.00 25.66 ? 561 HOH B O     1 
HETATM 7546 O  O     . HOH T 8 .   ? -32.372 37.870  -15.410 1.00 46.28 ? 562 HOH B O     1 
HETATM 7547 O  O     . HOH T 8 .   ? -52.696 2.776   1.969   1.00 40.14 ? 563 HOH B O     1 
HETATM 7548 O  O     . HOH T 8 .   ? -68.642 33.879  -5.945  1.00 24.43 ? 564 HOH B O     1 
HETATM 7549 O  O     . HOH T 8 .   ? -45.739 23.842  -9.116  1.00 24.29 ? 565 HOH B O     1 
HETATM 7550 O  O     . HOH T 8 .   ? -25.591 4.474   8.565   1.00 30.20 ? 566 HOH B O     1 
HETATM 7551 O  O     . HOH T 8 .   ? -56.669 18.950  -5.743  1.00 26.74 ? 567 HOH B O     1 
HETATM 7552 O  O     . HOH T 8 .   ? -39.111 39.447  24.680  1.00 30.72 ? 568 HOH B O     1 
HETATM 7553 O  O     . HOH T 8 .   ? -43.953 13.363  -11.473 1.00 25.47 ? 569 HOH B O     1 
HETATM 7554 O  O     . HOH T 8 .   ? -37.419 27.322  -15.188 1.00 23.41 ? 570 HOH B O     1 
HETATM 7555 O  O     . HOH T 8 .   ? -62.901 30.045  8.622   1.00 29.45 ? 571 HOH B O     1 
HETATM 7556 O  O     . HOH T 8 .   ? -31.393 14.877  15.671  1.00 35.17 ? 572 HOH B O     1 
HETATM 7557 O  O     . HOH T 8 .   ? -65.575 33.518  2.972   1.00 31.96 ? 573 HOH B O     1 
HETATM 7558 O  O     . HOH T 8 .   ? -53.222 27.443  -9.968  1.00 20.64 ? 574 HOH B O     1 
HETATM 7559 O  O     . HOH T 8 .   ? -51.879 39.712  6.201   1.00 33.81 ? 575 HOH B O     1 
HETATM 7560 O  O     . HOH T 8 .   ? -28.219 32.304  1.797   1.00 37.53 ? 576 HOH B O     1 
HETATM 7561 O  O     . HOH T 8 .   ? -23.438 10.547  13.215  1.00 33.41 ? 577 HOH B O     1 
HETATM 7562 O  O     . HOH T 8 .   ? -32.072 39.685  25.518  1.00 30.65 ? 578 HOH B O     1 
HETATM 7563 O  O     . HOH T 8 .   ? -26.339 16.416  -14.700 1.00 39.82 ? 579 HOH B O     1 
HETATM 7564 O  O     . HOH T 8 .   ? -47.214 6.980   -12.834 1.00 42.58 ? 580 HOH B O     1 
HETATM 7565 O  O     . HOH T 8 .   ? -18.123 18.935  8.613   1.00 32.75 ? 581 HOH B O     1 
HETATM 7566 O  O     . HOH T 8 .   ? -43.918 40.403  -12.449 1.00 44.26 ? 582 HOH B O     1 
HETATM 7567 O  O     . HOH T 8 .   ? -33.928 23.104  13.918  1.00 36.51 ? 583 HOH B O     1 
HETATM 7568 O  O     . HOH T 8 .   ? -39.528 35.210  22.997  1.00 36.88 ? 584 HOH B O     1 
HETATM 7569 O  O     . HOH T 8 .   ? -56.236 40.334  -10.335 1.00 46.22 ? 585 HOH B O     1 
HETATM 7570 O  O     . HOH T 8 .   ? -20.981 13.123  6.510   1.00 28.00 ? 586 HOH B O     1 
HETATM 7571 O  O     . HOH T 8 .   ? -39.419 27.865  14.850  1.00 38.30 ? 587 HOH B O     1 
HETATM 7572 O  O     . HOH T 8 .   ? -52.199 9.860   -8.077  1.00 29.17 ? 588 HOH B O     1 
HETATM 7573 O  O     . HOH T 8 .   ? -39.249 0.483   -3.689  1.00 44.53 ? 589 HOH B O     1 
HETATM 7574 O  O     . HOH T 8 .   ? -24.082 11.817  1.717   1.00 25.79 ? 590 HOH B O     1 
HETATM 7575 O  O     . HOH T 8 .   ? -49.085 3.491   -8.205  1.00 30.54 ? 591 HOH B O     1 
HETATM 7576 O  O     . HOH T 8 .   ? -42.192 35.023  12.166  1.00 47.25 ? 592 HOH B O     1 
HETATM 7577 O  O     . HOH T 8 .   ? -61.022 27.783  -9.029  1.00 39.67 ? 593 HOH B O     1 
HETATM 7578 O  O     . HOH T 8 .   ? -48.130 7.834   6.215   1.00 31.11 ? 594 HOH B O     1 
HETATM 7579 O  O     . HOH T 8 .   ? -46.122 25.730  6.702   1.00 20.62 ? 595 HOH B O     1 
HETATM 7580 O  O     . HOH T 8 .   ? -28.734 12.150  -9.180  1.00 36.76 ? 596 HOH B O     1 
HETATM 7581 O  O     . HOH T 8 .   ? -44.446 4.716   -6.833  1.00 24.18 ? 597 HOH B O     1 
HETATM 7582 O  O     . HOH T 8 .   ? -21.418 17.551  12.000  1.00 38.99 ? 598 HOH B O     1 
HETATM 7583 O  O     . HOH T 8 .   ? -51.687 19.316  6.324   1.00 19.03 ? 599 HOH B O     1 
HETATM 7584 O  O     . HOH T 8 .   ? -29.267 3.023   -8.783  1.00 32.91 ? 600 HOH B O     1 
HETATM 7585 O  O     . HOH T 8 .   ? -36.620 1.932   -7.351  1.00 30.17 ? 601 HOH B O     1 
HETATM 7586 O  O     . HOH T 8 .   ? -28.203 29.318  -14.432 1.00 39.73 ? 602 HOH B O     1 
HETATM 7587 O  O     . HOH T 8 .   ? -55.755 18.807  7.020   1.00 28.56 ? 603 HOH B O     1 
HETATM 7588 O  O     . HOH T 8 .   ? -38.310 25.984  13.294  1.00 26.92 ? 604 HOH B O     1 
HETATM 7589 O  O     . HOH T 8 .   ? -55.478 22.913  3.904   1.00 21.85 ? 605 HOH B O     1 
HETATM 7590 O  O     . HOH T 8 .   ? -51.627 30.744  -15.883 1.00 35.55 ? 606 HOH B O     1 
HETATM 7591 O  O     . HOH T 8 .   ? -22.446 11.078  -0.395  1.00 26.13 ? 607 HOH B O     1 
HETATM 7592 O  O     . HOH T 8 .   ? -45.908 39.325  -20.700 1.00 50.42 ? 608 HOH B O     1 
HETATM 7593 O  O     . HOH T 8 .   ? -31.958 4.530   9.859   1.00 27.27 ? 609 HOH B O     1 
HETATM 7594 O  O     . HOH T 8 .   ? -41.713 5.664   7.072   1.00 32.69 ? 610 HOH B O     1 
HETATM 7595 O  O     . HOH T 8 .   ? -26.766 29.220  3.642   1.00 35.36 ? 611 HOH B O     1 
HETATM 7596 O  O     . HOH T 8 .   ? -40.277 33.561  19.671  1.00 46.30 ? 612 HOH B O     1 
HETATM 7597 O  O     . HOH T 8 .   ? -55.328 22.584  6.710   1.00 26.47 ? 613 HOH B O     1 
HETATM 7598 O  O     . HOH T 8 .   ? -29.780 3.644   -1.961  1.00 47.32 ? 614 HOH B O     1 
HETATM 7599 O  O     . HOH T 8 .   ? -44.343 12.851  7.790   1.00 21.27 ? 615 HOH B O     1 
HETATM 7600 O  O     . HOH T 8 .   ? -24.681 27.447  0.638   1.00 39.60 ? 616 HOH B O     1 
HETATM 7601 O  O     . HOH T 8 .   ? -24.500 12.612  -6.674  1.00 42.97 ? 617 HOH B O     1 
HETATM 7602 O  O     . HOH T 8 .   ? -25.511 22.670  -12.646 1.00 46.22 ? 618 HOH B O     1 
HETATM 7603 O  O     . HOH T 8 .   ? -39.875 26.669  1.439   1.00 33.38 ? 619 HOH B O     1 
HETATM 7604 O  O     . HOH T 8 .   ? -40.879 22.949  18.591  1.00 41.54 ? 620 HOH B O     1 
HETATM 7605 O  O     . HOH T 8 .   ? -40.801 19.293  16.745  1.00 35.59 ? 621 HOH B O     1 
HETATM 7606 O  O     . HOH T 8 .   ? -48.801 25.823  5.541   1.00 21.40 ? 622 HOH B O     1 
HETATM 7607 O  O     . HOH T 8 .   ? -45.524 28.382  3.972   1.00 20.89 ? 623 HOH B O     1 
HETATM 7608 O  O     . HOH T 8 .   ? -36.575 22.726  -10.790 1.00 25.34 ? 624 HOH B O     1 
HETATM 7609 O  O     . HOH T 8 .   ? -33.799 40.821  -8.089  1.00 49.59 ? 625 HOH B O     1 
HETATM 7610 O  O     . HOH T 8 .   ? -53.687 19.159  18.223  1.00 32.27 ? 626 HOH B O     1 
HETATM 7611 O  O     . HOH T 8 .   ? -41.852 22.852  10.280  1.00 21.24 ? 627 HOH B O     1 
HETATM 7612 O  O     . HOH T 8 .   ? -47.378 12.245  -10.685 1.00 24.72 ? 628 HOH B O     1 
HETATM 7613 O  O     . HOH T 8 .   ? -26.612 24.691  8.882   1.00 37.88 ? 629 HOH B O     1 
HETATM 7614 O  O     . HOH T 8 .   ? -55.863 20.145  21.224  1.00 43.27 ? 630 HOH B O     1 
HETATM 7615 O  O     . HOH T 8 .   ? -42.197 13.283  -14.818 1.00 33.14 ? 631 HOH B O     1 
HETATM 7616 O  O     . HOH T 8 .   ? -25.565 20.128  -12.385 1.00 34.55 ? 632 HOH B O     1 
HETATM 7617 O  O     . HOH T 8 .   ? -41.835 20.116  -19.606 1.00 41.64 ? 633 HOH B O     1 
HETATM 7618 O  O     . HOH T 8 .   ? -34.608 17.222  -6.404  1.00 32.93 ? 634 HOH B O     1 
HETATM 7619 O  O     . HOH T 8 .   ? -20.729 29.402  1.366   1.00 36.88 ? 635 HOH B O     1 
HETATM 7620 O  O     . HOH T 8 .   ? -32.371 -0.281  9.897   1.00 52.55 ? 636 HOH B O     1 
HETATM 7621 O  O     . HOH T 8 .   ? -27.267 29.164  7.663   1.00 46.26 ? 637 HOH B O     1 
HETATM 7622 O  O     . HOH T 8 .   ? -57.083 15.979  -15.382 1.00 49.07 ? 638 HOH B O     1 
HETATM 7623 O  O     . HOH T 8 .   ? -43.399 27.375  15.572  1.00 23.02 ? 639 HOH B O     1 
HETATM 7624 O  O     . HOH T 8 .   ? -55.791 30.805  13.853  1.00 36.14 ? 640 HOH B O     1 
HETATM 7625 O  O     . HOH T 8 .   ? -23.240 20.624  12.485  1.00 36.94 ? 641 HOH B O     1 
HETATM 7626 O  O     . HOH T 8 .   ? -33.723 19.061  15.654  1.00 32.83 ? 642 HOH B O     1 
HETATM 7627 O  O     . HOH T 8 .   ? -50.559 16.735  11.935  1.00 30.35 ? 643 HOH B O     1 
HETATM 7628 O  O     . HOH T 8 .   ? -23.866 6.414   -6.801  1.00 37.84 ? 644 HOH B O     1 
HETATM 7629 O  O     . HOH T 8 .   ? -52.908 31.395  12.944  1.00 33.36 ? 645 HOH B O     1 
HETATM 7630 O  O     . HOH T 8 .   ? -44.079 13.601  16.270  1.00 44.49 ? 646 HOH B O     1 
HETATM 7631 O  O     . HOH T 8 .   ? -55.794 23.881  15.849  1.00 30.08 ? 647 HOH B O     1 
HETATM 7632 O  O     . HOH T 8 .   ? -39.233 6.476   -10.646 1.00 39.59 ? 648 HOH B O     1 
HETATM 7633 O  O     . HOH T 8 .   ? -30.960 18.696  15.692  1.00 45.26 ? 649 HOH B O     1 
HETATM 7634 O  O     . HOH T 8 .   ? -26.253 29.639  0.938   1.00 35.36 ? 650 HOH B O     1 
HETATM 7635 O  O     . HOH T 8 .   ? -31.020 17.981  -4.971  1.00 27.70 ? 651 HOH B O     1 
HETATM 7636 O  O     . HOH T 8 .   ? -52.143 12.111  12.445  1.00 45.94 ? 652 HOH B O     1 
HETATM 7637 O  O     . HOH T 8 .   ? -21.601 12.923  -2.373  1.00 29.83 ? 653 HOH B O     1 
HETATM 7638 O  O     . HOH T 8 .   ? -43.650 21.873  -19.604 1.00 47.03 ? 654 HOH B O     1 
HETATM 7639 O  O     . HOH T 8 .   ? -27.334 34.653  -16.236 1.00 48.58 ? 655 HOH B O     1 
HETATM 7640 O  O     . HOH T 8 .   ? -40.209 1.361   14.901  1.00 37.59 ? 656 HOH B O     1 
HETATM 7641 O  O     . HOH T 8 .   ? -61.832 23.328  11.303  1.00 50.42 ? 657 HOH B O     1 
HETATM 7642 O  O     . HOH T 8 .   ? -29.664 4.105   2.925   1.00 26.86 ? 658 HOH B O     1 
HETATM 7643 O  O     . HOH T 8 .   ? -37.567 41.906  -0.018  1.00 42.95 ? 659 HOH B O     1 
HETATM 7644 O  O     . HOH T 8 .   ? -62.071 36.118  1.298   1.00 26.68 ? 660 HOH B O     1 
HETATM 7645 O  O     . HOH T 8 .   ? -37.267 5.045   -9.486  1.00 37.81 ? 661 HOH B O     1 
HETATM 7646 O  O     . HOH T 8 .   ? -30.241 20.071  -6.654  1.00 30.08 ? 662 HOH B O     1 
HETATM 7647 O  O     . HOH T 8 .   ? -61.268 31.892  8.772   1.00 41.80 ? 663 HOH B O     1 
HETATM 7648 O  O     . HOH T 8 .   ? -33.446 41.453  -1.291  1.00 41.14 ? 664 HOH B O     1 
HETATM 7649 O  O     . HOH T 8 .   ? -54.722 22.308  17.242  1.00 35.14 ? 665 HOH B O     1 
HETATM 7650 O  O     . HOH T 8 .   ? -46.077 15.834  -15.072 1.00 24.45 ? 666 HOH B O     1 
HETATM 7651 O  O     . HOH T 8 .   ? -54.174 20.148  5.175   1.00 33.04 ? 667 HOH B O     1 
HETATM 7652 O  O     . HOH T 8 .   ? -56.130 18.689  -16.779 1.00 44.87 ? 668 HOH B O     1 
HETATM 7653 O  O     . HOH T 8 .   ? -44.083 16.292  -17.298 1.00 39.93 ? 669 HOH B O     1 
HETATM 7654 O  O     . HOH T 8 .   ? -52.487 39.524  -14.111 1.00 46.41 ? 670 HOH B O     1 
HETATM 7655 O  O     . HOH T 8 .   ? -52.036 -1.505  -4.233  1.00 38.99 ? 671 HOH B O     1 
HETATM 7656 O  O     . HOH T 8 .   ? -62.481 18.327  8.994   1.00 40.44 ? 672 HOH B O     1 
HETATM 7657 O  O     . HOH T 8 .   ? -41.444 28.405  16.975  1.00 43.13 ? 673 HOH B O     1 
HETATM 7658 O  O     . HOH T 8 .   ? -34.966 26.951  10.641  1.00 23.93 ? 674 HOH B O     1 
HETATM 7659 O  O     . HOH T 8 .   ? -64.935 20.956  -3.791  1.00 40.56 ? 675 HOH B O     1 
HETATM 7660 O  O     . HOH T 8 .   ? -26.963 41.245  -5.872  1.00 49.14 ? 676 HOH B O     1 
HETATM 7661 O  O     . HOH T 8 .   ? -64.857 25.336  -6.234  1.00 27.69 ? 677 HOH B O     1 
HETATM 7662 O  O     . HOH T 8 .   ? -30.065 17.957  18.304  1.00 53.69 ? 678 HOH B O     1 
HETATM 7663 O  O     . HOH T 8 .   ? -24.690 15.999  18.303  1.00 50.39 ? 679 HOH B O     1 
HETATM 7664 O  O     . HOH T 8 .   ? -25.270 22.856  12.827  1.00 39.71 ? 680 HOH B O     1 
HETATM 7665 O  O     . HOH T 8 .   ? -35.230 29.376  -13.804 1.00 33.69 ? 681 HOH B O     1 
HETATM 7666 O  O     . HOH T 8 .   ? -29.283 31.011  4.263   1.00 30.83 ? 682 HOH B O     1 
HETATM 7667 O  O     . HOH T 8 .   ? -62.822 19.609  2.430   1.00 36.67 ? 683 HOH B O     1 
HETATM 7668 O  O     . HOH T 8 .   ? -42.634 1.364   13.080  1.00 35.02 ? 684 HOH B O     1 
HETATM 7669 O  O     . HOH T 8 .   ? -45.990 9.620   13.596  1.00 32.41 ? 685 HOH B O     1 
HETATM 7670 O  O     . HOH T 8 .   ? -60.073 34.867  11.134  1.00 42.02 ? 686 HOH B O     1 
HETATM 7671 O  O     . HOH T 8 .   ? -45.829 6.826   11.799  1.00 44.74 ? 687 HOH B O     1 
HETATM 7672 O  O     . HOH T 8 .   ? -61.722 28.036  10.365  1.00 32.05 ? 688 HOH B O     1 
HETATM 7673 O  O     . HOH T 8 .   ? -31.273 14.211  -8.698  1.00 36.42 ? 689 HOH B O     1 
HETATM 7674 O  O     . HOH T 8 .   ? -40.797 8.524   14.743  1.00 43.46 ? 690 HOH B O     1 
HETATM 7675 O  O     . HOH T 8 .   ? -43.674 2.066   -6.300  1.00 36.68 ? 691 HOH B O     1 
HETATM 7676 O  O     . HOH T 8 .   ? -50.874 3.393   -12.187 1.00 49.06 ? 692 HOH B O     1 
HETATM 7677 O  O     . HOH T 8 .   ? -63.601 35.389  3.381   1.00 35.12 ? 693 HOH B O     1 
HETATM 7678 O  O     . HOH T 8 .   ? -55.139 25.577  -17.279 1.00 34.28 ? 694 HOH B O     1 
HETATM 7679 O  O     . HOH T 8 .   ? -65.415 30.246  10.018  1.00 49.17 ? 695 HOH B O     1 
HETATM 7680 O  O     . HOH T 8 .   ? -47.945 39.762  5.299   1.00 34.90 ? 696 HOH B O     1 
HETATM 7681 O  O     . HOH T 8 .   ? -66.218 25.200  1.114   1.00 28.36 ? 697 HOH B O     1 
HETATM 7682 O  O     . HOH T 8 .   ? -62.125 39.959  1.482   1.00 45.02 ? 698 HOH B O     1 
HETATM 7683 O  O     . HOH T 8 .   ? -56.917 38.660  10.060  1.00 48.45 ? 699 HOH B O     1 
HETATM 7684 O  O     . HOH T 8 .   ? -59.713 17.724  -8.969  1.00 48.08 ? 700 HOH B O     1 
HETATM 7685 O  O     . HOH T 8 .   ? -23.454 36.268  -13.102 1.00 54.40 ? 701 HOH B O     1 
HETATM 7686 O  O     . HOH T 8 .   ? -35.631 4.165   -11.652 1.00 46.24 ? 702 HOH B O     1 
HETATM 7687 O  O     . HOH T 8 .   ? -58.242 23.295  14.867  1.00 34.17 ? 703 HOH B O     1 
HETATM 7688 O  O     . HOH T 8 .   ? -64.800 22.508  -5.972  1.00 43.84 ? 704 HOH B O     1 
HETATM 7689 O  O     . HOH T 8 .   ? -29.151 31.266  -21.451 1.00 44.03 ? 705 HOH B O     1 
HETATM 7690 O  O     . HOH T 8 .   ? -41.589 17.619  -17.597 1.00 33.17 ? 706 HOH B O     1 
HETATM 7691 O  O     . HOH T 8 .   ? -51.116 27.145  18.220  1.00 47.42 ? 707 HOH B O     1 
HETATM 7692 O  O     . HOH T 8 .   ? -61.322 42.068  3.308   1.00 43.25 ? 708 HOH B O     1 
HETATM 7693 O  O     . HOH T 8 .   ? -46.107 4.424   11.127  1.00 50.70 ? 709 HOH B O     1 
HETATM 7694 O  O     . HOH T 8 .   ? -47.197 11.256  -13.279 1.00 31.57 ? 710 HOH B O     1 
HETATM 7695 O  O     . HOH T 8 .   ? -20.793 14.064  11.549  1.00 47.93 ? 711 HOH B O     1 
HETATM 7696 O  O     . HOH T 8 .   ? -35.414 32.091  -15.632 1.00 40.69 ? 712 HOH B O     1 
HETATM 7697 O  O     . HOH T 8 .   ? -32.264 15.734  -6.507  1.00 30.98 ? 713 HOH B O     1 
HETATM 7698 O  O     . HOH T 8 .   ? -65.326 38.155  6.768   1.00 52.70 ? 714 HOH B O     1 
HETATM 7699 O  O     . HOH T 8 .   ? -45.331 13.485  -13.874 1.00 29.30 ? 715 HOH B O     1 
HETATM 7700 O  O     . HOH T 8 .   ? -46.630 42.151  22.065  1.00 37.56 ? 716 HOH B O     1 
HETATM 7701 O  O     . HOH T 8 .   ? -56.416 21.838  19.278  1.00 49.13 ? 717 HOH B O     1 
HETATM 7702 O  O     . HOH T 8 .   ? -52.728 15.854  -16.621 1.00 51.94 ? 718 HOH B O     1 
HETATM 7703 O  O     . HOH T 8 .   ? -45.608 14.139  -9.456  1.00 25.28 ? 719 HOH B O     1 
HETATM 7704 O  O     . HOH T 8 .   ? -48.287 38.117  -20.411 1.00 47.44 ? 720 HOH B O     1 
HETATM 7705 O  O     . HOH T 8 .   ? -38.231 23.885  14.789  1.00 39.46 ? 721 HOH B O     1 
HETATM 7706 O  O     . HOH T 8 .   ? -26.809 4.992   1.788   1.00 41.53 ? 722 HOH B O     1 
HETATM 7707 O  O     . HOH T 8 .   ? -44.445 4.875   -9.727  1.00 37.60 ? 723 HOH B O     1 
HETATM 7708 O  O     . HOH T 8 .   ? -60.935 34.782  7.074   1.00 41.18 ? 724 HOH B O     1 
HETATM 7709 O  O     . HOH T 8 .   ? -56.434 24.440  20.050  1.00 47.82 ? 725 HOH B O     1 
HETATM 7710 O  O     . HOH T 8 .   ? -56.344 40.749  9.546   1.00 50.72 ? 726 HOH B O     1 
HETATM 7711 O  O     . HOH T 8 .   ? -55.937 17.871  17.613  1.00 39.73 ? 727 HOH B O     1 
HETATM 7712 O  O     . HOH T 8 .   ? -46.945 3.158   -9.316  1.00 41.49 ? 728 HOH B O     1 
HETATM 7713 O  O     . HOH T 8 .   ? -46.654 5.037   6.489   1.00 39.93 ? 729 HOH B O     1 
HETATM 7714 O  O     . HOH T 8 .   ? -60.851 37.556  5.254   1.00 38.41 ? 730 HOH B O     1 
HETATM 7715 O  O     . HOH T 8 .   ? -42.945 38.755  -14.550 1.00 40.06 ? 731 HOH B O     1 
HETATM 7716 O  O     . HOH T 8 .   ? -59.456 15.530  -5.201  1.00 41.94 ? 732 HOH B O     1 
HETATM 7717 O  O     . HOH T 8 .   ? -54.478 9.448   -9.441  1.00 39.42 ? 733 HOH B O     1 
HETATM 7718 O  O     . HOH T 8 .   ? -53.740 27.634  18.583  1.00 42.38 ? 734 HOH B O     1 
HETATM 7719 O  O     . HOH T 8 .   ? -55.398 14.830  14.669  1.00 44.59 ? 735 HOH B O     1 
HETATM 7720 O  O     . HOH T 8 .   ? -33.994 28.075  -21.372 1.00 44.52 ? 736 HOH B O     1 
HETATM 7721 O  O     . HOH T 8 .   ? -34.847 25.406  13.092  1.00 45.49 ? 737 HOH B O     1 
HETATM 7722 O  O     . HOH T 8 .   ? -55.629 25.999  18.041  1.00 42.52 ? 738 HOH B O     1 
HETATM 7723 O  O     . HOH T 8 .   ? -63.069 22.665  -10.151 1.00 54.59 ? 739 HOH B O     1 
HETATM 7724 O  O     . HOH T 8 .   ? -62.807 20.624  -10.955 1.00 44.88 ? 740 HOH B O     1 
HETATM 7725 O  O     . HOH T 8 .   ? -54.766 41.287  -12.579 1.00 50.80 ? 741 HOH B O     1 
HETATM 7726 O  O     . HOH T 8 .   ? -48.339 15.806  -16.519 1.00 36.63 ? 742 HOH B O     1 
HETATM 7727 O  O     . HOH T 8 .   ? -32.096 27.060  -22.511 1.00 48.05 ? 743 HOH B O     1 
HETATM 7728 O  O     . HOH T 8 .   ? -17.083 13.320  11.614  1.00 33.47 ? 744 HOH B O     1 
HETATM 7729 O  O     . HOH T 8 .   ? -62.540 44.332  -0.895  1.00 51.08 ? 745 HOH B O     1 
HETATM 7730 O  O     . HOH T 8 .   ? -27.220 3.232   -10.322 1.00 39.91 ? 746 HOH B O     1 
HETATM 7731 O  O     . HOH T 8 .   ? -63.222 25.143  -8.331  1.00 44.38 ? 747 HOH B O     1 
HETATM 7732 O  O     . HOH T 8 .   ? -31.057 1.532   -10.120 1.00 42.63 ? 748 HOH B O     1 
HETATM 7733 O  O     . HOH T 8 .   ? -36.774 29.967  -16.451 1.00 38.69 ? 749 HOH B O     1 
HETATM 7734 O  O     . HOH T 8 .   ? -29.874 32.533  6.261   1.00 39.88 ? 750 HOH B O     1 
HETATM 7735 O  O     . HOH T 8 .   ? -34.586 -0.260  -6.844  1.00 49.16 ? 751 HOH B O     1 
HETATM 7736 O  O     . HOH T 8 .   ? -43.746 10.706  16.167  1.00 48.27 ? 752 HOH B O     1 
HETATM 7737 O  O     . HOH U 8 .   ? -0.760  40.993  10.450  1.00 39.40 ? 501 HOH C O     1 
HETATM 7738 O  O     . HOH U 8 .   ? 4.978   25.575  -5.885  1.00 37.85 ? 502 HOH C O     1 
HETATM 7739 O  O     . HOH U 8 .   ? -22.434 39.479  -0.956  1.00 32.15 ? 503 HOH C O     1 
HETATM 7740 O  O     . HOH U 8 .   ? -9.219  38.572  -22.906 1.00 46.86 ? 504 HOH C O     1 
HETATM 7741 O  O     . HOH U 8 .   ? -1.368  45.208  8.278   1.00 29.37 ? 505 HOH C O     1 
HETATM 7742 O  O     . HOH U 8 .   ? 16.240  32.797  1.889   1.00 34.62 ? 506 HOH C O     1 
HETATM 7743 O  O     . HOH U 8 .   ? 9.738   27.724  -16.174 1.00 44.91 ? 507 HOH C O     1 
HETATM 7744 O  O     . HOH U 8 .   ? -14.891 63.068  -17.545 1.00 40.45 ? 508 HOH C O     1 
HETATM 7745 O  O     . HOH U 8 .   ? 11.205  33.424  7.397   1.00 45.08 ? 509 HOH C O     1 
HETATM 7746 O  O     . HOH U 8 .   ? -4.428  32.745  4.545   1.00 35.58 ? 510 HOH C O     1 
HETATM 7747 O  O     . HOH U 8 .   ? -0.403  30.938  8.915   1.00 43.41 ? 511 HOH C O     1 
HETATM 7748 O  O     . HOH U 8 .   ? 4.549   56.806  14.176  1.00 47.43 ? 512 HOH C O     1 
HETATM 7749 O  O     . HOH U 8 .   ? -13.668 55.021  0.279   1.00 31.95 ? 513 HOH C O     1 
HETATM 7750 O  O     . HOH U 8 .   ? -11.698 55.503  2.279   1.00 46.52 ? 514 HOH C O     1 
HETATM 7751 O  O     . HOH U 8 .   ? -4.975  36.680  -17.765 1.00 26.21 ? 515 HOH C O     1 
HETATM 7752 O  O     . HOH U 8 .   ? -3.986  26.813  -8.158  1.00 29.18 ? 516 HOH C O     1 
HETATM 7753 O  O     . HOH U 8 .   ? -4.930  54.744  -18.662 1.00 42.57 ? 517 HOH C O     1 
HETATM 7754 O  O     . HOH U 8 .   ? -5.021  63.993  -12.269 1.00 33.11 ? 518 HOH C O     1 
HETATM 7755 O  O     . HOH U 8 .   ? -15.379 30.017  -0.193  1.00 42.90 ? 519 HOH C O     1 
HETATM 7756 O  O     . HOH U 8 .   ? 9.565   38.758  -18.083 1.00 35.57 ? 520 HOH C O     1 
HETATM 7757 O  O     . HOH U 8 .   ? -12.882 56.518  -19.637 1.00 37.15 ? 521 HOH C O     1 
HETATM 7758 O  O     . HOH U 8 .   ? -6.634  42.121  5.235   1.00 22.04 ? 522 HOH C O     1 
HETATM 7759 O  O     . HOH U 8 .   ? -21.988 56.617  -4.251  1.00 42.00 ? 523 HOH C O     1 
HETATM 7760 O  O     . HOH U 8 .   ? -18.996 69.926  -11.758 1.00 31.45 ? 524 HOH C O     1 
HETATM 7761 O  O     . HOH U 8 .   ? 15.322  36.799  -12.903 1.00 38.47 ? 525 HOH C O     1 
HETATM 7762 O  O     . HOH U 8 .   ? -17.691 41.229  -15.576 1.00 45.69 ? 526 HOH C O     1 
HETATM 7763 O  O     . HOH U 8 .   ? -1.746  33.085  4.197   1.00 28.81 ? 527 HOH C O     1 
HETATM 7764 O  O     . HOH U 8 .   ? 10.856  64.068  0.867   1.00 43.05 ? 528 HOH C O     1 
HETATM 7765 O  O     . HOH U 8 .   ? 15.948  50.080  7.057   1.00 34.69 ? 529 HOH C O     1 
HETATM 7766 O  O     . HOH U 8 .   ? -2.014  37.046  -22.430 1.00 35.60 ? 530 HOH C O     1 
HETATM 7767 O  O     . HOH U 8 .   ? 3.614   47.824  -11.947 1.00 20.28 ? 531 HOH C O     1 
HETATM 7768 O  O     . HOH U 8 .   ? -4.499  29.487  -8.882  1.00 26.25 ? 532 HOH C O     1 
HETATM 7769 O  O     . HOH U 8 .   ? -18.238 61.762  -5.855  1.00 42.29 ? 533 HOH C O     1 
HETATM 7770 O  O     . HOH U 8 .   ? 14.967  44.282  -14.510 1.00 34.59 ? 534 HOH C O     1 
HETATM 7771 O  O     . HOH U 8 .   ? 18.755  40.375  6.265   1.00 30.61 ? 535 HOH C O     1 
HETATM 7772 O  O     . HOH U 8 .   ? 20.941  43.120  0.616   1.00 40.23 ? 536 HOH C O     1 
HETATM 7773 O  O     . HOH U 8 .   ? -18.609 51.089  7.106   1.00 43.77 ? 537 HOH C O     1 
HETATM 7774 O  O     . HOH U 8 .   ? -24.836 58.212  -12.828 1.00 35.53 ? 538 HOH C O     1 
HETATM 7775 O  O     . HOH U 8 .   ? 15.938  25.969  1.389   1.00 33.91 ? 539 HOH C O     1 
HETATM 7776 O  O     . HOH U 8 .   ? 1.893   45.903  -10.612 1.00 19.54 ? 540 HOH C O     1 
HETATM 7777 O  O     . HOH U 8 .   ? 9.547   52.675  -16.088 1.00 37.73 ? 541 HOH C O     1 
HETATM 7778 O  O     . HOH U 8 .   ? -1.366  33.511  1.454   1.00 24.73 ? 542 HOH C O     1 
HETATM 7779 O  O     . HOH U 8 .   ? -5.706  49.900  -18.098 1.00 29.58 ? 543 HOH C O     1 
HETATM 7780 O  O     . HOH U 8 .   ? -3.268  32.349  -0.245  1.00 32.68 ? 544 HOH C O     1 
HETATM 7781 O  O     . HOH U 8 .   ? -9.932  51.335  -3.610  1.00 25.87 ? 545 HOH C O     1 
HETATM 7782 O  O     . HOH U 8 .   ? 3.798   32.790  -16.063 1.00 26.77 ? 546 HOH C O     1 
HETATM 7783 O  O     . HOH U 8 .   ? -10.791 45.172  10.819  1.00 40.22 ? 547 HOH C O     1 
HETATM 7784 O  O     . HOH U 8 .   ? -3.452  35.124  14.840  1.00 43.00 ? 548 HOH C O     1 
HETATM 7785 O  O     . HOH U 8 .   ? 5.718   39.351  5.834   1.00 20.47 ? 549 HOH C O     1 
HETATM 7786 O  O     . HOH U 8 .   ? -0.393  38.518  2.564   1.00 20.73 ? 550 HOH C O     1 
HETATM 7787 O  O     . HOH U 8 .   ? -0.665  49.397  14.544  1.00 27.05 ? 551 HOH C O     1 
HETATM 7788 O  O     . HOH U 8 .   ? 6.069   31.874  -14.311 1.00 24.25 ? 552 HOH C O     1 
HETATM 7789 O  O     . HOH U 8 .   ? 17.723  36.175  -6.798  1.00 25.79 ? 553 HOH C O     1 
HETATM 7790 O  O     . HOH U 8 .   ? 9.106   24.541  -5.652  1.00 41.07 ? 554 HOH C O     1 
HETATM 7791 O  O     . HOH U 8 .   ? -7.261  30.010  -3.329  1.00 34.48 ? 555 HOH C O     1 
HETATM 7792 O  O     . HOH U 8 .   ? 10.647  59.901  -6.942  1.00 44.02 ? 556 HOH C O     1 
HETATM 7793 O  O     . HOH U 8 .   ? -0.132  64.639  -9.483  1.00 50.26 ? 557 HOH C O     1 
HETATM 7794 O  O     . HOH U 8 .   ? -2.766  37.826  -26.352 1.00 34.02 ? 558 HOH C O     1 
HETATM 7795 O  O     . HOH U 8 .   ? -18.096 64.883  -9.249  1.00 42.27 ? 559 HOH C O     1 
HETATM 7796 O  O     . HOH U 8 .   ? -8.626  31.316  2.811   1.00 38.58 ? 560 HOH C O     1 
HETATM 7797 O  O     . HOH U 8 .   ? -15.386 43.570  -17.292 1.00 34.70 ? 561 HOH C O     1 
HETATM 7798 O  O     . HOH U 8 .   ? -10.964 43.696  -11.889 1.00 19.30 ? 562 HOH C O     1 
HETATM 7799 O  O     . HOH U 8 .   ? -17.484 42.685  -10.694 1.00 25.49 ? 563 HOH C O     1 
HETATM 7800 O  O     . HOH U 8 .   ? -12.701 35.798  -10.444 1.00 48.47 ? 564 HOH C O     1 
HETATM 7801 O  O     . HOH U 8 .   ? -13.915 32.784  7.282   1.00 44.08 ? 565 HOH C O     1 
HETATM 7802 O  O     . HOH U 8 .   ? 8.088   58.997  13.890  1.00 47.65 ? 566 HOH C O     1 
HETATM 7803 O  O     . HOH U 8 .   ? 1.067   54.319  11.174  1.00 26.90 ? 567 HOH C O     1 
HETATM 7804 O  O     . HOH U 8 .   ? 9.044   25.821  -10.244 1.00 31.66 ? 568 HOH C O     1 
HETATM 7805 O  O     . HOH U 8 .   ? -0.516  38.514  8.382   1.00 26.13 ? 569 HOH C O     1 
HETATM 7806 O  O     . HOH U 8 .   ? -9.770  38.152  10.792  1.00 35.78 ? 570 HOH C O     1 
HETATM 7807 O  O     . HOH U 8 .   ? 13.335  50.775  -15.925 1.00 40.82 ? 571 HOH C O     1 
HETATM 7808 O  O     . HOH U 8 .   ? -7.173  71.205  -5.367  1.00 36.17 ? 572 HOH C O     1 
HETATM 7809 O  O     . HOH U 8 .   ? -4.128  53.686  7.004   1.00 30.66 ? 573 HOH C O     1 
HETATM 7810 O  O     . HOH U 8 .   ? -19.333 40.483  -13.780 1.00 37.76 ? 574 HOH C O     1 
HETATM 7811 O  O     . HOH U 8 .   ? -20.566 30.755  7.523   1.00 44.83 ? 575 HOH C O     1 
HETATM 7812 O  O     . HOH U 8 .   ? -22.445 52.227  -14.351 1.00 32.11 ? 576 HOH C O     1 
HETATM 7813 O  O     . HOH U 8 .   ? -11.302 34.868  3.796   1.00 25.42 ? 577 HOH C O     1 
HETATM 7814 O  O     . HOH U 8 .   ? -14.446 63.595  -22.191 1.00 47.74 ? 578 HOH C O     1 
HETATM 7815 O  O     . HOH U 8 .   ? -20.673 31.386  -2.872  1.00 34.18 ? 579 HOH C O     1 
HETATM 7816 O  O     . HOH U 8 .   ? -0.786  26.214  -3.275  1.00 31.57 ? 580 HOH C O     1 
HETATM 7817 O  O     . HOH U 8 .   ? 10.438  35.815  9.767   1.00 35.11 ? 581 HOH C O     1 
HETATM 7818 O  O     . HOH U 8 .   ? -18.349 35.573  4.050   1.00 28.49 ? 582 HOH C O     1 
HETATM 7819 O  O     . HOH U 8 .   ? 8.366   31.766  4.472   1.00 34.32 ? 583 HOH C O     1 
HETATM 7820 O  O     . HOH U 8 .   ? 8.331   30.967  -18.150 1.00 45.46 ? 584 HOH C O     1 
HETATM 7821 O  O     . HOH U 8 .   ? -7.614  37.389  -18.337 1.00 36.40 ? 585 HOH C O     1 
HETATM 7822 O  O     . HOH U 8 .   ? -7.281  31.792  -1.479  1.00 39.72 ? 586 HOH C O     1 
HETATM 7823 O  O     . HOH U 8 .   ? 2.105   52.864  -18.791 1.00 33.20 ? 587 HOH C O     1 
HETATM 7824 O  O     . HOH U 8 .   ? -10.475 43.640  7.424   1.00 25.81 ? 588 HOH C O     1 
HETATM 7825 O  O     . HOH U 8 .   ? -24.254 55.350  -16.472 1.00 39.21 ? 589 HOH C O     1 
HETATM 7826 O  O     . HOH U 8 .   ? 9.485   41.544  -16.980 1.00 36.58 ? 590 HOH C O     1 
HETATM 7827 O  O     . HOH U 8 .   ? 13.628  50.779  12.646  1.00 40.05 ? 591 HOH C O     1 
HETATM 7828 O  O     . HOH U 8 .   ? 14.241  61.779  7.725   1.00 48.97 ? 592 HOH C O     1 
HETATM 7829 O  O     . HOH U 8 .   ? -4.786  28.167  -0.971  1.00 39.32 ? 593 HOH C O     1 
HETATM 7830 O  O     . HOH U 8 .   ? 4.350   47.252  -7.873  1.00 21.34 ? 594 HOH C O     1 
HETATM 7831 O  O     . HOH U 8 .   ? 3.750   38.229  -25.538 1.00 29.92 ? 595 HOH C O     1 
HETATM 7832 O  O     . HOH U 8 .   ? 16.972  44.681  -10.335 1.00 31.57 ? 596 HOH C O     1 
HETATM 7833 O  O     . HOH U 8 .   ? -1.751  34.777  -11.201 1.00 24.13 ? 597 HOH C O     1 
HETATM 7834 O  O     . HOH U 8 .   ? 15.027  29.503  -7.605  1.00 25.00 ? 598 HOH C O     1 
HETATM 7835 O  O     . HOH U 8 .   ? -2.497  38.675  -10.474 1.00 19.37 ? 599 HOH C O     1 
HETATM 7836 O  O     . HOH U 8 .   ? -23.871 53.870  -7.741  1.00 46.60 ? 600 HOH C O     1 
HETATM 7837 O  O     . HOH U 8 .   ? -21.064 37.455  -8.446  1.00 38.71 ? 601 HOH C O     1 
HETATM 7838 O  O     . HOH U 8 .   ? -24.605 30.521  4.446   1.00 48.51 ? 602 HOH C O     1 
HETATM 7839 O  O     . HOH U 8 .   ? 2.097   36.042  -8.086  1.00 20.58 ? 603 HOH C O     1 
HETATM 7840 O  O     . HOH U 8 .   ? -22.941 40.213  -10.923 1.00 46.30 ? 604 HOH C O     1 
HETATM 7841 O  O     . HOH U 8 .   ? 7.447   27.693  1.638   1.00 30.66 ? 605 HOH C O     1 
HETATM 7842 O  O     . HOH U 8 .   ? -8.635  65.466  -20.548 1.00 59.48 ? 606 HOH C O     1 
HETATM 7843 O  O     . HOH U 8 .   ? -15.453 45.798  -18.689 1.00 55.27 ? 607 HOH C O     1 
HETATM 7844 O  O     . HOH U 8 .   ? -7.513  47.078  -22.582 1.00 38.20 ? 608 HOH C O     1 
HETATM 7845 O  O     . HOH U 8 .   ? 19.143  37.407  0.543   1.00 35.64 ? 609 HOH C O     1 
HETATM 7846 O  O     . HOH U 8 .   ? -1.991  49.177  -14.115 1.00 22.79 ? 610 HOH C O     1 
HETATM 7847 O  O     . HOH U 8 .   ? 1.834   36.024  -10.910 1.00 22.18 ? 611 HOH C O     1 
HETATM 7848 O  O     . HOH U 8 .   ? 1.026   51.951  -5.308  1.00 35.19 ? 612 HOH C O     1 
HETATM 7849 O  O     . HOH U 8 .   ? 2.857   43.306  -9.608  1.00 22.47 ? 613 HOH C O     1 
HETATM 7850 O  O     . HOH U 8 .   ? -0.016  65.730  -4.441  1.00 37.63 ? 614 HOH C O     1 
HETATM 7851 O  O     . HOH U 8 .   ? -18.629 40.709  2.779   1.00 26.80 ? 615 HOH C O     1 
HETATM 7852 O  O     . HOH U 8 .   ? -0.071  45.470  5.109   1.00 28.53 ? 616 HOH C O     1 
HETATM 7853 O  O     . HOH U 8 .   ? 21.192  48.565  -9.192  1.00 47.71 ? 617 HOH C O     1 
HETATM 7854 O  O     . HOH U 8 .   ? -17.391 43.416  6.717   1.00 50.16 ? 618 HOH C O     1 
HETATM 7855 O  O     . HOH U 8 .   ? 3.117   35.667  -19.609 1.00 43.53 ? 619 HOH C O     1 
HETATM 7856 O  O     . HOH U 8 .   ? 4.276   59.277  -14.147 1.00 44.89 ? 620 HOH C O     1 
HETATM 7857 O  O     . HOH U 8 .   ? -17.776 32.031  -6.241  1.00 38.15 ? 621 HOH C O     1 
HETATM 7858 O  O     . HOH U 8 .   ? -5.400  38.823  -15.972 1.00 26.06 ? 622 HOH C O     1 
HETATM 7859 O  O     . HOH U 8 .   ? -10.618 40.207  6.459   1.00 28.87 ? 623 HOH C O     1 
HETATM 7860 O  O     . HOH U 8 .   ? 8.265   41.934  11.784  1.00 32.63 ? 624 HOH C O     1 
HETATM 7861 O  O     . HOH U 8 .   ? -10.080 36.173  -9.682  1.00 33.74 ? 625 HOH C O     1 
HETATM 7862 O  O     . HOH U 8 .   ? -16.189 39.189  -14.887 1.00 47.72 ? 626 HOH C O     1 
HETATM 7863 O  O     . HOH U 8 .   ? -0.962  36.611  -9.135  1.00 23.29 ? 627 HOH C O     1 
HETATM 7864 O  O     . HOH U 8 .   ? 14.632  57.357  7.350   1.00 37.67 ? 628 HOH C O     1 
HETATM 7865 O  O     . HOH U 8 .   ? 16.164  32.284  -8.173  1.00 33.78 ? 629 HOH C O     1 
HETATM 7866 O  O     . HOH U 8 .   ? -17.380 40.457  -12.097 1.00 52.64 ? 630 HOH C O     1 
HETATM 7867 O  O     . HOH U 8 .   ? -8.241  56.094  -19.541 1.00 42.16 ? 631 HOH C O     1 
HETATM 7868 O  O     . HOH U 8 .   ? -16.385 57.679  5.179   1.00 50.91 ? 632 HOH C O     1 
HETATM 7869 O  O     . HOH U 8 .   ? -14.916 38.488  -10.353 1.00 25.82 ? 633 HOH C O     1 
HETATM 7870 O  O     . HOH U 8 .   ? 8.565   60.669  -5.879  1.00 42.92 ? 634 HOH C O     1 
HETATM 7871 O  O     . HOH U 8 .   ? 2.908   49.099  -19.290 1.00 23.63 ? 635 HOH C O     1 
HETATM 7872 O  O     . HOH U 8 .   ? -19.168 63.320  -16.856 1.00 45.55 ? 636 HOH C O     1 
HETATM 7873 O  O     . HOH U 8 .   ? -3.577  50.473  -22.506 1.00 45.11 ? 637 HOH C O     1 
HETATM 7874 O  O     . HOH U 8 .   ? -14.058 67.220  -15.556 1.00 47.76 ? 638 HOH C O     1 
HETATM 7875 O  O     . HOH U 8 .   ? -0.689  40.633  15.780  1.00 48.48 ? 639 HOH C O     1 
HETATM 7876 O  O     . HOH U 8 .   ? 4.703   57.223  11.869  1.00 41.22 ? 640 HOH C O     1 
HETATM 7877 O  O     . HOH U 8 .   ? -8.665  58.665  2.953   1.00 41.07 ? 641 HOH C O     1 
HETATM 7878 O  O     . HOH U 8 .   ? 15.470  52.399  8.423   1.00 38.58 ? 642 HOH C O     1 
HETATM 7879 O  O     . HOH U 8 .   ? -7.373  42.412  11.006  1.00 26.66 ? 643 HOH C O     1 
HETATM 7880 O  O     . HOH U 8 .   ? -1.732  33.897  12.543  1.00 45.96 ? 644 HOH C O     1 
HETATM 7881 O  O     . HOH U 8 .   ? -0.143  56.818  -14.530 1.00 31.03 ? 645 HOH C O     1 
HETATM 7882 O  O     . HOH U 8 .   ? 12.899  61.751  4.038   1.00 34.98 ? 646 HOH C O     1 
HETATM 7883 O  O     . HOH U 8 .   ? 2.141   64.956  -5.483  1.00 37.58 ? 647 HOH C O     1 
HETATM 7884 O  O     . HOH U 8 .   ? 4.565   37.032  12.951  1.00 36.26 ? 648 HOH C O     1 
HETATM 7885 O  O     . HOH U 8 .   ? -5.751  49.223  -21.079 1.00 42.47 ? 649 HOH C O     1 
HETATM 7886 O  O     . HOH U 8 .   ? 4.145   27.023  1.307   1.00 43.82 ? 650 HOH C O     1 
HETATM 7887 O  O     . HOH U 8 .   ? 3.992   56.916  -17.380 1.00 40.14 ? 651 HOH C O     1 
HETATM 7888 O  O     . HOH U 8 .   ? -0.039  53.559  -17.374 1.00 27.01 ? 652 HOH C O     1 
HETATM 7889 O  O     . HOH U 8 .   ? 7.025   26.542  -5.585  1.00 31.67 ? 653 HOH C O     1 
HETATM 7890 O  O     . HOH U 8 .   ? -11.475 26.883  -7.612  1.00 46.44 ? 654 HOH C O     1 
HETATM 7891 O  O     . HOH U 8 .   ? 2.836   26.237  -1.015  1.00 38.66 ? 655 HOH C O     1 
HETATM 7892 O  O     . HOH U 8 .   ? 1.597   63.497  -7.917  1.00 32.32 ? 656 HOH C O     1 
HETATM 7893 O  O     . HOH U 8 .   ? -7.429  44.200  13.241  1.00 35.95 ? 657 HOH C O     1 
HETATM 7894 O  O     . HOH U 8 .   ? 1.994   57.010  9.823   1.00 33.82 ? 658 HOH C O     1 
HETATM 7895 O  O     . HOH U 8 .   ? 16.065  48.071  -9.485  1.00 31.96 ? 659 HOH C O     1 
HETATM 7896 O  O     . HOH U 8 .   ? 15.145  49.425  16.080  1.00 47.10 ? 660 HOH C O     1 
HETATM 7897 O  O     . HOH U 8 .   ? -0.286  64.065  10.885  1.00 35.98 ? 661 HOH C O     1 
HETATM 7898 O  O     . HOH U 8 .   ? -13.493 41.608  -17.661 1.00 28.30 ? 662 HOH C O     1 
HETATM 7899 O  O     . HOH U 8 .   ? -21.154 40.750  2.421   1.00 38.85 ? 663 HOH C O     1 
HETATM 7900 O  O     . HOH U 8 .   ? -8.766  57.474  5.244   1.00 49.20 ? 664 HOH C O     1 
HETATM 7901 O  O     . HOH U 8 .   ? 21.226  36.863  -1.068  1.00 36.62 ? 665 HOH C O     1 
HETATM 7902 O  O     . HOH U 8 .   ? -22.831 62.019  -14.637 1.00 39.10 ? 666 HOH C O     1 
HETATM 7903 O  O     . HOH U 8 .   ? -7.301  64.937  -16.437 1.00 45.52 ? 667 HOH C O     1 
HETATM 7904 O  O     . HOH U 8 .   ? -20.888 41.139  -17.959 1.00 43.18 ? 668 HOH C O     1 
HETATM 7905 O  O     . HOH U 8 .   ? -25.889 52.360  -7.168  1.00 49.80 ? 669 HOH C O     1 
HETATM 7906 O  O     . HOH U 8 .   ? -23.456 61.083  2.531   1.00 50.02 ? 670 HOH C O     1 
HETATM 7907 O  O     . HOH U 8 .   ? -11.556 40.293  9.182   1.00 31.69 ? 671 HOH C O     1 
HETATM 7908 O  O     . HOH U 8 .   ? -17.106 59.690  3.536   1.00 43.91 ? 672 HOH C O     1 
HETATM 7909 O  O     . HOH U 8 .   ? -9.360  36.457  -16.291 1.00 45.39 ? 673 HOH C O     1 
HETATM 7910 O  O     . HOH U 8 .   ? 1.919   36.853  -21.195 1.00 39.22 ? 674 HOH C O     1 
HETATM 7911 O  O     . HOH U 8 .   ? 3.524   63.291  -9.994  1.00 41.47 ? 675 HOH C O     1 
HETATM 7912 O  O     . HOH U 8 .   ? -10.316 57.746  1.251   1.00 45.19 ? 676 HOH C O     1 
HETATM 7913 O  O     . HOH U 8 .   ? -2.016  55.797  14.713  1.00 42.54 ? 677 HOH C O     1 
HETATM 7914 O  O     . HOH U 8 .   ? 19.212  41.358  3.531   1.00 34.02 ? 678 HOH C O     1 
HETATM 7915 O  O     . HOH U 8 .   ? -2.088  29.156  3.126   1.00 47.53 ? 679 HOH C O     1 
HETATM 7916 O  O     . HOH U 8 .   ? -10.933 37.420  -14.534 1.00 37.45 ? 680 HOH C O     1 
HETATM 7917 O  O     . HOH U 8 .   ? -7.083  46.610  13.458  1.00 42.27 ? 681 HOH C O     1 
HETATM 7918 O  O     . HOH U 8 .   ? -9.965  42.415  10.012  1.00 29.94 ? 682 HOH C O     1 
HETATM 7919 O  O     . HOH U 8 .   ? 10.665  30.261  4.117   1.00 46.13 ? 683 HOH C O     1 
HETATM 7920 O  O     . HOH U 8 .   ? -23.564 56.113  -6.565  1.00 40.52 ? 684 HOH C O     1 
HETATM 7921 O  O     . HOH U 8 .   ? -5.465  33.901  -18.637 1.00 38.29 ? 685 HOH C O     1 
HETATM 7922 O  O     . HOH U 8 .   ? 18.733  36.116  -9.302  1.00 31.02 ? 686 HOH C O     1 
HETATM 7923 O  O     . HOH U 8 .   ? 13.773  52.829  9.898   1.00 41.64 ? 687 HOH C O     1 
HETATM 7924 O  O     . HOH U 8 .   ? -19.482 37.649  4.861   1.00 47.15 ? 688 HOH C O     1 
HETATM 7925 O  O     . HOH U 8 .   ? -2.323  57.068  -17.111 1.00 54.06 ? 689 HOH C O     1 
HETATM 7926 O  O     . HOH U 8 .   ? -18.778 62.382  -19.686 1.00 49.23 ? 690 HOH C O     1 
HETATM 7927 O  O     . HOH U 8 .   ? -11.233 32.812  5.956   1.00 39.67 ? 691 HOH C O     1 
HETATM 7928 O  O     . HOH U 8 .   ? -9.237  42.499  5.376   1.00 23.75 ? 692 HOH C O     1 
HETATM 7929 O  O     . HOH U 8 .   ? -18.477 41.111  5.658   1.00 33.35 ? 693 HOH C O     1 
HETATM 7930 O  O     . HOH U 8 .   ? -5.114  30.755  6.227   1.00 40.23 ? 694 HOH C O     1 
HETATM 7931 O  O     . HOH U 8 .   ? 4.104   74.348  -6.160  1.00 40.15 ? 695 HOH C O     1 
HETATM 7932 O  O     . HOH U 8 .   ? -26.072 56.506  -14.986 1.00 40.61 ? 696 HOH C O     1 
HETATM 7933 O  O     . HOH U 8 .   ? 6.134   31.819  -19.126 1.00 50.64 ? 697 HOH C O     1 
HETATM 7934 O  O     . HOH U 8 .   ? 0.171   64.996  -11.943 1.00 48.86 ? 698 HOH C O     1 
HETATM 7935 O  O     . HOH U 8 .   ? 11.108  47.664  -17.200 1.00 43.24 ? 699 HOH C O     1 
HETATM 7936 O  O     . HOH U 8 .   ? 5.062   49.115  -21.406 1.00 42.04 ? 700 HOH C O     1 
HETATM 7937 O  O     . HOH U 8 .   ? -17.277 64.343  -20.294 1.00 45.64 ? 701 HOH C O     1 
HETATM 7938 O  O     . HOH U 8 .   ? -10.554 35.526  -12.182 1.00 33.03 ? 702 HOH C O     1 
HETATM 7939 O  O     . HOH U 8 .   ? -8.030  26.214  -10.855 1.00 47.45 ? 703 HOH C O     1 
HETATM 7940 O  O     . HOH U 8 .   ? 2.786   55.254  -19.125 1.00 44.96 ? 704 HOH C O     1 
HETATM 7941 O  O     . HOH U 8 .   ? 10.964  50.565  -16.802 1.00 50.66 ? 705 HOH C O     1 
HETATM 7942 O  O     . HOH U 8 .   ? 20.598  38.984  2.356   1.00 31.78 ? 706 HOH C O     1 
HETATM 7943 O  O     . HOH U 8 .   ? -4.236  56.520  14.798  1.00 47.87 ? 707 HOH C O     1 
HETATM 7944 O  O     . HOH U 8 .   ? 2.410   57.787  -15.430 1.00 42.17 ? 708 HOH C O     1 
HETATM 7945 O  O     . HOH U 8 .   ? 6.573   29.338  3.922   1.00 42.24 ? 709 HOH C O     1 
HETATM 7946 O  O     . HOH U 8 .   ? -21.894 38.671  3.885   1.00 43.27 ? 710 HOH C O     1 
HETATM 7947 O  O     . HOH U 8 .   ? 1.044   52.007  -21.018 1.00 38.28 ? 711 HOH C O     1 
HETATM 7948 O  O     . HOH U 8 .   ? -6.931  40.309  12.347  1.00 45.76 ? 712 HOH C O     1 
HETATM 7949 O  O     . HOH U 8 .   ? -17.897 37.965  -10.480 1.00 48.58 ? 713 HOH C O     1 
HETATM 7950 O  O     . HOH U 8 .   ? -11.191 36.091  12.074  1.00 48.02 ? 714 HOH C O     1 
HETATM 7951 O  O     . HOH U 8 .   ? 21.410  43.214  3.569   1.00 36.40 ? 715 HOH C O     1 
HETATM 7952 O  O     . HOH U 8 .   ? 16.978  41.999  -15.485 1.00 45.08 ? 716 HOH C O     1 
HETATM 7953 O  O     . HOH U 8 .   ? 21.343  37.662  4.730   1.00 37.89 ? 717 HOH C O     1 
# 
