data_9BO5
# 
_entry.id   9BO5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9BO5         pdb_00009bo5 10.2210/pdb9bo5/pdb 
WWPDB D_1000282933 ?            ?                   
# 
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 2025-03-12 ? 
# 
_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.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BO5 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-03 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              karen.anderson@yale.edu 
_pdbx_contact_author.name_first         Karen 
_pdbx_contact_author.name_last          Anderson 
_pdbx_contact_author.name_mi            S 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3433-0780 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Papini, C.'     1 0000-0002-6098-4959 
'Anderson, K.S.' 2 0000-0003-3433-0780 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Bio Med Chem Au' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2694-2437 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            5 
_citation.language                  ? 
_citation.page_first                215 
_citation.page_last                 226 
_citation.title                     
'Exploring Possible Drug-Resistant Variants of SARS-CoV-2 Main Protease (M pro ) with Noncovalent Preclinical Candidate, Mpro61.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsbiomedchemau.4c00109 
_citation.pdbx_database_id_PubMed   39990941 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kenneson, J.R.'  1 ? 
primary 'Papini, C.'      2 ? 
primary 'Tang, S.'        3 ? 
primary 'Huynh, K.'       4 ? 
primary 'Zhang, C.H.'     5 ? 
primary 'Jorgensen, W.L.' 6 ? 
primary 'Anderson, K.S.'  7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '3C-like proteinase nsp5' 33837.602 2   3.4.22.69 ? ? ? 
2 non-polymer syn 
;(1R,2S,5S)-N-{(1E,2S)-1-imino-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-6,6-dimethyl-3-[3-methyl-N-(trifluoroacetyl)-L-valyl]-3-azabicyclo[3.1.0]hexane-2-carboxamide
;
501.542   2   ?         ? ? ? 
3 water       nat water 18.015    213 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQIAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQIAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(1R,2S,5S)-N-{(1E,2S)-1-imino-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-6,6-dimethyl-3-[3-methyl-N-(trifluoroacetyl)-L-valyl]-3-azabicyclo[3.1.0]hexane-2-carboxamide
;
4WI 
3 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 ILE n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
4WI non-polymer         . 
;(1R,2S,5S)-N-{(1E,2S)-1-imino-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-6,6-dimethyl-3-[3-methyl-N-(trifluoroacetyl)-L-valyl]-3-azabicyclo[3.1.0]hexane-2-carboxamide
;
'PF-07321332, bound form; nirmatrelvir, bound form; Paxlovid, bound form' 'C23 H34 F3 N5 O4' 501.542 
ALA 'L-peptide linking' y ALANINE ?                                                                         'C3 H7 N O2'       
89.093  
ARG 'L-peptide linking' y ARGININE ?                                                                         'C6 H15 N4 O2 1'   
175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                                                                         'C4 H8 N2 O3'      
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                                                                         'C4 H7 N O4' 
133.103 
CYS 'L-peptide linking' y CYSTEINE ?                                                                         'C3 H7 N O2 S'     
121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                                                                         'C5 H10 N2 O3'     
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                                                                         'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE ?                                                                         'C2 H5 N O2'       
75.067  
HIS 'L-peptide linking' y HISTIDINE ?                                                                         'C6 H10 N3 O2 1'   
156.162 
HOH non-polymer         . WATER ?                                                                         'H2 O'             
18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                                                                         'C6 H13 N O2'      
131.173 
LEU 'L-peptide linking' y LEUCINE ?                                                                         'C6 H13 N O2'      
131.173 
LYS 'L-peptide linking' y LYSINE ?                                                                         'C6 H15 N2 O2 1'   
147.195 
MET 'L-peptide linking' y METHIONINE ?                                                                         'C5 H11 N O2 S'    
149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                                                                         'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE ?                                                                         'C5 H9 N O2'       
115.130 
SER 'L-peptide linking' y SERINE ?                                                                         'C3 H7 N O3'       
105.093 
THR 'L-peptide linking' y THREONINE ?                                                                         'C4 H9 N O3'       
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                                                                         'C11 H12 N2 O2'    
204.225 
TYR 'L-peptide linking' y TYROSINE ?                                                                         'C9 H11 N O3'      
181.189 
VAL 'L-peptide linking' y VALINE ?                                                                         'C5 H11 N O2'      
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 ?   ?   ?   A . n 
A 1 304 THR 304 304 ?   ?   ?   A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
B 1 1   SER 1   1   ?   ?   ?   B . n 
B 1 2   GLY 2   2   ?   ?   ?   B . n 
B 1 3   PHE 3   3   ?   ?   ?   B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  CYS 16  16  16  CYS CYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  CYS 44  44  44  CYS CYS B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 CYS 145 145 145 CYS CYS B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 ILE 190 190 190 ILE ILE B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 TRP 207 207 207 TRP TRP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLN 273 273 273 GLN GLN B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 ASN 277 277 277 ASN ASN B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 VAL 303 303 ?   ?   ?   B . n 
B 1 304 THR 304 304 ?   ?   ?   B . n 
B 1 305 PHE 305 305 ?   ?   ?   B . n 
B 1 306 GLN 306 306 ?   ?   ?   B . 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 4WI ? ? 4WI ? ? 'SUBJECT OF INVESTIGATION' ? 
2 4WI ? ? 4WI ? ? '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 
C 2 4WI 1   401 999 4WI NMB A . 
D 2 4WI 1   401 999 4WI NMA B . 
E 3 HOH 1   501 59  HOH HOH A . 
E 3 HOH 2   502 71  HOH HOH A . 
E 3 HOH 3   503 85  HOH HOH A . 
E 3 HOH 4   504 140 HOH HOH A . 
E 3 HOH 5   505 169 HOH HOH A . 
E 3 HOH 6   506 194 HOH HOH A . 
E 3 HOH 7   507 92  HOH HOH A . 
E 3 HOH 8   508 126 HOH HOH A . 
E 3 HOH 9   509 28  HOH HOH A . 
E 3 HOH 10  510 120 HOH HOH A . 
E 3 HOH 11  511 82  HOH HOH A . 
E 3 HOH 12  512 20  HOH HOH A . 
E 3 HOH 13  513 78  HOH HOH A . 
E 3 HOH 14  514 33  HOH HOH A . 
E 3 HOH 15  515 36  HOH HOH A . 
E 3 HOH 16  516 104 HOH HOH A . 
E 3 HOH 17  517 76  HOH HOH A . 
E 3 HOH 18  518 143 HOH HOH A . 
E 3 HOH 19  519 45  HOH HOH A . 
E 3 HOH 20  520 110 HOH HOH A . 
E 3 HOH 21  521 50  HOH HOH A . 
E 3 HOH 22  522 66  HOH HOH A . 
E 3 HOH 23  523 9   HOH HOH A . 
E 3 HOH 24  524 141 HOH HOH A . 
E 3 HOH 25  525 266 HOH HOH A . 
E 3 HOH 26  526 272 HOH HOH A . 
E 3 HOH 27  527 54  HOH HOH A . 
E 3 HOH 28  528 14  HOH HOH A . 
E 3 HOH 29  529 99  HOH HOH A . 
E 3 HOH 30  530 182 HOH HOH A . 
E 3 HOH 31  531 180 HOH HOH A . 
E 3 HOH 32  532 13  HOH HOH A . 
E 3 HOH 33  533 58  HOH HOH A . 
E 3 HOH 34  534 80  HOH HOH A . 
E 3 HOH 35  535 105 HOH HOH A . 
E 3 HOH 36  536 68  HOH HOH A . 
E 3 HOH 37  537 109 HOH HOH A . 
E 3 HOH 38  538 47  HOH HOH A . 
E 3 HOH 39  539 119 HOH HOH A . 
E 3 HOH 40  540 67  HOH HOH A . 
E 3 HOH 41  541 139 HOH HOH A . 
E 3 HOH 42  542 48  HOH HOH A . 
E 3 HOH 43  543 251 HOH HOH A . 
E 3 HOH 44  544 122 HOH HOH A . 
E 3 HOH 45  545 124 HOH HOH A . 
E 3 HOH 46  546 62  HOH HOH A . 
E 3 HOH 47  547 84  HOH HOH A . 
E 3 HOH 48  548 89  HOH HOH A . 
E 3 HOH 49  549 125 HOH HOH A . 
E 3 HOH 50  550 74  HOH HOH A . 
E 3 HOH 51  551 283 HOH HOH A . 
E 3 HOH 52  552 87  HOH HOH A . 
E 3 HOH 53  553 226 HOH HOH A . 
E 3 HOH 54  554 161 HOH HOH A . 
E 3 HOH 55  555 228 HOH HOH A . 
E 3 HOH 56  556 29  HOH HOH A . 
E 3 HOH 57  557 132 HOH HOH A . 
E 3 HOH 58  558 255 HOH HOH A . 
E 3 HOH 59  559 17  HOH HOH A . 
E 3 HOH 60  560 133 HOH HOH A . 
E 3 HOH 61  561 107 HOH HOH A . 
E 3 HOH 62  562 118 HOH HOH A . 
E 3 HOH 63  563 21  HOH HOH A . 
E 3 HOH 64  564 4   HOH HOH A . 
E 3 HOH 65  565 123 HOH HOH A . 
E 3 HOH 66  566 19  HOH HOH A . 
E 3 HOH 67  567 152 HOH HOH A . 
E 3 HOH 68  568 190 HOH HOH A . 
E 3 HOH 69  569 95  HOH HOH A . 
E 3 HOH 70  570 83  HOH HOH A . 
E 3 HOH 71  571 176 HOH HOH A . 
E 3 HOH 72  572 8   HOH HOH A . 
E 3 HOH 73  573 60  HOH HOH A . 
E 3 HOH 74  574 57  HOH HOH A . 
E 3 HOH 75  575 41  HOH HOH A . 
E 3 HOH 76  576 230 HOH HOH A . 
E 3 HOH 77  577 166 HOH HOH A . 
E 3 HOH 78  578 212 HOH HOH A . 
E 3 HOH 79  579 154 HOH HOH A . 
E 3 HOH 80  580 273 HOH HOH A . 
E 3 HOH 81  581 232 HOH HOH A . 
E 3 HOH 82  582 151 HOH HOH A . 
E 3 HOH 83  583 158 HOH HOH A . 
E 3 HOH 84  584 286 HOH HOH A . 
E 3 HOH 85  585 239 HOH HOH A . 
E 3 HOH 86  586 234 HOH HOH A . 
E 3 HOH 87  587 117 HOH HOH A . 
E 3 HOH 88  588 156 HOH HOH A . 
E 3 HOH 89  589 167 HOH HOH A . 
E 3 HOH 90  590 108 HOH HOH A . 
E 3 HOH 91  591 56  HOH HOH A . 
E 3 HOH 92  592 289 HOH HOH A . 
E 3 HOH 93  593 238 HOH HOH A . 
E 3 HOH 94  594 287 HOH HOH A . 
E 3 HOH 95  595 111 HOH HOH A . 
E 3 HOH 96  596 229 HOH HOH A . 
E 3 HOH 97  597 277 HOH HOH A . 
E 3 HOH 98  598 35  HOH HOH A . 
E 3 HOH 99  599 248 HOH HOH A . 
E 3 HOH 100 600 112 HOH HOH A . 
E 3 HOH 101 601 233 HOH HOH A . 
E 3 HOH 102 602 116 HOH HOH A . 
E 3 HOH 103 603 86  HOH HOH A . 
E 3 HOH 104 604 210 HOH HOH A . 
E 3 HOH 105 605 221 HOH HOH A . 
F 3 HOH 1   501 162 HOH HOH B . 
F 3 HOH 2   502 197 HOH HOH B . 
F 3 HOH 3   503 195 HOH HOH B . 
F 3 HOH 4   504 157 HOH HOH B . 
F 3 HOH 5   505 142 HOH HOH B . 
F 3 HOH 6   506 145 HOH HOH B . 
F 3 HOH 7   507 144 HOH HOH B . 
F 3 HOH 8   508 129 HOH HOH B . 
F 3 HOH 9   509 219 HOH HOH B . 
F 3 HOH 10  510 199 HOH HOH B . 
F 3 HOH 11  511 98  HOH HOH B . 
F 3 HOH 12  512 235 HOH HOH B . 
F 3 HOH 13  513 171 HOH HOH B . 
F 3 HOH 14  514 39  HOH HOH B . 
F 3 HOH 15  515 115 HOH HOH B . 
F 3 HOH 16  516 173 HOH HOH B . 
F 3 HOH 17  517 70  HOH HOH B . 
F 3 HOH 18  518 187 HOH HOH B . 
F 3 HOH 19  519 18  HOH HOH B . 
F 3 HOH 20  520 25  HOH HOH B . 
F 3 HOH 21  521 135 HOH HOH B . 
F 3 HOH 22  522 96  HOH HOH B . 
F 3 HOH 23  523 253 HOH HOH B . 
F 3 HOH 24  524 163 HOH HOH B . 
F 3 HOH 25  525 153 HOH HOH B . 
F 3 HOH 26  526 75  HOH HOH B . 
F 3 HOH 27  527 65  HOH HOH B . 
F 3 HOH 28  528 55  HOH HOH B . 
F 3 HOH 29  529 6   HOH HOH B . 
F 3 HOH 30  530 77  HOH HOH B . 
F 3 HOH 31  531 136 HOH HOH B . 
F 3 HOH 32  532 280 HOH HOH B . 
F 3 HOH 33  533 30  HOH HOH B . 
F 3 HOH 34  534 172 HOH HOH B . 
F 3 HOH 35  535 63  HOH HOH B . 
F 3 HOH 36  536 73  HOH HOH B . 
F 3 HOH 37  537 52  HOH HOH B . 
F 3 HOH 38  538 88  HOH HOH B . 
F 3 HOH 39  539 12  HOH HOH B . 
F 3 HOH 40  540 128 HOH HOH B . 
F 3 HOH 41  541 32  HOH HOH B . 
F 3 HOH 42  542 51  HOH HOH B . 
F 3 HOH 43  543 155 HOH HOH B . 
F 3 HOH 44  544 2   HOH HOH B . 
F 3 HOH 45  545 49  HOH HOH B . 
F 3 HOH 46  546 93  HOH HOH B . 
F 3 HOH 47  547 15  HOH HOH B . 
F 3 HOH 48  548 254 HOH HOH B . 
F 3 HOH 49  549 103 HOH HOH B . 
F 3 HOH 50  550 79  HOH HOH B . 
F 3 HOH 51  551 1   HOH HOH B . 
F 3 HOH 52  552 42  HOH HOH B . 
F 3 HOH 53  553 131 HOH HOH B . 
F 3 HOH 54  554 94  HOH HOH B . 
F 3 HOH 55  555 31  HOH HOH B . 
F 3 HOH 56  556 244 HOH HOH B . 
F 3 HOH 57  557 23  HOH HOH B . 
F 3 HOH 58  558 3   HOH HOH B . 
F 3 HOH 59  559 97  HOH HOH B . 
F 3 HOH 60  560 38  HOH HOH B . 
F 3 HOH 61  561 106 HOH HOH B . 
F 3 HOH 62  562 90  HOH HOH B . 
F 3 HOH 63  563 170 HOH HOH B . 
F 3 HOH 64  564 24  HOH HOH B . 
F 3 HOH 65  565 214 HOH HOH B . 
F 3 HOH 66  566 146 HOH HOH B . 
F 3 HOH 67  567 130 HOH HOH B . 
F 3 HOH 68  568 37  HOH HOH B . 
F 3 HOH 69  569 22  HOH HOH B . 
F 3 HOH 70  570 113 HOH HOH B . 
F 3 HOH 71  571 72  HOH HOH B . 
F 3 HOH 72  572 44  HOH HOH B . 
F 3 HOH 73  573 114 HOH HOH B . 
F 3 HOH 74  574 64  HOH HOH B . 
F 3 HOH 75  575 91  HOH HOH B . 
F 3 HOH 76  576 11  HOH HOH B . 
F 3 HOH 77  577 43  HOH HOH B . 
F 3 HOH 78  578 192 HOH HOH B . 
F 3 HOH 79  579 186 HOH HOH B . 
F 3 HOH 80  580 179 HOH HOH B . 
F 3 HOH 81  581 26  HOH HOH B . 
F 3 HOH 82  582 81  HOH HOH B . 
F 3 HOH 83  583 46  HOH HOH B . 
F 3 HOH 84  584 164 HOH HOH B . 
F 3 HOH 85  585 5   HOH HOH B . 
F 3 HOH 86  586 7   HOH HOH B . 
F 3 HOH 87  587 16  HOH HOH B . 
F 3 HOH 88  588 61  HOH HOH B . 
F 3 HOH 89  589 10  HOH HOH B . 
F 3 HOH 90  590 257 HOH HOH B . 
F 3 HOH 91  591 34  HOH HOH B . 
F 3 HOH 92  592 101 HOH HOH B . 
F 3 HOH 93  593 53  HOH HOH B . 
F 3 HOH 94  594 216 HOH HOH B . 
F 3 HOH 95  595 249 HOH HOH B . 
F 3 HOH 96  596 27  HOH HOH B . 
F 3 HOH 97  597 40  HOH HOH B . 
F 3 HOH 98  598 231 HOH HOH B . 
F 3 HOH 99  599 246 HOH HOH B . 
F 3 HOH 100 600 252 HOH HOH B . 
F 3 HOH 101 601 236 HOH HOH B . 
F 3 HOH 102 602 181 HOH HOH B . 
F 3 HOH 103 603 148 HOH HOH B . 
F 3 HOH 104 604 240 HOH HOH B . 
F 3 HOH 105 605 159 HOH HOH B . 
F 3 HOH 106 606 183 HOH HOH B . 
F 3 HOH 107 607 288 HOH HOH B . 
F 3 HOH 108 608 160 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 47  ? CG  ? A GLU 47  CG  
2  1 Y 1 A GLU 47  ? CD  ? A GLU 47  CD  
3  1 Y 1 A GLU 47  ? OE1 ? A GLU 47  OE1 
4  1 Y 1 A GLU 47  ? OE2 ? A GLU 47  OE2 
5  1 Y 1 A ASN 51  ? CG  ? A ASN 51  CG  
6  1 Y 1 A ASN 51  ? OD1 ? A ASN 51  OD1 
7  1 Y 1 A ASN 51  ? ND2 ? A ASN 51  ND2 
8  1 Y 1 A GLN 69  ? CG  ? A GLN 69  CG  
9  1 Y 1 A GLN 69  ? CD  ? A GLN 69  CD  
10 1 Y 1 A GLN 69  ? OE1 ? A GLN 69  OE1 
11 1 Y 1 A GLN 69  ? NE2 ? A GLN 69  NE2 
12 1 Y 1 A ASN 72  ? CG  ? A ASN 72  CG  
13 1 Y 1 A ASN 72  ? OD1 ? A ASN 72  OD1 
14 1 Y 1 A ASN 72  ? ND2 ? A ASN 72  ND2 
15 1 Y 1 A LYS 90  ? CG  ? A LYS 90  CG  
16 1 Y 1 A LYS 90  ? CD  ? A LYS 90  CD  
17 1 Y 1 A LYS 90  ? CE  ? A LYS 90  CE  
18 1 Y 1 A LYS 90  ? NZ  ? A LYS 90  NZ  
19 1 Y 1 A LYS 102 ? CG  ? A LYS 102 CG  
20 1 Y 1 A LYS 102 ? CD  ? A LYS 102 CD  
21 1 Y 1 A LYS 102 ? CE  ? A LYS 102 CE  
22 1 Y 1 A LYS 102 ? NZ  ? A LYS 102 NZ  
23 1 Y 1 A ASP 153 ? CG  ? A ASP 153 CG  
24 1 Y 1 A ASP 153 ? OD1 ? A ASP 153 OD1 
25 1 Y 1 A ASP 153 ? OD2 ? A ASP 153 OD2 
26 1 Y 1 A TYR 154 ? CG  ? A TYR 154 CG  
27 1 Y 1 A TYR 154 ? CD1 ? A TYR 154 CD1 
28 1 Y 1 A TYR 154 ? CD2 ? A TYR 154 CD2 
29 1 Y 1 A TYR 154 ? CE1 ? A TYR 154 CE1 
30 1 Y 1 A TYR 154 ? CE2 ? A TYR 154 CE2 
31 1 Y 1 A TYR 154 ? CZ  ? A TYR 154 CZ  
32 1 Y 1 A TYR 154 ? OH  ? A TYR 154 OH  
33 1 Y 1 A PHE 294 ? CG  ? A PHE 294 CG  
34 1 Y 1 A PHE 294 ? CD1 ? A PHE 294 CD1 
35 1 Y 1 A PHE 294 ? CD2 ? A PHE 294 CD2 
36 1 Y 1 A PHE 294 ? CE1 ? A PHE 294 CE1 
37 1 Y 1 A PHE 294 ? CE2 ? A PHE 294 CE2 
38 1 Y 1 A PHE 294 ? CZ  ? A PHE 294 CZ  
39 1 Y 1 B LYS 5   ? CG  ? B LYS 5   CG  
40 1 Y 1 B LYS 5   ? CD  ? B LYS 5   CD  
41 1 Y 1 B LYS 5   ? CE  ? B LYS 5   CE  
42 1 Y 1 B LYS 5   ? NZ  ? B LYS 5   NZ  
43 1 Y 1 B LEU 50  ? CG  ? B LEU 50  CG  
44 1 Y 1 B LEU 50  ? CD1 ? B LEU 50  CD1 
45 1 Y 1 B LEU 50  ? CD2 ? B LEU 50  CD2 
46 1 Y 1 B ILE 59  ? CG1 ? B ILE 59  CG1 
47 1 Y 1 B ILE 59  ? CG2 ? B ILE 59  CG2 
48 1 Y 1 B ILE 59  ? CD1 ? B ILE 59  CD1 
49 1 Y 1 B ARG 60  ? CG  ? B ARG 60  CG  
50 1 Y 1 B ARG 60  ? CD  ? B ARG 60  CD  
51 1 Y 1 B ARG 60  ? NE  ? B ARG 60  NE  
52 1 Y 1 B ARG 60  ? CZ  ? B ARG 60  CZ  
53 1 Y 1 B ARG 60  ? NH1 ? B ARG 60  NH1 
54 1 Y 1 B ARG 60  ? NH2 ? B ARG 60  NH2 
55 1 Y 1 B LYS 100 ? CG  ? B LYS 100 CG  
56 1 Y 1 B LYS 100 ? CD  ? B LYS 100 CD  
57 1 Y 1 B LYS 100 ? CE  ? B LYS 100 CE  
58 1 Y 1 B LYS 100 ? NZ  ? B LYS 100 NZ  
59 1 Y 1 B ASP 153 ? CG  ? B ASP 153 CG  
60 1 Y 1 B ASP 153 ? OD1 ? B ASP 153 OD1 
61 1 Y 1 B ASP 153 ? OD2 ? B ASP 153 OD2 
62 1 Y 1 B TYR 154 ? CG  ? B TYR 154 CG  
63 1 Y 1 B TYR 154 ? CD1 ? B TYR 154 CD1 
64 1 Y 1 B TYR 154 ? CD2 ? B TYR 154 CD2 
65 1 Y 1 B TYR 154 ? CE1 ? B TYR 154 CE1 
66 1 Y 1 B TYR 154 ? CE2 ? B TYR 154 CE2 
67 1 Y 1 B TYR 154 ? CZ  ? B TYR 154 CZ  
68 1 Y 1 B TYR 154 ? OH  ? B TYR 154 OH  
69 1 Y 1 B ARG 222 ? CG  ? B ARG 222 CG  
70 1 Y 1 B ARG 222 ? CD  ? B ARG 222 CD  
71 1 Y 1 B ARG 222 ? NE  ? B ARG 222 NE  
72 1 Y 1 B ARG 222 ? CZ  ? B ARG 222 CZ  
73 1 Y 1 B ARG 222 ? NH1 ? B ARG 222 NH1 
74 1 Y 1 B ARG 222 ? NH2 ? B ARG 222 NH2 
75 1 Y 1 B PHE 223 ? CG  ? B PHE 223 CG  
76 1 Y 1 B PHE 223 ? CD1 ? B PHE 223 CD1 
77 1 Y 1 B PHE 223 ? CD2 ? B PHE 223 CD2 
78 1 Y 1 B PHE 223 ? CE1 ? B PHE 223 CE1 
79 1 Y 1 B PHE 223 ? CE2 ? B PHE 223 CE2 
80 1 Y 1 B PHE 223 ? CZ  ? B PHE 223 CZ  
81 1 Y 1 B ASN 277 ? CG  ? B ASN 277 CG  
82 1 Y 1 B ASN 277 ? OD1 ? B ASN 277 OD1 
83 1 Y 1 B ASN 277 ? ND2 ? B ASN 277 ND2 
84 1 Y 1 B ARG 279 ? CG  ? B ARG 279 CG  
85 1 Y 1 B ARG 279 ? CD  ? B ARG 279 CD  
86 1 Y 1 B ARG 279 ? NE  ? B ARG 279 NE  
87 1 Y 1 B ARG 279 ? CZ  ? B ARG 279 CZ  
88 1 Y 1 B ARG 279 ? NH1 ? B ARG 279 NH1 
89 1 Y 1 B ARG 279 ? NH2 ? B ARG 279 NH2 
90 1 Y 1 B GLN 299 ? CG  ? B GLN 299 CG  
91 1 Y 1 B GLN 299 ? CD  ? B GLN 299 CD  
92 1 Y 1 B GLN 299 ? OE1 ? B GLN 299 OE1 
93 1 Y 1 B GLN 299 ? NE2 ? B GLN 299 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   107.896 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BO5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.664 
_cell.length_a_esd                 ? 
_cell.length_b                     98.671 
_cell.length_b_esd                 ? 
_cell.length_c                     59.244 
_cell.length_c_esd                 ? 
_cell.volume                       309649.217 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9BO5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BO5 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.24 
_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              9.0 
_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    '10% v/v Polyethylene glycol 200, 0.1 M BIS-TRIS propane, 18% w/v Polyethylene glycol 8,000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-01-27 
_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   0.920037 
_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-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.920037 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          27.51 
_reflns.entry_id                                       9BO5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.84 
_reflns.d_resolution_low                               36.10 
_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                                     52710 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.42 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.68 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1395 
_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                                    1.84 
_reflns_shell.d_res_low                                     1.906 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.05 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5109 
_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                               6.5 
_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                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.386 
_reflns_shell.pdbx_CC_star                                  0.747 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.11 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               31.12 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BO5 
_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                            1.84 
_refine.ls_d_res_low                             36.10 
_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                     52666 
_refine.ls_number_reflns_R_free                  2500 
_refine.ls_number_reflns_R_work                  50166 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.42 
_refine.ls_percent_reflns_R_free                 4.75 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1948 
_refine.ls_R_factor_R_free                       0.2224 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1934 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 25.5832 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2417 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.84 
_refine_hist.d_res_low                        36.10 
_refine_hist.number_atoms_solvent             213 
_refine_hist.number_atoms_total               4837 
_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        4554 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         70 
_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' ? 0.0066  ? 4748 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8853  ? 6486 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0536  ? 740  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0064  ? 836  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.2011 ? 1667 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.84 1.87  . . 146 2684 96.55 . . . . 0.2874 . . . . . . . . . . . 0.3502 
'X-RAY DIFFRACTION' 1.87 1.91  . . 117 2774 97.73 . . . . 0.2735 . . . . . . . . . . . 0.3200 
'X-RAY DIFFRACTION' 1.91 1.95  . . 137 2706 98.78 . . . . 0.2568 . . . . . . . . . . . 0.2827 
'X-RAY DIFFRACTION' 1.95 2.00  . . 128 2820 99.53 . . . . 0.2380 . . . . . . . . . . . 0.2678 
'X-RAY DIFFRACTION' 2.00 2.05  . . 140 2800 99.83 . . . . 0.2337 . . . . . . . . . . . 0.2900 
'X-RAY DIFFRACTION' 2.05 2.10  . . 132 2788 99.93 . . . . 0.2206 . . . . . . . . . . . 0.2508 
'X-RAY DIFFRACTION' 2.10 2.17  . . 135 2787 99.97 . . . . 0.2156 . . . . . . . . . . . 0.2659 
'X-RAY DIFFRACTION' 2.17 2.24  . . 133 2796 99.93 . . . . 0.2154 . . . . . . . . . . . 0.2564 
'X-RAY DIFFRACTION' 2.24 2.32  . . 137 2808 99.83 . . . . 0.2056 . . . . . . . . . . . 0.2439 
'X-RAY DIFFRACTION' 2.32 2.41  . . 124 2790 99.79 . . . . 0.2097 . . . . . . . . . . . 0.2517 
'X-RAY DIFFRACTION' 2.41 2.52  . . 145 2805 99.73 . . . . 0.2110 . . . . . . . . . . . 0.2464 
'X-RAY DIFFRACTION' 2.52 2.65  . . 158 2780 99.63 . . . . 0.1954 . . . . . . . . . . . 0.2668 
'X-RAY DIFFRACTION' 2.65 2.82  . . 146 2779 99.63 . . . . 0.2070 . . . . . . . . . . . 0.2424 
'X-RAY DIFFRACTION' 2.82 3.03  . . 141 2773 99.76 . . . . 0.1987 . . . . . . . . . . . 0.2068 
'X-RAY DIFFRACTION' 3.03 3.34  . . 107 2836 99.86 . . . . 0.1932 . . . . . . . . . . . 0.1944 
'X-RAY DIFFRACTION' 3.34 3.82  . . 180 2770 99.73 . . . . 0.1736 . . . . . . . . . . . 0.2018 
'X-RAY DIFFRACTION' 3.82 4.81  . . 177 2783 99.83 . . . . 0.1530 . . . . . . . . . . . 0.1713 
'X-RAY DIFFRACTION' 4.81 36.10 . . 117 2887 99.77 . . . . 0.1746 . . . . . . . . . . . 0.2160 
# 
_struct.entry_id                     9BO5 
_struct.title                        'Crystal Structure of T190I SARS-CoV-2 Main Protease in Complex with Nirmatrelvir' 
_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        9BO5 
_struct_keywords.text            'Hydrolase, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9BO5 A 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
2 1 9BO5 B 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
# 
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 9BO5 ILE A 190 ? UNP P0DTD1 THR 3453 conflict 190 1 
2 9BO5 ILE B 190 ? UNP P0DTD1 THR 3453 conflict 190 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2250  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  25130 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 THR A 45  ? ASN A 51  ? THR A 45  ASN A 51  1 ? 7  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? PHE A 66  ? SER A 62  PHE A 66  5 ? 5  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
HELX_P HELX_P12 AB3 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P13 AB4 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P14 AB5 THR B 45  ? ASN B 51  ? THR B 45  ASN B 51  1 ? 7  
HELX_P HELX_P15 AB6 ASN B 53  ? LYS B 61  ? ASN B 53  LYS B 61  1 ? 9  
HELX_P HELX_P16 AB7 SER B 62  ? PHE B 66  ? SER B 62  PHE B 66  5 ? 5  
HELX_P HELX_P17 AB8 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P18 AB9 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P19 AC1 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P20 AC2 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P21 AC3 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P22 AC4 THR B 292 ? GLY B 302 ? THR B 292 GLY B 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale none ? A CYS 145 SG ? ? ? 1_555 C 4WI . C3 ? ? A CYS 145 A 4WI 401 1_555 ? ? ? ? ? ? ? 1.766 ? ? 
covale2 covale none ? B CYS 145 SG ? ? ? 1_555 D 4WI . C3 ? ? B CYS 145 B 4WI 401 1_555 ? ? ? ? ? ? ? 1.768 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 4WI C . ? CYS A 145 ? 4WI A 401 ? 1_555 CYS A 145 ? 1_555 C3 SG CYS 1 4WI None 'Covalent chemical modification' 
2 4WI D . ? CYS B 145 ? 4WI B 401 ? 1_555 CYS B 145 ? 1_555 C3 SG CYS 1 4WI None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 LEU A 67  ? ALA A 70  ? LEU A 67  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA4 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA4 2 LEU B 67  ? ALA B 70  ? LEU B 67  ALA B 70  
AA4 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA4 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA5 1 LYS B 100 ? PHE B 103 ? LYS B 100 PHE B 103 
AA5 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA5 3 VAL B 148 ? ASP B 153 ? VAL B 148 ASP B 153 
AA5 4 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA5 5 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA6 1 LYS B 100 ? PHE B 103 ? LYS B 100 PHE B 103 
AA6 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA6 3 HIS B 172 ? THR B 175 ? HIS B 172 THR B 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O GLN A 69  ? O GLN A 69  N GLN A 19  ? N GLN A 19  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
AA4 1 2 O LEU B 75  ? O LEU B 75  N VAL B 68  ? N VAL B 68  
AA4 2 3 O GLN B 69  ? O GLN B 69  N GLN B 19  ? N GLN B 19  
AA4 3 4 N CYS B 22  ? N CYS B 22  O THR B 25  ? O THR B 25  
AA4 4 5 N LEU B 30  ? N LEU B 30  O TYR B 37  ? O TYR B 37  
AA4 5 6 N CYS B 38  ? N CYS B 38  O LEU B 87  ? O LEU B 87  
AA4 6 7 O LYS B 90  ? O LYS B 90  N ILE B 78  ? N ILE B 78  
AA5 1 2 N LYS B 100 ? N LYS B 100 O VAL B 157 ? O VAL B 157 
AA5 2 3 O SER B 158 ? O SER B 158 N ASN B 151 ? N ASN B 151 
AA5 3 4 O PHE B 150 ? O PHE B 150 N SER B 113 ? N SER B 113 
AA5 4 5 N ALA B 116 ? N ALA B 116 O SER B 123 ? O SER B 123 
AA6 1 2 N LYS B 100 ? N LYS B 100 O VAL B 157 ? O VAL B 157 
AA6 2 3 N MET B 165 ? N MET B 165 O ALA B 173 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   9BO5 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 ASP A 33  ? ? 55.75   -128.01 
2  1 HIS A 41  ? ? -68.58  4.62    
3  1 ASN A 51  ? ? -166.31 82.61   
4  1 ASN A 84  ? ? 55.81   -124.04 
5  1 TYR A 154 ? ? 62.00   -105.77 
6  1 PRO A 184 ? ? -85.99  40.54   
7  1 ASP B 33  ? ? 50.64   -125.03 
8  1 ASN B 51  ? ? -165.91 68.63   
9  1 ASN B 84  ? ? 53.07   -118.68 
10 1 TYR B 154 ? ? 67.73   -114.82 
11 1 PRO B 184 ? ? -91.34  41.70   
12 1 ARG B 217 ? ? -144.67 26.26   
13 1 ASN B 277 ? ? -66.40  80.83   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
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 VAL 303 ? A VAL 303 
2  1 Y 1 A THR 304 ? A THR 304 
3  1 Y 1 A PHE 305 ? A PHE 305 
4  1 Y 1 A GLN 306 ? A GLN 306 
5  1 Y 1 B SER 1   ? B SER 1   
6  1 Y 1 B GLY 2   ? B GLY 2   
7  1 Y 1 B PHE 3   ? B PHE 3   
8  1 Y 1 B VAL 303 ? B VAL 303 
9  1 Y 1 B THR 304 ? B THR 304 
10 1 Y 1 B PHE 305 ? B PHE 305 
11 1 Y 1 B GLN 306 ? B GLN 306 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
4WI C8   C N N 1   
4WI C3   C N N 2   
4WI C1   C N N 3   
4WI C13  C N N 4   
4WI C21  C N N 5   
4WI C6   C N N 6   
4WI C7   C N N 7   
4WI C10  C N N 8   
4WI C5   C N S 9   
4WI C9   C N S 10  
4WI C11  C N S 11  
4WI C12  C N R 12  
4WI C18  C N N 13  
4WI C19  C N N 14  
4WI C20  C N N 15  
4WI C16  C N N 16  
4WI C17  C N N 17  
4WI C23  C N N 18  
4WI C4   C N N 19  
4WI C2   C N S 20  
4WI C14  C N S 21  
4WI C22  C N N 22  
4WI C15  C N N 23  
4WI N5   N N N 24  
4WI N2   N N N 25  
4WI N3   N N N 26  
4WI N1   N N N 27  
4WI N4   N N N 28  
4WI O1   O N N 29  
4WI O2   O N N 30  
4WI O3   O N N 31  
4WI O4   O N N 32  
4WI F1   F N N 33  
4WI F2   F N N 34  
4WI F3   F N N 35  
4WI H33  H N N 36  
4WI H5   H N N 37  
4WI H6   H N N 38  
4WI H7   H N N 39  
4WI H8   H N N 40  
4WI H11  H N N 41  
4WI H12  H N N 42  
4WI H4   H N N 43  
4WI H10  H N N 44  
4WI H13  H N N 45  
4WI H14  H N N 46  
4WI H23  H N N 47  
4WI H24  H N N 48  
4WI H25  H N N 49  
4WI H26  H N N 50  
4WI H27  H N N 51  
4WI H28  H N N 52  
4WI H17  H N N 53  
4WI H19  H N N 54  
4WI H18  H N N 55  
4WI H20  H N N 56  
4WI H21  H N N 57  
4WI H22  H N N 58  
4WI H29  H N N 59  
4WI H30  H N N 60  
4WI H31  H N N 61  
4WI H2   H N N 62  
4WI H3   H N N 63  
4WI H32  H N N 64  
4WI H15  H N N 65  
4WI H36  H N N 66  
4WI H9   H N N 67  
4WI H1   H N N 68  
4WI H16  H N N 69  
ALA N    N N N 70  
ALA CA   C N S 71  
ALA C    C N N 72  
ALA O    O N N 73  
ALA CB   C N N 74  
ALA OXT  O N N 75  
ALA H    H N N 76  
ALA H2   H N N 77  
ALA HA   H N N 78  
ALA HB1  H N N 79  
ALA HB2  H N N 80  
ALA HB3  H N N 81  
ALA HXT  H N N 82  
ARG N    N N N 83  
ARG CA   C N S 84  
ARG C    C N N 85  
ARG O    O N N 86  
ARG CB   C N N 87  
ARG CG   C N N 88  
ARG CD   C N N 89  
ARG NE   N N N 90  
ARG CZ   C N N 91  
ARG NH1  N N N 92  
ARG NH2  N N N 93  
ARG OXT  O N N 94  
ARG H    H N N 95  
ARG H2   H N N 96  
ARG HA   H N N 97  
ARG HB2  H N N 98  
ARG HB3  H N N 99  
ARG HG2  H N N 100 
ARG HG3  H N N 101 
ARG HD2  H N N 102 
ARG HD3  H N N 103 
ARG HE   H N N 104 
ARG HH11 H N N 105 
ARG HH12 H N N 106 
ARG HH21 H N N 107 
ARG HH22 H N N 108 
ARG HXT  H N N 109 
ASN N    N N N 110 
ASN CA   C N S 111 
ASN C    C N N 112 
ASN O    O N N 113 
ASN CB   C N N 114 
ASN CG   C N N 115 
ASN OD1  O N N 116 
ASN ND2  N N N 117 
ASN OXT  O N N 118 
ASN H    H N N 119 
ASN H2   H N N 120 
ASN HA   H N N 121 
ASN HB2  H N N 122 
ASN HB3  H N N 123 
ASN HD21 H N N 124 
ASN HD22 H N N 125 
ASN HXT  H N N 126 
ASP N    N N N 127 
ASP CA   C N S 128 
ASP C    C N N 129 
ASP O    O N N 130 
ASP CB   C N N 131 
ASP CG   C N N 132 
ASP OD1  O N N 133 
ASP OD2  O N N 134 
ASP OXT  O N N 135 
ASP H    H N N 136 
ASP H2   H N N 137 
ASP HA   H N N 138 
ASP HB2  H N N 139 
ASP HB3  H N N 140 
ASP HD2  H N N 141 
ASP HXT  H N N 142 
CYS N    N N N 143 
CYS CA   C N R 144 
CYS C    C N N 145 
CYS O    O N N 146 
CYS CB   C N N 147 
CYS SG   S N N 148 
CYS OXT  O N N 149 
CYS H    H N N 150 
CYS H2   H N N 151 
CYS HA   H N N 152 
CYS HB2  H N N 153 
CYS HB3  H N N 154 
CYS HG   H N N 155 
CYS HXT  H N N 156 
GLN N    N N N 157 
GLN CA   C N S 158 
GLN C    C N N 159 
GLN O    O N N 160 
GLN CB   C N N 161 
GLN CG   C N N 162 
GLN CD   C N N 163 
GLN OE1  O N N 164 
GLN NE2  N N N 165 
GLN OXT  O N N 166 
GLN H    H N N 167 
GLN H2   H N N 168 
GLN HA   H N N 169 
GLN HB2  H N N 170 
GLN HB3  H N N 171 
GLN HG2  H N N 172 
GLN HG3  H N N 173 
GLN HE21 H N N 174 
GLN HE22 H N N 175 
GLN HXT  H N N 176 
GLU N    N N N 177 
GLU CA   C N S 178 
GLU C    C N N 179 
GLU O    O N N 180 
GLU CB   C N N 181 
GLU CG   C N N 182 
GLU CD   C N N 183 
GLU OE1  O N N 184 
GLU OE2  O N N 185 
GLU OXT  O N N 186 
GLU H    H N N 187 
GLU H2   H N N 188 
GLU HA   H N N 189 
GLU HB2  H N N 190 
GLU HB3  H N N 191 
GLU HG2  H N N 192 
GLU HG3  H N N 193 
GLU HE2  H N N 194 
GLU HXT  H N N 195 
GLY N    N N N 196 
GLY CA   C N N 197 
GLY C    C N N 198 
GLY O    O N N 199 
GLY OXT  O N N 200 
GLY H    H N N 201 
GLY H2   H N N 202 
GLY HA2  H N N 203 
GLY HA3  H N N 204 
GLY HXT  H N N 205 
HIS N    N N N 206 
HIS CA   C N S 207 
HIS C    C N N 208 
HIS O    O N N 209 
HIS CB   C N N 210 
HIS CG   C Y N 211 
HIS ND1  N Y N 212 
HIS CD2  C Y N 213 
HIS CE1  C Y N 214 
HIS NE2  N Y N 215 
HIS OXT  O N N 216 
HIS H    H N N 217 
HIS H2   H N N 218 
HIS HA   H N N 219 
HIS HB2  H N N 220 
HIS HB3  H N N 221 
HIS HD1  H N N 222 
HIS HD2  H N N 223 
HIS HE1  H N N 224 
HIS HE2  H N N 225 
HIS HXT  H N N 226 
HOH O    O N N 227 
HOH H1   H N N 228 
HOH H2   H N N 229 
ILE N    N N N 230 
ILE CA   C N S 231 
ILE C    C N N 232 
ILE O    O N N 233 
ILE CB   C N S 234 
ILE CG1  C N N 235 
ILE CG2  C N N 236 
ILE CD1  C N N 237 
ILE OXT  O N N 238 
ILE H    H N N 239 
ILE H2   H N N 240 
ILE HA   H N N 241 
ILE HB   H N N 242 
ILE HG12 H N N 243 
ILE HG13 H N N 244 
ILE HG21 H N N 245 
ILE HG22 H N N 246 
ILE HG23 H N N 247 
ILE HD11 H N N 248 
ILE HD12 H N N 249 
ILE HD13 H N N 250 
ILE HXT  H N N 251 
LEU N    N N N 252 
LEU CA   C N S 253 
LEU C    C N N 254 
LEU O    O N N 255 
LEU CB   C N N 256 
LEU CG   C N N 257 
LEU CD1  C N N 258 
LEU CD2  C N N 259 
LEU OXT  O N N 260 
LEU H    H N N 261 
LEU H2   H N N 262 
LEU HA   H N N 263 
LEU HB2  H N N 264 
LEU HB3  H N N 265 
LEU HG   H N N 266 
LEU HD11 H N N 267 
LEU HD12 H N N 268 
LEU HD13 H N N 269 
LEU HD21 H N N 270 
LEU HD22 H N N 271 
LEU HD23 H N N 272 
LEU HXT  H N N 273 
LYS N    N N N 274 
LYS CA   C N S 275 
LYS C    C N N 276 
LYS O    O N N 277 
LYS CB   C N N 278 
LYS CG   C N N 279 
LYS CD   C N N 280 
LYS CE   C N N 281 
LYS NZ   N N N 282 
LYS OXT  O N N 283 
LYS H    H N N 284 
LYS H2   H N N 285 
LYS HA   H N N 286 
LYS HB2  H N N 287 
LYS HB3  H N N 288 
LYS HG2  H N N 289 
LYS HG3  H N N 290 
LYS HD2  H N N 291 
LYS HD3  H N N 292 
LYS HE2  H N N 293 
LYS HE3  H N N 294 
LYS HZ1  H N N 295 
LYS HZ2  H N N 296 
LYS HZ3  H N N 297 
LYS HXT  H N N 298 
MET N    N N N 299 
MET CA   C N S 300 
MET C    C N N 301 
MET O    O N N 302 
MET CB   C N N 303 
MET CG   C N N 304 
MET SD   S N N 305 
MET CE   C N N 306 
MET OXT  O N N 307 
MET H    H N N 308 
MET H2   H N N 309 
MET HA   H N N 310 
MET HB2  H N N 311 
MET HB3  H N N 312 
MET HG2  H N N 313 
MET HG3  H N N 314 
MET HE1  H N N 315 
MET HE2  H N N 316 
MET HE3  H N N 317 
MET HXT  H N N 318 
PHE N    N N N 319 
PHE CA   C N S 320 
PHE C    C N N 321 
PHE O    O N N 322 
PHE CB   C N N 323 
PHE CG   C Y N 324 
PHE CD1  C Y N 325 
PHE CD2  C Y N 326 
PHE CE1  C Y N 327 
PHE CE2  C Y N 328 
PHE CZ   C Y N 329 
PHE OXT  O N N 330 
PHE H    H N N 331 
PHE H2   H N N 332 
PHE HA   H N N 333 
PHE HB2  H N N 334 
PHE HB3  H N N 335 
PHE HD1  H N N 336 
PHE HD2  H N N 337 
PHE HE1  H N N 338 
PHE HE2  H N N 339 
PHE HZ   H N N 340 
PHE HXT  H N N 341 
PRO N    N N N 342 
PRO CA   C N S 343 
PRO C    C N N 344 
PRO O    O N N 345 
PRO CB   C N N 346 
PRO CG   C N N 347 
PRO CD   C N N 348 
PRO OXT  O N N 349 
PRO H    H N N 350 
PRO HA   H N N 351 
PRO HB2  H N N 352 
PRO HB3  H N N 353 
PRO HG2  H N N 354 
PRO HG3  H N N 355 
PRO HD2  H N N 356 
PRO HD3  H N N 357 
PRO HXT  H N N 358 
SER N    N N N 359 
SER CA   C N S 360 
SER C    C N N 361 
SER O    O N N 362 
SER CB   C N N 363 
SER OG   O N N 364 
SER OXT  O N N 365 
SER H    H N N 366 
SER H2   H N N 367 
SER HA   H N N 368 
SER HB2  H N N 369 
SER HB3  H N N 370 
SER HG   H N N 371 
SER HXT  H N N 372 
THR N    N N N 373 
THR CA   C N S 374 
THR C    C N N 375 
THR O    O N N 376 
THR CB   C N R 377 
THR OG1  O N N 378 
THR CG2  C N N 379 
THR OXT  O N N 380 
THR H    H N N 381 
THR H2   H N N 382 
THR HA   H N N 383 
THR HB   H N N 384 
THR HG1  H N N 385 
THR HG21 H N N 386 
THR HG22 H N N 387 
THR HG23 H N N 388 
THR HXT  H N N 389 
TRP N    N N N 390 
TRP CA   C N S 391 
TRP C    C N N 392 
TRP O    O N N 393 
TRP CB   C N N 394 
TRP CG   C Y N 395 
TRP CD1  C Y N 396 
TRP CD2  C Y N 397 
TRP NE1  N Y N 398 
TRP CE2  C Y N 399 
TRP CE3  C Y N 400 
TRP CZ2  C Y N 401 
TRP CZ3  C Y N 402 
TRP CH2  C Y N 403 
TRP OXT  O N N 404 
TRP H    H N N 405 
TRP H2   H N N 406 
TRP HA   H N N 407 
TRP HB2  H N N 408 
TRP HB3  H N N 409 
TRP HD1  H N N 410 
TRP HE1  H N N 411 
TRP HE3  H N N 412 
TRP HZ2  H N N 413 
TRP HZ3  H N N 414 
TRP HH2  H N N 415 
TRP HXT  H N N 416 
TYR N    N N N 417 
TYR CA   C N S 418 
TYR C    C N N 419 
TYR O    O N N 420 
TYR CB   C N N 421 
TYR CG   C Y N 422 
TYR CD1  C Y N 423 
TYR CD2  C Y N 424 
TYR CE1  C Y N 425 
TYR CE2  C Y N 426 
TYR CZ   C Y N 427 
TYR OH   O N N 428 
TYR OXT  O N N 429 
TYR H    H N N 430 
TYR H2   H N N 431 
TYR HA   H N N 432 
TYR HB2  H N N 433 
TYR HB3  H N N 434 
TYR HD1  H N N 435 
TYR HD2  H N N 436 
TYR HE1  H N N 437 
TYR HE2  H N N 438 
TYR HH   H N N 439 
TYR HXT  H N N 440 
VAL N    N N N 441 
VAL CA   C N S 442 
VAL C    C N N 443 
VAL O    O N N 444 
VAL CB   C N N 445 
VAL CG1  C N N 446 
VAL CG2  C N N 447 
VAL OXT  O N N 448 
VAL H    H N N 449 
VAL H2   H N N 450 
VAL HA   H N N 451 
VAL HB   H N N 452 
VAL HG11 H N N 453 
VAL HG12 H N N 454 
VAL HG13 H N N 455 
VAL HG21 H N N 456 
VAL HG22 H N N 457 
VAL HG23 H N N 458 
VAL HXT  H N N 459 
# 
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 
4WI O1  C8   doub N N 1   
4WI C8  N2   sing N N 2   
4WI C8  C5   sing N N 3   
4WI N2  C7   sing N N 4   
4WI C4  C5   sing N N 5   
4WI C4  C2   sing N N 6   
4WI C5  C6   sing N N 7   
4WI N5  C3   doub N N 8   
4WI C3  C2   sing N N 9   
4WI C7  C6   sing N N 10  
4WI C2  N1   sing N N 11  
4WI N1  C1   sing N N 12  
4WI F1  C22  sing N N 13  
4WI O3  C13  doub N N 14  
4WI C1  C9   sing N N 15  
4WI C1  O2   doub N N 16  
4WI F3  C22  sing N N 17  
4WI C23 C15  sing N N 18  
4WI C22 F2   sing N N 19  
4WI C22 C21  sing N N 20  
4WI C9  N3   sing N N 21  
4WI C9  C12  sing N N 22  
4WI C13 N3   sing N N 23  
4WI C13 C14  sing N N 24  
4WI N4  C21  sing N N 25  
4WI N4  C14  sing N N 26  
4WI C19 C18  sing N N 27  
4WI N3  C10  sing N N 28  
4WI C21 O4   doub N N 29  
4WI C12 C18  sing N N 30  
4WI C12 C11  sing N N 31  
4WI C14 C15  sing N N 32  
4WI C15 C17  sing N N 33  
4WI C15 C16  sing N N 34  
4WI C18 C20  sing N N 35  
4WI C18 C11  sing N N 36  
4WI C10 C11  sing N N 37  
4WI C3  H33  sing N N 38  
4WI C6  H5   sing N N 39  
4WI C6  H6   sing N N 40  
4WI C7  H7   sing N N 41  
4WI C7  H8   sing N N 42  
4WI C10 H11  sing N N 43  
4WI C10 H12  sing N N 44  
4WI C5  H4   sing N N 45  
4WI C9  H10  sing N N 46  
4WI C11 H13  sing N N 47  
4WI C12 H14  sing N N 48  
4WI C19 H23  sing N N 49  
4WI C19 H24  sing N N 50  
4WI C19 H25  sing N N 51  
4WI C20 H26  sing N N 52  
4WI C20 H27  sing N N 53  
4WI C20 H28  sing N N 54  
4WI C16 H17  sing N N 55  
4WI C16 H19  sing N N 56  
4WI C16 H18  sing N N 57  
4WI C17 H20  sing N N 58  
4WI C17 H21  sing N N 59  
4WI C17 H22  sing N N 60  
4WI C23 H29  sing N N 61  
4WI C23 H30  sing N N 62  
4WI C23 H31  sing N N 63  
4WI C4  H2   sing N N 64  
4WI C4  H3   sing N N 65  
4WI C2  H32  sing N N 66  
4WI C14 H15  sing N N 67  
4WI N5  H36  sing N N 68  
4WI N2  H9   sing N N 69  
4WI N1  H1   sing N N 70  
4WI N4  H16  sing N N 71  
ALA N   CA   sing N N 72  
ALA N   H    sing N N 73  
ALA N   H2   sing N N 74  
ALA CA  C    sing N N 75  
ALA CA  CB   sing N N 76  
ALA CA  HA   sing N N 77  
ALA C   O    doub N N 78  
ALA C   OXT  sing N N 79  
ALA CB  HB1  sing N N 80  
ALA CB  HB2  sing N N 81  
ALA CB  HB3  sing N N 82  
ALA OXT HXT  sing N N 83  
ARG N   CA   sing N N 84  
ARG N   H    sing N N 85  
ARG N   H2   sing N N 86  
ARG CA  C    sing N N 87  
ARG CA  CB   sing N N 88  
ARG CA  HA   sing N N 89  
ARG C   O    doub N N 90  
ARG C   OXT  sing N N 91  
ARG CB  CG   sing N N 92  
ARG CB  HB2  sing N N 93  
ARG CB  HB3  sing N N 94  
ARG CG  CD   sing N N 95  
ARG CG  HG2  sing N N 96  
ARG CG  HG3  sing N N 97  
ARG CD  NE   sing N N 98  
ARG CD  HD2  sing N N 99  
ARG CD  HD3  sing N N 100 
ARG NE  CZ   sing N N 101 
ARG NE  HE   sing N N 102 
ARG CZ  NH1  sing N N 103 
ARG CZ  NH2  doub N N 104 
ARG NH1 HH11 sing N N 105 
ARG NH1 HH12 sing N N 106 
ARG NH2 HH21 sing N N 107 
ARG NH2 HH22 sing N N 108 
ARG OXT HXT  sing N N 109 
ASN N   CA   sing N N 110 
ASN N   H    sing N N 111 
ASN N   H2   sing N N 112 
ASN CA  C    sing N N 113 
ASN CA  CB   sing N N 114 
ASN CA  HA   sing N N 115 
ASN C   O    doub N N 116 
ASN C   OXT  sing N N 117 
ASN CB  CG   sing N N 118 
ASN CB  HB2  sing N N 119 
ASN CB  HB3  sing N N 120 
ASN CG  OD1  doub N N 121 
ASN CG  ND2  sing N N 122 
ASN ND2 HD21 sing N N 123 
ASN ND2 HD22 sing N N 124 
ASN OXT HXT  sing N N 125 
ASP N   CA   sing N N 126 
ASP N   H    sing N N 127 
ASP N   H2   sing N N 128 
ASP CA  C    sing N N 129 
ASP CA  CB   sing N N 130 
ASP CA  HA   sing N N 131 
ASP C   O    doub N N 132 
ASP C   OXT  sing N N 133 
ASP CB  CG   sing N N 134 
ASP CB  HB2  sing N N 135 
ASP CB  HB3  sing N N 136 
ASP CG  OD1  doub N N 137 
ASP CG  OD2  sing N N 138 
ASP OD2 HD2  sing N N 139 
ASP OXT HXT  sing N N 140 
CYS N   CA   sing N N 141 
CYS N   H    sing N N 142 
CYS N   H2   sing N N 143 
CYS CA  C    sing N N 144 
CYS CA  CB   sing N N 145 
CYS CA  HA   sing N N 146 
CYS C   O    doub N N 147 
CYS C   OXT  sing N N 148 
CYS CB  SG   sing N N 149 
CYS CB  HB2  sing N N 150 
CYS CB  HB3  sing N N 151 
CYS SG  HG   sing N N 152 
CYS OXT HXT  sing N N 153 
GLN N   CA   sing N N 154 
GLN N   H    sing N N 155 
GLN N   H2   sing N N 156 
GLN CA  C    sing N N 157 
GLN CA  CB   sing N N 158 
GLN CA  HA   sing N N 159 
GLN C   O    doub N N 160 
GLN C   OXT  sing N N 161 
GLN CB  CG   sing N N 162 
GLN CB  HB2  sing N N 163 
GLN CB  HB3  sing N N 164 
GLN CG  CD   sing N N 165 
GLN CG  HG2  sing N N 166 
GLN CG  HG3  sing N N 167 
GLN CD  OE1  doub N N 168 
GLN CD  NE2  sing N N 169 
GLN NE2 HE21 sing N N 170 
GLN NE2 HE22 sing N N 171 
GLN OXT HXT  sing N N 172 
GLU N   CA   sing N N 173 
GLU N   H    sing N N 174 
GLU N   H2   sing N N 175 
GLU CA  C    sing N N 176 
GLU CA  CB   sing N N 177 
GLU CA  HA   sing N N 178 
GLU C   O    doub N N 179 
GLU C   OXT  sing N N 180 
GLU CB  CG   sing N N 181 
GLU CB  HB2  sing N N 182 
GLU CB  HB3  sing N N 183 
GLU CG  CD   sing N N 184 
GLU CG  HG2  sing N N 185 
GLU CG  HG3  sing N N 186 
GLU CD  OE1  doub N N 187 
GLU CD  OE2  sing N N 188 
GLU OE2 HE2  sing N N 189 
GLU OXT HXT  sing N N 190 
GLY N   CA   sing N N 191 
GLY N   H    sing N N 192 
GLY N   H2   sing N N 193 
GLY CA  C    sing N N 194 
GLY CA  HA2  sing N N 195 
GLY CA  HA3  sing N N 196 
GLY C   O    doub N N 197 
GLY C   OXT  sing N N 198 
GLY OXT HXT  sing N N 199 
HIS N   CA   sing N N 200 
HIS N   H    sing N N 201 
HIS N   H2   sing N N 202 
HIS CA  C    sing N N 203 
HIS CA  CB   sing N N 204 
HIS CA  HA   sing N N 205 
HIS C   O    doub N N 206 
HIS C   OXT  sing N N 207 
HIS CB  CG   sing N N 208 
HIS CB  HB2  sing N N 209 
HIS CB  HB3  sing N N 210 
HIS CG  ND1  sing Y N 211 
HIS CG  CD2  doub Y N 212 
HIS ND1 CE1  doub Y N 213 
HIS ND1 HD1  sing N N 214 
HIS CD2 NE2  sing Y N 215 
HIS CD2 HD2  sing N N 216 
HIS CE1 NE2  sing Y N 217 
HIS CE1 HE1  sing N N 218 
HIS NE2 HE2  sing N N 219 
HIS OXT HXT  sing N N 220 
HOH O   H1   sing N N 221 
HOH O   H2   sing N N 222 
ILE N   CA   sing N N 223 
ILE N   H    sing N N 224 
ILE N   H2   sing N N 225 
ILE CA  C    sing N N 226 
ILE CA  CB   sing N N 227 
ILE CA  HA   sing N N 228 
ILE C   O    doub N N 229 
ILE C   OXT  sing N N 230 
ILE CB  CG1  sing N N 231 
ILE CB  CG2  sing N N 232 
ILE CB  HB   sing N N 233 
ILE CG1 CD1  sing N N 234 
ILE CG1 HG12 sing N N 235 
ILE CG1 HG13 sing N N 236 
ILE CG2 HG21 sing N N 237 
ILE CG2 HG22 sing N N 238 
ILE CG2 HG23 sing N N 239 
ILE CD1 HD11 sing N N 240 
ILE CD1 HD12 sing N N 241 
ILE CD1 HD13 sing N N 242 
ILE OXT HXT  sing N N 243 
LEU N   CA   sing N N 244 
LEU N   H    sing N N 245 
LEU N   H2   sing N N 246 
LEU CA  C    sing N N 247 
LEU CA  CB   sing N N 248 
LEU CA  HA   sing N N 249 
LEU C   O    doub N N 250 
LEU C   OXT  sing N N 251 
LEU CB  CG   sing N N 252 
LEU CB  HB2  sing N N 253 
LEU CB  HB3  sing N N 254 
LEU CG  CD1  sing N N 255 
LEU CG  CD2  sing N N 256 
LEU CG  HG   sing N N 257 
LEU CD1 HD11 sing N N 258 
LEU CD1 HD12 sing N N 259 
LEU CD1 HD13 sing N N 260 
LEU CD2 HD21 sing N N 261 
LEU CD2 HD22 sing N N 262 
LEU CD2 HD23 sing N N 263 
LEU OXT HXT  sing N N 264 
LYS N   CA   sing N N 265 
LYS N   H    sing N N 266 
LYS N   H2   sing N N 267 
LYS CA  C    sing N N 268 
LYS CA  CB   sing N N 269 
LYS CA  HA   sing N N 270 
LYS C   O    doub N N 271 
LYS C   OXT  sing N N 272 
LYS CB  CG   sing N N 273 
LYS CB  HB2  sing N N 274 
LYS CB  HB3  sing N N 275 
LYS CG  CD   sing N N 276 
LYS CG  HG2  sing N N 277 
LYS CG  HG3  sing N N 278 
LYS CD  CE   sing N N 279 
LYS CD  HD2  sing N N 280 
LYS CD  HD3  sing N N 281 
LYS CE  NZ   sing N N 282 
LYS CE  HE2  sing N N 283 
LYS CE  HE3  sing N N 284 
LYS NZ  HZ1  sing N N 285 
LYS NZ  HZ2  sing N N 286 
LYS NZ  HZ3  sing N N 287 
LYS OXT HXT  sing N N 288 
MET N   CA   sing N N 289 
MET N   H    sing N N 290 
MET N   H2   sing N N 291 
MET CA  C    sing N N 292 
MET CA  CB   sing N N 293 
MET CA  HA   sing N N 294 
MET C   O    doub N N 295 
MET C   OXT  sing N N 296 
MET CB  CG   sing N N 297 
MET CB  HB2  sing N N 298 
MET CB  HB3  sing N N 299 
MET CG  SD   sing N N 300 
MET CG  HG2  sing N N 301 
MET CG  HG3  sing N N 302 
MET SD  CE   sing N N 303 
MET CE  HE1  sing N N 304 
MET CE  HE2  sing N N 305 
MET CE  HE3  sing N N 306 
MET OXT HXT  sing N N 307 
PHE N   CA   sing N N 308 
PHE N   H    sing N N 309 
PHE N   H2   sing N N 310 
PHE CA  C    sing N N 311 
PHE CA  CB   sing N N 312 
PHE CA  HA   sing N N 313 
PHE C   O    doub N N 314 
PHE C   OXT  sing N N 315 
PHE CB  CG   sing N N 316 
PHE CB  HB2  sing N N 317 
PHE CB  HB3  sing N N 318 
PHE CG  CD1  doub Y N 319 
PHE CG  CD2  sing Y N 320 
PHE CD1 CE1  sing Y N 321 
PHE CD1 HD1  sing N N 322 
PHE CD2 CE2  doub Y N 323 
PHE CD2 HD2  sing N N 324 
PHE CE1 CZ   doub Y N 325 
PHE CE1 HE1  sing N N 326 
PHE CE2 CZ   sing Y N 327 
PHE CE2 HE2  sing N N 328 
PHE CZ  HZ   sing N N 329 
PHE OXT HXT  sing N N 330 
PRO N   CA   sing N N 331 
PRO N   CD   sing N N 332 
PRO N   H    sing N N 333 
PRO CA  C    sing N N 334 
PRO CA  CB   sing N N 335 
PRO CA  HA   sing N N 336 
PRO C   O    doub N N 337 
PRO C   OXT  sing N N 338 
PRO CB  CG   sing N N 339 
PRO CB  HB2  sing N N 340 
PRO CB  HB3  sing N N 341 
PRO CG  CD   sing N N 342 
PRO CG  HG2  sing N N 343 
PRO CG  HG3  sing N N 344 
PRO CD  HD2  sing N N 345 
PRO CD  HD3  sing N N 346 
PRO OXT HXT  sing N N 347 
SER N   CA   sing N N 348 
SER N   H    sing N N 349 
SER N   H2   sing N N 350 
SER CA  C    sing N N 351 
SER CA  CB   sing N N 352 
SER CA  HA   sing N N 353 
SER C   O    doub N N 354 
SER C   OXT  sing N N 355 
SER CB  OG   sing N N 356 
SER CB  HB2  sing N N 357 
SER CB  HB3  sing N N 358 
SER OG  HG   sing N N 359 
SER OXT HXT  sing N N 360 
THR N   CA   sing N N 361 
THR N   H    sing N N 362 
THR N   H2   sing N N 363 
THR CA  C    sing N N 364 
THR CA  CB   sing N N 365 
THR CA  HA   sing N N 366 
THR C   O    doub N N 367 
THR C   OXT  sing N N 368 
THR CB  OG1  sing N N 369 
THR CB  CG2  sing N N 370 
THR CB  HB   sing N N 371 
THR OG1 HG1  sing N N 372 
THR CG2 HG21 sing N N 373 
THR CG2 HG22 sing N N 374 
THR CG2 HG23 sing N N 375 
THR OXT HXT  sing N N 376 
TRP N   CA   sing N N 377 
TRP N   H    sing N N 378 
TRP N   H2   sing N N 379 
TRP CA  C    sing N N 380 
TRP CA  CB   sing N N 381 
TRP CA  HA   sing N N 382 
TRP C   O    doub N N 383 
TRP C   OXT  sing N N 384 
TRP CB  CG   sing N N 385 
TRP CB  HB2  sing N N 386 
TRP CB  HB3  sing N N 387 
TRP CG  CD1  doub Y N 388 
TRP CG  CD2  sing Y N 389 
TRP CD1 NE1  sing Y N 390 
TRP CD1 HD1  sing N N 391 
TRP CD2 CE2  doub Y N 392 
TRP CD2 CE3  sing Y N 393 
TRP NE1 CE2  sing Y N 394 
TRP NE1 HE1  sing N N 395 
TRP CE2 CZ2  sing Y N 396 
TRP CE3 CZ3  doub Y N 397 
TRP CE3 HE3  sing N N 398 
TRP CZ2 CH2  doub Y N 399 
TRP CZ2 HZ2  sing N N 400 
TRP CZ3 CH2  sing Y N 401 
TRP CZ3 HZ3  sing N N 402 
TRP CH2 HH2  sing N N 403 
TRP OXT HXT  sing N N 404 
TYR N   CA   sing N N 405 
TYR N   H    sing N N 406 
TYR N   H2   sing N N 407 
TYR CA  C    sing N N 408 
TYR CA  CB   sing N N 409 
TYR CA  HA   sing N N 410 
TYR C   O    doub N N 411 
TYR C   OXT  sing N N 412 
TYR CB  CG   sing N N 413 
TYR CB  HB2  sing N N 414 
TYR CB  HB3  sing N N 415 
TYR CG  CD1  doub Y N 416 
TYR CG  CD2  sing Y N 417 
TYR CD1 CE1  sing Y N 418 
TYR CD1 HD1  sing N N 419 
TYR CD2 CE2  doub Y N 420 
TYR CD2 HD2  sing N N 421 
TYR CE1 CZ   doub Y N 422 
TYR CE1 HE1  sing N N 423 
TYR CE2 CZ   sing Y N 424 
TYR CE2 HE2  sing N N 425 
TYR CZ  OH   sing N N 426 
TYR OH  HH   sing N N 427 
TYR OXT HXT  sing N N 428 
VAL N   CA   sing N N 429 
VAL N   H    sing N N 430 
VAL N   H2   sing N N 431 
VAL CA  C    sing N N 432 
VAL CA  CB   sing N N 433 
VAL CA  HA   sing N N 434 
VAL C   O    doub N N 435 
VAL C   OXT  sing N N 436 
VAL CB  CG1  sing N N 437 
VAL CB  CG2  sing N N 438 
VAL CB  HB   sing N N 439 
VAL CG1 HG11 sing N N 440 
VAL CG1 HG12 sing N N 441 
VAL CG1 HG13 sing N N 442 
VAL CG2 HG21 sing N N 443 
VAL CG2 HG22 sing N N 444 
VAL CG2 HG23 sing N N 445 
VAL OXT HXT  sing N N 446 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 'P30 GM133893' 1 
'Department of Energy (DOE, United States)'                                                'United States' KP1607011      2 
'Other government'                                                                         ?               DE-SC0012704   3 
# 
_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   7U29 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BO5 
_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]   0.017965 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005801 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010135 
_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]   0.017738 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 1   ? 3.45846   2.77009   26.96026  1.000 24.27012 ? 1   SER A N   1 
ATOM   2    C CA  . SER A 1 1   ? 2.95331   4.07912   27.35201  1.000 30.29760 ? 1   SER A CA  1 
ATOM   3    C C   . SER A 1 1   ? 3.13549   5.08130   26.21022  1.000 30.55577 ? 1   SER A C   1 
ATOM   4    O O   . SER A 1 1   ? 3.46649   4.69518   25.08758  1.000 28.57348 ? 1   SER A O   1 
ATOM   5    C CB  . SER A 1 1   ? 3.64542   4.56159   28.63711  1.000 31.43854 ? 1   SER A CB  1 
ATOM   6    O OG  . SER A 1 1   ? 4.98526   4.95066   28.39599  1.000 36.12143 ? 1   SER A OG  1 
ATOM   7    N N   . GLY A 1 2   ? 2.93390   6.35994   26.50723  1.000 25.16351 ? 2   GLY A N   1 
ATOM   8    C CA  . GLY A 1 2   ? 2.76721   7.39405   25.50746  1.000 26.89084 ? 2   GLY A CA  1 
ATOM   9    C C   . GLY A 1 2   ? 1.29613   7.68225   25.25451  1.000 27.18621 ? 2   GLY A C   1 
ATOM   10   O O   . GLY A 1 2   ? 0.41208   6.90196   25.60122  1.000 26.75393 ? 2   GLY A O   1 
ATOM   11   N N   . PHE A 1 3   ? 1.01988   8.83658   24.64241  1.000 23.30981 ? 3   PHE A N   1 
ATOM   12   C CA  . PHE A 1 3   ? -0.36868  9.20245   24.37314  1.000 29.25093 ? 3   PHE A CA  1 
ATOM   13   C C   . PHE A 1 3   ? -0.45953  10.04614  23.11382  1.000 29.08914 ? 3   PHE A C   1 
ATOM   14   O O   . PHE A 1 3   ? 0.08486   11.15289  23.06449  1.000 30.09975 ? 3   PHE A O   1 
ATOM   15   C CB  . PHE A 1 3   ? -0.98992  9.95666   25.54011  1.000 29.97055 ? 3   PHE A CB  1 
ATOM   16   C CG  . PHE A 1 3   ? -2.48688  9.98253   25.49066  1.000 30.14063 ? 3   PHE A CG  1 
ATOM   17   C CD1 . PHE A 1 3   ? -3.21205  8.86014   25.83611  1.000 26.54252 ? 3   PHE A CD1 1 
ATOM   18   C CD2 . PHE A 1 3   ? -3.16468  11.12955  25.10470  1.000 27.10439 ? 3   PHE A CD2 1 
ATOM   19   C CE1 . PHE A 1 3   ? -4.59712  8.87155   25.78644  1.000 30.95852 ? 3   PHE A CE1 1 
ATOM   20   C CE2 . PHE A 1 3   ? -4.54345  11.14338  25.06634  1.000 31.95115 ? 3   PHE A CE2 1 
ATOM   21   C CZ  . PHE A 1 3   ? -5.25252  10.01491  25.39501  1.000 28.05594 ? 3   PHE A CZ  1 
ATOM   22   N N   . ARG A 1 4   ? -1.18140  9.54068   22.12096  1.000 27.05731 ? 4   ARG A N   1 
ATOM   23   C CA  . ARG A 1 4   ? -1.30938  10.19897  20.82827  1.000 26.93495 ? 4   ARG A CA  1 
ATOM   24   C C   . ARG A 1 4   ? -2.78164  10.30487  20.45891  1.000 25.44651 ? 4   ARG A C   1 
ATOM   25   O O   . ARG A 1 4   ? -3.57508  9.43642   20.80963  1.000 23.13514 ? 4   ARG A O   1 
ATOM   26   C CB  . ARG A 1 4   ? -0.55804  9.41323   19.74997  1.000 24.13688 ? 4   ARG A CB  1 
ATOM   27   C CG  . ARG A 1 4   ? 0.95368   9.67028   19.72968  1.000 23.45285 ? 4   ARG A CG  1 
ATOM   28   C CD  . ARG A 1 4   ? 1.24284   11.05469  19.15888  1.000 28.09909 ? 4   ARG A CD  1 
ATOM   29   N NE  . ARG A 1 4   ? 2.67310   11.29964  19.00412  1.000 27.05768 ? 4   ARG A NE  1 
ATOM   30   C CZ  . ARG A 1 4   ? 3.19648   12.38334  18.44658  1.000 28.76379 ? 4   ARG A CZ  1 
ATOM   31   N NH1 . ARG A 1 4   ? 2.43304   13.34641  17.94266  1.000 29.90188 ? 4   ARG A NH1 1 
ATOM   32   N NH2 . ARG A 1 4   ? 4.51786   12.50839  18.39395  1.000 27.44708 ? 4   ARG A NH2 1 
ATOM   33   N N   . LYS A 1 5   ? -3.14833  11.37467  19.75426  1.000 28.54096 ? 5   LYS A N   1 
ATOM   34   C CA  . LYS A 1 5   ? -4.44393  11.37632  19.07884  1.000 26.72250 ? 5   LYS A CA  1 
ATOM   35   C C   . LYS A 1 5   ? -4.44175  10.26702  18.03437  1.000 27.73907 ? 5   LYS A C   1 
ATOM   36   O O   . LYS A 1 5   ? -3.65144  10.28788  17.08777  1.000 38.02790 ? 5   LYS A O   1 
ATOM   37   C CB  . LYS A 1 5   ? -4.71580  12.73733  18.43929  1.000 29.85108 ? 5   LYS A CB  1 
ATOM   38   C CG  . LYS A 1 5   ? -6.21677  13.16665  18.37794  1.000 36.47161 ? 5   LYS A CG  1 
ATOM   39   C CD  . LYS A 1 5   ? -6.35961  14.71795  18.51996  1.000 46.92777 ? 5   LYS A CD  1 
ATOM   40   C CE  . LYS A 1 5   ? -7.74575  15.20293  19.00850  1.000 45.63034 ? 5   LYS A CE  1 
ATOM   41   N NZ  . LYS A 1 5   ? -8.79221  15.46416  17.91815  1.000 38.55728 ? 5   LYS A NZ  1 
ATOM   42   N N   . MET A 1 6   ? -5.28962  9.27286   18.22955  1.000 27.08010 ? 6   MET A N   1 
ATOM   43   C CA  . MET A 1 6   ? -5.22676  8.04703   17.44924  1.000 27.09449 ? 6   MET A CA  1 
ATOM   44   C C   . MET A 1 6   ? -6.54001  7.82501   16.71497  1.000 26.23163 ? 6   MET A C   1 
ATOM   45   O O   . MET A 1 6   ? -7.61374  7.91630   17.32179  1.000 24.20950 ? 6   MET A O   1 
ATOM   46   C CB  . MET A 1 6   ? -4.91800  6.86364   18.37610  1.000 27.08788 ? 6   MET A CB  1 
ATOM   47   C CG  . MET A 1 6   ? -4.37090  5.63766   17.67729  1.000 34.22527 ? 6   MET A CG  1 
ATOM   48   S SD  . MET A 1 6   ? -3.87259  4.43002   18.91677  1.000 47.94221 ? 6   MET A SD  1 
ATOM   49   C CE  . MET A 1 6   ? -2.50592  5.27529   19.68302  1.000 36.49704 ? 6   MET A CE  1 
ATOM   50   N N   . ALA A 1 7   ? -6.45759  7.51959   15.41613  1.000 25.24842 ? 7   ALA A N   1 
ATOM   51   C CA  . ALA A 1 7   ? -7.62705  7.13221   14.64670  1.000 19.64328 ? 7   ALA A CA  1 
ATOM   52   C C   . ALA A 1 7   ? -7.68127  5.61915   14.48595  1.000 25.17679 ? 7   ALA A C   1 
ATOM   53   O O   . ALA A 1 7   ? -6.69316  4.91338   14.69707  1.000 22.97317 ? 7   ALA A O   1 
ATOM   54   C CB  . ALA A 1 7   ? -7.62362  7.80527   13.26513  1.000 25.26971 ? 7   ALA A CB  1 
ATOM   55   N N   . PHE A 1 8   ? -8.86469  5.12526   14.12271  1.000 25.45342 ? 8   PHE A N   1 
ATOM   56   C CA  . PHE A 1 8   ? -9.00538  3.73393   13.73446  1.000 22.73995 ? 8   PHE A CA  1 
ATOM   57   C C   . PHE A 1 8   ? -8.28833  3.47643   12.41223  1.000 21.60732 ? 8   PHE A C   1 
ATOM   58   O O   . PHE A 1 8   ? -8.24737  4.35066   11.53704  1.000 21.87560 ? 8   PHE A O   1 
ATOM   59   C CB  . PHE A 1 8   ? -10.48114 3.35191   13.59886  1.000 27.18037 ? 8   PHE A CB  1 
ATOM   60   C CG  . PHE A 1 8   ? -11.18724 3.21181   14.92928  1.000 26.71712 ? 8   PHE A CG  1 
ATOM   61   C CD1 . PHE A 1 8   ? -11.00845 2.06999   15.70386  1.000 28.86402 ? 8   PHE A CD1 1 
ATOM   62   C CD2 . PHE A 1 8   ? -11.98629 4.23789   15.42207  1.000 30.99672 ? 8   PHE A CD2 1 
ATOM   63   C CE1 . PHE A 1 8   ? -11.63354 1.94060   16.93584  1.000 26.96970 ? 8   PHE A CE1 1 
ATOM   64   C CE2 . PHE A 1 8   ? -12.61847 4.11374   16.66367  1.000 28.02877 ? 8   PHE A CE2 1 
ATOM   65   C CZ  . PHE A 1 8   ? -12.44268 2.96136   17.40648  1.000 29.42554 ? 8   PHE A CZ  1 
ATOM   66   N N   . PRO A 1 9   ? -7.72535  2.28152   12.23512  1.000 23.86813 ? 9   PRO A N   1 
ATOM   67   C CA  . PRO A 1 9   ? -7.19295  1.91445   10.91815  1.000 24.81938 ? 9   PRO A CA  1 
ATOM   68   C C   . PRO A 1 9   ? -8.27801  2.07671   9.86827   1.000 23.56993 ? 9   PRO A C   1 
ATOM   69   O O   . PRO A 1 9   ? -9.43574  1.69932   10.08287  1.000 24.27882 ? 9   PRO A O   1 
ATOM   70   C CB  . PRO A 1 9   ? -6.78519  0.44198   11.09340  1.000 25.36842 ? 9   PRO A CB  1 
ATOM   71   C CG  . PRO A 1 9   ? -6.59973  0.28225   12.59249  1.000 23.97252 ? 9   PRO A CG  1 
ATOM   72   C CD  . PRO A 1 9   ? -7.68613  1.14882   13.17842  1.000 22.81562 ? 9   PRO A CD  1 
ATOM   73   N N   . SER A 1 10  ? -7.90033  2.65937   8.73098   1.000 23.42336 ? 10  SER A N   1 
ATOM   74   C CA  . SER A 1 10  ? -8.86849  3.11897   7.74829   1.000 21.63764 ? 10  SER A CA  1 
ATOM   75   C C   . SER A 1 10  ? -9.08674  2.15206   6.59738   1.000 24.27739 ? 10  SER A C   1 
ATOM   76   O O   . SER A 1 10  ? -9.89330  2.46098   5.71181   1.000 23.95184 ? 10  SER A O   1 
ATOM   77   C CB  . SER A 1 10  ? -8.43517  4.46952   7.17205   1.000 20.50388 ? 10  SER A CB  1 
ATOM   78   O OG  . SER A 1 10  ? -7.11718  4.37543   6.65426   1.000 23.73714 ? 10  SER A OG  1 
ATOM   79   N N   . GLY A 1 11  ? -8.39243  1.00949   6.58921   1.000 21.50559 ? 11  GLY A N   1 
ATOM   80   C CA  . GLY A 1 11  ? -8.44994  0.10223   5.44791   1.000 20.83229 ? 11  GLY A CA  1 
ATOM   81   C C   . GLY A 1 11  ? -9.85820  -0.32212  5.07236   1.000 26.61448 ? 11  GLY A C   1 
ATOM   82   O O   . GLY A 1 11  ? -10.22451 -0.33814  3.89265   1.000 24.00785 ? 11  GLY A O   1 
ATOM   83   N N   . LYS A 1 12  ? -10.65555 -0.72486  6.06123   1.000 23.50603 ? 12  LYS A N   1 
ATOM   84   C CA  . LYS A 1 12  ? -11.99505 -1.20204  5.73085   1.000 24.31548 ? 12  LYS A CA  1 
ATOM   85   C C   . LYS A 1 12  ? -12.83001 -0.12065  5.05381   1.000 23.84568 ? 12  LYS A C   1 
ATOM   86   O O   . LYS A 1 12  ? -13.70703 -0.44642  4.25547   1.000 22.71787 ? 12  LYS A O   1 
ATOM   87   C CB  . LYS A 1 12  ? -12.70518 -1.72890  6.97872   1.000 26.24818 ? 12  LYS A CB  1 
ATOM   88   C CG  . LYS A 1 12  ? -12.07848 -3.00729  7.55335   1.000 28.54798 ? 12  LYS A CG  1 
ATOM   89   C CD  . LYS A 1 12  ? -12.82663 -3.48639  8.77460   1.000 31.93447 ? 12  LYS A CD  1 
ATOM   90   C CE  . LYS A 1 12  ? -12.46048 -4.93159  9.08371   1.000 36.34769 ? 12  LYS A CE  1 
ATOM   91   N NZ  . LYS A 1 12  ? -10.97387 -5.09272  9.24341   1.000 44.70166 ? 12  LYS A NZ  1 
ATOM   92   N N   . VAL A 1 13  ? -12.58854 1.16307   5.35580   1.000 23.16246 ? 13  VAL A N   1 
ATOM   93   C CA  . VAL A 1 13  ? -13.35108 2.22984   4.69199   1.000 22.63358 ? 13  VAL A CA  1 
ATOM   94   C C   . VAL A 1 13  ? -12.74324 2.58403   3.33715   1.000 21.26011 ? 13  VAL A C   1 
ATOM   95   O O   . VAL A 1 13  ? -13.46280 2.90318   2.38041   1.000 24.61239 ? 13  VAL A O   1 
ATOM   96   C CB  . VAL A 1 13  ? -13.44385 3.47571   5.60089   1.000 24.33734 ? 13  VAL A CB  1 
ATOM   97   C CG1 . VAL A 1 13  ? -14.31163 4.54929   4.93861   1.000 23.90144 ? 13  VAL A CG1 1 
ATOM   98   C CG2 . VAL A 1 13  ? -13.99103 3.10148   6.98951   1.000 23.37215 ? 13  VAL A CG2 1 
ATOM   99   N N   . GLU A 1 14  ? -11.41196 2.56538   3.22950   1.000 21.37524 ? 14  GLU A N   1 
ATOM   100  C CA  . GLU A 1 14  ? -10.77727 2.83981   1.94231   1.000 18.95235 ? 14  GLU A CA  1 
ATOM   101  C C   . GLU A 1 14  ? -11.35623 1.95149   0.84040   1.000 23.32796 ? 14  GLU A C   1 
ATOM   102  O O   . GLU A 1 14  ? -11.54558 2.39482   -0.30272  1.000 25.80113 ? 14  GLU A O   1 
ATOM   103  C CB  . GLU A 1 14  ? -9.25700  2.63424   2.05594   1.000 21.37716 ? 14  GLU A CB  1 
ATOM   104  C CG  . GLU A 1 14  ? -8.57401  3.58521   3.00455   1.000 24.39464 ? 14  GLU A CG  1 
ATOM   105  C CD  . GLU A 1 14  ? -7.12452  3.21298   3.28757   1.000 25.16089 ? 14  GLU A CD  1 
ATOM   106  O OE1 . GLU A 1 14  ? -6.36938  2.90614   2.34595   1.000 24.78738 ? 14  GLU A OE1 1 
ATOM   107  O OE2 . GLU A 1 14  ? -6.75964  3.20542   4.46613   1.000 24.14106 ? 14  GLU A OE2 1 
ATOM   108  N N   . GLY A 1 15  ? -11.63742 0.68872   1.15955   1.000 25.09528 ? 15  GLY A N   1 
ATOM   109  C CA  . GLY A 1 15  ? -12.17930 -0.22314  0.16307   1.000 27.79363 ? 15  GLY A CA  1 
ATOM   110  C C   . GLY A 1 15  ? -13.57938 0.10573   -0.31961  1.000 29.79303 ? 15  GLY A C   1 
ATOM   111  O O   . GLY A 1 15  ? -14.08455 -0.58562  -1.21170  1.000 28.26108 ? 15  GLY A O   1 
ATOM   112  N N   . CYS A 1 16  ? -14.22416 1.12669   0.24751   1.000 24.73358 ? 16  CYS A N   1 
ATOM   113  C CA  . CYS A 1 16  ? -15.59166 1.48779   -0.11601  1.000 24.52119 ? 16  CYS A CA  1 
ATOM   114  C C   . CYS A 1 16  ? -15.67790 2.81232   -0.85228  1.000 25.34358 ? 16  CYS A C   1 
ATOM   115  O O   . CYS A 1 16  ? -16.77814 3.20291   -1.27604  1.000 26.06094 ? 16  CYS A O   1 
ATOM   116  C CB  . CYS A 1 16  ? -16.47396 1.57444   1.12984   1.000 23.60179 ? 16  CYS A CB  1 
ATOM   117  S SG  . CYS A 1 16  ? -16.55766 0.07387   2.08831   1.000 30.57102 ? 16  CYS A SG  1 
ATOM   118  N N   . MET A 1 17  ? -14.56550 3.52525   -0.99700  1.000 26.07771 ? 17  MET A N   1 
ATOM   119  C CA  . MET A 1 17  ? -14.61192 4.88388   -1.52725  1.000 23.50149 ? 17  MET A CA  1 
ATOM   120  C C   . MET A 1 17  ? -14.60958 4.85447   -3.04684  1.000 27.44849 ? 17  MET A C   1 
ATOM   121  O O   . MET A 1 17  ? -13.87858 4.07236   -3.66638  1.000 24.98733 ? 17  MET A O   1 
ATOM   122  C CB  . MET A 1 17  ? -13.43002 5.71765   -1.02760  1.000 24.04254 ? 17  MET A CB  1 
ATOM   123  C CG  . MET A 1 17  ? -13.39871 5.97730   0.49130   1.000 23.21355 ? 17  MET A CG  1 
ATOM   124  S SD  . MET A 1 17  ? -14.98435 6.43740   1.23786   1.000 26.69318 ? 17  MET A SD  1 
ATOM   125  C CE  . MET A 1 17  ? -15.32694 8.02629   0.48689   1.000 26.54812 ? 17  MET A CE  1 
ATOM   126  N N   . VAL A 1 18  ? -15.45329 5.69404   -3.64843  1.000 22.95374 ? 18  VAL A N   1 
ATOM   127  C CA  . VAL A 1 18  ? -15.52616 5.83657   -5.10158  1.000 21.57964 ? 18  VAL A CA  1 
ATOM   128  C C   . VAL A 1 18  ? -15.77439 7.29965   -5.43268  1.000 23.58646 ? 18  VAL A C   1 
ATOM   129  O O   . VAL A 1 18  ? -15.93922 8.14811   -4.55192  1.000 23.69983 ? 18  VAL A O   1 
ATOM   130  C CB  . VAL A 1 18  ? -16.61696 4.94521   -5.73871  1.000 20.86276 ? 18  VAL A CB  1 
ATOM   131  C CG1 . VAL A 1 18  ? -16.39425 3.47830   -5.34882  1.000 21.68901 ? 18  VAL A CG1 1 
ATOM   132  C CG2 . VAL A 1 18  ? -18.01711 5.40645   -5.30108  1.000 23.92856 ? 18  VAL A CG2 1 
ATOM   133  N N   . GLN A 1 19  ? -15.74931 7.59664   -6.72205  1.000 25.50113 ? 19  GLN A N   1 
ATOM   134  C CA  . GLN A 1 19  ? -15.95932 8.93900   -7.23235  1.000 28.86081 ? 19  GLN A CA  1 
ATOM   135  C C   . GLN A 1 19  ? -17.33503 9.00421   -7.87516  1.000 27.43768 ? 19  GLN A C   1 
ATOM   136  O O   . GLN A 1 19  ? -17.75976 8.04837   -8.53243  1.000 28.24460 ? 19  GLN A O   1 
ATOM   137  C CB  . GLN A 1 19  ? -14.88110 9.30371   -8.25903  1.000 36.23946 ? 19  GLN A CB  1 
ATOM   138  C CG  . GLN A 1 19  ? -14.87116 10.75922  -8.70749  1.000 37.05117 ? 19  GLN A CG  1 
ATOM   139  C CD  . GLN A 1 19  ? -13.73118 11.03526  -9.67137  1.000 40.32421 ? 19  GLN A CD  1 
ATOM   140  O OE1 . GLN A 1 19  ? -13.24307 10.12690  -10.33415 1.000 48.37267 ? 19  GLN A OE1 1 
ATOM   141  N NE2 . GLN A 1 19  ? -13.29496 12.28450  -9.74171  1.000 42.25551 ? 19  GLN A NE2 1 
ATOM   142  N N   . VAL A 1 20  ? -18.02475 10.13112  -7.68626  1.000 28.08942 ? 20  VAL A N   1 
ATOM   143  C CA  . VAL A 1 20  ? -19.35128 10.37250  -8.26342  1.000 23.97125 ? 20  VAL A CA  1 
ATOM   144  C C   . VAL A 1 20  ? -19.34638 11.72073  -8.96250  1.000 28.43119 ? 20  VAL A C   1 
ATOM   145  O O   . VAL A 1 20  ? -19.04496 12.74075  -8.33335  1.000 30.19674 ? 20  VAL A O   1 
ATOM   146  C CB  . VAL A 1 20  ? -20.45308 10.36342  -7.18804  1.000 26.26988 ? 20  VAL A CB  1 
ATOM   147  C CG1 . VAL A 1 20  ? -21.80458 10.65407  -7.82328  1.000 25.07273 ? 20  VAL A CG1 1 
ATOM   148  C CG2 . VAL A 1 20  ? -20.45997 9.04577   -6.44091  1.000 31.95418 ? 20  VAL A CG2 1 
ATOM   149  N N   . THR A 1 21  ? -19.74425 11.74601  -10.24199 1.000 27.57287 ? 21  THR A N   1 
ATOM   150  C CA  . THR A 1 21  ? -19.75374 12.99091  -11.00214 1.000 28.31285 ? 21  THR A CA  1 
ATOM   151  C C   . THR A 1 21  ? -21.11694 13.25047  -11.63412 1.000 32.88104 ? 21  THR A C   1 
ATOM   152  O O   . THR A 1 21  ? -21.74383 12.33959  -12.18271 1.000 27.71828 ? 21  THR A O   1 
ATOM   153  C CB  . THR A 1 21  ? -18.69497 12.98487  -12.10832 1.000 34.39276 ? 21  THR A CB  1 
ATOM   154  O OG1 . THR A 1 21  ? -17.40334 12.77635  -11.53077 1.000 33.50572 ? 21  THR A OG1 1 
ATOM   155  C CG2 . THR A 1 21  ? -18.70000 14.31163  -12.84232 1.000 35.41350 ? 21  THR A CG2 1 
ATOM   156  N N   . CYS A 1 22  ? -21.56258 14.50364  -11.53846 1.000 29.51521 ? 22  CYS A N   1 
ATOM   157  C CA  . CYS A 1 22  ? -22.71825 15.02044  -12.25725 1.000 29.42595 ? 22  CYS A CA  1 
ATOM   158  C C   . CYS A 1 22  ? -22.28476 16.28736  -12.96688 1.000 36.39496 ? 22  CYS A C   1 
ATOM   159  O O   . CYS A 1 22  ? -21.92401 17.26931  -12.30992 1.000 31.86292 ? 22  CYS A O   1 
ATOM   160  C CB  . CYS A 1 22  ? -23.88185 15.32512  -11.32073 1.000 34.40880 ? 22  CYS A CB  1 
ATOM   161  S SG  . CYS A 1 22  ? -24.77209 13.87770  -10.83032 1.000 37.32337 ? 22  CYS A SG  1 
ATOM   162  N N   . GLY A 1 23  ? -22.31870 16.26465  -14.29707 1.000 36.49508 ? 23  GLY A N   1 
ATOM   163  C CA  . GLY A 1 23  ? -21.85799 17.41825  -15.04871 1.000 32.56718 ? 23  GLY A CA  1 
ATOM   164  C C   . GLY A 1 23  ? -20.42416 17.74307  -14.68639 1.000 29.57808 ? 23  GLY A C   1 
ATOM   165  O O   . GLY A 1 23  ? -19.51393 16.92787  -14.86939 1.000 36.56965 ? 23  GLY A O   1 
ATOM   166  N N   . THR A 1 24  ? -20.19678 18.94723  -14.16969 1.000 30.21190 ? 24  THR A N   1 
ATOM   167  C CA  . THR A 1 24  ? -18.86416 19.37244  -13.76299 1.000 32.13411 ? 24  THR A CA  1 
ATOM   168  C C   . THR A 1 24  ? -18.61628 19.21648  -12.26612 1.000 40.13254 ? 24  THR A C   1 
ATOM   169  O O   . THR A 1 24  ? -17.52902 19.56658  -11.79506 1.000 42.14907 ? 24  THR A O   1 
ATOM   170  C CB  . THR A 1 24  ? -18.62810 20.82848  -14.15331 1.000 34.41820 ? 24  THR A CB  1 
ATOM   171  O OG1 . THR A 1 24  ? -19.50201 21.66866  -13.39124 1.000 36.54311 ? 24  THR A OG1 1 
ATOM   172  C CG2 . THR A 1 24  ? -18.91499 21.03226  -15.63430 1.000 43.72510 ? 24  THR A CG2 1 
ATOM   173  N N   . THR A 1 25  ? -19.59119 18.72050  -11.51018 1.000 37.33892 ? 25  THR A N   1 
ATOM   174  C CA  . THR A 1 25  ? -19.45964 18.55542  -10.06457 1.000 39.47285 ? 25  THR A CA  1 
ATOM   175  C C   . THR A 1 25  ? -19.00908 17.13488  -9.74180  1.000 38.19058 ? 25  THR A C   1 
ATOM   176  O O   . THR A 1 25  ? -19.63649 16.16156  -10.17514 1.000 35.16144 ? 25  THR A O   1 
ATOM   177  C CB  . THR A 1 25  ? -20.78558 18.85522  -9.36467  1.000 45.46988 ? 25  THR A CB  1 
ATOM   178  O OG1 . THR A 1 25  ? -21.21514 20.18596  -9.69073  1.000 44.47594 ? 25  THR A OG1 1 
ATOM   179  C CG2 . THR A 1 25  ? -20.63519 18.71622  -7.85001  1.000 43.56465 ? 25  THR A CG2 1 
ATOM   180  N N   . THR A 1 26  ? -17.92512 17.01490  -8.98650  1.000 36.09595 ? 26  THR A N   1 
ATOM   181  C CA  . THR A 1 26  ? -17.39372 15.71251  -8.61999  1.000 34.73866 ? 26  THR A CA  1 
ATOM   182  C C   . THR A 1 26  ? -17.13619 15.66290  -7.11804  1.000 34.77655 ? 26  THR A C   1 
ATOM   183  O O   . THR A 1 26  ? -16.60222 16.61293  -6.53179  1.000 32.14820 ? 26  THR A O   1 
ATOM   184  C CB  . THR A 1 26  ? -16.11319 15.41152  -9.39189  1.000 35.42394 ? 26  THR A CB  1 
ATOM   185  O OG1 . THR A 1 26  ? -16.38373 15.50289  -10.79751 1.000 48.44906 ? 26  THR A OG1 1 
ATOM   186  C CG2 . THR A 1 26  ? -15.61707 14.01584  -9.08644  1.000 34.11560 ? 26  THR A CG2 1 
ATOM   187  N N   . LEU A 1 27  ? -17.53919 14.56140  -6.49573  1.000 26.46371 ? 27  LEU A N   1 
ATOM   188  C CA  . LEU A 1 27  ? -17.24306 14.35552  -5.08377  1.000 24.85133 ? 27  LEU A CA  1 
ATOM   189  C C   . LEU A 1 27  ? -17.13147 12.85753  -4.81391  1.000 22.54921 ? 27  LEU A C   1 
ATOM   190  O O   . LEU A 1 27  ? -17.06080 12.04191  -5.73672  1.000 24.12519 ? 27  LEU A O   1 
ATOM   191  C CB  . LEU A 1 27  ? -18.28647 15.05081  -4.20018  1.000 26.25507 ? 27  LEU A CB  1 
ATOM   192  C CG  . LEU A 1 27  ? -19.77102 14.95089  -4.56869  1.000 25.66341 ? 27  LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 27  ? -20.28087 13.50119  -4.48188  1.000 29.46890 ? 27  LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 27  ? -20.57192 15.85648  -3.64870  1.000 23.11974 ? 27  LEU A CD2 1 
ATOM   195  N N   . ASN A 1 28  ? -17.06784 12.49635  -3.52946  1.000 21.00382 ? 28  ASN A N   1 
ATOM   196  C CA  . ASN A 1 28  ? -16.83638 11.12157  -3.10940  1.000 18.44383 ? 28  ASN A CA  1 
ATOM   197  C C   . ASN A 1 28  ? -18.14350 10.42059  -2.77534  1.000 22.98623 ? 28  ASN A C   1 
ATOM   198  O O   . ASN A 1 28  ? -19.11226 11.05241  -2.35327  1.000 23.02778 ? 28  ASN A O   1 
ATOM   199  C CB  . ASN A 1 28  ? -15.93380 11.08272  -1.87160  1.000 20.09264 ? 28  ASN A CB  1 
ATOM   200  C CG  . ASN A 1 28  ? -14.68300 11.90490  -2.04788  1.000 21.95063 ? 28  ASN A CG  1 
ATOM   201  O OD1 . ASN A 1 28  ? -13.72411 11.44819  -2.68079  1.000 24.55229 ? 28  ASN A OD1 1 
ATOM   202  N ND2 . ASN A 1 28  ? -14.67542 13.13092  -1.48908  1.000 23.49492 ? 28  ASN A ND2 1 
ATOM   203  N N   . GLY A 1 29  ? -18.14304 9.09568   -2.92649  1.000 25.42671 ? 29  GLY A N   1 
ATOM   204  C CA  . GLY A 1 29  ? -19.27127 8.28269   -2.52069  1.000 29.46366 ? 29  GLY A CA  1 
ATOM   205  C C   . GLY A 1 29  ? -18.80144 7.05973   -1.75740  1.000 24.25692 ? 29  GLY A C   1 
ATOM   206  O O   . GLY A 1 29  ? -17.64188 6.64637   -1.84077  1.000 23.79538 ? 29  GLY A O   1 
ATOM   207  N N   . LEU A 1 30  ? -19.72748 6.48721   -1.00092  1.000 21.07907 ? 30  LEU A N   1 
ATOM   208  C CA  . LEU A 1 30  ? -19.47522 5.32668   -0.16095  1.000 23.53408 ? 30  LEU A CA  1 
ATOM   209  C C   . LEU A 1 30  ? -20.19551 4.12918   -0.76997  1.000 26.24662 ? 30  LEU A C   1 
ATOM   210  O O   . LEU A 1 30  ? -21.42970 4.09585   -0.81856  1.000 23.46211 ? 30  LEU A O   1 
ATOM   211  C CB  . LEU A 1 30  ? -19.94828 5.58240   1.26482   1.000 21.05737 ? 30  LEU A CB  1 
ATOM   212  C CG  . LEU A 1 30  ? -19.58517 4.50234   2.27871   1.000 24.88627 ? 30  LEU A CG  1 
ATOM   213  C CD1 . LEU A 1 30  ? -18.11242 4.55510   2.62549   1.000 23.42733 ? 30  LEU A CD1 1 
ATOM   214  C CD2 . LEU A 1 30  ? -20.43156 4.64701   3.52134   1.000 22.22240 ? 30  LEU A CD2 1 
ATOM   215  N N   . TRP A 1 31  ? -19.42742 3.14840   -1.22417  1.000 23.21259 ? 31  TRP A N   1 
ATOM   216  C CA  . TRP A 1 31  ? -19.95817 2.00113   -1.96408  1.000 26.16928 ? 31  TRP A CA  1 
ATOM   217  C C   . TRP A 1 31  ? -20.07336 0.80854   -1.01773  1.000 24.42639 ? 31  TRP A C   1 
ATOM   218  O O   . TRP A 1 31  ? -19.06329 0.20541   -0.63890  1.000 29.61718 ? 31  TRP A O   1 
ATOM   219  C CB  . TRP A 1 31  ? -19.05525 1.69416   -3.15671  1.000 23.09338 ? 31  TRP A CB  1 
ATOM   220  C CG  . TRP A 1 31  ? -19.48172 0.55463   -4.07682  1.000 26.05905 ? 31  TRP A CG  1 
ATOM   221  C CD1 . TRP A 1 31  ? -20.73655 0.03507   -4.24488  1.000 26.78499 ? 31  TRP A CD1 1 
ATOM   222  C CD2 . TRP A 1 31  ? -18.62135 -0.18277  -4.95650  1.000 27.58020 ? 31  TRP A CD2 1 
ATOM   223  N NE1 . TRP A 1 31  ? -20.70289 -0.99404  -5.16390  1.000 26.34646 ? 31  TRP A NE1 1 
ATOM   224  C CE2 . TRP A 1 31  ? -19.41532 -1.14697  -5.61191  1.000 31.28972 ? 31  TRP A CE2 1 
ATOM   225  C CE3 . TRP A 1 31  ? -17.24378 -0.13704  -5.22940  1.000 26.40843 ? 31  TRP A CE3 1 
ATOM   226  C CZ2 . TRP A 1 31  ? -18.88921 -2.03278  -6.55108  1.000 26.39505 ? 31  TRP A CZ2 1 
ATOM   227  C CZ3 . TRP A 1 31  ? -16.71895 -1.03037  -6.14119  1.000 26.25094 ? 31  TRP A CZ3 1 
ATOM   228  C CH2 . TRP A 1 31  ? -17.54003 -1.96738  -6.79133  1.000 27.68423 ? 31  TRP A CH2 1 
ATOM   229  N N   . LEU A 1 32  ? -21.30720 0.47687   -0.63183  1.000 25.93935 ? 32  LEU A N   1 
ATOM   230  C CA  . LEU A 1 32  ? -21.61093 -0.66350  0.22511   1.000 24.39679 ? 32  LEU A CA  1 
ATOM   231  C C   . LEU A 1 32  ? -22.59496 -1.56823  -0.50118  1.000 28.30965 ? 32  LEU A C   1 
ATOM   232  O O   . LEU A 1 32  ? -23.68237 -1.12246  -0.87949  1.000 26.21157 ? 32  LEU A O   1 
ATOM   233  C CB  . LEU A 1 32  ? -22.21495 -0.20740  1.55537   1.000 26.33930 ? 32  LEU A CB  1 
ATOM   234  C CG  . LEU A 1 32  ? -21.35776 0.74987   2.38542   1.000 29.84531 ? 32  LEU A CG  1 
ATOM   235  C CD1 . LEU A 1 32  ? -22.16304 1.33106   3.54802   1.000 24.13922 ? 32  LEU A CD1 1 
ATOM   236  C CD2 . LEU A 1 32  ? -20.11519 0.05171   2.87343   1.000 27.68465 ? 32  LEU A CD2 1 
ATOM   237  N N   . ASP A 1 33  ? -22.23321 -2.83648  -0.66543  1.000 31.46290 ? 33  ASP A N   1 
ATOM   238  C CA  . ASP A 1 33  ? -23.06326 -3.79154  -1.41513  1.000 30.75949 ? 33  ASP A CA  1 
ATOM   239  C C   . ASP A 1 33  ? -23.28368 -3.18605  -2.79540  1.000 31.98140 ? 33  ASP A C   1 
ATOM   240  O O   . ASP A 1 33  ? -22.30044 -2.78148  -3.43949  1.000 32.04845 ? 33  ASP A O   1 
ATOM   241  C CB  . ASP A 1 33  ? -24.32364 -4.10397  -0.62632  1.000 34.01046 ? 33  ASP A CB  1 
ATOM   242  C CG  . ASP A 1 33  ? -24.03370 -4.88408  0.64185   1.000 37.30976 ? 33  ASP A CG  1 
ATOM   243  O OD1 . ASP A 1 33  ? -23.14065 -5.75890  0.60262   1.000 40.02107 ? 33  ASP A OD1 1 
ATOM   244  O OD2 . ASP A 1 33  ? -24.69246 -4.62157  1.67355   1.000 41.47495 ? 33  ASP A OD2 1 
ATOM   245  N N   . ASP A 1 34  ? -24.51907 -3.07258  -3.28123  1.000 28.27310 ? 34  ASP A N   1 
ATOM   246  C CA  . ASP A 1 34  ? -24.78035 -2.52323  -4.60442  1.000 30.82887 ? 34  ASP A CA  1 
ATOM   247  C C   . ASP A 1 34  ? -25.34949 -1.11000  -4.53749  1.000 30.13475 ? 34  ASP A C   1 
ATOM   248  O O   . ASP A 1 34  ? -26.05327 -0.67842  -5.45120  1.000 28.59289 ? 34  ASP A O   1 
ATOM   249  C CB  . ASP A 1 34  ? -25.70993 -3.44047  -5.39938  1.000 30.23804 ? 34  ASP A CB  1 
ATOM   250  C CG  . ASP A 1 34  ? -27.06014 -3.61361  -4.74033  1.000 35.93939 ? 34  ASP A CG  1 
ATOM   251  O OD1 . ASP A 1 34  ? -27.17784 -3.26478  -3.54763  1.000 30.27848 ? 34  ASP A OD1 1 
ATOM   252  O OD2 . ASP A 1 34  ? -27.99787 -4.10906  -5.41254  1.000 36.25158 ? 34  ASP A OD2 1 
ATOM   253  N N   . VAL A 1 35  ? -25.02515 -0.35849  -3.48115  1.000 29.93447 ? 35  VAL A N   1 
ATOM   254  C CA  . VAL A 1 35  ? -25.51325 1.00583   -3.32737  1.000 24.79603 ? 35  VAL A CA  1 
ATOM   255  C C   . VAL A 1 35  ? -24.33620 1.94544   -3.10336  1.000 24.84380 ? 35  VAL A C   1 
ATOM   256  O O   . VAL A 1 35  ? -23.40729 1.61412   -2.36742  1.000 25.59231 ? 35  VAL A O   1 
ATOM   257  C CB  . VAL A 1 35  ? -26.51330 1.10916   -2.16219  1.000 26.88315 ? 35  VAL A CB  1 
ATOM   258  C CG1 . VAL A 1 35  ? -27.05596 2.52383   -2.06261  1.000 28.05908 ? 35  VAL A CG1 1 
ATOM   259  C CG2 . VAL A 1 35  ? -27.63525 0.09735   -2.33885  1.000 25.44804 ? 35  VAL A CG2 1 
ATOM   260  N N   . VAL A 1 36  ? -24.38540 3.12803   -3.71285  1.000 27.48805 ? 36  VAL A N   1 
ATOM   261  C CA  . VAL A 1 36  ? -23.40018 4.18070   -3.47718  1.000 20.70772 ? 36  VAL A CA  1 
ATOM   262  C C   . VAL A 1 36  ? -24.11340 5.34115   -2.79706  1.000 26.83785 ? 36  VAL A C   1 
ATOM   263  O O   . VAL A 1 36  ? -25.12582 5.83162   -3.30791  1.000 25.70101 ? 36  VAL A O   1 
ATOM   264  C CB  . VAL A 1 36  ? -22.73245 4.63721   -4.78397  1.000 25.75281 ? 36  VAL A CB  1 
ATOM   265  C CG1 . VAL A 1 36  ? -21.89132 5.89487   -4.53620  1.000 23.89523 ? 36  VAL A CG1 1 
ATOM   266  C CG2 . VAL A 1 36  ? -21.88977 3.51606   -5.36621  1.000 25.32496 ? 36  VAL A CG2 1 
ATOM   267  N N   . TYR A 1 37  ? -23.58960 5.77375   -1.64646  1.000 22.78135 ? 37  TYR A N   1 
ATOM   268  C CA  . TYR A 1 37  ? -24.13050 6.88382   -0.86583  1.000 23.37430 ? 37  TYR A CA  1 
ATOM   269  C C   . TYR A 1 37  ? -23.28111 8.12126   -1.09282  1.000 25.98829 ? 37  TYR A C   1 
ATOM   270  O O   . TYR A 1 37  ? -22.04891 8.03971   -1.01195  1.000 25.78153 ? 37  TYR A O   1 
ATOM   271  C CB  . TYR A 1 37  ? -24.11752 6.53436   0.62911   1.000 22.38740 ? 37  TYR A CB  1 
ATOM   272  C CG  . TYR A 1 37  ? -24.90784 5.28685   0.96140   1.000 26.29385 ? 37  TYR A CG  1 
ATOM   273  C CD1 . TYR A 1 37  ? -24.38777 4.02777   0.71814   1.000 25.10188 ? 37  TYR A CD1 1 
ATOM   274  C CD2 . TYR A 1 37  ? -26.19449 5.37529   1.50122   1.000 27.09685 ? 37  TYR A CD2 1 
ATOM   275  C CE1 . TYR A 1 37  ? -25.11475 2.87810   1.01090   1.000 25.12226 ? 37  TYR A CE1 1 
ATOM   276  C CE2 . TYR A 1 37  ? -26.93550 4.23399   1.78627   1.000 26.17242 ? 37  TYR A CE2 1 
ATOM   277  C CZ  . TYR A 1 37  ? -26.38785 2.99244   1.54358   1.000 25.35819 ? 37  TYR A CZ  1 
ATOM   278  O OH  . TYR A 1 37  ? -27.09877 1.85885   1.83974   1.000 27.85887 ? 37  TYR A OH  1 
ATOM   279  N N   . CYS A 1 38  ? -23.91691 9.27302   -1.32908  1.000 23.67393 ? 38  CYS A N   1 
ATOM   280  C CA  . CYS A 1 38  ? -23.14633 10.49544  -1.50442  1.000 24.77595 ? 38  CYS A CA  1 
ATOM   281  C C   . CYS A 1 38  ? -24.02917 11.70568  -1.21185  1.000 23.71336 ? 38  CYS A C   1 
ATOM   282  O O   . CYS A 1 38  ? -25.26839 11.59423  -1.20582  1.000 23.92281 ? 38  CYS A O   1 
ATOM   283  C CB  . CYS A 1 38  ? -22.55290 10.57973  -2.91678  1.000 28.00136 ? 38  CYS A CB  1 
ATOM   284  S SG  . CYS A 1 38  ? -23.74921 11.00055  -4.17232  1.000 28.06246 ? 38  CYS A SG  1 
ATOM   285  N N   . PRO A 1 39  ? -23.43689 12.87296  -0.95412  1.000 20.80648 ? 39  PRO A N   1 
ATOM   286  C CA  . PRO A 1 39  ? -24.23972 14.07596  -0.68515  1.000 21.20642 ? 39  PRO A CA  1 
ATOM   287  C C   . PRO A 1 39  ? -25.10920 14.44376  -1.88527  1.000 25.65867 ? 39  PRO A C   1 
ATOM   288  O O   . PRO A 1 39  ? -24.67012 14.38359  -3.03244  1.000 23.21242 ? 39  PRO A O   1 
ATOM   289  C CB  . PRO A 1 39  ? -23.18614 15.15614  -0.41219  1.000 25.23505 ? 39  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 39  ? -21.95374 14.38735  0.00257   1.000 24.07962 ? 39  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 39  ? -21.98995 13.12745  -0.80585  1.000 21.43487 ? 39  PRO A CD  1 
ATOM   292  N N   . ARG A 1 40  ? -26.35208 14.85092  -1.62117  1.000 25.29147 ? 40  ARG A N   1 
ATOM   293  C CA  . ARG A 1 40  ? -27.22673 15.13835  -2.75374  1.000 23.98297 ? 40  ARG A CA  1 
ATOM   294  C C   . ARG A 1 40  ? -26.81111 16.38077  -3.51201  1.000 24.57727 ? 40  ARG A C   1 
ATOM   295  O O   . ARG A 1 40  ? -27.15357 16.50269  -4.69585  1.000 26.43671 ? 40  ARG A O   1 
ATOM   296  C CB  . ARG A 1 40  ? -28.68066 15.28848  -2.31231  1.000 24.03267 ? 40  ARG A CB  1 
ATOM   297  C CG  . ARG A 1 40  ? -28.95685 16.51247  -1.46704  1.000 21.85256 ? 40  ARG A CG  1 
ATOM   298  C CD  . ARG A 1 40  ? -30.40739 16.46660  -0.98198  1.000 23.70335 ? 40  ARG A CD  1 
ATOM   299  N NE  . ARG A 1 40  ? -30.71895 17.61829  -0.15193  1.000 24.77530 ? 40  ARG A NE  1 
ATOM   300  C CZ  . ARG A 1 40  ? -31.92256 17.88959  0.33272   1.000 27.71833 ? 40  ARG A CZ  1 
ATOM   301  N NH1 . ARG A 1 40  ? -32.96544 17.12782  0.05828   1.000 21.40848 ? 40  ARG A NH1 1 
ATOM   302  N NH2 . ARG A 1 40  ? -32.08394 18.95963  1.10037   1.000 26.30152 ? 40  ARG A NH2 1 
ATOM   303  N N   . HIS A 1 41  ? -26.05953 17.29987  -2.89581  1.000 24.80141 ? 41  HIS A N   1 
ATOM   304  C CA  . HIS A 1 41  ? -25.74942 18.48749  -3.69466  1.000 24.55323 ? 41  HIS A CA  1 
ATOM   305  C C   . HIS A 1 41  ? -24.81029 18.18693  -4.85709  1.000 25.70682 ? 41  HIS A C   1 
ATOM   306  O O   . HIS A 1 41  ? -24.42785 19.12224  -5.56411  1.000 26.45027 ? 41  HIS A O   1 
ATOM   307  C CB  . HIS A 1 41  ? -25.17307 19.62426  -2.83330  1.000 22.67279 ? 41  HIS A CB  1 
ATOM   308  C CG  . HIS A 1 41  ? -23.77835 19.38819  -2.31278  1.000 25.46824 ? 41  HIS A CG  1 
ATOM   309  N ND1 . HIS A 1 41  ? -23.51345 19.11023  -0.98647  1.000 28.87298 ? 41  HIS A ND1 1 
ATOM   310  C CD2 . HIS A 1 41  ? -22.57409 19.41762  -2.93354  1.000 27.27220 ? 41  HIS A CD2 1 
ATOM   311  C CE1 . HIS A 1 41  ? -22.20842 18.97824  -0.81418  1.000 27.01989 ? 41  HIS A CE1 1 
ATOM   312  N NE2 . HIS A 1 41  ? -21.61674 19.15738  -1.98188  1.000 28.81127 ? 41  HIS A NE2 1 
ATOM   313  N N   . VAL A 1 42  ? -24.45502 16.91791  -5.08513  1.000 22.02868 ? 42  VAL A N   1 
ATOM   314  C CA  . VAL A 1 42  ? -23.70717 16.58869  -6.29639  1.000 29.55433 ? 42  VAL A CA  1 
ATOM   315  C C   . VAL A 1 42  ? -24.53281 16.93583  -7.53249  1.000 34.69952 ? 42  VAL A C   1 
ATOM   316  O O   . VAL A 1 42  ? -23.98368 17.23897  -8.60316  1.000 30.37323 ? 42  VAL A O   1 
ATOM   317  C CB  . VAL A 1 42  ? -23.28224 15.10357  -6.29140  1.000 25.64011 ? 42  VAL A CB  1 
ATOM   318  C CG1 . VAL A 1 42  ? -24.47223 14.20697  -6.57784  1.000 23.40693 ? 42  VAL A CG1 1 
ATOM   319  C CG2 . VAL A 1 42  ? -22.16066 14.85804  -7.32263  1.000 30.17864 ? 42  VAL A CG2 1 
ATOM   320  N N   . ILE A 1 43  ? -25.86394 16.91089  -7.41449  1.000 29.40469 ? 43  ILE A N   1 
ATOM   321  C CA  . ILE A 1 43  ? -26.70795 17.19790  -8.57044  1.000 28.33562 ? 43  ILE A CA  1 
ATOM   322  C C   . ILE A 1 43  ? -26.87526 18.68377  -8.84119  1.000 28.23140 ? 43  ILE A C   1 
ATOM   323  O O   . ILE A 1 43  ? -27.60272 19.04534  -9.77295  1.000 34.96055 ? 43  ILE A O   1 
ATOM   324  C CB  . ILE A 1 43  ? -28.11783 16.58251  -8.43544  1.000 30.85702 ? 43  ILE A CB  1 
ATOM   325  C CG1 . ILE A 1 43  ? -28.91417 17.28823  -7.34571  1.000 33.52657 ? 43  ILE A CG1 1 
ATOM   326  C CG2 . ILE A 1 43  ? -28.03975 15.09470  -8.11157  1.000 29.05681 ? 43  ILE A CG2 1 
ATOM   327  C CD1 . ILE A 1 43  ? -30.30767 16.73957  -7.16676  1.000 25.69938 ? 43  ILE A CD1 1 
ATOM   328  N N   . CYS A 1 44  ? -26.19619 19.55403  -8.10102  1.000 35.53543 ? 44  CYS A N   1 
ATOM   329  C CA  . CYS A 1 44  ? -26.37849 20.99633  -8.22856  1.000 30.94989 ? 44  CYS A CA  1 
ATOM   330  C C   . CYS A 1 44  ? -25.31179 21.63430  -9.11055  1.000 36.01395 ? 44  CYS A C   1 
ATOM   331  O O   . CYS A 1 44  ? -24.11913 21.34251  -8.96998  1.000 35.86650 ? 44  CYS A O   1 
ATOM   332  C CB  . CYS A 1 44  ? -26.33815 21.67731  -6.85954  1.000 31.72771 ? 44  CYS A CB  1 
ATOM   333  S SG  . CYS A 1 44  ? -27.76086 21.29261  -5.84152  1.000 32.40165 ? 44  CYS A SG  1 
ATOM   334  N N   . THR A 1 45  ? -25.74868 22.53599  -9.99778  1.000 33.07669 ? 45  THR A N   1 
ATOM   335  C CA  . THR A 1 45  ? -24.83901 23.48739  -10.61795 1.000 38.30536 ? 45  THR A CA  1 
ATOM   336  C C   . THR A 1 45  ? -24.51338 24.60585  -9.63297  1.000 43.22172 ? 45  THR A C   1 
ATOM   337  O O   . THR A 1 45  ? -25.07485 24.69226  -8.53674  1.000 36.57204 ? 45  THR A O   1 
ATOM   338  C CB  . THR A 1 45  ? -25.44287 24.10532  -11.87537 1.000 36.37878 ? 45  THR A CB  1 
ATOM   339  O OG1 . THR A 1 45  ? -26.46563 25.03228  -11.48445 1.000 34.07089 ? 45  THR A OG1 1 
ATOM   340  C CG2 . THR A 1 45  ? -26.01632 23.03631  -12.79325 1.000 38.91116 ? 45  THR A CG2 1 
ATOM   341  N N   . SER A 1 46  ? -23.61377 25.49855  -10.05018 1.000 42.77820 ? 46  SER A N   1 
ATOM   342  C CA  . SER A 1 46  ? -23.24046 26.62615  -9.20419  1.000 48.60168 ? 46  SER A CA  1 
ATOM   343  C C   . SER A 1 46  ? -24.46720 27.44317  -8.81141  1.000 46.51454 ? 46  SER A C   1 
ATOM   344  O O   . SER A 1 46  ? -24.65220 27.78596  -7.63675  1.000 43.58195 ? 46  SER A O   1 
ATOM   345  C CB  . SER A 1 46  ? -22.21125 27.49494  -9.92979  1.000 53.15664 ? 46  SER A CB  1 
ATOM   346  O OG  . SER A 1 46  ? -21.52127 28.33612  -9.02785  1.000 62.82802 ? 46  SER A OG  1 
ATOM   347  N N   . GLU A 1 47  ? -25.32428 27.76315  -9.78382  1.000 41.10689 ? 47  GLU A N   1 
ATOM   348  C CA  . GLU A 1 47  ? -26.52640 28.52700  -9.46800  1.000 38.32108 ? 47  GLU A CA  1 
ATOM   349  C C   . GLU A 1 47  ? -27.48952 27.72874  -8.59945  1.000 38.61791 ? 47  GLU A C   1 
ATOM   350  O O   . GLU A 1 47  ? -28.16600 28.30955  -7.74294  1.000 44.09882 ? 47  GLU A O   1 
ATOM   351  C CB  . GLU A 1 47  ? -27.22153 28.99119  -10.74868 1.000 40.45555 ? 47  GLU A CB  1 
ATOM   352  N N   . ASP A 1 48  ? -27.54875 26.40551  -8.78173  1.000 34.17921 ? 48  ASP A N   1 
ATOM   353  C CA  . ASP A 1 48  ? -28.45738 25.58851  -7.98310  1.000 37.39521 ? 48  ASP A CA  1 
ATOM   354  C C   . ASP A 1 48  ? -28.08785 25.63800  -6.50573  1.000 37.91649 ? 48  ASP A C   1 
ATOM   355  O O   . ASP A 1 48  ? -28.96578 25.71294  -5.64035  1.000 37.39225 ? 48  ASP A O   1 
ATOM   356  C CB  . ASP A 1 48  ? -28.44126 24.14201  -8.47287  1.000 34.57716 ? 48  ASP A CB  1 
ATOM   357  C CG  . ASP A 1 48  ? -29.07777 23.97310  -9.83991  1.000 32.32292 ? 48  ASP A CG  1 
ATOM   358  O OD1 . ASP A 1 48  ? -30.00347 24.73695  -10.17203 1.000 35.99878 ? 48  ASP A OD1 1 
ATOM   359  O OD2 . ASP A 1 48  ? -28.65398 23.06022  -10.56955 1.000 33.83931 ? 48  ASP A OD2 1 
ATOM   360  N N   . MET A 1 49  ? -26.79085 25.58057  -6.19881  1.000 37.68068 ? 49  MET A N   1 
ATOM   361  C CA  . MET A 1 49  ? -26.36747 25.56197  -4.80115  1.000 33.26531 ? 49  MET A CA  1 
ATOM   362  C C   . MET A 1 49  ? -26.80785 26.81561  -4.06108  1.000 33.45999 ? 49  MET A C   1 
ATOM   363  O O   . MET A 1 49  ? -27.06383 26.76010  -2.85233  1.000 37.03555 ? 49  MET A O   1 
ATOM   364  C CB  . MET A 1 49  ? -24.85467 25.39041  -4.72477  1.000 31.70469 ? 49  MET A CB  1 
ATOM   365  C CG  . MET A 1 49  ? -24.40496 23.96761  -5.02855  1.000 40.14201 ? 49  MET A CG  1 
ATOM   366  S SD  . MET A 1 49  ? -22.63613 23.84583  -5.36572  1.000 54.62646 ? 49  MET A SD  1 
ATOM   367  C CE  . MET A 1 49  ? -22.47775 22.07591  -5.61460  1.000 40.71001 ? 49  MET A CE  1 
ATOM   368  N N   . LEU A 1 50  ? -26.89783 27.95483  -4.75709  1.000 31.59212 ? 50  LEU A N   1 
ATOM   369  C CA  . LEU A 1 50  ? -27.31418 29.19299  -4.10118  1.000 36.17674 ? 50  LEU A CA  1 
ATOM   370  C C   . LEU A 1 50  ? -28.77646 29.15664  -3.65818  1.000 38.77626 ? 50  LEU A C   1 
ATOM   371  O O   . LEU A 1 50  ? -29.15587 29.92187  -2.76700  1.000 43.75833 ? 50  LEU A O   1 
ATOM   372  C CB  . LEU A 1 50  ? -27.07564 30.40069  -5.02198  1.000 38.65681 ? 50  LEU A CB  1 
ATOM   373  C CG  . LEU A 1 50  ? -25.62310 30.68493  -5.45134  1.000 45.41506 ? 50  LEU A CG  1 
ATOM   374  C CD1 . LEU A 1 50  ? -25.53047 31.86081  -6.42059  1.000 38.30708 ? 50  LEU A CD1 1 
ATOM   375  C CD2 . LEU A 1 50  ? -24.71053 30.91894  -4.26116  1.000 36.94059 ? 50  LEU A CD2 1 
ATOM   376  N N   . ASN A 1 51  ? -29.60147 28.28176  -4.24847  1.000 49.93636 ? 51  ASN A N   1 
ATOM   377  C CA  . ASN A 1 51  ? -31.00851 28.12111  -3.87546  1.000 49.03034 ? 51  ASN A CA  1 
ATOM   378  C C   . ASN A 1 51  ? -31.56145 26.83539  -4.48859  1.000 44.90718 ? 51  ASN A C   1 
ATOM   379  O O   . ASN A 1 51  ? -32.20660 26.87220  -5.54635  1.000 49.94992 ? 51  ASN A O   1 
ATOM   380  C CB  . ASN A 1 51  ? -31.83832 29.32902  -4.31890  1.000 53.44883 ? 51  ASN A CB  1 
ATOM   381  N N   . PRO A 1 52  ? -31.33556 25.68743  -3.85371  1.000 42.77114 ? 52  PRO A N   1 
ATOM   382  C CA  . PRO A 1 52  ? -31.65361 24.40806  -4.50489  1.000 40.05259 ? 52  PRO A CA  1 
ATOM   383  C C   . PRO A 1 52  ? -33.10199 23.98695  -4.31720  1.000 41.38654 ? 52  PRO A C   1 
ATOM   384  O O   . PRO A 1 52  ? -33.65661 24.06353  -3.21995  1.000 45.59503 ? 52  PRO A O   1 
ATOM   385  C CB  . PRO A 1 52  ? -30.71473 23.41943  -3.79943  1.000 30.08138 ? 52  PRO A CB  1 
ATOM   386  C CG  . PRO A 1 52  ? -30.57734 23.99902  -2.41846  1.000 31.94327 ? 52  PRO A CG  1 
ATOM   387  C CD  . PRO A 1 52  ? -30.61061 25.50186  -2.58257  1.000 40.62036 ? 52  PRO A CD  1 
ATOM   388  N N   . ASN A 1 53  ? -33.69312 23.47276  -5.39288  1.000 40.17975 ? 53  ASN A N   1 
ATOM   389  C CA  . ASN A 1 53  ? -34.98121 22.78224  -5.34080  1.000 37.33954 ? 53  ASN A CA  1 
ATOM   390  C C   . ASN A 1 53  ? -34.70284 21.29534  -5.56123  1.000 37.92675 ? 53  ASN A C   1 
ATOM   391  O O   . ASN A 1 53  ? -34.82715 20.77911  -6.67281  1.000 37.53356 ? 53  ASN A O   1 
ATOM   392  C CB  . ASN A 1 53  ? -35.93981 23.35281  -6.40192  1.000 44.38912 ? 53  ASN A CB  1 
ATOM   393  C CG  . ASN A 1 53  ? -37.32602 22.75106  -6.32066  1.000 56.19583 ? 53  ASN A CG  1 
ATOM   394  O OD1 . ASN A 1 53  ? -37.66379 22.06265  -5.35169  1.000 53.65155 ? 53  ASN A OD1 1 
ATOM   395  N ND2 . ASN A 1 53  ? -38.14506 23.01082  -7.34120  1.000 55.37384 ? 53  ASN A ND2 1 
ATOM   396  N N   . TYR A 1 54  ? -34.32547 20.60093  -4.48236  1.000 31.35069 ? 54  TYR A N   1 
ATOM   397  C CA  . TYR A 1 54  ? -33.66318 19.30556  -4.62785  1.000 35.29683 ? 54  TYR A CA  1 
ATOM   398  C C   . TYR A 1 54  ? -34.56113 18.26987  -5.29248  1.000 27.24692 ? 54  TYR A C   1 
ATOM   399  O O   . TYR A 1 54  ? -34.12008 17.54308  -6.18583  1.000 30.27979 ? 54  TYR A O   1 
ATOM   400  C CB  . TYR A 1 54  ? -33.17707 18.79774  -3.26700  1.000 26.69728 ? 54  TYR A CB  1 
ATOM   401  C CG  . TYR A 1 54  ? -31.82827 19.36444  -2.89165  1.000 27.54842 ? 54  TYR A CG  1 
ATOM   402  C CD1 . TYR A 1 54  ? -30.69986 19.05960  -3.64764  1.000 26.54982 ? 54  TYR A CD1 1 
ATOM   403  C CD2 . TYR A 1 54  ? -31.68243 20.21767  -1.80769  1.000 24.69635 ? 54  TYR A CD2 1 
ATOM   404  C CE1 . TYR A 1 54  ? -29.46429 19.56898  -3.32448  1.000 27.96320 ? 54  TYR A CE1 1 
ATOM   405  C CE2 . TYR A 1 54  ? -30.42541 20.73365  -1.46414  1.000 25.59313 ? 54  TYR A CE2 1 
ATOM   406  C CZ  . TYR A 1 54  ? -29.32946 20.40386  -2.23423  1.000 25.90402 ? 54  TYR A CZ  1 
ATOM   407  O OH  . TYR A 1 54  ? -28.07729 20.89255  -1.92404  1.000 24.22024 ? 54  TYR A OH  1 
ATOM   408  N N   . GLU A 1 55  ? -35.81885 18.17075  -4.86602  1.000 28.83323 ? 55  GLU A N   1 
ATOM   409  C CA  . GLU A 1 55  ? -36.67828 17.13712  -5.43552  1.000 35.29628 ? 55  GLU A CA  1 
ATOM   410  C C   . GLU A 1 55  ? -36.88862 17.34728  -6.94055  1.000 33.52770 ? 55  GLU A C   1 
ATOM   411  O O   . GLU A 1 55  ? -36.90156 16.38006  -7.71536  1.000 32.61092 ? 55  GLU A O   1 
ATOM   412  C CB  . GLU A 1 55  ? -38.01336 17.09211  -4.69573  1.000 34.73785 ? 55  GLU A CB  1 
ATOM   413  C CG  . GLU A 1 55  ? -38.73563 15.77673  -4.90833  1.000 48.89418 ? 55  GLU A CG  1 
ATOM   414  C CD  . GLU A 1 55  ? -40.11471 15.75117  -4.28942  1.000 60.68601 ? 55  GLU A CD  1 
ATOM   415  O OE1 . GLU A 1 55  ? -40.35670 16.53437  -3.34589  1.000 66.85984 ? 55  GLU A OE1 1 
ATOM   416  O OE2 . GLU A 1 55  ? -40.95532 14.94988  -4.75347  1.000 59.23729 ? 55  GLU A OE2 1 
ATOM   417  N N   . ASP A 1 56  ? -37.04966 18.60255  -7.37120  1.000 38.85191 ? 56  ASP A N   1 
ATOM   418  C CA  . ASP A 1 56  ? -37.16975 18.89254  -8.79857  1.000 39.85124 ? 56  ASP A CA  1 
ATOM   419  C C   . ASP A 1 56  ? -35.90348 18.50886  -9.53857  1.000 34.97089 ? 56  ASP A C   1 
ATOM   420  O O   . ASP A 1 56  ? -35.95512 17.91608  -10.62462 1.000 34.99331 ? 56  ASP A O   1 
ATOM   421  C CB  . ASP A 1 56  ? -37.44773 20.37473  -9.02530  1.000 42.19167 ? 56  ASP A CB  1 
ATOM   422  C CG  . ASP A 1 56  ? -38.91689 20.69202  -9.10569  1.000 46.93651 ? 56  ASP A CG  1 
ATOM   423  O OD1 . ASP A 1 56  ? -39.74160 19.76779  -8.94378  1.000 40.27905 ? 56  ASP A OD1 1 
ATOM   424  O OD2 . ASP A 1 56  ? -39.23585 21.87807  -9.33599  1.000 48.37795 ? 56  ASP A OD2 1 
ATOM   425  N N   . LEU A 1 57  ? -34.75082 18.90485  -9.00043  1.000 27.76012 ? 57  LEU A N   1 
ATOM   426  C CA  . LEU A 1 57  ? -33.50641 18.60292  -9.69048  1.000 27.46551 ? 57  LEU A CA  1 
ATOM   427  C C   . LEU A 1 57  ? -33.32797 17.09857  -9.84955  1.000 32.14109 ? 57  LEU A C   1 
ATOM   428  O O   . LEU A 1 57  ? -32.84621 16.63052  -10.88680 1.000 36.59532 ? 57  LEU A O   1 
ATOM   429  C CB  . LEU A 1 57  ? -32.32957 19.23354  -8.94794  1.000 32.55764 ? 57  LEU A CB  1 
ATOM   430  C CG  . LEU A 1 57  ? -32.17404 20.75358  -9.03673  1.000 33.96439 ? 57  LEU A CG  1 
ATOM   431  C CD1 . LEU A 1 57  ? -31.10582 21.24722  -8.04514  1.000 32.78930 ? 57  LEU A CD1 1 
ATOM   432  C CD2 . LEU A 1 57  ? -31.82922 21.17895  -10.45579 1.000 36.70082 ? 57  LEU A CD2 1 
ATOM   433  N N   . LEU A 1 58  ? -33.74509 16.31552  -8.84972  1.000 27.43462 ? 58  LEU A N   1 
ATOM   434  C CA  . LEU A 1 58  ? -33.51862 14.87932  -8.92434  1.000 30.41862 ? 58  LEU A CA  1 
ATOM   435  C C   . LEU A 1 58  ? -34.48506 14.21050  -9.89775  1.000 32.55122 ? 58  LEU A C   1 
ATOM   436  O O   . LEU A 1 58  ? -34.10290 13.26968  -10.60409 1.000 32.16299 ? 58  LEU A O   1 
ATOM   437  C CB  . LEU A 1 58  ? -33.61668 14.24811  -7.53081  1.000 26.08987 ? 58  LEU A CB  1 
ATOM   438  C CG  . LEU A 1 58  ? -33.24208 12.75766  -7.51357  1.000 37.20399 ? 58  LEU A CG  1 
ATOM   439  C CD1 . LEU A 1 58  ? -31.83817 12.54503  -8.06724  1.000 37.43381 ? 58  LEU A CD1 1 
ATOM   440  C CD2 . LEU A 1 58  ? -33.35139 12.15541  -6.12374  1.000 31.00779 ? 58  LEU A CD2 1 
ATOM   441  N N   . ILE A 1 59  ? -35.73465 14.67820  -9.96312  1.000 30.44713 ? 59  ILE A N   1 
ATOM   442  C CA  . ILE A 1 59  ? -36.66389 14.09371  -10.92706 1.000 31.54001 ? 59  ILE A CA  1 
ATOM   443  C C   . ILE A 1 59  ? -36.18402 14.31890  -12.35748 1.000 32.88772 ? 59  ILE A C   1 
ATOM   444  O O   . ILE A 1 59  ? -36.49565 13.52595  -13.25385 1.000 37.12748 ? 59  ILE A O   1 
ATOM   445  C CB  . ILE A 1 59  ? -38.08325 14.65138  -10.73284 1.000 33.66388 ? 59  ILE A CB  1 
ATOM   446  C CG1 . ILE A 1 59  ? -38.69261 14.12621  -9.43856  1.000 33.94227 ? 59  ILE A CG1 1 
ATOM   447  C CG2 . ILE A 1 59  ? -38.95847 14.25474  -11.90054 1.000 35.25905 ? 59  ILE A CG2 1 
ATOM   448  C CD1 . ILE A 1 59  ? -40.01133 14.77617  -9.09038  1.000 42.27211 ? 59  ILE A CD1 1 
ATOM   449  N N   . ARG A 1 60  ? -35.42563 15.39130  -12.59980 1.000 29.50745 ? 60  ARG A N   1 
ATOM   450  C CA  . ARG A 1 60  ? -34.95197 15.69552  -13.94564 1.000 32.40145 ? 60  ARG A CA  1 
ATOM   451  C C   . ARG A 1 60  ? -33.68709 14.94601  -14.31299 1.000 35.73732 ? 60  ARG A C   1 
ATOM   452  O O   . ARG A 1 60  ? -33.25390 15.02485  -15.46510 1.000 34.06116 ? 60  ARG A O   1 
ATOM   453  C CB  . ARG A 1 60  ? -34.71231 17.19771  -14.09552 1.000 30.69530 ? 60  ARG A CB  1 
ATOM   454  C CG  . ARG A 1 60  ? -35.98541 17.94945  -14.02344 1.000 31.50448 ? 60  ARG A CG  1 
ATOM   455  C CD  . ARG A 1 60  ? -35.79423 19.41201  -13.81298 1.000 27.31479 ? 60  ARG A CD  1 
ATOM   456  N NE  . ARG A 1 60  ? -37.08803 19.98520  -13.47381 1.000 37.36689 ? 60  ARG A NE  1 
ATOM   457  C CZ  . ARG A 1 60  ? -37.26294 21.15169  -12.87511 1.000 31.81218 ? 60  ARG A CZ  1 
ATOM   458  N NH1 . ARG A 1 60  ? -36.23700 21.91029  -12.53541 1.000 38.69097 ? 60  ARG A NH1 1 
ATOM   459  N NH2 . ARG A 1 60  ? -38.50001 21.56185  -12.60828 1.000 37.26119 ? 60  ARG A NH2 1 
ATOM   460  N N   . LYS A 1 61  ? -33.08686 14.22973  -13.37907 1.000 35.58348 ? 61  LYS A N   1 
ATOM   461  C CA  . LYS A 1 61  ? -31.90653 13.44144  -13.68966 1.000 40.42981 ? 61  LYS A CA  1 
ATOM   462  C C   . LYS A 1 61  ? -32.31133 12.03894  -14.12790 1.000 35.36346 ? 61  LYS A C   1 
ATOM   463  O O   . LYS A 1 61  ? -33.40589 11.55748  -13.82928 1.000 34.25328 ? 61  LYS A O   1 
ATOM   464  C CB  . LYS A 1 61  ? -30.97374 13.37150  -12.47633 1.000 40.96143 ? 61  LYS A CB  1 
ATOM   465  C CG  . LYS A 1 61  ? -30.35539 14.71301  -12.07964 1.000 38.76385 ? 61  LYS A CG  1 
ATOM   466  C CD  . LYS A 1 61  ? -28.98822 14.95210  -12.74826 1.000 44.07440 ? 61  LYS A CD  1 
ATOM   467  C CE  . LYS A 1 61  ? -27.92913 13.95624  -12.27886 1.000 42.45251 ? 61  LYS A CE  1 
ATOM   468  N NZ  . LYS A 1 61  ? -26.51077 14.37984  -12.57395 1.000 34.46786 ? 61  LYS A NZ  1 
ATOM   469  N N   . SER A 1 62  ? -31.41359 11.38714  -14.86145 1.000 40.09705 ? 62  SER A N   1 
ATOM   470  C CA  . SER A 1 62  ? -31.55763 9.97460   -15.18266 1.000 37.14189 ? 62  SER A CA  1 
ATOM   471  C C   . SER A 1 62  ? -30.30330 9.22730   -14.74596 1.000 34.79794 ? 62  SER A C   1 
ATOM   472  O O   . SER A 1 62  ? -29.24166 9.82032   -14.54338 1.000 37.65771 ? 62  SER A O   1 
ATOM   473  C CB  . SER A 1 62  ? -31.80791 9.75234   -16.67753 1.000 41.88211 ? 62  SER A CB  1 
ATOM   474  O OG  . SER A 1 62  ? -30.79951 10.38699  -17.43407 1.000 47.34751 ? 62  SER A OG  1 
ATOM   475  N N   . ASN A 1 63  ? -30.44412 7.90843   -14.60523 1.000 30.48560 ? 63  ASN A N   1 
ATOM   476  C CA  . ASN A 1 63  ? -29.32102 7.07420   -14.19562 1.000 33.75286 ? 63  ASN A CA  1 
ATOM   477  C C   . ASN A 1 63  ? -28.04340 7.41714   -14.96159 1.000 39.25501 ? 63  ASN A C   1 
ATOM   478  O O   . ASN A 1 63  ? -26.96027 7.47805   -14.36962 1.000 36.41044 ? 63  ASN A O   1 
ATOM   479  C CB  . ASN A 1 63  ? -29.67758 5.59313   -14.36712 1.000 30.03950 ? 63  ASN A CB  1 
ATOM   480  C CG  . ASN A 1 63  ? -30.86347 5.16825   -13.50231 1.000 36.49118 ? 63  ASN A CG  1 
ATOM   481  O OD1 . ASN A 1 63  ? -31.08074 5.70473   -12.41517 1.000 38.85346 ? 63  ASN A OD1 1 
ATOM   482  N ND2 . ASN A 1 63  ? -31.62361 4.19384   -13.97843 1.000 29.93511 ? 63  ASN A ND2 1 
ATOM   483  N N   . HIS A 1 64  ? -28.14204 7.67040   -16.27308 1.000 40.16693 ? 64  HIS A N   1 
ATOM   484  C CA  . HIS A 1 64  ? -26.91706 7.81423   -17.05953 1.000 38.52204 ? 64  HIS A CA  1 
ATOM   485  C C   . HIS A 1 64  ? -26.21737 9.14667   -16.81948 1.000 39.82185 ? 64  HIS A C   1 
ATOM   486  O O   . HIS A 1 64  ? -25.03780 9.28537   -17.16304 1.000 38.41270 ? 64  HIS A O   1 
ATOM   487  C CB  . HIS A 1 64  ? -27.19350 7.61037   -18.56161 1.000 38.89206 ? 64  HIS A CB  1 
ATOM   488  C CG  . HIS A 1 64  ? -28.18172 8.57031   -19.14783 1.000 39.87509 ? 64  HIS A CG  1 
ATOM   489  N ND1 . HIS A 1 64  ? -29.46021 8.19205   -19.49817 1.000 44.34515 ? 64  HIS A ND1 1 
ATOM   490  C CD2 . HIS A 1 64  ? -28.07447 9.88057   -19.47506 1.000 35.69152 ? 64  HIS A CD2 1 
ATOM   491  C CE1 . HIS A 1 64  ? -30.10325 9.23013   -20.00170 1.000 38.24746 ? 64  HIS A CE1 1 
ATOM   492  N NE2 . HIS A 1 64  ? -29.28754 10.26929  -19.99310 1.000 40.35949 ? 64  HIS A NE2 1 
ATOM   493  N N   . ASN A 1 65  ? -26.89529 10.12739  -16.22742 1.000 33.00979 ? 65  ASN A N   1 
ATOM   494  C CA  . ASN A 1 65  ? -26.19312 11.35656  -15.88382 1.000 38.77758 ? 65  ASN A CA  1 
ATOM   495  C C   . ASN A 1 65  ? -25.20265 11.15199  -14.73833 1.000 36.09619 ? 65  ASN A C   1 
ATOM   496  O O   . ASN A 1 65  ? -24.31040 11.98582  -14.55248 1.000 40.56477 ? 65  ASN A O   1 
ATOM   497  C CB  . ASN A 1 65  ? -27.17709 12.46753  -15.50434 1.000 36.45342 ? 65  ASN A CB  1 
ATOM   498  C CG  . ASN A 1 65  ? -28.18907 12.74509  -16.57753 1.000 42.32650 ? 65  ASN A CG  1 
ATOM   499  O OD1 . ASN A 1 65  ? -29.38502 12.85643  -16.30457 1.000 40.79240 ? 65  ASN A OD1 1 
ATOM   500  N ND2 . ASN A 1 65  ? -27.72184 12.86605  -17.81313 1.000 36.51463 ? 65  ASN A ND2 1 
ATOM   501  N N   . PHE A 1 66  ? -25.33620 10.07269  -13.96902 1.000 34.42450 ? 66  PHE A N   1 
ATOM   502  C CA  . PHE A 1 66  ? -24.44298 9.80843   -12.84237 1.000 36.00092 ? 66  PHE A CA  1 
ATOM   503  C C   . PHE A 1 66  ? -23.24194 8.99863   -13.31226 1.000 32.82785 ? 66  PHE A C   1 
ATOM   504  O O   . PHE A 1 66  ? -23.39622 7.85532   -13.74582 1.000 37.49560 ? 66  PHE A O   1 
ATOM   505  C CB  . PHE A 1 66  ? -25.16238 9.04760   -11.73306 1.000 31.42314 ? 66  PHE A CB  1 
ATOM   506  C CG  . PHE A 1 66  ? -26.23052 9.83702   -11.04543 1.000 30.98307 ? 66  PHE A CG  1 
ATOM   507  C CD1 . PHE A 1 66  ? -25.89761 10.82928  -10.13678 1.000 31.96250 ? 66  PHE A CD1 1 
ATOM   508  C CD2 . PHE A 1 66  ? -27.56420 9.56373   -11.27949 1.000 27.79634 ? 66  PHE A CD2 1 
ATOM   509  C CE1 . PHE A 1 66  ? -26.87180 11.54905  -9.48260  1.000 35.60856 ? 66  PHE A CE1 1 
ATOM   510  C CE2 . PHE A 1 66  ? -28.55109 10.28303  -10.63518 1.000 34.98097 ? 66  PHE A CE2 1 
ATOM   511  C CZ  . PHE A 1 66  ? -28.20390 11.28292  -9.73402  1.000 32.97282 ? 66  PHE A CZ  1 
ATOM   512  N N   . LEU A 1 67  ? -22.04794 9.57353   -13.19055 1.000 29.45632 ? 67  LEU A N   1 
ATOM   513  C CA  . LEU A 1 67  ? -20.80605 8.88095   -13.51603 1.000 29.61241 ? 67  LEU A CA  1 
ATOM   514  C C   . LEU A 1 67  ? -20.13823 8.44309   -12.21220 1.000 32.34911 ? 67  LEU A C   1 
ATOM   515  O O   . LEU A 1 67  ? -19.63240 9.27949   -11.45547 1.000 32.43196 ? 67  LEU A O   1 
ATOM   516  C CB  . LEU A 1 67  ? -19.89179 9.78803   -14.33537 1.000 33.92628 ? 67  LEU A CB  1 
ATOM   517  C CG  . LEU A 1 67  ? -18.49813 9.25523   -14.66762 1.000 40.85622 ? 67  LEU A CG  1 
ATOM   518  C CD1 . LEU A 1 67  ? -18.57874 7.85631   -15.28316 1.000 48.75354 ? 67  LEU A CD1 1 
ATOM   519  C CD2 . LEU A 1 67  ? -17.79473 10.22778  -15.61301 1.000 46.38597 ? 67  LEU A CD2 1 
ATOM   520  N N   . VAL A 1 68  ? -20.13994 7.13787   -11.95664 1.000 31.79091 ? 68  VAL A N   1 
ATOM   521  C CA  . VAL A 1 68  ? -19.54470 6.54037   -10.76401 1.000 29.89138 ? 68  VAL A CA  1 
ATOM   522  C C   . VAL A 1 68  ? -18.29417 5.79272   -11.19924 1.000 33.71229 ? 68  VAL A C   1 
ATOM   523  O O   . VAL A 1 68  ? -18.35622 4.93748   -12.09263 1.000 33.82264 ? 68  VAL A O   1 
ATOM   524  C CB  . VAL A 1 68  ? -20.53398 5.59186   -10.06304 1.000 33.12512 ? 68  VAL A CB  1 
ATOM   525  C CG1 . VAL A 1 68  ? -19.86696 4.84859   -8.91054  1.000 25.92663 ? 68  VAL A CG1 1 
ATOM   526  C CG2 . VAL A 1 68  ? -21.76068 6.35819   -9.57014  1.000 27.59998 ? 68  VAL A CG2 1 
ATOM   527  N N   . GLN A 1 69  ? -17.16250 6.11279   -10.57868 1.000 29.68165 ? 69  GLN A N   1 
ATOM   528  C CA  . GLN A 1 69  ? -15.88489 5.49652   -10.91412 1.000 28.49883 ? 69  GLN A CA  1 
ATOM   529  C C   . GLN A 1 69  ? -15.29413 4.84940   -9.66878  1.000 30.50635 ? 69  GLN A C   1 
ATOM   530  O O   . GLN A 1 69  ? -15.09740 5.51868   -8.64571  1.000 27.59212 ? 69  GLN A O   1 
ATOM   531  C CB  . GLN A 1 69  ? -14.92030 6.52685   -11.50347 1.000 30.74754 ? 69  GLN A CB  1 
ATOM   532  N N   . ALA A 1 70  ? -15.03607 3.54616   -9.74930  1.000 33.16812 ? 70  ALA A N   1 
ATOM   533  C CA  . ALA A 1 70  ? -14.30051 2.81502   -8.72261  1.000 38.84264 ? 70  ALA A CA  1 
ATOM   534  C C   . ALA A 1 70  ? -12.93995 2.47183   -9.31521  1.000 42.57853 ? 70  ALA A C   1 
ATOM   535  O O   . ALA A 1 70  ? -12.85082 1.70398   -10.28088 1.000 40.34145 ? 70  ALA A O   1 
ATOM   536  C CB  . ALA A 1 70  ? -15.05106 1.56076   -8.27715  1.000 34.18268 ? 70  ALA A CB  1 
ATOM   537  N N   . GLY A 1 71  ? -11.89429 3.04876   -8.75233  1.000 40.64645 ? 71  GLY A N   1 
ATOM   538  C CA  . GLY A 1 71  ? -10.58444 2.91503   -9.36279  1.000 41.78178 ? 71  GLY A CA  1 
ATOM   539  C C   . GLY A 1 71  ? -10.61544 3.50912   -10.75456 1.000 47.65260 ? 71  GLY A C   1 
ATOM   540  O O   . GLY A 1 71  ? -10.97034 4.68030   -10.95054 1.000 51.19513 ? 71  GLY A O   1 
ATOM   541  N N   . ASN A 1 72  ? -10.25627 2.69729   -11.74682 1.000 51.33794 ? 72  ASN A N   1 
ATOM   542  C CA  . ASN A 1 72  ? -10.29383 3.10512   -13.14346 1.000 51.59765 ? 72  ASN A CA  1 
ATOM   543  C C   . ASN A 1 72  ? -11.50616 2.55893   -13.87525 1.000 49.70206 ? 72  ASN A C   1 
ATOM   544  O O   . ASN A 1 72  ? -11.59904 2.71825   -15.09437 1.000 58.04935 ? 72  ASN A O   1 
ATOM   545  C CB  . ASN A 1 72  ? -9.01788  2.65990   -13.86283 1.000 47.82521 ? 72  ASN A CB  1 
ATOM   546  N N   . VAL A 1 73  ? -12.43525 1.92304   -13.16682 1.000 38.39643 ? 73  VAL A N   1 
ATOM   547  C CA  . VAL A 1 73  ? -13.57104 1.24285   -13.77697 1.000 36.98666 ? 73  VAL A CA  1 
ATOM   548  C C   . VAL A 1 73  ? -14.84410 2.01622   -13.46270 1.000 39.50252 ? 73  VAL A C   1 
ATOM   549  O O   . VAL A 1 73  ? -15.05333 2.45475   -12.32565 1.000 39.66366 ? 73  VAL A O   1 
ATOM   550  C CB  . VAL A 1 73  ? -13.66987 -0.21554  -13.28454 1.000 39.77015 ? 73  VAL A CB  1 
ATOM   551  C CG1 . VAL A 1 73  ? -14.91803 -0.87799  -13.82214 1.000 38.46558 ? 73  VAL A CG1 1 
ATOM   552  C CG2 . VAL A 1 73  ? -12.44215 -0.99301  -13.71293 1.000 42.30922 ? 73  VAL A CG2 1 
ATOM   553  N N   . GLN A 1 74  ? -15.68872 2.19564   -14.47503 1.000 39.08144 ? 74  GLN A N   1 
ATOM   554  C CA  . GLN A 1 74  ? -16.98399 2.83720   -14.29569 1.000 31.88756 ? 74  GLN A CA  1 
ATOM   555  C C   . GLN A 1 74  ? -18.01130 1.80731   -13.84683 1.000 39.40266 ? 74  GLN A C   1 
ATOM   556  O O   . GLN A 1 74  ? -18.06486 0.69623   -14.38172 1.000 39.51149 ? 74  GLN A O   1 
ATOM   557  C CB  . GLN A 1 74  ? -17.46016 3.49317   -15.59282 1.000 39.98346 ? 74  GLN A CB  1 
ATOM   558  C CG  . GLN A 1 74  ? -16.59096 4.61869   -16.09657 1.000 46.58926 ? 74  GLN A CG  1 
ATOM   559  C CD  . GLN A 1 74  ? -17.27060 5.41828   -17.19860 1.000 66.46644 ? 74  GLN A CD  1 
ATOM   560  O OE1 . GLN A 1 74  ? -18.48878 5.32037   -17.39906 1.000 58.79269 ? 74  GLN A OE1 1 
ATOM   561  N NE2 . GLN A 1 74  ? -16.48491 6.21171   -17.92335 1.000 70.44841 ? 74  GLN A NE2 1 
ATOM   562  N N   . LEU A 1 75  ? -18.82858 2.18061   -12.86630 1.000 30.15264 ? 75  LEU A N   1 
ATOM   563  C CA  . LEU A 1 75  ? -19.96416 1.37443   -12.44641 1.000 26.79842 ? 75  LEU A CA  1 
ATOM   564  C C   . LEU A 1 75  ? -21.22871 1.94006   -13.08327 1.000 40.45431 ? 75  LEU A C   1 
ATOM   565  O O   . LEU A 1 75  ? -21.38882 3.16073   -13.18224 1.000 39.99415 ? 75  LEU A O   1 
ATOM   566  C CB  . LEU A 1 75  ? -20.09996 1.35844   -10.91896 1.000 30.68125 ? 75  LEU A CB  1 
ATOM   567  C CG  . LEU A 1 75  ? -18.85813 1.03301   -10.07447 1.000 28.02450 ? 75  LEU A CG  1 
ATOM   568  C CD1 . LEU A 1 75  ? -19.20427 1.03173   -8.60026  1.000 29.41267 ? 75  LEU A CD1 1 
ATOM   569  C CD2 . LEU A 1 75  ? -18.24399 -0.29011  -10.46669 1.000 32.43198 ? 75  LEU A CD2 1 
ATOM   570  N N   . ARG A 1 76  ? -22.12518 1.05421   -13.52141 1.000 32.01253 ? 76  ARG A N   1 
ATOM   571  C CA  . ARG A 1 76  ? -23.36423 1.48140   -14.16368 1.000 36.51132 ? 76  ARG A CA  1 
ATOM   572  C C   . ARG A 1 76  ? -24.45031 1.67950   -13.11236 1.000 32.49417 ? 76  ARG A C   1 
ATOM   573  O O   . ARG A 1 76  ? -24.82818 0.73310   -12.41017 1.000 29.23735 ? 76  ARG A O   1 
ATOM   574  C CB  . ARG A 1 76  ? -23.83213 0.47482   -15.21668 1.000 37.66774 ? 76  ARG A CB  1 
ATOM   575  C CG  . ARG A 1 76  ? -24.94319 1.03632   -16.10888 1.000 46.33999 ? 76  ARG A CG  1 
ATOM   576  C CD  . ARG A 1 76  ? -25.23247 0.15764   -17.32392 1.000 50.65308 ? 76  ARG A CD  1 
ATOM   577  N NE  . ARG A 1 76  ? -26.10045 -0.96783  -16.99771 1.000 61.60367 ? 76  ARG A NE  1 
ATOM   578  C CZ  . ARG A 1 76  ? -27.42081 -0.95836  -17.13225 1.000 63.83814 ? 76  ARG A CZ  1 
ATOM   579  N NH1 . ARG A 1 76  ? -28.06270 0.10453   -17.59369 1.000 65.03171 ? 76  ARG A NH1 1 
ATOM   580  N NH2 . ARG A 1 76  ? -28.11568 -2.04134  -16.79342 1.000 58.05991 ? 76  ARG A NH2 1 
ATOM   581  N N   . VAL A 1 77  ? -24.95394 2.90830   -13.02677 1.000 33.30820 ? 77  VAL A N   1 
ATOM   582  C CA  . VAL A 1 77  ? -26.08509 3.23569   -12.16948 1.000 32.66810 ? 77  VAL A CA  1 
ATOM   583  C C   . VAL A 1 77  ? -27.36557 2.68323   -12.78359 1.000 31.20386 ? 77  VAL A C   1 
ATOM   584  O O   . VAL A 1 77  ? -27.66227 2.92920   -13.95978 1.000 30.59747 ? 77  VAL A O   1 
ATOM   585  C CB  . VAL A 1 77  ? -26.18020 4.75970   -11.99137 1.000 35.78663 ? 77  VAL A CB  1 
ATOM   586  C CG1 . VAL A 1 77  ? -27.34397 5.13846   -11.08695 1.000 33.35897 ? 77  VAL A CG1 1 
ATOM   587  C CG2 . VAL A 1 77  ? -24.85066 5.32370   -11.47593 1.000 33.23664 ? 77  VAL A CG2 1 
ATOM   588  N N   . ILE A 1 78  ? -28.14713 1.96049   -11.98451 1.000 29.49642 ? 78  ILE A N   1 
ATOM   589  C CA  . ILE A 1 78  ? -29.39877 1.37217   -12.44945 1.000 29.96735 ? 78  ILE A CA  1 
ATOM   590  C C   . ILE A 1 78  ? -30.60732 1.85414   -11.66170 1.000 37.49435 ? 78  ILE A C   1 
ATOM   591  O O   . ILE A 1 78  ? -31.73657 1.43126   -11.95449 1.000 32.35749 ? 78  ILE A O   1 
ATOM   592  C CB  . ILE A 1 78  ? -29.33594 -0.16806  -12.43359 1.000 35.43290 ? 78  ILE A CB  1 
ATOM   593  C CG1 . ILE A 1 78  ? -29.06029 -0.66244  -11.00833 1.000 32.58960 ? 78  ILE A CG1 1 
ATOM   594  C CG2 . ILE A 1 78  ? -28.29280 -0.65325  -13.42602 1.000 34.69388 ? 78  ILE A CG2 1 
ATOM   595  C CD1 . ILE A 1 78  ? -29.08708 -2.16031  -10.84830 1.000 34.95693 ? 78  ILE A CD1 1 
ATOM   596  N N   . GLY A 1 79  ? -30.41056 2.73349   -10.68446 1.000 33.79276 ? 79  GLY A N   1 
ATOM   597  C CA  . GLY A 1 79  ? -31.51093 3.31923   -9.94382  1.000 29.66756 ? 79  GLY A CA  1 
ATOM   598  C C   . GLY A 1 79  ? -30.97060 4.40862   -9.04677  1.000 35.61246 ? 79  GLY A C   1 
ATOM   599  O O   . GLY A 1 79  ? -29.75783 4.51249   -8.83478  1.000 29.05158 ? 79  GLY A O   1 
ATOM   600  N N   . HIS A 1 80  ? -31.87964 5.24506   -8.54902  1.000 33.10724 ? 80  HIS A N   1 
ATOM   601  C CA  . HIS A 1 80  ? -31.45189 6.31888   -7.66026  1.000 33.49300 ? 80  HIS A CA  1 
ATOM   602  C C   . HIS A 1 80  ? -32.64655 6.85111   -6.89248  1.000 37.55764 ? 80  HIS A C   1 
ATOM   603  O O   . HIS A 1 80  ? -33.74172 6.98678   -7.44554  1.000 35.11860 ? 80  HIS A O   1 
ATOM   604  C CB  . HIS A 1 80  ? -30.76014 7.46213   -8.41972  1.000 32.85523 ? 80  HIS A CB  1 
ATOM   605  C CG  . HIS A 1 80  ? -31.64666 8.20322   -9.37596  1.000 34.14962 ? 80  HIS A CG  1 
ATOM   606  N ND1 . HIS A 1 80  ? -31.84780 7.79496   -10.67907 1.000 39.65591 ? 80  HIS A ND1 1 
ATOM   607  C CD2 . HIS A 1 80  ? -32.34895 9.35325   -9.23217  1.000 39.78821 ? 80  HIS A CD2 1 
ATOM   608  C CE1 . HIS A 1 80  ? -32.65683 8.64650   -11.28576 1.000 30.99224 ? 80  HIS A CE1 1 
ATOM   609  N NE2 . HIS A 1 80  ? -32.96868 9.60591   -10.43321 1.000 35.37484 ? 80  HIS A NE2 1 
ATOM   610  N N   . SER A 1 81  ? -32.42138 7.14389   -5.61546  1.000 31.81856 ? 81  SER A N   1 
ATOM   611  C CA  . SER A 1 81  ? -33.43335 7.71771   -4.74333  1.000 36.95451 ? 81  SER A CA  1 
ATOM   612  C C   . SER A 1 81  ? -32.75092 8.71071   -3.81408  1.000 32.52277 ? 81  SER A C   1 
ATOM   613  O O   . SER A 1 81  ? -31.52123 8.81187   -3.77646  1.000 29.03080 ? 81  SER A O   1 
ATOM   614  C CB  . SER A 1 81  ? -34.16527 6.64502   -3.93726  1.000 34.37226 ? 81  SER A CB  1 
ATOM   615  O OG  . SER A 1 81  ? -33.24720 5.93050   -3.14749  1.000 34.11846 ? 81  SER A OG  1 
ATOM   616  N N   . MET A 1 82  ? -33.56148 9.45563   -3.07007  1.000 23.13535 ? 82  MET A N   1 
ATOM   617  C CA  . MET A 1 82  ? -33.06838 10.48366  -2.16612  1.000 28.26025 ? 82  MET A CA  1 
ATOM   618  C C   . MET A 1 82  ? -33.61349 10.22056  -0.77061  1.000 27.19140 ? 82  MET A C   1 
ATOM   619  O O   . MET A 1 82  ? -34.82470 10.05072  -0.59629  1.000 29.79462 ? 82  MET A O   1 
ATOM   620  C CB  . MET A 1 82  ? -33.48294 11.87084  -2.65666  1.000 31.83645 ? 82  MET A CB  1 
ATOM   621  C CG  . MET A 1 82  ? -32.96252 12.99798  -1.81099  1.000 29.40251 ? 82  MET A CG  1 
ATOM   622  S SD  . MET A 1 82  ? -33.14004 14.59738  -2.61073  1.000 30.16684 ? 82  MET A SD  1 
ATOM   623  C CE  . MET A 1 82  ? -34.91261 14.84247  -2.51932  1.000 31.94639 ? 82  MET A CE  1 
ATOM   624  N N   . GLN A 1 83  ? -32.72230 10.14694  0.21389   1.000 28.63543 ? 83  GLN A N   1 
ATOM   625  C CA  . GLN A 1 83  ? -33.11601 10.02159  1.61623   1.000 28.90104 ? 83  GLN A CA  1 
ATOM   626  C C   . GLN A 1 83  ? -32.55784 11.23713  2.34824   1.000 27.88945 ? 83  GLN A C   1 
ATOM   627  O O   . GLN A 1 83  ? -31.35706 11.30615  2.63494   1.000 23.17303 ? 83  GLN A O   1 
ATOM   628  C CB  . GLN A 1 83  ? -32.61972 8.71869   2.23808   1.000 30.23535 ? 83  GLN A CB  1 
ATOM   629  C CG  . GLN A 1 83  ? -32.96166 8.58631   3.72581   1.000 28.16019 ? 83  GLN A CG  1 
ATOM   630  C CD  . GLN A 1 83  ? -32.47808 7.26434   4.32538   1.000 32.03638 ? 83  GLN A CD  1 
ATOM   631  O OE1 . GLN A 1 83  ? -31.78943 6.49177   3.66965   1.000 31.28275 ? 83  GLN A OE1 1 
ATOM   632  N NE2 . GLN A 1 83  ? -32.85339 7.00255   5.56948   1.000 34.39578 ? 83  GLN A NE2 1 
ATOM   633  N N   . ASN A 1 84  ? -33.42424 12.20397  2.62450   1.000 25.80620 ? 84  ASN A N   1 
ATOM   634  C CA  . ASN A 1 84  ? -33.03552 13.46220  3.26980   1.000 26.49035 ? 84  ASN A CA  1 
ATOM   635  C C   . ASN A 1 84  ? -31.93288 14.10107  2.42929   1.000 28.72843 ? 84  ASN A C   1 
ATOM   636  O O   . ASN A 1 84  ? -32.15209 14.32592  1.22630   1.000 23.13585 ? 84  ASN A O   1 
ATOM   637  C CB  . ASN A 1 84  ? -32.69176 13.16867  4.72839   1.000 22.62940 ? 84  ASN A CB  1 
ATOM   638  C CG  . ASN A 1 84  ? -33.86507 12.61437  5.49965   1.000 26.94389 ? 84  ASN A CG  1 
ATOM   639  O OD1 . ASN A 1 84  ? -34.95546 13.19252  5.48450   1.000 26.55525 ? 84  ASN A OD1 1 
ATOM   640  N ND2 . ASN A 1 84  ? -33.66264 11.46991  6.16055   1.000 26.61796 ? 84  ASN A ND2 1 
ATOM   641  N N   . CYS A 1 85  ? -30.76391 14.40903  2.98491   1.000 24.13522 ? 85  CYS A N   1 
ATOM   642  C CA  . CYS A 1 85  ? -29.71021 15.07210  2.22530   1.000 25.52388 ? 85  CYS A CA  1 
ATOM   643  C C   . CYS A 1 85  ? -28.71925 14.09505  1.59960   1.000 26.03274 ? 85  CYS A C   1 
ATOM   644  O O   . CYS A 1 85  ? -27.62655 14.50896  1.18636   1.000 22.88867 ? 85  CYS A O   1 
ATOM   645  C CB  . CYS A 1 85  ? -28.98058 16.08013  3.11560   1.000 27.92794 ? 85  CYS A CB  1 
ATOM   646  S SG  . CYS A 1 85  ? -30.08954 17.33484  3.82704   1.000 23.28047 ? 85  CYS A SG  1 
ATOM   647  N N   . VAL A 1 86  ? -29.07551 12.81690  1.49559   1.000 27.60560 ? 86  VAL A N   1 
ATOM   648  C CA  . VAL A 1 86  ? -28.19343 11.81328  0.91359   1.000 28.56432 ? 86  VAL A CA  1 
ATOM   649  C C   . VAL A 1 86  ? -28.82907 11.20305  -0.33078  1.000 29.33215 ? 86  VAL A C   1 
ATOM   650  O O   . VAL A 1 86  ? -30.02629 10.89115  -0.36193  1.000 25.25259 ? 86  VAL A O   1 
ATOM   651  C CB  . VAL A 1 86  ? -27.84734 10.70890  1.92703   1.000 30.03792 ? 86  VAL A CB  1 
ATOM   652  C CG1 . VAL A 1 86  ? -27.46435 9.44146   1.19409   1.000 33.01011 ? 86  VAL A CG1 1 
ATOM   653  C CG2 . VAL A 1 86  ? -26.72364 11.18433  2.80898   1.000 28.22008 ? 86  VAL A CG2 1 
ATOM   654  N N   . LEU A 1 87  ? -28.00082 10.98651  -1.33615  1.000 27.34267 ? 87  LEU A N   1 
ATOM   655  C CA  . LEU A 1 87  ? -28.39844 10.29623  -2.55221  1.000 27.62335 ? 87  LEU A CA  1 
ATOM   656  C C   . LEU A 1 87  ? -27.95049 8.84085   -2.46234  1.000 29.13545 ? 87  LEU A C   1 
ATOM   657  O O   . LEU A 1 87  ? -26.81875 8.56120   -2.04814  1.000 25.49069 ? 87  LEU A O   1 
ATOM   658  C CB  . LEU A 1 87  ? -27.76727 11.00383  -3.74675  1.000 31.13006 ? 87  LEU A CB  1 
ATOM   659  C CG  . LEU A 1 87  ? -28.21727 10.74465  -5.17300  1.000 33.56967 ? 87  LEU A CG  1 
ATOM   660  C CD1 . LEU A 1 87  ? -29.73719 10.65596  -5.24376  1.000 34.32201 ? 87  LEU A CD1 1 
ATOM   661  C CD2 . LEU A 1 87  ? -27.69490 11.91759  -5.99532  1.000 34.49213 ? 87  LEU A CD2 1 
ATOM   662  N N   . LYS A 1 88  ? -28.83794 7.91586   -2.82445  1.000 24.32504 ? 88  LYS A N   1 
ATOM   663  C CA  . LYS A 1 88  ? -28.50614 6.49696   -2.92352  1.000 23.34826 ? 88  LYS A CA  1 
ATOM   664  C C   . LYS A 1 88  ? -28.56600 6.07355   -4.38712  1.000 34.45207 ? 88  LYS A C   1 
ATOM   665  O O   . LYS A 1 88  ? -29.62549 6.16458   -5.02226  1.000 28.48103 ? 88  LYS A O   1 
ATOM   666  C CB  . LYS A 1 88  ? -29.44689 5.64736   -2.07326  1.000 24.24447 ? 88  LYS A CB  1 
ATOM   667  C CG  . LYS A 1 88  ? -29.33133 5.97291   -0.56981  1.000 30.10725 ? 88  LYS A CG  1 
ATOM   668  C CD  . LYS A 1 88  ? -30.21479 5.09638   0.30302   1.000 32.22348 ? 88  LYS A CD  1 
ATOM   669  C CE  . LYS A 1 88  ? -31.67310 5.46825   0.15907   1.000 36.61883 ? 88  LYS A CE  1 
ATOM   670  N NZ  . LYS A 1 88  ? -32.52665 4.69205   1.09335   1.000 40.33116 ? 88  LYS A NZ  1 
ATOM   671  N N   . LEU A 1 89  ? -27.42048 5.64710   -4.92455  1.000 29.21487 ? 89  LEU A N   1 
ATOM   672  C CA  . LEU A 1 89  ? -27.29602 5.21305   -6.31279  1.000 27.16544 ? 89  LEU A CA  1 
ATOM   673  C C   . LEU A 1 89  ? -27.18392 3.69480   -6.30474  1.000 33.42076 ? 89  LEU A C   1 
ATOM   674  O O   . LEU A 1 89  ? -26.19828 3.14224   -5.80543  1.000 29.36321 ? 89  LEU A O   1 
ATOM   675  C CB  . LEU A 1 89  ? -26.08491 5.85445   -6.99067  1.000 24.09694 ? 89  LEU A CB  1 
ATOM   676  C CG  . LEU A 1 89  ? -26.03481 7.38433   -6.91133  1.000 24.47521 ? 89  LEU A CG  1 
ATOM   677  C CD1 . LEU A 1 89  ? -24.77239 7.92827   -7.54929  1.000 25.60909 ? 89  LEU A CD1 1 
ATOM   678  C CD2 . LEU A 1 89  ? -27.26196 7.98185   -7.58593  1.000 28.76026 ? 89  LEU A CD2 1 
ATOM   679  N N   . LYS A 1 90  ? -28.20006 3.02071   -6.83385  1.000 29.21868 ? 90  LYS A N   1 
ATOM   680  C CA  . LYS A 1 90  ? -28.11076 1.58107   -7.03847  1.000 30.72614 ? 90  LYS A CA  1 
ATOM   681  C C   . LYS A 1 90  ? -27.23114 1.31070   -8.25083  1.000 32.79172 ? 90  LYS A C   1 
ATOM   682  O O   . LYS A 1 90  ? -27.45549 1.88085   -9.32734  1.000 28.34368 ? 90  LYS A O   1 
ATOM   683  C CB  . LYS A 1 90  ? -29.49557 0.97323   -7.24458  1.000 30.24053 ? 90  LYS A CB  1 
ATOM   684  N N   . VAL A 1 91  ? -26.20821 0.47428   -8.06821  1.000 30.82303 ? 91  VAL A N   1 
ATOM   685  C CA  . VAL A 1 91  ? -25.32192 0.07601   -9.15991  1.000 31.54390 ? 91  VAL A CA  1 
ATOM   686  C C   . VAL A 1 91  ? -25.51751 -1.41031  -9.43314  1.000 31.58624 ? 91  VAL A C   1 
ATOM   687  O O   . VAL A 1 91  ? -26.06587 -2.15285  -8.61525  1.000 28.03756 ? 91  VAL A O   1 
ATOM   688  C CB  . VAL A 1 91  ? -23.83784 0.38952   -8.86263  1.000 25.31683 ? 91  VAL A CB  1 
ATOM   689  C CG1 . VAL A 1 91  ? -23.59293 1.88404   -8.99287  1.000 30.31250 ? 91  VAL A CG1 1 
ATOM   690  C CG2 . VAL A 1 91  ? -23.45322 -0.09703  -7.47198  1.000 31.70065 ? 91  VAL A CG2 1 
ATOM   691  N N   . ASP A 1 92  ? -25.04396 -1.85177  -10.59724 1.000 32.13575 ? 92  ASP A N   1 
ATOM   692  C CA  . ASP A 1 92  ? -25.26055 -3.22742  -11.02744 1.000 35.53069 ? 92  ASP A CA  1 
ATOM   693  C C   . ASP A 1 92  ? -24.16390 -4.18553  -10.56359 1.000 43.92134 ? 92  ASP A C   1 
ATOM   694  O O   . ASP A 1 92  ? -24.10940 -5.32199  -11.04385 1.000 46.95837 ? 92  ASP A O   1 
ATOM   695  C CB  . ASP A 1 92  ? -25.40296 -3.28999  -12.55665 1.000 36.16293 ? 92  ASP A CB  1 
ATOM   696  C CG  . ASP A 1 92  ? -24.11155 -2.97549  -13.27810 1.000 43.39929 ? 92  ASP A CG  1 
ATOM   697  O OD1 . ASP A 1 92  ? -23.08286 -2.74727  -12.60423 1.000 44.17386 ? 92  ASP A OD1 1 
ATOM   698  O OD2 . ASP A 1 92  ? -24.12252 -2.95925  -14.52394 1.000 46.15526 ? 92  ASP A OD2 1 
ATOM   699  N N   . THR A 1 93  ? -23.29774 -3.76588  -9.64163  1.000 41.91519 ? 93  THR A N   1 
ATOM   700  C CA  . THR A 1 93  ? -22.24595 -4.63298  -9.12714  1.000 35.19473 ? 93  THR A CA  1 
ATOM   701  C C   . THR A 1 93  ? -22.09045 -4.40909  -7.62710  1.000 36.45759 ? 93  THR A C   1 
ATOM   702  O O   . THR A 1 93  ? -22.08392 -3.26513  -7.16071  1.000 29.91968 ? 93  THR A O   1 
ATOM   703  C CB  . THR A 1 93  ? -20.90794 -4.37927  -9.84999  1.000 42.34412 ? 93  THR A CB  1 
ATOM   704  O OG1 . THR A 1 93  ? -20.52122 -3.01468  -9.67704  1.000 46.52618 ? 93  THR A OG1 1 
ATOM   705  C CG2 . THR A 1 93  ? -21.04055 -4.64618  -11.33988 1.000 48.93028 ? 93  THR A CG2 1 
ATOM   706  N N   . ALA A 1 94  ? -21.97757 -5.50488  -6.87676  1.000 29.87591 ? 94  ALA A N   1 
ATOM   707  C CA  . ALA A 1 94  ? -21.77403 -5.42430  -5.43854  1.000 28.88923 ? 94  ALA A CA  1 
ATOM   708  C C   . ALA A 1 94  ? -20.29972 -5.23158  -5.11109  1.000 36.05682 ? 94  ALA A C   1 
ATOM   709  O O   . ALA A 1 94  ? -19.42467 -5.82094  -5.75085  1.000 30.87909 ? 94  ALA A O   1 
ATOM   710  C CB  . ALA A 1 94  ? -22.28499 -6.68285  -4.73917  1.000 32.93242 ? 94  ALA A CB  1 
ATOM   711  N N   . ASN A 1 95  ? -20.02560 -4.41750  -4.08472  1.000 26.74896 ? 95  ASN A N   1 
ATOM   712  C CA  . ASN A 1 95  ? -18.64024 -4.17746  -3.70476  1.000 24.96875 ? 95  ASN A CA  1 
ATOM   713  C C   . ASN A 1 95  ? -18.08791 -5.37974  -2.95069  1.000 28.77617 ? 95  ASN A C   1 
ATOM   714  O O   . ASN A 1 95  ? -18.51885 -5.66273  -1.82750  1.000 26.37215 ? 95  ASN A O   1 
ATOM   715  C CB  . ASN A 1 95  ? -18.51899 -2.91187  -2.85758  1.000 24.68190 ? 95  ASN A CB  1 
ATOM   716  C CG  . ASN A 1 95  ? -17.07697 -2.59713  -2.49037  1.000 31.64207 ? 95  ASN A CG  1 
ATOM   717  O OD1 . ASN A 1 95  ? -16.14989 -3.31130  -2.89214  1.000 26.99512 ? 95  ASN A OD1 1 
ATOM   718  N ND2 . ASN A 1 95  ? -16.88068 -1.53674  -1.70935  1.000 25.70099 ? 95  ASN A ND2 1 
ATOM   719  N N   . PRO A 1 96  ? -17.11812 -6.09923  -3.52082  1.000 29.33978 ? 96  PRO A N   1 
ATOM   720  C CA  . PRO A 1 96  ? -16.59173 -7.28521  -2.82630  1.000 31.57787 ? 96  PRO A CA  1 
ATOM   721  C C   . PRO A 1 96  ? -15.88617 -6.94934  -1.53344  1.000 34.18598 ? 96  PRO A C   1 
ATOM   722  O O   . PRO A 1 96  ? -15.76359 -7.82308  -0.66288  1.000 33.98798 ? 96  PRO A O   1 
ATOM   723  C CB  . PRO A 1 96  ? -15.62637 -7.89906  -3.84739  1.000 31.45006 ? 96  PRO A CB  1 
ATOM   724  C CG  . PRO A 1 96  ? -15.27280 -6.80586  -4.76015  1.000 29.65720 ? 96  PRO A CG  1 
ATOM   725  C CD  . PRO A 1 96  ? -16.42996 -5.83814  -4.79276  1.000 27.45873 ? 96  PRO A CD  1 
ATOM   726  N N   . LYS A 1 97  ? -15.44030 -5.70635  -1.37627  1.000 29.42919 ? 97  LYS A N   1 
ATOM   727  C CA  . LYS A 1 97  ? -14.74375 -5.24630  -0.19008  1.000 28.10897 ? 97  LYS A CA  1 
ATOM   728  C C   . LYS A 1 97  ? -15.67640 -4.70656  0.88642   1.000 29.83572 ? 97  LYS A C   1 
ATOM   729  O O   . LYS A 1 97  ? -15.18852 -4.16310  1.88113   1.000 33.42427 ? 97  LYS A O   1 
ATOM   730  C CB  . LYS A 1 97  ? -13.73361 -4.16479  -0.56813  1.000 30.63838 ? 97  LYS A CB  1 
ATOM   731  C CG  . LYS A 1 97  ? -12.61764 -4.62895  -1.48570  1.000 35.31033 ? 97  LYS A CG  1 
ATOM   732  C CD  . LYS A 1 97  ? -11.64264 -3.49383  -1.71872  1.000 39.75506 ? 97  LYS A CD  1 
ATOM   733  C CE  . LYS A 1 97  ? -10.47491 -3.92094  -2.58140  1.000 48.51730 ? 97  LYS A CE  1 
ATOM   734  N NZ  . LYS A 1 97  ? -9.76737  -2.72680  -3.13260  1.000 53.84339 ? 97  LYS A NZ  1 
ATOM   735  N N   . THR A 1 98  ? -16.98958 -4.84343  0.72604   1.000 25.44595 ? 98  THR A N   1 
ATOM   736  C CA  . THR A 1 98  ? -17.91699 -4.34377  1.73739   1.000 26.79827 ? 98  THR A CA  1 
ATOM   737  C C   . THR A 1 98  ? -17.62510 -4.96621  3.10324   1.000 29.69147 ? 98  THR A C   1 
ATOM   738  O O   . THR A 1 98  ? -17.67329 -6.19750  3.23752   1.000 29.39411 ? 98  THR A O   1 
ATOM   739  C CB  . THR A 1 98  ? -19.36762 -4.64058  1.35065   1.000 27.48111 ? 98  THR A CB  1 
ATOM   740  O OG1 . THR A 1 98  ? -19.65468 -4.09585  0.05695   1.000 27.01794 ? 98  THR A OG1 1 
ATOM   741  C CG2 . THR A 1 98  ? -20.31513 -4.03561  2.38215   1.000 24.95656 ? 98  THR A CG2 1 
ATOM   742  N N   . PRO A 1 99  ? -17.35449 -4.17494  4.13584   1.000 28.44871 ? 99  PRO A N   1 
ATOM   743  C CA  . PRO A 1 99  ? -17.18282 -4.73955  5.47394   1.000 26.95675 ? 99  PRO A CA  1 
ATOM   744  C C   . PRO A 1 99  ? -18.53530 -4.99414  6.12152   1.000 22.54277 ? 99  PRO A C   1 
ATOM   745  O O   . PRO A 1 99  ? -19.57480 -4.56967  5.63870   1.000 27.09543 ? 99  PRO A O   1 
ATOM   746  C CB  . PRO A 1 99  ? -16.41971 -3.63476  6.21471   1.000 33.89899 ? 99  PRO A CB  1 
ATOM   747  C CG  . PRO A 1 99  ? -16.92896 -2.36211  5.56238   1.000 30.76199 ? 99  PRO A CG  1 
ATOM   748  C CD  . PRO A 1 99  ? -17.20098 -2.70454  4.12691   1.000 30.48796 ? 99  PRO A CD  1 
ATOM   749  N N   . LYS A 1 100 ? -18.50543 -5.66745  7.26033   1.000 29.25317 ? 100 LYS A N   1 
ATOM   750  C CA  . LYS A 1 100 ? -19.66388 -5.61445  8.13548   1.000 30.35643 ? 100 LYS A CA  1 
ATOM   751  C C   . LYS A 1 100 ? -19.81192 -4.17803  8.63790   1.000 32.67572 ? 100 LYS A C   1 
ATOM   752  O O   . LYS A 1 100 ? -18.82304 -3.54364  9.01456   1.000 24.07371 ? 100 LYS A O   1 
ATOM   753  C CB  . LYS A 1 100 ? -19.48996 -6.59461  9.29282   1.000 31.50105 ? 100 LYS A CB  1 
ATOM   754  C CG  . LYS A 1 100 ? -18.76465 -7.87342  8.85225   1.000 41.96561 ? 100 LYS A CG  1 
ATOM   755  C CD  . LYS A 1 100 ? -19.11664 -9.07865  9.70845   1.000 49.83021 ? 100 LYS A CD  1 
ATOM   756  C CE  . LYS A 1 100 ? -18.79912 -8.84331  11.16623  1.000 48.32338 ? 100 LYS A CE  1 
ATOM   757  N NZ  . LYS A 1 100 ? -18.86622 -10.12688 11.92458  1.000 63.10308 ? 100 LYS A NZ  1 
ATOM   758  N N   . TYR A 1 101 ? -21.03293 -3.64760  8.62244   1.000 26.12924 ? 101 TYR A N   1 
ATOM   759  C CA  . TYR A 1 101 ? -21.18509 -2.22992  8.91763   1.000 26.49380 ? 101 TYR A CA  1 
ATOM   760  C C   . TYR A 1 101 ? -22.56369 -1.96386  9.49984   1.000 33.41352 ? 101 TYR A C   1 
ATOM   761  O O   . TYR A 1 101 ? -23.47483 -2.79047  9.39704   1.000 30.29433 ? 101 TYR A O   1 
ATOM   762  C CB  . TYR A 1 101 ? -20.95222 -1.37357  7.65979   1.000 26.94957 ? 101 TYR A CB  1 
ATOM   763  C CG  . TYR A 1 101 ? -22.05161 -1.48698  6.63071   1.000 28.41440 ? 101 TYR A CG  1 
ATOM   764  C CD1 . TYR A 1 101 ? -22.07512 -2.53734  5.72513   1.000 27.51874 ? 101 TYR A CD1 1 
ATOM   765  C CD2 . TYR A 1 101 ? -23.06954 -0.54252  6.57016   1.000 27.21146 ? 101 TYR A CD2 1 
ATOM   766  C CE1 . TYR A 1 101 ? -23.08308 -2.64620  4.77718   1.000 30.20662 ? 101 TYR A CE1 1 
ATOM   767  C CE2 . TYR A 1 101 ? -24.08119 -0.63756  5.63136   1.000 34.69781 ? 101 TYR A CE2 1 
ATOM   768  C CZ  . TYR A 1 101 ? -24.08431 -1.69022  4.73780   1.000 31.63588 ? 101 TYR A CZ  1 
ATOM   769  O OH  . TYR A 1 101 ? -25.09127 -1.78617  3.81731   1.000 40.03449 ? 101 TYR A OH  1 
ATOM   770  N N   . LYS A 1 102 ? -22.68594 -0.80623  10.15617  1.000 28.06212 ? 102 LYS A N   1 
ATOM   771  C CA  . LYS A 1 102 ? -23.97058 -0.26595  10.57773  1.000 27.61048 ? 102 LYS A CA  1 
ATOM   772  C C   . LYS A 1 102 ? -23.93719 1.25162   10.40267  1.000 31.06745 ? 102 LYS A C   1 
ATOM   773  O O   . LYS A 1 102 ? -22.86741 1.86827   10.34951  1.000 22.08074 ? 102 LYS A O   1 
ATOM   774  C CB  . LYS A 1 102 ? -24.28980 -0.64835  12.03167  1.000 31.99998 ? 102 LYS A CB  1 
ATOM   775  N N   . PHE A 1 103 ? -25.11820 1.84926   10.27225  1.000 23.61592 ? 103 PHE A N   1 
ATOM   776  C CA  . PHE A 1 103 ? -25.26079 3.30013   10.27954  1.000 25.24021 ? 103 PHE A CA  1 
ATOM   777  C C   . PHE A 1 103 ? -25.71452 3.74083   11.66616  1.000 32.13670 ? 103 PHE A C   1 
ATOM   778  O O   . PHE A 1 103 ? -26.73090 3.25698   12.17133  1.000 33.96595 ? 103 PHE A O   1 
ATOM   779  C CB  . PHE A 1 103 ? -26.28333 3.78181   9.24762   1.000 27.17058 ? 103 PHE A CB  1 
ATOM   780  C CG  . PHE A 1 103 ? -25.89866 3.53922   7.80461   1.000 22.69800 ? 103 PHE A CG  1 
ATOM   781  C CD1 . PHE A 1 103 ? -24.58705 3.27705   7.44364   1.000 19.97359 ? 103 PHE A CD1 1 
ATOM   782  C CD2 . PHE A 1 103 ? -26.86737 3.60134   6.81266   1.000 23.90241 ? 103 PHE A CD2 1 
ATOM   783  C CE1 . PHE A 1 103 ? -24.24690 3.07017   6.13443   1.000 23.70330 ? 103 PHE A CE1 1 
ATOM   784  C CE2 . PHE A 1 103 ? -26.54107 3.40265   5.49207   1.000 27.24642 ? 103 PHE A CE2 1 
ATOM   785  C CZ  . PHE A 1 103 ? -25.22530 3.12834   5.14922   1.000 26.86693 ? 103 PHE A CZ  1 
ATOM   786  N N   . VAL A 1 104 ? -24.98939 4.67539   12.27268  1.000 25.89495 ? 104 VAL A N   1 
ATOM   787  C CA  . VAL A 1 104 ? -25.37244 5.15455   13.59237  1.000 29.79482 ? 104 VAL A CA  1 
ATOM   788  C C   . VAL A 1 104 ? -25.38679 6.67845   13.59565  1.000 31.80510 ? 104 VAL A C   1 
ATOM   789  O O   . VAL A 1 104 ? -24.75020 7.33815   12.76960  1.000 30.94656 ? 104 VAL A O   1 
ATOM   790  C CB  . VAL A 1 104 ? -24.44482 4.62142   14.70923  1.000 29.78222 ? 104 VAL A CB  1 
ATOM   791  C CG1 . VAL A 1 104 ? -24.35163 3.10966   14.63891  1.000 29.83143 ? 104 VAL A CG1 1 
ATOM   792  C CG2 . VAL A 1 104 ? -23.06990 5.24250   14.60455  1.000 28.75841 ? 104 VAL A CG2 1 
ATOM   793  N N   . ARG A 1 105 ? -26.14153 7.23461   14.53679  1.000 24.53963 ? 105 ARG A N   1 
ATOM   794  C CA  . ARG A 1 105 ? -26.13965 8.66765   14.78780  1.000 26.71932 ? 105 ARG A CA  1 
ATOM   795  C C   . ARG A 1 105 ? -25.50124 8.90542   16.14853  1.000 32.51347 ? 105 ARG A C   1 
ATOM   796  O O   . ARG A 1 105 ? -25.99340 8.39911   17.16120  1.000 29.87941 ? 105 ARG A O   1 
ATOM   797  C CB  . ARG A 1 105 ? -27.55172 9.24770   14.73673  1.000 31.66073 ? 105 ARG A CB  1 
ATOM   798  C CG  . ARG A 1 105 ? -27.55974 10.76999  14.82508  1.000 27.61176 ? 105 ARG A CG  1 
ATOM   799  C CD  . ARG A 1 105 ? -28.91428 11.31844  14.48569  1.000 25.92332 ? 105 ARG A CD  1 
ATOM   800  N NE  . ARG A 1 105 ? -28.97008 12.75604  14.68719  1.000 27.77594 ? 105 ARG A NE  1 
ATOM   801  C CZ  . ARG A 1 105 ? -28.75384 13.66633  13.74439  1.000 34.48705 ? 105 ARG A CZ  1 
ATOM   802  N NH1 . ARG A 1 105 ? -28.41823 13.32337  12.50815  1.000 23.58543 ? 105 ARG A NH1 1 
ATOM   803  N NH2 . ARG A 1 105 ? -28.87716 14.95473  14.05101  1.000 25.84724 ? 105 ARG A NH2 1 
ATOM   804  N N   . ILE A 1 106 ? -24.39866 9.65472   16.17305  1.000 29.10212 ? 106 ILE A N   1 
ATOM   805  C CA  . ILE A 1 106 ? -23.66510 9.84654   17.41269  1.000 26.42278 ? 106 ILE A CA  1 
ATOM   806  C C   . ILE A 1 106 ? -24.19872 11.06242  18.15625  1.000 30.03281 ? 106 ILE A C   1 
ATOM   807  O O   . ILE A 1 106 ? -24.85853 11.94048  17.59523  1.000 28.94664 ? 106 ILE A O   1 
ATOM   808  C CB  . ILE A 1 106 ? -22.14286 9.98237   17.19639  1.000 27.63389 ? 106 ILE A CB  1 
ATOM   809  C CG1 . ILE A 1 106 ? -21.81892 11.13431  16.24490  1.000 27.03085 ? 106 ILE A CG1 1 
ATOM   810  C CG2 . ILE A 1 106 ? -21.53033 8.66341   16.77130  1.000 35.83159 ? 106 ILE A CG2 1 
ATOM   811  C CD1 . ILE A 1 106 ? -20.32933 11.44229  16.20720  1.000 28.02955 ? 106 ILE A CD1 1 
ATOM   812  N N   . GLN A 1 107 ? -23.87461 11.11763  19.45098  1.000 32.45028 ? 107 GLN A N   1 
ATOM   813  C CA  . GLN A 1 107 ? -24.18627 12.21513  20.34374  1.000 33.69844 ? 107 GLN A CA  1 
ATOM   814  C C   . GLN A 1 107 ? -22.99661 13.15867  20.46781  1.000 27.97836 ? 107 GLN A C   1 
ATOM   815  O O   . GLN A 1 107 ? -21.84000 12.73853  20.32950  1.000 29.90059 ? 107 GLN A O   1 
ATOM   816  C CB  . GLN A 1 107 ? -24.55908 11.67905  21.72666  1.000 38.25623 ? 107 GLN A CB  1 
ATOM   817  C CG  . GLN A 1 107 ? -25.59638 10.55516  21.69987  1.000 44.54106 ? 107 GLN A CG  1 
ATOM   818  C CD  . GLN A 1 107 ? -27.02177 11.06838  21.67061  1.000 60.93773 ? 107 GLN A CD  1 
ATOM   819  O OE1 . GLN A 1 107 ? -27.52354 11.49500  20.62918  1.000 71.38107 ? 107 GLN A OE1 1 
ATOM   820  N NE2 . GLN A 1 107 ? -27.68465 11.02975  22.81977  1.000 74.51949 ? 107 GLN A NE2 1 
ATOM   821  N N   . PRO A 1 108 ? -23.24056 14.43505  20.75955  1.000 33.09102 ? 108 PRO A N   1 
ATOM   822  C CA  . PRO A 1 108 ? -22.12843 15.34953  21.03452  1.000 30.29850 ? 108 PRO A CA  1 
ATOM   823  C C   . PRO A 1 108 ? -21.22845 14.79048  22.13115  1.000 34.18140 ? 108 PRO A C   1 
ATOM   824  O O   . PRO A 1 108 ? -21.69580 14.20660  23.10850  1.000 28.77940 ? 108 PRO A O   1 
ATOM   825  C CB  . PRO A 1 108 ? -22.83125 16.63872  21.47840  1.000 33.23575 ? 108 PRO A CB  1 
ATOM   826  C CG  . PRO A 1 108 ? -24.18722 16.54582  20.89790  1.000 37.72370 ? 108 PRO A CG  1 
ATOM   827  C CD  . PRO A 1 108 ? -24.54518 15.08878  20.94543  1.000 37.38831 ? 108 PRO A CD  1 
ATOM   828  N N   . GLY A 1 109 ? -19.91998 14.96832  21.95687  1.000 26.06473 ? 109 GLY A N   1 
ATOM   829  C CA  . GLY A 1 109 ? -18.92967 14.44911  22.85746  1.000 27.18569 ? 109 GLY A CA  1 
ATOM   830  C C   . GLY A 1 109 ? -18.29683 13.14909  22.40256  1.000 28.83590 ? 109 GLY A C   1 
ATOM   831  O O   . GLY A 1 109 ? -17.16513 12.85626  22.79482  1.000 31.23314 ? 109 GLY A O   1 
ATOM   832  N N   . GLN A 1 110 ? -18.99603 12.37001  21.58472  1.000 26.61688 ? 110 GLN A N   1 
ATOM   833  C CA  . GLN A 1 110 ? -18.44264 11.13046  21.07389  1.000 27.33935 ? 110 GLN A CA  1 
ATOM   834  C C   . GLN A 1 110 ? -17.42478 11.42362  19.97926  1.000 21.46389 ? 110 GLN A C   1 
ATOM   835  O O   . GLN A 1 110 ? -17.53404 12.40710  19.24201  1.000 26.23387 ? 110 GLN A O   1 
ATOM   836  C CB  . GLN A 1 110 ? -19.55686 10.22151  20.55589  1.000 31.19067 ? 110 GLN A CB  1 
ATOM   837  C CG  . GLN A 1 110 ? -20.66544 9.99268   21.57712  1.000 35.58002 ? 110 GLN A CG  1 
ATOM   838  C CD  . GLN A 1 110 ? -21.58260 8.82114   21.24432  1.000 47.93789 ? 110 GLN A CD  1 
ATOM   839  O OE1 . GLN A 1 110 ? -22.48178 8.92603   20.39927  1.000 39.72044 ? 110 GLN A OE1 1 
ATOM   840  N NE2 . GLN A 1 110 ? -21.37004 7.69794   21.92740  1.000 50.19394 ? 110 GLN A NE2 1 
ATOM   841  N N   . THR A 1 111 ? -16.42508 10.55763  19.87662  1.000 24.63394 ? 111 THR A N   1 
ATOM   842  C CA  . THR A 1 111 ? -15.34931 10.74130  18.91519  1.000 23.94964 ? 111 THR A CA  1 
ATOM   843  C C   . THR A 1 111 ? -15.51052 9.75602   17.75924  1.000 22.09182 ? 111 THR A C   1 
ATOM   844  O O   . THR A 1 111 ? -16.23386 8.75747   17.85456  1.000 25.38788 ? 111 THR A O   1 
ATOM   845  C CB  . THR A 1 111 ? -13.98515 10.55648  19.58930  1.000 26.23557 ? 111 THR A CB  1 
ATOM   846  O OG1 . THR A 1 111 ? -13.95610 9.28591   20.25856  1.000 26.95580 ? 111 THR A OG1 1 
ATOM   847  C CG2 . THR A 1 111 ? -13.73581 11.66711  20.60608  1.000 26.93733 ? 111 THR A CG2 1 
ATOM   848  N N   . PHE A 1 112 ? -14.81830 10.05278  16.66061  1.000 24.25617 ? 112 PHE A N   1 
ATOM   849  C CA  . PHE A 1 112 ? -14.82703 9.18648   15.48938  1.000 25.06540 ? 112 PHE A CA  1 
ATOM   850  C C   . PHE A 1 112 ? -13.67193 9.56588   14.57506  1.000 20.95269 ? 112 PHE A C   1 
ATOM   851  O O   . PHE A 1 112 ? -13.11904 10.66055  14.67040  1.000 25.16961 ? 112 PHE A O   1 
ATOM   852  C CB  . PHE A 1 112 ? -16.15929 9.27332   14.73699  1.000 21.11453 ? 112 PHE A CB  1 
ATOM   853  C CG  . PHE A 1 112 ? -16.48608 10.65776  14.21106  1.000 23.71920 ? 112 PHE A CG  1 
ATOM   854  C CD1 . PHE A 1 112 ? -17.08079 11.60093  15.03163  1.000 25.57615 ? 112 PHE A CD1 1 
ATOM   855  C CD2 . PHE A 1 112 ? -16.23903 10.99283  12.89450  1.000 21.53308 ? 112 PHE A CD2 1 
ATOM   856  C CE1 . PHE A 1 112 ? -17.39215 12.85944  14.55485  1.000 28.54894 ? 112 PHE A CE1 1 
ATOM   857  C CE2 . PHE A 1 112 ? -16.54101 12.26679  12.41332  1.000 26.14514 ? 112 PHE A CE2 1 
ATOM   858  C CZ  . PHE A 1 112 ? -17.12252 13.18924  13.24714  1.000 29.53776 ? 112 PHE A CZ  1 
ATOM   859  N N   . SER A 1 113 ? -13.31523 8.64430   13.68682  1.000 23.59289 ? 113 SER A N   1 
ATOM   860  C CA  . SER A 1 113 ? -12.25680 8.88037   12.71883  1.000 21.31196 ? 113 SER A CA  1 
ATOM   861  C C   . SER A 1 113 ? -12.85012 9.38359   11.41823  1.000 22.73849 ? 113 SER A C   1 
ATOM   862  O O   . SER A 1 113 ? -13.97042 9.02483   11.04450  1.000 24.31956 ? 113 SER A O   1 
ATOM   863  C CB  . SER A 1 113 ? -11.46865 7.60618   12.42977  1.000 21.49189 ? 113 SER A CB  1 
ATOM   864  O OG  . SER A 1 113 ? -10.95690 7.05482   13.61726  1.000 24.31540 ? 113 SER A OG  1 
ATOM   865  N N   . VAL A 1 114 ? -12.07954 10.19797  10.70971  1.000 21.93950 ? 114 VAL A N   1 
ATOM   866  C CA  . VAL A 1 114 ? -12.48667 10.69510  9.40202   1.000 21.95634 ? 114 VAL A CA  1 
ATOM   867  C C   . VAL A 1 114 ? -11.43387 10.26501  8.39735   1.000 20.98302 ? 114 VAL A C   1 
ATOM   868  O O   . VAL A 1 114 ? -10.23856 10.45310  8.63590   1.000 22.86391 ? 114 VAL A O   1 
ATOM   869  C CB  . VAL A 1 114 ? -12.66023 12.22452  9.41132   1.000 25.64202 ? 114 VAL A CB  1 
ATOM   870  C CG1 . VAL A 1 114 ? -12.75327 12.78199  7.96814   1.000 20.42302 ? 114 VAL A CG1 1 
ATOM   871  C CG2 . VAL A 1 114 ? -13.91383 12.60535  10.21644  1.000 22.28209 ? 114 VAL A CG2 1 
ATOM   872  N N   . LEU A 1 115 ? -11.87343 9.66395   7.29693   1.000 22.87977 ? 115 LEU A N   1 
ATOM   873  C CA  . LEU A 1 115 ? -11.00702 9.37759   6.15663   1.000 21.34008 ? 115 LEU A CA  1 
ATOM   874  C C   . LEU A 1 115 ? -11.28560 10.44925  5.10466   1.000 22.60273 ? 115 LEU A C   1 
ATOM   875  O O   . LEU A 1 115 ? -12.29817 10.39741  4.40688   1.000 21.17376 ? 115 LEU A O   1 
ATOM   876  C CB  . LEU A 1 115 ? -11.27534 7.97947   5.61139   1.000 17.93954 ? 115 LEU A CB  1 
ATOM   877  C CG  . LEU A 1 115 ? -10.45227 7.62739   4.37975   1.000 18.52414 ? 115 LEU A CG  1 
ATOM   878  C CD1 . LEU A 1 115 ? -8.99707  7.44350   4.77792   1.000 22.90592 ? 115 LEU A CD1 1 
ATOM   879  C CD2 . LEU A 1 115 ? -11.00338 6.37377   3.70989   1.000 21.66059 ? 115 LEU A CD2 1 
ATOM   880  N N   . ALA A 1 116 ? -10.40265 11.43834  5.01706   1.000 20.61111 ? 116 ALA A N   1 
ATOM   881  C CA  . ALA A 1 116 ? -10.52984 12.49117  4.02486   1.000 23.56135 ? 116 ALA A CA  1 
ATOM   882  C C   . ALA A 1 116 ? -10.15452 11.96891  2.64219   1.000 25.97418 ? 116 ALA A C   1 
ATOM   883  O O   . ALA A 1 116 ? -9.05808  11.43139  2.44988   1.000 27.42177 ? 116 ALA A O   1 
ATOM   884  C CB  . ALA A 1 116 ? -9.65372  13.68309  4.40291   1.000 24.31009 ? 116 ALA A CB  1 
ATOM   885  N N   . CYS A 1 117 ? -11.06173 12.14562  1.67588   1.000 21.93507 ? 117 CYS A N   1 
ATOM   886  C CA  . CYS A 1 117 ? -10.85492 11.70090  0.30082   1.000 21.90904 ? 117 CYS A CA  1 
ATOM   887  C C   . CYS A 1 117 ? -11.11283 12.82083  -0.70100  1.000 27.73774 ? 117 CYS A C   1 
ATOM   888  O O   . CYS A 1 117 ? -11.85216 13.77424  -0.43644  1.000 22.04384 ? 117 CYS A O   1 
ATOM   889  C CB  . CYS A 1 117 ? -11.77136 10.53466  -0.06588  1.000 25.57271 ? 117 CYS A CB  1 
ATOM   890  S SG  . CYS A 1 117 ? -11.66029 9.15116   1.05448   1.000 29.59555 ? 117 CYS A SG  1 
ATOM   891  N N   . TYR A 1 118 ? -10.50291 12.65802  -1.87983  1.000 26.04602 ? 118 TYR A N   1 
ATOM   892  C CA  . TYR A 1 118 ? -10.64995 13.56823  -3.00826  1.000 26.79682 ? 118 TYR A CA  1 
ATOM   893  C C   . TYR A 1 118 ? -10.68681 12.72605  -4.26952  1.000 25.93179 ? 118 TYR A C   1 
ATOM   894  O O   . TYR A 1 118 ? -9.86237  11.82132  -4.42630  1.000 24.39525 ? 118 TYR A O   1 
ATOM   895  C CB  . TYR A 1 118 ? -9.50091  14.58310  -3.04415  1.000 26.33487 ? 118 TYR A CB  1 
ATOM   896  C CG  . TYR A 1 118 ? -9.51571  15.43727  -1.80169  1.000 29.10803 ? 118 TYR A CG  1 
ATOM   897  C CD1 . TYR A 1 118 ? -8.83967  15.03764  -0.64690  1.000 29.42563 ? 118 TYR A CD1 1 
ATOM   898  C CD2 . TYR A 1 118 ? -10.26890 16.60124  -1.75129  1.000 25.06130 ? 118 TYR A CD2 1 
ATOM   899  C CE1 . TYR A 1 118 ? -8.87694  15.80333  0.50938   1.000 32.36514 ? 118 TYR A CE1 1 
ATOM   900  C CE2 . TYR A 1 118 ? -10.30961 17.38056  -0.59668  1.000 27.75407 ? 118 TYR A CE2 1 
ATOM   901  C CZ  . TYR A 1 118 ? -9.62612  16.97277  0.53129   1.000 28.62987 ? 118 TYR A CZ  1 
ATOM   902  O OH  . TYR A 1 118 ? -9.68554  17.74053  1.67445   1.000 30.52786 ? 118 TYR A OH  1 
ATOM   903  N N   . ASN A 1 119 ? -11.66997 12.98392  -5.13715  1.000 30.98479 ? 119 ASN A N   1 
ATOM   904  C CA  . ASN A 1 119 ? -11.83248 12.21825  -6.37530  1.000 29.09128 ? 119 ASN A CA  1 
ATOM   905  C C   . ASN A 1 119 ? -11.87086 10.71438  -6.10972  1.000 30.64730 ? 119 ASN A C   1 
ATOM   906  O O   . ASN A 1 119 ? -11.29570 9.91110   -6.84696  1.000 30.44260 ? 119 ASN A O   1 
ATOM   907  C CB  . ASN A 1 119 ? -10.72888 12.58264  -7.35877  1.000 34.88456 ? 119 ASN A CB  1 
ATOM   908  C CG  . ASN A 1 119 ? -10.70381 14.05974  -7.64564  1.000 37.15051 ? 119 ASN A CG  1 
ATOM   909  O OD1 . ASN A 1 119 ? -9.71729  14.73693  -7.37719  1.000 49.77384 ? 119 ASN A OD1 1 
ATOM   910  N ND2 . ASN A 1 119 ? -11.80859 14.57946  -8.15390  1.000 39.13800 ? 119 ASN A ND2 1 
ATOM   911  N N   . GLY A 1 120 ? -12.56702 10.32728  -5.04360  1.000 25.24715 ? 120 GLY A N   1 
ATOM   912  C CA  . GLY A 1 120 ? -12.68009 8.93108   -4.67233  1.000 29.72926 ? 120 GLY A CA  1 
ATOM   913  C C   . GLY A 1 120 ? -11.42783 8.29995   -4.10733  1.000 28.08919 ? 120 GLY A C   1 
ATOM   914  O O   . GLY A 1 120 ? -11.42239 7.08638   -3.86966  1.000 31.92840 ? 120 GLY A O   1 
ATOM   915  N N   . SER A 1 121 ? -10.36373 9.06388   -3.89792  1.000 27.12655 ? 121 SER A N   1 
ATOM   916  C CA  . SER A 1 121 ? -9.11207  8.49130   -3.44023  1.000 28.89398 ? 121 SER A CA  1 
ATOM   917  C C   . SER A 1 121 ? -8.79667  8.94143   -2.02269  1.000 25.50211 ? 121 SER A C   1 
ATOM   918  O O   . SER A 1 121 ? -8.86986  10.13918  -1.72539  1.000 26.77224 ? 121 SER A O   1 
ATOM   919  C CB  . SER A 1 121 ? -7.97986  8.88885   -4.38059  1.000 28.52445 ? 121 SER A CB  1 
ATOM   920  O OG  . SER A 1 121 ? -8.19094  8.29311   -5.65303  1.000 49.87317 ? 121 SER A OG  1 
ATOM   921  N N   . PRO A 1 122 ? -8.44987  8.02121   -1.12736  1.000 32.08914 ? 122 PRO A N   1 
ATOM   922  C CA  . PRO A 1 122 ? -8.18282  8.41140   0.26229   1.000 26.53891 ? 122 PRO A CA  1 
ATOM   923  C C   . PRO A 1 122 ? -6.90344  9.21632   0.39453   1.000 29.26982 ? 122 PRO A C   1 
ATOM   924  O O   . PRO A 1 122 ? -5.88195  8.90928   -0.22134  1.000 29.56897 ? 122 PRO A O   1 
ATOM   925  C CB  . PRO A 1 122 ? -8.06759  7.06695   0.98913   1.000 30.73108 ? 122 PRO A CB  1 
ATOM   926  C CG  . PRO A 1 122 ? -7.69483  6.08990   -0.08531  1.000 46.03201 ? 122 PRO A CG  1 
ATOM   927  C CD  . PRO A 1 122 ? -8.42843  6.55741   -1.30233  1.000 29.82873 ? 122 PRO A CD  1 
ATOM   928  N N   . SER A 1 123 ? -6.95262  10.22390  1.25078   1.000 24.14431 ? 123 SER A N   1 
ATOM   929  C CA  . SER A 1 123 ? -5.87808  11.20119  1.36903   1.000 28.44457 ? 123 SER A CA  1 
ATOM   930  C C   . SER A 1 123 ? -5.25665  11.25642  2.76202   1.000 31.51680 ? 123 SER A C   1 
ATOM   931  O O   . SER A 1 123 ? -4.03134  11.36117  2.89530   1.000 22.92961 ? 123 SER A O   1 
ATOM   932  C CB  . SER A 1 123 ? -6.42295  12.58105  0.97058   1.000 29.87987 ? 123 SER A CB  1 
ATOM   933  O OG  . SER A 1 123 ? -5.51203  13.61657  1.29496   1.000 37.77426 ? 123 SER A OG  1 
ATOM   934  N N   . GLY A 1 124 ? -6.06015  11.16970  3.80800   1.000 23.46906 ? 124 GLY A N   1 
ATOM   935  C CA  . GLY A 1 124 ? -5.53264  11.18734  5.16133   1.000 21.08116 ? 124 GLY A CA  1 
ATOM   936  C C   . GLY A 1 124 ? -6.61948  10.75665  6.11423   1.000 25.37671 ? 124 GLY A C   1 
ATOM   937  O O   . GLY A 1 124 ? -7.80330  10.72960  5.75734   1.000 26.97245 ? 124 GLY A O   1 
ATOM   938  N N   . VAL A 1 125 ? -6.20186  10.38451  7.32445   1.000 23.44746 ? 125 VAL A N   1 
ATOM   939  C CA  . VAL A 1 125 ? -7.12943  9.96977   8.36498   1.000 21.20611 ? 125 VAL A CA  1 
ATOM   940  C C   . VAL A 1 125 ? -6.78974  10.75443  9.62492   1.000 26.41957 ? 125 VAL A C   1 
ATOM   941  O O   . VAL A 1 125 ? -5.61321  11.02051  9.90642   1.000 23.76053 ? 125 VAL A O   1 
ATOM   942  C CB  . VAL A 1 125 ? -7.08059  8.43890   8.60516   1.000 27.10322 ? 125 VAL A CB  1 
ATOM   943  C CG1 . VAL A 1 125 ? -5.67407  7.97838   8.96754   1.000 30.20843 ? 125 VAL A CG1 1 
ATOM   944  C CG2 . VAL A 1 125 ? -8.03876  8.04018   9.71273   1.000 30.78492 ? 125 VAL A CG2 1 
ATOM   945  N N   . TYR A 1 126 ? -7.82107  11.17311  10.35513  1.000 19.63169 ? 126 TYR A N   1 
ATOM   946  C CA  . TYR A 1 126 ? -7.60781  11.90552  11.58891  1.000 20.38677 ? 126 TYR A CA  1 
ATOM   947  C C   . TYR A 1 126 ? -8.80049  11.66734  12.50129  1.000 27.29421 ? 126 TYR A C   1 
ATOM   948  O O   . TYR A 1 126 ? -9.85546  11.20748  12.06566  1.000 23.55824 ? 126 TYR A O   1 
ATOM   949  C CB  . TYR A 1 126 ? -7.37508  13.40254  11.34758  1.000 25.69375 ? 126 TYR A CB  1 
ATOM   950  C CG  . TYR A 1 126 ? -8.44436  14.09978  10.54530  1.000 29.59254 ? 126 TYR A CG  1 
ATOM   951  C CD1 . TYR A 1 126 ? -9.57055  14.61736  11.16352  1.000 29.24691 ? 126 TYR A CD1 1 
ATOM   952  C CD2 . TYR A 1 126 ? -8.32412  14.25025  9.16579   1.000 30.83775 ? 126 TYR A CD2 1 
ATOM   953  C CE1 . TYR A 1 126 ? -10.56367 15.25693  10.42293  1.000 30.05874 ? 126 TYR A CE1 1 
ATOM   954  C CE2 . TYR A 1 126 ? -9.29305  14.90328  8.42948   1.000 25.39952 ? 126 TYR A CE2 1 
ATOM   955  C CZ  . TYR A 1 126 ? -10.41553 15.39278  9.05881   1.000 27.98946 ? 126 TYR A CZ  1 
ATOM   956  O OH  . TYR A 1 126 ? -11.38606 16.03851  8.31197   1.000 37.69147 ? 126 TYR A OH  1 
ATOM   957  N N   . GLN A 1 127 ? -8.60681  11.97736  13.78250  1.000 26.00268 ? 127 GLN A N   1 
ATOM   958  C CA  . GLN A 1 127 ? -9.60987  11.77711  14.81674  1.000 27.29713 ? 127 GLN A CA  1 
ATOM   959  C C   . GLN A 1 127 ? -10.29545 13.10402  15.16642  1.000 27.14177 ? 127 GLN A C   1 
ATOM   960  O O   . GLN A 1 127 ? -9.63379  14.13833  15.31572  1.000 25.61663 ? 127 GLN A O   1 
ATOM   961  C CB  . GLN A 1 127 ? -8.93334  11.13624  16.03826  1.000 25.69526 ? 127 GLN A CB  1 
ATOM   962  C CG  . GLN A 1 127 ? -9.85054  10.61571  17.13956  1.000 25.59766 ? 127 GLN A CG  1 
ATOM   963  C CD  . GLN A 1 127 ? -10.59131 9.34366   16.78214  1.000 29.73896 ? 127 GLN A CD  1 
ATOM   964  O OE1 . GLN A 1 127 ? -10.53464 8.87012   15.65498  1.000 25.22335 ? 127 GLN A OE1 1 
ATOM   965  N NE2 . GLN A 1 127 ? -11.29531 8.78116   17.75497  1.000 28.78331 ? 127 GLN A NE2 1 
ATOM   966  N N   . CYS A 1 128 ? -11.63108 13.05842  15.29457  1.000 25.81029 ? 128 CYS A N   1 
ATOM   967  C CA  . CYS A 1 128 ? -12.52523 14.20045  15.49607  1.000 27.13849 ? 128 CYS A CA  1 
ATOM   968  C C   . CYS A 1 128 ? -13.47949 13.90436  16.64365  1.000 26.45810 ? 128 CYS A C   1 
ATOM   969  O O   . CYS A 1 128 ? -13.65080 12.75754  17.04486  1.000 22.88693 ? 128 CYS A O   1 
ATOM   970  C CB  . CYS A 1 128 ? -13.40615 14.48700  14.24848  1.000 27.34966 ? 128 CYS A CB  1 
ATOM   971  S SG  . CYS A 1 128 ? -12.61099 15.27554  12.89927  1.000 51.46493 ? 128 CYS A SG  1 
ATOM   972  N N   . ALA A 1 129 ? -14.19623 14.93168  17.10479  1.000 28.04198 ? 129 ALA A N   1 
ATOM   973  C CA  . ALA A 1 129 ? -15.35697 14.72362  17.96680  1.000 25.60417 ? 129 ALA A CA  1 
ATOM   974  C C   . ALA A 1 129 ? -16.53903 15.56602  17.49485  1.000 27.09909 ? 129 ALA A C   1 
ATOM   975  O O   . ALA A 1 129 ? -16.37625 16.64789  16.91601  1.000 25.15358 ? 129 ALA A O   1 
ATOM   976  C CB  . ALA A 1 129 ? -15.05338 15.04251  19.45701  1.000 26.22163 ? 129 ALA A CB  1 
ATOM   977  N N   . MET A 1 130 ? -17.73854 15.03669  17.72812  1.000 27.80400 ? 130 MET A N   1 
ATOM   978  C CA  . MET A 1 130 ? -18.97071 15.79023  17.52255  1.000 25.26955 ? 130 MET A CA  1 
ATOM   979  C C   . MET A 1 130 ? -19.05498 16.88165  18.58687  1.000 26.35375 ? 130 MET A C   1 
ATOM   980  O O   . MET A 1 130 ? -19.18321 16.57825  19.77848  1.000 23.83761 ? 130 MET A O   1 
ATOM   981  C CB  . MET A 1 130 ? -20.16719 14.84374  17.59355  1.000 28.14695 ? 130 MET A CB  1 
ATOM   982  C CG  . MET A 1 130 ? -21.53173 15.47416  17.29773  1.000 30.41350 ? 130 MET A CG  1 
ATOM   983  S SD  . MET A 1 130 ? -21.58637 16.40330  15.75401  1.000 30.27391 ? 130 MET A SD  1 
ATOM   984  C CE  . MET A 1 130 ? -21.30817 15.10021  14.53614  1.000 25.26236 ? 130 MET A CE  1 
ATOM   985  N N   . ARG A 1 131 ? -18.96538 18.14709  18.17745  1.000 23.15638 ? 131 ARG A N   1 
ATOM   986  C CA  . ARG A 1 131 ? -18.97863 19.23087  19.16038  1.000 21.34564 ? 131 ARG A CA  1 
ATOM   987  C C   . ARG A 1 131 ? -20.35826 19.33171  19.80183  1.000 26.40628 ? 131 ARG A C   1 
ATOM   988  O O   . ARG A 1 131 ? -21.34426 18.82049  19.26614  1.000 25.88846 ? 131 ARG A O   1 
ATOM   989  C CB  . ARG A 1 131 ? -18.61591 20.57095  18.52368  1.000 21.17068 ? 131 ARG A CB  1 
ATOM   990  C CG  . ARG A 1 131 ? -17.23150 20.63737  17.86252  1.000 25.46960 ? 131 ARG A CG  1 
ATOM   991  C CD  . ARG A 1 131 ? -16.11939 20.17357  18.81590  1.000 27.80108 ? 131 ARG A CD  1 
ATOM   992  N NE  . ARG A 1 131 ? -16.11385 20.93404  20.06489  1.000 28.90414 ? 131 ARG A NE  1 
ATOM   993  C CZ  . ARG A 1 131 ? -15.32439 20.67037  21.09359  1.000 29.55541 ? 131 ARG A CZ  1 
ATOM   994  N NH1 . ARG A 1 131 ? -14.41921 19.70548  21.03868  1.000 26.56446 ? 131 ARG A NH1 1 
ATOM   995  N NH2 . ARG A 1 131 ? -15.44270 21.39411  22.20516  1.000 24.83666 ? 131 ARG A NH2 1 
ATOM   996  N N   . PRO A 1 132 ? -20.45412 19.98374  20.96307  1.000 26.76085 ? 132 PRO A N   1 
ATOM   997  C CA  . PRO A 1 132 ? -21.78688 20.23407  21.54117  1.000 27.91431 ? 132 PRO A CA  1 
ATOM   998  C C   . PRO A 1 132 ? -22.68745 21.09533  20.66302  1.000 24.28322 ? 132 PRO A C   1 
ATOM   999  O O   . PRO A 1 132 ? -23.91522 20.96289  20.75081  1.000 27.20276 ? 132 PRO A O   1 
ATOM   1000 C CB  . PRO A 1 132 ? -21.45794 20.91711  22.87794  1.000 26.58025 ? 132 PRO A CB  1 
ATOM   1001 C CG  . PRO A 1 132 ? -20.11415 20.33450  23.24305  1.000 27.36696 ? 132 PRO A CG  1 
ATOM   1002 C CD  . PRO A 1 132 ? -19.37619 20.27573  21.92046  1.000 24.24146 ? 132 PRO A CD  1 
ATOM   1003 N N   . ASN A 1 133 ? -22.13011 21.96882  19.81829  1.000 25.94856 ? 133 ASN A N   1 
ATOM   1004 C CA  . ASN A 1 133 ? -22.92793 22.75072  18.87662  1.000 25.33714 ? 133 ASN A CA  1 
ATOM   1005 C C   . ASN A 1 133 ? -23.10075 22.05573  17.53301  1.000 25.79884 ? 133 ASN A C   1 
ATOM   1006 O O   . ASN A 1 133 ? -23.50518 22.70342  16.55497  1.000 25.02982 ? 133 ASN A O   1 
ATOM   1007 C CB  . ASN A 1 133 ? -22.32422 24.15055  18.67221  1.000 27.94060 ? 133 ASN A CB  1 
ATOM   1008 C CG  . ASN A 1 133 ? -20.99642 24.13448  17.91306  1.000 26.65403 ? 133 ASN A CG  1 
ATOM   1009 O OD1 . ASN A 1 133 ? -20.49743 23.07833  17.51570  1.000 28.44713 ? 133 ASN A OD1 1 
ATOM   1010 N ND2 . ASN A 1 133 ? -20.42995 25.32624  17.69023  1.000 23.18039 ? 133 ASN A ND2 1 
ATOM   1011 N N   . PHE A 1 134 ? -22.78813 20.76445  17.46834  1.000 26.79631 ? 134 PHE A N   1 
ATOM   1012 C CA  . PHE A 1 134 ? -23.03992 19.88218  16.32898  1.000 23.57608 ? 134 PHE A CA  1 
ATOM   1013 C C   . PHE A 1 134 ? -22.18763 20.19537  15.11631  1.000 27.26443 ? 134 PHE A C   1 
ATOM   1014 O O   . PHE A 1 134 ? -22.49168 19.73290  14.01390  1.000 30.07951 ? 134 PHE A O   1 
ATOM   1015 C CB  . PHE A 1 134 ? -24.52831 19.86823  15.96206  1.000 27.88006 ? 134 PHE A CB  1 
ATOM   1016 C CG  . PHE A 1 134 ? -25.35870 19.18936  16.99702  1.000 29.59109 ? 134 PHE A CG  1 
ATOM   1017 C CD1 . PHE A 1 134 ? -25.29846 17.81224  17.14479  1.000 33.67834 ? 134 PHE A CD1 1 
ATOM   1018 C CD2 . PHE A 1 134 ? -26.12644 19.91959  17.87835  1.000 34.79652 ? 134 PHE A CD2 1 
ATOM   1019 C CE1 . PHE A 1 134 ? -26.03721 17.17357  18.12663  1.000 37.91788 ? 134 PHE A CE1 1 
ATOM   1020 C CE2 . PHE A 1 134 ? -26.86828 19.28217  18.85446  1.000 31.12615 ? 134 PHE A CE2 1 
ATOM   1021 C CZ  . PHE A 1 134 ? -26.82042 17.91480  18.97563  1.000 30.52160 ? 134 PHE A CZ  1 
ATOM   1022 N N   . THR A 1 135 ? -21.10611 20.93364  15.28363  1.000 23.19899 ? 135 THR A N   1 
ATOM   1023 C CA  . THR A 1 135 ? -20.10079 21.03264  14.23812  1.000 27.35707 ? 135 THR A CA  1 
ATOM   1024 C C   . THR A 1 135 ? -18.97467 20.04881  14.52702  1.000 28.26423 ? 135 THR A C   1 
ATOM   1025 O O   . THR A 1 135 ? -18.92718 19.40794  15.58133  1.000 30.10358 ? 135 THR A O   1 
ATOM   1026 C CB  . THR A 1 135 ? -19.54476 22.45207  14.14346  1.000 29.30783 ? 135 THR A CB  1 
ATOM   1027 O OG1 . THR A 1 135 ? -18.86659 22.77044  15.36928  1.000 28.21414 ? 135 THR A OG1 1 
ATOM   1028 C CG2 . THR A 1 135 ? -20.68486 23.45453  13.90250  1.000 28.50404 ? 135 THR A CG2 1 
ATOM   1029 N N   . ILE A 1 136 ? -18.05924 19.92109  13.57556  1.000 24.98878 ? 136 ILE A N   1 
ATOM   1030 C CA  . ILE A 1 136 ? -16.82357 19.20153  13.83067  1.000 28.36358 ? 136 ILE A CA  1 
ATOM   1031 C C   . ILE A 1 136 ? -15.66565 20.05234  13.34168  1.000 30.58483 ? 136 ILE A C   1 
ATOM   1032 O O   . ILE A 1 136 ? -15.77932 20.77465  12.34302  1.000 25.95600 ? 136 ILE A O   1 
ATOM   1033 C CB  . ILE A 1 136 ? -16.79888 17.78293  13.20796  1.000 31.81311 ? 136 ILE A CB  1 
ATOM   1034 C CG1 . ILE A 1 136 ? -16.56212 17.80474  11.70445  1.000 29.40698 ? 136 ILE A CG1 1 
ATOM   1035 C CG2 . ILE A 1 136 ? -18.07597 17.01008  13.55284  1.000 26.29189 ? 136 ILE A CG2 1 
ATOM   1036 C CD1 . ILE A 1 136 ? -16.33318 16.40824  11.11388  1.000 26.15741 ? 136 ILE A CD1 1 
ATOM   1037 N N   . LYS A 1 137 ? -14.56128 19.99956  14.08630  1.000 28.06772 ? 137 LYS A N   1 
ATOM   1038 C CA  . LYS A 1 137 ? -13.35550 20.74208  13.74435  1.000 29.57695 ? 137 LYS A CA  1 
ATOM   1039 C C   . LYS A 1 137 ? -12.53305 19.83316  12.84722  1.000 37.83103 ? 137 LYS A C   1 
ATOM   1040 O O   . LYS A 1 137 ? -11.63455 19.10990  13.28084  1.000 38.75985 ? 137 LYS A O   1 
ATOM   1041 C CB  . LYS A 1 137 ? -12.59867 21.16178  14.99857  1.000 29.38330 ? 137 LYS A CB  1 
ATOM   1042 C CG  . LYS A 1 137 ? -13.42174 22.00767  15.95045  1.000 32.93154 ? 137 LYS A CG  1 
ATOM   1043 C CD  . LYS A 1 137 ? -12.64357 22.36171  17.21829  1.000 42.80105 ? 137 LYS A CD  1 
ATOM   1044 C CE  . LYS A 1 137 ? -13.54129 22.97850  18.28249  1.000 48.53978 ? 137 LYS A CE  1 
ATOM   1045 N NZ  . LYS A 1 137 ? -13.84533 24.41937  18.02792  1.000 55.76356 ? 137 LYS A NZ  1 
ATOM   1046 N N   . GLY A 1 138 ? -12.87124 19.85318  11.55954  1.000 30.45614 ? 138 GLY A N   1 
ATOM   1047 C CA  . GLY A 1 138 ? -12.22927 18.99350  10.59808  1.000 32.52474 ? 138 GLY A CA  1 
ATOM   1048 C C   . GLY A 1 138 ? -11.14587 19.71425  9.81601   1.000 34.52926 ? 138 GLY A C   1 
ATOM   1049 O O   . GLY A 1 138 ? -10.81119 20.87266  10.05925  1.000 31.67408 ? 138 GLY A O   1 
ATOM   1050 N N   . SER A 1 139 ? -10.58357 18.97748  8.86454   1.000 30.57527 ? 139 SER A N   1 
ATOM   1051 C CA  . SER A 1 139 ? -9.67741  19.52410  7.85635   1.000 34.08040 ? 139 SER A CA  1 
ATOM   1052 C C   . SER A 1 139 ? -10.18283 18.99592  6.51945   1.000 33.26160 ? 139 SER A C   1 
ATOM   1053 O O   . SER A 1 139 ? -9.94245  17.83389  6.17083   1.000 31.61542 ? 139 SER A O   1 
ATOM   1054 C CB  . SER A 1 139 ? -8.23126  19.11165  8.10386   1.000 32.40110 ? 139 SER A CB  1 
ATOM   1055 O OG  . SER A 1 139 ? -7.92537  19.18137  9.48047   1.000 50.10399 ? 139 SER A OG  1 
ATOM   1056 N N   . PHE A 1 140 ? -10.92182 19.82800  5.80556   1.000 31.25971 ? 140 PHE A N   1 
ATOM   1057 C CA  . PHE A 1 140 ? -11.56156 19.43269  4.55952   1.000 30.45023 ? 140 PHE A CA  1 
ATOM   1058 C C   . PHE A 1 140 ? -11.30586 20.51332  3.52081   1.000 32.80928 ? 140 PHE A C   1 
ATOM   1059 O O   . PHE A 1 140 ? -11.32521 21.70497  3.83970   1.000 33.40730 ? 140 PHE A O   1 
ATOM   1060 C CB  . PHE A 1 140 ? -13.07074 19.22910  4.73980   1.000 25.21839 ? 140 PHE A CB  1 
ATOM   1061 C CG  . PHE A 1 140 ? -13.44319 18.08414  5.64311   1.000 26.44470 ? 140 PHE A CG  1 
ATOM   1062 C CD1 . PHE A 1 140 ? -13.31976 16.76607  5.21214   1.000 28.01110 ? 140 PHE A CD1 1 
ATOM   1063 C CD2 . PHE A 1 140 ? -13.97395 18.32764  6.89577   1.000 24.88026 ? 140 PHE A CD2 1 
ATOM   1064 C CE1 . PHE A 1 140 ? -13.69850 15.70712  6.03019   1.000 28.15446 ? 140 PHE A CE1 1 
ATOM   1065 C CE2 . PHE A 1 140 ? -14.36094 17.27793  7.72580   1.000 24.73702 ? 140 PHE A CE2 1 
ATOM   1066 C CZ  . PHE A 1 140 ? -14.21796 15.96814  7.29499   1.000 27.29515 ? 140 PHE A CZ  1 
ATOM   1067 N N   . LEU A 1 141 ? -11.06029 20.09723  2.28502   1.000 29.01769 ? 141 LEU A N   1 
ATOM   1068 C CA  . LEU A 1 141 ? -10.79862 20.99898  1.17186   1.000 29.59829 ? 141 LEU A CA  1 
ATOM   1069 C C   . LEU A 1 141 ? -11.86178 20.80318  0.09156   1.000 31.35022 ? 141 LEU A C   1 
ATOM   1070 O O   . LEU A 1 141 ? -12.72972 19.93595  0.19708   1.000 30.13091 ? 141 LEU A O   1 
ATOM   1071 C CB  . LEU A 1 141 ? -9.39871  20.75813  0.60550   1.000 29.38358 ? 141 LEU A CB  1 
ATOM   1072 C CG  . LEU A 1 141 ? -8.25395  20.88198  1.60058   1.000 34.69364 ? 141 LEU A CG  1 
ATOM   1073 C CD1 . LEU A 1 141 ? -6.93276  20.59682  0.90947   1.000 43.00604 ? 141 LEU A CD1 1 
ATOM   1074 C CD2 . LEU A 1 141 ? -8.26979  22.27842  2.20567   1.000 37.43142 ? 141 LEU A CD2 1 
ATOM   1075 N N   . ASN A 1 142 ? -11.79340 21.62405  -0.95886  1.000 27.33413 ? 142 ASN A N   1 
ATOM   1076 C CA  . ASN A 1 142 ? -12.66295 21.41686  -2.10856  1.000 31.12807 ? 142 ASN A CA  1 
ATOM   1077 C C   . ASN A 1 142 ? -12.56624 19.96898  -2.57236  1.000 30.61968 ? 142 ASN A C   1 
ATOM   1078 O O   . ASN A 1 142 ? -11.47460 19.39985  -2.66919  1.000 28.50756 ? 142 ASN A O   1 
ATOM   1079 C CB  . ASN A 1 142 ? -12.28898 22.36129  -3.25431  1.000 32.26855 ? 142 ASN A CB  1 
ATOM   1080 C CG  . ASN A 1 142 ? -12.61266 23.81520  -2.95240  1.000 37.59697 ? 142 ASN A CG  1 
ATOM   1081 O OD1 . ASN A 1 142 ? -12.63938 24.23874  -1.79981  1.000 40.37451 ? 142 ASN A OD1 1 
ATOM   1082 N ND2 . ASN A 1 142 ? -12.84940 24.58395  -3.98958  1.000 33.52556 ? 142 ASN A ND2 1 
ATOM   1083 N N   . GLY A 1 143 ? -13.71996 19.37126  -2.84774  1.000 29.87588 ? 143 GLY A N   1 
ATOM   1084 C CA  . GLY A 1 143 ? -13.80033 18.01115  -3.33601  1.000 28.20500 ? 143 GLY A CA  1 
ATOM   1085 C C   . GLY A 1 143 ? -13.88391 16.95799  -2.25509  1.000 32.26168 ? 143 GLY A C   1 
ATOM   1086 O O   . GLY A 1 143 ? -13.95805 15.76018  -2.57840  1.000 26.36007 ? 143 GLY A O   1 
ATOM   1087 N N   . SER A 1 144 ? -13.90385 17.36480  -0.98507  1.000 27.46970 ? 144 SER A N   1 
ATOM   1088 C CA  . SER A 1 144 ? -13.89765 16.42514  0.12409   1.000 27.75074 ? 144 SER A CA  1 
ATOM   1089 C C   . SER A 1 144 ? -15.28160 15.90531  0.47892   1.000 26.58653 ? 144 SER A C   1 
ATOM   1090 O O   . SER A 1 144 ? -15.38131 14.98479  1.29266   1.000 21.85486 ? 144 SER A O   1 
ATOM   1091 C CB  . SER A 1 144 ? -13.28558 17.09657  1.35426   1.000 28.78705 ? 144 SER A CB  1 
ATOM   1092 O OG  . SER A 1 144 ? -14.06796 18.22361  1.72791   1.000 30.30005 ? 144 SER A OG  1 
ATOM   1093 N N   . CYS A 1 145 ? -16.34554 16.48787  -0.06437  1.000 22.63857 ? 145 CYS A N   1 
ATOM   1094 C CA  . CYS A 1 145 ? -17.67707 16.04513  0.33432   1.000 24.61437 ? 145 CYS A CA  1 
ATOM   1095 C C   . CYS A 1 145 ? -17.85841 14.56511  0.02577   1.000 26.56811 ? 145 CYS A C   1 
ATOM   1096 O O   . CYS A 1 145 ? -17.34082 14.04014  -0.96624  1.000 25.54458 ? 145 CYS A O   1 
ATOM   1097 C CB  . CYS A 1 145 ? -18.74946 16.88207  -0.35295  1.000 27.45159 ? 145 CYS A CB  1 
ATOM   1098 S SG  . CYS A 1 145 ? -18.85481 18.55126  0.35175   1.000 26.21707 ? 145 CYS A SG  1 
ATOM   1099 N N   . GLY A 1 146 ? -18.60000 13.88281  0.89727   1.000 22.11153 ? 146 GLY A N   1 
ATOM   1100 C CA  . GLY A 1 146 ? -18.75653 12.45475  0.78687   1.000 24.42096 ? 146 GLY A CA  1 
ATOM   1101 C C   . GLY A 1 146 ? -17.71940 11.65467  1.54061   1.000 20.13334 ? 146 GLY A C   1 
ATOM   1102 O O   . GLY A 1 146 ? -17.88290 10.43445  1.66839   1.000 20.21557 ? 146 GLY A O   1 
ATOM   1103 N N   . SER A 1 147 ? -16.63867 12.28854  1.99797   1.000 23.41717 ? 147 SER A N   1 
ATOM   1104 C CA  . SER A 1 147 ? -15.80490 11.67092  3.02295   1.000 22.91474 ? 147 SER A CA  1 
ATOM   1105 C C   . SER A 1 147 ? -16.65817 11.30510  4.22754   1.000 24.30936 ? 147 SER A C   1 
ATOM   1106 O O   . SER A 1 147 ? -17.58822 12.02770  4.58778   1.000 19.80914 ? 147 SER A O   1 
ATOM   1107 C CB  . SER A 1 147 ? -14.69072 12.62316  3.46296   1.000 22.79113 ? 147 SER A CB  1 
ATOM   1108 O OG  . SER A 1 147 ? -13.81622 12.92290  2.38694   1.000 22.53197 ? 147 SER A OG  1 
ATOM   1109 N N   . VAL A 1 148 ? -16.32090 10.18503  4.88243   1.000 23.90034 ? 148 VAL A N   1 
ATOM   1110 C CA  . VAL A 1 148 ? -17.14904 9.71214   5.98312   1.000 21.84663 ? 148 VAL A CA  1 
ATOM   1111 C C   . VAL A 1 148 ? -16.33518 9.63603   7.26595   1.000 22.58569 ? 148 VAL A C   1 
ATOM   1112 O O   . VAL A 1 148 ? -15.09925 9.54719   7.27023   1.000 21.72994 ? 148 VAL A O   1 
ATOM   1113 C CB  . VAL A 1 148 ? -17.82540 8.34689   5.69171   1.000 23.84195 ? 148 VAL A CB  1 
ATOM   1114 C CG1 . VAL A 1 148 ? -18.72428 8.43428   4.43816   1.000 23.03795 ? 148 VAL A CG1 1 
ATOM   1115 C CG2 . VAL A 1 148 ? -16.78915 7.22696   5.54958   1.000 23.41797 ? 148 VAL A CG2 1 
ATOM   1116 N N   . GLY A 1 149 ? -17.06136 9.67339   8.37508   1.000 20.58725 ? 149 GLY A N   1 
ATOM   1117 C CA  . GLY A 1 149 ? -16.50096 9.39461   9.68497   1.000 23.70963 ? 149 GLY A CA  1 
ATOM   1118 C C   . GLY A 1 149 ? -17.08120 8.10548   10.23630  1.000 24.74101 ? 149 GLY A C   1 
ATOM   1119 O O   . GLY A 1 149 ? -18.21589 7.73585   9.91551   1.000 21.92256 ? 149 GLY A O   1 
ATOM   1120 N N   . PHE A 1 150 ? -16.30810 7.42291   11.08710  1.000 23.99963 ? 150 PHE A N   1 
ATOM   1121 C CA  . PHE A 1 150 ? -16.66239 6.05948   11.46199  1.000 20.27989 ? 150 PHE A CA  1 
ATOM   1122 C C   . PHE A 1 150 ? -15.97224 5.66764   12.75777  1.000 24.27131 ? 150 PHE A C   1 
ATOM   1123 O O   . PHE A 1 150 ? -14.96768 6.26074   13.15640  1.000 20.02997 ? 150 PHE A O   1 
ATOM   1124 C CB  . PHE A 1 150 ? -16.26792 5.06281   10.36768  1.000 19.99503 ? 150 PHE A CB  1 
ATOM   1125 C CG  . PHE A 1 150 ? -14.78909 5.03798   10.08722  1.000 20.42155 ? 150 PHE A CG  1 
ATOM   1126 C CD1 . PHE A 1 150 ? -14.21255 5.99401   9.27017   1.000 23.96528 ? 150 PHE A CD1 1 
ATOM   1127 C CD2 . PHE A 1 150 ? -13.98325 4.07975   10.67300  1.000 22.25035 ? 150 PHE A CD2 1 
ATOM   1128 C CE1 . PHE A 1 150 ? -12.84596 5.98991   9.01773   1.000 26.20009 ? 150 PHE A CE1 1 
ATOM   1129 C CE2 . PHE A 1 150 ? -12.62154 4.05966   10.43267  1.000 24.86274 ? 150 PHE A CE2 1 
ATOM   1130 C CZ  . PHE A 1 150 ? -12.05271 5.02644   9.60000   1.000 25.41546 ? 150 PHE A CZ  1 
ATOM   1131 N N   . ASN A 1 151 ? -16.51973 4.63754   13.39918  1.000 24.26505 ? 151 ASN A N   1 
ATOM   1132 C CA  . ASN A 1 151 ? -15.81747 3.89533   14.43394  1.000 20.58186 ? 151 ASN A CA  1 
ATOM   1133 C C   . ASN A 1 151 ? -15.76243 2.43348   14.01345  1.000 25.38070 ? 151 ASN A C   1 
ATOM   1134 O O   . ASN A 1 151 ? -16.51996 1.99246   13.15169  1.000 27.53503 ? 151 ASN A O   1 
ATOM   1135 C CB  . ASN A 1 151 ? -16.50348 4.02663   15.79927  1.000 23.36686 ? 151 ASN A CB  1 
ATOM   1136 C CG  . ASN A 1 151 ? -16.28325 5.38355   16.42687  1.000 28.45744 ? 151 ASN A CG  1 
ATOM   1137 O OD1 . ASN A 1 151 ? -15.23903 5.63434   17.01745  1.000 34.32852 ? 151 ASN A OD1 1 
ATOM   1138 N ND2 . ASN A 1 151 ? -17.26082 6.27088   16.29143  1.000 28.33254 ? 151 ASN A ND2 1 
ATOM   1139 N N   . ILE A 1 152 ? -14.84857 1.67990   14.61115  1.000 25.37950 ? 152 ILE A N   1 
ATOM   1140 C CA  . ILE A 1 152 ? -14.76743 0.24869   14.35310  1.000 24.27867 ? 152 ILE A CA  1 
ATOM   1141 C C   . ILE A 1 152 ? -14.83585 -0.48371  15.68392  1.000 32.50634 ? 152 ILE A C   1 
ATOM   1142 O O   . ILE A 1 152 ? -14.11317 -0.13662  16.62462  1.000 33.77059 ? 152 ILE A O   1 
ATOM   1143 C CB  . ILE A 1 152 ? -13.49276 -0.11723  13.57548  1.000 27.71572 ? 152 ILE A CB  1 
ATOM   1144 C CG1 . ILE A 1 152 ? -13.40239 0.71285   12.29189  1.000 29.47626 ? 152 ILE A CG1 1 
ATOM   1145 C CG2 . ILE A 1 152 ? -13.50506 -1.60184  13.21603  1.000 32.89623 ? 152 ILE A CG2 1 
ATOM   1146 C CD1 . ILE A 1 152 ? -12.29868 0.27126   11.37864  1.000 31.18837 ? 152 ILE A CD1 1 
ATOM   1147 N N   . ASP A 1 153 ? -15.71812 -1.47929  15.76857  1.000 30.35566 ? 153 ASP A N   1 
ATOM   1148 C CA  . ASP A 1 153 ? -15.83901 -2.33390  16.94685  1.000 34.83913 ? 153 ASP A CA  1 
ATOM   1149 C C   . ASP A 1 153 ? -15.65252 -3.77647  16.49619  1.000 38.65564 ? 153 ASP A C   1 
ATOM   1150 O O   . ASP A 1 153 ? -16.48196 -4.31137  15.75380  1.000 43.34880 ? 153 ASP A O   1 
ATOM   1151 C CB  . ASP A 1 153 ? -17.18637 -2.13458  17.63654  1.000 36.09572 ? 153 ASP A CB  1 
ATOM   1152 N N   . TYR A 1 154 ? -14.55806 -4.39784  16.93248  1.000 44.82201 ? 154 TYR A N   1 
ATOM   1153 C CA  . TYR A 1 154 ? -14.17282 -5.71780  16.44556  1.000 40.31097 ? 154 TYR A CA  1 
ATOM   1154 C C   . TYR A 1 154 ? -13.90323 -5.65497  14.94800  1.000 48.88592 ? 154 TYR A C   1 
ATOM   1155 O O   . TYR A 1 154 ? -12.86856 -5.13528  14.51366  1.000 49.18674 ? 154 TYR A O   1 
ATOM   1156 C CB  . TYR A 1 154 ? -15.25462 -6.75589  16.75863  1.000 41.94794 ? 154 TYR A CB  1 
ATOM   1157 N N   . ASP A 1 155 ? -14.82145 -6.18753  14.14638  1.000 40.35226 ? 155 ASP A N   1 
ATOM   1158 C CA  . ASP A 1 155 ? -14.69758 -6.12062  12.69607  1.000 42.17989 ? 155 ASP A CA  1 
ATOM   1159 C C   . ASP A 1 155 ? -15.83527 -5.33783  12.05135  1.000 40.28366 ? 155 ASP A C   1 
ATOM   1160 O O   . ASP A 1 155 ? -16.02135 -5.42600  10.82953  1.000 39.90125 ? 155 ASP A O   1 
ATOM   1161 C CB  . ASP A 1 155 ? -14.62655 -7.53455  12.11155  1.000 45.24766 ? 155 ASP A CB  1 
ATOM   1162 C CG  . ASP A 1 155 ? -15.82845 -8.37853  12.48892  1.000 50.24662 ? 155 ASP A CG  1 
ATOM   1163 O OD1 . ASP A 1 155 ? -16.44147 -8.09775  13.54455  1.000 49.80530 ? 155 ASP A OD1 1 
ATOM   1164 O OD2 . ASP A 1 155 ? -16.15968 -9.31645  11.73350  1.000 51.43374 ? 155 ASP A OD2 1 
ATOM   1165 N N   . CYS A 1 156 ? -16.59986 -4.57706  12.83099  1.000 34.91623 ? 156 CYS A N   1 
ATOM   1166 C CA  . CYS A 1 156 ? -17.80173 -3.91469  12.34461  1.000 32.28991 ? 156 CYS A CA  1 
ATOM   1167 C C   . CYS A 1 156 ? -17.55880 -2.40828  12.28646  1.000 28.52940 ? 156 CYS A C   1 
ATOM   1168 O O   . CYS A 1 156 ? -17.19461 -1.79501  13.29666  1.000 27.22971 ? 156 CYS A O   1 
ATOM   1169 C CB  . CYS A 1 156 ? -18.99283 -4.24760  13.24079  1.000 33.55460 ? 156 CYS A CB  1 
ATOM   1170 S SG  . CYS A 1 156 ? -20.53794 -3.46054  12.75506  1.000 42.07743 ? 156 CYS A SG  1 
ATOM   1171 N N   . VAL A 1 157 ? -17.77126 -1.82537  11.11241  1.000 27.07817 ? 157 VAL A N   1 
ATOM   1172 C CA  . VAL A 1 157 ? -17.63790 -0.38518  10.89841  1.000 27.12171 ? 157 VAL A CA  1 
ATOM   1173 C C   . VAL A 1 157 ? -18.97272 0.28021   11.20120  1.000 28.31514 ? 157 VAL A C   1 
ATOM   1174 O O   . VAL A 1 157 ? -19.99361 -0.08134  10.61496  1.000 27.15738 ? 157 VAL A O   1 
ATOM   1175 C CB  . VAL A 1 157 ? -17.20581 -0.07565  9.46010   1.000 22.35644 ? 157 VAL A CB  1 
ATOM   1176 C CG1 . VAL A 1 157 ? -17.08119 1.44720   9.26353   1.000 24.10522 ? 157 VAL A CG1 1 
ATOM   1177 C CG2 . VAL A 1 157 ? -15.90082 -0.77876  9.13899   1.000 29.72693 ? 157 VAL A CG2 1 
ATOM   1178 N N   . SER A 1 158 ? -18.97282 1.24953   12.11425  1.000 23.78913 ? 158 SER A N   1 
ATOM   1179 C CA  . SER A 1 158 ? -20.15787 2.06302   12.38224  1.000 24.36650 ? 158 SER A CA  1 
ATOM   1180 C C   . SER A 1 158 ? -19.96166 3.40251   11.67679  1.000 21.11534 ? 158 SER A C   1 
ATOM   1181 O O   . SER A 1 158 ? -19.19462 4.23951   12.14391  1.000 24.41252 ? 158 SER A O   1 
ATOM   1182 C CB  . SER A 1 158 ? -20.34675 2.26767   13.88780  1.000 27.43630 ? 158 SER A CB  1 
ATOM   1183 O OG  . SER A 1 158 ? -20.84847 1.10845   14.51661  1.000 31.20018 ? 158 SER A OG  1 
ATOM   1184 N N   . PHE A 1 159 ? -20.63598 3.60907   10.54264  1.000 23.55087 ? 159 PHE A N   1 
ATOM   1185 C CA  . PHE A 1 159 ? -20.56663 4.90279   9.87557   1.000 19.82623 ? 159 PHE A CA  1 
ATOM   1186 C C   . PHE A 1 159 ? -21.47276 5.89003   10.59674  1.000 21.62467 ? 159 PHE A C   1 
ATOM   1187 O O   . PHE A 1 159 ? -22.65479 5.60777   10.81882  1.000 23.07512 ? 159 PHE A O   1 
ATOM   1188 C CB  . PHE A 1 159 ? -20.97860 4.77596   8.40330   1.000 24.12079 ? 159 PHE A CB  1 
ATOM   1189 C CG  . PHE A 1 159 ? -20.06287 3.89827   7.59625   1.000 25.17108 ? 159 PHE A CG  1 
ATOM   1190 C CD1 . PHE A 1 159 ? -18.82594 4.36541   7.19514   1.000 22.09999 ? 159 PHE A CD1 1 
ATOM   1191 C CD2 . PHE A 1 159 ? -20.43599 2.60235   7.25165   1.000 28.41668 ? 159 PHE A CD2 1 
ATOM   1192 C CE1 . PHE A 1 159 ? -17.97975 3.56712   6.45735   1.000 19.10876 ? 159 PHE A CE1 1 
ATOM   1193 C CE2 . PHE A 1 159 ? -19.59328 1.79256   6.50379   1.000 23.07375 ? 159 PHE A CE2 1 
ATOM   1194 C CZ  . PHE A 1 159 ? -18.35764 2.28008   6.11169   1.000 23.18388 ? 159 PHE A CZ  1 
ATOM   1195 N N   . CYS A 1 160 ? -20.91822 7.03291   10.99022  1.000 24.05199 ? 160 CYS A N   1 
ATOM   1196 C CA  . CYS A 1 160 ? -21.68631 8.02387   11.73561  1.000 24.51079 ? 160 CYS A CA  1 
ATOM   1197 C C   . CYS A 1 160 ? -21.74171 9.40340   11.08044  1.000 28.34897 ? 160 CYS A C   1 
ATOM   1198 O O   . CYS A 1 160 ? -22.55170 10.23873  11.50829  1.000 22.67085 ? 160 CYS A O   1 
ATOM   1199 C CB  . CYS A 1 160 ? -21.11788 8.15963   13.16184  1.000 21.51040 ? 160 CYS A CB  1 
ATOM   1200 S SG  . CYS A 1 160 ? -19.37819 8.69598   13.21991  1.000 23.74822 ? 160 CYS A SG  1 
ATOM   1201 N N   . TYR A 1 161 ? -20.93603 9.67196   10.05373  1.000 20.38621 ? 161 TYR A N   1 
ATOM   1202 C CA  . TYR A 1 161 ? -20.86342 11.02539  9.51750   1.000 22.15004 ? 161 TYR A CA  1 
ATOM   1203 C C   . TYR A 1 161 ? -20.55084 10.98912  8.02543   1.000 20.07972 ? 161 TYR A C   1 
ATOM   1204 O O   . TYR A 1 161 ? -19.78965 10.13409  7.55862   1.000 22.31253 ? 161 TYR A O   1 
ATOM   1205 C CB  . TYR A 1 161 ? -19.79821 11.84804  10.27931  1.000 19.01031 ? 161 TYR A CB  1 
ATOM   1206 C CG  . TYR A 1 161 ? -19.55767 13.27295  9.76901   1.000 19.60061 ? 161 TYR A CG  1 
ATOM   1207 C CD1 . TYR A 1 161 ? -20.32940 14.34092  10.22211  1.000 20.80342 ? 161 TYR A CD1 1 
ATOM   1208 C CD2 . TYR A 1 161 ? -18.53357 13.55244  8.86513   1.000 20.95685 ? 161 TYR A CD2 1 
ATOM   1209 C CE1 . TYR A 1 161 ? -20.10501 15.64101  9.76628   1.000 21.14731 ? 161 TYR A CE1 1 
ATOM   1210 C CE2 . TYR A 1 161 ? -18.30456 14.85204  8.40892   1.000 20.33780 ? 161 TYR A CE2 1 
ATOM   1211 C CZ  . TYR A 1 161 ? -19.08957 15.88119  8.86116   1.000 20.43353 ? 161 TYR A CZ  1 
ATOM   1212 O OH  . TYR A 1 161 ? -18.85277 17.15915  8.42236   1.000 22.10528 ? 161 TYR A OH  1 
ATOM   1213 N N   . MET A 1 162 ? -21.15805 11.90254  7.27515   1.000 20.74166 ? 162 MET A N   1 
ATOM   1214 C CA  . MET A 1 162 ? -20.74700 12.16418  5.89950   1.000 19.41020 ? 162 MET A CA  1 
ATOM   1215 C C   . MET A 1 162 ? -20.58387 13.67127  5.73981   1.000 20.30745 ? 162 MET A C   1 
ATOM   1216 O O   . MET A 1 162 ? -21.44121 14.44148  6.17537   1.000 21.99178 ? 162 MET A O   1 
ATOM   1217 C CB  . MET A 1 162 ? -21.75090 11.60402  4.87679   1.000 21.13818 ? 162 MET A CB  1 
ATOM   1218 C CG  . MET A 1 162 ? -21.41400 11.98943  3.42467   1.000 23.19709 ? 162 MET A CG  1 
ATOM   1219 S SD  . MET A 1 162 ? -22.36795 11.06481  2.20494   1.000 25.98077 ? 162 MET A SD  1 
ATOM   1220 C CE  . MET A 1 162 ? -21.42081 9.54418   2.09491   1.000 31.74439 ? 162 MET A CE  1 
ATOM   1221 N N   . HIS A 1 163 ? -19.48461 14.09692  5.13162   1.000 19.41236 ? 163 HIS A N   1 
ATOM   1222 C CA  . HIS A 1 163 ? -19.16270 15.51515  5.07517   1.000 18.98482 ? 163 HIS A CA  1 
ATOM   1223 C C   . HIS A 1 163 ? -19.93099 16.25567  3.97311   1.000 25.18558 ? 163 HIS A C   1 
ATOM   1224 O O   . HIS A 1 163 ? -19.99981 15.79588  2.83223   1.000 20.37341 ? 163 HIS A O   1 
ATOM   1225 C CB  . HIS A 1 163 ? -17.65615 15.67433  4.86429   1.000 20.52748 ? 163 HIS A CB  1 
ATOM   1226 C CG  . HIS A 1 163 ? -17.22704 17.09744  4.88817   1.000 19.00315 ? 163 HIS A CG  1 
ATOM   1227 N ND1 . HIS A 1 163 ? -17.56207 17.93762  5.92575   1.000 20.23874 ? 163 HIS A ND1 1 
ATOM   1228 C CD2 . HIS A 1 163 ? -16.59813 17.86046  3.96836   1.000 21.16191 ? 163 HIS A CD2 1 
ATOM   1229 C CE1 . HIS A 1 163 ? -17.10604 19.14906  5.66910   1.000 21.27835 ? 163 HIS A CE1 1 
ATOM   1230 N NE2 . HIS A 1 163 ? -16.53459 19.13486  4.47864   1.000 23.89417 ? 163 HIS A NE2 1 
ATOM   1231 N N   . HIS A 1 164 ? -20.47150 17.44804  4.30648   1.000 23.66240 ? 164 HIS A N   1 
ATOM   1232 C CA  . HIS A 1 164 ? -21.21856 18.29777  3.36350   1.000 24.07669 ? 164 HIS A CA  1 
ATOM   1233 C C   . HIS A 1 164 ? -20.68466 19.71614  3.17036   1.000 24.35019 ? 164 HIS A C   1 
ATOM   1234 O O   . HIS A 1 164 ? -20.73709 20.22561  2.04912   1.000 24.31766 ? 164 HIS A O   1 
ATOM   1235 C CB  . HIS A 1 164 ? -22.70974 18.40424  3.78520   1.000 18.23681 ? 164 HIS A CB  1 
ATOM   1236 C CG  . HIS A 1 164 ? -23.48399 17.14816  3.55694   1.000 23.16013 ? 164 HIS A CG  1 
ATOM   1237 N ND1 . HIS A 1 164 ? -24.42999 17.01853  2.55625   1.000 22.56925 ? 164 HIS A ND1 1 
ATOM   1238 C CD2 . HIS A 1 164 ? -23.44143 15.95309  4.19410   1.000 22.73928 ? 164 HIS A CD2 1 
ATOM   1239 C CE1 . HIS A 1 164 ? -24.92223 15.79493  2.58131   1.000 19.74709 ? 164 HIS A CE1 1 
ATOM   1240 N NE2 . HIS A 1 164 ? -24.35071 15.13196  3.57267   1.000 23.28632 ? 164 HIS A NE2 1 
ATOM   1241 N N   . MET A 1 165 ? -20.20949 20.42073  4.19866   1.000 22.77420 ? 165 MET A N   1 
ATOM   1242 C CA  . MET A 1 165 ? -19.96619 21.84853  3.99480   1.000 23.40557 ? 165 MET A CA  1 
ATOM   1243 C C   . MET A 1 165 ? -19.02445 22.38490  5.06374   1.000 21.77681 ? 165 MET A C   1 
ATOM   1244 O O   . MET A 1 165 ? -18.78097 21.74313  6.08797   1.000 26.94460 ? 165 MET A O   1 
ATOM   1245 C CB  . MET A 1 165 ? -21.27841 22.63612  4.02686   1.000 25.06387 ? 165 MET A CB  1 
ATOM   1246 C CG  . MET A 1 165 ? -21.99035 22.47850  5.35218   1.000 30.16078 ? 165 MET A CG  1 
ATOM   1247 S SD  . MET A 1 165 ? -23.73039 22.98621  5.25321   1.000 38.53280 ? 165 MET A SD  1 
ATOM   1248 C CE  . MET A 1 165 ? -23.53618 24.68911  4.71157   1.000 33.27185 ? 165 MET A CE  1 
ATOM   1249 N N   . GLU A 1 166 ? -18.53280 23.60123  4.82782   1.000 24.83718 ? 166 GLU A N   1 
ATOM   1250 C CA  . GLU A 1 166 ? -17.66066 24.29686  5.76776   1.000 27.97558 ? 166 GLU A CA  1 
ATOM   1251 C C   . GLU A 1 166 ? -18.26360 25.65279  6.12907   1.000 27.81351 ? 166 GLU A C   1 
ATOM   1252 O O   . GLU A 1 166 ? -18.66299 26.42112  5.24462   1.000 26.69817 ? 166 GLU A O   1 
ATOM   1253 C CB  . GLU A 1 166 ? -16.25676 24.47386  5.17338   1.000 26.95577 ? 166 GLU A CB  1 
ATOM   1254 C CG  . GLU A 1 166 ? -15.26617 25.22324  6.10791   1.000 20.91418 ? 166 GLU A CG  1 
ATOM   1255 C CD  . GLU A 1 166 ? -13.85024 25.27564  5.54271   1.000 31.64846 ? 166 GLU A CD  1 
ATOM   1256 O OE1 . GLU A 1 166 ? -13.27928 24.20505  5.25880   1.000 32.00471 ? 166 GLU A OE1 1 
ATOM   1257 O OE2 . GLU A 1 166 ? -13.31488 26.38797  5.35477   1.000 36.56952 ? 166 GLU A OE2 1 
ATOM   1258 N N   . LEU A 1 167 ? -18.33804 25.94204  7.42278   1.000 24.18794 ? 167 LEU A N   1 
ATOM   1259 C CA  . LEU A 1 167 ? -18.91015 27.20181  7.88065   1.000 31.56184 ? 167 LEU A CA  1 
ATOM   1260 C C   . LEU A 1 167 ? -17.86601 28.31421  7.86092   1.000 38.20525 ? 167 LEU A C   1 
ATOM   1261 O O   . LEU A 1 167 ? -16.65724 28.04496  7.85866   1.000 30.75059 ? 167 LEU A O   1 
ATOM   1262 C CB  . LEU A 1 167 ? -19.45377 27.04792  9.29403   1.000 29.98342 ? 167 LEU A CB  1 
ATOM   1263 C CG  . LEU A 1 167 ? -20.58235 26.03687  9.47867   1.000 30.17575 ? 167 LEU A CG  1 
ATOM   1264 C CD1 . LEU A 1 167 ? -21.00538 26.04416  10.93496  1.000 35.68700 ? 167 LEU A CD1 1 
ATOM   1265 C CD2 . LEU A 1 167 ? -21.75193 26.37672  8.59094   1.000 36.24086 ? 167 LEU A CD2 1 
ATOM   1266 N N   . PRO A 1 168 ? -18.31081 29.57776  7.88485   1.000 38.73049 ? 168 PRO A N   1 
ATOM   1267 C CA  . PRO A 1 168 ? -17.35868 30.70018  7.76426   1.000 37.65693 ? 168 PRO A CA  1 
ATOM   1268 C C   . PRO A 1 168 ? -16.28963 30.73631  8.84262   1.000 35.03622 ? 168 PRO A C   1 
ATOM   1269 O O   . PRO A 1 168 ? -15.21021 31.28753  8.60035   1.000 40.08695 ? 168 PRO A O   1 
ATOM   1270 C CB  . PRO A 1 168 ? -18.26582 31.93631  7.83797   1.000 35.04375 ? 168 PRO A CB  1 
ATOM   1271 C CG  . PRO A 1 168 ? -19.59564 31.45085  7.34834   1.000 35.53088 ? 168 PRO A CG  1 
ATOM   1272 C CD  . PRO A 1 168 ? -19.71412 30.03747  7.85221   1.000 32.60539 ? 168 PRO A CD  1 
ATOM   1273 N N   . THR A 1 169 ? -16.54592 30.19530  10.03026  1.000 34.28947 ? 169 THR A N   1 
ATOM   1274 C CA  . THR A 1 169 ? -15.49176 30.12396  11.03297  1.000 31.29420 ? 169 THR A CA  1 
ATOM   1275 C C   . THR A 1 169 ? -14.49094 29.00898  10.76599  1.000 31.43105 ? 169 THR A C   1 
ATOM   1276 O O   . THR A 1 169 ? -13.52485 28.88580  11.51853  1.000 37.48282 ? 169 THR A O   1 
ATOM   1277 C CB  . THR A 1 169 ? -16.07778 29.92691  12.43132  1.000 37.64635 ? 169 THR A CB  1 
ATOM   1278 O OG1 . THR A 1 169 ? -16.90978 28.76256  12.43828  1.000 37.43501 ? 169 THR A OG1 1 
ATOM   1279 C CG2 . THR A 1 169 ? -16.88520 31.13856  12.86722  1.000 28.95797 ? 169 THR A CG2 1 
ATOM   1280 N N   . GLY A 1 170 ? -14.69370 28.18996  9.73766   1.000 34.44565 ? 170 GLY A N   1 
ATOM   1281 C CA  . GLY A 1 170 ? -13.76523 27.12343  9.41054   1.000 30.13250 ? 170 GLY A CA  1 
ATOM   1282 C C   . GLY A 1 170 ? -14.07078 25.78130  10.04258  1.000 35.70108 ? 170 GLY A C   1 
ATOM   1283 O O   . GLY A 1 170 ? -13.27140 24.84464  9.88826   1.000 35.58710 ? 170 GLY A O   1 
ATOM   1284 N N   . VAL A 1 171 ? -15.18768 25.65661  10.75858  1.000 31.32492 ? 171 VAL A N   1 
ATOM   1285 C CA  . VAL A 1 171 ? -15.63404 24.37099  11.28633  1.000 26.86009 ? 171 VAL A CA  1 
ATOM   1286 C C   . VAL A 1 171 ? -16.50722 23.73316  10.21808  1.000 26.97137 ? 171 VAL A C   1 
ATOM   1287 O O   . VAL A 1 171 ? -16.82822 24.37515  9.21363   1.000 26.95954 ? 171 VAL A O   1 
ATOM   1288 C CB  . VAL A 1 171 ? -16.39338 24.53106  12.61514  1.000 29.75623 ? 171 VAL A CB  1 
ATOM   1289 C CG1 . VAL A 1 171 ? -15.51056 25.20605  13.64057  1.000 32.95037 ? 171 VAL A CG1 1 
ATOM   1290 C CG2 . VAL A 1 171 ? -17.67670 25.32494  12.40203  1.000 32.26296 ? 171 VAL A CG2 1 
ATOM   1291 N N   . HIS A 1 172 ? -16.91270 22.48375  10.42384  1.000 24.58351 ? 172 HIS A N   1 
ATOM   1292 C CA  . HIS A 1 172 ? -17.52291 21.71320  9.35386   1.000 29.50826 ? 172 HIS A CA  1 
ATOM   1293 C C   . HIS A 1 172 ? -18.86338 21.16086  9.79856   1.000 24.17545 ? 172 HIS A C   1 
ATOM   1294 O O   . HIS A 1 172 ? -19.14440 21.04914  10.99357  1.000 25.62494 ? 172 HIS A O   1 
ATOM   1295 C CB  . HIS A 1 172 ? -16.57401 20.61357  8.90713   1.000 27.49468 ? 172 HIS A CB  1 
ATOM   1296 C CG  . HIS A 1 172 ? -15.28263 21.15306  8.39815   1.000 28.47062 ? 172 HIS A CG  1 
ATOM   1297 N ND1 . HIS A 1 172 ? -14.16887 21.29837  9.19559   1.000 26.03119 ? 172 HIS A ND1 1 
ATOM   1298 C CD2 . HIS A 1 172 ? -14.95175 21.66496  7.18927   1.000 28.45426 ? 172 HIS A CD2 1 
ATOM   1299 C CE1 . HIS A 1 172 ? -13.19072 21.83044  8.48417   1.000 28.70353 ? 172 HIS A CE1 1 
ATOM   1300 N NE2 . HIS A 1 172 ? -13.64088 22.06612  7.26295   1.000 27.03332 ? 172 HIS A NE2 1 
ATOM   1301 N N   . ALA A 1 173 ? -19.70690 20.86063  8.81669   1.000 20.55052 ? 173 ALA A N   1 
ATOM   1302 C CA  . ALA A 1 173 ? -21.04105 20.34951  9.09567   1.000 23.58574 ? 173 ALA A CA  1 
ATOM   1303 C C   . ALA A 1 173 ? -21.39226 19.26028  8.09070   1.000 23.16663 ? 173 ALA A C   1 
ATOM   1304 O O   . ALA A 1 173 ? -21.01493 19.32139  6.91585   1.000 25.79904 ? 173 ALA A O   1 
ATOM   1305 C CB  . ALA A 1 173 ? -22.08878 21.46495  9.06773   1.000 20.13651 ? 173 ALA A CB  1 
ATOM   1306 N N   . GLY A 1 174 ? -22.13372 18.28184  8.56219   1.000 20.80337 ? 174 GLY A N   1 
ATOM   1307 C CA  . GLY A 1 174 ? -22.52584 17.16410  7.73871   1.000 20.63740 ? 174 GLY A CA  1 
ATOM   1308 C C   . GLY A 1 174 ? -23.68366 16.39684  8.34340   1.000 21.18397 ? 174 GLY A C   1 
ATOM   1309 O O   . GLY A 1 174 ? -24.36497 16.87881  9.24620   1.000 21.29672 ? 174 GLY A O   1 
ATOM   1310 N N   . THR A 1 175 ? -23.89829 15.18223  7.83051   1.000 23.80598 ? 175 THR A N   1 
ATOM   1311 C CA  . THR A 1 175 ? -25.08960 14.39586  8.12722   1.000 20.67204 ? 175 THR A CA  1 
ATOM   1312 C C   . THR A 1 175 ? -24.68221 13.01950  8.63329   1.000 23.23413 ? 175 THR A C   1 
ATOM   1313 O O   . THR A 1 175 ? -23.52121 12.60545  8.52271   1.000 20.46492 ? 175 THR A O   1 
ATOM   1314 C CB  . THR A 1 175 ? -25.98782 14.24388  6.88416   1.000 22.90953 ? 175 THR A CB  1 
ATOM   1315 O OG1 . THR A 1 175 ? -25.29856 13.47138  5.89861   1.000 19.96281 ? 175 THR A OG1 1 
ATOM   1316 C CG2 . THR A 1 175 ? -26.35272 15.61181  6.27731   1.000 24.94729 ? 175 THR A CG2 1 
ATOM   1317 N N   . ASP A 1 176 ? -25.65495 12.30368  9.19436   1.000 19.03551 ? 176 ASP A N   1 
ATOM   1318 C CA  . ASP A 1 176 ? -25.47914 10.87615  9.38962   1.000 23.31583 ? 176 ASP A CA  1 
ATOM   1319 C C   . ASP A 1 176 ? -25.73383 10.18635  8.05263   1.000 21.78049 ? 176 ASP A C   1 
ATOM   1320 O O   . ASP A 1 176 ? -26.01556 10.83987  7.04863   1.000 22.52793 ? 176 ASP A O   1 
ATOM   1321 C CB  . ASP A 1 176 ? -26.39277 10.37056  10.51173  1.000 25.77815 ? 176 ASP A CB  1 
ATOM   1322 C CG  . ASP A 1 176 ? -27.86224 10.62481  10.23287  1.000 30.97085 ? 176 ASP A CG  1 
ATOM   1323 O OD1 . ASP A 1 176 ? -28.21823 10.82122  9.04693   1.000 24.80381 ? 176 ASP A OD1 1 
ATOM   1324 O OD2 . ASP A 1 176 ? -28.65907 10.61825  11.20419  1.000 29.37969 ? 176 ASP A OD2 1 
ATOM   1325 N N   . LEU A 1 177 ? -25.61684 8.86581   8.00986   1.000 19.90424 ? 177 LEU A N   1 
ATOM   1326 C CA  . LEU A 1 177 ? -25.78326 8.17515   6.73705   1.000 22.28687 ? 177 LEU A CA  1 
ATOM   1327 C C   . LEU A 1 177 ? -27.25018 8.01084   6.35936   1.000 28.40522 ? 177 LEU A C   1 
ATOM   1328 O O   . LEU A 1 177 ? -27.54347 7.49615   5.26979   1.000 24.47521 ? 177 LEU A O   1 
ATOM   1329 C CB  . LEU A 1 177 ? -25.07309 6.81669   6.76721   1.000 24.08227 ? 177 LEU A CB  1 
ATOM   1330 C CG  . LEU A 1 177 ? -23.59237 6.86282   6.35163   1.000 21.37526 ? 177 LEU A CG  1 
ATOM   1331 C CD1 . LEU A 1 177 ? -23.43654 7.10701   4.85547   1.000 20.00111 ? 177 LEU A CD1 1 
ATOM   1332 C CD2 . LEU A 1 177 ? -22.86118 7.94331   7.12436   1.000 24.94604 ? 177 LEU A CD2 1 
ATOM   1333 N N   . GLU A 1 178 ? -28.16835 8.45632   7.21669   1.000 23.22878 ? 178 GLU A N   1 
ATOM   1334 C CA  . GLU A 1 178 ? -29.56801 8.64367   6.84311   1.000 24.53770 ? 178 GLU A CA  1 
ATOM   1335 C C   . GLU A 1 178 ? -29.81474 10.00538  6.21152   1.000 22.27029 ? 178 GLU A C   1 
ATOM   1336 O O   . GLU A 1 178 ? -30.95594 10.32186  5.85989   1.000 25.56969 ? 178 GLU A O   1 
ATOM   1337 C CB  . GLU A 1 178 ? -30.48269 8.49105   8.06607   1.000 29.82688 ? 178 GLU A CB  1 
ATOM   1338 C CG  . GLU A 1 178 ? -30.63599 7.06986   8.56080   1.000 32.84080 ? 178 GLU A CG  1 
ATOM   1339 C CD  . GLU A 1 178 ? -31.49448 6.98986   9.81824   1.000 40.17452 ? 178 GLU A CD  1 
ATOM   1340 O OE1 . GLU A 1 178 ? -32.09440 8.01769   10.20086  1.000 35.48333 ? 178 GLU A OE1 1 
ATOM   1341 O OE2 . GLU A 1 178 ? -31.58029 5.89710   10.41168  1.000 50.50758 ? 178 GLU A OE2 1 
ATOM   1342 N N   . GLY A 1 179 ? -28.78378 10.82102  6.08549   1.000 19.28189 ? 179 GLY A N   1 
ATOM   1343 C CA  . GLY A 1 179 ? -28.91836 12.09925  5.44093   1.000 20.34272 ? 179 GLY A CA  1 
ATOM   1344 C C   . GLY A 1 179 ? -29.42665 13.22038  6.31169   1.000 26.43115 ? 179 GLY A C   1 
ATOM   1345 O O   . GLY A 1 179 ? -29.74743 14.28835  5.77266   1.000 21.45582 ? 179 GLY A O   1 
ATOM   1346 N N   . ASN A 1 180 ? -29.51718 13.02173  7.63326   1.000 19.37753 ? 180 ASN A N   1 
ATOM   1347 C CA  . ASN A 1 180 ? -29.98911 14.06796  8.53427   1.000 24.56796 ? 180 ASN A CA  1 
ATOM   1348 C C   . ASN A 1 180 ? -28.80601 14.85419  9.08911   1.000 22.57249 ? 180 ASN A C   1 
ATOM   1349 O O   . ASN A 1 180 ? -27.87099 14.27137  9.63966   1.000 22.90525 ? 180 ASN A O   1 
ATOM   1350 C CB  . ASN A 1 180 ? -30.80600 13.46503  9.68072   1.000 29.37608 ? 180 ASN A CB  1 
ATOM   1351 C CG  . ASN A 1 180 ? -32.19409 13.00772  9.23871   1.000 29.80574 ? 180 ASN A CG  1 
ATOM   1352 O OD1 . ASN A 1 180 ? -32.59799 11.87863  9.49647   1.000 33.17768 ? 180 ASN A OD1 1 
ATOM   1353 N ND2 . ASN A 1 180 ? -32.92186 13.88825  8.58700   1.000 27.28649 ? 180 ASN A ND2 1 
ATOM   1354 N N   . PHE A 1 181 ? -28.83827 16.17010  8.91303   1.000 23.27772 ? 181 PHE A N   1 
ATOM   1355 C CA  . PHE A 1 181 ? -27.74908 17.00642  9.39100   1.000 27.11137 ? 181 PHE A CA  1 
ATOM   1356 C C   . PHE A 1 181 ? -27.59676 16.87914  10.89372  1.000 20.47473 ? 181 PHE A C   1 
ATOM   1357 O O   . PHE A 1 181 ? -28.57918 16.76131  11.62514  1.000 20.44316 ? 181 PHE A O   1 
ATOM   1358 C CB  . PHE A 1 181 ? -27.98963 18.47590  9.01139   1.000 22.54912 ? 181 PHE A CB  1 
ATOM   1359 C CG  . PHE A 1 181 ? -27.25422 18.88894  7.77611   1.000 18.78170 ? 181 PHE A CG  1 
ATOM   1360 C CD1 . PHE A 1 181 ? -25.95372 19.36425  7.86828   1.000 19.79735 ? 181 PHE A CD1 1 
ATOM   1361 C CD2 . PHE A 1 181 ? -27.84015 18.74349  6.52418   1.000 22.27067 ? 181 PHE A CD2 1 
ATOM   1362 C CE1 . PHE A 1 181 ? -25.26211 19.73034  6.73877   1.000 20.04951 ? 181 PHE A CE1 1 
ATOM   1363 C CE2 . PHE A 1 181 ? -27.15934 19.09519  5.38386   1.000 21.78449 ? 181 PHE A CE2 1 
ATOM   1364 C CZ  . PHE A 1 181 ? -25.86208 19.58837  5.48241   1.000 20.64715 ? 181 PHE A CZ  1 
ATOM   1365 N N   . TYR A 1 182 ? -26.34874 16.88226  11.34464  1.000 20.55468 ? 182 TYR A N   1 
ATOM   1366 C CA  . TYR A 1 182 ? -26.04186 17.21933  12.72015  1.000 20.89185 ? 182 TYR A CA  1 
ATOM   1367 C C   . TYR A 1 182 ? -26.12477 18.73095  12.83656  1.000 18.25140 ? 182 TYR A C   1 
ATOM   1368 O O   . TYR A 1 182 ? -25.37662 19.43845  12.16233  1.000 23.64005 ? 182 TYR A O   1 
ATOM   1369 C CB  . TYR A 1 182 ? -24.64266 16.73241  13.09704  1.000 22.16297 ? 182 TYR A CB  1 
ATOM   1370 C CG  . TYR A 1 182 ? -24.52631 15.23497  13.16656  1.000 25.13370 ? 182 TYR A CG  1 
ATOM   1371 C CD1 . TYR A 1 182 ? -24.92183 14.54108  14.30553  1.000 25.48467 ? 182 TYR A CD1 1 
ATOM   1372 C CD2 . TYR A 1 182 ? -24.02164 14.51400  12.09574  1.000 20.66741 ? 182 TYR A CD2 1 
ATOM   1373 C CE1 . TYR A 1 182 ? -24.80702 13.16394  14.36995  1.000 22.78859 ? 182 TYR A CE1 1 
ATOM   1374 C CE2 . TYR A 1 182 ? -23.91864 13.13992  12.13764  1.000 20.08375 ? 182 TYR A CE2 1 
ATOM   1375 C CZ  . TYR A 1 182 ? -24.31411 12.46853  13.27575  1.000 25.89308 ? 182 TYR A CZ  1 
ATOM   1376 O OH  . TYR A 1 182 ? -24.19891 11.10016  13.32552  1.000 25.88311 ? 182 TYR A OH  1 
ATOM   1377 N N   . GLY A 1 183 ? -27.02585 19.22291  13.67698  1.000 23.53436 ? 183 GLY A N   1 
ATOM   1378 C CA  . GLY A 1 183 ? -27.12254 20.64171  13.92226  1.000 22.30467 ? 183 GLY A CA  1 
ATOM   1379 C C   . GLY A 1 183 ? -28.12292 21.35108  13.02824  1.000 23.56579 ? 183 GLY A C   1 
ATOM   1380 O O   . GLY A 1 183 ? -28.72262 20.77123  12.10846  1.000 24.36361 ? 183 GLY A O   1 
ATOM   1381 N N   . PRO A 1 184 ? -28.27652 22.65714  13.25807  1.000 19.74736 ? 184 PRO A N   1 
ATOM   1382 C CA  . PRO A 1 184 ? -29.34222 23.41155  12.58289  1.000 20.20506 ? 184 PRO A CA  1 
ATOM   1383 C C   . PRO A 1 184 ? -28.95044 23.93149  11.20872  1.000 20.24399 ? 184 PRO A C   1 
ATOM   1384 O O   . PRO A 1 184 ? -29.30918 25.05514  10.84748  1.000 22.90717 ? 184 PRO A O   1 
ATOM   1385 C CB  . PRO A 1 184 ? -29.59984 24.56880  13.54879  1.000 20.96678 ? 184 PRO A CB  1 
ATOM   1386 C CG  . PRO A 1 184 ? -28.20318 24.82618  14.14877  1.000 26.53081 ? 184 PRO A CG  1 
ATOM   1387 C CD  . PRO A 1 184 ? -27.59531 23.43867  14.30820  1.000 22.16660 ? 184 PRO A CD  1 
ATOM   1388 N N   . PHE A 1 185 ? -28.23942 23.13599  10.42279  1.000 22.21043 ? 185 PHE A N   1 
ATOM   1389 C CA  . PHE A 1 185 ? -27.69406 23.59685  9.15565   1.000 21.02581 ? 185 PHE A CA  1 
ATOM   1390 C C   . PHE A 1 185 ? -28.47140 23.00480  7.98588   1.000 19.17774 ? 185 PHE A C   1 
ATOM   1391 O O   . PHE A 1 185 ? -29.21550 22.03605  8.13982   1.000 22.94414 ? 185 PHE A O   1 
ATOM   1392 C CB  . PHE A 1 185 ? -26.21446 23.22575  9.05277   1.000 21.07677 ? 185 PHE A CB  1 
ATOM   1393 C CG  . PHE A 1 185 ? -25.42746 23.56797  10.29471  1.000 26.93098 ? 185 PHE A CG  1 
ATOM   1394 C CD1 . PHE A 1 185 ? -25.23379 24.89471  10.65551  1.000 26.20653 ? 185 PHE A CD1 1 
ATOM   1395 C CD2 . PHE A 1 185 ? -24.90070 22.57234  11.09256  1.000 23.22262 ? 185 PHE A CD2 1 
ATOM   1396 C CE1 . PHE A 1 185 ? -24.52423 25.21993  11.78858  1.000 27.66024 ? 185 PHE A CE1 1 
ATOM   1397 C CE2 . PHE A 1 185 ? -24.19302 22.89064  12.25016  1.000 26.68969 ? 185 PHE A CE2 1 
ATOM   1398 C CZ  . PHE A 1 185 ? -24.01438 24.22347  12.58887  1.000 25.31777 ? 185 PHE A CZ  1 
ATOM   1399 N N   . VAL A 1 186 ? -28.29185 23.60470  6.80636   1.000 22.34428 ? 186 VAL A N   1 
ATOM   1400 C CA  . VAL A 1 186 ? -28.95369 23.15008  5.58650   1.000 20.60412 ? 186 VAL A CA  1 
ATOM   1401 C C   . VAL A 1 186 ? -27.93270 23.10686  4.46372   1.000 22.52948 ? 186 VAL A C   1 
ATOM   1402 O O   . VAL A 1 186 ? -26.98147 23.89468  4.43936   1.000 24.91976 ? 186 VAL A O   1 
ATOM   1403 C CB  . VAL A 1 186 ? -30.14836 24.04343  5.17775   1.000 21.50351 ? 186 VAL A CB  1 
ATOM   1404 C CG1 . VAL A 1 186 ? -31.25323 24.00808  6.23990   1.000 22.24991 ? 186 VAL A CG1 1 
ATOM   1405 C CG2 . VAL A 1 186 ? -29.69803 25.48648  4.90519   1.000 21.28760 ? 186 VAL A CG2 1 
ATOM   1406 N N   . ASP A 1 187 ? -28.14716 22.19037  3.51043   1.000 21.70660 ? 187 ASP A N   1 
ATOM   1407 C CA  . ASP A 1 187 ? -27.23885 22.06190  2.36708   1.000 21.59497 ? 187 ASP A CA  1 
ATOM   1408 C C   . ASP A 1 187 ? -27.64105 23.05220  1.26911   1.000 26.97358 ? 187 ASP A C   1 
ATOM   1409 O O   . ASP A 1 187 ? -28.11759 22.70652  0.17892   1.000 25.04165 ? 187 ASP A O   1 
ATOM   1410 C CB  . ASP A 1 187 ? -27.16729 20.61760  1.87128   1.000 21.21920 ? 187 ASP A CB  1 
ATOM   1411 C CG  . ASP A 1 187 ? -28.53701 19.96228  1.64446   1.000 24.98023 ? 187 ASP A CG  1 
ATOM   1412 O OD1 . ASP A 1 187 ? -29.58353 20.47350  2.10835   1.000 25.53416 ? 187 ASP A OD1 1 
ATOM   1413 O OD2 . ASP A 1 187 ? -28.54731 18.89072  0.99001   1.000 24.39220 ? 187 ASP A OD2 1 
ATOM   1414 N N   . ARG A 1 188 ? -27.38509 24.32284  1.58522   1.000 26.24057 ? 188 ARG A N   1 
ATOM   1415 C CA  . ARG A 1 188 ? -27.57256 25.44149  0.67330   1.000 26.52552 ? 188 ARG A CA  1 
ATOM   1416 C C   . ARG A 1 188 ? -26.42563 26.42330  0.86715   1.000 30.96845 ? 188 ARG A C   1 
ATOM   1417 O O   . ARG A 1 188 ? -25.94558 26.61395  1.98960   1.000 25.68048 ? 188 ARG A O   1 
ATOM   1418 C CB  . ARG A 1 188 ? -28.91637 26.12867  0.91753   1.000 28.48296 ? 188 ARG A CB  1 
ATOM   1419 C CG  . ARG A 1 188 ? -29.01117 27.51807  0.31142   1.000 32.35446 ? 188 ARG A CG  1 
ATOM   1420 C CD  . ARG A 1 188 ? -30.44376 28.04997  0.39891   1.000 41.67262 ? 188 ARG A CD  1 
ATOM   1421 N NE  . ARG A 1 188 ? -30.59551 29.28771  -0.35434  1.000 46.20869 ? 188 ARG A NE  1 
ATOM   1422 C CZ  . ARG A 1 188 ? -31.75871 29.84737  -0.66031  1.000 52.95112 ? 188 ARG A CZ  1 
ATOM   1423 N NH1 . ARG A 1 188 ? -32.90999 29.29519  -0.30508  1.000 47.87407 ? 188 ARG A NH1 1 
ATOM   1424 N NH2 . ARG A 1 188 ? -31.76671 30.98602  -1.34621  1.000 50.43297 ? 188 ARG A NH2 1 
ATOM   1425 N N   . GLN A 1 189 ? -25.96639 27.03286  -0.22852  1.000 30.20616 ? 189 GLN A N   1 
ATOM   1426 C CA  . GLN A 1 189 ? -24.83491 27.96248  -0.14566  1.000 29.85334 ? 189 GLN A CA  1 
ATOM   1427 C C   . GLN A 1 189 ? -25.36675 29.33596  0.25458   1.000 31.87107 ? 189 GLN A C   1 
ATOM   1428 O O   . GLN A 1 189 ? -25.60826 30.22724  -0.56429  1.000 31.61276 ? 189 GLN A O   1 
ATOM   1429 C CB  . GLN A 1 189 ? -24.05552 28.00758  -1.45304  1.000 27.73158 ? 189 GLN A CB  1 
ATOM   1430 C CG  . GLN A 1 189 ? -22.81966 28.86506  -1.38753  1.000 30.77102 ? 189 GLN A CG  1 
ATOM   1431 C CD  . GLN A 1 189 ? -21.81715 28.46311  -2.43824  1.000 39.22769 ? 189 GLN A CD  1 
ATOM   1432 O OE1 . GLN A 1 189 ? -22.05838 27.53547  -3.21230  1.000 39.51852 ? 189 GLN A OE1 1 
ATOM   1433 N NE2 . GLN A 1 189 ? -20.68411 29.14769  -2.47099  1.000 36.23628 ? 189 GLN A NE2 1 
ATOM   1434 N N   . ILE A 1 190 ? -25.57616 29.47711  1.55797   1.000 34.80026 ? 190 ILE A N   1 
ATOM   1435 C CA  A ILE A 1 190 ? -26.02434 30.71555  2.18257   0.500 34.44765 ? 190 ILE A CA  1 
ATOM   1436 C CA  B ILE A 1 190 ? -26.01178 30.72032  2.17360   0.500 34.45064 ? 190 ILE A CA  1 
ATOM   1437 C C   . ILE A 1 190 ? -25.29450 30.83753  3.50829   1.000 36.54883 ? 190 ILE A C   1 
ATOM   1438 O O   . ILE A 1 190 ? -24.91276 29.83287  4.11296   1.000 29.28763 ? 190 ILE A O   1 
ATOM   1439 C CB  A ILE A 1 190 ? -27.55246 30.74364  2.41135   0.500 34.42648 ? 190 ILE A CB  1 
ATOM   1440 C CB  B ILE A 1 190 ? -27.54215 30.75286  2.35985   0.500 34.42247 ? 190 ILE A CB  1 
ATOM   1441 C CG1 A ILE A 1 190 ? -28.01553 29.40493  2.99417   0.500 32.93654 ? 190 ILE A CG1 1 
ATOM   1442 C CG1 B ILE A 1 190 ? -28.01656 32.16438  2.69769   0.500 36.22509 ? 190 ILE A CG1 1 
ATOM   1443 C CG2 A ILE A 1 190 ? -28.29236 31.08063  1.12326   0.500 42.80295 ? 190 ILE A CG2 1 
ATOM   1444 C CG2 B ILE A 1 190 ? -27.96014 29.75531  3.43045   0.500 33.63271 ? 190 ILE A CG2 1 
ATOM   1445 C CD1 A ILE A 1 190 ? -29.48814 29.34393  3.30490   0.500 38.32283 ? 190 ILE A CD1 1 
ATOM   1446 C CD1 B ILE A 1 190 ? -29.51797 32.28228  2.78202   0.500 33.40220 ? 190 ILE A CD1 1 
ATOM   1447 N N   . ALA A 1 191 ? -25.10493 32.07664  3.96865   1.000 36.79917 ? 191 ALA A N   1 
ATOM   1448 C CA  . ALA A 1 191 ? -24.38665 32.29387  5.22178   1.000 43.99478 ? 191 ALA A CA  1 
ATOM   1449 C C   . ALA A 1 191 ? -25.05569 31.54229  6.36684   1.000 35.03787 ? 191 ALA A C   1 
ATOM   1450 O O   . ALA A 1 191 ? -26.26589 31.65369  6.58013   1.000 33.65412 ? 191 ALA A O   1 
ATOM   1451 C CB  . ALA A 1 191 ? -24.31462 33.78765  5.54739   1.000 45.23705 ? 191 ALA A CB  1 
ATOM   1452 N N   . GLN A 1 192 ? -24.27097 30.76964  7.10331   1.000 31.92081 ? 192 GLN A N   1 
ATOM   1453 C CA  . GLN A 1 192 ? -24.80362 30.03085  8.23759   1.000 32.41368 ? 192 GLN A CA  1 
ATOM   1454 C C   . GLN A 1 192 ? -23.78106 30.04009  9.35188   1.000 32.35882 ? 192 GLN A C   1 
ATOM   1455 O O   . GLN A 1 192 ? -22.58040 29.91072  9.10553   1.000 42.18308 ? 192 GLN A O   1 
ATOM   1456 C CB  . GLN A 1 192 ? -25.15966 28.58650  7.86844   1.000 28.44827 ? 192 GLN A CB  1 
ATOM   1457 C CG  . GLN A 1 192 ? -26.15392 28.47568  6.72176   1.000 30.81790 ? 192 GLN A CG  1 
ATOM   1458 C CD  . GLN A 1 192 ? -26.43403 27.03244  6.34545   1.000 28.69514 ? 192 GLN A CD  1 
ATOM   1459 O OE1 . GLN A 1 192 ? -26.87900 26.23859  7.17626   1.000 24.20015 ? 192 GLN A OE1 1 
ATOM   1460 N NE2 . GLN A 1 192 ? -26.14636 26.68010  5.10116   1.000 24.36013 ? 192 GLN A NE2 1 
ATOM   1461 N N   . ALA A 1 193 ? -24.26623 30.18997  10.57171  1.000 31.92265 ? 193 ALA A N   1 
ATOM   1462 C CA  . ALA A 1 193 ? -23.42281 30.25530  11.74959  1.000 35.70307 ? 193 ALA A CA  1 
ATOM   1463 C C   . ALA A 1 193 ? -23.87182 29.18568  12.72956  1.000 29.59978 ? 193 ALA A C   1 
ATOM   1464 O O   . ALA A 1 193 ? -25.03960 28.78684  12.73823  1.000 28.17170 ? 193 ALA A O   1 
ATOM   1465 C CB  . ALA A 1 193 ? -23.49140 31.64188  12.40246  1.000 34.56007 ? 193 ALA A CB  1 
ATOM   1466 N N   . ALA A 1 194 ? -22.93736 28.70071  13.53704  1.000 34.02761 ? 194 ALA A N   1 
ATOM   1467 C CA  . ALA A 1 194 ? -23.29226 27.70973  14.54047  1.000 33.22445 ? 194 ALA A CA  1 
ATOM   1468 C C   . ALA A 1 194 ? -23.60202 28.38365  15.86912  1.000 33.97637 ? 194 ALA A C   1 
ATOM   1469 O O   . ALA A 1 194 ? -23.22779 29.53085  16.11464  1.000 33.19472 ? 194 ALA A O   1 
ATOM   1470 C CB  . ALA A 1 194 ? -22.17113 26.68450  14.72508  1.000 35.87230 ? 194 ALA A CB  1 
ATOM   1471 N N   . GLY A 1 195 ? -24.31928 27.65956  16.71903  1.000 33.92421 ? 195 GLY A N   1 
ATOM   1472 C CA  . GLY A 1 195 ? -24.48795 28.08081  18.09419  1.000 37.63747 ? 195 GLY A CA  1 
ATOM   1473 C C   . GLY A 1 195 ? -23.15118 28.18546  18.80425  1.000 37.96339 ? 195 GLY A C   1 
ATOM   1474 O O   . GLY A 1 195 ? -22.09982 27.77823  18.30785  1.000 29.14244 ? 195 GLY A O   1 
ATOM   1475 N N   . THR A 1 196 ? -23.19536 28.77743  19.99463  1.000 31.53751 ? 196 THR A N   1 
ATOM   1476 C CA  . THR A 1 196 ? -22.00227 28.84620  20.82395  1.000 31.54766 ? 196 THR A CA  1 
ATOM   1477 C C   . THR A 1 196 ? -21.61397 27.44444  21.27534  1.000 25.10517 ? 196 THR A C   1 
ATOM   1478 O O   . THR A 1 196 ? -22.46759 26.64156  21.65654  1.000 29.14805 ? 196 THR A O   1 
ATOM   1479 C CB  . THR A 1 196 ? -22.24042 29.75287  22.03818  1.000 37.12842 ? 196 THR A CB  1 
ATOM   1480 O OG1 . THR A 1 196 ? -22.42241 31.10402  21.59877  1.000 38.82033 ? 196 THR A OG1 1 
ATOM   1481 C CG2 . THR A 1 196 ? -21.05348 29.70256  22.98600  1.000 37.61242 ? 196 THR A CG2 1 
ATOM   1482 N N   . ASP A 1 197 ? -20.32007 27.14866  21.23552  1.000 25.87072 ? 197 ASP A N   1 
ATOM   1483 C CA  . ASP A 1 197 ? -19.84772 25.82282  21.60509  1.000 27.00389 ? 197 ASP A CA  1 
ATOM   1484 C C   . ASP A 1 197 ? -19.48480 25.77066  23.09243  1.000 29.68696 ? 197 ASP A C   1 
ATOM   1485 O O   . ASP A 1 197 ? -19.34549 26.79515  23.75573  1.000 30.05901 ? 197 ASP A O   1 
ATOM   1486 C CB  . ASP A 1 197 ? -18.64084 25.43234  20.75312  1.000 24.59896 ? 197 ASP A CB  1 
ATOM   1487 C CG  . ASP A 1 197 ? -18.46428 23.92355  20.65155  1.000 29.45960 ? 197 ASP A CG  1 
ATOM   1488 O OD1 . ASP A 1 197 ? -19.43090 23.20402  20.93766  1.000 24.31275 ? 197 ASP A OD1 1 
ATOM   1489 O OD2 . ASP A 1 197 ? -17.36722 23.45345  20.28472  1.000 27.41684 ? 197 ASP A OD2 1 
ATOM   1490 N N   . THR A 1 198 ? -19.36140 24.55219  23.61794  1.000 28.56728 ? 198 THR A N   1 
ATOM   1491 C CA  . THR A 1 198 ? -18.92277 24.32780  24.99364  1.000 28.70038 ? 198 THR A CA  1 
ATOM   1492 C C   . THR A 1 198 ? -17.81671 23.28084  24.99629  1.000 28.76367 ? 198 THR A C   1 
ATOM   1493 O O   . THR A 1 198 ? -17.56817 22.60199  23.99409  1.000 24.55589 ? 198 THR A O   1 
ATOM   1494 C CB  . THR A 1 198 ? -20.08176 23.88004  25.90074  1.000 28.85499 ? 198 THR A CB  1 
ATOM   1495 O OG1 . THR A 1 198 ? -20.76878 22.77123  25.30089  1.000 32.31654 ? 198 THR A OG1 1 
ATOM   1496 C CG2 . THR A 1 198 ? -21.06281 25.03096  26.10685  1.000 27.15083 ? 198 THR A CG2 1 
ATOM   1497 N N   . THR A 1 199 ? -17.13918 23.14623  26.13596  1.000 23.41769 ? 199 THR A N   1 
ATOM   1498 C CA  . THR A 1 199 ? -16.10714 22.12956  26.26587  1.000 26.17891 ? 199 THR A CA  1 
ATOM   1499 C C   . THR A 1 199 ? -16.69606 20.83394  26.82225  1.000 25.25215 ? 199 THR A C   1 
ATOM   1500 O O   . THR A 1 199 ? -17.59708 20.86423  27.66837  1.000 26.92129 ? 199 THR A O   1 
ATOM   1501 C CB  . THR A 1 199 ? -14.96874 22.63678  27.15764  1.000 23.24280 ? 199 THR A CB  1 
ATOM   1502 O OG1 . THR A 1 199 ? -14.40824 23.82865  26.59113  1.000 29.15690 ? 199 THR A OG1 1 
ATOM   1503 C CG2 . THR A 1 199 ? -13.88939 21.56961  27.26365  1.000 23.33787 ? 199 THR A CG2 1 
ATOM   1504 N N   . ILE A 1 200 ? -16.19733 19.69683  26.32732  1.000 24.18494 ? 200 ILE A N   1 
ATOM   1505 C CA  . ILE A 1 200 ? -16.73100 18.37538  26.68619  1.000 22.13942 ? 200 ILE A CA  1 
ATOM   1506 C C   . ILE A 1 200 ? -16.02225 17.94613  27.97146  1.000 26.19730 ? 200 ILE A C   1 
ATOM   1507 O O   . ILE A 1 200 ? -14.94964 17.33630  27.94992  1.000 23.02574 ? 200 ILE A O   1 
ATOM   1508 C CB  . ILE A 1 200 ? -16.55213 17.35068  25.55909  1.000 21.69027 ? 200 ILE A CB  1 
ATOM   1509 C CG1 . ILE A 1 200 ? -17.11228 17.89154  24.23332  1.000 26.66766 ? 200 ILE A CG1 1 
ATOM   1510 C CG2 . ILE A 1 200 ? -17.17352 16.01383  25.95958  1.000 20.58292 ? 200 ILE A CG2 1 
ATOM   1511 C CD1 . ILE A 1 200 ? -16.62053 17.10422  23.00929  1.000 20.26107 ? 200 ILE A CD1 1 
ATOM   1512 N N   . THR A 1 201 ? -16.66407 18.21615  29.10803  1.000 23.59140 ? 201 THR A N   1 
ATOM   1513 C CA  . THR A 1 201 ? -15.99681 18.09708  30.40939  1.000 23.66539 ? 201 THR A CA  1 
ATOM   1514 C C   . THR A 1 201 ? -15.54604 16.66253  30.70358  1.000 23.12024 ? 201 THR A C   1 
ATOM   1515 O O   . THR A 1 201 ? -14.41455 16.43288  31.14092  1.000 23.94940 ? 201 THR A O   1 
ATOM   1516 C CB  . THR A 1 201 ? -16.93176 18.59373  31.51541  1.000 25.85527 ? 201 THR A CB  1 
ATOM   1517 O OG1 . THR A 1 201 ? -17.36344 19.92106  31.20583  1.000 23.07494 ? 201 THR A OG1 1 
ATOM   1518 C CG2 . THR A 1 201 ? -16.20550 18.59491  32.89358  1.000 24.01567 ? 201 THR A CG2 1 
ATOM   1519 N N   . VAL A 1 202 ? -16.42229 15.68137  30.49294  1.000 21.28263 ? 202 VAL A N   1 
ATOM   1520 C CA  . VAL A 1 202 ? -16.02432 14.30655  30.78044  1.000 23.26244 ? 202 VAL A CA  1 
ATOM   1521 C C   . VAL A 1 202 ? -14.80008 13.90203  29.96225  1.000 25.06389 ? 202 VAL A C   1 
ATOM   1522 O O   . VAL A 1 202 ? -13.96460 13.11308  30.43150  1.000 22.64951 ? 202 VAL A O   1 
ATOM   1523 C CB  . VAL A 1 202 ? -17.20078 13.33864  30.54594  1.000 23.77161 ? 202 VAL A CB  1 
ATOM   1524 C CG1 . VAL A 1 202 ? -17.63983 13.36132  29.07185  1.000 25.03032 ? 202 VAL A CG1 1 
ATOM   1525 C CG2 . VAL A 1 202 ? -16.81571 11.91685  30.99997  1.000 23.46149 ? 202 VAL A CG2 1 
ATOM   1526 N N   . ASN A 1 203 ? -14.67358 14.42111  28.73303  1.000 23.75823 ? 203 ASN A N   1 
ATOM   1527 C CA  . ASN A 1 203 ? -13.50620 14.11184  27.90901  1.000 22.72427 ? 203 ASN A CA  1 
ATOM   1528 C C   . ASN A 1 203 ? -12.24678 14.74692  28.47861  1.000 25.41980 ? 203 ASN A C   1 
ATOM   1529 O O   . ASN A 1 203 ? -11.17477 14.12605  28.46598  1.000 23.27741 ? 203 ASN A O   1 
ATOM   1530 C CB  . ASN A 1 203 ? -13.72423 14.58805  26.45996  1.000 17.86232 ? 203 ASN A CB  1 
ATOM   1531 C CG  . ASN A 1 203 ? -14.69776 13.70702  25.69078  1.000 26.35590 ? 203 ASN A CG  1 
ATOM   1532 O OD1 . ASN A 1 203 ? -15.30221 12.78583  26.25508  1.000 21.84865 ? 203 ASN A OD1 1 
ATOM   1533 N ND2 . ASN A 1 203 ? -14.85579 13.98466  24.38917  1.000 21.87574 ? 203 ASN A ND2 1 
ATOM   1534 N N   . VAL A 1 204 ? -12.34337 15.99996  28.93298  1.000 22.24267 ? 204 VAL A N   1 
ATOM   1535 C CA  . VAL A 1 204 ? -11.19210 16.65589  29.55747  1.000 23.85462 ? 204 VAL A CA  1 
ATOM   1536 C C   . VAL A 1 204 ? -10.71809 15.84838  30.75659  1.000 22.83341 ? 204 VAL A C   1 
ATOM   1537 O O   . VAL A 1 204 ? -9.51505  15.67945  30.97627  1.000 20.80846 ? 204 VAL A O   1 
ATOM   1538 C CB  . VAL A 1 204 ? -11.53719 18.10757  29.96388  1.000 21.92588 ? 204 VAL A CB  1 
ATOM   1539 C CG1 . VAL A 1 204 ? -10.36736 18.75373  30.72777  1.000 21.04529 ? 204 VAL A CG1 1 
ATOM   1540 C CG2 . VAL A 1 204 ? -11.88752 18.96325  28.73269  1.000 23.05662 ? 204 VAL A CG2 1 
ATOM   1541 N N   . LEU A 1 205 ? -11.65282 15.34579  31.56040  1.000 17.25903 ? 205 LEU A N   1 
ATOM   1542 C CA  . LEU A 1 205 ? -11.24482 14.57274  32.72610  1.000 23.35200 ? 205 LEU A CA  1 
ATOM   1543 C C   . LEU A 1 205 ? -10.59074 13.25945  32.30556  1.000 26.04479 ? 205 LEU A C   1 
ATOM   1544 O O   . LEU A 1 205 ? -9.57409  12.85726  32.88395  1.000 24.54574 ? 205 LEU A O   1 
ATOM   1545 C CB  . LEU A 1 205 ? -12.44752 14.31919  33.63194  1.000 22.54346 ? 205 LEU A CB  1 
ATOM   1546 C CG  . LEU A 1 205 ? -12.95432 15.48896  34.46767  1.000 22.51017 ? 205 LEU A CG  1 
ATOM   1547 C CD1 . LEU A 1 205 ? -14.36498 15.13686  34.92632  1.000 23.65009 ? 205 LEU A CD1 1 
ATOM   1548 C CD2 . LEU A 1 205 ? -12.01895 15.74954  35.66341  1.000 25.39881 ? 205 LEU A CD2 1 
ATOM   1549 N N   . ALA A 1 206 ? -11.14825 12.58213  31.28841  1.000 24.24462 ? 206 ALA A N   1 
ATOM   1550 C CA  . ALA A 1 206 ? -10.50491 11.36782  30.77966  1.000 26.94164 ? 206 ALA A CA  1 
ATOM   1551 C C   . ALA A 1 206 ? -9.06804  11.65342  30.33727  1.000 22.76346 ? 206 ALA A C   1 
ATOM   1552 O O   . ALA A 1 206 ? -8.15209  10.85644  30.59002  1.000 24.96111 ? 206 ALA A O   1 
ATOM   1553 C CB  . ALA A 1 206 ? -11.32802 10.78083  29.62086  1.000 21.87055 ? 206 ALA A CB  1 
ATOM   1554 N N   . TRP A 1 207 ? -8.85069  12.80299  29.70572  1.000 22.53492 ? 207 TRP A N   1 
ATOM   1555 C CA  . TRP A 1 207 ? -7.51413  13.17297  29.25083  1.000 23.44803 ? 207 TRP A CA  1 
ATOM   1556 C C   . TRP A 1 207 ? -6.59968  13.52106  30.42497  1.000 25.17225 ? 207 TRP A C   1 
ATOM   1557 O O   . TRP A 1 207 ? -5.40718  13.19478  30.39764  1.000 22.55108 ? 207 TRP A O   1 
ATOM   1558 C CB  . TRP A 1 207 ? -7.64341  14.32199  28.25209  1.000 22.72095 ? 207 TRP A CB  1 
ATOM   1559 C CG  . TRP A 1 207 ? -6.38379  14.97439  27.77589  1.000 27.30305 ? 207 TRP A CG  1 
ATOM   1560 C CD1 . TRP A 1 207 ? -5.54312  14.52986  26.79437  1.000 30.24702 ? 207 TRP A CD1 1 
ATOM   1561 C CD2 . TRP A 1 207 ? -5.87650  16.24270  28.19256  1.000 27.41773 ? 207 TRP A CD2 1 
ATOM   1562 N NE1 . TRP A 1 207 ? -4.51336  15.42335  26.61684  1.000 28.58755 ? 207 TRP A NE1 1 
ATOM   1563 C CE2 . TRP A 1 207 ? -4.70235  16.48602  27.45755  1.000 29.26241 ? 207 TRP A CE2 1 
ATOM   1564 C CE3 . TRP A 1 207 ? -6.28390  17.18302  29.14853  1.000 26.82293 ? 207 TRP A CE3 1 
ATOM   1565 C CZ2 . TRP A 1 207 ? -3.94373  17.63482  27.63303  1.000 32.82969 ? 207 TRP A CZ2 1 
ATOM   1566 C CZ3 . TRP A 1 207 ? -5.53670  18.32100  29.31561  1.000 27.66548 ? 207 TRP A CZ3 1 
ATOM   1567 C CH2 . TRP A 1 207 ? -4.37901  18.53945  28.56499  1.000 31.15499 ? 207 TRP A CH2 1 
ATOM   1568 N N   . LEU A 1 208 ? -7.13417  14.16164  31.47539  1.000 25.30929 ? 208 LEU A N   1 
ATOM   1569 C CA  . LEU A 1 208 ? -6.34301  14.34818  32.70075  1.000 22.71966 ? 208 LEU A CA  1 
ATOM   1570 C C   . LEU A 1 208 ? -5.89450  13.00874  33.28150  1.000 25.77768 ? 208 LEU A C   1 
ATOM   1571 O O   . LEU A 1 208 ? -4.74621  12.87038  33.72431  1.000 25.12404 ? 208 LEU A O   1 
ATOM   1572 C CB  . LEU A 1 208 ? -7.13301  15.16354  33.74244  1.000 20.69264 ? 208 LEU A CB  1 
ATOM   1573 C CG  . LEU A 1 208 ? -7.28605  16.65707  33.40024  1.000 20.85053 ? 208 LEU A CG  1 
ATOM   1574 C CD1 . LEU A 1 208 ? -8.07754  17.43803  34.45672  1.000 22.72563 ? 208 LEU A CD1 1 
ATOM   1575 C CD2 . LEU A 1 208 ? -5.93066  17.33848  33.17566  1.000 22.00252 ? 208 LEU A CD2 1 
ATOM   1576 N N   . TYR A 1 209 ? -6.77820  12.00594  33.28676  1.000 19.36136 ? 209 TYR A N   1 
ATOM   1577 C CA  . TYR A 1 209 ? -6.37321  10.66999  33.72609  1.000 25.57051 ? 209 TYR A CA  1 
ATOM   1578 C C   . TYR A 1 209 ? -5.28206  10.08295  32.82850  1.000 25.93968 ? 209 TYR A C   1 
ATOM   1579 O O   . TYR A 1 209 ? -4.35403  9.42705   33.31300  1.000 27.87295 ? 209 TYR A O   1 
ATOM   1580 C CB  . TYR A 1 209 ? -7.57816  9.73680   33.76823  1.000 27.46551 ? 209 TYR A CB  1 
ATOM   1581 C CG  . TYR A 1 209 ? -8.39994  9.86340   35.03886  1.000 27.53513 ? 209 TYR A CG  1 
ATOM   1582 C CD1 . TYR A 1 209 ? -7.89604  9.43011   36.25787  1.000 26.30530 ? 209 TYR A CD1 1 
ATOM   1583 C CD2 . TYR A 1 209 ? -9.69926  10.37586  35.00521  1.000 26.76769 ? 209 TYR A CD2 1 
ATOM   1584 C CE1 . TYR A 1 209 ? -8.65520  9.53328   37.42364  1.000 28.26920 ? 209 TYR A CE1 1 
ATOM   1585 C CE2 . TYR A 1 209 ? -10.46454 10.47696  36.14716  1.000 26.01054 ? 209 TYR A CE2 1 
ATOM   1586 C CZ  . TYR A 1 209 ? -9.92877  10.06066  37.36152  1.000 27.91090 ? 209 TYR A CZ  1 
ATOM   1587 O OH  . TYR A 1 209 ? -10.66914 10.15449  38.51252  1.000 25.46122 ? 209 TYR A OH  1 
ATOM   1588 N N   . ALA A 1 210 ? -5.38197  10.29948  31.51623  1.000 23.53018 ? 210 ALA A N   1 
ATOM   1589 C CA  . ALA A 1 210 ? -4.32389  9.85974   30.61663  1.000 23.49740 ? 210 ALA A CA  1 
ATOM   1590 C C   . ALA A 1 210 ? -3.00110  10.50649  30.98098  1.000 25.50242 ? 210 ALA A C   1 
ATOM   1591 O O   . ALA A 1 210 ? -1.94666  9.85891   30.92694  1.000 29.44610 ? 210 ALA A O   1 
ATOM   1592 C CB  . ALA A 1 210 ? -4.68382  10.18718  29.16159  1.000 23.86639 ? 210 ALA A CB  1 
ATOM   1593 N N   . ALA A 1 211 ? -3.03064  11.79446  31.32275  1.000 24.77904 ? 211 ALA A N   1 
ATOM   1594 C CA  . ALA A 1 211 ? -1.79637  12.48283  31.67091  1.000 29.08256 ? 211 ALA A CA  1 
ATOM   1595 C C   . ALA A 1 211 ? -1.19655  11.89907  32.94101  1.000 31.07401 ? 211 ALA A C   1 
ATOM   1596 O O   . ALA A 1 211 ? 0.02881   11.77270  33.05232  1.000 28.89489 ? 211 ALA A O   1 
ATOM   1597 C CB  . ALA A 1 211 ? -2.04421  13.97908  31.83398  1.000 28.77219 ? 211 ALA A CB  1 
ATOM   1598 N N   . VAL A 1 212 ? -2.04188  11.52680  33.90680  1.000 24.03690 ? 212 VAL A N   1 
ATOM   1599 C CA  . VAL A 1 212 ? -1.53117  10.88562  35.11453  1.000 24.14477 ? 212 VAL A CA  1 
ATOM   1600 C C   . VAL A 1 212 ? -0.95436  9.51526   34.78197  1.000 30.69605 ? 212 VAL A C   1 
ATOM   1601 O O   . VAL A 1 212 ? 0.16882   9.19177   35.18304  1.000 33.43901 ? 212 VAL A O   1 
ATOM   1602 C CB  . VAL A 1 212 ? -2.62509  10.79960  36.19262  1.000 27.00601 ? 212 VAL A CB  1 
ATOM   1603 C CG1 . VAL A 1 212 ? -2.18957  9.85982   37.32216  1.000 34.70734 ? 212 VAL A CG1 1 
ATOM   1604 C CG2 . VAL A 1 212 ? -2.90991  12.18716  36.75988  1.000 25.80460 ? 212 VAL A CG2 1 
ATOM   1605 N N   . ILE A 1 213 ? -1.69664  8.69429   34.02356  1.000 31.34193 ? 213 ILE A N   1 
ATOM   1606 C CA  . ILE A 1 213 ? -1.16331  7.37385   33.67553  1.000 28.79148 ? 213 ILE A CA  1 
ATOM   1607 C C   . ILE A 1 213 ? 0.21710   7.51016   33.05088  1.000 31.62783 ? 213 ILE A C   1 
ATOM   1608 O O   . ILE A 1 213 ? 1.08721   6.65998   33.25736  1.000 35.61750 ? 213 ILE A O   1 
ATOM   1609 C CB  . ILE A 1 213 ? -2.13262  6.60692   32.75517  1.000 27.87956 ? 213 ILE A CB  1 
ATOM   1610 C CG1 . ILE A 1 213 ? -3.46019  6.37510   33.47583  1.000 30.82534 ? 213 ILE A CG1 1 
ATOM   1611 C CG2 . ILE A 1 213 ? -1.52838  5.25961   32.33878  1.000 30.54913 ? 213 ILE A CG2 1 
ATOM   1612 C CD1 . ILE A 1 213 ? -4.54697  5.76095   32.61020  1.000 32.85053 ? 213 ILE A CD1 1 
ATOM   1613 N N   . ASN A 1 214 ? 0.45730   8.59905   32.32412  1.000 29.67971 ? 214 ASN A N   1 
ATOM   1614 C CA  . ASN A 1 214 ? 1.73012   8.83669   31.66105  1.000 30.04916 ? 214 ASN A CA  1 
ATOM   1615 C C   . ASN A 1 214 ? 2.69490   9.69395   32.47141  1.000 31.34532 ? 214 ASN A C   1 
ATOM   1616 O O   . ASN A 1 214 ? 3.63230   10.25493  31.89329  1.000 32.42552 ? 214 ASN A O   1 
ATOM   1617 C CB  . ASN A 1 214 ? 1.48978   9.46904   30.29368  1.000 30.96107 ? 214 ASN A CB  1 
ATOM   1618 C CG  . ASN A 1 214 ? 1.09821   8.44293   29.26274  1.000 33.31710 ? 214 ASN A CG  1 
ATOM   1619 O OD1 . ASN A 1 214 ? 1.96440   7.83153   28.63760  1.000 36.62175 ? 214 ASN A OD1 1 
ATOM   1620 N ND2 . ASN A 1 214 ? -0.20699  8.20800   29.10956  1.000 30.70918 ? 214 ASN A ND2 1 
ATOM   1621 N N   . GLY A 1 215 ? 2.50065   9.80238   33.78628  1.000 33.05703 ? 215 GLY A N   1 
ATOM   1622 C CA  . GLY A 1 215 ? 3.46465   10.46932  34.63831  1.000 31.86326 ? 215 GLY A CA  1 
ATOM   1623 C C   . GLY A 1 215 ? 3.43883   11.98083  34.63681  1.000 35.58483 ? 215 GLY A C   1 
ATOM   1624 O O   . GLY A 1 215 ? 4.39795   12.59612  35.11534  1.000 36.34589 ? 215 GLY A O   1 
ATOM   1625 N N   . ASP A 1 216 ? 2.38175   12.60409  34.12319  1.000 33.62540 ? 216 ASP A N   1 
ATOM   1626 C CA  . ASP A 1 216 ? 2.22090   14.05438  34.15309  1.000 29.63942 ? 216 ASP A CA  1 
ATOM   1627 C C   . ASP A 1 216 ? 1.22924   14.36040  35.27227  1.000 36.91632 ? 216 ASP A C   1 
ATOM   1628 O O   . ASP A 1 216 ? 0.02048   14.19633  35.09200  1.000 34.26997 ? 216 ASP A O   1 
ATOM   1629 C CB  . ASP A 1 216 ? 1.71616   14.54981  32.80218  1.000 36.32577 ? 216 ASP A CB  1 
ATOM   1630 C CG  . ASP A 1 216 ? 2.33531   15.85926  32.38236  1.000 41.51201 ? 216 ASP A CG  1 
ATOM   1631 O OD1 . ASP A 1 216 ? 3.01540   16.48452  33.21644  1.000 41.88186 ? 216 ASP A OD1 1 
ATOM   1632 O OD2 . ASP A 1 216 ? 2.13532   16.26056  31.20602  1.000 37.58701 ? 216 ASP A OD2 1 
ATOM   1633 N N   . ARG A 1 217 ? 1.73467   14.81252  36.42960  1.000 30.95976 ? 217 ARG A N   1 
ATOM   1634 C CA  . ARG A 1 217 ? 0.92410   14.91876  37.64367  1.000 31.25151 ? 217 ARG A CA  1 
ATOM   1635 C C   . ARG A 1 217 ? 0.86633   16.30513  38.27288  1.000 30.51658 ? 217 ARG A C   1 
ATOM   1636 O O   . ARG A 1 217 ? 0.25675   16.45374  39.33977  1.000 30.59177 ? 217 ARG A O   1 
ATOM   1637 C CB  . ARG A 1 217 ? 1.44314   13.95571  38.72046  1.000 34.87527 ? 217 ARG A CB  1 
ATOM   1638 C CG  . ARG A 1 217 ? 1.51432   12.51196  38.31269  1.000 35.31503 ? 217 ARG A CG  1 
ATOM   1639 C CD  . ARG A 1 217 ? 2.14765   11.69330  39.42317  1.000 30.65576 ? 217 ARG A CD  1 
ATOM   1640 N NE  . ARG A 1 217 ? 1.39312   11.79292  40.66328  1.000 30.46597 ? 217 ARG A NE  1 
ATOM   1641 C CZ  . ARG A 1 217 ? 0.44388   10.94064  41.02072  1.000 36.86850 ? 217 ARG A CZ  1 
ATOM   1642 N NH1 . ARG A 1 217 ? 0.10873   9.91951   40.25121  1.000 32.04059 ? 217 ARG A NH1 1 
ATOM   1643 N NH2 . ARG A 1 217 ? -0.17514  11.10825  42.18392  1.000 32.06176 ? 217 ARG A NH2 1 
ATOM   1644 N N   . TRP A 1 218 ? 1.46645   17.32093  37.66132  1.000 28.52411 ? 218 TRP A N   1 
ATOM   1645 C CA  . TRP A 1 218 ? 1.66720   18.58085  38.36845  1.000 28.22168 ? 218 TRP A CA  1 
ATOM   1646 C C   . TRP A 1 218 ? 0.36798   19.26390  38.77153  1.000 29.84689 ? 218 TRP A C   1 
ATOM   1647 O O   . TRP A 1 218 ? 0.37807   20.05803  39.71727  1.000 31.72973 ? 218 TRP A O   1 
ATOM   1648 C CB  . TRP A 1 218 ? 2.51346   19.52930  37.52412  1.000 29.79520 ? 218 TRP A CB  1 
ATOM   1649 C CG  . TRP A 1 218 ? 1.88091   19.98660  36.23127  1.000 36.88315 ? 218 TRP A CG  1 
ATOM   1650 C CD1 . TRP A 1 218 ? 2.08333   19.46316  34.97982  1.000 35.61156 ? 218 TRP A CD1 1 
ATOM   1651 C CD2 . TRP A 1 218 ? 0.97496   21.08751  36.06453  1.000 33.77516 ? 218 TRP A CD2 1 
ATOM   1652 N NE1 . TRP A 1 218 ? 1.34526   20.16594  34.04975  1.000 31.23965 ? 218 TRP A NE1 1 
ATOM   1653 C CE2 . TRP A 1 218 ? 0.65803   21.16507  34.69146  1.000 34.30326 ? 218 TRP A CE2 1 
ATOM   1654 C CE3 . TRP A 1 218 ? 0.38958   22.00456  36.94599  1.000 27.19203 ? 218 TRP A CE3 1 
ATOM   1655 C CZ2 . TRP A 1 218 ? -0.21368  22.12067  34.18467  1.000 32.88616 ? 218 TRP A CZ2 1 
ATOM   1656 C CZ3 . TRP A 1 218 ? -0.46937  22.95783  36.43917  1.000 38.66866 ? 218 TRP A CZ3 1 
ATOM   1657 C CH2 . TRP A 1 218 ? -0.76651  23.00968  35.06902  1.000 35.78053 ? 218 TRP A CH2 1 
ATOM   1658 N N   . PHE A 1 219 ? -0.74235  18.97156  38.09862  1.000 27.45971 ? 219 PHE A N   1 
ATOM   1659 C CA  . PHE A 1 219 ? -2.01160  19.66451  38.30524  1.000 26.48810 ? 219 PHE A CA  1 
ATOM   1660 C C   . PHE A 1 219 ? -2.85612  19.05267  39.41843  1.000 26.37115 ? 219 PHE A C   1 
ATOM   1661 O O   . PHE A 1 219 ? -3.93290  19.58494  39.72444  1.000 27.50808 ? 219 PHE A O   1 
ATOM   1662 C CB  . PHE A 1 219 ? -2.81114  19.65839  36.98946  1.000 23.85256 ? 219 PHE A CB  1 
ATOM   1663 C CG  . PHE A 1 219 ? -2.88987  18.29641  36.37275  1.000 21.65567 ? 219 PHE A CG  1 
ATOM   1664 C CD1 . PHE A 1 219 ? -3.86889  17.40126  36.76634  1.000 27.45308 ? 219 PHE A CD1 1 
ATOM   1665 C CD2 . PHE A 1 219 ? -1.92779  17.88287  35.46883  1.000 24.74496 ? 219 PHE A CD2 1 
ATOM   1666 C CE1 . PHE A 1 219 ? -3.92001  16.12358  36.23042  1.000 25.64496 ? 219 PHE A CE1 1 
ATOM   1667 C CE2 . PHE A 1 219 ? -1.97395  16.61196  34.92773  1.000 28.28366 ? 219 PHE A CE2 1 
ATOM   1668 C CZ  . PHE A 1 219 ? -2.96714  15.73418  35.31303  1.000 27.11515 ? 219 PHE A CZ  1 
ATOM   1669 N N   . LEU A 1 220 ? -2.41141  17.94970  40.02080  1.000 24.90345 ? 220 LEU A N   1 
ATOM   1670 C CA  . LEU A 1 220 ? -3.17721  17.31077  41.08290  1.000 25.00781 ? 220 LEU A CA  1 
ATOM   1671 C C   . LEU A 1 220 ? -3.10007  18.13066  42.36702  1.000 28.00369 ? 220 LEU A C   1 
ATOM   1672 O O   . LEU A 1 220 ? -2.15291  18.88624  42.58643  1.000 30.31638 ? 220 LEU A O   1 
ATOM   1673 C CB  . LEU A 1 220 ? -2.65798  15.89095  41.32962  1.000 27.93999 ? 220 LEU A CB  1 
ATOM   1674 C CG  . LEU A 1 220 ? -2.72280  14.92551  40.14063  1.000 27.44449 ? 220 LEU A CG  1 
ATOM   1675 C CD1 . LEU A 1 220 ? -2.12327  13.57931  40.52335  1.000 25.44900 ? 220 LEU A CD1 1 
ATOM   1676 C CD2 . LEU A 1 220 ? -4.17037  14.74888  39.65520  1.000 23.88561 ? 220 LEU A CD2 1 
ATOM   1677 N N   . ASN A 1 221 ? -4.12579  17.99704  43.20866  1.000 27.69110 ? 221 ASN A N   1 
ATOM   1678 C CA  . ASN A 1 221 ? -4.13721  18.65291  44.50716  1.000 36.26977 ? 221 ASN A CA  1 
ATOM   1679 C C   . ASN A 1 221 ? -4.77465  17.71733  45.52994  1.000 31.95911 ? 221 ASN A C   1 
ATOM   1680 O O   . ASN A 1 221 ? -5.24029  16.61754  45.20490  1.000 28.34046 ? 221 ASN A O   1 
ATOM   1681 C CB  . ASN A 1 221 ? -4.82808  20.02889  44.43702  1.000 30.06033 ? 221 ASN A CB  1 
ATOM   1682 C CG  . ASN A 1 221 ? -6.32216  19.94868  44.11961  1.000 30.20016 ? 221 ASN A CG  1 
ATOM   1683 O OD1 . ASN A 1 221 ? -7.00109  18.97704  44.42920  1.000 31.47327 ? 221 ASN A OD1 1 
ATOM   1684 N ND2 . ASN A 1 221 ? -6.83666  21.00470  43.49930  1.000 34.58025 ? 221 ASN A ND2 1 
ATOM   1685 N N   . ARG A 1 222 ? -4.77772  18.16423  46.78110  1.000 32.04469 ? 222 ARG A N   1 
ATOM   1686 C CA  . ARG A 1 222 ? -5.20079  17.35709  47.91232  1.000 40.90964 ? 222 ARG A CA  1 
ATOM   1687 C C   . ARG A 1 222 ? -6.69370  17.46368  48.17417  1.000 37.65685 ? 222 ARG A C   1 
ATOM   1688 O O   . ARG A 1 222 ? -7.19142  16.82694  49.10572  1.000 45.40900 ? 222 ARG A O   1 
ATOM   1689 C CB  . ARG A 1 222 ? -4.42464  17.77081  49.17331  1.000 37.18696 ? 222 ARG A CB  1 
ATOM   1690 C CG  . ARG A 1 222 ? -4.81904  19.13949  49.71688  1.000 50.15079 ? 222 ARG A CG  1 
ATOM   1691 C CD  . ARG A 1 222 ? -4.50248  19.27655  51.20868  1.000 55.19258 ? 222 ARG A CD  1 
ATOM   1692 N NE  . ARG A 1 222 ? -3.33983  20.12113  51.44921  1.000 61.61995 ? 222 ARG A NE  1 
ATOM   1693 C CZ  . ARG A 1 222 ? -2.73987  20.25720  52.62642  1.000 69.93646 ? 222 ARG A CZ  1 
ATOM   1694 N NH1 . ARG A 1 222 ? -3.17687  19.62388  53.70414  1.000 64.22131 ? 222 ARG A NH1 1 
ATOM   1695 N NH2 . ARG A 1 222 ? -1.66834  21.04302  52.72431  1.000 65.89697 ? 222 ARG A NH2 1 
ATOM   1696 N N   . PHE A 1 223 ? -7.42020  18.22144  47.36341  1.000 36.16325 ? 223 PHE A N   1 
ATOM   1697 C CA  . PHE A 1 223 ? -8.81033  18.54179  47.64410  1.000 37.62619 ? 223 PHE A CA  1 
ATOM   1698 C C   . PHE A 1 223 ? -9.77174  17.69142  46.81882  1.000 36.72210 ? 223 PHE A C   1 
ATOM   1699 O O   . PHE A 1 223 ? -9.42138  17.11372  45.78211  1.000 30.66032 ? 223 PHE A O   1 
ATOM   1700 C CB  . PHE A 1 223 ? -9.07497  20.03093  47.38792  1.000 34.68764 ? 223 PHE A CB  1 
ATOM   1701 C CG  . PHE A 1 223 ? -8.21795  20.94748  48.22150  1.000 44.56432 ? 223 PHE A CG  1 
ATOM   1702 C CD1 . PHE A 1 223 ? -8.33157  20.95259  49.60640  1.000 47.76706 ? 223 PHE A CD1 1 
ATOM   1703 C CD2 . PHE A 1 223 ? -7.29760  21.79335  47.62680  1.000 36.88854 ? 223 PHE A CD2 1 
ATOM   1704 C CE1 . PHE A 1 223 ? -7.54190  21.79184  50.38363  1.000 48.20184 ? 223 PHE A CE1 1 
ATOM   1705 C CE2 . PHE A 1 223 ? -6.50361  22.63740  48.39750  1.000 49.82491 ? 223 PHE A CE2 1 
ATOM   1706 C CZ  . PHE A 1 223 ? -6.62566  22.63572  49.77639  1.000 39.75092 ? 223 PHE A CZ  1 
ATOM   1707 N N   . THR A 1 224 ? -11.00290 17.62313  47.30729  1.000 28.39740 ? 224 THR A N   1 
ATOM   1708 C CA  . THR A 1 224 ? -12.11546 17.00706  46.60906  1.000 32.87872 ? 224 THR A CA  1 
ATOM   1709 C C   . THR A 1 224 ? -13.22983 18.04123  46.50198  1.000 37.73033 ? 224 THR A C   1 
ATOM   1710 O O   . THR A 1 224 ? -13.14578 19.12395  47.08568  1.000 37.54736 ? 224 THR A O   1 
ATOM   1711 C CB  . THR A 1 224 ? -12.59585 15.74718  47.33540  1.000 38.48542 ? 224 THR A CB  1 
ATOM   1712 O OG1 . THR A 1 224 ? -13.49772 15.02344  46.49476  1.000 43.24843 ? 224 THR A OG1 1 
ATOM   1713 C CG2 . THR A 1 224 ? -13.31707 16.11336  48.62676  1.000 36.32194 ? 224 THR A CG2 1 
ATOM   1714 N N   . THR A 1 225 ? -14.26805 17.71664  45.73001  1.000 28.45923 ? 225 THR A N   1 
ATOM   1715 C CA  . THR A 1 225 ? -15.40737 18.61285  45.58443  1.000 29.09585 ? 225 THR A CA  1 
ATOM   1716 C C   . THR A 1 225 ? -16.66874 17.78381  45.40465  1.000 29.01199 ? 225 THR A C   1 
ATOM   1717 O O   . THR A 1 225 ? -16.61115 16.60585  45.04861  1.000 35.13922 ? 225 THR A O   1 
ATOM   1718 C CB  . THR A 1 225 ? -15.21880 19.56392  44.39443  1.000 29.36622 ? 225 THR A CB  1 
ATOM   1719 O OG1 . THR A 1 225 ? -16.35491 20.43558  44.27593  1.000 32.74653 ? 225 THR A OG1 1 
ATOM   1720 C CG2 . THR A 1 225 ? -15.07883 18.75874  43.09525  1.000 32.02338 ? 225 THR A CG2 1 
ATOM   1721 N N   . THR A 1 226 ? -17.81859 18.40786  45.63596  1.000 28.91134 ? 226 THR A N   1 
ATOM   1722 C CA  . THR A 1 226 ? -19.07490 17.73333  45.33104  1.000 26.28790 ? 226 THR A CA  1 
ATOM   1723 C C   . THR A 1 226 ? -19.35613 17.78959  43.83294  1.000 27.54824 ? 226 THR A C   1 
ATOM   1724 O O   . THR A 1 226 ? -18.88645 18.68794  43.12660  1.000 30.89200 ? 226 THR A O   1 
ATOM   1725 C CB  . THR A 1 226 ? -20.24109 18.36134  46.09612  1.000 27.03655 ? 226 THR A CB  1 
ATOM   1726 O OG1 . THR A 1 226 ? -20.51555 19.66164  45.55804  1.000 28.26877 ? 226 THR A OG1 1 
ATOM   1727 C CG2 . THR A 1 226 ? -19.89184 18.47628  47.58037  1.000 29.90714 ? 226 THR A CG2 1 
ATOM   1728 N N   . LEU A 1 227 ? -20.12382 16.80964  43.34282  1.000 24.14211 ? 227 LEU A N   1 
ATOM   1729 C CA  . LEU A 1 227 ? -20.48178 16.82188  41.92467  1.000 24.53765 ? 227 LEU A CA  1 
ATOM   1730 C C   . LEU A 1 227 ? -21.20718 18.11476  41.56677  1.000 32.93979 ? 227 LEU A C   1 
ATOM   1731 O O   . LEU A 1 227 ? -20.90910 18.74420  40.54160  1.000 26.88751 ? 227 LEU A O   1 
ATOM   1732 C CB  . LEU A 1 227 ? -21.32916 15.58974  41.57469  1.000 25.39500 ? 227 LEU A CB  1 
ATOM   1733 C CG  . LEU A 1 227 ? -21.81260 15.41683  40.12021  1.000 28.07556 ? 227 LEU A CG  1 
ATOM   1734 C CD1 . LEU A 1 227 ? -20.61564 15.36545  39.18119  1.000 25.64375 ? 227 LEU A CD1 1 
ATOM   1735 C CD2 . LEU A 1 227 ? -22.69567 14.17165  39.92533  1.000 32.27246 ? 227 LEU A CD2 1 
ATOM   1736 N N   . ASN A 1 228 ? -22.14400 18.55081  42.41538  1.000 25.64863 ? 228 ASN A N   1 
ATOM   1737 C CA  . ASN A 1 228 ? -22.90360 19.75263  42.08711  1.000 28.58893 ? 228 ASN A CA  1 
ATOM   1738 C C   . ASN A 1 228 ? -22.03521 21.00028  42.13924  1.000 27.71349 ? 228 ASN A C   1 
ATOM   1739 O O   . ASN A 1 228 ? -22.17867 21.89121  41.29199  1.000 31.52441 ? 228 ASN A O   1 
ATOM   1740 C CB  . ASN A 1 228 ? -24.09695 19.93576  43.02041  1.000 30.24498 ? 228 ASN A CB  1 
ATOM   1741 C CG  . ASN A 1 228 ? -24.92700 21.14616  42.63691  1.000 34.02076 ? 228 ASN A CG  1 
ATOM   1742 O OD1 . ASN A 1 228 ? -25.72741 21.07331  41.71843  1.000 40.39754 ? 228 ASN A OD1 1 
ATOM   1743 N ND2 . ASN A 1 228 ? -24.70459 22.27968  43.31370  1.000 33.20105 ? 228 ASN A ND2 1 
ATOM   1744 N N   . ASP A 1 229 ? -21.15866 21.10884  43.13862  1.000 28.00134 ? 229 ASP A N   1 
ATOM   1745 C CA  . ASP A 1 229 ? -20.32386 22.29959  43.21703  1.000 26.57349 ? 229 ASP A CA  1 
ATOM   1746 C C   . ASP A 1 229 ? -19.34353 22.35051  42.06097  1.000 31.04933 ? 229 ASP A C   1 
ATOM   1747 O O   . ASP A 1 229 ? -18.99750 23.44448  41.59479  1.000 26.93245 ? 229 ASP A O   1 
ATOM   1748 C CB  . ASP A 1 229 ? -19.58752 22.36509  44.55594  1.000 28.90287 ? 229 ASP A CB  1 
ATOM   1749 C CG  . ASP A 1 229 ? -20.53244 22.62395  45.71821  1.000 37.40680 ? 229 ASP A CG  1 
ATOM   1750 O OD1 . ASP A 1 229 ? -21.49574 23.40803  45.53171  1.000 33.66966 ? 229 ASP A OD1 1 
ATOM   1751 O OD2 . ASP A 1 229 ? -20.32881 22.02215  46.79738  1.000 41.44757 ? 229 ASP A OD2 1 
ATOM   1752 N N   . PHE A 1 230 ? -18.89262 21.18729  41.58426  1.000 24.43761 ? 230 PHE A N   1 
ATOM   1753 C CA  . PHE A 1 230 ? -18.06703 21.17236  40.37875  1.000 27.89560 ? 230 PHE A CA  1 
ATOM   1754 C C   . PHE A 1 230 ? -18.85650 21.63737  39.16039  1.000 26.93219 ? 230 PHE A C   1 
ATOM   1755 O O   . PHE A 1 230 ? -18.37693 22.47183  38.38210  1.000 25.58120 ? 230 PHE A O   1 
ATOM   1756 C CB  . PHE A 1 230 ? -17.48284 19.78011  40.12926  1.000 27.97925 ? 230 PHE A CB  1 
ATOM   1757 C CG  . PHE A 1 230 ? -16.80876 19.66733  38.78807  1.000 26.62926 ? 230 PHE A CG  1 
ATOM   1758 C CD1 . PHE A 1 230 ? -15.54052 20.19490  38.59515  1.000 27.71322 ? 230 PHE A CD1 1 
ATOM   1759 C CD2 . PHE A 1 230 ? -17.46339 19.08709  37.70969  1.000 23.69347 ? 230 PHE A CD2 1 
ATOM   1760 C CE1 . PHE A 1 230 ? -14.92397 20.11917  37.35275  1.000 27.23934 ? 230 PHE A CE1 1 
ATOM   1761 C CE2 . PHE A 1 230 ? -16.85256 19.00560  36.46681  1.000 27.75312 ? 230 PHE A CE2 1 
ATOM   1762 C CZ  . PHE A 1 230 ? -15.58584 19.52528  36.28982  1.000 23.35687 ? 230 PHE A CZ  1 
ATOM   1763 N N   . ASN A 1 231 ? -20.07927 21.11565  38.97496  1.000 24.56727 ? 231 ASN A N   1 
ATOM   1764 C CA  . ASN A 1 231 ? -20.87189 21.50637  37.80976  1.000 24.92590 ? 231 ASN A CA  1 
ATOM   1765 C C   . ASN A 1 231 ? -21.18340 23.00265  37.81095  1.000 22.73912 ? 231 ASN A C   1 
ATOM   1766 O O   . ASN A 1 231 ? -21.25568 23.62803  36.74646  1.000 22.70815 ? 231 ASN A O   1 
ATOM   1767 C CB  . ASN A 1 231 ? -22.17061 20.69527  37.72985  1.000 25.15289 ? 231 ASN A CB  1 
ATOM   1768 C CG  . ASN A 1 231 ? -21.92754 19.23445  37.33871  1.000 31.64446 ? 231 ASN A CG  1 
ATOM   1769 O OD1 . ASN A 1 231 ? -20.90752 18.90331  36.74206  1.000 30.53691 ? 231 ASN A OD1 1 
ATOM   1770 N ND2 . ASN A 1 231 ? -22.86672 18.36718  37.67225  1.000 27.63861 ? 231 ASN A ND2 1 
ATOM   1771 N N   . LEU A 1 232 ? -21.39022 23.59418  38.98328  1.000 22.15219 ? 232 LEU A N   1 
ATOM   1772 C CA  . LEU A 1 232 ? -21.63123 25.03695  39.02528  1.000 24.32710 ? 232 LEU A CA  1 
ATOM   1773 C C   . LEU A 1 232 ? -20.47048 25.80437  38.39993  1.000 24.54016 ? 232 LEU A C   1 
ATOM   1774 O O   . LEU A 1 232 ? -20.67251 26.69001  37.56112  1.000 23.51055 ? 232 LEU A O   1 
ATOM   1775 C CB  . LEU A 1 232 ? -21.86074 25.48897  40.46744  1.000 23.46798 ? 232 LEU A CB  1 
ATOM   1776 C CG  . LEU A 1 232 ? -23.20245 25.09322  41.09075  1.000 26.09516 ? 232 LEU A CG  1 
ATOM   1777 C CD1 . LEU A 1 232 ? -23.22791 25.44242  42.57751  1.000 29.76260 ? 232 LEU A CD1 1 
ATOM   1778 C CD2 . LEU A 1 232 ? -24.34685 25.77024  40.35835  1.000 31.81718 ? 232 LEU A CD2 1 
ATOM   1779 N N   . VAL A 1 233 ? -19.24096 25.47609  38.79947  1.000 21.20838 ? 233 VAL A N   1 
ATOM   1780 C CA  . VAL A 1 233 ? -18.07614 26.17450  38.27493  1.000 26.10896 ? 233 VAL A CA  1 
ATOM   1781 C C   . VAL A 1 233 ? -17.87598 25.85852  36.79456  1.000 29.36149 ? 233 VAL A C   1 
ATOM   1782 O O   . VAL A 1 233 ? -17.61142 26.76025  35.98601  1.000 27.91808 ? 233 VAL A O   1 
ATOM   1783 C CB  . VAL A 1 233 ? -16.83639 25.82463  39.12004  1.000 27.14257 ? 233 VAL A CB  1 
ATOM   1784 C CG1 . VAL A 1 233 ? -15.58348 26.44194  38.51300  1.000 27.96485 ? 233 VAL A CG1 1 
ATOM   1785 C CG2 . VAL A 1 233 ? -17.02701 26.28670  40.58023  1.000 25.58813 ? 233 VAL A CG2 1 
ATOM   1786 N N   . ALA A 1 234 ? -18.01152 24.58236  36.40996  1.000 25.25729 ? 234 ALA A N   1 
ATOM   1787 C CA  . ALA A 1 234 ? -17.86909 24.20772  35.00079  1.000 26.82346 ? 234 ALA A CA  1 
ATOM   1788 C C   . ALA A 1 234 ? -18.78884 25.03039  34.10072  1.000 27.20458 ? 234 ALA A C   1 
ATOM   1789 O O   . ALA A 1 234 ? -18.35268 25.61173  33.10056  1.000 27.71089 ? 234 ALA A O   1 
ATOM   1790 C CB  . ALA A 1 234 ? -18.14638 22.71074  34.82662  1.000 24.91442 ? 234 ALA A CB  1 
ATOM   1791 N N   . MET A 1 235 ? -20.08057 25.07038  34.42373  1.000 23.63239 ? 235 MET A N   1 
ATOM   1792 C CA  . MET A 1 235 ? -21.00482 25.80954  33.58263  1.000 24.32182 ? 235 MET A CA  1 
ATOM   1793 C C   . MET A 1 235 ? -20.66648 27.29344  33.55697  1.000 27.86625 ? 235 MET A C   1 
ATOM   1794 O O   . MET A 1 235 ? -20.88356 27.95542  32.53748  1.000 27.85380 ? 235 MET A O   1 
ATOM   1795 C CB  . MET A 1 235 ? -22.43948 25.58173  34.05714  1.000 25.35495 ? 235 MET A CB  1 
ATOM   1796 C CG  . MET A 1 235 ? -22.87828 24.12462  33.93114  1.000 29.82291 ? 235 MET A CG  1 
ATOM   1797 S SD  . MET A 1 235 ? -24.59429 23.86388  34.42852  1.000 37.36488 ? 235 MET A SD  1 
ATOM   1798 C CE  . MET A 1 235 ? -24.47865 24.20440  36.18891  1.000 37.97752 ? 235 MET A CE  1 
ATOM   1799 N N   . LYS A 1 236 ? -20.12077 27.83280  34.65339  1.000 26.05753 ? 236 LYS A N   1 
ATOM   1800 C CA  . LYS A 1 236 ? -19.71295 29.23364  34.64009  1.000 26.70706 ? 236 LYS A CA  1 
ATOM   1801 C C   . LYS A 1 236 ? -18.67351 29.48674  33.55530  1.000 30.80801 ? 236 LYS A C   1 
ATOM   1802 O O   . LYS A 1 236 ? -18.68192 30.54817  32.92195  1.000 29.67724 ? 236 LYS A O   1 
ATOM   1803 C CB  . LYS A 1 236 ? -19.17646 29.64139  36.01621  1.000 22.53150 ? 236 LYS A CB  1 
ATOM   1804 C CG  . LYS A 1 236 ? -18.78010 31.10617  36.13650  1.000 25.97354 ? 236 LYS A CG  1 
ATOM   1805 C CD  . LYS A 1 236 ? -18.03678 31.37772  37.43427  1.000 28.60711 ? 236 LYS A CD  1 
ATOM   1806 C CE  . LYS A 1 236 ? -17.55941 32.83420  37.54278  1.000 30.55087 ? 236 LYS A CE  1 
ATOM   1807 N NZ  . LYS A 1 236 ? -16.67107 33.02032  38.73904  1.000 29.02613 ? 236 LYS A NZ  1 
ATOM   1808 N N   . TYR A 1 237 ? -17.79213 28.51526  33.30598  1.000 27.35242 ? 237 TYR A N   1 
ATOM   1809 C CA  . TYR A 1 237 ? -16.73569 28.64507  32.31328  1.000 29.58957 ? 237 TYR A CA  1 
ATOM   1810 C C   . TYR A 1 237 ? -17.11000 28.04610  30.95917  1.000 27.91843 ? 237 TYR A C   1 
ATOM   1811 O O   . TYR A 1 237 ? -16.22741 27.83729  30.12271  1.000 26.82786 ? 237 TYR A O   1 
ATOM   1812 C CB  . TYR A 1 237 ? -15.44908 28.00782  32.84652  1.000 29.68992 ? 237 TYR A CB  1 
ATOM   1813 C CG  . TYR A 1 237 ? -14.83092 28.80517  33.97363  1.000 31.29754 ? 237 TYR A CG  1 
ATOM   1814 C CD1 . TYR A 1 237 ? -15.24495 28.63617  35.28842  1.000 31.07739 ? 237 TYR A CD1 1 
ATOM   1815 C CD2 . TYR A 1 237 ? -13.84601 29.74873  33.71349  1.000 39.84858 ? 237 TYR A CD2 1 
ATOM   1816 C CE1 . TYR A 1 237 ? -14.68181 29.38512  36.32275  1.000 38.30793 ? 237 TYR A CE1 1 
ATOM   1817 C CE2 . TYR A 1 237 ? -13.28311 30.49750  34.72764  1.000 46.67243 ? 237 TYR A CE2 1 
ATOM   1818 C CZ  . TYR A 1 237 ? -13.70299 30.31411  36.02641  1.000 43.55259 ? 237 TYR A CZ  1 
ATOM   1819 O OH  . TYR A 1 237 ? -13.13511 31.07149  37.01350  1.000 45.07296 ? 237 TYR A OH  1 
ATOM   1820 N N   . ASN A 1 238 ? -18.39459 27.77212  30.72117  1.000 25.30007 ? 238 ASN A N   1 
ATOM   1821 C CA  . ASN A 1 238 ? -18.85904 27.22519  29.44943  1.000 29.33482 ? 238 ASN A CA  1 
ATOM   1822 C C   . ASN A 1 238 ? -18.37347 25.79635  29.20299  1.000 30.69989 ? 238 ASN A C   1 
ATOM   1823 O O   . ASN A 1 238 ? -18.08292 25.41782  28.05867  1.000 29.46183 ? 238 ASN A O   1 
ATOM   1824 C CB  . ASN A 1 238 ? -18.43377 28.12192  28.28916  1.000 38.70694 ? 238 ASN A CB  1 
ATOM   1825 C CG  . ASN A 1 238 ? -19.57660 28.47893  27.40280  1.000 38.65663 ? 238 ASN A CG  1 
ATOM   1826 O OD1 . ASN A 1 238 ? -20.73386 28.20070  27.72144  1.000 34.60296 ? 238 ASN A OD1 1 
ATOM   1827 N ND2 . ASN A 1 238 ? -19.27250 29.11456  26.28411  1.000 47.88942 ? 238 ASN A ND2 1 
ATOM   1828 N N   . TYR A 1 239 ? -18.24201 25.01438  30.26676  1.000 24.36919 ? 239 TYR A N   1 
ATOM   1829 C CA  . TYR A 1 239 ? -18.03923 23.57362  30.19860  1.000 21.35552 ? 239 TYR A CA  1 
ATOM   1830 C C   . TYR A 1 239 ? -19.37307 22.86810  30.40908  1.000 28.52932 ? 239 TYR A C   1 
ATOM   1831 O O   . TYR A 1 239 ? -20.22281 23.32810  31.17635  1.000 25.93716 ? 239 TYR A O   1 
ATOM   1832 C CB  . TYR A 1 239 ? -17.04426 23.08668  31.26508  1.000 24.62258 ? 239 TYR A CB  1 
ATOM   1833 C CG  . TYR A 1 239 ? -15.57392 23.24607  30.89688  1.000 24.34592 ? 239 TYR A CG  1 
ATOM   1834 C CD1 . TYR A 1 239 ? -15.05596 24.48942  30.55687  1.000 31.17840 ? 239 TYR A CD1 1 
ATOM   1835 C CD2 . TYR A 1 239 ? -14.71694 22.15919  30.88570  1.000 35.92063 ? 239 TYR A CD2 1 
ATOM   1836 C CE1 . TYR A 1 239 ? -13.72564 24.64362  30.22154  1.000 32.95418 ? 239 TYR A CE1 1 
ATOM   1837 C CE2 . TYR A 1 239 ? -13.37654 22.30891  30.55216  1.000 33.09636 ? 239 TYR A CE2 1 
ATOM   1838 C CZ  . TYR A 1 239 ? -12.89652 23.55531  30.22354  1.000 30.99774 ? 239 TYR A CZ  1 
ATOM   1839 O OH  . TYR A 1 239 ? -11.57658 23.71814  29.88242  1.000 35.72253 ? 239 TYR A OH  1 
ATOM   1840 N N   . GLU A 1 240 ? -19.54485 21.73539  29.72858  1.000 24.46055 ? 240 GLU A N   1 
ATOM   1841 C CA  . GLU A 1 240 ? -20.73257 20.91904  29.92639  1.000 28.36570 ? 240 GLU A CA  1 
ATOM   1842 C C   . GLU A 1 240 ? -20.80034 20.37450  31.35577  1.000 29.17551 ? 240 GLU A C   1 
ATOM   1843 O O   . GLU A 1 240 ? -19.77070 20.07141  31.96721  1.000 25.54263 ? 240 GLU A O   1 
ATOM   1844 C CB  . GLU A 1 240 ? -20.73215 19.75310  28.94024  1.000 28.03506 ? 240 GLU A CB  1 
ATOM   1845 C CG  . GLU A 1 240 ? -20.89148 20.20537  27.51333  1.000 29.03243 ? 240 GLU A CG  1 
ATOM   1846 C CD  . GLU A 1 240 ? -22.32569 20.56417  27.22073  1.000 35.44557 ? 240 GLU A CD  1 
ATOM   1847 O OE1 . GLU A 1 240 ? -23.19801 19.70961  27.48888  1.000 39.86381 ? 240 GLU A OE1 1 
ATOM   1848 O OE2 . GLU A 1 240 ? -22.58078 21.69116  26.73533  1.000 41.00766 ? 240 GLU A OE2 1 
ATOM   1849 N N   . PRO A 1 241 ? -22.00856 20.19137  31.88706  1.000 26.43294 ? 241 PRO A N   1 
ATOM   1850 C CA  . PRO A 1 241 ? -22.15337 19.53791  33.18487  1.000 30.71623 ? 241 PRO A CA  1 
ATOM   1851 C C   . PRO A 1 241 ? -21.71296 18.08721  33.11727  1.000 30.78965 ? 241 PRO A C   1 
ATOM   1852 O O   . PRO A 1 241 ? -21.78419 17.43338  32.07208  1.000 32.45714 ? 241 PRO A O   1 
ATOM   1853 C CB  . PRO A 1 241 ? -23.65997 19.63500  33.47603  1.000 35.99041 ? 241 PRO A CB  1 
ATOM   1854 C CG  . PRO A 1 241 ? -24.23553 20.49228  32.40637  1.000 33.13149 ? 241 PRO A CG  1 
ATOM   1855 C CD  . PRO A 1 241 ? -23.30812 20.43137  31.24342  1.000 31.41200 ? 241 PRO A CD  1 
ATOM   1856 N N   . LEU A 1 242 ? -21.27153 17.59121  34.26453  1.000 28.69031 ? 242 LEU A N   1 
ATOM   1857 C CA  . LEU A 1 242 ? -20.88501 16.19899  34.45223  1.000 29.84536 ? 242 LEU A CA  1 
ATOM   1858 C C   . LEU A 1 242 ? -22.05447 15.44667  35.06861  1.000 33.27481 ? 242 LEU A C   1 
ATOM   1859 O O   . LEU A 1 242 ? -22.58178 15.86194  36.10324  1.000 30.79715 ? 242 LEU A O   1 
ATOM   1860 C CB  . LEU A 1 242 ? -19.66217 16.11413  35.36786  1.000 28.33049 ? 242 LEU A CB  1 
ATOM   1861 C CG  . LEU A 1 242 ? -18.85708 14.81554  35.47279  1.000 33.13145 ? 242 LEU A CG  1 
ATOM   1862 C CD1 . LEU A 1 242 ? -18.28968 14.43033  34.10292  1.000 33.14127 ? 242 LEU A CD1 1 
ATOM   1863 C CD2 . LEU A 1 242 ? -17.72590 14.97268  36.49016  1.000 29.12544 ? 242 LEU A CD2 1 
ATOM   1864 N N   . THR A 1 243 ? -22.46107 14.35162  34.43514  1.000 34.43303 ? 243 THR A N   1 
ATOM   1865 C CA  . THR A 1 243 ? -23.55717 13.54587  34.94130  1.000 31.43285 ? 243 THR A CA  1 
ATOM   1866 C C   . THR A 1 243 ? -23.01304 12.39850  35.78164  1.000 34.85325 ? 243 THR A C   1 
ATOM   1867 O O   . THR A 1 243 ? -21.81832 12.10126  35.77359  1.000 30.00093 ? 243 THR A O   1 
ATOM   1868 C CB  . THR A 1 243 ? -24.40204 13.00719  33.78605  1.000 39.50044 ? 243 THR A CB  1 
ATOM   1869 O OG1 . THR A 1 243 ? -25.57463 12.37630  34.30850  1.000 47.78576 ? 243 THR A OG1 1 
ATOM   1870 C CG2 . THR A 1 243 ? -23.61764 11.98261  33.00307  1.000 29.65953 ? 243 THR A CG2 1 
ATOM   1871 N N   . GLN A 1 244 ? -23.90958 11.74156  36.51959  1.000 31.02305 ? 244 GLN A N   1 
ATOM   1872 C CA  . GLN A 1 244 ? -23.48802 10.56200  37.26808  1.000 36.24460 ? 244 GLN A CA  1 
ATOM   1873 C C   . GLN A 1 244 ? -23.09570 9.42012   36.33397  1.000 26.96606 ? 244 GLN A C   1 
ATOM   1874 O O   . GLN A 1 244 ? -22.23901 8.60021   36.68265  1.000 31.84990 ? 244 GLN A O   1 
ATOM   1875 C CB  . GLN A 1 244 ? -24.59055 10.11320  38.23075  1.000 38.74222 ? 244 GLN A CB  1 
ATOM   1876 C CG  . GLN A 1 244 ? -24.18904 8.92875   39.10022  1.000 38.50007 ? 244 GLN A CG  1 
ATOM   1877 C CD  . GLN A 1 244 ? -23.02472 9.24679   40.01432  1.000 44.13977 ? 244 GLN A CD  1 
ATOM   1878 O OE1 . GLN A 1 244 ? -23.00506 10.28352  40.68545  1.000 38.36508 ? 244 GLN A OE1 1 
ATOM   1879 N NE2 . GLN A 1 244 ? -22.03991 8.35565   40.04438  1.000 42.29025 ? 244 GLN A NE2 1 
ATOM   1880 N N   . ASP A 1 245 ? -23.69728 9.34499   35.14516  1.000 30.80995 ? 245 ASP A N   1 
ATOM   1881 C CA  . ASP A 1 245 ? -23.23347 8.35755   34.17763  1.000 30.76594 ? 245 ASP A CA  1 
ATOM   1882 C C   . ASP A 1 245 ? -21.81303 8.66141   33.70830  1.000 35.09479 ? 245 ASP A C   1 
ATOM   1883 O O   . ASP A 1 245 ? -21.03327 7.73999   33.44139  1.000 34.00905 ? 245 ASP A O   1 
ATOM   1884 C CB  . ASP A 1 245 ? -24.18226 8.28620   32.98313  1.000 35.89652 ? 245 ASP A CB  1 
ATOM   1885 C CG  . ASP A 1 245 ? -23.72892 7.26536   31.95339  1.000 50.80767 ? 245 ASP A CG  1 
ATOM   1886 O OD1 . ASP A 1 245 ? -23.54544 6.08186   32.32837  1.000 50.79608 ? 245 ASP A OD1 1 
ATOM   1887 O OD2 . ASP A 1 245 ? -23.53511 7.65060   30.78045  1.000 50.96492 ? 245 ASP A OD2 1 
ATOM   1888 N N   . HIS A 1 246 ? -21.46736 9.94554   33.56749  1.000 29.03496 ? 246 HIS A N   1 
ATOM   1889 C CA  . HIS A 1 246 ? -20.08459 10.30848  33.25743  1.000 28.12552 ? 246 HIS A CA  1 
ATOM   1890 C C   . HIS A 1 246 ? -19.14051 9.89679   34.38189  1.000 32.31538 ? 246 HIS A C   1 
ATOM   1891 O O   . HIS A 1 246 ? -18.03889 9.39011   34.13051  1.000 27.85064 ? 246 HIS A O   1 
ATOM   1892 C CB  . HIS A 1 246 ? -19.96606 11.81709  33.02660  1.000 30.77727 ? 246 HIS A CB  1 
ATOM   1893 C CG  . HIS A 1 246 ? -20.67556 12.32303  31.80753  1.000 26.64993 ? 246 HIS A CG  1 
ATOM   1894 N ND1 . HIS A 1 246 ? -21.14158 13.61804  31.70777  1.000 27.72274 ? 246 HIS A ND1 1 
ATOM   1895 C CD2 . HIS A 1 246 ? -20.99499 11.71963  30.63570  1.000 30.74869 ? 246 HIS A CD2 1 
ATOM   1896 C CE1 . HIS A 1 246 ? -21.71571 13.79041  30.52813  1.000 31.59841 ? 246 HIS A CE1 1 
ATOM   1897 N NE2 . HIS A 1 246 ? -21.64089 12.65496  29.85785  1.000 28.86059 ? 246 HIS A NE2 1 
ATOM   1898 N N   . VAL A 1 247 ? -19.53318 10.16196  35.63215  1.000 27.04237 ? 247 VAL A N   1 
ATOM   1899 C CA  . VAL A 1 247 ? -18.73755 9.72737   36.77923  1.000 30.34710 ? 247 VAL A CA  1 
ATOM   1900 C C   . VAL A 1 247 ? -18.47777 8.22575   36.70073  1.000 30.23696 ? 247 VAL A C   1 
ATOM   1901 O O   . VAL A 1 247 ? -17.33675 7.76850   36.80491  1.000 27.07545 ? 247 VAL A O   1 
ATOM   1902 C CB  . VAL A 1 247 ? -19.44313 10.12085  38.08886  1.000 28.28036 ? 247 VAL A CB  1 
ATOM   1903 C CG1 . VAL A 1 247 ? -18.69216 9.58837   39.29323  1.000 29.57850 ? 247 VAL A CG1 1 
ATOM   1904 C CG2 . VAL A 1 247 ? -19.58149 11.65534  38.16886  1.000 30.90866 ? 247 VAL A CG2 1 
ATOM   1905 N N   . ASP A 1 248 ? -19.53657 7.44207   36.47443  1.000 37.83728 ? 248 ASP A N   1 
ATOM   1906 C CA  . ASP A 1 248 ? -19.40583 5.98510   36.40311  1.000 31.03099 ? 248 ASP A CA  1 
ATOM   1907 C C   . ASP A 1 248 ? -18.47233 5.54657   35.28185  1.000 35.01152 ? 248 ASP A C   1 
ATOM   1908 O O   . ASP A 1 248 ? -17.66864 4.62428   35.46069  1.000 37.35701 ? 248 ASP A O   1 
ATOM   1909 C CB  . ASP A 1 248 ? -20.77819 5.34919   36.20682  1.000 30.36140 ? 248 ASP A CB  1 
ATOM   1910 C CG  . ASP A 1 248 ? -21.68391 5.54810   37.39087  1.000 30.91494 ? 248 ASP A CG  1 
ATOM   1911 O OD1 . ASP A 1 248 ? -21.19033 5.94768   38.45677  1.000 40.56906 ? 248 ASP A OD1 1 
ATOM   1912 O OD2 . ASP A 1 248 ? -22.90070 5.31787   37.25471  1.000 41.76024 ? 248 ASP A OD2 1 
ATOM   1913 N N   . ILE A 1 249 ? -18.58263 6.16718   34.10508  1.000 26.25542 ? 249 ILE A N   1 
ATOM   1914 C CA  . ILE A 1 249 ? -17.78421 5.71786   32.97334  1.000 28.37915 ? 249 ILE A CA  1 
ATOM   1915 C C   . ILE A 1 249 ? -16.32025 6.04979   33.18189  1.000 33.51407 ? 249 ILE A C   1 
ATOM   1916 O O   . ILE A 1 249 ? -15.44583 5.43097   32.56825  1.000 33.01746 ? 249 ILE A O   1 
ATOM   1917 C CB  . ILE A 1 249 ? -18.32169 6.32803   31.66690  1.000 34.86800 ? 249 ILE A CB  1 
ATOM   1918 C CG1 . ILE A 1 249 ? -19.68230 5.72211   31.33033  1.000 31.24159 ? 249 ILE A CG1 1 
ATOM   1919 C CG2 . ILE A 1 249 ? -17.35538 6.09517   30.53607  1.000 43.89822 ? 249 ILE A CG2 1 
ATOM   1920 C CD1 . ILE A 1 249 ? -20.62073 6.70387   30.62614  1.000 43.84768 ? 249 ILE A CD1 1 
ATOM   1921 N N   . LEU A 1 250 ? -16.02300 7.01339   34.04278  1.000 30.54083 ? 250 LEU A N   1 
ATOM   1922 C CA  . LEU A 1 250 ? -14.63801 7.28102   34.39243  1.000 29.71100 ? 250 LEU A CA  1 
ATOM   1923 C C   . LEU A 1 250 ? -14.09450 6.29485   35.42037  1.000 28.67275 ? 250 LEU A C   1 
ATOM   1924 O O   . LEU A 1 250 ? -12.88160 6.27542   35.65415  1.000 33.79507 ? 250 LEU A O   1 
ATOM   1925 C CB  . LEU A 1 250 ? -14.51177 8.71952   34.90929  1.000 27.33650 ? 250 LEU A CB  1 
ATOM   1926 C CG  . LEU A 1 250 ? -14.77094 9.81191   33.86810  1.000 28.00397 ? 250 LEU A CG  1 
ATOM   1927 C CD1 . LEU A 1 250 ? -14.93915 11.13743  34.58460  1.000 25.48157 ? 250 LEU A CD1 1 
ATOM   1928 C CD2 . LEU A 1 250 ? -13.59900 9.90017   32.87048  1.000 28.05816 ? 250 LEU A CD2 1 
ATOM   1929 N N   . GLY A 1 251 ? -14.95619 5.47783   36.02296  1.000 29.78136 ? 251 GLY A N   1 
ATOM   1930 C CA  . GLY A 1 251 ? -14.57744 4.56402   37.07841  1.000 34.28987 ? 251 GLY A CA  1 
ATOM   1931 C C   . GLY A 1 251 ? -13.28971 3.79705   36.83969  1.000 36.17888 ? 251 GLY A C   1 
ATOM   1932 O O   . GLY A 1 251 ? -12.37972 3.81145   37.67091  1.000 33.84281 ? 251 GLY A O   1 
ATOM   1933 N N   . PRO A 1 252 ? -13.18014 3.10280   35.70469  1.000 37.97999 ? 252 PRO A N   1 
ATOM   1934 C CA  . PRO A 1 252 ? -11.96288 2.30094   35.48198  1.000 38.10322 ? 252 PRO A CA  1 
ATOM   1935 C C   . PRO A 1 252 ? -10.68755 3.13266   35.49711  1.000 34.92692 ? 252 PRO A C   1 
ATOM   1936 O O   . PRO A 1 252 ? -9.65615  2.67312   36.01077  1.000 33.78833 ? 252 PRO A O   1 
ATOM   1937 C CB  . PRO A 1 252 ? -12.22057 1.64441   34.11785  1.000 39.87953 ? 252 PRO A CB  1 
ATOM   1938 C CG  . PRO A 1 252 ? -13.70103 1.64248   33.97153  1.000 41.16554 ? 252 PRO A CG  1 
ATOM   1939 C CD  . PRO A 1 252 ? -14.16790 2.91256   34.63281  1.000 40.30732 ? 252 PRO A CD  1 
ATOM   1940 N N   . LEU A 1 253 ? -10.72694 4.35682   34.96969  1.000 29.25923 ? 253 LEU A N   1 
ATOM   1941 C CA  . LEU A 1 253 ? -9.54713  5.21416   35.03663  1.000 29.98318 ? 253 LEU A CA  1 
ATOM   1942 C C   . LEU A 1 253 ? -9.26262  5.64583   36.46926  1.000 29.84937 ? 253 LEU A C   1 
ATOM   1943 O O   . LEU A 1 253 ? -8.10231  5.69974   36.88975  1.000 27.12496 ? 253 LEU A O   1 
ATOM   1944 C CB  . LEU A 1 253 ? -9.73167  6.43230   34.13036  1.000 24.65016 ? 253 LEU A CB  1 
ATOM   1945 C CG  . LEU A 1 253 ? -9.75223  6.08676   32.63716  1.000 30.01839 ? 253 LEU A CG  1 
ATOM   1946 C CD1 . LEU A 1 253 ? -10.17753 7.28617   31.80712  1.000 24.31632 ? 253 LEU A CD1 1 
ATOM   1947 C CD2 . LEU A 1 253 ? -8.39271  5.60528   32.19700  1.000 29.88621 ? 253 LEU A CD2 1 
ATOM   1948 N N   . SER A 1 254 ? -10.31080 5.97160   37.22443  1.000 32.17946 ? 254 SER A N   1 
ATOM   1949 C CA  . SER A 1 254 ? -10.15312 6.24089   38.64792  1.000 27.66865 ? 254 SER A CA  1 
ATOM   1950 C C   . SER A 1 254 ? -9.49274  5.06306   39.34923  1.000 30.58510 ? 254 SER A C   1 
ATOM   1951 O O   . SER A 1 254 ? -8.56836  5.23470   40.15543  1.000 33.66442 ? 254 SER A O   1 
ATOM   1952 C CB  . SER A 1 254 ? -11.52064 6.53468   39.26245  1.000 28.23513 ? 254 SER A CB  1 
ATOM   1953 O OG  . SER A 1 254 ? -11.38696 6.71270   40.66556  1.000 34.82294 ? 254 SER A OG  1 
ATOM   1954 N N   . ALA A 1 255 ? -9.95168  3.85027   39.04130  1.000 27.14339 ? 255 ALA A N   1 
ATOM   1955 C CA  . ALA A 1 255 ? -9.39564  2.65896   39.68033  1.000 32.21289 ? 255 ALA A CA  1 
ATOM   1956 C C   . ALA A 1 255 ? -7.92660  2.46213   39.32678  1.000 31.22772 ? 255 ALA A C   1 
ATOM   1957 O O   . ALA A 1 255 ? -7.11065  2.14004   40.19627  1.000 34.73841 ? 255 ALA A O   1 
ATOM   1958 C CB  . ALA A 1 255 ? -10.20718 1.43380   39.27524  1.000 38.26800 ? 255 ALA A CB  1 
ATOM   1959 N N   . GLN A 1 256 ? -7.56750  2.65426   38.05579  1.000 38.01937 ? 256 GLN A N   1 
ATOM   1960 C CA  . GLN A 1 256 ? -6.18345  2.43175   37.63567  1.000 33.81037 ? 256 GLN A CA  1 
ATOM   1961 C C   . GLN A 1 256 ? -5.22915  3.39764   38.32505  1.000 38.59883 ? 256 GLN A C   1 
ATOM   1962 O O   . GLN A 1 256 ? -4.12057  3.01521   38.71890  1.000 36.12496 ? 256 GLN A O   1 
ATOM   1963 C CB  . GLN A 1 256 ? -6.06525  2.55887   36.11614  1.000 28.44721 ? 256 GLN A CB  1 
ATOM   1964 C CG  . GLN A 1 256 ? -4.64334  2.42452   35.56827  1.000 31.57963 ? 256 GLN A CG  1 
ATOM   1965 C CD  . GLN A 1 256 ? -4.61045  2.34225   34.04781  1.000 40.43471 ? 256 GLN A CD  1 
ATOM   1966 O OE1 . GLN A 1 256 ? -5.65460  2.29924   33.39518  1.000 45.38575 ? 256 GLN A OE1 1 
ATOM   1967 N NE2 . GLN A 1 256 ? -3.41051  2.32135   33.47721  1.000 41.25183 ? 256 GLN A NE2 1 
ATOM   1968 N N   . THR A 1 257 ? -5.63652  4.65473   38.48034  1.000 35.31319 ? 257 THR A N   1 
ATOM   1969 C CA  . THR A 1 257 ? -4.75184  5.67253   39.02533  1.000 26.70078 ? 257 THR A CA  1 
ATOM   1970 C C   . THR A 1 257 ? -4.88678  5.84132   40.52887  1.000 33.57661 ? 257 THR A C   1 
ATOM   1971 O O   . THR A 1 257 ? -4.01116  6.46144   41.14231  1.000 34.13911 ? 257 THR A O   1 
ATOM   1972 C CB  . THR A 1 257 ? -5.02863  7.02148   38.36016  1.000 27.33989 ? 257 THR A CB  1 
ATOM   1973 O OG1 . THR A 1 257 ? -6.41521  7.34318   38.53064  1.000 29.21597 ? 257 THR A OG1 1 
ATOM   1974 C CG2 . THR A 1 257 ? -4.68730  6.98517   36.84920  1.000 24.30597 ? 257 THR A CG2 1 
ATOM   1975 N N   . GLY A 1 258 ? -5.95663  5.31760   41.13105  1.000 32.07694 ? 258 GLY A N   1 
ATOM   1976 C CA  . GLY A 1 258 ? -6.22026  5.57986   42.52923  1.000 34.02914 ? 258 GLY A CA  1 
ATOM   1977 C C   . GLY A 1 258 ? -6.65904  6.99455   42.83108  1.000 35.84641 ? 258 GLY A C   1 
ATOM   1978 O O   . GLY A 1 258 ? -6.47816  7.46537   43.95690  1.000 35.12629 ? 258 GLY A O   1 
ATOM   1979 N N   . ILE A 1 259 ? -7.22997  7.69564   41.85618  1.000 29.16850 ? 259 ILE A N   1 
ATOM   1980 C CA  . ILE A 1 259 ? -7.65124  9.07807   42.03623  1.000 31.40195 ? 259 ILE A CA  1 
ATOM   1981 C C   . ILE A 1 259 ? -9.15541  9.12181   41.81809  1.000 29.22658 ? 259 ILE A C   1 
ATOM   1982 O O   . ILE A 1 259 ? -9.63850  8.90580   40.69425  1.000 28.86118 ? 259 ILE A O   1 
ATOM   1983 C CB  . ILE A 1 259 ? -6.90942  10.02847  41.08745  1.000 30.36481 ? 259 ILE A CB  1 
ATOM   1984 C CG1 . ILE A 1 259 ? -5.40863  9.95804   41.36776  1.000 30.28432 ? 259 ILE A CG1 1 
ATOM   1985 C CG2 . ILE A 1 259 ? -7.43673  11.46225  41.20611  1.000 32.34193 ? 259 ILE A CG2 1 
ATOM   1986 C CD1 . ILE A 1 259 ? -4.56633  10.74067  40.41053  1.000 26.22970 ? 259 ILE A CD1 1 
ATOM   1987 N N   . ALA A 1 260 ? -9.89753  9.38470   42.89024  1.000 24.48616 ? 260 ALA A N   1 
ATOM   1988 C CA  . ALA A 1 260 ? -11.34669 9.47710   42.79288  1.000 28.71045 ? 260 ALA A CA  1 
ATOM   1989 C C   . ALA A 1 260 ? -11.75084 10.53042  41.76440  1.000 25.35187 ? 260 ALA A C   1 
ATOM   1990 O O   . ALA A 1 260 ? -11.05863 11.53101  41.56322  1.000 26.25007 ? 260 ALA A O   1 
ATOM   1991 C CB  . ALA A 1 260 ? -11.95376 9.82342   44.15596  1.000 30.40972 ? 260 ALA A CB  1 
ATOM   1992 N N   . VAL A 1 261 ? -12.89632 10.30074  41.12242  1.000 26.04529 ? 261 VAL A N   1 
ATOM   1993 C CA  . VAL A 1 261 ? -13.35839 11.21551  40.08306  1.000 27.71077 ? 261 VAL A CA  1 
ATOM   1994 C C   . VAL A 1 261 ? -13.53859 12.61275  40.65581  1.000 28.87078 ? 261 VAL A C   1 
ATOM   1995 O O   . VAL A 1 261 ? -13.15094 13.61046  40.03616  1.000 23.58388 ? 261 VAL A O   1 
ATOM   1996 C CB  . VAL A 1 261 ? -14.65901 10.69220  39.44250  1.000 29.77549 ? 261 VAL A CB  1 
ATOM   1997 C CG1 . VAL A 1 261 ? -15.18908 11.69744  38.42435  1.000 25.56734 ? 261 VAL A CG1 1 
ATOM   1998 C CG2 . VAL A 1 261 ? -14.42485 9.33924   38.77911  1.000 30.53549 ? 261 VAL A CG2 1 
ATOM   1999 N N   . LEU A 1 262 ? -14.09557 12.70931  41.86635  1.000 23.47181 ? 262 LEU A N   1 
ATOM   2000 C CA  . LEU A 1 262 ? -14.33588 14.03158  42.43305  1.000 25.20714 ? 262 LEU A CA  1 
ATOM   2001 C C   . LEU A 1 262 ? -13.06005 14.66992  42.96499  1.000 27.83437 ? 262 LEU A C   1 
ATOM   2002 O O   . LEU A 1 262 ? -13.01901 15.89126  43.15500  1.000 31.67805 ? 262 LEU A O   1 
ATOM   2003 C CB  . LEU A 1 262 ? -15.42695 13.94559  43.50784  1.000 22.58560 ? 262 LEU A CB  1 
ATOM   2004 C CG  . LEU A 1 262 ? -16.82223 13.69604  42.91591  1.000 28.75694 ? 262 LEU A CG  1 
ATOM   2005 C CD1 . LEU A 1 262 ? -17.85251 13.48265  44.01785  1.000 31.85681 ? 262 LEU A CD1 1 
ATOM   2006 C CD2 . LEU A 1 262 ? -17.23853 14.87667  42.00708  1.000 25.60389 ? 262 LEU A CD2 1 
ATOM   2007 N N   . ASP A 1 263 ? -12.00997 13.88127  43.16141  1.000 23.82353 ? 263 ASP A N   1 
ATOM   2008 C CA  . ASP A 1 263 ? -10.69501 14.44257  43.42984  1.000 30.46733 ? 263 ASP A CA  1 
ATOM   2009 C C   . ASP A 1 263 ? -10.12196 15.07407  42.16355  1.000 23.91891 ? 263 ASP A C   1 
ATOM   2010 O O   . ASP A 1 263 ? -9.62675  16.20722  42.18527  1.000 26.12154 ? 263 ASP A O   1 
ATOM   2011 C CB  . ASP A 1 263 ? -9.80851  13.32480  43.99598  1.000 27.10566 ? 263 ASP A CB  1 
ATOM   2012 C CG  . ASP A 1 263 ? -8.39560  13.76819  44.33064  1.000 33.90749 ? 263 ASP A CG  1 
ATOM   2013 O OD1 . ASP A 1 263 ? -8.01412  14.93737  44.06730  1.000 38.04048 ? 263 ASP A OD1 1 
ATOM   2014 O OD2 . ASP A 1 263 ? -7.66627  12.90745  44.88494  1.000 41.07419 ? 263 ASP A OD2 1 
ATOM   2015 N N   . MET A 1 264 ? -10.22814 14.37451  41.03286  1.000 25.99678 ? 264 MET A N   1 
ATOM   2016 C CA  . MET A 1 264 ? -9.80142  14.95301  39.75934  1.000 26.21977 ? 264 MET A CA  1 
ATOM   2017 C C   . MET A 1 264 ? -10.62198 16.19238  39.40604  1.000 27.90230 ? 264 MET A C   1 
ATOM   2018 O O   . MET A 1 264 ? -10.09825 17.15750  38.83457  1.000 23.33117 ? 264 MET A O   1 
ATOM   2019 C CB  . MET A 1 264 ? -9.90937  13.89775  38.65579  1.000 20.19174 ? 264 MET A CB  1 
ATOM   2020 C CG  . MET A 1 264 ? -9.25073  14.31178  37.38395  1.000 24.97624 ? 264 MET A CG  1 
ATOM   2021 S SD  . MET A 1 264 ? -7.45672  14.44455  37.51053  1.000 26.64999 ? 264 MET A SD  1 
ATOM   2022 C CE  . MET A 1 264 ? -7.02485  12.72196  37.25663  1.000 27.59948 ? 264 MET A CE  1 
ATOM   2023 N N   . CYS A 1 265 ? -11.91569 16.18578  39.72670  1.000 22.02083 ? 265 CYS A N   1 
ATOM   2024 C CA  . CYS A 1 265 ? -12.74149 17.36357  39.47318  1.000 20.24308 ? 265 CYS A CA  1 
ATOM   2025 C C   . CYS A 1 265 ? -12.20920 18.59834  40.19811  1.000 27.43948 ? 265 CYS A C   1 
ATOM   2026 O O   . CYS A 1 265 ? -12.24911 19.71590  39.65586  1.000 25.39100 ? 265 CYS A O   1 
ATOM   2027 C CB  . CYS A 1 265 ? -14.18750 17.07381  39.87876  1.000 23.46338 ? 265 CYS A CB  1 
ATOM   2028 S SG  . CYS A 1 265 ? -15.07065 16.07761  38.66642  1.000 25.87154 ? 265 CYS A SG  1 
ATOM   2029 N N   . ALA A 1 266 ? -11.70640 18.42252  41.43108  1.000 28.19155 ? 266 ALA A N   1 
ATOM   2030 C CA  . ALA A 1 266 ? -11.13587 19.54818  42.15775  1.000 28.34144 ? 266 ALA A CA  1 
ATOM   2031 C C   . ALA A 1 266 ? -9.90070  20.08597  41.44971  1.000 28.19413 ? 266 ALA A C   1 
ATOM   2032 O O   . ALA A 1 266 ? -9.65396  21.29483  41.46735  1.000 24.84275 ? 266 ALA A O   1 
ATOM   2033 C CB  . ALA A 1 266 ? -10.79087 19.14963  43.60134  1.000 24.59940 ? 266 ALA A CB  1 
ATOM   2034 N N   . SER A 1 267 ? -9.12538  19.21311  40.80614  1.000 26.14062 ? 267 SER A N   1 
ATOM   2035 C CA  . SER A 1 267 ? -7.97492  19.68725  40.04521  1.000 26.22984 ? 267 SER A CA  1 
ATOM   2036 C C   . SER A 1 267 ? -8.42001  20.46217  38.81280  1.000 23.61119 ? 267 SER A C   1 
ATOM   2037 O O   . SER A 1 267 ? -7.90384  21.54941  38.53158  1.000 29.58979 ? 267 SER A O   1 
ATOM   2038 C CB  . SER A 1 267 ? -7.08115  18.50814  39.65334  1.000 30.24263 ? 267 SER A CB  1 
ATOM   2039 O OG  . SER A 1 267 ? -6.73048  17.74996  40.78857  1.000 35.96215 ? 267 SER A OG  1 
ATOM   2040 N N   . LEU A 1 268 ? -9.39965  19.93158  38.07802  1.000 26.51947 ? 268 LEU A N   1 
ATOM   2041 C CA  . LEU A 1 268 ? -9.91922  20.64704  36.90892  1.000 25.59148 ? 268 LEU A CA  1 
ATOM   2042 C C   . LEU A 1 268 ? -10.52188 21.99487  37.30174  1.000 30.76259 ? 268 LEU A C   1 
ATOM   2043 O O   . LEU A 1 268 ? -10.36443 22.99129  36.58308  1.000 27.53843 ? 268 LEU A O   1 
ATOM   2044 C CB  . LEU A 1 268 ? -10.95507 19.78283  36.18868  1.000 29.95423 ? 268 LEU A CB  1 
ATOM   2045 C CG  . LEU A 1 268 ? -11.63140 20.40970  34.95876  1.000 27.55633 ? 268 LEU A CG  1 
ATOM   2046 C CD1 . LEU A 1 268 ? -10.58576 20.99006  34.02887  1.000 27.12539 ? 268 LEU A CD1 1 
ATOM   2047 C CD2 . LEU A 1 268 ? -12.48256 19.38425  34.24208  1.000 24.45980 ? 268 LEU A CD2 1 
ATOM   2048 N N   . LYS A 1 269 ? -11.24922 22.03441  38.42118  1.000 29.26499 ? 269 LYS A N   1 
ATOM   2049 C CA  . LYS A 1 269 ? -11.75980 23.29886  38.93753  1.000 30.76483 ? 269 LYS A CA  1 
ATOM   2050 C C   . LYS A 1 269 ? -10.63206 24.30780  39.14559  1.000 31.62011 ? 269 LYS A C   1 
ATOM   2051 O O   . LYS A 1 269 ? -10.77218 25.48990  38.80472  1.000 37.02430 ? 269 LYS A O   1 
ATOM   2052 C CB  . LYS A 1 269 ? -12.50924 23.06052  40.25320  1.000 28.18788 ? 269 LYS A CB  1 
ATOM   2053 C CG  . LYS A 1 269 ? -13.09543 24.32692  40.85571  1.000 38.27537 ? 269 LYS A CG  1 
ATOM   2054 C CD  . LYS A 1 269 ? -13.72605 24.06871  42.21517  1.000 38.60799 ? 269 LYS A CD  1 
ATOM   2055 C CE  . LYS A 1 269 ? -14.91719 23.12937  42.10832  1.000 32.68606 ? 269 LYS A CE  1 
ATOM   2056 N NZ  . LYS A 1 269 ? -15.63733 23.01205  43.41070  1.000 33.72718 ? 269 LYS A NZ  1 
ATOM   2057 N N   . GLU A 1 270 ? -9.50801  23.86349  39.71028  1.000 27.99493 ? 270 GLU A N   1 
ATOM   2058 C CA  . GLU A 1 270 ? -8.39528  24.78093  39.94374  1.000 33.93193 ? 270 GLU A CA  1 
ATOM   2059 C C   . GLU A 1 270 ? -7.76919  25.22603  38.62729  1.000 36.53389 ? 270 GLU A C   1 
ATOM   2060 O O   . GLU A 1 270 ? -7.41195  26.39862  38.47238  1.000 38.51585 ? 270 GLU A O   1 
ATOM   2061 C CB  . GLU A 1 270 ? -7.35661  24.13561  40.86826  1.000 34.99152 ? 270 GLU A CB  1 
ATOM   2062 C CG  . GLU A 1 270 ? -6.12143  25.00729  41.12449  1.000 37.82261 ? 270 GLU A CG  1 
ATOM   2063 C CD  . GLU A 1 270 ? -5.34610  24.63835  42.39209  1.000 55.60037 ? 270 GLU A CD  1 
ATOM   2064 O OE1 . GLU A 1 270 ? -5.06523  23.43855  42.63307  1.000 47.51436 ? 270 GLU A OE1 1 
ATOM   2065 O OE2 . GLU A 1 270 ? -5.00500  25.56834  43.15385  1.000 57.17075 ? 270 GLU A OE2 1 
ATOM   2066 N N   . LEU A 1 271 ? -7.65935  24.31252  37.65552  1.000 34.02823 ? 271 LEU A N   1 
ATOM   2067 C CA  . LEU A 1 271 ? -7.20558  24.69359  36.31852  1.000 31.69514 ? 271 LEU A CA  1 
ATOM   2068 C C   . LEU A 1 271 ? -8.11796  25.74424  35.68957  1.000 37.74229 ? 271 LEU A C   1 
ATOM   2069 O O   . LEU A 1 271 ? -7.64077  26.66467  35.01585  1.000 39.42489 ? 271 LEU A O   1 
ATOM   2070 C CB  . LEU A 1 271 ? -7.11979  23.45800  35.41964  1.000 26.66129 ? 271 LEU A CB  1 
ATOM   2071 C CG  . LEU A 1 271 ? -5.94945  22.52185  35.70298  1.000 28.88427 ? 271 LEU A CG  1 
ATOM   2072 C CD1 . LEU A 1 271 ? -6.06262  21.23845  34.89029  1.000 25.74470 ? 271 LEU A CD1 1 
ATOM   2073 C CD2 . LEU A 1 271 ? -4.63049  23.24155  35.43539  1.000 30.79133 ? 271 LEU A CD2 1 
ATOM   2074 N N   . LEU A 1 272 ? -9.43453  25.61820  35.87792  1.000 31.44366 ? 272 LEU A N   1 
ATOM   2075 C CA  . LEU A 1 272 ? -10.34961 26.56859  35.24931  1.000 30.10826 ? 272 LEU A CA  1 
ATOM   2076 C C   . LEU A 1 272 ? -10.25089 27.94636  35.89708  1.000 39.03525 ? 272 LEU A C   1 
ATOM   2077 O O   . LEU A 1 272 ? -10.35655 28.97338  35.21879  1.000 37.49830 ? 272 LEU A O   1 
ATOM   2078 C CB  . LEU A 1 272 ? -11.78402 26.04460  35.32235  1.000 31.42523 ? 272 LEU A CB  1 
ATOM   2079 C CG  . LEU A 1 272 ? -12.12864 24.79990  34.49353  1.000 32.84856 ? 272 LEU A CG  1 
ATOM   2080 C CD1 . LEU A 1 272 ? -13.55551 24.34702  34.79041  1.000 26.71739 ? 272 LEU A CD1 1 
ATOM   2081 C CD2 . LEU A 1 272 ? -11.96301 25.08801  33.02349  1.000 31.77252 ? 272 LEU A CD2 1 
ATOM   2082 N N   . GLN A 1 273 ? -10.04473 27.99232  37.20566  1.000 35.18370 ? 273 GLN A N   1 
ATOM   2083 C CA  . GLN A 1 273 ? -10.02360 29.26842  37.90588  1.000 43.84555 ? 273 GLN A CA  1 
ATOM   2084 C C   . GLN A 1 273 ? -8.65706  29.95075  37.87410  1.000 44.19301 ? 273 GLN A C   1 
ATOM   2085 O O   . GLN A 1 273 ? -8.59111  31.18208  37.93824  1.000 48.57960 ? 273 GLN A O   1 
ATOM   2086 C CB  . GLN A 1 273 ? -10.49074 29.06045  39.35245  1.000 42.96895 ? 273 GLN A CB  1 
ATOM   2087 C CG  . GLN A 1 273 ? -11.93092 28.54650  39.44579  1.000 40.23606 ? 273 GLN A CG  1 
ATOM   2088 C CD  . GLN A 1 273 ? -12.35084 28.16651  40.85947  1.000 44.04427 ? 273 GLN A CD  1 
ATOM   2089 O OE1 . GLN A 1 273 ? -11.58422 27.56130  41.61152  1.000 47.16240 ? 273 GLN A OE1 1 
ATOM   2090 N NE2 . GLN A 1 273 ? -13.57918 28.51856  41.22384  1.000 48.80897 ? 273 GLN A NE2 1 
ATOM   2091 N N   . ASN A 1 274 ? -7.56519  29.19698  37.74575  1.000 40.06674 ? 274 ASN A N   1 
ATOM   2092 C CA  . ASN A 1 274 ? -6.22983  29.77355  37.80354  1.000 43.97501 ? 274 ASN A CA  1 
ATOM   2093 C C   . ASN A 1 274 ? -5.43125  29.65878  36.51105  1.000 46.43393 ? 274 ASN A C   1 
ATOM   2094 O O   . ASN A 1 274 ? -4.33433  30.22599  36.43422  1.000 44.48913 ? 274 ASN A O   1 
ATOM   2095 C CB  . ASN A 1 274 ? -5.42310  29.12761  38.94307  1.000 39.94678 ? 274 ASN A CB  1 
ATOM   2096 C CG  . ASN A 1 274 ? -6.17599  29.12932  40.25676  1.000 49.85360 ? 274 ASN A CG  1 
ATOM   2097 O OD1 . ASN A 1 274 ? -6.90227  30.07557  40.56581  1.000 56.69959 ? 274 ASN A OD1 1 
ATOM   2098 N ND2 . ASN A 1 274 ? -6.01865  28.06267  41.03442  1.000 52.75166 ? 274 ASN A ND2 1 
ATOM   2099 N N   . GLY A 1 275 ? -5.93442  28.96240  35.49949  1.000 45.16366 ? 275 GLY A N   1 
ATOM   2100 C CA  . GLY A 1 275 ? -5.12781  28.73585  34.32003  1.000 42.37738 ? 275 GLY A CA  1 
ATOM   2101 C C   . GLY A 1 275 ? -4.01758  27.72140  34.57017  1.000 43.92413 ? 275 GLY A C   1 
ATOM   2102 O O   . GLY A 1 275 ? -3.90081  27.11111  35.63482  1.000 42.62488 ? 275 GLY A O   1 
ATOM   2103 N N   . MET A 1 276 ? -3.17978  27.56292  33.54836  1.000 41.09786 ? 276 MET A N   1 
ATOM   2104 C CA  . MET A 1 276 ? -2.11884  26.56657  33.54804  1.000 41.57999 ? 276 MET A CA  1 
ATOM   2105 C C   . MET A 1 276 ? -0.73840  27.16277  33.78593  1.000 45.26240 ? 276 MET A C   1 
ATOM   2106 O O   . MET A 1 276 ? 0.25002   26.42845  33.73209  1.000 46.72662 ? 276 MET A O   1 
ATOM   2107 C CB  . MET A 1 276 ? -2.13653  25.78155  32.22699  1.000 43.01085 ? 276 MET A CB  1 
ATOM   2108 C CG  . MET A 1 276 ? -3.20807  24.69690  32.18260  1.000 40.05268 ? 276 MET A CG  1 
ATOM   2109 S SD  . MET A 1 276 ? -3.52113  24.03954  30.53796  1.000 49.21765 ? 276 MET A SD  1 
ATOM   2110 C CE  . MET A 1 276 ? -1.95847  23.24765  30.21812  1.000 30.50657 ? 276 MET A CE  1 
ATOM   2111 N N   . ASN A 1 277 ? -0.64584  28.46509  34.06657  1.000 52.03003 ? 277 ASN A N   1 
ATOM   2112 C CA  . ASN A 1 277 ? 0.62329   29.10923  34.41798  1.000 58.09988 ? 277 ASN A CA  1 
ATOM   2113 C C   . ASN A 1 277 ? 1.66655   28.95563  33.31724  1.000 54.90765 ? 277 ASN A C   1 
ATOM   2114 O O   . ASN A 1 277 ? 2.86949   28.94134  33.58916  1.000 54.84552 ? 277 ASN A O   1 
ATOM   2115 C CB  . ASN A 1 277 ? 1.18338   28.56318  35.73575  1.000 55.08306 ? 277 ASN A CB  1 
ATOM   2116 C CG  . ASN A 1 277 ? 0.41967   29.05274  36.94105  1.000 63.42555 ? 277 ASN A CG  1 
ATOM   2117 O OD1 . ASN A 1 277 ? -0.80421  29.18798  36.90183  1.000 68.57751 ? 277 ASN A OD1 1 
ATOM   2118 N ND2 . ASN A 1 277 ? 1.14012   29.33014  38.02583  1.000 65.49720 ? 277 ASN A ND2 1 
ATOM   2119 N N   . GLY A 1 278 ? 1.22369   28.83625  32.06909  1.000 56.14977 ? 278 GLY A N   1 
ATOM   2120 C CA  . GLY A 1 278 ? 2.15665   28.54807  31.00018  1.000 56.38949 ? 278 GLY A CA  1 
ATOM   2121 C C   . GLY A 1 278 ? 2.77905   27.16769  31.03584  1.000 56.14302 ? 278 GLY A C   1 
ATOM   2122 O O   . GLY A 1 278 ? 3.69692   26.90289  30.25498  1.000 61.11359 ? 278 GLY A O   1 
ATOM   2123 N N   . ARG A 1 279 ? 2.32678   26.28138  31.92063  1.000 44.68874 ? 279 ARG A N   1 
ATOM   2124 C CA  . ARG A 1 279 ? 2.77118   24.89870  31.88567  1.000 43.74783 ? 279 ARG A CA  1 
ATOM   2125 C C   . ARG A 1 279 ? 1.98990   24.12760  30.82461  1.000 33.54174 ? 279 ARG A C   1 
ATOM   2126 O O   . ARG A 1 279 ? 1.04270   24.63708  30.22087  1.000 41.44441 ? 279 ARG A O   1 
ATOM   2127 C CB  . ARG A 1 279 ? 2.60439   24.24733  33.25787  1.000 42.23029 ? 279 ARG A CB  1 
ATOM   2128 C CG  . ARG A 1 279 ? 3.31674   24.98535  34.38656  1.000 49.49957 ? 279 ARG A CG  1 
ATOM   2129 C CD  . ARG A 1 279 ? 2.92698   24.41059  35.73025  1.000 45.40604 ? 279 ARG A CD  1 
ATOM   2130 N NE  . ARG A 1 279 ? 4.02063   23.71049  36.39437  1.000 55.35938 ? 279 ARG A NE  1 
ATOM   2131 C CZ  . ARG A 1 279 ? 4.53420   22.55357  35.99519  1.000 49.76634 ? 279 ARG A CZ  1 
ATOM   2132 N NH1 . ARG A 1 279 ? 4.14605   21.97363  34.86943  1.000 50.90385 ? 279 ARG A NH1 1 
ATOM   2133 N NH2 . ARG A 1 279 ? 5.46655   21.96706  36.74060  1.000 47.41350 ? 279 ARG A NH2 1 
ATOM   2134 N N   . THR A 1 280 ? 2.39116   22.88260  30.58972  1.000 38.79397 ? 280 THR A N   1 
ATOM   2135 C CA  . THR A 1 280 ? 1.69128   22.03250  29.63892  1.000 30.51971 ? 280 THR A CA  1 
ATOM   2136 C C   . THR A 1 280 ? 1.25286   20.73260  30.29569  1.000 30.55850 ? 280 THR A C   1 
ATOM   2137 O O   . THR A 1 280 ? 1.78798   20.30953  31.32146  1.000 35.00672 ? 280 THR A O   1 
ATOM   2138 C CB  . THR A 1 280 ? 2.55250   21.69316  28.41568  1.000 38.44224 ? 280 THR A CB  1 
ATOM   2139 O OG1 . THR A 1 280 ? 3.82070   21.19354  28.85322  1.000 32.63508 ? 280 THR A OG1 1 
ATOM   2140 C CG2 . THR A 1 280 ? 2.75010   22.90931  27.51829  1.000 38.65424 ? 280 THR A CG2 1 
ATOM   2141 N N   . ILE A 1 281 ? 0.26545   20.09765  29.67184  1.000 27.76484 ? 281 ILE A N   1 
ATOM   2142 C CA  . ILE A 1 281 ? -0.19483  18.76601  30.04196  1.000 26.17191 ? 281 ILE A CA  1 
ATOM   2143 C C   . ILE A 1 281 ? -0.10875  17.89888  28.79800  1.000 34.58174 ? 281 ILE A C   1 
ATOM   2144 O O   . ILE A 1 281 ? -0.70352  18.23233  27.76312  1.000 28.11736 ? 281 ILE A O   1 
ATOM   2145 C CB  . ILE A 1 281 ? -1.62829  18.78388  30.58880  1.000 25.43415 ? 281 ILE A CB  1 
ATOM   2146 C CG1 . ILE A 1 281 ? -1.72924  19.65578  31.84972  1.000 29.24442 ? 281 ILE A CG1 1 
ATOM   2147 C CG2 . ILE A 1 281 ? -2.09358  17.37282  30.85621  1.000 23.36292 ? 281 ILE A CG2 1 
ATOM   2148 C CD1 . ILE A 1 281 ? -3.13460  19.75764  32.39967  1.000 26.81548 ? 281 ILE A CD1 1 
ATOM   2149 N N   . LEU A 1 282 ? 0.63162   16.79406  28.89526  1.000 31.51735 ? 282 LEU A N   1 
ATOM   2150 C CA  . LEU A 1 282 ? 0.85301   15.91015  27.75445  1.000 32.60227 ? 282 LEU A CA  1 
ATOM   2151 C C   . LEU A 1 282 ? 1.28884   16.71015  26.52524  1.000 32.44114 ? 282 LEU A C   1 
ATOM   2152 O O   . LEU A 1 282 ? 0.88188   16.43169  25.39588  1.000 40.47438 ? 282 LEU A O   1 
ATOM   2153 C CB  . LEU A 1 282 ? -0.40040  15.08397  27.46071  1.000 26.97200 ? 282 LEU A CB  1 
ATOM   2154 C CG  . LEU A 1 282 ? -0.62429  13.85572  28.35278  1.000 28.97009 ? 282 LEU A CG  1 
ATOM   2155 C CD1 . LEU A 1 282 ? -1.98752  13.20171  28.10506  1.000 25.71475 ? 282 LEU A CD1 1 
ATOM   2156 C CD2 . LEU A 1 282 ? 0.49157   12.83468  28.13139  1.000 30.98207 ? 282 LEU A CD2 1 
ATOM   2157 N N   . GLY A 1 283 ? 2.11907   17.72747  26.75168  1.000 34.61082 ? 283 GLY A N   1 
ATOM   2158 C CA  . GLY A 1 283 ? 2.59806   18.55658  25.66072  1.000 36.71568 ? 283 GLY A CA  1 
ATOM   2159 C C   . GLY A 1 283 ? 1.59075   19.52631  25.08704  1.000 39.57204 ? 283 GLY A C   1 
ATOM   2160 O O   . GLY A 1 283 ? 1.86019   20.13700  24.04800  1.000 39.80570 ? 283 GLY A O   1 
ATOM   2161 N N   . SER A 1 284 ? 0.43180   19.68301  25.71345  1.000 31.98813 ? 284 SER A N   1 
ATOM   2162 C CA  . SER A 1 284 ? -0.57548  20.63089  25.26697  1.000 29.74351 ? 284 SER A CA  1 
ATOM   2163 C C   . SER A 1 284 ? -0.63997  21.83793  26.19732  1.000 32.84999 ? 284 SER A C   1 
ATOM   2164 O O   . SER A 1 284 ? -0.56906  21.69593  27.42363  1.000 27.76288 ? 284 SER A O   1 
ATOM   2165 C CB  . SER A 1 284 ? -1.94363  19.95284  25.19382  1.000 34.02940 ? 284 SER A CB  1 
ATOM   2166 O OG  . SER A 1 284 ? -2.96124  20.89924  24.95465  1.000 37.12592 ? 284 SER A OG  1 
ATOM   2167 N N   . ALA A 1 285 ? -0.80455  23.02972  25.60867  1.000 30.53313 ? 285 ALA A N   1 
ATOM   2168 C CA  . ALA A 1 285 ? -1.01336  24.25374  26.37119  1.000 32.65384 ? 285 ALA A CA  1 
ATOM   2169 C C   . ALA A 1 285 ? -2.48362  24.53924  26.63452  1.000 33.66875 ? 285 ALA A C   1 
ATOM   2170 O O   . ALA A 1 285 ? -2.79961  25.49693  27.34907  1.000 39.96264 ? 285 ALA A O   1 
ATOM   2171 C CB  . ALA A 1 285 ? -0.38725  25.44816  25.64769  1.000 38.24837 ? 285 ALA A CB  1 
ATOM   2172 N N   . LEU A 1 286 ? -3.37735  23.73425  26.07901  1.000 32.40064 ? 286 LEU A N   1 
ATOM   2173 C CA  . LEU A 1 286 ? -4.81180  23.86091  26.26857  1.000 34.68753 ? 286 LEU A CA  1 
ATOM   2174 C C   . LEU A 1 286 ? -5.36590  22.53625  26.77556  1.000 32.76317 ? 286 LEU A C   1 
ATOM   2175 O O   . LEU A 1 286 ? -4.79426  21.46784  26.53823  1.000 31.06356 ? 286 LEU A O   1 
ATOM   2176 C CB  . LEU A 1 286 ? -5.52123  24.24574  24.95988  1.000 37.69969 ? 286 LEU A CB  1 
ATOM   2177 C CG  . LEU A 1 286 ? -5.20844  25.58678  24.29366  1.000 37.71594 ? 286 LEU A CG  1 
ATOM   2178 C CD1 . LEU A 1 286 ? -5.95837  25.72924  22.98053  1.000 44.14860 ? 286 LEU A CD1 1 
ATOM   2179 C CD2 . LEU A 1 286 ? -5.55372  26.75084  25.23684  1.000 47.70881 ? 286 LEU A CD2 1 
ATOM   2180 N N   . LEU A 1 287 ? -6.49901  22.60926  27.46546  1.000 32.68389 ? 287 LEU A N   1 
ATOM   2181 C CA  . LEU A 1 287 ? -7.16374  21.40115  27.93345  1.000 32.74775 ? 287 LEU A CA  1 
ATOM   2182 C C   . LEU A 1 287 ? -7.82062  20.67889  26.75705  1.000 34.80908 ? 287 LEU A C   1 
ATOM   2183 O O   . LEU A 1 287 ? -8.67358  21.25121  26.07617  1.000 34.67193 ? 287 LEU A O   1 
ATOM   2184 C CB  . LEU A 1 287 ? -8.19312  21.75872  29.00278  1.000 27.47914 ? 287 LEU A CB  1 
ATOM   2185 C CG  . LEU A 1 287 ? -7.65853  22.51649  30.22145  1.000 28.28337 ? 287 LEU A CG  1 
ATOM   2186 C CD1 . LEU A 1 287 ? -8.72993  22.64302  31.29916  1.000 27.30225 ? 287 LEU A CD1 1 
ATOM   2187 C CD2 . LEU A 1 287 ? -6.40654  21.84829  30.79444  1.000 33.32059 ? 287 LEU A CD2 1 
ATOM   2188 N N   . GLU A 1 288 ? -7.42811  19.42600  26.51559  1.000 27.47235 ? 288 GLU A N   1 
ATOM   2189 C CA  . GLU A 1 288 ? -7.91656  18.67274  25.35942  1.000 26.17299 ? 288 GLU A CA  1 
ATOM   2190 C C   . GLU A 1 288 ? -9.25125  18.01295  25.67978  1.000 27.92475 ? 288 GLU A C   1 
ATOM   2191 O O   . GLU A 1 288 ? -9.37581  17.37536  26.72383  1.000 24.12532 ? 288 GLU A O   1 
ATOM   2192 C CB  . GLU A 1 288 ? -6.91168  17.59016  24.97195  1.000 28.07595 ? 288 GLU A CB  1 
ATOM   2193 C CG  . GLU A 1 288 ? -5.78528  18.07347  24.09667  1.000 42.29509 ? 288 GLU A CG  1 
ATOM   2194 C CD  . GLU A 1 288 ? -6.23389  18.24021  22.65580  1.000 54.63582 ? 288 GLU A CD  1 
ATOM   2195 O OE1 . GLU A 1 288 ? -7.14784  17.49449  22.21668  1.000 51.45999 ? 288 GLU A OE1 1 
ATOM   2196 O OE2 . GLU A 1 288 ? -5.67816  19.12550  21.97298  1.000 68.88657 ? 288 GLU A OE2 1 
ATOM   2197 N N   . ASP A 1 289 ? -10.23814 18.10260  24.76783  1.000 23.95247 ? 289 ASP A N   1 
ATOM   2198 C CA  . ASP A 1 289 ? -11.52983 17.47546  25.05978  1.000 25.07086 ? 289 ASP A CA  1 
ATOM   2199 C C   . ASP A 1 289 ? -12.01717 16.52534  23.96520  1.000 25.08657 ? 289 ASP A C   1 
ATOM   2200 O O   . ASP A 1 289 ? -13.20630 16.18491  23.92438  1.000 26.77219 ? 289 ASP A O   1 
ATOM   2201 C CB  . ASP A 1 289 ? -12.59596 18.52877  25.37442  1.000 23.38980 ? 289 ASP A CB  1 
ATOM   2202 C CG  . ASP A 1 289 ? -13.08943 19.28554  24.14493  1.000 31.51380 ? 289 ASP A CG  1 
ATOM   2203 O OD1 . ASP A 1 289 ? -12.47976 19.16632  23.06326  1.000 30.72762 ? 289 ASP A OD1 1 
ATOM   2204 O OD2 . ASP A 1 289 ? -14.11692 19.99611  24.27682  1.000 26.14511 ? 289 ASP A OD2 1 
ATOM   2205 N N   . GLU A 1 290 ? -11.13732 16.02637  23.11231  1.000 21.69885 ? 290 GLU A N   1 
ATOM   2206 C CA  . GLU A 1 290 ? -11.57654 15.10603  22.07689  1.000 22.91629 ? 290 GLU A CA  1 
ATOM   2207 C C   . GLU A 1 290 ? -11.02231 13.69373  22.28241  1.000 26.69045 ? 290 GLU A C   1 
ATOM   2208 O O   . GLU A 1 290 ? -10.74954 12.97998  21.31210  1.000 25.96506 ? 290 GLU A O   1 
ATOM   2209 C CB  . GLU A 1 290 ? -11.23334 15.66941  20.69516  1.000 27.39378 ? 290 GLU A CB  1 
ATOM   2210 C CG  . GLU A 1 290 ? -11.90183 17.04111  20.42656  1.000 27.69944 ? 290 GLU A CG  1 
ATOM   2211 C CD  . GLU A 1 290 ? -12.14448 17.34250  18.94504  1.000 34.16092 ? 290 GLU A CD  1 
ATOM   2212 O OE1 . GLU A 1 290 ? -11.44571 16.78309  18.07915  1.000 29.63810 ? 290 GLU A OE1 1 
ATOM   2213 O OE2 . GLU A 1 290 ? -13.03149 18.17457  18.65050  1.000 30.22979 ? 290 GLU A OE2 1 
ATOM   2214 N N   . PHE A 1 291 ? -10.86618 13.27461  23.54569  1.000 20.67337 ? 291 PHE A N   1 
ATOM   2215 C CA  . PHE A 1 291 ? -10.67148 11.87279  23.92125  1.000 23.46814 ? 291 PHE A CA  1 
ATOM   2216 C C   . PHE A 1 291 ? -11.77191 11.46522  24.89058  1.000 23.64831 ? 291 PHE A C   1 
ATOM   2217 O O   . PHE A 1 291 ? -11.85778 12.02745  25.98583  1.000 24.98456 ? 291 PHE A O   1 
ATOM   2218 C CB  . PHE A 1 291 ? -9.33770  11.64203  24.63080  1.000 28.04805 ? 291 PHE A CB  1 
ATOM   2219 C CG  . PHE A 1 291 ? -8.12971  11.91140  23.80479  1.000 30.42557 ? 291 PHE A CG  1 
ATOM   2220 C CD1 . PHE A 1 291 ? -7.60077  10.92151  22.99254  1.000 28.08069 ? 291 PHE A CD1 1 
ATOM   2221 C CD2 . PHE A 1 291 ? -7.47647  13.13552  23.89832  1.000 24.43856 ? 291 PHE A CD2 1 
ATOM   2222 C CE1 . PHE A 1 291 ? -6.44473  11.16478  22.25132  1.000 29.07592 ? 291 PHE A CE1 1 
ATOM   2223 C CE2 . PHE A 1 291 ? -6.33505  13.38411  23.17153  1.000 26.41513 ? 291 PHE A CE2 1 
ATOM   2224 C CZ  . PHE A 1 291 ? -5.81939  12.40697  22.34654  1.000 33.23739 ? 291 PHE A CZ  1 
ATOM   2225 N N   . THR A 1 292 ? -12.56230 10.45757  24.53644  1.000 25.57446 ? 292 THR A N   1 
ATOM   2226 C CA  . THR A 1 292 ? -13.55748 9.96609   25.47929  1.000 25.36208 ? 292 THR A CA  1 
ATOM   2227 C C   . THR A 1 292 ? -12.90246 9.07893   26.52618  1.000 25.38739 ? 292 THR A C   1 
ATOM   2228 O O   . THR A 1 292 ? -11.75828 8.63239   26.38720  1.000 26.51472 ? 292 THR A O   1 
ATOM   2229 C CB  . THR A 1 292 ? -14.64487 9.16628   24.76661  1.000 29.53937 ? 292 THR A CB  1 
ATOM   2230 O OG1 . THR A 1 292 ? -14.07911 7.93093   24.28445  1.000 30.06286 ? 292 THR A OG1 1 
ATOM   2231 C CG2 . THR A 1 292 ? -15.28194 9.97690   23.62397  1.000 24.29480 ? 292 THR A CG2 1 
ATOM   2232 N N   . PRO A 1 293 ? -13.62347 8.77298   27.59447  1.000 25.04567 ? 293 PRO A N   1 
ATOM   2233 C CA  . PRO A 1 293 ? -13.09489 7.78731   28.55096  1.000 26.05827 ? 293 PRO A CA  1 
ATOM   2234 C C   . PRO A 1 293 ? -12.76551 6.45455   27.89340  1.000 29.65987 ? 293 PRO A C   1 
ATOM   2235 O O   . PRO A 1 293 ? -11.71411 5.86240   28.19688  1.000 27.18540 ? 293 PRO A O   1 
ATOM   2236 C CB  . PRO A 1 293 ? -14.22222 7.67919   29.58439  1.000 23.12448 ? 293 PRO A CB  1 
ATOM   2237 C CG  . PRO A 1 293 ? -14.86328 9.05607   29.55156  1.000 22.77427 ? 293 PRO A CG  1 
ATOM   2238 C CD  . PRO A 1 293 ? -14.85998 9.41189   28.06807  1.000 25.07166 ? 293 PRO A CD  1 
ATOM   2239 N N   . PHE A 1 294 ? -13.60454 6.00669   26.94603  1.000 28.74814 ? 294 PHE A N   1 
ATOM   2240 C CA  . PHE A 1 294 ? -13.32519 4.77660   26.20627  1.000 25.84053 ? 294 PHE A CA  1 
ATOM   2241 C C   . PHE A 1 294 ? -12.02827 4.89534   25.40488  1.000 26.48496 ? 294 PHE A C   1 
ATOM   2242 O O   . PHE A 1 294 ? -11.18413 3.98642   25.42754  1.000 28.23755 ? 294 PHE A O   1 
ATOM   2243 C CB  . PHE A 1 294 ? -14.50461 4.43569   25.29369  1.000 30.54015 ? 294 PHE A CB  1 
ATOM   2244 N N   . ASP A 1 295 ? -11.85237 6.01330   24.69116  1.000 28.34953 ? 295 ASP A N   1 
ATOM   2245 C CA  . ASP A 1 295 ? -10.60735 6.25956   23.96079  1.000 25.69959 ? 295 ASP A CA  1 
ATOM   2246 C C   . ASP A 1 295 ? -9.39074  6.09133   24.86572  1.000 30.75533 ? 295 ASP A C   1 
ATOM   2247 O O   . ASP A 1 295 ? -8.39320  5.46565   24.48189  1.000 30.11176 ? 295 ASP A O   1 
ATOM   2248 C CB  . ASP A 1 295 ? -10.61730 7.67264   23.35509  1.000 24.13843 ? 295 ASP A CB  1 
ATOM   2249 C CG  . ASP A 1 295 ? -11.69310 7.84967   22.29445  1.000 30.53811 ? 295 ASP A CG  1 
ATOM   2250 O OD1 . ASP A 1 295 ? -12.23633 6.81241   21.85176  1.000 31.12657 ? 295 ASP A OD1 1 
ATOM   2251 O OD2 . ASP A 1 295 ? -11.99253 9.01906   21.91034  1.000 26.53342 ? 295 ASP A OD2 1 
ATOM   2252 N N   . VAL A 1 296 ? -9.44523  6.66881   26.07203  1.000 27.97667 ? 296 VAL A N   1 
ATOM   2253 C CA  . VAL A 1 296 ? -8.28611  6.63938   26.96514  1.000 26.68526 ? 296 VAL A CA  1 
ATOM   2254 C C   . VAL A 1 296 ? -8.05942  5.23190   27.50959  1.000 25.47298 ? 296 VAL A C   1 
ATOM   2255 O O   . VAL A 1 296 ? -6.92316  4.74102   27.55832  1.000 27.04388 ? 296 VAL A O   1 
ATOM   2256 C CB  . VAL A 1 296 ? -8.45753  7.67005   28.09980  1.000 24.11753 ? 296 VAL A CB  1 
ATOM   2257 C CG1 . VAL A 1 296 ? -7.35094  7.53293   29.14438  1.000 25.51174 ? 296 VAL A CG1 1 
ATOM   2258 C CG2 . VAL A 1 296 ? -8.45613  9.08368   27.54132  1.000 21.96053 ? 296 VAL A CG2 1 
ATOM   2259 N N   . VAL A 1 297 ? -9.12072  4.56335   27.95177  1.000 25.69157 ? 297 VAL A N   1 
ATOM   2260 C CA  . VAL A 1 297 ? -8.95515  3.18459   28.41550  1.000 25.91141 ? 297 VAL A CA  1 
ATOM   2261 C C   . VAL A 1 297 ? -8.35117  2.32697   27.31100  1.000 29.82292 ? 297 VAL A C   1 
ATOM   2262 O O   . VAL A 1 297 ? -7.40243  1.56685   27.53925  1.000 34.04293 ? 297 VAL A O   1 
ATOM   2263 C CB  . VAL A 1 297 ? -10.29101 2.60646   28.91442  1.000 27.50640 ? 297 VAL A CB  1 
ATOM   2264 C CG1 . VAL A 1 297 ? -10.23645 1.08210   28.91376  1.000 31.35551 ? 297 VAL A CG1 1 
ATOM   2265 C CG2 . VAL A 1 297 ? -10.56655 3.10895   30.31083  1.000 28.68691 ? 297 VAL A CG2 1 
ATOM   2266 N N   . ARG A 1 298 ? -8.87247  2.46138   26.08828  1.000 27.83461 ? 298 ARG A N   1 
ATOM   2267 C CA  . ARG A 1 298 ? -8.41321  1.62102   24.98894  1.000 28.90952 ? 298 ARG A CA  1 
ATOM   2268 C C   . ARG A 1 298 ? -6.93504  1.85316   24.70661  1.000 36.20602 ? 298 ARG A C   1 
ATOM   2269 O O   . ARG A 1 298 ? -6.18225  0.89908   24.47042  1.000 39.14139 ? 298 ARG A O   1 
ATOM   2270 C CB  . ARG A 1 298 ? -9.25671  1.88319   23.73771  1.000 34.20852 ? 298 ARG A CB  1 
ATOM   2271 C CG  . ARG A 1 298 ? -8.98321  0.92597   22.57550  1.000 35.20862 ? 298 ARG A CG  1 
ATOM   2272 C CD  . ARG A 1 298 ? -9.83659  1.25971   21.35685  1.000 47.85533 ? 298 ARG A CD  1 
ATOM   2273 N NE  . ARG A 1 298 ? -9.60086  0.35445   20.23334  1.000 48.48232 ? 298 ARG A NE  1 
ATOM   2274 C CZ  . ARG A 1 298 ? -8.84882  0.64318   19.17634  1.000 54.15807 ? 298 ARG A CZ  1 
ATOM   2275 N NH1 . ARG A 1 298 ? -8.21774  1.80413   19.07258  1.000 52.46201 ? 298 ARG A NH1 1 
ATOM   2276 N NH2 . ARG A 1 298 ? -8.74263  -0.24681  18.18705  1.000 37.08284 ? 298 ARG A NH2 1 
ATOM   2277 N N   . GLN A 1 299 ? -6.48976  3.11041   24.75947  1.000 31.11107 ? 299 GLN A N   1 
ATOM   2278 C CA  . GLN A 1 299 ? -5.11145  3.41023   24.38927  1.000 31.14344 ? 299 GLN A CA  1 
ATOM   2279 C C   . GLN A 1 299 ? -4.13518  3.20451   25.54956  1.000 38.40541 ? 299 GLN A C   1 
ATOM   2280 O O   . GLN A 1 299 ? -2.96063  2.90905   25.30965  1.000 35.64541 ? 299 GLN A O   1 
ATOM   2281 C CB  . GLN A 1 299 ? -4.99563  4.84340   23.84553  1.000 28.90696 ? 299 GLN A CB  1 
ATOM   2282 C CG  . GLN A 1 299 ? -3.59323  5.16486   23.36380  1.000 27.07542 ? 299 GLN A CG  1 
ATOM   2283 C CD  . GLN A 1 299 ? -3.43758  6.56746   22.80394  1.000 28.88767 ? 299 GLN A CD  1 
ATOM   2284 O OE1 . GLN A 1 299 ? -2.31744  7.04500   22.64269  1.000 24.55011 ? 299 GLN A OE1 1 
ATOM   2285 N NE2 . GLN A 1 299 ? -4.56139  7.23924   22.50769  1.000 29.31560 ? 299 GLN A NE2 1 
ATOM   2286 N N   . CYS A 1 300 ? -4.58246  3.34902   26.80070  1.000 31.95930 ? 300 CYS A N   1 
ATOM   2287 C CA  . CYS A 1 300 ? -3.68468  3.26815   27.95045  1.000 30.92333 ? 300 CYS A CA  1 
ATOM   2288 C C   . CYS A 1 300 ? -3.72936  1.93447   28.68463  1.000 44.86331 ? 300 CYS A C   1 
ATOM   2289 O O   . CYS A 1 300 ? -2.89310  1.71063   29.56678  1.000 50.13773 ? 300 CYS A O   1 
ATOM   2290 C CB  . CYS A 1 300 ? -3.98842  4.38769   28.95574  1.000 32.53456 ? 300 CYS A CB  1 
ATOM   2291 S SG  . CYS A 1 300 ? -3.65669  6.02217   28.30915  1.000 41.74506 ? 300 CYS A SG  1 
ATOM   2292 N N   . SER A 1 301 ? -4.67458  1.05476   28.35812  1.000 38.88063 ? 301 SER A N   1 
ATOM   2293 C CA  . SER A 1 301 ? -4.82426  -0.20911  29.07514  1.000 46.96315 ? 301 SER A CA  1 
ATOM   2294 C C   . SER A 1 301 ? -4.83017  -1.38550  28.10426  1.000 50.00643 ? 301 SER A C   1 
ATOM   2295 O O   . SER A 1 301 ? -4.38832  -2.48856  28.44779  1.000 56.74895 ? 301 SER A O   1 
ATOM   2296 C CB  . SER A 1 301 ? -6.11628  -0.20492  29.90031  1.000 45.65420 ? 301 SER A CB  1 
ATOM   2297 O OG  . SER A 1 301 ? -6.25610  0.99874   30.64163  1.000 51.23270 ? 301 SER A OG  1 
ATOM   2298 N N   . GLY A 1 302 ? -5.34303  -1.16117  26.89553  1.000 42.56340 ? 302 GLY A N   1 
ATOM   2299 C CA  . GLY A 1 302 ? -5.43853  -2.20470  25.88752  1.000 45.91473 ? 302 GLY A CA  1 
ATOM   2300 C C   . GLY A 1 302 ? -6.86427  -2.54556  25.48956  1.000 54.80936 ? 302 GLY A C   1 
ATOM   2301 O O   . GLY A 1 302 ? -7.81068  -2.28094  26.23459  1.000 59.49313 ? 302 GLY A O   1 
ATOM   2302 N N   . ARG B 1 4   ? -4.57444  20.42277  10.38727  1.000 48.44543 ? 4   ARG B N   1 
ATOM   2303 C CA  . ARG B 1 4   ? -4.24566  19.59057  11.53977  1.000 45.80741 ? 4   ARG B CA  1 
ATOM   2304 C C   . ARG B 1 4   ? -3.23600  18.49881  11.18042  1.000 46.25658 ? 4   ARG B C   1 
ATOM   2305 O O   . ARG B 1 4   ? -2.80218  18.37963  10.02976  1.000 51.21764 ? 4   ARG B O   1 
ATOM   2306 C CB  . ARG B 1 4   ? -5.49870  18.93880  12.10725  1.000 44.82919 ? 4   ARG B CB  1 
ATOM   2307 C CG  . ARG B 1 4   ? -6.08528  17.88858  11.17705  1.000 44.67020 ? 4   ARG B CG  1 
ATOM   2308 C CD  . ARG B 1 4   ? -7.14309  17.07668  11.88905  1.000 43.36446 ? 4   ARG B CD  1 
ATOM   2309 N NE  . ARG B 1 4   ? -8.06994  17.94094  12.60575  1.000 43.54484 ? 4   ARG B NE  1 
ATOM   2310 C CZ  . ARG B 1 4   ? -8.84628  17.53237  13.59647  1.000 41.47788 ? 4   ARG B CZ  1 
ATOM   2311 N NH1 . ARG B 1 4   ? -8.84017  16.27361  14.00300  1.000 46.40876 ? 4   ARG B NH1 1 
ATOM   2312 N NH2 . ARG B 1 4   ? -9.62769  18.41256  14.21329  1.000 54.03912 ? 4   ARG B NH2 1 
ATOM   2313 N N   . LYS B 1 5   ? -2.87493  17.69670  12.17513  1.000 43.81772 ? 5   LYS B N   1 
ATOM   2314 C CA  . LYS B 1 5   ? -1.96544  16.57873  11.97389  1.000 50.72540 ? 5   LYS B CA  1 
ATOM   2315 C C   . LYS B 1 5   ? -2.77800  15.36619  11.54107  1.000 42.00101 ? 5   LYS B C   1 
ATOM   2316 O O   . LYS B 1 5   ? -3.63238  14.88455  12.29282  1.000 47.68630 ? 5   LYS B O   1 
ATOM   2317 C CB  . LYS B 1 5   ? -1.17495  16.28003  13.24698  1.000 46.91583 ? 5   LYS B CB  1 
ATOM   2318 N N   . MET B 1 6   ? -2.51943  14.88516  10.33194  1.000 38.69485 ? 6   MET B N   1 
ATOM   2319 C CA  . MET B 1 6   ? -3.18479  13.71323  9.79050   1.000 31.24821 ? 6   MET B CA  1 
ATOM   2320 C C   . MET B 1 6   ? -2.21510  12.54922  9.66508   1.000 31.35861 ? 6   MET B C   1 
ATOM   2321 O O   . MET B 1 6   ? -1.00863  12.73774  9.47405   1.000 32.20689 ? 6   MET B O   1 
ATOM   2322 C CB  . MET B 1 6   ? -3.76367  13.98929  8.40598   1.000 28.16015 ? 6   MET B CB  1 
ATOM   2323 C CG  . MET B 1 6   ? -4.76906  15.09259  8.34547   1.000 42.61593 ? 6   MET B CG  1 
ATOM   2324 S SD  . MET B 1 6   ? -5.32722  15.17346  6.63639   1.000 49.96212 ? 6   MET B SD  1 
ATOM   2325 C CE  . MET B 1 6   ? -6.79248  16.18374  6.84854   1.000 44.86379 ? 6   MET B CE  1 
ATOM   2326 N N   . ALA B 1 7   ? -2.76383  11.34242  9.74239   1.000 25.87899 ? 7   ALA B N   1 
ATOM   2327 C CA  . ALA B 1 7   ? -2.03300  10.16478  9.30578   1.000 23.27146 ? 7   ALA B CA  1 
ATOM   2328 C C   . ALA B 1 7   ? -2.34329  9.88564   7.83534   1.000 27.58462 ? 7   ALA B C   1 
ATOM   2329 O O   . ALA B 1 7   ? -3.34356  10.35939  7.29067   1.000 20.08878 ? 7   ALA B O   1 
ATOM   2330 C CB  . ALA B 1 7   ? -2.38932  8.95572   10.17191  1.000 24.95515 ? 7   ALA B CB  1 
ATOM   2331 N N   . PHE B 1 8   ? -1.44342  9.14778   7.18320   1.000 28.50707 ? 8   PHE B N   1 
ATOM   2332 C CA  . PHE B 1 8   ? -1.75186  8.55849   5.89249   1.000 25.16659 ? 8   PHE B CA  1 
ATOM   2333 C C   . PHE B 1 8   ? -2.80033  7.46530   6.05966   1.000 22.41078 ? 8   PHE B C   1 
ATOM   2334 O O   . PHE B 1 8   ? -2.82093  6.78206   7.08346   1.000 23.26603 ? 8   PHE B O   1 
ATOM   2335 C CB  . PHE B 1 8   ? -0.50990  7.93661   5.27093   1.000 28.59309 ? 8   PHE B CB  1 
ATOM   2336 C CG  . PHE B 1 8   ? 0.49329   8.93604   4.78176   1.000 26.97633 ? 8   PHE B CG  1 
ATOM   2337 C CD1 . PHE B 1 8   ? 0.32064   9.57502   3.55346   1.000 34.07046 ? 8   PHE B CD1 1 
ATOM   2338 C CD2 . PHE B 1 8   ? 1.62489   9.21613   5.53318   1.000 32.18317 ? 8   PHE B CD2 1 
ATOM   2339 C CE1 . PHE B 1 8   ? 1.25581   10.50263  3.10171   1.000 29.11577 ? 8   PHE B CE1 1 
ATOM   2340 C CE2 . PHE B 1 8   ? 2.56309   10.13252  5.08337   1.000 35.87382 ? 8   PHE B CE2 1 
ATOM   2341 C CZ  . PHE B 1 8   ? 2.37593   10.76740  3.86185   1.000 28.88545 ? 8   PHE B CZ  1 
ATOM   2342 N N   . PRO B 1 9   ? -3.65992  7.25713   5.06092   1.000 22.38496 ? 9   PRO B N   1 
ATOM   2343 C CA  . PRO B 1 9   ? -4.57980  6.11120   5.12632   1.000 25.16327 ? 9   PRO B CA  1 
ATOM   2344 C C   . PRO B 1 9   ? -3.75895  4.84196   5.30270   1.000 24.03707 ? 9   PRO B C   1 
ATOM   2345 O O   . PRO B 1 9   ? -2.73139  4.66018   4.64759   1.000 27.13550 ? 9   PRO B O   1 
ATOM   2346 C CB  . PRO B 1 9   ? -5.30627  6.14586   3.76818   1.000 22.17260 ? 9   PRO B CB  1 
ATOM   2347 C CG  . PRO B 1 9   ? -5.04790  7.51960   3.20774   1.000 23.48851 ? 9   PRO B CG  1 
ATOM   2348 C CD  . PRO B 1 9   ? -3.70096  7.92820   3.74391   1.000 25.79337 ? 9   PRO B CD  1 
ATOM   2349 N N   . SER B 1 10  ? -4.18605  3.98472   6.22067   1.000 19.97570 ? 10  SER B N   1 
ATOM   2350 C CA  . SER B 1 10  ? -3.36974  2.84007   6.62863   1.000 23.40823 ? 10  SER B CA  1 
ATOM   2351 C C   . SER B 1 10  ? -3.68123  1.54592   5.87768   1.000 22.17542 ? 10  SER B C   1 
ATOM   2352 O O   . SER B 1 10  ? -3.04809  0.52089   6.15635   1.000 23.54735 ? 10  SER B O   1 
ATOM   2353 C CB  . SER B 1 10  ? -3.54209  2.59066   8.12775   1.000 24.35749 ? 10  SER B CB  1 
ATOM   2354 O OG  . SER B 1 10  ? -4.91145  2.36536   8.42620   1.000 24.97981 ? 10  SER B OG  1 
ATOM   2355 N N   . GLY B 1 11  ? -4.62142  1.56207   4.93396   1.000 24.46444 ? 11  GLY B N   1 
ATOM   2356 C CA  . GLY B 1 11  ? -5.09035  0.30839   4.34581   1.000 23.72364 ? 11  GLY B CA  1 
ATOM   2357 C C   . GLY B 1 11  ? -3.98642  -0.51145  3.70178   1.000 26.11858 ? 11  GLY B C   1 
ATOM   2358 O O   . GLY B 1 11  ? -3.95428  -1.74256  3.83107   1.000 24.54553 ? 11  GLY B O   1 
ATOM   2359 N N   . LYS B 1 12  ? -3.06911  0.15262   2.99306   1.000 26.85640 ? 12  LYS B N   1 
ATOM   2360 C CA  . LYS B 1 12  ? -2.00638  -0.57955  2.30942   1.000 29.01501 ? 12  LYS B CA  1 
ATOM   2361 C C   . LYS B 1 12  ? -1.06336  -1.26364  3.28779   1.000 26.57349 ? 12  LYS B C   1 
ATOM   2362 O O   . LYS B 1 12  ? -0.45721  -2.28516  2.94329   1.000 26.94963 ? 12  LYS B O   1 
ATOM   2363 C CB  . LYS B 1 12  ? -1.22115  0.36046   1.39654   1.000 29.73388 ? 12  LYS B CB  1 
ATOM   2364 C CG  . LYS B 1 12  ? -1.97123  0.76213   0.12708   1.000 30.63266 ? 12  LYS B CG  1 
ATOM   2365 C CD  . LYS B 1 12  ? -1.32624  1.99066   -0.52665  1.000 33.77920 ? 12  LYS B CD  1 
ATOM   2366 C CE  . LYS B 1 12  ? -2.02858  2.35726   -1.83588  1.000 42.03468 ? 12  LYS B CE  1 
ATOM   2367 N NZ  . LYS B 1 12  ? -1.83703  1.29232   -2.84932  1.000 50.67044 ? 12  LYS B NZ  1 
ATOM   2368 N N   . VAL B 1 13  ? -0.91676  -0.72257  4.49735   1.000 24.79825 ? 13  VAL B N   1 
ATOM   2369 C CA  . VAL B 1 13  ? -0.06596  -1.36521  5.49742   1.000 22.60641 ? 13  VAL B CA  1 
ATOM   2370 C C   . VAL B 1 13  ? -0.84220  -2.43622  6.24695   1.000 24.55591 ? 13  VAL B C   1 
ATOM   2371 O O   . VAL B 1 13  ? -0.29393  -3.49256  6.57969   1.000 22.61180 ? 13  VAL B O   1 
ATOM   2372 C CB  . VAL B 1 13  ? 0.52387   -0.32308  6.47051   1.000 23.66916 ? 13  VAL B CB  1 
ATOM   2373 C CG1 . VAL B 1 13  ? 1.44097   -1.01062  7.49164   1.000 19.40128 ? 13  VAL B CG1 1 
ATOM   2374 C CG2 . VAL B 1 13  ? 1.26099   0.77177   5.70040   1.000 28.00739 ? 13  VAL B CG2 1 
ATOM   2375 N N   . GLU B 1 14  ? -2.12284  -2.17830  6.54183   1.000 20.05345 ? 14  GLU B N   1 
ATOM   2376 C CA  . GLU B 1 14  ? -2.93472  -3.18369  7.21712   1.000 20.21788 ? 14  GLU B CA  1 
ATOM   2377 C C   . GLU B 1 14  ? -2.86105  -4.52444  6.50094   1.000 21.85944 ? 14  GLU B C   1 
ATOM   2378 O O   . GLU B 1 14  ? -2.80353  -5.58046  7.13812   1.000 22.78743 ? 14  GLU B O   1 
ATOM   2379 C CB  . GLU B 1 14  ? -4.39503  -2.72116  7.29383   1.000 19.87208 ? 14  GLU B CB  1 
ATOM   2380 C CG  . GLU B 1 14  ? -4.64939  -1.60243  8.29341   1.000 20.50776 ? 14  GLU B CG  1 
ATOM   2381 C CD  . GLU B 1 14  ? -6.03424  -0.99460  8.11451   1.000 28.24474 ? 14  GLU B CD  1 
ATOM   2382 O OE1 . GLU B 1 14  ? -7.03508  -1.74595  8.18580   1.000 24.29784 ? 14  GLU B OE1 1 
ATOM   2383 O OE2 . GLU B 1 14  ? -6.11259  0.22636   7.86021   1.000 28.24665 ? 14  GLU B OE2 1 
ATOM   2384 N N   . GLY B 1 15  ? -2.88161  -4.50475  5.16680   1.000 22.39951 ? 15  GLY B N   1 
ATOM   2385 C CA  . GLY B 1 15  ? -2.87039  -5.74824  4.42885   1.000 21.55094 ? 15  GLY B CA  1 
ATOM   2386 C C   . GLY B 1 15  ? -1.56612  -6.49570  4.47395   1.000 25.64314 ? 15  GLY B C   1 
ATOM   2387 O O   . GLY B 1 15  ? -1.49277  -7.59405  3.91188   1.000 25.07308 ? 15  GLY B O   1 
ATOM   2388 N N   . CYS B 1 16  ? -0.54965  -5.93883  5.14042   1.000 21.52208 ? 16  CYS B N   1 
ATOM   2389 C CA  . CYS B 1 16  ? 0.75983   -6.55387  5.28533   1.000 20.20805 ? 16  CYS B CA  1 
ATOM   2390 C C   . CYS B 1 16  ? 1.07629   -7.00486  6.70617   1.000 24.51389 ? 16  CYS B C   1 
ATOM   2391 O O   . CYS B 1 16  ? 2.16684   -7.54495  6.93416   1.000 22.03380 ? 16  CYS B O   1 
ATOM   2392 C CB  . CYS B 1 16  ? 1.84526   -5.58128  4.82943   1.000 19.64646 ? 16  CYS B CB  1 
ATOM   2393 S SG  . CYS B 1 16  ? 1.64342   -5.06336  3.13042   1.000 25.04691 ? 16  CYS B SG  1 
ATOM   2394 N N   . MET B 1 17  ? 0.16617   -6.83249  7.66128   1.000 19.27826 ? 17  MET B N   1 
ATOM   2395 C CA  . MET B 1 17  ? 0.47649   -7.12660  9.05926   1.000 21.08679 ? 17  MET B CA  1 
ATOM   2396 C C   . MET B 1 17  ? 0.16677   -8.58885  9.38576   1.000 24.36493 ? 17  MET B C   1 
ATOM   2397 O O   . MET B 1 17  ? -0.91280  -9.09146  9.04916   1.000 24.41691 ? 17  MET B O   1 
ATOM   2398 C CB  . MET B 1 17  ? -0.28887  -6.19642  10.00430  1.000 23.41302 ? 17  MET B CB  1 
ATOM   2399 C CG  . MET B 1 17  ? 0.10584   -4.69952  9.89231   1.000 20.92698 ? 17  MET B CG  1 
ATOM   2400 S SD  . MET B 1 17  ? 1.89029   -4.35537  9.86446   1.000 21.17785 ? 17  MET B SD  1 
ATOM   2401 C CE  . MET B 1 17  ? 2.42976   -4.97901  11.46507  1.000 22.54858 ? 17  MET B CE  1 
ATOM   2402 N N   . VAL B 1 18  ? 1.12717   -9.26571  10.02629  1.000 22.33457 ? 18  VAL B N   1 
ATOM   2403 C CA  . VAL B 1 18  ? 1.00559   -10.65981 10.46763  1.000 19.12556 ? 18  VAL B CA  1 
ATOM   2404 C C   . VAL B 1 18  ? 1.53953   -10.75757 11.89111  1.000 20.16347 ? 18  VAL B C   1 
ATOM   2405 O O   . VAL B 1 18  ? 2.06885   -9.79615  12.44959  1.000 21.78637 ? 18  VAL B O   1 
ATOM   2406 C CB  . VAL B 1 18  ? 1.75663   -11.65089 9.55282   1.000 19.36843 ? 18  VAL B CB  1 
ATOM   2407 C CG1 . VAL B 1 18  ? 1.22254   -11.58664 8.11943   1.000 19.47663 ? 18  VAL B CG1 1 
ATOM   2408 C CG2 . VAL B 1 18  ? 3.26505   -11.38902 9.58474   1.000 18.18931 ? 18  VAL B CG2 1 
ATOM   2409 N N   . GLN B 1 19  ? 1.38965   -11.93593 12.49067  1.000 19.27408 ? 19  GLN B N   1 
ATOM   2410 C CA  . GLN B 1 19  ? 1.98693   -12.17177 13.80178  1.000 24.12028 ? 19  GLN B CA  1 
ATOM   2411 C C   . GLN B 1 19  ? 3.03915   -13.26918 13.70839  1.000 21.17632 ? 19  GLN B C   1 
ATOM   2412 O O   . GLN B 1 19  ? 2.90975   -14.20839 12.91682  1.000 27.58631 ? 19  GLN B O   1 
ATOM   2413 C CB  . GLN B 1 19  ? 0.92658   -12.49347 14.87983  1.000 29.27922 ? 19  GLN B CB  1 
ATOM   2414 C CG  . GLN B 1 19  ? -0.00198  -13.66063 14.62874  1.000 30.60166 ? 19  GLN B CG  1 
ATOM   2415 C CD  . GLN B 1 19  ? -1.15290  -13.70347 15.65479  1.000 35.64451 ? 19  GLN B CD  1 
ATOM   2416 O OE1 . GLN B 1 19  ? -2.32283  -13.86492 15.29209  1.000 37.55374 ? 19  GLN B OE1 1 
ATOM   2417 N NE2 . GLN B 1 19  ? -0.81533  -13.55394 16.93137  1.000 25.37166 ? 19  GLN B NE2 1 
ATOM   2418 N N   . VAL B 1 20  ? 4.10629   -13.09500 14.48163  1.000 19.91979 ? 20  VAL B N   1 
ATOM   2419 C CA  . VAL B 1 20  ? 5.24559   -13.99923 14.54304  1.000 19.35706 ? 20  VAL B CA  1 
ATOM   2420 C C   . VAL B 1 20  ? 5.42252   -14.43254 15.99177  1.000 23.06959 ? 20  VAL B C   1 
ATOM   2421 O O   . VAL B 1 20  ? 5.51185   -13.58689 16.89334  1.000 23.81168 ? 20  VAL B O   1 
ATOM   2422 C CB  . VAL B 1 20  ? 6.52854   -13.32829 14.01739  1.000 19.59903 ? 20  VAL B CB  1 
ATOM   2423 C CG1 . VAL B 1 20  ? 7.68278   -14.30847 14.01367  1.000 25.70234 ? 20  VAL B CG1 1 
ATOM   2424 C CG2 . VAL B 1 20  ? 6.28369   -12.76049 12.61310  1.000 21.60153 ? 20  VAL B CG2 1 
ATOM   2425 N N   . THR B 1 21  ? 5.51809   -15.73966 16.20267  1.000 23.87505 ? 21  THR B N   1 
ATOM   2426 C CA  . THR B 1 21  ? 5.59679   -16.33372 17.52909  1.000 22.39803 ? 21  THR B CA  1 
ATOM   2427 C C   . THR B 1 21  ? 6.72349   -17.35427 17.57879  1.000 25.69667 ? 21  THR B C   1 
ATOM   2428 O O   . THR B 1 21  ? 6.83132   -18.22007 16.69902  1.000 22.87802 ? 21  THR B O   1 
ATOM   2429 C CB  . THR B 1 21  ? 4.27398   -17.00790 17.90025  1.000 22.65365 ? 21  THR B CB  1 
ATOM   2430 O OG1 . THR B 1 21  ? 3.23281   -16.02347 17.89583  1.000 25.07723 ? 21  THR B OG1 1 
ATOM   2431 C CG2 . THR B 1 21  ? 4.36313   -17.65153 19.27548  1.000 28.90359 ? 21  THR B CG2 1 
ATOM   2432 N N   . CYS B 1 22  ? 7.55156   -17.24441 18.61103  1.000 24.98294 ? 22  CYS B N   1 
ATOM   2433 C CA  . CYS B 1 22  ? 8.52449   -18.25671 19.00315  1.000 25.96028 ? 22  CYS B CA  1 
ATOM   2434 C C   . CYS B 1 22  ? 8.17851   -18.68548 20.42533  1.000 24.59891 ? 22  CYS B C   1 
ATOM   2435 O O   . CYS B 1 22  ? 8.17858   -17.85044 21.33605  1.000 27.07862 ? 22  CYS B O   1 
ATOM   2436 C CB  . CYS B 1 22  ? 9.95369   -17.70124 18.96916  1.000 29.97215 ? 22  CYS B CB  1 
ATOM   2437 S SG  . CYS B 1 22  ? 10.73992  -17.52426 17.36840  1.000 30.75230 ? 22  CYS B SG  1 
ATOM   2438 N N   . GLY B 1 23  ? 7.86948   -19.96639 20.61843  1.000 24.96456 ? 23  GLY B N   1 
ATOM   2439 C CA  . GLY B 1 23  ? 7.49614   -20.40904 21.95907  1.000 23.58384 ? 23  GLY B CA  1 
ATOM   2440 C C   . GLY B 1 23  ? 6.23299   -19.69401 22.40316  1.000 26.39644 ? 23  GLY B C   1 
ATOM   2441 O O   . GLY B 1 23  ? 5.18214   -19.81617 21.76471  1.000 24.73072 ? 23  GLY B O   1 
ATOM   2442 N N   . THR B 1 24  ? 6.30310   -18.93939 23.50685  1.000 25.96440 ? 24  THR B N   1 
ATOM   2443 C CA  . THR B 1 24  ? 5.18609   -18.08622 23.90709  1.000 31.02827 ? 24  THR B CA  1 
ATOM   2444 C C   . THR B 1 24  ? 5.41341   -16.61695 23.57029  1.000 31.30213 ? 24  THR B C   1 
ATOM   2445 O O   . THR B 1 24  ? 4.52719   -15.79928 23.81766  1.000 31.38240 ? 24  THR B O   1 
ATOM   2446 C CB  . THR B 1 24  ? 4.89424   -18.20161 25.41287  1.000 34.72508 ? 24  THR B CB  1 
ATOM   2447 O OG1 . THR B 1 24  ? 5.99779   -17.66813 26.14513  1.000 30.18453 ? 24  THR B OG1 1 
ATOM   2448 C CG2 . THR B 1 24  ? 4.65409   -19.63991 25.82235  1.000 32.95751 ? 24  THR B CG2 1 
ATOM   2449 N N   . THR B 1 25  ? 6.56924   -16.25642 23.02450  1.000 29.79982 ? 25  THR B N   1 
ATOM   2450 C CA  . THR B 1 25  ? 6.83839   -14.86134 22.68758  1.000 30.44666 ? 25  THR B CA  1 
ATOM   2451 C C   . THR B 1 25  ? 6.21388   -14.54299 21.32756  1.000 35.27821 ? 25  THR B C   1 
ATOM   2452 O O   . THR B 1 25  ? 6.54053   -15.19184 20.32987  1.000 31.80083 ? 25  THR B O   1 
ATOM   2453 C CB  . THR B 1 25  ? 8.34459   -14.60634 22.66282  1.000 34.12453 ? 25  THR B CB  1 
ATOM   2454 O OG1 . THR B 1 25  ? 8.93115   -14.93335 23.93971  1.000 34.97068 ? 25  THR B OG1 1 
ATOM   2455 C CG2 . THR B 1 25  ? 8.64492   -13.14682 22.31207  1.000 35.18364 ? 25  THR B CG2 1 
ATOM   2456 N N   . THR B 1 26  ? 5.31858   -13.55062 21.28506  1.000 30.77059 ? 26  THR B N   1 
ATOM   2457 C CA  . THR B 1 26  ? 4.61601   -13.16870 20.06770  1.000 28.97976 ? 26  THR B CA  1 
ATOM   2458 C C   . THR B 1 26  ? 4.76971   -11.67325 19.82987  1.000 36.03117 ? 26  THR B C   1 
ATOM   2459 O O   . THR B 1 26  ? 4.72256   -10.87397 20.76902  1.000 30.07137 ? 26  THR B O   1 
ATOM   2460 C CB  . THR B 1 26  ? 3.11369   -13.51297 20.12254  1.000 33.21769 ? 26  THR B CB  1 
ATOM   2461 O OG1 . THR B 1 26  ? 2.93252   -14.93064 20.08099  1.000 42.25952 ? 26  THR B OG1 1 
ATOM   2462 C CG2 . THR B 1 26  ? 2.37776   -12.91878 18.92384  1.000 32.36394 ? 26  THR B CG2 1 
ATOM   2463 N N   . LEU B 1 27  ? 4.95497   -11.29851 18.57049  1.000 21.54023 ? 27  LEU B N   1 
ATOM   2464 C CA  . LEU B 1 27  ? 4.93180   -9.89498  18.19062  1.000 22.17046 ? 27  LEU B CA  1 
ATOM   2465 C C   . LEU B 1 27  ? 4.42262   -9.81988  16.75891  1.000 25.79525 ? 27  LEU B C   1 
ATOM   2466 O O   . LEU B 1 27  ? 3.88348   -10.79648 16.22346  1.000 23.18180 ? 27  LEU B O   1 
ATOM   2467 C CB  . LEU B 1 27  ? 6.30390   -9.23132  18.36914  1.000 25.04631 ? 27  LEU B CB  1 
ATOM   2468 C CG  . LEU B 1 27  ? 7.58562   -10.01069 18.04117  1.000 29.15779 ? 27  LEU B CG  1 
ATOM   2469 C CD1 . LEU B 1 27  ? 7.74738   -10.24045 16.53899  1.000 27.30646 ? 27  LEU B CD1 1 
ATOM   2470 C CD2 . LEU B 1 27  ? 8.81416   -9.30505  18.60174  1.000 26.00391 ? 27  LEU B CD2 1 
ATOM   2471 N N   . ASN B 1 28  ? 4.57104   -8.64623  16.15478  1.000 20.36089 ? 28  ASN B N   1 
ATOM   2472 C CA  . ASN B 1 28  ? 4.05359   -8.35405  14.82700  1.000 17.86160 ? 28  ASN B CA  1 
ATOM   2473 C C   . ASN B 1 28  ? 5.16755   -8.48049  13.79700  1.000 24.23290 ? 28  ASN B C   1 
ATOM   2474 O O   . ASN B 1 28  ? 6.32835   -8.20156  14.09616  1.000 20.06886 ? 28  ASN B O   1 
ATOM   2475 C CB  . ASN B 1 28  ? 3.48907   -6.93209  14.76930  1.000 19.24524 ? 28  ASN B CB  1 
ATOM   2476 C CG  . ASN B 1 28  ? 2.43613   -6.67705  15.81871  1.000 22.32052 ? 28  ASN B CG  1 
ATOM   2477 O OD1 . ASN B 1 28  ? 1.29415   -7.10525  15.67660  1.000 22.69912 ? 28  ASN B OD1 1 
ATOM   2478 N ND2 . ASN B 1 28  ? 2.81542   -5.96703  16.88591  1.000 23.95855 ? 28  ASN B ND2 1 
ATOM   2479 N N   . GLY B 1 29  ? 4.79225   -8.85766  12.56422  1.000 20.06200 ? 29  GLY B N   1 
ATOM   2480 C CA  . GLY B 1 29  ? 5.71220   -8.84344  11.44604  1.000 22.29460 ? 29  GLY B CA  1 
ATOM   2481 C C   . GLY B 1 29  ? 5.08084   -8.15997  10.24065  1.000 23.31698 ? 29  GLY B C   1 
ATOM   2482 O O   . GLY B 1 29  ? 3.86815   -7.93481  10.19464  1.000 20.90430 ? 29  GLY B O   1 
ATOM   2483 N N   . LEU B 1 30  ? 5.92031   -7.86511  9.24803   1.000 20.31029 ? 30  LEU B N   1 
ATOM   2484 C CA  . LEU B 1 30  ? 5.50825   -7.15083  8.04482   1.000 23.08376 ? 30  LEU B CA  1 
ATOM   2485 C C   . LEU B 1 30  ? 5.71129   -8.05818  6.83661   1.000 20.22765 ? 30  LEU B C   1 
ATOM   2486 O O   . LEU B 1 30  ? 6.84206   -8.44360  6.53228   1.000 18.98587 ? 30  LEU B O   1 
ATOM   2487 C CB  . LEU B 1 30  ? 6.29884   -5.83631  7.90860   1.000 20.07895 ? 30  LEU B CB  1 
ATOM   2488 C CG  . LEU B 1 30  ? 6.02556   -4.99092  6.65542   1.000 19.12757 ? 30  LEU B CG  1 
ATOM   2489 C CD1 . LEU B 1 30  ? 4.62471   -4.34934  6.74698   1.000 20.50278 ? 30  LEU B CD1 1 
ATOM   2490 C CD2 . LEU B 1 30  ? 7.08003   -3.92003  6.42599   1.000 21.22390 ? 30  LEU B CD2 1 
ATOM   2491 N N   . TRP B 1 31  ? 4.62040   -8.37217  6.12909   1.000 18.07082 ? 31  TRP B N   1 
ATOM   2492 C CA  . TRP B 1 31  ? 4.60025   -9.37466  5.06171   1.000 22.59417 ? 31  TRP B CA  1 
ATOM   2493 C C   . TRP B 1 31  ? 4.54856   -8.70509  3.69201   1.000 20.34476 ? 31  TRP B C   1 
ATOM   2494 O O   . TRP B 1 31  ? 3.50085   -8.18690  3.28520   1.000 21.04544 ? 31  TRP B O   1 
ATOM   2495 C CB  . TRP B 1 31  ? 3.39719   -10.29571 5.26017   1.000 22.22569 ? 31  TRP B CB  1 
ATOM   2496 C CG  . TRP B 1 31  ? 3.26559   -11.43539 4.26952   1.000 21.83572 ? 31  TRP B CG  1 
ATOM   2497 C CD1 . TRP B 1 31  ? 4.24783   -11.98552 3.48397   1.000 22.92826 ? 31  TRP B CD1 1 
ATOM   2498 C CD2 . TRP B 1 31  ? 2.07359   -12.15690 3.98696   1.000 21.08119 ? 31  TRP B CD2 1 
ATOM   2499 N NE1 . TRP B 1 31  ? 3.72306   -13.01059 2.72132   1.000 24.16177 ? 31  TRP B NE1 1 
ATOM   2500 C CE2 . TRP B 1 31  ? 2.38742   -13.13230 3.01470   1.000 24.54981 ? 31  TRP B CE2 1 
ATOM   2501 C CE3 . TRP B 1 31  ? 0.75874   -12.06472 4.45142   1.000 24.82802 ? 31  TRP B CE3 1 
ATOM   2502 C CZ2 . TRP B 1 31  ? 1.43132   -14.00650 2.50235   1.000 23.99192 ? 31  TRP B CZ2 1 
ATOM   2503 C CZ3 . TRP B 1 31  ? -0.18696  -12.93741 3.94737   1.000 27.09460 ? 31  TRP B CZ3 1 
ATOM   2504 C CH2 . TRP B 1 31  ? 0.15371   -13.89460 2.97926   1.000 25.39475 ? 31  TRP B CH2 1 
ATOM   2505 N N   . LEU B 1 32  ? 5.66954   -8.74062  2.97282   1.000 20.28791 ? 32  LEU B N   1 
ATOM   2506 C CA  . LEU B 1 32  ? 5.78427   -8.15964  1.64011   1.000 23.77412 ? 32  LEU B CA  1 
ATOM   2507 C C   . LEU B 1 32  ? 6.31594   -9.23135  0.69905   1.000 21.96373 ? 32  LEU B C   1 
ATOM   2508 O O   . LEU B 1 32  ? 7.35154   -9.84247  0.97928   1.000 25.31368 ? 32  LEU B O   1 
ATOM   2509 C CB  . LEU B 1 32  ? 6.71936   -6.93710  1.65865   1.000 25.71738 ? 32  LEU B CB  1 
ATOM   2510 C CG  . LEU B 1 32  ? 6.31105   -5.84700  2.65510   1.000 19.44803 ? 32  LEU B CG  1 
ATOM   2511 C CD1 . LEU B 1 32  ? 7.47377   -4.90510  2.94173   1.000 22.10805 ? 32  LEU B CD1 1 
ATOM   2512 C CD2 . LEU B 1 32  ? 5.11091   -5.06779  2.04407   1.000 19.51784 ? 32  LEU B CD2 1 
ATOM   2513 N N   . ASP B 1 33  ? 5.61881   -9.44455  -0.41649  1.000 24.99246 ? 33  ASP B N   1 
ATOM   2514 C CA  . ASP B 1 33  ? 5.93746   -10.55191 -1.31173  1.000 26.41803 ? 33  ASP B CA  1 
ATOM   2515 C C   . ASP B 1 33  ? 6.02635   -11.84229 -0.49127  1.000 26.01281 ? 33  ASP B C   1 
ATOM   2516 O O   . ASP B 1 33  ? 5.06736   -12.16509 0.21224   1.000 22.34520 ? 33  ASP B O   1 
ATOM   2517 C CB  . ASP B 1 33  ? 7.20138   -10.21765 -2.10264  1.000 25.76164 ? 33  ASP B CB  1 
ATOM   2518 C CG  . ASP B 1 33  ? 6.97338   -9.03471  -3.06308  1.000 31.74617 ? 33  ASP B CG  1 
ATOM   2519 O OD1 . ASP B 1 33  ? 5.90014   -8.98985  -3.72012  1.000 31.34046 ? 33  ASP B OD1 1 
ATOM   2520 O OD2 . ASP B 1 33  ? 7.83673   -8.13366  -3.13175  1.000 32.38189 ? 33  ASP B OD2 1 
ATOM   2521 N N   . ASP B 1 34  ? 7.12916   -12.59441 -0.54476  1.000 24.36576 ? 34  ASP B N   1 
ATOM   2522 C CA  . ASP B 1 34  ? 7.21941   -13.84071 0.21139   1.000 25.80801 ? 34  ASP B CA  1 
ATOM   2523 C C   . ASP B 1 34  ? 8.20780   -13.75551 1.37776   1.000 25.33807 ? 34  ASP B C   1 
ATOM   2524 O O   . ASP B 1 34  ? 8.86791   -14.74816 1.70494   1.000 24.04161 ? 34  ASP B O   1 
ATOM   2525 C CB  . ASP B 1 34  ? 7.57315   -15.01077 -0.70647  1.000 23.64787 ? 34  ASP B CB  1 
ATOM   2526 C CG  . ASP B 1 34  ? 8.93411   -14.85257 -1.37547  1.000 31.81874 ? 34  ASP B CG  1 
ATOM   2527 O OD1 . ASP B 1 34  ? 9.51471   -13.74642 -1.33247  1.000 27.88438 ? 34  ASP B OD1 1 
ATOM   2528 O OD2 . ASP B 1 34  ? 9.42614   -15.85285 -1.94346  1.000 38.69625 ? 34  ASP B OD2 1 
ATOM   2529 N N   . VAL B 1 35  ? 8.31015   -12.58184 2.02105   1.000 22.09440 ? 35  VAL B N   1 
ATOM   2530 C CA  . VAL B 1 35  ? 9.20833   -12.35890 3.14436   1.000 23.45786 ? 35  VAL B CA  1 
ATOM   2531 C C   . VAL B 1 35  ? 8.45464   -11.66848 4.27426   1.000 23.67705 ? 35  VAL B C   1 
ATOM   2532 O O   . VAL B 1 35  ? 7.69177   -10.72653 4.03601   1.000 24.10059 ? 35  VAL B O   1 
ATOM   2533 C CB  . VAL B 1 35  ? 10.42373  -11.50692 2.73745   1.000 21.72786 ? 35  VAL B CB  1 
ATOM   2534 C CG1 . VAL B 1 35  ? 11.31697  -11.26910 3.97575   1.000 21.69252 ? 35  VAL B CG1 1 
ATOM   2535 C CG2 . VAL B 1 35  ? 11.17287  -12.18266 1.59433   1.000 25.53534 ? 35  VAL B CG2 1 
ATOM   2536 N N   . VAL B 1 36  ? 8.68716   -12.12104 5.50540   1.000 19.39314 ? 36  VAL B N   1 
ATOM   2537 C CA  . VAL B 1 36  ? 8.14985   -11.47830 6.70557   1.000 22.98289 ? 36  VAL B CA  1 
ATOM   2538 C C   . VAL B 1 36  ? 9.30691   -10.87882 7.49701   1.000 20.86982 ? 36  VAL B C   1 
ATOM   2539 O O   . VAL B 1 36  ? 10.29294  -11.56627 7.77499   1.000 22.26603 ? 36  VAL B O   1 
ATOM   2540 C CB  . VAL B 1 36  ? 7.34328   -12.48026 7.55412   1.000 23.50103 ? 36  VAL B CB  1 
ATOM   2541 C CG1 . VAL B 1 36  ? 7.01589   -11.90090 8.91419   1.000 21.86222 ? 36  VAL B CG1 1 
ATOM   2542 C CG2 . VAL B 1 36  ? 6.05467   -12.86018 6.81460   1.000 24.64472 ? 36  VAL B CG2 1 
ATOM   2543 N N   . TYR B 1 37  ? 9.18356   -9.59952  7.86520   1.000 20.28327 ? 37  TYR B N   1 
ATOM   2544 C CA  . TYR B 1 37  ? 10.20516  -8.88034  8.61299   1.000 20.69652 ? 37  TYR B CA  1 
ATOM   2545 C C   . TYR B 1 37  ? 9.70908   -8.63763  10.03678  1.000 19.96726 ? 37  TYR B C   1 
ATOM   2546 O O   . TYR B 1 37  ? 8.55177   -8.25379  10.23264  1.000 23.65088 ? 37  TYR B O   1 
ATOM   2547 C CB  . TYR B 1 37  ? 10.53706  -7.53201  7.94641   1.000 19.34222 ? 37  TYR B CB  1 
ATOM   2548 C CG  . TYR B 1 37  ? 10.88214  -7.62850  6.46327   1.000 22.61650 ? 37  TYR B CG  1 
ATOM   2549 C CD1 . TYR B 1 37  ? 9.89580   -7.74279  5.50173   1.000 20.62630 ? 37  TYR B CD1 1 
ATOM   2550 C CD2 . TYR B 1 37  ? 12.20664  -7.58883  6.03895   1.000 25.03596 ? 37  TYR B CD2 1 
ATOM   2551 C CE1 . TYR B 1 37  ? 10.21124  -7.84038  4.15867   1.000 23.08642 ? 37  TYR B CE1 1 
ATOM   2552 C CE2 . TYR B 1 37  ? 12.52673  -7.68076  4.70450   1.000 22.21851 ? 37  TYR B CE2 1 
ATOM   2553 C CZ  . TYR B 1 37  ? 11.52977  -7.81209  3.77565   1.000 21.77940 ? 37  TYR B CZ  1 
ATOM   2554 O OH  . TYR B 1 37  ? 11.85653  -7.91297  2.44667   1.000 27.25325 ? 37  TYR B OH  1 
ATOM   2555 N N   . CYS B 1 38  ? 10.56711  -8.86300  11.03078  1.000 23.96173 ? 38  CYS B N   1 
ATOM   2556 C CA  . CYS B 1 38  ? 10.15016  -8.64704  12.41873  1.000 23.61245 ? 38  CYS B CA  1 
ATOM   2557 C C   . CYS B 1 38  ? 11.39414  -8.43970  13.28833  1.000 24.12670 ? 38  CYS B C   1 
ATOM   2558 O O   . CYS B 1 38  ? 12.51602  -8.73789  12.87116  1.000 22.37287 ? 38  CYS B O   1 
ATOM   2559 C CB  . CYS B 1 38  ? 9.31471   -9.83159  12.93805  1.000 24.72267 ? 38  CYS B CB  1 
ATOM   2560 S SG  . CYS B 1 38  ? 10.27606  -11.37008 13.30129  1.000 24.40859 ? 38  CYS B SG  1 
ATOM   2561 N N   . PRO B 1 39  ? 11.20827  -7.91848  14.50822  1.000 23.41940 ? 39  PRO B N   1 
ATOM   2562 C CA  . PRO B 1 39  ? 12.36400  -7.74555  15.41408  1.000 20.85830 ? 39  PRO B CA  1 
ATOM   2563 C C   . PRO B 1 39  ? 12.92349  -9.10072  15.82800  1.000 22.23483 ? 39  PRO B C   1 
ATOM   2564 O O   . PRO B 1 39  ? 12.17939  -10.02030 16.16926  1.000 23.62381 ? 39  PRO B O   1 
ATOM   2565 C CB  . PRO B 1 39  ? 11.76631  -6.98675  16.60962  1.000 21.72152 ? 39  PRO B CB  1 
ATOM   2566 C CG  . PRO B 1 39  ? 10.44461  -6.42424  16.10468  1.000 20.28638 ? 39  PRO B CG  1 
ATOM   2567 C CD  . PRO B 1 39  ? 9.95414   -7.44335  15.10744  1.000 19.65452 ? 39  PRO B CD  1 
ATOM   2568 N N   . ARG B 1 40  ? 14.25320  -9.22763  15.78238  1.000 24.74857 ? 40  ARG B N   1 
ATOM   2569 C CA  . ARG B 1 40  ? 14.88760  -10.49018 16.15011  1.000 23.24283 ? 40  ARG B CA  1 
ATOM   2570 C C   . ARG B 1 40  ? 14.64226  -10.87672 17.60910  1.000 25.87874 ? 40  ARG B C   1 
ATOM   2571 O O   . ARG B 1 40  ? 14.76443  -12.05694 17.94669  1.000 24.96563 ? 40  ARG B O   1 
ATOM   2572 C CB  . ARG B 1 40  ? 16.39474  -10.41778 15.86530  1.000 20.30657 ? 40  ARG B CB  1 
ATOM   2573 C CG  . ARG B 1 40  ? 17.15612  -9.40325  16.73049  1.000 23.64130 ? 40  ARG B CG  1 
ATOM   2574 C CD  . ARG B 1 40  ? 18.64441  -9.41920  16.40268  1.000 22.44598 ? 40  ARG B CD  1 
ATOM   2575 N NE  . ARG B 1 40  ? 19.37887  -8.41718  17.17260  1.000 24.46578 ? 40  ARG B NE  1 
ATOM   2576 C CZ  . ARG B 1 40  ? 20.70411  -8.31834  17.19888  1.000 26.24139 ? 40  ARG B CZ  1 
ATOM   2577 N NH1 . ARG B 1 40  ? 21.47326  -9.13004  16.49237  1.000 25.62073 ? 40  ARG B NH1 1 
ATOM   2578 N NH2 . ARG B 1 40  ? 21.27020  -7.38201  17.94983  1.000 25.48915 ? 40  ARG B NH2 1 
ATOM   2579 N N   . HIS B 1 41  ? 14.26587  -9.93910  18.48397  1.000 24.17914 ? 41  HIS B N   1 
ATOM   2580 C CA  . HIS B 1 41  ? 14.12467  -10.38561 19.87332  1.000 27.60842 ? 41  HIS B CA  1 
ATOM   2581 C C   . HIS B 1 41  ? 12.90584  -11.27684 20.09995  1.000 27.77523 ? 41  HIS B C   1 
ATOM   2582 O O   . HIS B 1 41  ? 12.70263  -11.76288 21.22157  1.000 25.81971 ? 41  HIS B O   1 
ATOM   2583 C CB  . HIS B 1 41  ? 14.13770  -9.18736  20.84154  1.000 24.56647 ? 41  HIS B CB  1 
ATOM   2584 C CG  . HIS B 1 41  ? 12.89030  -8.34752  20.86922  1.000 25.10432 ? 41  HIS B CG  1 
ATOM   2585 N ND1 . HIS B 1 41  ? 12.88687  -7.01421  20.51242  1.000 32.81684 ? 41  HIS B ND1 1 
ATOM   2586 C CD2 . HIS B 1 41  ? 11.64038  -8.61476  21.32295  1.000 27.85652 ? 41  HIS B CD2 1 
ATOM   2587 C CE1 . HIS B 1 41  ? 11.67797  -6.50864  20.70199  1.000 27.28868 ? 41  HIS B CE1 1 
ATOM   2588 N NE2 . HIS B 1 41  ? 10.90198  -7.46317  21.18792  1.000 29.28936 ? 41  HIS B NE2 1 
ATOM   2589 N N   . VAL B 1 42  ? 12.12092  -11.54613 19.05620  1.000 25.89001 ? 42  VAL B N   1 
ATOM   2590 C CA  . VAL B 1 42  ? 11.08712  -12.56178 19.14114  1.000 26.73042 ? 42  VAL B CA  1 
ATOM   2591 C C   . VAL B 1 42  ? 11.68139  -13.92091 19.49284  1.000 24.77455 ? 42  VAL B C   1 
ATOM   2592 O O   . VAL B 1 42  ? 10.96367  -14.80719 19.96302  1.000 23.86353 ? 42  VAL B O   1 
ATOM   2593 C CB  . VAL B 1 42  ? 10.30916  -12.62523 17.80610  1.000 25.00112 ? 42  VAL B CB  1 
ATOM   2594 C CG1 . VAL B 1 42  ? 11.20967  -13.17793 16.68640  1.000 20.02922 ? 42  VAL B CG1 1 
ATOM   2595 C CG2 . VAL B 1 42  ? 9.02127   -13.47019 17.93435  1.000 25.20535 ? 42  VAL B CG2 1 
ATOM   2596 N N   . ILE B 1 43  ? 12.97631  -14.12119 19.25601  1.000 20.43699 ? 43  ILE B N   1 
ATOM   2597 C CA  . ILE B 1 43  ? 13.57005  -15.43578 19.49088  1.000 23.21557 ? 43  ILE B CA  1 
ATOM   2598 C C   . ILE B 1 43  ? 14.05464  -15.54826 20.93899  1.000 29.71356 ? 43  ILE B C   1 
ATOM   2599 O O   . ILE B 1 43  ? 14.72498  -16.52620 21.29768  1.000 30.76126 ? 43  ILE B O   1 
ATOM   2600 C CB  . ILE B 1 43  ? 14.73429  -15.72021 18.51920  1.000 24.49464 ? 43  ILE B CB  1 
ATOM   2601 C CG1 . ILE B 1 43  ? 15.94595  -14.84052 18.87232  1.000 28.24624 ? 43  ILE B CG1 1 
ATOM   2602 C CG2 . ILE B 1 43  ? 14.29233  -15.59012 17.04706  1.000 27.65354 ? 43  ILE B CG2 1 
ATOM   2603 C CD1 . ILE B 1 43  ? 17.11790  -14.96034 17.89472  1.000 24.89735 ? 43  ILE B CD1 1 
ATOM   2604 N N   . CYS B 1 44  ? 13.70212  -14.57104 21.77999  1.000 30.65158 ? 44  CYS B N   1 
ATOM   2605 C CA  . CYS B 1 44  ? 14.19198  -14.46549 23.15421  1.000 30.68904 ? 44  CYS B CA  1 
ATOM   2606 C C   . CYS B 1 44  ? 13.12913  -14.86890 24.16800  1.000 30.88520 ? 44  CYS B C   1 
ATOM   2607 O O   . CYS B 1 44  ? 11.94971  -14.53758 24.01084  1.000 31.86148 ? 44  CYS B O   1 
ATOM   2608 C CB  . CYS B 1 44  ? 14.63022  -13.03184 23.47641  1.000 28.74118 ? 44  CYS B CB  1 
ATOM   2609 S SG  . CYS B 1 44  ? 16.16638  -12.50584 22.72946  1.000 30.93662 ? 44  CYS B SG  1 
ATOM   2610 N N   . THR B 1 45  ? 13.55572  -15.57847 25.21376  1.000 35.50575 ? 45  THR B N   1 
ATOM   2611 C CA  . THR B 1 45  ? 12.76963  -15.67899 26.43443  1.000 36.04403 ? 45  THR B CA  1 
ATOM   2612 C C   . THR B 1 45  ? 12.89002  -14.38241 27.23499  1.000 38.09411 ? 45  THR B C   1 
ATOM   2613 O O   . THR B 1 45  ? 13.67670  -13.49431 26.90623  1.000 41.88396 ? 45  THR B O   1 
ATOM   2614 C CB  . THR B 1 45  ? 13.24071  -16.84889 27.29682  1.000 38.81413 ? 45  THR B CB  1 
ATOM   2615 O OG1 . THR B 1 45  ? 14.52538  -16.54143 27.85627  1.000 39.41096 ? 45  THR B OG1 1 
ATOM   2616 C CG2 . THR B 1 45  ? 13.35663  -18.12368 26.47235  1.000 37.62712 ? 45  THR B CG2 1 
ATOM   2617 N N   . SER B 1 46  ? 12.11454  -14.29052 28.31999  1.000 42.83427 ? 46  SER B N   1 
ATOM   2618 C CA  . SER B 1 46  ? 12.23624  -13.15083 29.23121  1.000 37.51454 ? 46  SER B CA  1 
ATOM   2619 C C   . SER B 1 46  ? 13.65288  -13.01696 29.77129  1.000 42.53555 ? 46  SER B C   1 
ATOM   2620 O O   . SER B 1 46  ? 14.22617  -11.91985 29.77012  1.000 43.09370 ? 46  SER B O   1 
ATOM   2621 C CB  . SER B 1 46  ? 11.25220  -13.28371 30.39258  1.000 41.96343 ? 46  SER B CB  1 
ATOM   2622 O OG  . SER B 1 46  ? 9.91975   -13.20393 29.94213  1.000 56.43284 ? 46  SER B OG  1 
ATOM   2623 N N   . GLU B 1 47  ? 14.22269  -14.11608 30.28569  1.000 41.05882 ? 47  GLU B N   1 
ATOM   2624 C CA  . GLU B 1 47  ? 15.59541  -14.05562 30.78403  1.000 44.83222 ? 47  GLU B CA  1 
ATOM   2625 C C   . GLU B 1 47  ? 16.57996  -13.75621 29.66171  1.000 37.60080 ? 47  GLU B C   1 
ATOM   2626 O O   . GLU B 1 47  ? 17.56809  -13.04185 29.87443  1.000 34.90803 ? 47  GLU B O   1 
ATOM   2627 C CB  . GLU B 1 47  ? 15.98125  -15.36300 31.48429  1.000 44.48247 ? 47  GLU B CB  1 
ATOM   2628 C CG  . GLU B 1 47  ? 15.45509  -15.50497 32.90095  1.000 48.94238 ? 47  GLU B CG  1 
ATOM   2629 C CD  . GLU B 1 47  ? 16.09247  -14.52949 33.89036  1.000 40.69848 ? 47  GLU B CD  1 
ATOM   2630 O OE1 . GLU B 1 47  ? 17.33710  -14.37955 33.90778  1.000 37.52151 ? 47  GLU B OE1 1 
ATOM   2631 O OE2 . GLU B 1 47  ? 15.33019  -13.90529 34.65345  1.000 47.86593 ? 47  GLU B OE2 1 
ATOM   2632 N N   . ASP B 1 48  ? 16.34453  -14.31830 28.46535  1.000 36.02343 ? 48  ASP B N   1 
ATOM   2633 C CA  . ASP B 1 48  ? 17.23752  -14.06930 27.33438  1.000 33.85575 ? 48  ASP B CA  1 
ATOM   2634 C C   . ASP B 1 48  ? 17.41124  -12.57695 27.08268  1.000 34.74804 ? 48  ASP B C   1 
ATOM   2635 O O   . ASP B 1 48  ? 18.50995  -12.11151 26.76061  1.000 35.10413 ? 48  ASP B O   1 
ATOM   2636 C CB  . ASP B 1 48  ? 16.69854  -14.73709 26.06364  1.000 36.36796 ? 48  ASP B CB  1 
ATOM   2637 C CG  . ASP B 1 48  ? 16.86631  -16.24801 26.06365  1.000 44.01642 ? 48  ASP B CG  1 
ATOM   2638 O OD1 . ASP B 1 48  ? 17.88130  -16.74486 26.60236  1.000 44.17337 ? 48  ASP B OD1 1 
ATOM   2639 O OD2 . ASP B 1 48  ? 15.98677  -16.93227 25.49639  1.000 44.28314 ? 48  ASP B OD2 1 
ATOM   2640 N N   . MET B 1 49  ? 16.32812  -11.81371 27.20680  1.000 32.95682 ? 49  MET B N   1 
ATOM   2641 C CA  . MET B 1 49  ? 16.38219  -10.40459 26.85537  1.000 30.03792 ? 49  MET B CA  1 
ATOM   2642 C C   . MET B 1 49  ? 17.31768  -9.62731  27.76938  1.000 34.08257 ? 49  MET B C   1 
ATOM   2643 O O   . MET B 1 49  ? 17.85899  -8.59440  27.35341  1.000 32.41326 ? 49  MET B O   1 
ATOM   2644 C CB  . MET B 1 49  ? 14.96374  -9.83239  26.87948  1.000 35.29954 ? 49  MET B CB  1 
ATOM   2645 C CG  . MET B 1 49  ? 14.07145  -10.48278 25.81763  1.000 35.34585 ? 49  MET B CG  1 
ATOM   2646 S SD  . MET B 1 49  ? 12.32465  -10.06288 25.98964  1.000 47.82120 ? 49  MET B SD  1 
ATOM   2647 C CE  . MET B 1 49  ? 11.57512  -11.29103 24.92851  1.000 41.99679 ? 49  MET B CE  1 
ATOM   2648 N N   . LEU B 1 50  ? 17.55339  -10.11152 28.99497  1.000 29.61525 ? 50  LEU B N   1 
ATOM   2649 C CA  . LEU B 1 50  ? 18.42446  -9.36852  29.90140  1.000 30.28783 ? 50  LEU B CA  1 
ATOM   2650 C C   . LEU B 1 50  ? 19.85861  -9.30200  29.38223  1.000 32.46525 ? 50  LEU B C   1 
ATOM   2651 O O   . LEU B 1 50  ? 20.58647  -8.35958  29.71073  1.000 36.84252 ? 50  LEU B O   1 
ATOM   2652 C CB  . LEU B 1 50  ? 18.38496  -9.98449  31.30534  1.000 32.84292 ? 50  LEU B CB  1 
ATOM   2653 N N   . ASN B 1 51  ? 20.27884  -10.27460 28.56559  1.000 35.63010 ? 51  ASN B N   1 
ATOM   2654 C CA  . ASN B 1 51  ? 21.66074  -10.35325 28.09305  1.000 35.38639 ? 51  ASN B CA  1 
ATOM   2655 C C   . ASN B 1 51  ? 21.76973  -11.33051 26.92761  1.000 41.94250 ? 51  ASN B C   1 
ATOM   2656 O O   . ASN B 1 51  ? 22.38586  -12.39819 27.06794  1.000 38.92525 ? 51  ASN B O   1 
ATOM   2657 C CB  . ASN B 1 51  ? 22.58730  -10.78019 29.23725  1.000 41.53850 ? 51  ASN B CB  1 
ATOM   2658 C CG  . ASN B 1 51  ? 24.05002  -10.78937 28.83751  1.000 43.02236 ? 51  ASN B CG  1 
ATOM   2659 O OD1 . ASN B 1 51  ? 24.44551  -10.15609 27.85334  1.000 37.26729 ? 51  ASN B OD1 1 
ATOM   2660 N ND2 . ASN B 1 51  ? 24.86704  -11.51166 29.60427  1.000 41.71674 ? 51  ASN B ND2 1 
ATOM   2661 N N   . PRO B 1 52  ? 21.20371  -11.00323 25.76644  1.000 36.89577 ? 52  PRO B N   1 
ATOM   2662 C CA  . PRO B 1 52  ? 21.03751  -12.01181 24.71444  1.000 42.19826 ? 52  PRO B CA  1 
ATOM   2663 C C   . PRO B 1 52  ? 22.27431  -12.18594 23.85283  1.000 40.65729 ? 52  PRO B C   1 
ATOM   2664 O O   . PRO B 1 52  ? 23.03785  -11.24925 23.60945  1.000 39.98281 ? 52  PRO B O   1 
ATOM   2665 C CB  . PRO B 1 52  ? 19.87967  -11.45346 23.88108  1.000 34.57156 ? 52  PRO B CB  1 
ATOM   2666 C CG  . PRO B 1 52  ? 20.07936  -9.97337  23.97599  1.000 33.44166 ? 52  PRO B CG  1 
ATOM   2667 C CD  . PRO B 1 52  ? 20.59867  -9.71252  25.38947  1.000 33.91084 ? 52  PRO B CD  1 
ATOM   2668 N N   . ASN B 1 53  ? 22.45187  -13.41861 23.38621  1.000 33.64543 ? 53  ASN B N   1 
ATOM   2669 C CA  . ASN B 1 53  ? 23.43997  -13.77898 22.37111  1.000 35.69987 ? 53  ASN B CA  1 
ATOM   2670 C C   . ASN B 1 53  ? 22.64060  -14.19266 21.13620  1.000 39.35562 ? 53  ASN B C   1 
ATOM   2671 O O   . ASN B 1 53  ? 22.28016  -15.36110 20.96895  1.000 36.25477 ? 53  ASN B O   1 
ATOM   2672 C CB  . ASN B 1 53  ? 24.35631  -14.90422 22.86509  1.000 41.29198 ? 53  ASN B CB  1 
ATOM   2673 C CG  . ASN B 1 53  ? 25.39272  -15.32046 21.83256  1.000 42.47613 ? 53  ASN B CG  1 
ATOM   2674 O OD1 . ASN B 1 53  ? 25.31478  -14.95359 20.65710  1.000 36.80223 ? 53  ASN B OD1 1 
ATOM   2675 N ND2 . ASN B 1 53  ? 26.36722  -16.10816 22.27195  1.000 50.54069 ? 53  ASN B ND2 1 
ATOM   2676 N N   . TYR B 1 54  ? 22.34702  -13.21917 20.27326  1.000 35.35947 ? 54  TYR B N   1 
ATOM   2677 C CA  . TYR B 1 54  ? 21.43689  -13.48875 19.16485  1.000 33.24454 ? 54  TYR B CA  1 
ATOM   2678 C C   . TYR B 1 54  ? 22.02029  -14.50079 18.18701  1.000 40.08932 ? 54  TYR B C   1 
ATOM   2679 O O   . TYR B 1 54  ? 21.28859  -15.34647 17.66105  1.000 36.17980 ? 54  TYR B O   1 
ATOM   2680 C CB  . TYR B 1 54  ? 21.06968  -12.19064 18.44643  1.000 32.42798 ? 54  TYR B CB  1 
ATOM   2681 C CG  . TYR B 1 54  ? 20.09825  -11.33049 19.23218  1.000 28.88497 ? 54  TYR B CG  1 
ATOM   2682 C CD1 . TYR B 1 54  ? 18.75868  -11.68394 19.33286  1.000 26.26113 ? 54  TYR B CD1 1 
ATOM   2683 C CD2 . TYR B 1 54  ? 20.52179  -10.17405 19.87340  1.000 26.58661 ? 54  TYR B CD2 1 
ATOM   2684 C CE1 . TYR B 1 54  ? 17.86763  -10.89942 20.04658  1.000 29.03379 ? 54  TYR B CE1 1 
ATOM   2685 C CE2 . TYR B 1 54  ? 19.64009  -9.37801  20.58861  1.000 28.18379 ? 54  TYR B CE2 1 
ATOM   2686 C CZ  . TYR B 1 54  ? 18.31537  -9.74876  20.67291  1.000 30.42928 ? 54  TYR B CZ  1 
ATOM   2687 O OH  . TYR B 1 54  ? 17.42244  -8.96975  21.37426  1.000 25.39071 ? 54  TYR B OH  1 
ATOM   2688 N N   . GLU B 1 55  ? 23.32445  -14.42780 17.91358  1.000 38.18116 ? 55  GLU B N   1 
ATOM   2689 C CA  . GLU B 1 55  ? 23.91413  -15.37743 16.97407  1.000 39.35367 ? 55  GLU B CA  1 
ATOM   2690 C C   . GLU B 1 55  ? 23.72496  -16.80689 17.46004  1.000 36.29145 ? 55  GLU B C   1 
ATOM   2691 O O   . GLU B 1 55  ? 23.40380  -17.70507 16.67373  1.000 34.57067 ? 55  GLU B O   1 
ATOM   2692 C CB  . GLU B 1 55  ? 25.40133  -15.07465 16.76197  1.000 38.97806 ? 55  GLU B CB  1 
ATOM   2693 C CG  . GLU B 1 55  ? 25.67788  -13.87911 15.84309  1.000 49.31861 ? 55  GLU B CG  1 
ATOM   2694 C CD  . GLU B 1 55  ? 25.30898  -12.54317 16.47545  1.000 55.12622 ? 55  GLU B CD  1 
ATOM   2695 O OE1 . GLU B 1 55  ? 25.26615  -12.45788 17.72731  1.000 56.96862 ? 55  GLU B OE1 1 
ATOM   2696 O OE2 . GLU B 1 55  ? 25.05808  -11.57800 15.71835  1.000 57.56781 ? 55  GLU B OE2 1 
ATOM   2697 N N   . ASP B 1 56  ? 23.91602  -17.03134 18.75660  1.000 38.72655 ? 56  ASP B N   1 
ATOM   2698 C CA  . ASP B 1 56  ? 23.77557  -18.37083 19.31091  1.000 45.03358 ? 56  ASP B CA  1 
ATOM   2699 C C   . ASP B 1 56  ? 22.31447  -18.78322 19.41276  1.000 44.18026 ? 56  ASP B C   1 
ATOM   2700 O O   . ASP B 1 56  ? 21.99361  -19.96842 19.27723  1.000 39.56727 ? 56  ASP B O   1 
ATOM   2701 C CB  . ASP B 1 56  ? 24.44716  -18.43025 20.68148  1.000 38.39192 ? 56  ASP B CB  1 
ATOM   2702 C CG  . ASP B 1 56  ? 24.22048  -19.74920 21.38392  1.000 48.91703 ? 56  ASP B CG  1 
ATOM   2703 O OD1 . ASP B 1 56  ? 23.06040  -20.04489 21.73512  1.000 56.81856 ? 56  ASP B OD1 1 
ATOM   2704 O OD2 . ASP B 1 56  ? 25.20323  -20.49498 21.58243  1.000 66.81364 ? 56  ASP B OD2 1 
ATOM   2705 N N   . LEU B 1 57  ? 21.41683  -17.83086 19.65874  1.000 34.84100 ? 57  LEU B N   1 
ATOM   2706 C CA  . LEU B 1 57  ? 20.00744  -18.18474 19.74662  1.000 34.63245 ? 57  LEU B CA  1 
ATOM   2707 C C   . LEU B 1 57  ? 19.46197  -18.57893 18.37857  1.000 32.89061 ? 57  LEU B C   1 
ATOM   2708 O O   . LEU B 1 57  ? 18.63825  -19.49621 18.27291  1.000 39.00187 ? 57  LEU B O   1 
ATOM   2709 C CB  . LEU B 1 57  ? 19.21600  -17.02228 20.34286  1.000 31.34998 ? 57  LEU B CB  1 
ATOM   2710 C CG  . LEU B 1 57  ? 19.35006  -16.72221 21.83849  1.000 39.56117 ? 57  LEU B CG  1 
ATOM   2711 C CD1 . LEU B 1 57  ? 18.79034  -15.33227 22.18170  1.000 31.45910 ? 57  LEU B CD1 1 
ATOM   2712 C CD2 . LEU B 1 57  ? 18.65646  -17.78631 22.66394  1.000 35.01422 ? 57  LEU B CD2 1 
ATOM   2713 N N   . LEU B 1 58  ? 19.92931  -17.91784 17.31372  1.000 33.11865 ? 58  LEU B N   1 
ATOM   2714 C CA  . LEU B 1 58  ? 19.44354  -18.25136 15.97973  1.000 35.57346 ? 58  LEU B CA  1 
ATOM   2715 C C   . LEU B 1 58  ? 20.04654  -19.54713 15.45284  1.000 37.76818 ? 58  LEU B C   1 
ATOM   2716 O O   . LEU B 1 58  ? 19.37750  -20.26918 14.70588  1.000 34.05256 ? 58  LEU B O   1 
ATOM   2717 C CB  . LEU B 1 58  ? 19.72410  -17.10350 15.00240  1.000 34.33069 ? 58  LEU B CB  1 
ATOM   2718 C CG  . LEU B 1 58  ? 18.92204  -17.16807 13.69285  1.000 40.88939 ? 58  LEU B CG  1 
ATOM   2719 C CD1 . LEU B 1 58  ? 17.43745  -16.92290 13.94290  1.000 36.48155 ? 58  LEU B CD1 1 
ATOM   2720 C CD2 . LEU B 1 58  ? 19.45599  -16.19095 12.65743  1.000 37.79798 ? 58  LEU B CD2 1 
ATOM   2721 N N   . ILE B 1 59  ? 21.29583  -19.85663 15.81995  1.000 39.95287 ? 59  ILE B N   1 
ATOM   2722 C CA  . ILE B 1 59  ? 21.92843  -21.08804 15.35005  1.000 42.44191 ? 59  ILE B CA  1 
ATOM   2723 C C   . ILE B 1 59  ? 21.09968  -22.29931 15.75518  1.000 39.36933 ? 59  ILE B C   1 
ATOM   2724 O O   . ILE B 1 59  ? 20.98521  -23.27324 15.00208  1.000 44.77872 ? 59  ILE B O   1 
ATOM   2725 C CB  . ILE B 1 59  ? 23.37248  -21.18991 15.88352  1.000 40.47028 ? 59  ILE B CB  1 
ATOM   2726 N N   . ARG B 1 60  ? 20.50729  -22.25624 16.94532  1.000 36.22295 ? 60  ARG B N   1 
ATOM   2727 C CA  . ARG B 1 60  ? 19.69099  -23.35625 17.44047  1.000 38.10252 ? 60  ARG B CA  1 
ATOM   2728 C C   . ARG B 1 60  ? 18.29298  -23.38437 16.81943  1.000 43.40409 ? 60  ARG B C   1 
ATOM   2729 O O   . ARG B 1 60  ? 17.61750  -24.42098 16.87873  1.000 41.19724 ? 60  ARG B O   1 
ATOM   2730 C CB  . ARG B 1 60  ? 19.59095  -23.27192 18.96691  1.000 41.55198 ? 60  ARG B CB  1 
ATOM   2731 N N   . LYS B 1 61  ? 17.85405  -22.28130 16.22642  1.000 35.13736 ? 61  LYS B N   1 
ATOM   2732 C CA  . LYS B 1 61  ? 16.53784  -22.18582 15.61266  1.000 35.51137 ? 61  LYS B CA  1 
ATOM   2733 C C   . LYS B 1 61  ? 16.51916  -22.87202 14.25054  1.000 34.02878 ? 61  LYS B C   1 
ATOM   2734 O O   . LYS B 1 61  ? 17.51030  -22.86161 13.51537  1.000 33.67760 ? 61  LYS B O   1 
ATOM   2735 C CB  . LYS B 1 61  ? 16.14876  -20.71427 15.43047  1.000 33.68348 ? 61  LYS B CB  1 
ATOM   2736 C CG  . LYS B 1 61  ? 15.70467  -19.99119 16.68753  1.000 34.86188 ? 61  LYS B CG  1 
ATOM   2737 C CD  . LYS B 1 61  ? 14.32987  -20.46511 17.10815  1.000 45.50892 ? 61  LYS B CD  1 
ATOM   2738 C CE  . LYS B 1 61  ? 13.46983  -19.32547 17.58981  1.000 29.74652 ? 61  LYS B CE  1 
ATOM   2739 N NZ  . LYS B 1 61  ? 12.05639  -19.77501 17.80477  1.000 37.54530 ? 61  LYS B NZ  1 
ATOM   2740 N N   . SER B 1 62  ? 15.36849  -23.45347 13.90999  1.000 27.51208 ? 62  SER B N   1 
ATOM   2741 C CA  . SER B 1 62  ? 15.09385  -23.95591 12.57373  1.000 25.10169 ? 62  SER B CA  1 
ATOM   2742 C C   . SER B 1 62  ? 13.84791  -23.28289 12.01285  1.000 29.98270 ? 62  SER B C   1 
ATOM   2743 O O   . SER B 1 62  ? 13.05476  -22.67811 12.74438  1.000 26.00756 ? 62  SER B O   1 
ATOM   2744 C CB  . SER B 1 62  ? 14.88219  -25.48635 12.56804  1.000 27.61102 ? 62  SER B CB  1 
ATOM   2745 O OG  . SER B 1 62  ? 15.95720  -26.16032 13.19334  1.000 34.59832 ? 62  SER B OG  1 
ATOM   2746 N N   . ASN B 1 63  ? 13.67632  -23.42637 10.69797  1.000 22.76293 ? 63  ASN B N   1 
ATOM   2747 C CA  . ASN B 1 63  ? 12.46649  -22.93691 10.04733  1.000 28.88219 ? 63  ASN B CA  1 
ATOM   2748 C C   . ASN B 1 63  ? 11.21774  -23.36520 10.80252  1.000 32.44305 ? 63  ASN B C   1 
ATOM   2749 O O   . ASN B 1 63  ? 10.28428  -22.57238 10.96311  1.000 28.55748 ? 63  ASN B O   1 
ATOM   2750 C CB  . ASN B 1 63  ? 12.37724  -23.43951 8.60320   1.000 30.91879 ? 63  ASN B CB  1 
ATOM   2751 C CG  . ASN B 1 63  ? 13.34546  -22.74051 7.66612   1.000 34.25957 ? 63  ASN B CG  1 
ATOM   2752 O OD1 . ASN B 1 63  ? 13.76628  -21.59566 7.89853   1.000 30.82594 ? 63  ASN B OD1 1 
ATOM   2753 N ND2 . ASN B 1 63  ? 13.68295  -23.42239 6.57340   1.000 28.66575 ? 63  ASN B ND2 1 
ATOM   2754 N N   . HIS B 1 64  ? 11.16786  -24.61932 11.25746  1.000 27.88398 ? 64  HIS B N   1 
ATOM   2755 C CA  . HIS B 1 64  ? 9.91449   -25.13120 11.79912  1.000 32.73654 ? 64  HIS B CA  1 
ATOM   2756 C C   . HIS B 1 64  ? 9.62655   -24.63868 13.20593  1.000 31.57180 ? 64  HIS B C   1 
ATOM   2757 O O   . HIS B 1 64  ? 8.56056   -24.96291 13.74145  1.000 35.42519 ? 64  HIS B O   1 
ATOM   2758 C CB  . HIS B 1 64  ? 9.87961   -26.66854 11.76231  1.000 36.05449 ? 64  HIS B CB  1 
ATOM   2759 C CG  . HIS B 1 64  ? 11.01330  -27.32451 12.47952  1.000 36.52233 ? 64  HIS B CG  1 
ATOM   2760 N ND1 . HIS B 1 64  ? 11.03198  -27.49457 13.84673  1.000 47.67504 ? 64  HIS B ND1 1 
ATOM   2761 C CD2 . HIS B 1 64  ? 12.16534  -27.86403 12.01705  1.000 38.57798 ? 64  HIS B CD2 1 
ATOM   2762 C CE1 . HIS B 1 64  ? 12.15107  -28.10354 14.19679  1.000 41.99991 ? 64  HIS B CE1 1 
ATOM   2763 N NE2 . HIS B 1 64  ? 12.85874  -28.33353 13.10469  1.000 43.54164 ? 64  HIS B NE2 1 
ATOM   2764 N N   . ASN B 1 65  ? 10.51958  -23.84880 13.80399  1.000 25.63133 ? 65  ASN B N   1 
ATOM   2765 C CA  . ASN B 1 65  ? 10.24278  -23.23025 15.09388  1.000 28.72770 ? 65  ASN B CA  1 
ATOM   2766 C C   . ASN B 1 65  ? 9.45650   -21.91717 15.00251  1.000 25.06382 ? 65  ASN B C   1 
ATOM   2767 O O   . ASN B 1 65  ? 8.99345   -21.43549 16.04078  1.000 27.06321 ? 65  ASN B O   1 
ATOM   2768 C CB  . ASN B 1 65  ? 11.54743  -22.96184 15.84051  1.000 27.21429 ? 65  ASN B CB  1 
ATOM   2769 C CG  . ASN B 1 65  ? 12.25491  -24.23310 16.23998  1.000 36.75005 ? 65  ASN B CG  1 
ATOM   2770 O OD1 . ASN B 1 65  ? 13.46763  -24.36639 16.05822  1.000 30.38871 ? 65  ASN B OD1 1 
ATOM   2771 N ND2 . ASN B 1 65  ? 11.49664  -25.18619 16.76930  1.000 33.03714 ? 65  ASN B ND2 1 
ATOM   2772 N N   . PHE B 1 66  ? 9.31089   -21.31446 13.81732  1.000 27.54484 ? 66  PHE B N   1 
ATOM   2773 C CA  . PHE B 1 66  ? 8.67591   -20.00043 13.67221  1.000 22.55804 ? 66  PHE B CA  1 
ATOM   2774 C C   . PHE B 1 66  ? 7.21862   -20.17563 13.25917  1.000 22.09700 ? 66  PHE B C   1 
ATOM   2775 O O   . PHE B 1 66  ? 6.93693   -20.79978 12.23631  1.000 27.53255 ? 66  PHE B O   1 
ATOM   2776 C CB  . PHE B 1 66  ? 9.38884   -19.13887 12.62654  1.000 22.70220 ? 66  PHE B CB  1 
ATOM   2777 C CG  . PHE B 1 66  ? 10.78096  -18.72855 13.00623  1.000 21.57931 ? 66  PHE B CG  1 
ATOM   2778 C CD1 . PHE B 1 66  ? 10.99435  -17.61994 13.81487  1.000 24.38917 ? 66  PHE B CD1 1 
ATOM   2779 C CD2 . PHE B 1 66  ? 11.87567  -19.43804 12.53751  1.000 24.79646 ? 66  PHE B CD2 1 
ATOM   2780 C CE1 . PHE B 1 66  ? 12.27264  -17.23217 14.15353  1.000 25.14657 ? 66  PHE B CE1 1 
ATOM   2781 C CE2 . PHE B 1 66  ? 13.15823  -19.06140 12.87403  1.000 24.10144 ? 66  PHE B CE2 1 
ATOM   2782 C CZ  . PHE B 1 66  ? 13.36072  -17.95810 13.68511  1.000 23.84335 ? 66  PHE B CZ  1 
ATOM   2783 N N   . LEU B 1 67  ? 6.30567   -19.59086 14.02888  1.000 20.38261 ? 67  LEU B N   1 
ATOM   2784 C CA  . LEU B 1 67  ? 4.87923   -19.62184 13.73482  1.000 19.99935 ? 67  LEU B CA  1 
ATOM   2785 C C   . LEU B 1 67  ? 4.49966   -18.24970 13.18928  1.000 20.93696 ? 67  LEU B C   1 
ATOM   2786 O O   . LEU B 1 67  ? 4.55935   -17.25122 13.91272  1.000 23.97247 ? 67  LEU B O   1 
ATOM   2787 C CB  . LEU B 1 67  ? 4.06423   -19.95892 14.98616  1.000 24.65378 ? 67  LEU B CB  1 
ATOM   2788 C CG  . LEU B 1 67  ? 2.53212   -19.80118 14.85756  1.000 22.13929 ? 67  LEU B CG  1 
ATOM   2789 C CD1 . LEU B 1 67  ? 1.93125   -20.68701 13.76606  1.000 22.75610 ? 67  LEU B CD1 1 
ATOM   2790 C CD2 . LEU B 1 67  ? 1.84982   -20.08116 16.20882  1.000 22.06586 ? 67  LEU B CD2 1 
ATOM   2791 N N   . VAL B 1 68  ? 4.09396   -18.20315 11.92332  1.000 22.20597 ? 68  VAL B N   1 
ATOM   2792 C CA  . VAL B 1 68  ? 3.67640   -16.96233 11.28412  1.000 22.46360 ? 68  VAL B CA  1 
ATOM   2793 C C   . VAL B 1 68  ? 2.21396   -17.10748 10.88706  1.000 20.23134 ? 68  VAL B C   1 
ATOM   2794 O O   . VAL B 1 68  ? 1.83934   -18.08794 10.23405  1.000 25.08808 ? 68  VAL B O   1 
ATOM   2795 C CB  . VAL B 1 68  ? 4.56462   -16.63152 10.07179  1.000 20.97371 ? 68  VAL B CB  1 
ATOM   2796 C CG1 . VAL B 1 68  ? 4.01628   -15.41964 9.34201   1.000 22.87075 ? 68  VAL B CG1 1 
ATOM   2797 C CG2 . VAL B 1 68  ? 6.00212   -16.36512 10.54378  1.000 22.54264 ? 68  VAL B CG2 1 
ATOM   2798 N N   . GLN B 1 69  ? 1.38629   -16.15136 11.30085  1.000 21.49494 ? 69  GLN B N   1 
ATOM   2799 C CA  . GLN B 1 69  ? -0.04671  -16.21733 11.04071  1.000 22.58411 ? 69  GLN B CA  1 
ATOM   2800 C C   . GLN B 1 69  ? -0.54839  -14.88677 10.50284  1.000 27.05855 ? 69  GLN B C   1 
ATOM   2801 O O   . GLN B 1 69  ? -0.24017  -13.82504 11.06037  1.000 25.05478 ? 69  GLN B O   1 
ATOM   2802 C CB  . GLN B 1 69  ? -0.82521  -16.59155 12.30555  1.000 22.20548 ? 69  GLN B CB  1 
ATOM   2803 C CG  . GLN B 1 69  ? -0.32318  -17.87351 12.97269  1.000 24.91264 ? 69  GLN B CG  1 
ATOM   2804 C CD  . GLN B 1 69  ? -0.88741  -18.04781 14.36590  1.000 30.07406 ? 69  GLN B CD  1 
ATOM   2805 O OE1 . GLN B 1 69  ? -0.49050  -17.34307 15.30744  1.000 29.15790 ? 69  GLN B OE1 1 
ATOM   2806 N NE2 . GLN B 1 69  ? -1.83220  -18.98026 14.50676  1.000 29.13803 ? 69  GLN B NE2 1 
ATOM   2807 N N   . ALA B 1 70  ? -1.31107  -14.95046 9.41780   1.000 26.68736 ? 70  ALA B N   1 
ATOM   2808 C CA  . ALA B 1 70  ? -2.13158  -13.83820 8.95422   1.000 32.50601 ? 70  ALA B CA  1 
ATOM   2809 C C   . ALA B 1 70  ? -3.54855  -14.14434 9.42567   1.000 32.41566 ? 70  ALA B C   1 
ATOM   2810 O O   . ALA B 1 70  ? -4.17163  -15.09762 8.95578   1.000 32.95136 ? 70  ALA B O   1 
ATOM   2811 C CB  . ALA B 1 70  ? -2.05979  -13.68270 7.43927   1.000 29.50703 ? 70  ALA B CB  1 
ATOM   2812 N N   . GLY B 1 71  ? -4.03492  -13.37784 10.38721  1.000 37.45847 ? 71  GLY B N   1 
ATOM   2813 C CA  . GLY B 1 71  ? -5.22636  -13.82246 11.08520  1.000 36.29633 ? 71  GLY B CA  1 
ATOM   2814 C C   . GLY B 1 71  ? -4.91975  -15.13610 11.76734  1.000 34.94856 ? 71  GLY B C   1 
ATOM   2815 O O   . GLY B 1 71  ? -3.92994  -15.26763 12.49439  1.000 46.87269 ? 71  GLY B O   1 
ATOM   2816 N N   . ASN B 1 72  ? -5.76284  -16.13510 11.53581  1.000 39.45935 ? 72  ASN B N   1 
ATOM   2817 C CA  . ASN B 1 72  ? -5.50717  -17.48030 12.02439  1.000 37.96793 ? 72  ASN B CA  1 
ATOM   2818 C C   . ASN B 1 72  ? -4.97764  -18.40716 10.93894  1.000 43.28959 ? 72  ASN B C   1 
ATOM   2819 O O   . ASN B 1 72  ? -4.88045  -19.62331 11.16308  1.000 38.83567 ? 72  ASN B O   1 
ATOM   2820 C CB  . ASN B 1 72  ? -6.77341  -18.06033 12.65018  1.000 53.05205 ? 72  ASN B CB  1 
ATOM   2821 C CG  . ASN B 1 72  ? -7.00007  -17.54826 14.05260  1.000 50.21432 ? 72  ASN B CG  1 
ATOM   2822 O OD1 . ASN B 1 72  ? -6.04265  -17.29893 14.79519  1.000 54.21021 ? 72  ASN B OD1 1 
ATOM   2823 N ND2 . ASN B 1 72  ? -8.26251  -17.38130 14.42621  1.000 54.42959 ? 72  ASN B ND2 1 
ATOM   2824 N N   . VAL B 1 73  ? -4.62476  -17.86537 9.77578   1.000 31.56778 ? 73  VAL B N   1 
ATOM   2825 C CA  . VAL B 1 73  ? -4.03853  -18.66026 8.70697   1.000 28.54204 ? 73  VAL B CA  1 
ATOM   2826 C C   . VAL B 1 73  ? -2.52867  -18.68859 8.90366   1.000 28.08528 ? 73  VAL B C   1 
ATOM   2827 O O   . VAL B 1 73  ? -1.88173  -17.64004 8.94758   1.000 26.68039 ? 73  VAL B O   1 
ATOM   2828 C CB  . VAL B 1 73  ? -4.40773  -18.09769 7.32890   1.000 34.20568 ? 73  VAL B CB  1 
ATOM   2829 C CG1 . VAL B 1 73  ? -3.75814  -18.93177 6.24074   1.000 35.71147 ? 73  VAL B CG1 1 
ATOM   2830 C CG2 . VAL B 1 73  ? -5.91212  -18.07821 7.17157   1.000 31.19493 ? 73  VAL B CG2 1 
ATOM   2831 N N   . GLN B 1 74  ? -1.96474  -19.88313 9.01896   1.000 24.78710 ? 74  GLN B N   1 
ATOM   2832 C CA  . GLN B 1 74  ? -0.52101  -20.00870 9.18353   1.000 25.80257 ? 74  GLN B CA  1 
ATOM   2833 C C   . GLN B 1 74  ? 0.18745   -19.88832 7.84224   1.000 30.46148 ? 74  GLN B C   1 
ATOM   2834 O O   . GLN B 1 74  ? -0.26382  -20.44219 6.83897   1.000 29.99773 ? 74  GLN B O   1 
ATOM   2835 C CB  . GLN B 1 74  ? -0.15790  -21.35062 9.82090   1.000 26.04249 ? 74  GLN B CB  1 
ATOM   2836 C CG  . GLN B 1 74  ? 1.35884   -21.59734 9.90409   1.000 28.38560 ? 74  GLN B CG  1 
ATOM   2837 C CD  . GLN B 1 74  ? 1.71351   -22.92827 10.57043  1.000 33.77455 ? 74  GLN B CD  1 
ATOM   2838 O OE1 . GLN B 1 74  ? 0.83305   -23.70121 10.93692  1.000 35.59765 ? 74  GLN B OE1 1 
ATOM   2839 N NE2 . GLN B 1 74  ? 3.00661   -23.19730 10.71693  1.000 29.41737 ? 74  GLN B NE2 1 
ATOM   2840 N N   . LEU B 1 75  ? 1.33073   -19.20983 7.84473   1.000 24.34517 ? 75  LEU B N   1 
ATOM   2841 C CA  . LEU B 1 75  ? 2.21845   -19.12778 6.68895   1.000 26.57203 ? 75  LEU B CA  1 
ATOM   2842 C C   . LEU B 1 75  ? 3.48253   -19.91272 7.01933   1.000 27.27679 ? 75  LEU B C   1 
ATOM   2843 O O   . LEU B 1 75  ? 4.17610   -19.59392 7.98695   1.000 28.77568 ? 75  LEU B O   1 
ATOM   2844 C CB  . LEU B 1 75  ? 2.57209   -17.67423 6.35093   1.000 25.56933 ? 75  LEU B CB  1 
ATOM   2845 C CG  . LEU B 1 75  ? 1.44191   -16.65943 6.17177   1.000 29.21028 ? 75  LEU B CG  1 
ATOM   2846 C CD1 . LEU B 1 75  ? 2.01324   -15.28857 5.80972   1.000 25.75197 ? 75  LEU B CD1 1 
ATOM   2847 C CD2 . LEU B 1 75  ? 0.47322   -17.12698 5.10281   1.000 29.35045 ? 75  LEU B CD2 1 
ATOM   2848 N N   . ARG B 1 76  ? 3.78637   -20.92380 6.21840   1.000 30.37692 ? 76  ARG B N   1 
ATOM   2849 C CA  . ARG B 1 76  ? 4.92396   -21.77787 6.52007   1.000 32.98374 ? 76  ARG B CA  1 
ATOM   2850 C C   . ARG B 1 76  ? 6.22174   -21.04214 6.21302   1.000 28.26824 ? 76  ARG B C   1 
ATOM   2851 O O   . ARG B 1 76  ? 6.38424   -20.47503 5.12751   1.000 30.75203 ? 76  ARG B O   1 
ATOM   2852 C CB  . ARG B 1 76  ? 4.84940   -23.07404 5.71455   1.000 35.13413 ? 76  ARG B CB  1 
ATOM   2853 C CG  . ARG B 1 76  ? 5.39451   -24.27733 6.44353   1.000 43.70265 ? 76  ARG B CG  1 
ATOM   2854 C CD  . ARG B 1 76  ? 4.37445   -24.75361 7.47156   1.000 48.85169 ? 76  ARG B CD  1 
ATOM   2855 N NE  . ARG B 1 76  ? 3.11656   -25.12253 6.83268   1.000 55.70697 ? 76  ARG B NE  1 
ATOM   2856 C CZ  . ARG B 1 76  ? 2.65813   -26.36326 6.73414   1.000 49.99552 ? 76  ARG B CZ  1 
ATOM   2857 N NH1 . ARG B 1 76  ? 3.30848   -27.38331 7.26878   1.000 53.23837 ? 76  ARG B NH1 1 
ATOM   2858 N NH2 . ARG B 1 76  ? 1.51384   -26.58478 6.08823   1.000 54.78906 ? 76  ARG B NH2 1 
ATOM   2859 N N   . VAL B 1 77  ? 7.13213   -21.05267 7.17782   1.000 26.21010 ? 77  VAL B N   1 
ATOM   2860 C CA  . VAL B 1 77  ? 8.46909   -20.49151 7.01180   1.000 29.21881 ? 77  VAL B CA  1 
ATOM   2861 C C   . VAL B 1 77  ? 9.35011   -21.50616 6.29601   1.000 31.07201 ? 77  VAL B C   1 
ATOM   2862 O O   . VAL B 1 77  ? 9.46756   -22.65936 6.72808   1.000 24.13023 ? 77  VAL B O   1 
ATOM   2863 C CB  . VAL B 1 77  ? 9.06816   -20.11174 8.37629   1.000 28.42339 ? 77  VAL B CB  1 
ATOM   2864 C CG1 . VAL B 1 77  ? 10.54114  -19.70915 8.24021   1.000 25.79811 ? 77  VAL B CG1 1 
ATOM   2865 C CG2 . VAL B 1 77  ? 8.25310   -18.99899 9.02272   1.000 25.55035 ? 77  VAL B CG2 1 
ATOM   2866 N N   . ILE B 1 78  ? 10.00223  -21.07078 5.21378   1.000 29.49635 ? 78  ILE B N   1 
ATOM   2867 C CA  . ILE B 1 78  ? 10.87895  -21.93468 4.43373   1.000 28.20835 ? 78  ILE B CA  1 
ATOM   2868 C C   . ILE B 1 78  ? 12.32183  -21.44783 4.39002   1.000 28.78138 ? 78  ILE B C   1 
ATOM   2869 O O   . ILE B 1 78  ? 13.14447  -22.05724 3.69585   1.000 27.97504 ? 78  ILE B O   1 
ATOM   2870 C CB  . ILE B 1 78  ? 10.34461  -22.12494 3.00207   1.000 29.68822 ? 78  ILE B CB  1 
ATOM   2871 C CG1 . ILE B 1 78  ? 10.19620  -20.77490 2.29535   1.000 25.67532 ? 78  ILE B CG1 1 
ATOM   2872 C CG2 . ILE B 1 78  ? 9.00234   -22.86638 3.04573   1.000 31.05048 ? 78  ILE B CG2 1 
ATOM   2873 C CD1 . ILE B 1 78  ? 9.85813   -20.90164 0.79607   1.000 24.91251 ? 78  ILE B CD1 1 
ATOM   2874 N N   . GLY B 1 79  ? 12.65498  -20.37848 5.10729   1.000 26.37188 ? 79  GLY B N   1 
ATOM   2875 C CA  . GLY B 1 79  ? 14.02070  -19.91019 5.24673   1.000 27.73139 ? 79  GLY B CA  1 
ATOM   2876 C C   . GLY B 1 79  ? 14.06945  -18.77814 6.25554   1.000 28.45802 ? 79  GLY B C   1 
ATOM   2877 O O   . GLY B 1 79  ? 13.06924  -18.08098 6.44746   1.000 27.43419 ? 79  GLY B O   1 
ATOM   2878 N N   . HIS B 1 80  ? 15.20253  -18.58030 6.92156   1.000 26.34524 ? 80  HIS B N   1 
ATOM   2879 C CA  . HIS B 1 80  ? 15.29100  -17.48084 7.86937   1.000 26.89533 ? 80  HIS B CA  1 
ATOM   2880 C C   . HIS B 1 80  ? 16.70652  -16.92869 7.86815   1.000 33.36281 ? 80  HIS B C   1 
ATOM   2881 O O   . HIS B 1 80  ? 17.67338  -17.66255 7.65620   1.000 26.70953 ? 80  HIS B O   1 
ATOM   2882 C CB  . HIS B 1 80  ? 14.87313  -17.91913 9.29069   1.000 31.28335 ? 80  HIS B CB  1 
ATOM   2883 C CG  . HIS B 1 80  ? 15.78990  -18.92360 9.92567   1.000 31.75588 ? 80  HIS B CG  1 
ATOM   2884 N ND1 . HIS B 1 80  ? 15.68031  -20.28250 9.70509   1.000 36.54275 ? 80  HIS B ND1 1 
ATOM   2885 C CD2 . HIS B 1 80  ? 16.81406  -18.76838 10.79769  1.000 33.06469 ? 80  HIS B CD2 1 
ATOM   2886 C CE1 . HIS B 1 80  ? 16.60792  -20.91731 10.40321  1.000 33.54774 ? 80  HIS B CE1 1 
ATOM   2887 N NE2 . HIS B 1 80  ? 17.30814  -20.02080 11.07430  1.000 37.38408 ? 80  HIS B NE2 1 
ATOM   2888 N N   . SER B 1 81  ? 16.81365  -15.62085 8.08856   1.000 28.83324 ? 81  SER B N   1 
ATOM   2889 C CA  . SER B 1 81  ? 18.10834  -14.98528 8.25161   1.000 33.74120 ? 81  SER B CA  1 
ATOM   2890 C C   . SER B 1 81  ? 17.96219  -13.74528 9.12098   1.000 29.70154 ? 81  SER B C   1 
ATOM   2891 O O   . SER B 1 81  ? 16.86775  -13.19815 9.29411   1.000 25.51452 ? 81  SER B O   1 
ATOM   2892 C CB  . SER B 1 81  ? 18.72894  -14.62232 6.90319   1.000 26.50412 ? 81  SER B CB  1 
ATOM   2893 O OG  . SER B 1 81  ? 17.97601  -13.62309 6.23367   1.000 39.50773 ? 81  SER B OG  1 
ATOM   2894 N N   . MET B 1 82  ? 19.09052  -13.30367 9.65996   1.000 31.21802 ? 82  MET B N   1 
ATOM   2895 C CA  . MET B 1 82  ? 19.14843  -12.13572 10.52364  1.000 28.51022 ? 82  MET B CA  1 
ATOM   2896 C C   . MET B 1 82  ? 19.92799  -11.04325 9.81092   1.000 34.35680 ? 82  MET B C   1 
ATOM   2897 O O   . MET B 1 82  ? 21.05702  -11.27518 9.36069   1.000 32.37614 ? 82  MET B O   1 
ATOM   2898 C CB  . MET B 1 82  ? 19.80843  -12.49173 11.86179  1.000 31.35417 ? 82  MET B CB  1 
ATOM   2899 C CG  . MET B 1 82  ? 19.89017  -11.35375 12.85694  1.000 31.31780 ? 82  MET B CG  1 
ATOM   2900 S SD  . MET B 1 82  ? 20.47383  -11.87606 14.49115  1.000 33.84806 ? 82  MET B SD  1 
ATOM   2901 C CE  . MET B 1 82  ? 22.19237  -12.27536 14.15907  1.000 37.08846 ? 82  MET B CE  1 
ATOM   2902 N N   . GLN B 1 83  ? 19.31882  -9.86315  9.68511   1.000 29.16191 ? 83  GLN B N   1 
ATOM   2903 C CA  . GLN B 1 83  ? 20.00247  -8.68513  9.15904   1.000 28.90506 ? 83  GLN B CA  1 
ATOM   2904 C C   . GLN B 1 83  ? 19.98238  -7.61224  10.23456  1.000 29.49426 ? 83  GLN B C   1 
ATOM   2905 O O   . GLN B 1 83  ? 18.93584  -7.00994  10.50055  1.000 24.55014 ? 83  GLN B O   1 
ATOM   2906 C CB  . GLN B 1 83  ? 19.35909  -8.18214  7.88072   1.000 32.44418 ? 83  GLN B CB  1 
ATOM   2907 C CG  . GLN B 1 83  ? 20.16023  -7.09338  7.20530   1.000 33.16300 ? 83  GLN B CG  1 
ATOM   2908 C CD  . GLN B 1 83  ? 19.47647  -6.59588  5.96309   1.000 33.32969 ? 83  GLN B CD  1 
ATOM   2909 O OE1 . GLN B 1 83  ? 18.36177  -7.00418  5.66187   1.000 39.19637 ? 83  GLN B OE1 1 
ATOM   2910 N NE2 . GLN B 1 83  ? 20.13556  -5.71258  5.23288   1.000 35.75363 ? 83  GLN B NE2 1 
ATOM   2911 N N   . ASN B 1 84  ? 21.13934  -7.38633  10.84990  1.000 25.85898 ? 84  ASN B N   1 
ATOM   2912 C CA  . ASN B 1 84  ? 21.23479  -6.47018  11.97592  1.000 25.07658 ? 84  ASN B CA  1 
ATOM   2913 C C   . ASN B 1 84  ? 20.20374  -6.86537  13.02343  1.000 30.13019 ? 84  ASN B C   1 
ATOM   2914 O O   . ASN B 1 84  ? 20.27236  -7.98803  13.52982  1.000 26.04722 ? 84  ASN B O   1 
ATOM   2915 C CB  . ASN B 1 84  ? 21.07303  -5.04022  11.47047  1.000 23.39585 ? 84  ASN B CB  1 
ATOM   2916 C CG  . ASN B 1 84  ? 22.12100  -4.69722  10.38620  1.000 28.40845 ? 84  ASN B CG  1 
ATOM   2917 O OD1 . ASN B 1 84  ? 23.32071  -4.87444  10.61228  1.000 29.52842 ? 84  ASN B OD1 1 
ATOM   2918 N ND2 . ASN B 1 84  ? 21.66983  -4.29369  9.19898   1.000 23.59147 ? 84  ASN B ND2 1 
ATOM   2919 N N   . CYS B 1 85  ? 19.24045  -6.00501  13.36295  1.000 23.84257 ? 85  CYS B N   1 
ATOM   2920 C CA  . CYS B 1 85  ? 18.31659  -6.35729  14.44608  1.000 25.87267 ? 85  CYS B CA  1 
ATOM   2921 C C   . CYS B 1 85  ? 16.93745  -6.82193  13.94782  1.000 20.85165 ? 85  CYS B C   1 
ATOM   2922 O O   . CYS B 1 85  ? 15.99667  -6.91209  14.74080  1.000 21.80081 ? 85  CYS B O   1 
ATOM   2923 C CB  . CYS B 1 85  ? 18.15225  -5.19237  15.43395  1.000 23.12209 ? 85  CYS B CB  1 
ATOM   2924 S SG  . CYS B 1 85  ? 19.70372  -4.60101  16.21346  1.000 24.67864 ? 85  CYS B SG  1 
ATOM   2925 N N   . VAL B 1 86  ? 16.80767  -7.17207  12.67517  1.000 24.43772 ? 86  VAL B N   1 
ATOM   2926 C CA  . VAL B 1 86  ? 15.54811  -7.65203  12.11743  1.000 22.88016 ? 86  VAL B CA  1 
ATOM   2927 C C   . VAL B 1 86  ? 15.74390  -9.09000  11.65206  1.000 24.51440 ? 86  VAL B C   1 
ATOM   2928 O O   . VAL B 1 86  ? 16.82039  -9.45426  11.16024  1.000 26.54883 ? 86  VAL B O   1 
ATOM   2929 C CB  . VAL B 1 86  ? 15.07178  -6.74776  10.96010  1.000 29.18137 ? 86  VAL B CB  1 
ATOM   2930 C CG1 . VAL B 1 86  ? 14.06299  -7.47570  10.08319  1.000 30.06093 ? 86  VAL B CG1 1 
ATOM   2931 C CG2 . VAL B 1 86  ? 14.46340  -5.45799  11.51688  1.000 24.23194 ? 86  VAL B CG2 1 
ATOM   2932 N N   . LEU B 1 87  ? 14.72590  -9.91939  11.85978  1.000 21.49246 ? 87  LEU B N   1 
ATOM   2933 C CA  . LEU B 1 87  ? 14.66672  -11.22096 11.20177  1.000 26.60277 ? 87  LEU B CA  1 
ATOM   2934 C C   . LEU B 1 87  ? 13.94216  -11.11094 9.86168   1.000 31.07093 ? 87  LEU B C   1 
ATOM   2935 O O   . LEU B 1 87  ? 12.99457  -10.33342 9.69934   1.000 24.74932 ? 87  LEU B O   1 
ATOM   2936 C CB  . LEU B 1 87  ? 13.95300  -12.24810 12.07311  1.000 25.97716 ? 87  LEU B CB  1 
ATOM   2937 C CG  . LEU B 1 87  ? 14.67080  -12.89733 13.23557  1.000 35.56625 ? 87  LEU B CG  1 
ATOM   2938 C CD1 . LEU B 1 87  ? 13.72417  -13.92203 13.84821  1.000 32.51393 ? 87  LEU B CD1 1 
ATOM   2939 C CD2 . LEU B 1 87  ? 15.95571  -13.54672 12.76691  1.000 34.94424 ? 87  LEU B CD2 1 
ATOM   2940 N N   . LYS B 1 88  ? 14.40137  -11.90383 8.89664   1.000 24.70136 ? 88  LYS B N   1 
ATOM   2941 C CA  . LYS B 1 88  ? 13.75324  -12.03517 7.59696   1.000 28.97950 ? 88  LYS B CA  1 
ATOM   2942 C C   . LYS B 1 88  ? 13.34023  -13.49226 7.42745   1.000 25.08087 ? 88  LYS B C   1 
ATOM   2943 O O   . LYS B 1 88  ? 14.19788  -14.37216 7.30013   1.000 24.92472 ? 88  LYS B O   1 
ATOM   2944 C CB  . LYS B 1 88  ? 14.69115  -11.58670 6.48098   1.000 24.70911 ? 88  LYS B CB  1 
ATOM   2945 C CG  . LYS B 1 88  ? 15.03366  -10.10723 6.54761   1.000 24.46341 ? 88  LYS B CG  1 
ATOM   2946 C CD  . LYS B 1 88  ? 15.64544  -9.60410  5.25008   1.000 32.51998 ? 88  LYS B CD  1 
ATOM   2947 C CE  . LYS B 1 88  ? 16.98037  -10.23921 5.01935   1.000 36.60488 ? 88  LYS B CE  1 
ATOM   2948 N NZ  . LYS B 1 88  ? 17.88698  -9.32603  4.28002   1.000 36.98377 ? 88  LYS B NZ  1 
ATOM   2949 N N   . LEU B 1 89  ? 12.03062  -13.75444 7.45199   1.000 24.35714 ? 89  LEU B N   1 
ATOM   2950 C CA  . LEU B 1 89  ? 11.50214  -15.11230 7.33775   1.000 25.48431 ? 89  LEU B CA  1 
ATOM   2951 C C   . LEU B 1 89  ? 10.87771  -15.26918 5.95982   1.000 26.43848 ? 89  LEU B C   1 
ATOM   2952 O O   . LEU B 1 89  ? 9.85576   -14.63700 5.65022   1.000 24.50983 ? 89  LEU B O   1 
ATOM   2953 C CB  . LEU B 1 89  ? 10.47108  -15.40901 8.42803   1.000 21.76523 ? 89  LEU B CB  1 
ATOM   2954 C CG  . LEU B 1 89  ? 10.84945  -15.00395 9.85965   1.000 23.47426 ? 89  LEU B CG  1 
ATOM   2955 C CD1 . LEU B 1 89  ? 9.66966   -15.22821 10.82519  1.000 24.21322 ? 89  LEU B CD1 1 
ATOM   2956 C CD2 . LEU B 1 89  ? 12.06705  -15.79821 10.30535  1.000 24.23677 ? 89  LEU B CD2 1 
ATOM   2957 N N   . LYS B 1 90  ? 11.47691  -16.11517 5.13359   1.000 27.83231 ? 90  LYS B N   1 
ATOM   2958 C CA  . LYS B 1 90  ? 10.85392  -16.45266 3.86355   1.000 21.75526 ? 90  LYS B CA  1 
ATOM   2959 C C   . LYS B 1 90  ? 9.70451   -17.42231 4.11242   1.000 21.97035 ? 90  LYS B C   1 
ATOM   2960 O O   . LYS B 1 90  ? 9.85703   -18.39707 4.85677   1.000 23.25795 ? 90  LYS B O   1 
ATOM   2961 C CB  . LYS B 1 90  ? 11.87225  -17.07020 2.91160   1.000 28.05632 ? 90  LYS B CB  1 
ATOM   2962 C CG  . LYS B 1 90  ? 11.43118  -16.99007 1.45295   1.000 25.94161 ? 90  LYS B CG  1 
ATOM   2963 C CD  . LYS B 1 90  ? 12.48667  -17.54070 0.54455   1.000 34.02648 ? 90  LYS B CD  1 
ATOM   2964 C CE  . LYS B 1 90  ? 12.13113  -17.27115 -0.90892  1.000 42.77236 ? 90  LYS B CE  1 
ATOM   2965 N NZ  . LYS B 1 90  ? 12.43867  -18.46347 -1.75387  1.000 59.71622 ? 90  LYS B NZ  1 
ATOM   2966 N N   . VAL B 1 91  ? 8.55688   -17.14783 3.49523   1.000 28.52995 ? 91  VAL B N   1 
ATOM   2967 C CA  . VAL B 1 91  ? 7.34394   -17.93845 3.65961   1.000 25.89629 ? 91  VAL B CA  1 
ATOM   2968 C C   . VAL B 1 91  ? 6.93837   -18.50944 2.29801   1.000 27.21149 ? 91  VAL B C   1 
ATOM   2969 O O   . VAL B 1 91  ? 7.44387   -18.10213 1.25751   1.000 23.82868 ? 91  VAL B O   1 
ATOM   2970 C CB  . VAL B 1 91  ? 6.19857   -17.11352 4.28453   1.000 25.34494 ? 91  VAL B CB  1 
ATOM   2971 C CG1 . VAL B 1 91  ? 6.56015   -16.73033 5.71398   1.000 25.95787 ? 91  VAL B CG1 1 
ATOM   2972 C CG2 . VAL B 1 91  ? 5.91893   -15.87706 3.46224   1.000 22.96586 ? 91  VAL B CG2 1 
ATOM   2973 N N   . ASP B 1 92  ? 6.00178   -19.45960 2.32399   1.000 25.35254 ? 92  ASP B N   1 
ATOM   2974 C CA  . ASP B 1 92  ? 5.56535   -20.17978 1.13551   1.000 32.54610 ? 92  ASP B CA  1 
ATOM   2975 C C   . ASP B 1 92  ? 4.46709   -19.46828 0.34713   1.000 33.51088 ? 92  ASP B C   1 
ATOM   2976 O O   . ASP B 1 92  ? 3.99037   -20.02402 -0.64393  1.000 33.19544 ? 92  ASP B O   1 
ATOM   2977 C CB  . ASP B 1 92  ? 5.07959   -21.59153 1.52080   1.000 36.04920 ? 92  ASP B CB  1 
ATOM   2978 C CG  . ASP B 1 92  ? 3.94969   -21.57092 2.53835   1.000 41.59936 ? 92  ASP B CG  1 
ATOM   2979 O OD1 . ASP B 1 92  ? 3.35027   -20.50027 2.76533   1.000 37.63683 ? 92  ASP B OD1 1 
ATOM   2980 O OD2 . ASP B 1 92  ? 3.66897   -22.62739 3.13944   1.000 48.09594 ? 92  ASP B OD2 1 
ATOM   2981 N N   . THR B 1 93  ? 4.05254   -18.26759 0.74586   1.000 27.44934 ? 93  THR B N   1 
ATOM   2982 C CA  . THR B 1 93  ? 2.97575   -17.55330 0.07266   1.000 27.13092 ? 93  THR B CA  1 
ATOM   2983 C C   . THR B 1 93  ? 3.38821   -16.10005 -0.14252  1.000 31.79918 ? 93  THR B C   1 
ATOM   2984 O O   . THR B 1 93  ? 3.80838   -15.42216 0.80220   1.000 25.91435 ? 93  THR B O   1 
ATOM   2985 C CB  . THR B 1 93  ? 1.67912   -17.62832 0.89327   1.000 32.42820 ? 93  THR B CB  1 
ATOM   2986 O OG1 . THR B 1 93  ? 1.38234   -19.00019 1.19762   1.000 31.38641 ? 93  THR B OG1 1 
ATOM   2987 C CG2 . THR B 1 93  ? 0.50420   -17.00953 0.12558   1.000 30.29146 ? 93  THR B CG2 1 
ATOM   2988 N N   . ALA B 1 94  ? 3.31029   -15.64530 -1.38999  1.000 22.18937 ? 94  ALA B N   1 
ATOM   2989 C CA  . ALA B 1 94  ? 3.48275   -14.23010 -1.70510  1.000 23.38144 ? 94  ALA B CA  1 
ATOM   2990 C C   . ALA B 1 94  ? 2.23296   -13.44893 -1.30257  1.000 24.99250 ? 94  ALA B C   1 
ATOM   2991 O O   . ALA B 1 94  ? 1.11905   -13.80985 -1.68755  1.000 26.33792 ? 94  ALA B O   1 
ATOM   2992 C CB  . ALA B 1 94  ? 3.74995   -14.05628 -3.20236  1.000 26.04429 ? 94  ALA B CB  1 
ATOM   2993 N N   . ASN B 1 95  ? 2.40871   -12.37590 -0.53321  1.000 24.18181 ? 95  ASN B N   1 
ATOM   2994 C CA  . ASN B 1 95  ? 1.25601   -11.61123 -0.05026  1.000 24.77607 ? 95  ASN B CA  1 
ATOM   2995 C C   . ASN B 1 95  ? 0.50457   -10.98458 -1.21915  1.000 25.99288 ? 95  ASN B C   1 
ATOM   2996 O O   . ASN B 1 95  ? 1.07102   -10.13544 -1.92407  1.000 25.52615 ? 95  ASN B O   1 
ATOM   2997 C CB  . ASN B 1 95  ? 1.70616   -10.52662 0.94691   1.000 23.38558 ? 95  ASN B CB  1 
ATOM   2998 C CG  . ASN B 1 95  ? 0.53072   -9.74488  1.54094   1.000 25.60492 ? 95  ASN B CG  1 
ATOM   2999 O OD1 . ASN B 1 95  ? -0.63422  -9.99422  1.21577   1.000 23.82729 ? 95  ASN B OD1 1 
ATOM   3000 N ND2 . ASN B 1 95  ? 0.83651   -8.79998  2.42584   1.000 25.39015 ? 95  ASN B ND2 1 
ATOM   3001 N N   . PRO B 1 96  ? -0.75872  -11.36360 -1.46319  1.000 24.12767 ? 96  PRO B N   1 
ATOM   3002 C CA  . PRO B 1 96  ? -1.48711  -10.79462 -2.59919  1.000 24.59502 ? 96  PRO B CA  1 
ATOM   3003 C C   . PRO B 1 96  ? -1.78934  -9.32934  -2.43677  1.000 27.08252 ? 96  PRO B C   1 
ATOM   3004 O O   . PRO B 1 96  ? -2.11134  -8.67518  -3.43452  1.000 23.03236 ? 96  PRO B O   1 
ATOM   3005 C CB  . PRO B 1 96  ? -2.78971  -11.61669 -2.64644  1.000 30.15725 ? 96  PRO B CB  1 
ATOM   3006 C CG  . PRO B 1 96  ? -2.56000  -12.78123 -1.75286  1.000 33.61891 ? 96  PRO B CG  1 
ATOM   3007 C CD  . PRO B 1 96  ? -1.57867  -12.32779 -0.71781  1.000 24.36423 ? 96  PRO B CD  1 
ATOM   3008 N N   . LYS B 1 97  ? -1.68628  -8.79267  -1.22146  1.000 22.34520 ? 97  LYS B N   1 
ATOM   3009 C CA  . LYS B 1 97  ? -1.92686  -7.38496  -0.95033  1.000 22.62855 ? 97  LYS B CA  1 
ATOM   3010 C C   . LYS B 1 97  ? -0.63920  -6.58667  -0.87005  1.000 24.90486 ? 97  LYS B C   1 
ATOM   3011 O O   . LYS B 1 97  ? -0.64080  -5.46258  -0.35497  1.000 26.86913 ? 97  LYS B O   1 
ATOM   3012 C CB  . LYS B 1 97  ? -2.72362  -7.23018  0.34506   1.000 25.65751 ? 97  LYS B CB  1 
ATOM   3013 C CG  . LYS B 1 97  ? -4.10973  -7.85404  0.30166   1.000 28.99135 ? 97  LYS B CG  1 
ATOM   3014 C CD  . LYS B 1 97  ? -4.74005  -7.79696  1.67827   1.000 34.92536 ? 97  LYS B CD  1 
ATOM   3015 C CE  . LYS B 1 97  ? -6.13919  -8.37551  1.68492   1.000 43.85796 ? 97  LYS B CE  1 
ATOM   3016 N NZ  . LYS B 1 97  ? -6.74223  -8.25644  3.04754   1.000 63.71592 ? 97  LYS B NZ  1 
ATOM   3017 N N   . THR B 1 98  ? 0.46130   -7.14114  -1.34142  1.000 23.61094 ? 98  THR B N   1 
ATOM   3018 C CA  . THR B 1 98  ? 1.70403   -6.38557  -1.32391  1.000 23.40813 ? 98  THR B CA  1 
ATOM   3019 C C   . THR B 1 98  ? 1.52135   -5.10361  -2.12928  1.000 24.37919 ? 98  THR B C   1 
ATOM   3020 O O   . THR B 1 98  ? 1.12503   -5.17582  -3.30651  1.000 23.76015 ? 98  THR B O   1 
ATOM   3021 C CB  . THR B 1 98  ? 2.85741   -7.20205  -1.90839  1.000 24.08828 ? 98  THR B CB  1 
ATOM   3022 O OG1 . THR B 1 98  ? 3.00242   -8.45050  -1.19857  1.000 24.17506 ? 98  THR B OG1 1 
ATOM   3023 C CG2 . THR B 1 98  ? 4.15608   -6.40673  -1.80443  1.000 26.08682 ? 98  THR B CG2 1 
ATOM   3024 N N   . PRO B 1 99  ? 1.77771   -3.93067  -1.55736  1.000 24.90314 ? 99  PRO B N   1 
ATOM   3025 C CA  . PRO B 1 99  ? 1.75389   -2.69109  -2.33609  1.000 28.90503 ? 99  PRO B CA  1 
ATOM   3026 C C   . PRO B 1 99  ? 3.11777   -2.44516  -2.96747  1.000 27.74737 ? 99  PRO B C   1 
ATOM   3027 O O   . PRO B 1 99  ? 4.10924   -3.08469  -2.62086  1.000 25.63277 ? 99  PRO B O   1 
ATOM   3028 C CB  . PRO B 1 99  ? 1.45258   -1.62428  -1.27417  1.000 27.48966 ? 99  PRO B CB  1 
ATOM   3029 C CG  . PRO B 1 99  ? 2.16372   -2.14848  -0.06207  1.000 28.92739 ? 99  PRO B CG  1 
ATOM   3030 C CD  . PRO B 1 99  ? 2.05463   -3.67551  -0.13017  1.000 24.98977 ? 99  PRO B CD  1 
ATOM   3031 N N   . LYS B 1 100 ? 3.15357   -1.49330  -3.90714  1.000 26.72692 ? 100 LYS B N   1 
ATOM   3032 C CA  . LYS B 1 100 ? 4.44816   -0.93713  -4.27994  1.000 26.05131 ? 100 LYS B CA  1 
ATOM   3033 C C   . LYS B 1 100 ? 5.11139   -0.37897  -3.02355  1.000 26.41820 ? 100 LYS B C   1 
ATOM   3034 O O   . LYS B 1 100 ? 4.45029   0.25784   -2.20286  1.000 29.10661 ? 100 LYS B O   1 
ATOM   3035 C CB  . LYS B 1 100 ? 4.27488   0.16094   -5.33410  1.000 36.43813 ? 100 LYS B CB  1 
ATOM   3036 N N   . TYR B 1 101 ? 6.41348   -0.62764  -2.84673  1.000 22.92210 ? 101 TYR B N   1 
ATOM   3037 C CA  . TYR B 1 101 ? 7.04325   -0.22394  -1.59087  1.000 28.46649 ? 101 TYR B CA  1 
ATOM   3038 C C   . TYR B 1 101 ? 8.54966   -0.07028  -1.76310  1.000 28.49504 ? 101 TYR B C   1 
ATOM   3039 O O   . TYR B 1 101 ? 9.13619   -0.52733  -2.74757  1.000 25.39086 ? 101 TYR B O   1 
ATOM   3040 C CB  . TYR B 1 101 ? 6.75459   -1.22794  -0.46027  1.000 27.03471 ? 101 TYR B CB  1 
ATOM   3041 C CG  . TYR B 1 101 ? 7.46464   -2.54820  -0.66130  1.000 27.87215 ? 101 TYR B CG  1 
ATOM   3042 C CD1 . TYR B 1 101 ? 6.93491   -3.52179  -1.50759  1.000 30.31199 ? 101 TYR B CD1 1 
ATOM   3043 C CD2 . TYR B 1 101 ? 8.68088   -2.81288  -0.03754  1.000 29.13680 ? 101 TYR B CD2 1 
ATOM   3044 C CE1 . TYR B 1 101 ? 7.58864   -4.72697  -1.71379  1.000 29.66816 ? 101 TYR B CE1 1 
ATOM   3045 C CE2 . TYR B 1 101 ? 9.34276   -4.01854  -0.24486  1.000 27.49153 ? 101 TYR B CE2 1 
ATOM   3046 C CZ  . TYR B 1 101 ? 8.78922   -4.96877  -1.08083  1.000 27.98036 ? 101 TYR B CZ  1 
ATOM   3047 O OH  . TYR B 1 101 ? 9.44812   -6.16462  -1.28889  1.000 33.91882 ? 101 TYR B OH  1 
ATOM   3048 N N   . LYS B 1 102 ? 9.15757   0.60752   -0.78601  1.000 26.23424 ? 102 LYS B N   1 
ATOM   3049 C CA  . LYS B 1 102 ? 10.60192  0.69877   -0.65145  1.000 24.13498 ? 102 LYS B CA  1 
ATOM   3050 C C   . LYS B 1 102 ? 10.92002  0.83476   0.83001   1.000 26.17375 ? 102 LYS B C   1 
ATOM   3051 O O   . LYS B 1 102 ? 10.04178  1.13781   1.64306   1.000 22.58832 ? 102 LYS B O   1 
ATOM   3052 C CB  . LYS B 1 102 ? 11.18512  1.87717   -1.45078  1.000 30.04764 ? 102 LYS B CB  1 
ATOM   3053 C CG  . LYS B 1 102 ? 10.48640  3.21166   -1.21864  1.000 34.86977 ? 102 LYS B CG  1 
ATOM   3054 C CD  . LYS B 1 102 ? 11.01161  4.31894   -2.14972  1.000 38.57773 ? 102 LYS B CD  1 
ATOM   3055 C CE  . LYS B 1 102 ? 12.36160  4.83637   -1.67949  1.000 47.36408 ? 102 LYS B CE  1 
ATOM   3056 N NZ  . LYS B 1 102 ? 12.75692  6.13546   -2.31882  1.000 58.65722 ? 102 LYS B NZ  1 
ATOM   3057 N N   . PHE B 1 103 ? 12.17260  0.54980   1.18169   1.000 23.42715 ? 103 PHE B N   1 
ATOM   3058 C CA  . PHE B 1 103 ? 12.68782  0.74659   2.53803   1.000 25.32115 ? 103 PHE B CA  1 
ATOM   3059 C C   . PHE B 1 103 ? 13.53742  2.00962   2.53327   1.000 30.26712 ? 103 PHE B C   1 
ATOM   3060 O O   . PHE B 1 103 ? 14.41320  2.15642   1.67420   1.000 30.04829 ? 103 PHE B O   1 
ATOM   3061 C CB  . PHE B 1 103 ? 13.55097  -0.43303  3.00169   1.000 21.52468 ? 103 PHE B CB  1 
ATOM   3062 C CG  . PHE B 1 103 ? 12.79655  -1.71663  3.18309   1.000 24.95349 ? 103 PHE B CG  1 
ATOM   3063 C CD1 . PHE B 1 103 ? 11.41076  -1.73041  3.19974   1.000 19.54512 ? 103 PHE B CD1 1 
ATOM   3064 C CD2 . PHE B 1 103 ? 13.47765  -2.91314  3.34305   1.000 27.67340 ? 103 PHE B CD2 1 
ATOM   3065 C CE1 . PHE B 1 103 ? 10.72107  -2.90794  3.37762   1.000 27.48152 ? 103 PHE B CE1 1 
ATOM   3066 C CE2 . PHE B 1 103 ? 12.79264  -4.10162  3.52640   1.000 25.07033 ? 103 PHE B CE2 1 
ATOM   3067 C CZ  . PHE B 1 103 ? 11.40521  -4.09774  3.54383   1.000 27.69528 ? 103 PHE B CZ  1 
ATOM   3068 N N   . VAL B 1 104 ? 13.29243  2.91656   3.48127   1.000 24.50103 ? 104 VAL B N   1 
ATOM   3069 C CA  . VAL B 1 104 ? 14.06462  4.15269   3.54825   1.000 27.28659 ? 104 VAL B CA  1 
ATOM   3070 C C   . VAL B 1 104 ? 14.50739  4.39310   4.97866   1.000 27.83194 ? 104 VAL B C   1 
ATOM   3071 O O   . VAL B 1 104 ? 13.82567  4.01639   5.93616   1.000 29.59809 ? 104 VAL B O   1 
ATOM   3072 C CB  . VAL B 1 104 ? 13.28103  5.37944   3.02121   1.000 26.72774 ? 104 VAL B CB  1 
ATOM   3073 C CG1 . VAL B 1 104 ? 12.69208  5.08457   1.63950   1.000 27.13397 ? 104 VAL B CG1 1 
ATOM   3074 C CG2 . VAL B 1 104 ? 12.19512  5.76671   4.00403   1.000 34.39753 ? 104 VAL B CG2 1 
ATOM   3075 N N   . ARG B 1 105 ? 15.66940  5.02060   5.11675   1.000 29.60984 ? 105 ARG B N   1 
ATOM   3076 C CA  . ARG B 1 105 ? 16.15791  5.50391   6.39841   1.000 30.29593 ? 105 ARG B CA  1 
ATOM   3077 C C   . ARG B 1 105 ? 15.91011  7.00473   6.45815   1.000 32.20229 ? 105 ARG B C   1 
ATOM   3078 O O   . ARG B 1 105 ? 16.41848  7.75250   5.61832   1.000 27.79468 ? 105 ARG B O   1 
ATOM   3079 C CB  . ARG B 1 105 ? 17.64266  5.18443   6.57501   1.000 30.58153 ? 105 ARG B CB  1 
ATOM   3080 C CG  . ARG B 1 105 ? 18.10573  5.24135   8.02465   1.000 30.11689 ? 105 ARG B CG  1 
ATOM   3081 C CD  . ARG B 1 105 ? 19.51574  4.70454   8.19378   1.000 24.90920 ? 105 ARG B CD  1 
ATOM   3082 N NE  . ARG B 1 105 ? 20.03149  5.02037   9.51761   1.000 28.75387 ? 105 ARG B NE  1 
ATOM   3083 C CZ  . ARG B 1 105 ? 19.68397  4.40018   10.63661  1.000 29.11237 ? 105 ARG B CZ  1 
ATOM   3084 N NH1 . ARG B 1 105 ? 18.84040  3.37653   10.63030  1.000 28.12744 ? 105 ARG B NH1 1 
ATOM   3085 N NH2 . ARG B 1 105 ? 20.18234  4.82804   11.79447  1.000 24.43265 ? 105 ARG B NH2 1 
ATOM   3086 N N   . ILE B 1 106 ? 15.11265  7.44251   7.42563   1.000 31.07604 ? 106 ILE B N   1 
ATOM   3087 C CA  . ILE B 1 106 ? 14.71494  8.84363   7.49078   1.000 32.84336 ? 106 ILE B CA  1 
ATOM   3088 C C   . ILE B 1 106 ? 15.68036  9.60951   8.38501   1.000 28.61028 ? 106 ILE B C   1 
ATOM   3089 O O   . ILE B 1 106 ? 16.43300  9.03373   9.17306   1.000 27.64364 ? 106 ILE B O   1 
ATOM   3090 C CB  . ILE B 1 106 ? 13.26139  9.00952   7.98558   1.000 28.21488 ? 106 ILE B CB  1 
ATOM   3091 C CG1 . ILE B 1 106 ? 13.11202  8.41611   9.38273   1.000 30.40488 ? 106 ILE B CG1 1 
ATOM   3092 C CG2 . ILE B 1 106 ? 12.29813  8.35933   7.00340   1.000 35.50969 ? 106 ILE B CG2 1 
ATOM   3093 C CD1 . ILE B 1 106 ? 11.73633  8.59536   9.96494   1.000 34.08405 ? 106 ILE B CD1 1 
ATOM   3094 N N   . GLN B 1 107 ? 15.64376  10.94629  8.26063   1.000 29.17849 ? 107 GLN B N   1 
ATOM   3095 C CA  . GLN B 1 107 ? 16.43120  11.88022  9.05322   1.000 28.75635 ? 107 GLN B CA  1 
ATOM   3096 C C   . GLN B 1 107 ? 15.64814  12.37479  10.25952  1.000 30.98604 ? 107 GLN B C   1 
ATOM   3097 O O   . GLN B 1 107 ? 14.41417  12.40022  10.25110  1.000 26.02723 ? 107 GLN B O   1 
ATOM   3098 C CB  . GLN B 1 107 ? 16.84090  13.07520  8.19960   1.000 36.50780 ? 107 GLN B CB  1 
ATOM   3099 C CG  . GLN B 1 107 ? 17.95429  12.78348  7.23134   1.000 38.62590 ? 107 GLN B CG  1 
ATOM   3100 C CD  . GLN B 1 107 ? 19.29193  12.63431  7.93324   1.000 41.75615 ? 107 GLN B CD  1 
ATOM   3101 O OE1 . GLN B 1 107 ? 19.82349  11.52476  8.04491   1.000 43.93625 ? 107 GLN B OE1 1 
ATOM   3102 N NE2 . GLN B 1 107 ? 19.84516  13.75448  8.41843   1.000 35.13053 ? 107 GLN B NE2 1 
ATOM   3103 N N   . PRO B 1 108 ? 16.34163  12.80622  11.31365  1.000 31.91303 ? 108 PRO B N   1 
ATOM   3104 C CA  . PRO B 1 108 ? 15.64505  13.46305  12.41621  1.000 26.34709 ? 108 PRO B CA  1 
ATOM   3105 C C   . PRO B 1 108 ? 14.78965  14.59574  11.87270  1.000 27.98083 ? 108 PRO B C   1 
ATOM   3106 O O   . PRO B 1 108 ? 15.17930  15.30185  10.93995  1.000 26.83802 ? 108 PRO B O   1 
ATOM   3107 C CB  . PRO B 1 108 ? 16.78579  13.97714  13.30017  1.000 29.28466 ? 108 PRO B CB  1 
ATOM   3108 C CG  . PRO B 1 108 ? 17.95944  13.16454  12.92718  1.000 27.63328 ? 108 PRO B CG  1 
ATOM   3109 C CD  . PRO B 1 108 ? 17.80534  12.84566  11.48548  1.000 32.96240 ? 108 PRO B CD  1 
ATOM   3110 N N   . GLY B 1 109 ? 13.59005  14.73812  12.42819  1.000 29.91257 ? 109 GLY B N   1 
ATOM   3111 C CA  . GLY B 1 109 ? 12.65330  15.73737  11.96995  1.000 24.20357 ? 109 GLY B CA  1 
ATOM   3112 C C   . GLY B 1 109 ? 11.64066  15.24929  10.95859  1.000 33.44333 ? 109 GLY B C   1 
ATOM   3113 O O   . GLY B 1 109 ? 10.58072  15.86856  10.81626  1.000 31.43856 ? 109 GLY B O   1 
ATOM   3114 N N   . GLN B 1 110 ? 11.92930  14.16892  10.24003  1.000 28.38030 ? 110 GLN B N   1 
ATOM   3115 C CA  . GLN B 1 110 ? 10.96359  13.66895  9.27472   1.000 23.40235 ? 110 GLN B CA  1 
ATOM   3116 C C   . GLN B 1 110 ? 9.78372   13.06589  10.01537  1.000 23.01126 ? 110 GLN B C   1 
ATOM   3117 O O   . GLN B 1 110 ? 9.93962   12.48132  11.09659  1.000 25.40770 ? 110 GLN B O   1 
ATOM   3118 C CB  . GLN B 1 110 ? 11.60977  12.63719  8.35248   1.000 30.56837 ? 110 GLN B CB  1 
ATOM   3119 C CG  . GLN B 1 110 ? 12.43419  13.28247  7.23661   1.000 46.84934 ? 110 GLN B CG  1 
ATOM   3120 C CD  . GLN B 1 110 ? 12.90267  12.29281  6.18257   1.000 41.43751 ? 110 GLN B CD  1 
ATOM   3121 O OE1 . GLN B 1 110 ? 14.08725  11.95635  6.11271   1.000 35.07738 ? 110 GLN B OE1 1 
ATOM   3122 N NE2 . GLN B 1 110 ? 11.97330  11.82759  5.35079   1.000 47.92221 ? 110 GLN B NE2 1 
ATOM   3123 N N   . THR B 1 111 ? 8.59409   13.25361  9.46134   1.000 23.55869 ? 111 THR B N   1 
ATOM   3124 C CA  . THR B 1 111 ? 7.39741   12.67196  10.04535  1.000 28.19233 ? 111 THR B CA  1 
ATOM   3125 C C   . THR B 1 111 ? 6.99850   11.40158  9.29853   1.000 27.93370 ? 111 THR B C   1 
ATOM   3126 O O   . THR B 1 111 ? 7.43096   11.15988  8.16974   1.000 27.49089 ? 111 THR B O   1 
ATOM   3127 C CB  . THR B 1 111 ? 6.25261   13.67810  10.01666  1.000 24.90074 ? 111 THR B CB  1 
ATOM   3128 O OG1 . THR B 1 111 ? 6.05597   14.11313  8.66518   1.000 24.68314 ? 111 THR B OG1 1 
ATOM   3129 C CG2 . THR B 1 111 ? 6.59650   14.87820  10.91885  1.000 27.41198 ? 111 THR B CG2 1 
ATOM   3130 N N   . PHE B 1 112 ? 6.15137   10.59850  9.95086   1.000 24.35652 ? 112 PHE B N   1 
ATOM   3131 C CA  . PHE B 1 112 ? 5.61989   9.36470   9.37929   1.000 28.45308 ? 112 PHE B CA  1 
ATOM   3132 C C   . PHE B 1 112 ? 4.40201   8.93443   10.19428  1.000 27.92772 ? 112 PHE B C   1 
ATOM   3133 O O   . PHE B 1 112 ? 4.19495   9.39569   11.31978  1.000 27.40553 ? 112 PHE B O   1 
ATOM   3134 C CB  . PHE B 1 112 ? 6.69138   8.25557   9.34251   1.000 20.49430 ? 112 PHE B CB  1 
ATOM   3135 C CG  . PHE B 1 112 ? 7.31268   7.95016   10.68936  1.000 30.11440 ? 112 PHE B CG  1 
ATOM   3136 C CD1 . PHE B 1 112 ? 8.40693   8.67576   11.15318  1.000 24.56432 ? 112 PHE B CD1 1 
ATOM   3137 C CD2 . PHE B 1 112 ? 6.80399   6.93512   11.48830  1.000 23.23891 ? 112 PHE B CD2 1 
ATOM   3138 C CE1 . PHE B 1 112 ? 8.98027   8.37668   12.40694  1.000 29.94356 ? 112 PHE B CE1 1 
ATOM   3139 C CE2 . PHE B 1 112 ? 7.36215   6.63204   12.70916  1.000 27.64379 ? 112 PHE B CE2 1 
ATOM   3140 C CZ  . PHE B 1 112 ? 8.45501   7.35405   13.17773  1.000 24.08362 ? 112 PHE B CZ  1 
ATOM   3141 N N   . SER B 1 113 ? 3.59339   8.04830   9.61012   1.000 24.54438 ? 113 SER B N   1 
ATOM   3142 C CA  . SER B 1 113 ? 2.47299   7.45374   10.31961  1.000 21.95236 ? 113 SER B CA  1 
ATOM   3143 C C   . SER B 1 113 ? 2.89515   6.12639   10.93051  1.000 24.96793 ? 113 SER B C   1 
ATOM   3144 O O   . SER B 1 113 ? 3.72983   5.40409   10.37822  1.000 25.17520 ? 113 SER B O   1 
ATOM   3145 C CB  . SER B 1 113 ? 1.27932   7.21936   9.38796   1.000 26.90365 ? 113 SER B CB  1 
ATOM   3146 O OG  . SER B 1 113 ? 0.86347   8.41798   8.77110   1.000 24.06208 ? 113 SER B OG  1 
ATOM   3147 N N   . VAL B 1 114 ? 2.32307   5.81302   12.09089  1.000 23.75016 ? 114 VAL B N   1 
ATOM   3148 C CA  . VAL B 1 114 ? 2.53065   4.52624   12.74468  1.000 17.99519 ? 114 VAL B CA  1 
ATOM   3149 C C   . VAL B 1 114 ? 1.20889   3.78549   12.78566  1.000 21.20820 ? 114 VAL B C   1 
ATOM   3150 O O   . VAL B 1 114 ? 0.18776   4.35733   13.18623  1.000 18.89150 ? 114 VAL B O   1 
ATOM   3151 C CB  . VAL B 1 114 ? 3.08955   4.68377   14.17024  1.000 23.16734 ? 114 VAL B CB  1 
ATOM   3152 C CG1 . VAL B 1 114 ? 3.00056   3.35689   14.90299  1.000 20.98341 ? 114 VAL B CG1 1 
ATOM   3153 C CG2 . VAL B 1 114 ? 4.52263   5.15990   14.10624  1.000 26.36002 ? 114 VAL B CG2 1 
ATOM   3154 N N   . LEU B 1 115 ? 1.23661   2.51117   12.39292  1.000 21.29335 ? 115 LEU B N   1 
ATOM   3155 C CA  . LEU B 1 115 ? 0.09188   1.61227   12.52840  1.000 20.39207 ? 115 LEU B CA  1 
ATOM   3156 C C   . LEU B 1 115 ? 0.38247   0.73315   13.74074  1.000 20.22936 ? 115 LEU B C   1 
ATOM   3157 O O   . LEU B 1 115 ? 1.17762   -0.21047  13.66384  1.000 23.20971 ? 115 LEU B O   1 
ATOM   3158 C CB  . LEU B 1 115 ? -0.11877  0.78853   11.25810  1.000 20.40502 ? 115 LEU B CB  1 
ATOM   3159 C CG  . LEU B 1 115 ? -1.32666  -0.15365  11.28959  1.000 18.50249 ? 115 LEU B CG  1 
ATOM   3160 C CD1 . LEU B 1 115 ? -2.59403  0.66706   11.38994  1.000 21.08991 ? 115 LEU B CD1 1 
ATOM   3161 C CD2 . LEU B 1 115 ? -1.36187  -1.12619  10.09326  1.000 20.68480 ? 115 LEU B CD2 1 
ATOM   3162 N N   . ALA B 1 116 ? -0.22466  1.06968   14.87862  1.000 20.50529 ? 116 ALA B N   1 
ATOM   3163 C CA  . ALA B 1 116 ? -0.01716  0.28612   16.08928  1.000 19.52769 ? 116 ALA B CA  1 
ATOM   3164 C C   . ALA B 1 116 ? -0.81028  -1.01019  16.00638  1.000 22.23946 ? 116 ALA B C   1 
ATOM   3165 O O   . ALA B 1 116 ? -2.02150  -0.99356  15.76181  1.000 27.70328 ? 116 ALA B O   1 
ATOM   3166 C CB  . ALA B 1 116 ? -0.42132  1.08936   17.32771  1.000 24.01314 ? 116 ALA B CB  1 
ATOM   3167 N N   . CYS B 1 117 ? -0.12312  -2.13160  16.18565  1.000 21.99613 ? 117 CYS B N   1 
ATOM   3168 C CA  . CYS B 1 117 ? -0.72159  -3.45120  16.01862  1.000 23.68192 ? 117 CYS B CA  1 
ATOM   3169 C C   . CYS B 1 117 ? -0.43306  -4.31899  17.23053  1.000 21.39154 ? 117 CYS B C   1 
ATOM   3170 O O   . CYS B 1 117 ? 0.60637   -4.18373  17.87274  1.000 24.24956 ? 117 CYS B O   1 
ATOM   3171 C CB  . CYS B 1 117 ? -0.19260  -4.18936  14.79004  1.000 28.63700 ? 117 CYS B CB  1 
ATOM   3172 S SG  . CYS B 1 117 ? -0.48001  -3.38013  13.25749  1.000 32.58808 ? 117 CYS B SG  1 
ATOM   3173 N N   . TYR B 1 118 ? -1.33901  -5.26055  17.48959  1.000 22.77530 ? 118 TYR B N   1 
ATOM   3174 C CA  . TYR B 1 118 ? -1.17827  -6.20582  18.58991  1.000 25.27148 ? 118 TYR B CA  1 
ATOM   3175 C C   . TYR B 1 118 ? -1.63191  -7.57133  18.10227  1.000 24.81193 ? 118 TYR B C   1 
ATOM   3176 O O   . TYR B 1 118 ? -2.70098  -7.68761  17.49535  1.000 26.01765 ? 118 TYR B O   1 
ATOM   3177 C CB  . TYR B 1 118 ? -1.96883  -5.74944  19.82935  1.000 21.97532 ? 118 TYR B CB  1 
ATOM   3178 C CG  . TYR B 1 118 ? -1.45042  -4.42654  20.33639  1.000 24.15364 ? 118 TYR B CG  1 
ATOM   3179 C CD1 . TYR B 1 118 ? -1.93449  -3.21993  19.83778  1.000 22.44647 ? 118 TYR B CD1 1 
ATOM   3180 C CD2 . TYR B 1 118 ? -0.42166  -4.38786  21.26997  1.000 19.96758 ? 118 TYR B CD2 1 
ATOM   3181 C CE1 . TYR B 1 118 ? -1.41549  -2.00387  20.28163  1.000 25.83837 ? 118 TYR B CE1 1 
ATOM   3182 C CE2 . TYR B 1 118 ? 0.09474   -3.20176  21.71861  1.000 25.52531 ? 118 TYR B CE2 1 
ATOM   3183 C CZ  . TYR B 1 118 ? -0.39974  -2.00657  21.22416  1.000 22.74786 ? 118 TYR B CZ  1 
ATOM   3184 O OH  . TYR B 1 118 ? 0.15499   -0.83938  21.68987  1.000 25.11365 ? 118 TYR B OH  1 
ATOM   3185 N N   . ASN B 1 119 ? -0.80770  -8.59575  18.32097  1.000 26.78204 ? 119 ASN B N   1 
ATOM   3186 C CA  . ASN B 1 119 ? -1.15829  -9.94726  17.86920  1.000 24.46441 ? 119 ASN B CA  1 
ATOM   3187 C C   . ASN B 1 119 ? -1.46513  -9.94422  16.37421  1.000 24.52689 ? 119 ASN B C   1 
ATOM   3188 O O   . ASN B 1 119 ? -2.36325  -10.63935 15.89592  1.000 27.36876 ? 119 ASN B O   1 
ATOM   3189 C CB  . ASN B 1 119 ? -2.34177  -10.49800 18.66036  1.000 25.62083 ? 119 ASN B CB  1 
ATOM   3190 C CG  . ASN B 1 119 ? -2.05965  -10.55443 20.13008  1.000 35.22638 ? 119 ASN B CG  1 
ATOM   3191 O OD1 . ASN B 1 119 ? -2.72635  -9.90234  20.92212  1.000 44.35823 ? 119 ASN B OD1 1 
ATOM   3192 N ND2 . ASN B 1 119 ? -1.04504  -11.31355 20.50511  1.000 35.65902 ? 119 ASN B ND2 1 
ATOM   3193 N N   . GLY B 1 120 ? -0.71264  -9.13768  15.63164  1.000 24.91447 ? 120 GLY B N   1 
ATOM   3194 C CA  . GLY B 1 120 ? -0.91973  -8.99687  14.20404  1.000 24.08173 ? 120 GLY B CA  1 
ATOM   3195 C C   . GLY B 1 120 ? -2.15322  -8.22888  13.80577  1.000 36.17241 ? 120 GLY B C   1 
ATOM   3196 O O   . GLY B 1 120 ? -2.46533  -8.16962  12.61280  1.000 29.06270 ? 120 GLY B O   1 
ATOM   3197 N N   . SER B 1 121 ? -2.86289  -7.62712  14.75548  1.000 25.78414 ? 121 SER B N   1 
ATOM   3198 C CA  . SER B 1 121 ? -4.14607  -7.00560  14.45427  1.000 28.15680 ? 121 SER B CA  1 
ATOM   3199 C C   . SER B 1 121 ? -4.03367  -5.48800  14.56852  1.000 29.55071 ? 121 SER B C   1 
ATOM   3200 O O   . SER B 1 121 ? -3.75988  -4.97399  15.66405  1.000 24.65824 ? 121 SER B O   1 
ATOM   3201 C CB  . SER B 1 121 ? -5.21913  -7.54017  15.40017  1.000 27.63230 ? 121 SER B CB  1 
ATOM   3202 O OG  . SER B 1 121 ? -6.47009  -6.97792  15.09104  1.000 37.68606 ? 121 SER B OG  1 
ATOM   3203 N N   . PRO B 1 122 ? -4.19240  -4.74096  13.47691  1.000 27.97183 ? 122 PRO B N   1 
ATOM   3204 C CA  . PRO B 1 122 ? -4.10247  -3.27570  13.55978  1.000 26.04172 ? 122 PRO B CA  1 
ATOM   3205 C C   . PRO B 1 122 ? -5.07875  -2.71315  14.57395  1.000 28.75338 ? 122 PRO B C   1 
ATOM   3206 O O   . PRO B 1 122 ? -6.26499  -3.04681  14.56776  1.000 31.08429 ? 122 PRO B O   1 
ATOM   3207 C CB  . PRO B 1 122 ? -4.45616  -2.82159  12.13938  1.000 25.69338 ? 122 PRO B CB  1 
ATOM   3208 C CG  . PRO B 1 122 ? -4.00484  -3.96851  11.27095  1.000 25.78469 ? 122 PRO B CG  1 
ATOM   3209 C CD  . PRO B 1 122 ? -4.25260  -5.22129  12.07937  1.000 29.73456 ? 122 PRO B CD  1 
ATOM   3210 N N   . SER B 1 123 ? -4.57857  -1.81903  15.41797  1.000 27.67372 ? 123 SER B N   1 
ATOM   3211 C CA  . SER B 1 123 ? -5.34923  -1.23170  16.50160  1.000 27.93823 ? 123 SER B CA  1 
ATOM   3212 C C   . SER B 1 123 ? -5.63600  0.25325   16.31954  1.000 27.60581 ? 123 SER B C   1 
ATOM   3213 O O   . SER B 1 123 ? -6.70745  0.71948   16.71473  1.000 27.97609 ? 123 SER B O   1 
ATOM   3214 C CB  . SER B 1 123 ? -4.61308  -1.43853  17.82798  1.000 24.87580 ? 123 SER B CB  1 
ATOM   3215 O OG  . SER B 1 123 ? -5.23324  -0.69797  18.85161  1.000 46.57574 ? 123 SER B OG  1 
ATOM   3216 N N   . GLY B 1 124 ? -4.70045  1.01249   15.76152  1.000 22.99416 ? 124 GLY B N   1 
ATOM   3217 C CA  . GLY B 1 124 ? -4.89943  2.43698   15.55080  1.000 21.95188 ? 124 GLY B CA  1 
ATOM   3218 C C   . GLY B 1 124 ? -3.75298  2.99723   14.74493  1.000 23.37806 ? 124 GLY B C   1 
ATOM   3219 O O   . GLY B 1 124 ? -2.71220  2.35360   14.56926  1.000 23.65307 ? 124 GLY B O   1 
ATOM   3220 N N   . VAL B 1 125 ? -3.95244  4.21478   14.24801  1.000 23.48240 ? 125 VAL B N   1 
ATOM   3221 C CA  . VAL B 1 125 ? -2.94136  4.87426   13.43706  1.000 24.62644 ? 125 VAL B CA  1 
ATOM   3222 C C   . VAL B 1 125 ? -2.74763  6.30110   13.94379  1.000 24.96333 ? 125 VAL B C   1 
ATOM   3223 O O   . VAL B 1 125 ? -3.71047  6.98462   14.31095  1.000 24.28182 ? 125 VAL B O   1 
ATOM   3224 C CB  . VAL B 1 125 ? -3.30871  4.81262   11.92926  1.000 23.10563 ? 125 VAL B CB  1 
ATOM   3225 C CG1 . VAL B 1 125 ? -4.71372  5.28736   11.68534  1.000 28.23657 ? 125 VAL B CG1 1 
ATOM   3226 C CG2 . VAL B 1 125 ? -2.30977  5.61131   11.08616  1.000 21.18453 ? 125 VAL B CG2 1 
ATOM   3227 N N   . TYR B 1 126 ? -1.49284  6.73783   14.01304  1.000 19.62644 ? 126 TYR B N   1 
ATOM   3228 C CA  . TYR B 1 126 ? -1.21574  8.08516   14.49065  1.000 22.10481 ? 126 TYR B CA  1 
ATOM   3229 C C   . TYR B 1 126 ? 0.02216   8.60503   13.77892  1.000 27.70035 ? 126 TYR B C   1 
ATOM   3230 O O   . TYR B 1 126 ? 0.73513   7.86389   13.10043  1.000 26.14036 ? 126 TYR B O   1 
ATOM   3231 C CB  . TYR B 1 126 ? -1.05532  8.13734   16.02579  1.000 21.83975 ? 126 TYR B CB  1 
ATOM   3232 C CG  . TYR B 1 126 ? 0.05026   7.26319   16.59871  1.000 28.89698 ? 126 TYR B CG  1 
ATOM   3233 C CD1 . TYR B 1 126 ? 1.37647   7.70259   16.62335  1.000 24.03720 ? 126 TYR B CD1 1 
ATOM   3234 C CD2 . TYR B 1 126 ? -0.23441  6.00750   17.13027  1.000 23.67263 ? 126 TYR B CD2 1 
ATOM   3235 C CE1 . TYR B 1 126 ? 2.36799   6.91844   17.15398  1.000 27.29838 ? 126 TYR B CE1 1 
ATOM   3236 C CE2 . TYR B 1 126 ? 0.75988   5.21427   17.65465  1.000 24.82573 ? 126 TYR B CE2 1 
ATOM   3237 C CZ  . TYR B 1 126 ? 2.05702   5.67145   17.66414  1.000 27.25737 ? 126 TYR B CZ  1 
ATOM   3238 O OH  . TYR B 1 126 ? 3.04339   4.87780   18.20273  1.000 32.68606 ? 126 TYR B OH  1 
ATOM   3239 N N   . GLN B 1 127 ? 0.23322   9.90814   13.90483  1.000 25.74239 ? 127 GLN B N   1 
ATOM   3240 C CA  . GLN B 1 127 ? 1.30478   10.62323  13.23370  1.000 27.25812 ? 127 GLN B CA  1 
ATOM   3241 C C   . GLN B 1 127 ? 2.35592   11.02387  14.26178  1.000 28.46503 ? 127 GLN B C   1 
ATOM   3242 O O   . GLN B 1 127 ? 2.01577   11.46341  15.36405  1.000 23.55273 ? 127 GLN B O   1 
ATOM   3243 C CB  . GLN B 1 127 ? 0.73646   11.86242  12.52971  1.000 32.19384 ? 127 GLN B CB  1 
ATOM   3244 C CG  . GLN B 1 127 ? 1.71612   12.60757  11.66341  1.000 33.79959 ? 127 GLN B CG  1 
ATOM   3245 C CD  . GLN B 1 127 ? 2.13160   11.81124  10.44526  1.000 41.86903 ? 127 GLN B CD  1 
ATOM   3246 O OE1 . GLN B 1 127 ? 1.56841   10.73462  10.15009  1.000 37.09560 ? 127 GLN B OE1 1 
ATOM   3247 N NE2 . GLN B 1 127 ? 3.11945   12.34016  9.71090   1.000 41.02499 ? 127 GLN B NE2 1 
ATOM   3248 N N   . CYS B 1 128 ? 3.63434   10.89488  13.90826  1.000 22.19816 ? 128 CYS B N   1 
ATOM   3249 C CA  . CYS B 1 128 ? 4.68311   11.29927  14.83204  1.000 25.68585 ? 128 CYS B CA  1 
ATOM   3250 C C   . CYS B 1 128 ? 5.93285   11.67715  14.04299  1.000 26.56957 ? 128 CYS B C   1 
ATOM   3251 O O   . CYS B 1 128 ? 5.94265   11.67200  12.81028  1.000 24.84484 ? 128 CYS B O   1 
ATOM   3252 C CB  . CYS B 1 128 ? 4.96457   10.19385  15.84245  1.000 33.28761 ? 128 CYS B CB  1 
ATOM   3253 S SG  . CYS B 1 128 ? 5.61864   8.75297   15.06163  1.000 38.08877 ? 128 CYS B SG  1 
ATOM   3254 N N   . ALA B 1 129 ? 6.99548   12.02734  14.75888  1.000 30.13918 ? 129 ALA B N   1 
ATOM   3255 C CA  . ALA B 1 129 ? 8.21993   12.42503  14.08068  1.000 26.19170 ? 129 ALA B CA  1 
ATOM   3256 C C   . ALA B 1 129 ? 9.43468   11.80649  14.75948  1.000 24.31050 ? 129 ALA B C   1 
ATOM   3257 O O   . ALA B 1 129 ? 9.43245   11.52165  15.96265  1.000 26.25003 ? 129 ALA B O   1 
ATOM   3258 C CB  . ALA B 1 129 ? 8.36082   13.95370  14.02106  1.000 28.37100 ? 129 ALA B CB  1 
ATOM   3259 N N   . MET B 1 130 ? 10.46895  11.58025  13.95762  1.000 23.72083 ? 130 MET B N   1 
ATOM   3260 C CA  . MET B 1 130 ? 11.76441  11.18795  14.49318  1.000 26.70213 ? 130 MET B CA  1 
ATOM   3261 C C   . MET B 1 130 ? 12.38967  12.38475  15.19740  1.000 28.18008 ? 130 MET B C   1 
ATOM   3262 O O   . MET B 1 130 ? 12.65490  13.41121  14.56092  1.000 27.73556 ? 130 MET B O   1 
ATOM   3263 C CB  . MET B 1 130 ? 12.66543  10.70183  13.36309  1.000 25.25806 ? 130 MET B CB  1 
ATOM   3264 C CG  . MET B 1 130 ? 14.04631  10.27693  13.81003  1.000 26.47632 ? 130 MET B CG  1 
ATOM   3265 S SD  . MET B 1 130 ? 14.01443  8.80622   14.84773  1.000 29.67675 ? 130 MET B SD  1 
ATOM   3266 C CE  . MET B 1 130 ? 13.27734  7.61189   13.70871  1.000 28.47570 ? 130 MET B CE  1 
ATOM   3267 N N   . ARG B 1 131 ? 12.62284  12.26792  16.50150  1.000 27.68616 ? 131 ARG B N   1 
ATOM   3268 C CA  . ARG B 1 131 ? 13.20615  13.38981  17.21610  1.000 21.26625 ? 131 ARG B CA  1 
ATOM   3269 C C   . ARG B 1 131 ? 14.69246  13.51321  16.88701  1.000 24.98174 ? 131 ARG B C   1 
ATOM   3270 O O   . ARG B 1 131 ? 15.30282  12.57770  16.35941  1.000 22.80536 ? 131 ARG B O   1 
ATOM   3271 C CB  . ARG B 1 131 ? 13.00690  13.23360  18.72416  1.000 21.80773 ? 131 ARG B CB  1 
ATOM   3272 C CG  . ARG B 1 131 ? 11.54063  13.10448  19.17097  1.000 26.03763 ? 131 ARG B CG  1 
ATOM   3273 C CD  . ARG B 1 131 ? 10.68048  14.30253  18.77423  1.000 26.51029 ? 131 ARG B CD  1 
ATOM   3274 N NE  . ARG B 1 131 ? 11.25421  15.58109  19.18730  1.000 22.37526 ? 131 ARG B NE  1 
ATOM   3275 C CZ  . ARG B 1 131 ? 10.73115  16.76336  18.87687  1.000 28.87663 ? 131 ARG B CZ  1 
ATOM   3276 N NH1 . ARG B 1 131 ? 9.59269   16.85688  18.20927  1.000 24.14631 ? 131 ARG B NH1 1 
ATOM   3277 N NH2 . ARG B 1 131 ? 11.36654  17.87915  19.24607  1.000 18.55775 ? 131 ARG B NH2 1 
ATOM   3278 N N   . PRO B 1 132 ? 15.28641  14.68390  17.14055  1.000 23.91457 ? 132 PRO B N   1 
ATOM   3279 C CA  . PRO B 1 132 ? 16.74015  14.82300  16.94389  1.000 24.19374 ? 132 PRO B CA  1 
ATOM   3280 C C   . PRO B 1 132 ? 17.57238  13.89332  17.81377  1.000 27.28232 ? 132 PRO B C   1 
ATOM   3281 O O   . PRO B 1 132 ? 18.71332  13.58720  17.44272  1.000 29.78437 ? 132 PRO B O   1 
ATOM   3282 C CB  . PRO B 1 132 ? 16.99681  16.29586  17.28977  1.000 26.86308 ? 132 PRO B CB  1 
ATOM   3283 C CG  . PRO B 1 132 ? 15.66890  16.98760  16.96214  1.000 25.56018 ? 132 PRO B CG  1 
ATOM   3284 C CD  . PRO B 1 132 ? 14.63934  15.97800  17.43313  1.000 21.52244 ? 132 PRO B CD  1 
ATOM   3285 N N   . ASN B 1 133 ? 17.06210  13.44932  18.96654  1.000 24.05860 ? 133 ASN B N   1 
ATOM   3286 C CA  . ASN B 1 133 ? 17.76510  12.45734  19.77251  1.000 21.37395 ? 133 ASN B CA  1 
ATOM   3287 C C   . ASN B 1 133 ? 17.43106  11.01940  19.35052  1.000 25.42637 ? 133 ASN B C   1 
ATOM   3288 O O   . ASN B 1 133 ? 17.72878  10.07272  20.09141  1.000 26.07063 ? 133 ASN B O   1 
ATOM   3289 C CB  . ASN B 1 133 ? 17.47991  12.68728  21.26877  1.000 24.26846 ? 133 ASN B CB  1 
ATOM   3290 C CG  . ASN B 1 133 ? 16.07574  12.29365  21.66847  1.000 26.78045 ? 133 ASN B CG  1 
ATOM   3291 O OD1 . ASN B 1 133 ? 15.27021  11.90998  20.82279  1.000 25.42946 ? 133 ASN B OD1 1 
ATOM   3292 N ND2 . ASN B 1 133 ? 15.77421  12.37463  22.96472  1.000 25.10809 ? 133 ASN B ND2 1 
ATOM   3293 N N   . PHE B 1 134 ? 16.82501  10.85108  18.16811  1.000 24.43944 ? 134 PHE B N   1 
ATOM   3294 C CA  . PHE B 1 134 ? 16.58815  9.55692   17.51901  1.000 23.41223 ? 134 PHE B CA  1 
ATOM   3295 C C   . PHE B 1 134 ? 15.59092  8.69063   18.27887  1.000 29.33198 ? 134 PHE B C   1 
ATOM   3296 O O   . PHE B 1 134 ? 15.61092  7.46243   18.18052  1.000 28.26750 ? 134 PHE B O   1 
ATOM   3297 C CB  . PHE B 1 134 ? 17.90347  8.80623   17.27078  1.000 24.71551 ? 134 PHE B CB  1 
ATOM   3298 C CG  . PHE B 1 134 ? 18.70838  9.39612   16.14655  1.000 30.88162 ? 134 PHE B CG  1 
ATOM   3299 C CD1 . PHE B 1 134 ? 18.17620  9.45884   14.85875  1.000 31.19290 ? 134 PHE B CD1 1 
ATOM   3300 C CD2 . PHE B 1 134 ? 19.96616  9.91915   16.36852  1.000 29.50866 ? 134 PHE B CD2 1 
ATOM   3301 C CE1 . PHE B 1 134 ? 18.89114  10.01747  13.81293  1.000 31.77829 ? 134 PHE B CE1 1 
ATOM   3302 C CE2 . PHE B 1 134 ? 20.68289  10.48453  15.32931  1.000 33.94325 ? 134 PHE B CE2 1 
ATOM   3303 C CZ  . PHE B 1 134 ? 20.14646  10.53231  14.04732  1.000 33.66009 ? 134 PHE B CZ  1 
ATOM   3304 N N   . THR B 1 135 ? 14.69370  9.31542   19.02169  1.000 28.21542 ? 135 THR B N   1 
ATOM   3305 C CA  . THR B 1 135 ? 13.55227  8.62853   19.59469  1.000 22.40822 ? 135 THR B CA  1 
ATOM   3306 C C   . THR B 1 135 ? 12.29472  9.18013   18.94573  1.000 26.99017 ? 135 THR B C   1 
ATOM   3307 O O   . THR B 1 135 ? 12.32325  10.18349  18.22545  1.000 24.65883 ? 135 THR B O   1 
ATOM   3308 C CB  . THR B 1 135 ? 13.48929  8.80685   21.12093  1.000 22.10078 ? 135 THR B CB  1 
ATOM   3309 O OG1 . THR B 1 135 ? 13.27816  10.19382  21.42256  1.000 26.10176 ? 135 THR B OG1 1 
ATOM   3310 C CG2 . THR B 1 135 ? 14.79301  8.32181   21.78384  1.000 25.91904 ? 135 THR B CG2 1 
ATOM   3311 N N   . ILE B 1 136 ? 11.18026  8.51205   19.19510  1.000 23.40800 ? 136 ILE B N   1 
ATOM   3312 C CA  . ILE B 1 136 ? 9.88939   9.02698   18.76545  1.000 24.94740 ? 136 ILE B CA  1 
ATOM   3313 C C   . ILE B 1 136 ? 8.98324   9.08184   19.97780  1.000 28.24292 ? 136 ILE B C   1 
ATOM   3314 O O   . ILE B 1 136 ? 9.06500   8.22246   20.86570  1.000 24.70603 ? 136 ILE B O   1 
ATOM   3315 C CB  . ILE B 1 136 ? 9.25601   8.18395   17.63270  1.000 32.42109 ? 136 ILE B CB  1 
ATOM   3316 C CG1 . ILE B 1 136 ? 8.81310   6.81611   18.13553  1.000 26.97483 ? 136 ILE B CG1 1 
ATOM   3317 C CG2 . ILE B 1 136 ? 10.24210  7.99407   16.49029  1.000 31.55773 ? 136 ILE B CG2 1 
ATOM   3318 C CD1 . ILE B 1 136 ? 8.04062   6.02444   17.05932  1.000 26.88425 ? 136 ILE B CD1 1 
ATOM   3319 N N   . LYS B 1 137 ? 8.13637   10.11121  20.02573  1.000 26.35031 ? 137 LYS B N   1 
ATOM   3320 C CA  . LYS B 1 137 ? 7.12089   10.22280  21.06721  1.000 29.73258 ? 137 LYS B CA  1 
ATOM   3321 C C   . LYS B 1 137 ? 5.91124   9.43659   20.57750  1.000 27.65487 ? 137 LYS B C   1 
ATOM   3322 O O   . LYS B 1 137 ? 4.98135   9.96393   19.97006  1.000 26.93429 ? 137 LYS B O   1 
ATOM   3323 C CB  . LYS B 1 137 ? 6.80637   11.68549  21.36478  1.000 27.72548 ? 137 LYS B CB  1 
ATOM   3324 C CG  . LYS B 1 137 ? 7.97654   12.42882  22.00902  1.000 34.49520 ? 137 LYS B CG  1 
ATOM   3325 C CD  . LYS B 1 137 ? 7.74161   13.92606  22.00405  1.000 41.94697 ? 137 LYS B CD  1 
ATOM   3326 C CE  . LYS B 1 137 ? 8.62888   14.62139  23.01479  1.000 48.96393 ? 137 LYS B CE  1 
ATOM   3327 N NZ  . LYS B 1 137 ? 8.33374   14.16354  24.40724  1.000 59.11070 ? 137 LYS B NZ  1 
ATOM   3328 N N   . GLY B 1 138 ? 5.95874   8.12599   20.81260  1.000 29.27445 ? 138 GLY B N   1 
ATOM   3329 C CA  . GLY B 1 138 ? 4.95598   7.21693   20.31149  1.000 25.26106 ? 138 GLY B CA  1 
ATOM   3330 C C   . GLY B 1 138 ? 3.91749   6.88994   21.36428  1.000 25.40520 ? 138 GLY B C   1 
ATOM   3331 O O   . GLY B 1 138 ? 3.86312   7.48409   22.44017  1.000 27.82083 ? 138 GLY B O   1 
ATOM   3332 N N   . SER B 1 139 ? 3.08369   5.91667   21.03057  1.000 22.40204 ? 139 SER B N   1 
ATOM   3333 C CA  . SER B 1 139 ? 2.10795   5.34102   21.94852  1.000 24.13565 ? 139 SER B CA  1 
ATOM   3334 C C   . SER B 1 139 ? 2.10646   3.84347   21.68493  1.000 27.48245 ? 139 SER B C   1 
ATOM   3335 O O   . SER B 1 139 ? 1.60349   3.40906   20.64533  1.000 23.95342 ? 139 SER B O   1 
ATOM   3336 C CB  . SER B 1 139 ? 0.72271   5.93755   21.71910  1.000 21.50535 ? 139 SER B CB  1 
ATOM   3337 O OG  . SER B 1 139 ? -0.24437  5.39227   22.59410  1.000 29.38228 ? 139 SER B OG  1 
ATOM   3338 N N   . PHE B 1 140 ? 2.65426   3.06319   22.61730  1.000 24.71441 ? 140 PHE B N   1 
ATOM   3339 C CA  . PHE B 1 140 ? 2.95412   1.65062   22.39731  1.000 23.31060 ? 140 PHE B CA  1 
ATOM   3340 C C   . PHE B 1 140 ? 2.77189   0.87528   23.69698  1.000 29.00497 ? 140 PHE B C   1 
ATOM   3341 O O   . PHE B 1 140 ? 3.36248   1.25717   24.70885  1.000 25.99571 ? 140 PHE B O   1 
ATOM   3342 C CB  . PHE B 1 140 ? 4.40536   1.47138   21.93342  1.000 18.49173 ? 140 PHE B CB  1 
ATOM   3343 C CG  . PHE B 1 140 ? 4.65602   1.82727   20.49421  1.000 23.44362 ? 140 PHE B CG  1 
ATOM   3344 C CD1 . PHE B 1 140 ? 3.92334   1.24723   19.48491  1.000 27.02610 ? 140 PHE B CD1 1 
ATOM   3345 C CD2 . PHE B 1 140 ? 5.68056   2.69469   20.15995  1.000 24.37731 ? 140 PHE B CD2 1 
ATOM   3346 C CE1 . PHE B 1 140 ? 4.18534   1.54709   18.16368  1.000 23.97824 ? 140 PHE B CE1 1 
ATOM   3347 C CE2 . PHE B 1 140 ? 5.94398   3.00832   18.84218  1.000 25.20302 ? 140 PHE B CE2 1 
ATOM   3348 C CZ  . PHE B 1 140 ? 5.20543   2.42927   17.84771  1.000 24.10717 ? 140 PHE B CZ  1 
ATOM   3349 N N   . LEU B 1 141 ? 2.02740   -0.23982  23.65795  1.000 25.47768 ? 141 LEU B N   1 
ATOM   3350 C CA  . LEU B 1 141 ? 1.82965   -1.10115  24.82626  1.000 27.67121 ? 141 LEU B CA  1 
ATOM   3351 C C   . LEU B 1 141 ? 2.54726   -2.43443  24.62384  1.000 28.28016 ? 141 LEU B C   1 
ATOM   3352 O O   . LEU B 1 141 ? 3.15877   -2.69143  23.58490  1.000 24.55939 ? 141 LEU B O   1 
ATOM   3353 C CB  . LEU B 1 141 ? 0.33524   -1.31436  25.10861  1.000 23.32610 ? 141 LEU B CB  1 
ATOM   3354 C CG  . LEU B 1 141 ? -0.48446  -0.03566  25.32159  1.000 29.01596 ? 141 LEU B CG  1 
ATOM   3355 C CD1 . LEU B 1 141 ? -1.98000  -0.32241  25.43241  1.000 31.30283 ? 141 LEU B CD1 1 
ATOM   3356 C CD2 . LEU B 1 141 ? -0.00272  0.71660   26.56361  1.000 26.29078 ? 141 LEU B CD2 1 
ATOM   3357 N N   . ASN B 1 142 ? 2.49808   -3.29162  25.64875  1.000 30.41994 ? 142 ASN B N   1 
ATOM   3358 C CA  . ASN B 1 142 ? 3.07734   -4.62311  25.51014  1.000 27.46024 ? 142 ASN B CA  1 
ATOM   3359 C C   . ASN B 1 142 ? 2.55508   -5.28950  24.25023  1.000 23.22415 ? 142 ASN B C   1 
ATOM   3360 O O   . ASN B 1 142 ? 1.35371   -5.25616  23.96568  1.000 27.12225 ? 142 ASN B O   1 
ATOM   3361 C CB  . ASN B 1 142 ? 2.74163   -5.49631  26.71241  1.000 23.91985 ? 142 ASN B CB  1 
ATOM   3362 C CG  . ASN B 1 142 ? 3.50193   -5.09766  27.94860  1.000 32.34638 ? 142 ASN B CG  1 
ATOM   3363 O OD1 . ASN B 1 142 ? 4.61033   -4.57514  27.86921  1.000 37.22744 ? 142 ASN B OD1 1 
ATOM   3364 N ND2 . ASN B 1 142 ? 2.91961   -5.36735  29.10632  1.000 39.14045 ? 142 ASN B ND2 1 
ATOM   3365 N N   . GLY B 1 143 ? 3.46304   -5.91889  23.50507  1.000 26.16744 ? 143 GLY B N   1 
ATOM   3366 C CA  . GLY B 1 143 ? 3.09303   -6.66447  22.31778  1.000 23.39137 ? 143 GLY B CA  1 
ATOM   3367 C C   . GLY B 1 143 ? 3.06475   -5.85973  21.03603  1.000 22.78004 ? 143 GLY B C   1 
ATOM   3368 O O   . GLY B 1 143 ? 2.68744   -6.40651  19.98928  1.000 24.23381 ? 143 GLY B O   1 
ATOM   3369 N N   . SER B 1 144 ? 3.45599   -4.58406  21.07784  1.000 23.09679 ? 144 SER B N   1 
ATOM   3370 C CA  . SER B 1 144 ? 3.43449   -3.70430  19.91180  1.000 21.43596 ? 144 SER B CA  1 
ATOM   3371 C C   . SER B 1 144 ? 4.66713   -3.85383  19.02651  1.000 20.04883 ? 144 SER B C   1 
ATOM   3372 O O   . SER B 1 144 ? 4.67646   -3.34627  17.89950  1.000 19.97616 ? 144 SER B O   1 
ATOM   3373 C CB  . SER B 1 144 ? 3.31938   -2.25075  20.37551  1.000 23.35692 ? 144 SER B CB  1 
ATOM   3374 O OG  . SER B 1 144 ? 4.39435   -1.90782  21.23756  1.000 25.62850 ? 144 SER B OG  1 
ATOM   3375 N N   . CYS B 1 145 ? 5.71049   -4.51944  19.49787  1.000 18.67148 ? 145 CYS B N   1 
ATOM   3376 C CA  . CYS B 1 145 ? 6.92628   -4.62089  18.69936  1.000 18.30358 ? 145 CYS B CA  1 
ATOM   3377 C C   . CYS B 1 145 ? 6.60702   -5.19501  17.32288  1.000 21.90704 ? 145 CYS B C   1 
ATOM   3378 O O   . CYS B 1 145 ? 5.70062   -6.01677  17.17258  1.000 24.41732 ? 145 CYS B O   1 
ATOM   3379 C CB  . CYS B 1 145 ? 7.96478   -5.46704  19.44024  1.000 23.32096 ? 145 CYS B CB  1 
ATOM   3380 S SG  . CYS B 1 145 ? 8.67734   -4.51216  20.78296  1.000 25.53134 ? 145 CYS B SG  1 
ATOM   3381 N N   . GLY B 1 146 ? 7.32359   -4.70734  16.30031  1.000 17.61780 ? 146 GLY B N   1 
ATOM   3382 C CA  . GLY B 1 146 ? 6.99282   -5.01192  14.92207  1.000 16.63052 ? 146 GLY B CA  1 
ATOM   3383 C C   . GLY B 1 146 ? 6.00934   -4.06895  14.25213  1.000 20.73289 ? 146 GLY B C   1 
ATOM   3384 O O   . GLY B 1 146 ? 5.87484   -4.11170  13.01643  1.000 20.04156 ? 146 GLY B O   1 
ATOM   3385 N N   . SER B 1 147 ? 5.28689   -3.24006  15.00552  1.000 24.36374 ? 147 SER B N   1 
ATOM   3386 C CA  . SER B 1 147 ? 4.53581   -2.17239  14.34767  1.000 22.17914 ? 147 SER B CA  1 
ATOM   3387 C C   . SER B 1 147 ? 5.48701   -1.30789  13.52682  1.000 22.62846 ? 147 SER B C   1 
ATOM   3388 O O   . SER B 1 147 ? 6.65124   -1.10575  13.89307  1.000 21.19763 ? 147 SER B O   1 
ATOM   3389 C CB  . SER B 1 147 ? 3.80256   -1.32344  15.37632  1.000 22.32113 ? 147 SER B CB  1 
ATOM   3390 O OG  . SER B 1 147 ? 2.89328   -2.11698  16.13759  1.000 25.09979 ? 147 SER B OG  1 
ATOM   3391 N N   . VAL B 1 148 ? 4.99378   -0.79346  12.39685  1.000 22.31448 ? 148 VAL B N   1 
ATOM   3392 C CA  . VAL B 1 148 ? 5.86563   -0.06793  11.48503  1.000 19.33538 ? 148 VAL B CA  1 
ATOM   3393 C C   . VAL B 1 148 ? 5.39184   1.37637   11.34487  1.000 20.30812 ? 148 VAL B C   1 
ATOM   3394 O O   . VAL B 1 148 ? 4.21110   1.70723   11.52127  1.000 21.76843 ? 148 VAL B O   1 
ATOM   3395 C CB  . VAL B 1 148 ? 5.94977   -0.75647  10.09918  1.000 24.77393 ? 148 VAL B CB  1 
ATOM   3396 C CG1 . VAL B 1 148 ? 6.58889   -2.14532  10.23461  1.000 20.77374 ? 148 VAL B CG1 1 
ATOM   3397 C CG2 . VAL B 1 148 ? 4.56632   -0.85704  9.44954   1.000 21.49441 ? 148 VAL B CG2 1 
ATOM   3398 N N   . GLY B 1 149 ? 6.33084   2.23583   10.98970  1.000 20.45042 ? 149 GLY B N   1 
ATOM   3399 C CA  . GLY B 1 149 ? 6.03521   3.59752   10.56555  1.000 21.43018 ? 149 GLY B CA  1 
ATOM   3400 C C   . GLY B 1 149 ? 6.27897   3.73876   9.07293   1.000 24.18109 ? 149 GLY B C   1 
ATOM   3401 O O   . GLY B 1 149 ? 7.15714   3.07510   8.51341   1.000 23.08707 ? 149 GLY B O   1 
ATOM   3402 N N   . PHE B 1 150 ? 5.51452   4.61818   8.41894   1.000 23.49793 ? 150 PHE B N   1 
ATOM   3403 C CA  . PHE B 1 150 ? 5.56439   4.66110   6.96137   1.000 22.35926 ? 150 PHE B CA  1 
ATOM   3404 C C   . PHE B 1 150 ? 5.10806   6.01569   6.43204   1.000 25.07223 ? 150 PHE B C   1 
ATOM   3405 O O   . PHE B 1 150 ? 4.46547   6.80425   7.12843   1.000 24.61043 ? 150 PHE B O   1 
ATOM   3406 C CB  . PHE B 1 150 ? 4.69381   3.55505   6.35312   1.000 22.76279 ? 150 PHE B CB  1 
ATOM   3407 C CG  . PHE B 1 150 ? 3.24209   3.68052   6.70832   1.000 19.93905 ? 150 PHE B CG  1 
ATOM   3408 C CD1 . PHE B 1 150 ? 2.77340   3.23626   7.93355   1.000 23.46310 ? 150 PHE B CD1 1 
ATOM   3409 C CD2 . PHE B 1 150 ? 2.34332   4.24871   5.81928   1.000 24.86211 ? 150 PHE B CD2 1 
ATOM   3410 C CE1 . PHE B 1 150 ? 1.41575   3.36854   8.26656   1.000 23.67295 ? 150 PHE B CE1 1 
ATOM   3411 C CE2 . PHE B 1 150 ? 0.99928   4.36947   6.14876   1.000 25.42156 ? 150 PHE B CE2 1 
ATOM   3412 C CZ  . PHE B 1 150 ? 0.54374   3.92281   7.37726   1.000 26.20162 ? 150 PHE B CZ  1 
ATOM   3413 N N   . ASN B 1 151 ? 5.43371   6.25047   5.16480   1.000 23.70443 ? 151 ASN B N   1 
ATOM   3414 C CA  . ASN B 1 151 ? 4.90544   7.34858   4.37717   1.000 24.77687 ? 151 ASN B CA  1 
ATOM   3415 C C   . ASN B 1 151 ? 4.38131   6.75650   3.07561   1.000 22.99245 ? 151 ASN B C   1 
ATOM   3416 O O   . ASN B 1 151 ? 4.81944   5.68465   2.65888   1.000 26.86301 ? 151 ASN B O   1 
ATOM   3417 C CB  . ASN B 1 151 ? 5.98958   8.41180   4.08423   1.000 27.07226 ? 151 ASN B CB  1 
ATOM   3418 C CG  . ASN B 1 151 ? 6.24966   9.33845   5.26301   1.000 33.78946 ? 151 ASN B CG  1 
ATOM   3419 O OD1 . ASN B 1 151 ? 5.59836   10.36851  5.40458   1.000 33.72703 ? 151 ASN B OD1 1 
ATOM   3420 N ND2 . ASN B 1 151 ? 7.22131   8.99074   6.09544   1.000 26.87505 ? 151 ASN B ND2 1 
ATOM   3421 N N   . ILE B 1 152 ? 3.42232   7.43346   2.44855   1.000 25.28075 ? 152 ILE B N   1 
ATOM   3422 C CA  . ILE B 1 152 ? 2.90407   7.03353   1.14346   1.000 21.39494 ? 152 ILE B CA  1 
ATOM   3423 C C   . ILE B 1 152 ? 3.09941   8.19649   0.18263   1.000 30.87759 ? 152 ILE B C   1 
ATOM   3424 O O   . ILE B 1 152 ? 2.71626   9.32745   0.49306   1.000 36.11711 ? 152 ILE B O   1 
ATOM   3425 C CB  . ILE B 1 152 ? 1.42067   6.63296   1.20763   1.000 25.64902 ? 152 ILE B CB  1 
ATOM   3426 C CG1 . ILE B 1 152 ? 1.18000   5.61546   2.32354   1.000 28.32251 ? 152 ILE B CG1 1 
ATOM   3427 C CG2 . ILE B 1 152 ? 0.96397   6.08461   -0.15791  1.000 31.42749 ? 152 ILE B CG2 1 
ATOM   3428 C CD1 . ILE B 1 152 ? -0.23769  5.06391   2.37244   1.000 27.63917 ? 152 ILE B CD1 1 
ATOM   3429 N N   . ASP B 1 153 ? 3.69876   7.91703   -0.97366  1.000 38.92730 ? 153 ASP B N   1 
ATOM   3430 C CA  . ASP B 1 153 ? 3.83217   8.88155   -2.05888  1.000 39.31873 ? 153 ASP B CA  1 
ATOM   3431 C C   . ASP B 1 153 ? 3.25185   8.24718   -3.30881  1.000 43.92726 ? 153 ASP B C   1 
ATOM   3432 O O   . ASP B 1 153 ? 3.76839   7.23035   -3.78555  1.000 43.67455 ? 153 ASP B O   1 
ATOM   3433 C CB  . ASP B 1 153 ? 5.29428   9.27496   -2.28558  1.000 44.22564 ? 153 ASP B CB  1 
ATOM   3434 N N   . TYR B 1 154 ? 2.17274   8.83035   -3.82479  1.000 45.62216 ? 154 TYR B N   1 
ATOM   3435 C CA  . TYR B 1 154 ? 1.50033   8.25752   -4.98180  1.000 49.63904 ? 154 TYR B CA  1 
ATOM   3436 C C   . TYR B 1 154 ? 0.86062   6.93537   -4.57699  1.000 53.10006 ? 154 TYR B C   1 
ATOM   3437 O O   . TYR B 1 154 ? -0.05382  6.90703   -3.74534  1.000 51.75354 ? 154 TYR B O   1 
ATOM   3438 C CB  . TYR B 1 154 ? 2.48803   8.06741   -6.13407  1.000 52.07497 ? 154 TYR B CB  1 
ATOM   3439 N N   . ASP B 1 155 ? 1.33483   5.83090   -5.14430  1.000 46.30185 ? 155 ASP B N   1 
ATOM   3440 C CA  . ASP B 1 155 ? 0.87015   4.51473   -4.73220  1.000 49.82002 ? 155 ASP B CA  1 
ATOM   3441 C C   . ASP B 1 155 ? 1.96055   3.71797   -4.01849  1.000 43.79936 ? 155 ASP B C   1 
ATOM   3442 O O   . ASP B 1 155 ? 1.82060   2.50084   -3.84374  1.000 41.57012 ? 155 ASP B O   1 
ATOM   3443 C CB  . ASP B 1 155 ? 0.33335   3.74393   -5.93846  1.000 49.15008 ? 155 ASP B CB  1 
ATOM   3444 C CG  . ASP B 1 155 ? -1.17306  3.53308   -5.87100  1.000 60.71665 ? 155 ASP B CG  1 
ATOM   3445 O OD1 . ASP B 1 155 ? -1.80553  3.98807   -4.89088  1.000 58.88229 ? 155 ASP B OD1 1 
ATOM   3446 O OD2 . ASP B 1 155 ? -1.72678  2.90789   -6.79928  1.000 72.82215 ? 155 ASP B OD2 1 
ATOM   3447 N N   . CYS B 1 156 ? 3.03104   4.38613   -3.58614  1.000 36.13489 ? 156 CYS B N   1 
ATOM   3448 C CA  . CYS B 1 156 ? 4.22400   3.73002   -3.06378  1.000 34.98461 ? 156 CYS B CA  1 
ATOM   3449 C C   . CYS B 1 156 ? 4.30727   3.93553   -1.55581  1.000 30.09716 ? 156 CYS B C   1 
ATOM   3450 O O   . CYS B 1 156 ? 4.29242   5.07347   -1.07573  1.000 28.79978 ? 156 CYS B O   1 
ATOM   3451 C CB  . CYS B 1 156 ? 5.48115   4.26355   -3.75054  1.000 35.29860 ? 156 CYS B CB  1 
ATOM   3452 S SG  . CYS B 1 156 ? 6.98268   3.36183   -3.33328  1.000 37.37030 ? 156 CYS B SG  1 
ATOM   3453 N N   . VAL B 1 157 ? 4.40389   2.84009   -0.81525  1.000 27.06551 ? 157 VAL B N   1 
ATOM   3454 C CA  . VAL B 1 157 ? 4.61396   2.89957   0.62691   1.000 23.48015 ? 157 VAL B CA  1 
ATOM   3455 C C   . VAL B 1 157 ? 6.11386   2.84154   0.90608   1.000 30.37061 ? 157 VAL B C   1 
ATOM   3456 O O   . VAL B 1 157 ? 6.77879   1.85523   0.56074   1.000 28.47270 ? 157 VAL B O   1 
ATOM   3457 C CB  . VAL B 1 157 ? 3.87946   1.76149   1.34489   1.000 24.15914 ? 157 VAL B CB  1 
ATOM   3458 C CG1 . VAL B 1 157 ? 4.11861   1.85625   2.85235   1.000 19.51731 ? 157 VAL B CG1 1 
ATOM   3459 C CG2 . VAL B 1 157 ? 2.37698   1.81605   1.04914   1.000 22.54372 ? 157 VAL B CG2 1 
ATOM   3460 N N   . SER B 1 158 ? 6.64439   3.90422   1.52814   1.000 22.51285 ? 158 SER B N   1 
ATOM   3461 C CA  . SER B 1 158 ? 8.02490   3.95586   2.00705   1.000 20.71140 ? 158 SER B CA  1 
ATOM   3462 C C   . SER B 1 158 ? 8.03215   3.57411   3.47993   1.000 19.66346 ? 158 SER B C   1 
ATOM   3463 O O   . SER B 1 158 ? 7.63520   4.37411   4.33043   1.000 27.71846 ? 158 SER B O   1 
ATOM   3464 C CB  . SER B 1 158 ? 8.61374   5.35267   1.82028   1.000 26.84603 ? 158 SER B CB  1 
ATOM   3465 O OG  . SER B 1 158 ? 8.84715   5.62538   0.44838   1.000 33.13551 ? 158 SER B OG  1 
ATOM   3466 N N   . PHE B 1 159 ? 8.49335   2.36756   3.78898   1.000 23.49186 ? 159 PHE B N   1 
ATOM   3467 C CA  . PHE B 1 159 ? 8.60405   1.94133   5.18301   1.000 23.36068 ? 159 PHE B CA  1 
ATOM   3468 C C   . PHE B 1 159 ? 9.90063   2.46241   5.80015   1.000 27.82744 ? 159 PHE B C   1 
ATOM   3469 O O   . PHE B 1 159 ? 10.98687  2.24737   5.24704   1.000 25.63274 ? 159 PHE B O   1 
ATOM   3470 C CB  . PHE B 1 159 ? 8.55940   0.41316   5.28144   1.000 24.06370 ? 159 PHE B CB  1 
ATOM   3471 C CG  . PHE B 1 159 ? 7.24669   -0.19330  4.86754   1.000 19.47128 ? 159 PHE B CG  1 
ATOM   3472 C CD1 . PHE B 1 159 ? 6.16961   -0.19154  5.73385   1.000 22.12092 ? 159 PHE B CD1 1 
ATOM   3473 C CD2 . PHE B 1 159 ? 7.10253   -0.79123  3.62098   1.000 21.12843 ? 159 PHE B CD2 1 
ATOM   3474 C CE1 . PHE B 1 159 ? 4.97813   -0.76940  5.36901   1.000 19.63534 ? 159 PHE B CE1 1 
ATOM   3475 C CE2 . PHE B 1 159 ? 5.90970   -1.36735  3.23709   1.000 20.34497 ? 159 PHE B CE2 1 
ATOM   3476 C CZ  . PHE B 1 159 ? 4.83087   -1.34909  4.09039   1.000 16.51965 ? 159 PHE B CZ  1 
ATOM   3477 N N   . CYS B 1 160 ? 9.79221   3.11646   6.97171   1.000 21.73808 ? 160 CYS B N   1 
ATOM   3478 C CA  . CYS B 1 160 ? 10.94032  3.76710   7.59279   1.000 23.23637 ? 160 CYS B CA  1 
ATOM   3479 C C   . CYS B 1 160 ? 11.20936  3.36623   9.03392   1.000 21.77934 ? 160 CYS B C   1 
ATOM   3480 O O   . CYS B 1 160 ? 12.30873  3.64602   9.52086   1.000 27.19195 ? 160 CYS B O   1 
ATOM   3481 C CB  . CYS B 1 160 ? 10.79112  5.29955   7.54733   1.000 24.81387 ? 160 CYS B CB  1 
ATOM   3482 S SG  . CYS B 1 160 ? 9.28991   5.94565   8.40514   1.000 25.46144 ? 160 CYS B SG  1 
ATOM   3483 N N   . TYR B 1 161 ? 10.27299  2.73680   9.73445   1.000 21.30772 ? 161 TYR B N   1 
ATOM   3484 C CA  . TYR B 1 161 ? 10.46870  2.44567   11.15253  1.000 23.50642 ? 161 TYR B CA  1 
ATOM   3485 C C   . TYR B 1 161 ? 9.84385   1.09625   11.49658  1.000 22.56898 ? 161 TYR B C   1 
ATOM   3486 O O   . TYR B 1 161 ? 8.78049   0.74449   10.97382  1.000 20.11581 ? 161 TYR B O   1 
ATOM   3487 C CB  . TYR B 1 161 ? 9.85959   3.56401   12.02324  1.000 19.41547 ? 161 TYR B CB  1 
ATOM   3488 C CG  . TYR B 1 161 ? 9.96837   3.37350   13.54716  1.000 19.50964 ? 161 TYR B CG  1 
ATOM   3489 C CD1 . TYR B 1 161 ? 11.11838  3.72166   14.23590  1.000 22.07827 ? 161 TYR B CD1 1 
ATOM   3490 C CD2 . TYR B 1 161 ? 8.90082   2.85526   14.28125  1.000 19.25336 ? 161 TYR B CD2 1 
ATOM   3491 C CE1 . TYR B 1 161 ? 11.20783  3.55996   15.62076  1.000 22.20213 ? 161 TYR B CE1 1 
ATOM   3492 C CE2 . TYR B 1 161 ? 8.97487   2.68279   15.65131  1.000 17.87166 ? 161 TYR B CE2 1 
ATOM   3493 C CZ  . TYR B 1 161 ? 10.12345  3.02860   16.31990  1.000 25.52783 ? 161 TYR B CZ  1 
ATOM   3494 O OH  . TYR B 1 161 ? 10.20376  2.84599   17.69439  1.000 23.63149 ? 161 TYR B OH  1 
ATOM   3495 N N   . MET B 1 162 ? 10.51715  0.33260   12.35653  1.000 18.87720 ? 162 MET B N   1 
ATOM   3496 C CA  . MET B 1 162 ? 9.90331   -0.82630  12.99826  1.000 21.07926 ? 162 MET B CA  1 
ATOM   3497 C C   . MET B 1 162 ? 10.15812  -0.72095  14.49939  1.000 21.99771 ? 162 MET B C   1 
ATOM   3498 O O   . MET B 1 162 ? 11.27364  -0.40361  14.91711  1.000 21.39096 ? 162 MET B O   1 
ATOM   3499 C CB  . MET B 1 162 ? 10.44689  -2.14220  12.42405  1.000 18.96220 ? 162 MET B CB  1 
ATOM   3500 C CG  . MET B 1 162 ? 9.95989   -3.35947  13.18750  1.000 22.19573 ? 162 MET B CG  1 
ATOM   3501 S SD  . MET B 1 162 ? 10.26200  -4.92596  12.34305  1.000 27.93081 ? 162 MET B SD  1 
ATOM   3502 C CE  . MET B 1 162 ? 8.93146   -4.96861  11.14313  1.000 25.36491 ? 162 MET B CE  1 
ATOM   3503 N N   . HIS B 1 163 ? 9.12860   -0.96417  15.31152  1.000 20.02724 ? 163 HIS B N   1 
ATOM   3504 C CA  . HIS B 1 163 ? 9.22014   -0.67604  16.74027  1.000 20.80063 ? 163 HIS B CA  1 
ATOM   3505 C C   . HIS B 1 163 ? 9.86056   -1.81633  17.53153  1.000 23.00539 ? 163 HIS B C   1 
ATOM   3506 O O   . HIS B 1 163 ? 9.49799   -2.98470  17.36381  1.000 19.02564 ? 163 HIS B O   1 
ATOM   3507 C CB  . HIS B 1 163 ? 7.82512   -0.40053  17.31327  1.000 20.82381 ? 163 HIS B CB  1 
ATOM   3508 C CG  . HIS B 1 163 ? 7.86040   -0.00690  18.75624  1.000 23.21609 ? 163 HIS B CG  1 
ATOM   3509 N ND1 . HIS B 1 163 ? 8.59130   1.07061   19.20528  1.000 21.91411 ? 163 HIS B ND1 1 
ATOM   3510 C CD2 . HIS B 1 163 ? 7.31185   -0.57805  19.85407  1.000 23.49419 ? 163 HIS B CD2 1 
ATOM   3511 C CE1 . HIS B 1 163 ? 8.47849   1.15642   20.51965  1.000 23.32428 ? 163 HIS B CE1 1 
ATOM   3512 N NE2 . HIS B 1 163 ? 7.70104   0.17067   20.93709  1.000 21.21187 ? 163 HIS B NE2 1 
ATOM   3513 N N   . HIS B 1 164 ? 10.78156  -1.45776  18.44832  1.000 20.15590 ? 164 HIS B N   1 
ATOM   3514 C CA  . HIS B 1 164 ? 11.47662  -2.41257  19.30329  1.000 20.07927 ? 164 HIS B CA  1 
ATOM   3515 C C   . HIS B 1 164 ? 11.33552  -2.18562  20.80673  1.000 24.39644 ? 164 HIS B C   1 
ATOM   3516 O O   . HIS B 1 164 ? 11.26998  -3.16939  21.54008  1.000 23.80155 ? 164 HIS B O   1 
ATOM   3517 C CB  . HIS B 1 164 ? 12.98184  -2.43105  18.97460  1.000 18.35693 ? 164 HIS B CB  1 
ATOM   3518 C CG  . HIS B 1 164 ? 13.29380  -2.97488  17.62316  1.000 23.27540 ? 164 HIS B CG  1 
ATOM   3519 N ND1 . HIS B 1 164 ? 13.99382  -4.14446  17.43751  1.000 21.40620 ? 164 HIS B ND1 1 
ATOM   3520 C CD2 . HIS B 1 164 ? 12.98819  -2.51680  16.38804  1.000 20.94193 ? 164 HIS B CD2 1 
ATOM   3521 C CE1 . HIS B 1 164 ? 14.11189  -4.38172  16.14464  1.000 21.46391 ? 164 HIS B CE1 1 
ATOM   3522 N NE2 . HIS B 1 164 ? 13.50886  -3.41111  15.48547  1.000 24.02760 ? 164 HIS B NE2 1 
ATOM   3523 N N   . MET B 1 165 ? 11.34526  -0.95067  21.32506  1.000 21.55996 ? 165 MET B N   1 
ATOM   3524 C CA  . MET B 1 165 ? 11.49993  -0.82316  22.77806  1.000 22.77564 ? 165 MET B CA  1 
ATOM   3525 C C   . MET B 1 165 ? 11.01206  0.53430   23.27077  1.000 23.85568 ? 165 MET B C   1 
ATOM   3526 O O   . MET B 1 165 ? 10.84340  1.47931   22.49792  1.000 22.77231 ? 165 MET B O   1 
ATOM   3527 C CB  . MET B 1 165 ? 12.97022  -1.00813  23.18185  1.000 25.37035 ? 165 MET B CB  1 
ATOM   3528 C CG  . MET B 1 165 ? 13.87422  0.04381   22.53385  1.000 27.44763 ? 165 MET B CG  1 
ATOM   3529 S SD  . MET B 1 165 ? 15.63308  -0.38898  22.66732  1.000 35.97702 ? 165 MET B SD  1 
ATOM   3530 C CE  . MET B 1 165 ? 15.69482  -0.73899  24.41909  1.000 32.76730 ? 165 MET B CE  1 
ATOM   3531 N N   . GLU B 1 166 ? 10.84345  0.63532   24.59327  1.000 22.99079 ? 166 GLU B N   1 
ATOM   3532 C CA  . GLU B 1 166 ? 10.47778  1.88344   25.25106  1.000 24.38598 ? 166 GLU B CA  1 
ATOM   3533 C C   . GLU B 1 166 ? 11.53433  2.25258   26.28494  1.000 30.24529 ? 166 GLU B C   1 
ATOM   3534 O O   . GLU B 1 166 ? 11.95041  1.41084   27.09968  1.000 28.36758 ? 166 GLU B O   1 
ATOM   3535 C CB  . GLU B 1 166 ? 9.09933   1.77324   25.91402  1.000 27.37966 ? 166 GLU B CB  1 
ATOM   3536 C CG  . GLU B 1 166 ? 8.67679   3.01895   26.66330  1.000 30.74344 ? 166 GLU B CG  1 
ATOM   3537 C CD  . GLU B 1 166 ? 7.27412   2.89824   27.24303  1.000 39.06085 ? 166 GLU B CD  1 
ATOM   3538 O OE1 . GLU B 1 166 ? 6.33151   2.57250   26.49341  1.000 32.94019 ? 166 GLU B OE1 1 
ATOM   3539 O OE2 . GLU B 1 166 ? 7.11653   3.12911   28.45813  1.000 42.44504 ? 166 GLU B OE2 1 
ATOM   3540 N N   . LEU B 1 167 ? 11.94935  3.50857   26.25747  1.000 27.49652 ? 167 LEU B N   1 
ATOM   3541 C CA  . LEU B 1 167 ? 12.97181  4.02909   27.14885  1.000 27.86722 ? 167 LEU B CA  1 
ATOM   3542 C C   . LEU B 1 167 ? 12.34581  4.53026   28.44341  1.000 33.58389 ? 167 LEU B C   1 
ATOM   3543 O O   . LEU B 1 167 ? 11.12994  4.74337   28.52129  1.000 32.62926 ? 167 LEU B O   1 
ATOM   3544 C CB  . LEU B 1 167 ? 13.74410  5.15110   26.45157  1.000 28.24171 ? 167 LEU B CB  1 
ATOM   3545 C CG  . LEU B 1 167 ? 14.52874  4.63791   25.23054  1.000 31.62793 ? 167 LEU B CG  1 
ATOM   3546 C CD1 . LEU B 1 167 ? 14.82301  5.73527   24.22083  1.000 29.29808 ? 167 LEU B CD1 1 
ATOM   3547 C CD2 . LEU B 1 167 ? 15.82104  3.94283   25.65803  1.000 32.95878 ? 167 LEU B CD2 1 
ATOM   3548 N N   . PRO B 1 168 ? 13.15218  4.70848   29.49521  1.000 35.97477 ? 168 PRO B N   1 
ATOM   3549 C CA  . PRO B 1 168 ? 12.57029  5.08445   30.79507  1.000 34.51979 ? 168 PRO B CA  1 
ATOM   3550 C C   . PRO B 1 168 ? 11.74415  6.35713   30.76130  1.000 38.37346 ? 168 PRO B C   1 
ATOM   3551 O O   . PRO B 1 168 ? 10.74996  6.45803   31.48606  1.000 40.82733 ? 168 PRO B O   1 
ATOM   3552 C CB  . PRO B 1 168 ? 13.80692  5.22256   31.69234  1.000 36.31213 ? 168 PRO B CB  1 
ATOM   3553 C CG  . PRO B 1 168 ? 14.77737  4.23747   31.11629  1.000 34.92174 ? 168 PRO B CG  1 
ATOM   3554 C CD  . PRO B 1 168 ? 14.57029  4.31990   29.61704  1.000 35.48096 ? 168 PRO B CD  1 
ATOM   3555 N N   . THR B 1 169 ? 12.12061  7.33448   29.95552  1.000 35.23602 ? 169 THR B N   1 
ATOM   3556 C CA  . THR B 1 169 ? 11.31689  8.55232   29.89055  1.000 32.74227 ? 169 THR B CA  1 
ATOM   3557 C C   . THR B 1 169 ? 10.00796  8.36389   29.16256  1.000 35.35253 ? 169 THR B C   1 
ATOM   3558 O O   . THR B 1 169 ? 9.30542   9.35784   28.93207  1.000 34.56580 ? 169 THR B O   1 
ATOM   3559 C CB  . THR B 1 169 ? 12.11987  9.65460   29.21170  1.000 33.74064 ? 169 THR B CB  1 
ATOM   3560 O OG1 . THR B 1 169 ? 12.62685  9.15394   27.96910  1.000 38.63519 ? 169 THR B OG1 1 
ATOM   3561 C CG2 . THR B 1 169 ? 13.28083  10.08539  30.09303  1.000 31.00411 ? 169 THR B CG2 1 
ATOM   3562 N N   . GLY B 1 170 ? 9.66825   7.13812   28.77259  1.000 33.14187 ? 170 GLY B N   1 
ATOM   3563 C CA  . GLY B 1 170 ? 8.41535   6.89635   28.08791  1.000 30.27986 ? 170 GLY B CA  1 
ATOM   3564 C C   . GLY B 1 170 ? 8.42561   7.17785   26.60433  1.000 32.08356 ? 170 GLY B C   1 
ATOM   3565 O O   . GLY B 1 170 ? 7.35504   7.30274   26.00914  1.000 30.06658 ? 170 GLY B O   1 
ATOM   3566 N N   . VAL B 1 171 ? 9.60029   7.32782   25.99300  1.000 27.49125 ? 171 VAL B N   1 
ATOM   3567 C CA  . VAL B 1 171 ? 9.70463   7.51048   24.55376  1.000 21.94312 ? 171 VAL B CA  1 
ATOM   3568 C C   . VAL B 1 171 ? 10.16793  6.18757   23.95562  1.000 20.62972 ? 171 VAL B C   1 
ATOM   3569 O O   . VAL B 1 171 ? 10.46457  5.24027   24.68847  1.000 23.91363 ? 171 VAL B O   1 
ATOM   3570 C CB  . VAL B 1 171 ? 10.66186  8.65915   24.18618  1.000 25.38246 ? 171 VAL B CB  1 
ATOM   3571 C CG1 . VAL B 1 171 ? 10.13087  10.01063  24.69473  1.000 26.87049 ? 171 VAL B CG1 1 
ATOM   3572 C CG2 . VAL B 1 171 ? 12.05861  8.37730   24.74741  1.000 29.26253 ? 171 VAL B CG2 1 
ATOM   3573 N N   . HIS B 1 172 ? 10.25676  6.11118   22.62729  1.000 26.00280 ? 172 HIS B N   1 
ATOM   3574 C CA  . HIS B 1 172 ? 10.36333  4.82492   21.94866  1.000 23.53588 ? 172 HIS B CA  1 
ATOM   3575 C C   . HIS B 1 172 ? 11.49750  4.81051   20.93610  1.000 19.81001 ? 172 HIS B C   1 
ATOM   3576 O O   . HIS B 1 172 ? 11.86100  5.84442   20.37310  1.000 24.88035 ? 172 HIS B O   1 
ATOM   3577 C CB  . HIS B 1 172 ? 9.04462   4.49783   21.27083  1.000 21.27013 ? 172 HIS B CB  1 
ATOM   3578 C CG  . HIS B 1 172 ? 7.89725   4.47213   22.22869  1.000 24.45218 ? 172 HIS B CG  1 
ATOM   3579 N ND1 . HIS B 1 172 ? 6.94590   5.46822   22.28253  1.000 23.91989 ? 172 HIS B ND1 1 
ATOM   3580 C CD2 . HIS B 1 172 ? 7.58064   3.59423   23.20817  1.000 21.80313 ? 172 HIS B CD2 1 
ATOM   3581 C CE1 . HIS B 1 172 ? 6.07660   5.19228   23.24037  1.000 22.67100 ? 172 HIS B CE1 1 
ATOM   3582 N NE2 . HIS B 1 172 ? 6.43620   4.05757   23.81417  1.000 20.42908 ? 172 HIS B NE2 1 
ATOM   3583 N N   . ALA B 1 173 ? 12.00425  3.60747   20.66058  1.000 21.04473 ? 173 ALA B N   1 
ATOM   3584 C CA  . ALA B 1 173 ? 13.18433  3.44216   19.82749  1.000 20.77506 ? 173 ALA B CA  1 
ATOM   3585 C C   . ALA B 1 173 ? 13.04386  2.19264   18.97045  1.000 20.13708 ? 173 ALA B C   1 
ATOM   3586 O O   . ALA B 1 173 ? 12.41126  1.21089   19.36271  1.000 20.17296 ? 173 ALA B O   1 
ATOM   3587 C CB  . ALA B 1 173 ? 14.45260  3.36520   20.67859  1.000 20.87681 ? 173 ALA B CB  1 
ATOM   3588 N N   . GLY B 1 174 ? 13.61412  2.25456   17.78052  1.000 22.74134 ? 174 GLY B N   1 
ATOM   3589 C CA  . GLY B 1 174 ? 13.41210  1.18242   16.83493  1.000 19.11189 ? 174 GLY B CA  1 
ATOM   3590 C C   . GLY B 1 174 ? 14.41811  1.27192   15.71450  1.000 21.51301 ? 174 GLY B C   1 
ATOM   3591 O O   . GLY B 1 174 ? 15.40692  2.00156   15.80042  1.000 24.18498 ? 174 GLY B O   1 
ATOM   3592 N N   . THR B 1 175 ? 14.15057  0.51101   14.65412  1.000 21.62906 ? 175 THR B N   1 
ATOM   3593 C CA  . THR B 1 175 ? 15.08766  0.35926   13.55603  1.000 19.50890 ? 175 THR B CA  1 
ATOM   3594 C C   . THR B 1 175 ? 14.44114  0.78497   12.24905  1.000 22.40795 ? 175 THR B C   1 
ATOM   3595 O O   . THR B 1 175 ? 13.22696  1.00218   12.16525  1.000 23.94568 ? 175 THR B O   1 
ATOM   3596 C CB  . THR B 1 175 ? 15.57519  -1.09181  13.42795  1.000 21.43524 ? 175 THR B CB  1 
ATOM   3597 O OG1 . THR B 1 175 ? 14.47048  -1.94044  13.10131  1.000 21.72178 ? 175 THR B OG1 1 
ATOM   3598 C CG2 . THR B 1 175 ? 16.21250  -1.56171  14.73863  1.000 25.16658 ? 175 THR B CG2 1 
ATOM   3599 N N   . ASP B 1 176 ? 15.27330  0.88656   11.21440  1.000 21.42279 ? 176 ASP B N   1 
ATOM   3600 C CA  . ASP B 1 176 ? 14.73505  0.88936   9.86675   1.000 20.60965 ? 176 ASP B CA  1 
ATOM   3601 C C   . ASP B 1 176 ? 14.44838  -0.55414  9.46235   1.000 22.55665 ? 176 ASP B C   1 
ATOM   3602 O O   . ASP B 1 176 ? 14.60578  -1.49098  10.25453  1.000 23.42744 ? 176 ASP B O   1 
ATOM   3603 C CB  . ASP B 1 176 ? 15.68093  1.61459   8.89713   1.000 23.25450 ? 176 ASP B CB  1 
ATOM   3604 C CG  . ASP B 1 176 ? 17.05949  0.94293   8.77138   1.000 28.39273 ? 176 ASP B CG  1 
ATOM   3605 O OD1 . ASP B 1 176 ? 17.19898  -0.24771  9.12718   1.000 29.46546 ? 176 ASP B OD1 1 
ATOM   3606 O OD2 . ASP B 1 176 ? 18.00347  1.61586   8.28410   1.000 26.77102 ? 176 ASP B OD2 1 
ATOM   3607 N N   . LEU B 1 177 ? 13.99751  -0.75901  8.23266   1.000 21.38396 ? 177 LEU B N   1 
ATOM   3608 C CA  . LEU B 1 177 ? 13.63092  -2.10959  7.85376   1.000 20.28233 ? 177 LEU B CA  1 
ATOM   3609 C C   . LEU B 1 177 ? 14.83229  -2.95376  7.45150   1.000 24.75859 ? 177 LEU B C   1 
ATOM   3610 O O   . LEU B 1 177 ? 14.65480  -4.12510  7.11310   1.000 26.75753 ? 177 LEU B O   1 
ATOM   3611 C CB  . LEU B 1 177 ? 12.58404  -2.08549  6.73613   1.000 25.13595 ? 177 LEU B CB  1 
ATOM   3612 C CG  . LEU B 1 177 ? 11.14012  -2.10637  7.25937   1.000 23.90037 ? 177 LEU B CG  1 
ATOM   3613 C CD1 . LEU B 1 177 ? 10.82636  -3.43655  7.96464   1.000 26.19458 ? 177 LEU B CD1 1 
ATOM   3614 C CD2 . LEU B 1 177 ? 10.93413  -0.94876  8.20690   1.000 22.65580 ? 177 LEU B CD2 1 
ATOM   3615 N N   . GLU B 1 178 ? 16.03740  -2.39045  7.45774   1.000 26.54530 ? 178 GLU B N   1 
ATOM   3616 C CA  . GLU B 1 178 ? 17.26575  -3.17257  7.38104   1.000 26.86042 ? 178 GLU B CA  1 
ATOM   3617 C C   . GLU B 1 178 ? 17.82668  -3.51209  8.76707   1.000 26.46157 ? 178 GLU B C   1 
ATOM   3618 O O   . GLU B 1 178 ? 18.94930  -4.02532  8.87605   1.000 28.08100 ? 178 GLU B O   1 
ATOM   3619 C CB  . GLU B 1 178 ? 18.31060  -2.43191  6.53661   1.000 30.76376 ? 178 GLU B CB  1 
ATOM   3620 C CG  . GLU B 1 178 ? 17.88219  -2.25273  5.07293   1.000 38.30525 ? 178 GLU B CG  1 
ATOM   3621 C CD  . GLU B 1 178 ? 18.94357  -1.57499  4.20802   1.000 51.86636 ? 178 GLU B CD  1 
ATOM   3622 O OE1 . GLU B 1 178 ? 19.58483  -0.60354  4.67586   1.000 47.92486 ? 178 GLU B OE1 1 
ATOM   3623 O OE2 . GLU B 1 178 ? 19.13381  -2.01606  3.05419   1.000 49.95058 ? 178 GLU B OE2 1 
ATOM   3624 N N   . GLY B 1 179 ? 17.06712  -3.23780  9.82298   1.000 25.08635 ? 179 GLY B N   1 
ATOM   3625 C CA  . GLY B 1 179 ? 17.43231  -3.65037  11.16179  1.000 24.58841 ? 179 GLY B CA  1 
ATOM   3626 C C   . GLY B 1 179 ? 18.43388  -2.77526  11.87899  1.000 24.02269 ? 179 GLY B C   1 
ATOM   3627 O O   . GLY B 1 179 ? 18.91024  -3.17450  12.93833  1.000 22.25204 ? 179 GLY B O   1 
ATOM   3628 N N   . ASN B 1 180 ? 18.77110  -1.60108  11.34684  1.000 25.78363 ? 180 ASN B N   1 
ATOM   3629 C CA  . ASN B 1 180 ? 19.72517  -0.70435  11.98968  1.000 32.36225 ? 180 ASN B CA  1 
ATOM   3630 C C   . ASN B 1 180 ? 18.98334  0.27259   12.89368  1.000 26.95182 ? 180 ASN B C   1 
ATOM   3631 O O   . ASN B 1 180 ? 18.12679  1.03143   12.42173  1.000 23.73275 ? 180 ASN B O   1 
ATOM   3632 C CB  . ASN B 1 180 ? 20.54279  0.05877   10.94990  1.000 26.39887 ? 180 ASN B CB  1 
ATOM   3633 C CG  . ASN B 1 180 ? 21.47662  -0.84702  10.17377  1.000 27.80841 ? 180 ASN B CG  1 
ATOM   3634 O OD1 . ASN B 1 180 ? 21.39814  -0.92895  8.94778   1.000 34.16901 ? 180 ASN B OD1 1 
ATOM   3635 N ND2 . ASN B 1 180 ? 22.34967  -1.54441  10.88417  1.000 30.64795 ? 180 ASN B ND2 1 
ATOM   3636 N N   . PHE B 1 181 ? 19.33251  0.27189   14.17975  1.000 23.80088 ? 181 PHE B N   1 
ATOM   3637 C CA  . PHE B 1 181 ? 18.66246  1.15572   15.11368  1.000 22.88399 ? 181 PHE B CA  1 
ATOM   3638 C C   . PHE B 1 181 ? 18.81989  2.60272   14.67603  1.000 26.39183 ? 181 PHE B C   1 
ATOM   3639 O O   . PHE B 1 181 ? 19.84345  2.99747   14.11154  1.000 25.32647 ? 181 PHE B O   1 
ATOM   3640 C CB  . PHE B 1 181 ? 19.20908  0.98326   16.53783  1.000 25.10345 ? 181 PHE B CB  1 
ATOM   3641 C CG  . PHE B 1 181 ? 18.35929  0.09839   17.40237  1.000 26.68165 ? 181 PHE B CG  1 
ATOM   3642 C CD1 . PHE B 1 181 ? 17.30584  0.62435   18.13730  1.000 24.29664 ? 181 PHE B CD1 1 
ATOM   3643 C CD2 . PHE B 1 181 ? 18.59821  -1.26864  17.45858  1.000 25.64139 ? 181 PHE B CD2 1 
ATOM   3644 C CE1 . PHE B 1 181 ? 16.51256  -0.20610  18.93470  1.000 23.89749 ? 181 PHE B CE1 1 
ATOM   3645 C CE2 . PHE B 1 181 ? 17.81348  -2.09800  18.23302  1.000 22.89783 ? 181 PHE B CE2 1 
ATOM   3646 C CZ  . PHE B 1 181 ? 16.76781  -1.57393  18.97338  1.000 23.87159 ? 181 PHE B CZ  1 
ATOM   3647 N N   . TYR B 1 182 ? 17.77380  3.37943   14.90695  1.000 22.69053 ? 182 TYR B N   1 
ATOM   3648 C CA  . TYR B 1 182 ? 17.89184  4.82825   14.95169  1.000 25.56547 ? 182 TYR B CA  1 
ATOM   3649 C C   . TYR B 1 182 ? 18.44208  5.17744   16.32304  1.000 24.10524 ? 182 TYR B C   1 
ATOM   3650 O O   . TYR B 1 182 ? 17.88084  4.75585   17.33845  1.000 27.60967 ? 182 TYR B O   1 
ATOM   3651 C CB  . TYR B 1 182 ? 16.53438  5.49688   14.71231  1.000 22.41293 ? 182 TYR B CB  1 
ATOM   3652 C CG  . TYR B 1 182 ? 15.99882  5.36028   13.29918  1.000 26.46218 ? 182 TYR B CG  1 
ATOM   3653 C CD1 . TYR B 1 182 ? 16.44424  6.21713   12.28312  1.000 29.23734 ? 182 TYR B CD1 1 
ATOM   3654 C CD2 . TYR B 1 182 ? 15.03679  4.40327   12.97657  1.000 22.24379 ? 182 TYR B CD2 1 
ATOM   3655 C CE1 . TYR B 1 182 ? 15.97222  6.10456   10.98732  1.000 27.38049 ? 182 TYR B CE1 1 
ATOM   3656 C CE2 . TYR B 1 182 ? 14.55997  4.28543   11.68822  1.000 21.07021 ? 182 TYR B CE2 1 
ATOM   3657 C CZ  . TYR B 1 182 ? 15.02626  5.14119   10.69700  1.000 24.69822 ? 182 TYR B CZ  1 
ATOM   3658 O OH  . TYR B 1 182 ? 14.55781  5.04349   9.40524   1.000 24.94614 ? 182 TYR B OH  1 
ATOM   3659 N N   . GLY B 1 183 ? 19.56565  5.89355   16.35885  1.000 29.11341 ? 183 GLY B N   1 
ATOM   3660 C CA  . GLY B 1 183 ? 20.15316  6.28909   17.61405  1.000 26.57147 ? 183 GLY B CA  1 
ATOM   3661 C C   . GLY B 1 183 ? 21.09723  5.24216   18.17889  1.000 29.97853 ? 183 GLY B C   1 
ATOM   3662 O O   . GLY B 1 183 ? 21.33064  4.18668   17.57906  1.000 29.30527 ? 183 GLY B O   1 
ATOM   3663 N N   . PRO B 1 184 ? 21.65394  5.52066   19.35673  1.000 31.65524 ? 184 PRO B N   1 
ATOM   3664 C CA  . PRO B 1 184 ? 22.66393  4.62143   19.94075  1.000 31.70928 ? 184 PRO B CA  1 
ATOM   3665 C C   . PRO B 1 184 ? 22.07047  3.55782   20.85235  1.000 31.84657 ? 184 PRO B C   1 
ATOM   3666 O O   . PRO B 1 184 ? 22.60860  3.30283   21.93246  1.000 43.34383 ? 184 PRO B O   1 
ATOM   3667 C CB  . PRO B 1 184 ? 23.53750  5.58329   20.74201  1.000 34.99175 ? 184 PRO B CB  1 
ATOM   3668 C CG  . PRO B 1 184 ? 22.51882  6.58217   21.27254  1.000 40.22327 ? 184 PRO B CG  1 
ATOM   3669 C CD  . PRO B 1 184 ? 21.47603  6.74114   20.16372  1.000 33.27584 ? 184 PRO B CD  1 
ATOM   3670 N N   . PHE B 1 185 ? 20.95246  2.96044   20.46520  1.000 27.89236 ? 185 PHE B N   1 
ATOM   3671 C CA  . PHE B 1 185 ? 20.25564  1.99793   21.30551  1.000 30.14713 ? 185 PHE B CA  1 
ATOM   3672 C C   . PHE B 1 185 ? 20.54999  0.57408   20.85073  1.000 30.18132 ? 185 PHE B C   1 
ATOM   3673 O O   . PHE B 1 185 ? 20.95015  0.33936   19.70905  1.000 27.50681 ? 185 PHE B O   1 
ATOM   3674 C CB  . PHE B 1 185 ? 18.74894  2.28476   21.28128  1.000 27.76225 ? 185 PHE B CB  1 
ATOM   3675 C CG  . PHE B 1 185 ? 18.42641  3.71424   21.61695  1.000 22.38661 ? 185 PHE B CG  1 
ATOM   3676 C CD1 . PHE B 1 185 ? 18.67317  4.20882   22.89922  1.000 28.86926 ? 185 PHE B CD1 1 
ATOM   3677 C CD2 . PHE B 1 185 ? 17.94253  4.57747   20.65576  1.000 26.24198 ? 185 PHE B CD2 1 
ATOM   3678 C CE1 . PHE B 1 185 ? 18.40495  5.53719   23.21194  1.000 31.85476 ? 185 PHE B CE1 1 
ATOM   3679 C CE2 . PHE B 1 185 ? 17.67409  5.90958   20.96583  1.000 29.16865 ? 185 PHE B CE2 1 
ATOM   3680 C CZ  . PHE B 1 185 ? 17.91148  6.38707   22.24574  1.000 29.05745 ? 185 PHE B CZ  1 
ATOM   3681 N N   . VAL B 1 186 ? 20.35968  -0.38000  21.77384  1.000 24.06583 ? 186 VAL B N   1 
ATOM   3682 C CA  . VAL B 1 186 ? 20.56357  -1.79641  21.48849  1.000 28.72163 ? 186 VAL B CA  1 
ATOM   3683 C C   . VAL B 1 186 ? 19.37673  -2.58624  22.02194  1.000 24.26633 ? 186 VAL B C   1 
ATOM   3684 O O   . VAL B 1 186 ? 18.72859  -2.18131  22.99156  1.000 26.31726 ? 186 VAL B O   1 
ATOM   3685 C CB  . VAL B 1 186 ? 21.88680  -2.31804  22.08526  1.000 30.21162 ? 186 VAL B CB  1 
ATOM   3686 C CG1 . VAL B 1 186 ? 23.05416  -1.57482  21.45154  1.000 25.33181 ? 186 VAL B CG1 1 
ATOM   3687 C CG2 . VAL B 1 186 ? 21.89050  -2.15240  23.61445  1.000 30.30808 ? 186 VAL B CG2 1 
ATOM   3688 N N   . ASP B 1 187 ? 19.05970  -3.69738  21.35104  1.000 26.80118 ? 187 ASP B N   1 
ATOM   3689 C CA  . ASP B 1 187 ? 17.89598  -4.50329  21.73010  1.000 26.59055 ? 187 ASP B CA  1 
ATOM   3690 C C   . ASP B 1 187 ? 18.28420  -5.49499  22.83474  1.000 29.45139 ? 187 ASP B C   1 
ATOM   3691 O O   . ASP B 1 187 ? 18.34348  -6.71795  22.66216  1.000 31.51583 ? 187 ASP B O   1 
ATOM   3692 C CB  . ASP B 1 187 ? 17.26091  -5.17853  20.50826  1.000 29.43914 ? 187 ASP B CB  1 
ATOM   3693 C CG  . ASP B 1 187 ? 18.24615  -5.97268  19.62207  1.000 27.62930 ? 187 ASP B CG  1 
ATOM   3694 O OD1 . ASP B 1 187 ? 19.48399  -5.87080  19.78002  1.000 28.42167 ? 187 ASP B OD1 1 
ATOM   3695 O OD2 . ASP B 1 187 ? 17.74031  -6.71633  18.73036  1.000 26.10911 ? 187 ASP B OD2 1 
ATOM   3696 N N   . ARG B 1 188 ? 18.54215  -4.91289  24.00412  1.000 28.08491 ? 188 ARG B N   1 
ATOM   3697 C CA  . ARG B 1 188 ? 18.85604  -5.63470  25.22739  1.000 27.63379 ? 188 ARG B CA  1 
ATOM   3698 C C   . ARG B 1 188 ? 18.16171  -4.94734  26.39085  1.000 29.86657 ? 188 ARG B C   1 
ATOM   3699 O O   . ARG B 1 188 ? 18.10492  -3.71578  26.44478  1.000 30.18655 ? 188 ARG B O   1 
ATOM   3700 C CB  . ARG B 1 188 ? 20.36910  -5.68409  25.47942  1.000 31.07366 ? 188 ARG B CB  1 
ATOM   3701 C CG  . ARG B 1 188 ? 20.72396  -6.34990  26.79337  1.000 36.08979 ? 188 ARG B CG  1 
ATOM   3702 C CD  . ARG B 1 188 ? 22.21416  -6.30027  27.06136  1.000 43.17709 ? 188 ARG B CD  1 
ATOM   3703 N NE  . ARG B 1 188 ? 22.53887  -6.81236  28.38780  1.000 42.53477 ? 188 ARG B NE  1 
ATOM   3704 C CZ  . ARG B 1 188 ? 23.75727  -6.79934  28.91033  1.000 44.34213 ? 188 ARG B CZ  1 
ATOM   3705 N NH1 . ARG B 1 188 ? 24.78882  -6.31832  28.23958  1.000 49.38968 ? 188 ARG B NH1 1 
ATOM   3706 N NH2 . ARG B 1 188 ? 23.94414  -7.28006  30.13539  1.000 37.53043 ? 188 ARG B NH2 1 
ATOM   3707 N N   . GLN B 1 189 ? 17.63716  -5.73751  27.32960  1.000 28.80252 ? 189 GLN B N   1 
ATOM   3708 C CA  . GLN B 1 189 ? 16.92150  -5.16732  28.47442  1.000 30.45692 ? 189 GLN B CA  1 
ATOM   3709 C C   . GLN B 1 189 ? 17.94663  -4.76982  29.53197  1.000 34.65503 ? 189 GLN B C   1 
ATOM   3710 O O   . GLN B 1 189 ? 18.24113  -5.49757  30.48525  1.000 34.92982 ? 189 GLN B O   1 
ATOM   3711 C CB  . GLN B 1 189 ? 15.87836  -6.13728  29.01187  1.000 37.33080 ? 189 GLN B CB  1 
ATOM   3712 C CG  . GLN B 1 189 ? 14.92844  -5.51862  30.04189  1.000 32.95290 ? 189 GLN B CG  1 
ATOM   3713 C CD  . GLN B 1 189 ? 13.59911  -6.22995  30.08614  1.000 29.01717 ? 189 GLN B CD  1 
ATOM   3714 O OE1 . GLN B 1 189 ? 13.39918  -7.22776  29.40213  1.000 32.86553 ? 189 GLN B OE1 1 
ATOM   3715 N NE2 . GLN B 1 189 ? 12.68100  -5.72307  30.89066  1.000 37.51974 ? 189 GLN B NE2 1 
ATOM   3716 N N   . ILE B 1 190 ? 18.50323  -3.57714  29.33305  1.000 34.23897 ? 190 ILE B N   1 
ATOM   3717 C CA  A ILE B 1 190 ? 19.51308  -2.99738  30.20756  0.500 33.98329 ? 190 ILE B CA  1 
ATOM   3718 C CA  B ILE B 1 190 ? 19.50159  -3.00199  30.21855  0.500 33.98067 ? 190 ILE B CA  1 
ATOM   3719 C C   . ILE B 1 190 ? 19.28083  -1.49748  30.23179  1.000 38.84480 ? 190 ILE B C   1 
ATOM   3720 O O   . ILE B 1 190 ? 18.74899  -0.92836  29.27997  1.000 32.99818 ? 190 ILE B O   1 
ATOM   3721 C CB  A ILE B 1 190 ? 20.94931  -3.29183  29.72300  0.500 38.01886 ? 190 ILE B CB  1 
ATOM   3722 C CB  B ILE B 1 190 ? 20.93258  -3.34549  29.75305  0.500 37.99773 ? 190 ILE B CB  1 
ATOM   3723 C CG1 A ILE B 1 190 ? 21.04745  -3.05456  28.21121  0.500 35.68592 ? 190 ILE B CG1 1 
ATOM   3724 C CG1 B ILE B 1 190 ? 21.94835  -3.01353  30.84457  0.500 37.90109 ? 190 ILE B CG1 1 
ATOM   3725 C CG2 A ILE B 1 190 ? 21.38107  -4.68802  30.13042  0.500 40.41990 ? 190 ILE B CG2 1 
ATOM   3726 C CG2 B ILE B 1 190 ? 21.26641  -2.58911  28.47494  0.500 35.16482 ? 190 ILE B CG2 1 
ATOM   3727 C CD1 A ILE B 1 190 ? 22.42199  -2.64369  27.73101  0.500 36.08690 ? 190 ILE B CD1 1 
ATOM   3728 C CD1 B ILE B 1 190 ? 23.36793  -3.36563  30.46749  0.500 40.22148 ? 190 ILE B CD1 1 
ATOM   3729 N N   . ALA B 1 191 ? 19.71809  -0.85840  31.31532  1.000 36.97071 ? 191 ALA B N   1 
ATOM   3730 C CA  . ALA B 1 191 ? 19.54798  0.58372   31.46050  1.000 39.92766 ? 191 ALA B CA  1 
ATOM   3731 C C   . ALA B 1 191 ? 20.03563  1.32849   30.22367  1.000 33.57546 ? 191 ALA B C   1 
ATOM   3732 O O   . ALA B 1 191 ? 21.19531  1.20277   29.82027  1.000 33.22056 ? 191 ALA B O   1 
ATOM   3733 C CB  . ALA B 1 191 ? 20.29524  1.06774   32.70314  1.000 36.14139 ? 191 ALA B CB  1 
ATOM   3734 N N   . GLN B 1 192 ? 19.13550  2.09484   29.61434  1.000 35.93566 ? 192 GLN B N   1 
ATOM   3735 C CA  . GLN B 1 192 ? 19.47036  2.93712   28.47827  1.000 29.93460 ? 192 GLN B CA  1 
ATOM   3736 C C   . GLN B 1 192 ? 18.68981  4.23554   28.60139  1.000 28.55328 ? 192 GLN B C   1 
ATOM   3737 O O   . GLN B 1 192 ? 17.59109  4.25614   29.16007  1.000 36.72928 ? 192 GLN B O   1 
ATOM   3738 C CB  . GLN B 1 192 ? 19.15620  2.24569   27.14299  1.000 35.12364 ? 192 GLN B CB  1 
ATOM   3739 C CG  . GLN B 1 192 ? 20.02048  1.03573   26.85543  1.000 35.44868 ? 192 GLN B CG  1 
ATOM   3740 C CD  . GLN B 1 192 ? 19.62843  0.32433   25.57835  1.000 33.39166 ? 192 GLN B CD  1 
ATOM   3741 O OE1 . GLN B 1 192 ? 19.81544  0.84857   24.47968  1.000 32.88383 ? 192 GLN B OE1 1 
ATOM   3742 N NE2 . GLN B 1 192 ? 19.08381  -0.88597  25.71600  1.000 30.11570 ? 192 GLN B NE2 1 
ATOM   3743 N N   . ALA B 1 193 ? 19.25466  5.32063   28.07948  1.000 29.63384 ? 193 ALA B N   1 
ATOM   3744 C CA  . ALA B 1 193 ? 18.62280  6.62646   28.23704  1.000 34.59305 ? 193 ALA B CA  1 
ATOM   3745 C C   . ALA B 1 193 ? 18.69146  7.42993   26.94831  1.000 33.12902 ? 193 ALA B C   1 
ATOM   3746 O O   . ALA B 1 193 ? 19.71620  7.43463   26.26489  1.000 32.71363 ? 193 ALA B O   1 
ATOM   3747 C CB  . ALA B 1 193 ? 19.27597  7.43949   29.35924  1.000 37.91915 ? 193 ALA B CB  1 
ATOM   3748 N N   . ALA B 1 194 ? 17.60523  8.13763   26.64685  1.000 30.75245 ? 194 ALA B N   1 
ATOM   3749 C CA  . ALA B 1 194 ? 17.61391  9.06726   25.52398  1.000 35.90951 ? 194 ALA B CA  1 
ATOM   3750 C C   . ALA B 1 194 ? 18.48451  10.28029  25.83408  1.000 41.70339 ? 194 ALA B C   1 
ATOM   3751 O O   . ALA B 1 194 ? 18.51099  10.77355  26.96585  1.000 41.38763 ? 194 ALA B O   1 
ATOM   3752 C CB  . ALA B 1 194 ? 16.19128  9.52156   25.20106  1.000 33.89404 ? 194 ALA B CB  1 
ATOM   3753 N N   . GLY B 1 195 ? 19.20869  10.75801  24.82506  1.000 38.27864 ? 195 GLY B N   1 
ATOM   3754 C CA  . GLY B 1 195 ? 19.92208  12.00945  24.96546  1.000 40.07467 ? 195 GLY B CA  1 
ATOM   3755 C C   . GLY B 1 195 ? 18.96754  13.18384  25.10440  1.000 38.20238 ? 195 GLY B C   1 
ATOM   3756 O O   . GLY B 1 195 ? 17.75865  13.07527  24.89741  1.000 36.57478 ? 195 GLY B O   1 
ATOM   3757 N N   . THR B 1 196 ? 19.51834  14.33228  25.49801  1.000 40.66797 ? 196 THR B N   1 
ATOM   3758 C CA  . THR B 1 196 ? 18.69681  15.53286  25.60041  1.000 38.61414 ? 196 THR B CA  1 
ATOM   3759 C C   . THR B 1 196 ? 18.14423  15.88785  24.22500  1.000 33.81314 ? 196 THR B C   1 
ATOM   3760 O O   . THR B 1 196 ? 18.89359  15.96859  23.24937  1.000 34.18606 ? 196 THR B O   1 
ATOM   3761 C CB  . THR B 1 196 ? 19.50537  16.70850  26.15883  1.000 38.31307 ? 196 THR B CB  1 
ATOM   3762 O OG1 . THR B 1 196 ? 19.99823  16.38698  27.47047  1.000 47.64600 ? 196 THR B OG1 1 
ATOM   3763 C CG2 . THR B 1 196 ? 18.62787  17.92582  26.25781  1.000 43.40885 ? 196 THR B CG2 1 
ATOM   3764 N N   . ASP B 1 197 ? 16.83153  16.08765  24.14484  1.000 26.21522 ? 197 ASP B N   1 
ATOM   3765 C CA  . ASP B 1 197 ? 16.22294  16.38759  22.85874  1.000 26.70555 ? 197 ASP B CA  1 
ATOM   3766 C C   . ASP B 1 197 ? 16.32743  17.87814  22.54240  1.000 32.16358 ? 197 ASP B C   1 
ATOM   3767 O O   . ASP B 1 197 ? 16.58740  18.70955  23.41770  1.000 31.58098 ? 197 ASP B O   1 
ATOM   3768 C CB  . ASP B 1 197 ? 14.75819  15.95384  22.83591  1.000 26.92589 ? 197 ASP B CB  1 
ATOM   3769 C CG  . ASP B 1 197 ? 14.25285  15.70801  21.42148  1.000 32.00619 ? 197 ASP B CG  1 
ATOM   3770 O OD1 . ASP B 1 197 ? 15.10036  15.50366  20.52838  1.000 27.33387 ? 197 ASP B OD1 1 
ATOM   3771 O OD2 . ASP B 1 197 ? 13.02594  15.74695  21.19562  1.000 28.28234 ? 197 ASP B OD2 1 
ATOM   3772 N N   . THR B 1 198 ? 16.13767  18.20695  21.26318  1.000 27.21047 ? 198 THR B N   1 
ATOM   3773 C CA  . THR B 1 198 ? 16.10477  19.58414  20.77630  1.000 27.62156 ? 198 THR B CA  1 
ATOM   3774 C C   . THR B 1 198 ? 14.86090  19.79530  19.91538  1.000 25.02535 ? 198 THR B C   1 
ATOM   3775 O O   . THR B 1 198 ? 14.19661  18.83873  19.50157  1.000 29.54206 ? 198 THR B O   1 
ATOM   3776 C CB  . THR B 1 198 ? 17.35977  19.91626  19.95767  1.000 29.66741 ? 198 THR B CB  1 
ATOM   3777 O OG1 . THR B 1 198 ? 17.51833  18.93948  18.91885  1.000 29.77151 ? 198 THR B OG1 1 
ATOM   3778 C CG2 . THR B 1 198 ? 18.60795  19.93183  20.85061  1.000 34.93966 ? 198 THR B CG2 1 
ATOM   3779 N N   . THR B 1 199 ? 14.55659  21.06373  19.62098  1.000 25.13559 ? 199 THR B N   1 
ATOM   3780 C CA  . THR B 1 199 ? 13.41151  21.41608  18.78560  1.000 26.02390 ? 199 THR B CA  1 
ATOM   3781 C C   . THR B 1 199 ? 13.81496  21.38842  17.31444  1.000 22.19919 ? 199 THR B C   1 
ATOM   3782 O O   . THR B 1 199 ? 14.92730  21.78868  16.96359  1.000 23.85387 ? 199 THR B O   1 
ATOM   3783 C CB  . THR B 1 199 ? 12.86934  22.79354  19.17464  1.000 26.06051 ? 199 THR B CB  1 
ATOM   3784 O OG1 . THR B 1 199 ? 12.47702  22.76849  20.54843  1.000 28.31369 ? 199 THR B OG1 1 
ATOM   3785 C CG2 . THR B 1 199 ? 11.65342  23.18491  18.32850  1.000 24.41417 ? 199 THR B CG2 1 
ATOM   3786 N N   . ILE B 1 200 ? 12.90729  20.90537  16.46345  1.000 22.43714 ? 200 ILE B N   1 
ATOM   3787 C CA  . ILE B 1 200 ? 13.18913  20.66861  15.04158  1.000 23.59375 ? 200 ILE B CA  1 
ATOM   3788 C C   . ILE B 1 200 ? 12.96762  21.98275  14.29367  1.000 22.81853 ? 200 ILE B C   1 
ATOM   3789 O O   . ILE B 1 200 ? 11.83995  22.34834  13.97257  1.000 22.96541 ? 200 ILE B O   1 
ATOM   3790 C CB  . ILE B 1 200 ? 12.33140  19.53559  14.47016  1.000 22.57862 ? 200 ILE B CB  1 
ATOM   3791 C CG1 . ILE B 1 200 ? 12.52350  18.26132  15.31163  1.000 22.08005 ? 200 ILE B CG1 1 
ATOM   3792 C CG2 . ILE B 1 200 ? 12.66807  19.29021  12.98726  1.000 23.17956 ? 200 ILE B CG2 1 
ATOM   3793 C CD1 . ILE B 1 200 ? 11.38593  17.25660  15.14464  1.000 23.46862 ? 200 ILE B CD1 1 
ATOM   3794 N N   . THR B 1 201 ? 14.05897  22.69041  14.00557  1.000 22.70990 ? 201 THR B N   1 
ATOM   3795 C CA  . THR B 1 201 ? 13.96321  24.05298  13.49057  1.000 21.21651 ? 201 THR B CA  1 
ATOM   3796 C C   . THR B 1 201 ? 13.31787  24.09108  12.10711  1.000 22.98124 ? 201 THR B C   1 
ATOM   3797 O O   . THR B 1 201 ? 12.44536  24.93012  11.84866  1.000 22.82374 ? 201 THR B O   1 
ATOM   3798 C CB  . THR B 1 201 ? 15.35567  24.67891  13.47125  1.000 22.66564 ? 201 THR B CB  1 
ATOM   3799 O OG1 . THR B 1 201 ? 15.95022  24.53144  14.77187  1.000 25.64717 ? 201 THR B OG1 1 
ATOM   3800 C CG2 . THR B 1 201 ? 15.27160  26.18039  13.10940  1.000 22.28869 ? 201 THR B CG2 1 
ATOM   3801 N N   . VAL B 1 202 ? 13.69408  23.17140  11.21079  1.000 22.43247 ? 202 VAL B N   1 
ATOM   3802 C CA  . VAL B 1 202 ? 13.12923  23.22565  9.85964   1.000 23.56022 ? 202 VAL B CA  1 
ATOM   3803 C C   . VAL B 1 202 ? 11.60647  23.13711  9.91212   1.000 26.68447 ? 202 VAL B C   1 
ATOM   3804 O O   . VAL B 1 202 ? 10.90463  23.83548  9.16391   1.000 23.36819 ? 202 VAL B O   1 
ATOM   3805 C CB  . VAL B 1 202 ? 13.72565  22.12528  8.96566   1.000 23.97990 ? 202 VAL B CB  1 
ATOM   3806 C CG1 . VAL B 1 202 ? 13.31350  20.76256  9.47876   1.000 25.40179 ? 202 VAL B CG1 1 
ATOM   3807 C CG2 . VAL B 1 202 ? 13.24339  22.32322  7.51545   1.000 22.97382 ? 202 VAL B CG2 1 
ATOM   3808 N N   . ASN B 1 203 ? 11.07652  22.31316  10.82881  1.000 23.72264 ? 203 ASN B N   1 
ATOM   3809 C CA  . ASN B 1 203 ? 9.63175   22.13097  10.97403  1.000 23.79271 ? 203 ASN B CA  1 
ATOM   3810 C C   . ASN B 1 203 ? 8.95560   23.34448  11.59634  1.000 23.46733 ? 203 ASN B C   1 
ATOM   3811 O O   . ASN B 1 203 ? 7.83886   23.70128  11.20324  1.000 22.69748 ? 203 ASN B O   1 
ATOM   3812 C CB  . ASN B 1 203 ? 9.32445   20.89528  11.82595  1.000 22.43721 ? 203 ASN B CB  1 
ATOM   3813 C CG  . ASN B 1 203 ? 9.64965   19.61705  11.11435  1.000 22.70820 ? 203 ASN B CG  1 
ATOM   3814 O OD1 . ASN B 1 203 ? 10.11343  19.63845  9.98137   1.000 23.99844 ? 203 ASN B OD1 1 
ATOM   3815 N ND2 . ASN B 1 203 ? 9.41244   18.48958  11.77244  1.000 20.77225 ? 203 ASN B ND2 1 
ATOM   3816 N N   . VAL B 1 204 ? 9.57119   23.95245  12.60834  1.000 25.25724 ? 204 VAL B N   1 
ATOM   3817 C CA  . VAL B 1 204 ? 8.99686   25.18230  13.14449  1.000 26.42606 ? 204 VAL B CA  1 
ATOM   3818 C C   . VAL B 1 204 ? 8.87450   26.21051  12.03311  1.000 24.50775 ? 204 VAL B C   1 
ATOM   3819 O O   . VAL B 1 204 ? 7.82091   26.83756  11.84742  1.000 23.61113 ? 204 VAL B O   1 
ATOM   3820 C CB  . VAL B 1 204 ? 9.83000   25.70920  14.32457  1.000 26.67760 ? 204 VAL B CB  1 
ATOM   3821 C CG1 . VAL B 1 204 ? 9.33561   27.09110  14.73474  1.000 26.74765 ? 204 VAL B CG1 1 
ATOM   3822 C CG2 . VAL B 1 204 ? 9.73502   24.74638  15.50533  1.000 25.74376 ? 204 VAL B CG2 1 
ATOM   3823 N N   . LEU B 1 205 ? 9.93389   26.36376  11.23762  1.000 21.48307 ? 205 LEU B N   1 
ATOM   3824 C CA  . LEU B 1 205 ? 9.87095   27.28999  10.10418  1.000 23.51204 ? 205 LEU B CA  1 
ATOM   3825 C C   . LEU B 1 205 ? 8.71907   26.95728  9.15219   1.000 26.88223 ? 205 LEU B C   1 
ATOM   3826 O O   . LEU B 1 205 ? 7.99620   27.85719  8.69866   1.000 24.28634 ? 205 LEU B O   1 
ATOM   3827 C CB  . LEU B 1 205 ? 11.20723  27.28923  9.35077   1.000 22.35206 ? 205 LEU B CB  1 
ATOM   3828 C CG  . LEU B 1 205 ? 12.37452  27.86654  10.14930  1.000 21.11352 ? 205 LEU B CG  1 
ATOM   3829 C CD1 . LEU B 1 205 ? 13.70044  27.57708  9.45023   1.000 20.97335 ? 205 LEU B CD1 1 
ATOM   3830 C CD2 . LEU B 1 205 ? 12.20000  29.38600  10.43771  1.000 20.68504 ? 205 LEU B CD2 1 
ATOM   3831 N N   . ALA B 1 206 ? 8.54372   25.67765  8.80603   1.000 24.41976 ? 206 ALA B N   1 
ATOM   3832 C CA  . ALA B 1 206 ? 7.44652   25.31719  7.90708   1.000 21.50495 ? 206 ALA B CA  1 
ATOM   3833 C C   . ALA B 1 206 ? 6.11354   25.70209  8.51292   1.000 26.92644 ? 206 ALA B C   1 
ATOM   3834 O O   . ALA B 1 206 ? 5.17393   26.07966  7.80195   1.000 25.61418 ? 206 ALA B O   1 
ATOM   3835 C CB  . ALA B 1 206 ? 7.47138   23.81641  7.61125   1.000 22.73255 ? 206 ALA B CB  1 
ATOM   3836 N N   . TRP B 1 207 ? 6.01322   25.60002  9.83351   1.000 22.65508 ? 207 TRP B N   1 
ATOM   3837 C CA  . TRP B 1 207 ? 4.76675   25.93060  10.50594  1.000 28.78158 ? 207 TRP B CA  1 
ATOM   3838 C C   . TRP B 1 207 ? 4.52038   27.43774  10.46936  1.000 26.41039 ? 207 TRP B C   1 
ATOM   3839 O O   . TRP B 1 207 ? 3.37864   27.88682  10.31820  1.000 25.81609 ? 207 TRP B O   1 
ATOM   3840 C CB  . TRP B 1 207 ? 4.83109   25.38956  11.92932  1.000 24.91065 ? 207 TRP B CB  1 
ATOM   3841 C CG  . TRP B 1 207 ? 3.52776   25.39131  12.66275  1.000 30.86798 ? 207 TRP B CG  1 
ATOM   3842 C CD1 . TRP B 1 207 ? 2.46683   24.54107  12.48175  1.000 27.30821 ? 207 TRP B CD1 1 
ATOM   3843 C CD2 . TRP B 1 207 ? 3.17114   26.26141  13.72956  1.000 28.76714 ? 207 TRP B CD2 1 
ATOM   3844 N NE1 . TRP B 1 207 ? 1.45878   24.85759  13.36504  1.000 38.78171 ? 207 TRP B NE1 1 
ATOM   3845 C CE2 . TRP B 1 207 ? 1.86974   25.91083  14.14077  1.000 29.70955 ? 207 TRP B CE2 1 
ATOM   3846 C CE3 . TRP B 1 207 ? 3.81686   27.32121  14.36360  1.000 33.57399 ? 207 TRP B CE3 1 
ATOM   3847 C CZ2 . TRP B 1 207 ? 1.21155   26.57939  15.16627  1.000 41.59764 ? 207 TRP B CZ2 1 
ATOM   3848 C CZ3 . TRP B 1 207 ? 3.16396   27.98203  15.38233  1.000 38.89161 ? 207 TRP B CZ3 1 
ATOM   3849 C CH2 . TRP B 1 207 ? 1.87830   27.60807  15.77821  1.000 44.31244 ? 207 TRP B CH2 1 
ATOM   3850 N N   . LEU B 1 208 ? 5.58712   28.23283  10.55373  1.000 24.07025 ? 208 LEU B N   1 
ATOM   3851 C CA  . LEU B 1 208 ? 5.43791   29.67778  10.40523  1.000 24.71307 ? 208 LEU B CA  1 
ATOM   3852 C C   . LEU B 1 208 ? 5.04035   30.04939  8.97806   1.000 25.06673 ? 208 LEU B C   1 
ATOM   3853 O O   . LEU B 1 208 ? 4.24676   30.97219  8.77330   1.000 27.15157 ? 208 LEU B O   1 
ATOM   3854 C CB  . LEU B 1 208 ? 6.72699   30.39202  10.78939  1.000 24.65128 ? 208 LEU B CB  1 
ATOM   3855 C CG  . LEU B 1 208 ? 7.19030   30.26308  12.25127  1.000 26.50009 ? 208 LEU B CG  1 
ATOM   3856 C CD1 . LEU B 1 208 ? 8.54124   30.94205  12.42789  1.000 22.78924 ? 208 LEU B CD1 1 
ATOM   3857 C CD2 . LEU B 1 208 ? 6.13888   30.82439  13.20766  1.000 28.60735 ? 208 LEU B CD2 1 
ATOM   3858 N N   . TYR B 1 209 ? 5.58496   29.35191  7.97801   1.000 26.93277 ? 209 TYR B N   1 
ATOM   3859 C CA  . TYR B 1 209 ? 5.14017   29.56960  6.60198   1.000 26.82139 ? 209 TYR B CA  1 
ATOM   3860 C C   . TYR B 1 209 ? 3.65497   29.23711  6.45226   1.000 27.46415 ? 209 TYR B C   1 
ATOM   3861 O O   . TYR B 1 209 ? 2.88199   30.00595  5.86278   1.000 29.91783 ? 209 TYR B O   1 
ATOM   3862 C CB  . TYR B 1 209 ? 5.98628   28.72837  5.65008   1.000 24.53275 ? 209 TYR B CB  1 
ATOM   3863 C CG  . TYR B 1 209 ? 7.28480   29.38543  5.23835   1.000 23.77598 ? 209 TYR B CG  1 
ATOM   3864 C CD1 . TYR B 1 209 ? 7.28622   30.53118  4.44043   1.000 26.62306 ? 209 TYR B CD1 1 
ATOM   3865 C CD2 . TYR B 1 209 ? 8.50985   28.83218  5.59088   1.000 27.54354 ? 209 TYR B CD2 1 
ATOM   3866 C CE1 . TYR B 1 209 ? 8.48853   31.13424  4.04522   1.000 26.10231 ? 209 TYR B CE1 1 
ATOM   3867 C CE2 . TYR B 1 209 ? 9.72081   29.42482  5.19932   1.000 24.13243 ? 209 TYR B CE2 1 
ATOM   3868 C CZ  . TYR B 1 209 ? 9.69091   30.58108  4.42951   1.000 25.30827 ? 209 TYR B CZ  1 
ATOM   3869 O OH  . TYR B 1 209 ? 10.86222  31.16950  4.02481   1.000 24.20827 ? 209 TYR B OH  1 
ATOM   3870 N N   . ALA B 1 210 ? 3.23722   28.09590  6.99927   1.000 30.17796 ? 210 ALA B N   1 
ATOM   3871 C CA  . ALA B 1 210 ? 1.81751   27.74935  7.04270   1.000 25.16981 ? 210 ALA B CA  1 
ATOM   3872 C C   . ALA B 1 210 ? 0.98813   28.87526  7.64831   1.000 25.73455 ? 210 ALA B C   1 
ATOM   3873 O O   . ALA B 1 210 ? -0.10385  29.19104  7.16291   1.000 30.65043 ? 210 ALA B O   1 
ATOM   3874 C CB  . ALA B 1 210 ? 1.61847   26.46496  7.84817   1.000 28.95153 ? 210 ALA B CB  1 
ATOM   3875 N N   . ALA B 1 211 ? 1.45720   29.44088  8.76017   1.000 28.29139 ? 211 ALA B N   1 
ATOM   3876 C CA  . ALA B 1 211 ? 0.72614   30.53570  9.38709   1.000 34.26957 ? 211 ALA B CA  1 
ATOM   3877 C C   . ALA B 1 211 ? 0.57310   31.70296  8.42567   1.000 28.21386 ? 211 ALA B C   1 
ATOM   3878 O O   . ALA B 1 211 ? -0.50205  32.30545  8.33402   1.000 29.05335 ? 211 ALA B O   1 
ATOM   3879 C CB  . ALA B 1 211 ? 1.43882   30.99316  10.65998  1.000 25.73200 ? 211 ALA B CB  1 
ATOM   3880 N N   . VAL B 1 212 ? 1.64904   32.04532  7.71617   1.000 24.17807 ? 212 VAL B N   1 
ATOM   3881 C CA  . VAL B 1 212 ? 1.60200   33.15450  6.76741   1.000 24.18225 ? 212 VAL B CA  1 
ATOM   3882 C C   . VAL B 1 212 ? 0.61606   32.84867  5.65065   1.000 30.20453 ? 212 VAL B C   1 
ATOM   3883 O O   . VAL B 1 212 ? -0.16848  33.71278  5.24137   1.000 27.41793 ? 212 VAL B O   1 
ATOM   3884 C CB  . VAL B 1 212 ? 3.01269   33.45274  6.22038   1.000 27.37688 ? 212 VAL B CB  1 
ATOM   3885 C CG1 . VAL B 1 212 ? 2.96665   34.58199  5.21137   1.000 27.53000 ? 212 VAL B CG1 1 
ATOM   3886 C CG2 . VAL B 1 212 ? 3.94908   33.81796  7.36683   1.000 31.36640 ? 212 VAL B CG2 1 
ATOM   3887 N N   . ILE B 1 213 ? 0.63050   31.60752  5.15084   1.000 28.21206 ? 213 ILE B N   1 
ATOM   3888 C CA  . ILE B 1 213 ? -0.28906  31.22246  4.08808   1.000 27.75834 ? 213 ILE B CA  1 
ATOM   3889 C C   . ILE B 1 213 ? -1.72724  31.44821  4.51736   1.000 28.84259 ? 213 ILE B C   1 
ATOM   3890 O O   . ILE B 1 213 ? -2.56311  31.87764  3.71813   1.000 28.44089 ? 213 ILE B O   1 
ATOM   3891 C CB  . ILE B 1 213 ? -0.04475  29.76248  3.67854   1.000 26.08003 ? 213 ILE B CB  1 
ATOM   3892 C CG1 . ILE B 1 213 ? 1.28640   29.66488  2.91216   1.000 27.41759 ? 213 ILE B CG1 1 
ATOM   3893 C CG2 . ILE B 1 213 ? -1.21581  29.24518  2.86966   1.000 28.22894 ? 213 ILE B CG2 1 
ATOM   3894 C CD1 . ILE B 1 213 ? 1.68755   28.23940  2.54204   1.000 29.02676 ? 213 ILE B CD1 1 
ATOM   3895 N N   . ASN B 1 214 ? -2.03547  31.19326  5.78816   1.000 30.69087 ? 214 ASN B N   1 
ATOM   3896 C CA  . ASN B 1 214 ? -3.37932  31.40449  6.31435   1.000 30.50906 ? 214 ASN B CA  1 
ATOM   3897 C C   . ASN B 1 214 ? -3.63175  32.83804  6.76287   1.000 28.88673 ? 214 ASN B C   1 
ATOM   3898 O O   . ASN B 1 214 ? -4.67681  33.10630  7.35778   1.000 35.63606 ? 214 ASN B O   1 
ATOM   3899 C CB  . ASN B 1 214 ? -3.64849  30.44044  7.47520   1.000 31.99065 ? 214 ASN B CB  1 
ATOM   3900 C CG  . ASN B 1 214 ? -3.86721  29.02585  6.99472   1.000 45.81016 ? 214 ASN B CG  1 
ATOM   3901 O OD1 . ASN B 1 214 ? -4.98865  28.63863  6.67113   1.000 53.08815 ? 214 ASN B OD1 1 
ATOM   3902 N ND2 . ASN B 1 214 ? -2.79002  28.25570  6.90662   1.000 42.01413 ? 214 ASN B ND2 1 
ATOM   3903 N N   . GLY B 1 215 ? -2.71318  33.75995  6.49424   1.000 28.87077 ? 215 GLY B N   1 
ATOM   3904 C CA  . GLY B 1 215 ? -2.91877  35.15874  6.83441   1.000 30.41116 ? 215 GLY B CA  1 
ATOM   3905 C C   . GLY B 1 215 ? -2.49267  35.57961  8.22602   1.000 33.49072 ? 215 GLY B C   1 
ATOM   3906 O O   . GLY B 1 215 ? -2.79101  36.71046  8.62889   1.000 36.48683 ? 215 GLY B O   1 
ATOM   3907 N N   . ASP B 1 216 ? -1.78678  34.72396  8.96644   1.000 29.72358 ? 216 ASP B N   1 
ATOM   3908 C CA  . ASP B 1 216 ? -1.33270  35.02598  10.32906  1.000 31.79694 ? 216 ASP B CA  1 
ATOM   3909 C C   . ASP B 1 216 ? 0.15477   35.36314  10.24697  1.000 34.82330 ? 216 ASP B C   1 
ATOM   3910 O O   . ASP B 1 216 ? 0.99814   34.46525  10.14780  1.000 36.42119 ? 216 ASP B O   1 
ATOM   3911 C CB  . ASP B 1 216 ? -1.59269  33.83710  11.24817  1.000 30.90531 ? 216 ASP B CB  1 
ATOM   3912 C CG  . ASP B 1 216 ? -1.70028  34.23366  12.71551  1.000 40.86428 ? 216 ASP B CG  1 
ATOM   3913 O OD1 . ASP B 1 216 ? -1.53514  35.42811  13.03972  1.000 42.14404 ? 216 ASP B OD1 1 
ATOM   3914 O OD2 . ASP B 1 216 ? -1.96379  33.34291  13.54535  1.000 40.22764 ? 216 ASP B OD2 1 
ATOM   3915 N N   . ARG B 1 217 ? 0.48646   36.66042  10.27542  1.000 32.83266 ? 217 ARG B N   1 
ATOM   3916 C CA  . ARG B 1 217 ? 1.84229   37.06906  9.91261   1.000 34.13454 ? 217 ARG B CA  1 
ATOM   3917 C C   . ARG B 1 217 ? 2.33697   38.25464  10.73488  1.000 35.78904 ? 217 ARG B C   1 
ATOM   3918 O O   . ARG B 1 217 ? 3.22274   38.99987  10.29657  1.000 30.60147 ? 217 ARG B O   1 
ATOM   3919 C CB  . ARG B 1 217 ? 1.91942   37.39717  8.42116   1.000 39.40254 ? 217 ARG B CB  1 
ATOM   3920 C CG  . ARG B 1 217 ? 0.82550   38.33045  7.96681   1.000 33.42517 ? 217 ARG B CG  1 
ATOM   3921 C CD  . ARG B 1 217 ? 0.91996   38.63226  6.48718   1.000 35.12029 ? 217 ARG B CD  1 
ATOM   3922 N NE  . ARG B 1 217 ? 0.01985   39.72103  6.13227   1.000 38.03415 ? 217 ARG B NE  1 
ATOM   3923 C CZ  . ARG B 1 217 ? -1.22144  39.56110  5.69619   1.000 31.75414 ? 217 ARG B CZ  1 
ATOM   3924 N NH1 . ARG B 1 217 ? -1.74324  38.35741  5.51344   1.000 36.51293 ? 217 ARG B NH1 1 
ATOM   3925 N NH2 . ARG B 1 217 ? -1.96095  40.63571  5.44378   1.000 33.18213 ? 217 ARG B NH2 1 
ATOM   3926 N N   . TRP B 1 218 ? 1.81182   38.42714  11.94357  1.000 30.42607 ? 218 TRP B N   1 
ATOM   3927 C CA  . TRP B 1 218 ? 2.27061   39.53403  12.77196  1.000 34.64843 ? 218 TRP B CA  1 
ATOM   3928 C C   . TRP B 1 218 ? 3.74797   39.39983  13.12541  1.000 37.74457 ? 218 TRP B C   1 
ATOM   3929 O O   . TRP B 1 218 ? 4.42349   40.41059  13.35921  1.000 35.18145 ? 218 TRP B O   1 
ATOM   3930 C CB  . TRP B 1 218 ? 1.42355   39.60747  14.03778  1.000 34.26084 ? 218 TRP B CB  1 
ATOM   3931 C CG  . TRP B 1 218 ? 1.45603   38.34717  14.83000  1.000 37.06671 ? 218 TRP B CG  1 
ATOM   3932 C CD1 . TRP B 1 218 ? 0.60097   37.28958  14.72395  1.000 39.02907 ? 218 TRP B CD1 1 
ATOM   3933 C CD2 . TRP B 1 218 ? 2.39139   38.00633  15.87200  1.000 43.51400 ? 218 TRP B CD2 1 
ATOM   3934 N NE1 . TRP B 1 218 ? 0.94799   36.30584  15.62755  1.000 41.05919 ? 218 TRP B NE1 1 
ATOM   3935 C CE2 . TRP B 1 218 ? 2.03891   36.72563  16.34524  1.000 36.29061 ? 218 TRP B CE2 1 
ATOM   3936 C CE3 . TRP B 1 218 ? 3.49205   38.65959  16.44395  1.000 37.93111 ? 218 TRP B CE3 1 
ATOM   3937 C CZ2 . TRP B 1 218 ? 2.75113   36.08434  17.35728  1.000 39.88761 ? 218 TRP B CZ2 1 
ATOM   3938 C CZ3 . TRP B 1 218 ? 4.19406   38.02485  17.44608  1.000 42.13505 ? 218 TRP B CZ3 1 
ATOM   3939 C CH2 . TRP B 1 218 ? 3.82160   36.75150  17.89666  1.000 35.79714 ? 218 TRP B CH2 1 
ATOM   3940 N N   . PHE B 1 219 ? 4.26892   38.16594  13.16048  1.000 36.03273 ? 219 PHE B N   1 
ATOM   3941 C CA  . PHE B 1 219 ? 5.62134   37.87755  13.63607  1.000 30.91429 ? 219 PHE B CA  1 
ATOM   3942 C C   . PHE B 1 219 ? 6.71288   38.18867  12.62109  1.000 36.50724 ? 219 PHE B C   1 
ATOM   3943 O O   . PHE B 1 219 ? 7.89487   37.98517  12.92750  1.000 35.42936 ? 219 PHE B O   1 
ATOM   3944 C CB  . PHE B 1 219 ? 5.73183   36.40482  14.04668  1.000 32.30529 ? 219 PHE B CB  1 
ATOM   3945 C CG  . PHE B 1 219 ? 5.19129   35.45670  13.01979  1.000 30.80184 ? 219 PHE B CG  1 
ATOM   3946 C CD1 . PHE B 1 219 ? 5.98463   35.01562  11.97894  1.000 28.71279 ? 219 PHE B CD1 1 
ATOM   3947 C CD2 . PHE B 1 219 ? 3.88044   35.03123  13.08307  1.000 28.97255 ? 219 PHE B CD2 1 
ATOM   3948 C CE1 . PHE B 1 219 ? 5.48518   34.14908  11.02730  1.000 29.22522 ? 219 PHE B CE1 1 
ATOM   3949 C CE2 . PHE B 1 219 ? 3.36520   34.16888  12.13083  1.000 27.53314 ? 219 PHE B CE2 1 
ATOM   3950 C CZ  . PHE B 1 219 ? 4.17145   33.72270  11.10186  1.000 29.97145 ? 219 PHE B CZ  1 
ATOM   3951 N N   . LEU B 1 220 ? 6.36387   38.65526  11.43016  1.000 33.11014 ? 220 LEU B N   1 
ATOM   3952 C CA  . LEU B 1 220 ? 7.36294   38.93529  10.40746  1.000 41.78257 ? 220 LEU B CA  1 
ATOM   3953 C C   . LEU B 1 220 ? 8.03835   40.27223  10.69212  1.000 45.65749 ? 220 LEU B C   1 
ATOM   3954 O O   . LEU B 1 220 ? 7.36031   41.27602  10.92203  1.000 39.44906 ? 220 LEU B O   1 
ATOM   3955 C CB  . LEU B 1 220 ? 6.71158   38.95881  9.02124   1.000 36.64355 ? 220 LEU B CB  1 
ATOM   3956 C CG  . LEU B 1 220 ? 6.02030   37.68334  8.52323   1.000 32.68902 ? 220 LEU B CG  1 
ATOM   3957 C CD1 . LEU B 1 220 ? 5.36227   37.95320  7.18472   1.000 30.40280 ? 220 LEU B CD1 1 
ATOM   3958 C CD2 . LEU B 1 220 ? 6.99698   36.50447  8.40410   1.000 33.08831 ? 220 LEU B CD2 1 
ATOM   3959 N N   . ASN B 1 221 ? 9.36896   40.29139  10.67801  1.000 45.03969 ? 221 ASN B N   1 
ATOM   3960 C CA  . ASN B 1 221 ? 10.12002  41.53608  10.79736  1.000 42.16284 ? 221 ASN B CA  1 
ATOM   3961 C C   . ASN B 1 221 ? 10.75004  41.88608  9.45512   1.000 40.50822 ? 221 ASN B C   1 
ATOM   3962 O O   . ASN B 1 221 ? 10.73576  41.09598  8.50728   1.000 52.77358 ? 221 ASN B O   1 
ATOM   3963 C CB  . ASN B 1 221 ? 11.18616  41.45224  11.91100  1.000 43.23265 ? 221 ASN B CB  1 
ATOM   3964 C CG  . ASN B 1 221 ? 12.28330  40.42894  11.62395  1.000 34.37985 ? 221 ASN B CG  1 
ATOM   3965 O OD1 . ASN B 1 221 ? 12.45730  39.97812  10.49021  1.000 44.39484 ? 221 ASN B OD1 1 
ATOM   3966 N ND2 . ASN B 1 221 ? 13.03706  40.06942  12.66036  1.000 42.58642 ? 221 ASN B ND2 1 
ATOM   3967 N N   . ARG B 1 222 ? 11.30071  43.09853  9.37302   1.000 44.81832 ? 222 ARG B N   1 
ATOM   3968 C CA  . ARG B 1 222 ? 11.90786  43.58752  8.14038   1.000 44.51033 ? 222 ARG B CA  1 
ATOM   3969 C C   . ARG B 1 222 ? 13.40403  43.30358  8.06442   1.000 43.62827 ? 222 ARG B C   1 
ATOM   3970 O O   . ARG B 1 222 ? 14.12907  44.02462  7.36613   1.000 46.34195 ? 222 ARG B O   1 
ATOM   3971 C CB  . ARG B 1 222 ? 11.64556  45.08682  7.98285   1.000 53.69055 ? 222 ARG B CB  1 
ATOM   3972 N N   . PHE B 1 223 ? 13.88631  42.26991  8.75138   1.000 36.96318 ? 223 PHE B N   1 
ATOM   3973 C CA  . PHE B 1 223 ? 15.30680  41.96221  8.81901   1.000 29.55758 ? 223 PHE B CA  1 
ATOM   3974 C C   . PHE B 1 223 ? 15.57010  40.55475  8.29235   1.000 34.42276 ? 223 PHE B C   1 
ATOM   3975 O O   . PHE B 1 223 ? 14.65426  39.74970  8.10009   1.000 33.88877 ? 223 PHE B O   1 
ATOM   3976 C CB  . PHE B 1 223 ? 15.82644  42.09483  10.26026  1.000 38.44387 ? 223 PHE B CB  1 
ATOM   3977 N N   . THR B 1 224 ? 16.84897  40.26522  8.05348   1.000 33.70484 ? 224 THR B N   1 
ATOM   3978 C CA  . THR B 1 224 ? 17.29661  38.94184  7.63741   1.000 33.70093 ? 224 THR B CA  1 
ATOM   3979 C C   . THR B 1 224 ? 18.52767  38.56740  8.46592   1.000 32.38056 ? 224 THR B C   1 
ATOM   3980 O O   . THR B 1 224 ? 19.00354  39.34555  9.28727   1.000 30.55416 ? 224 THR B O   1 
ATOM   3981 C CB  . THR B 1 224 ? 17.56407  38.90307  6.12219   1.000 34.30533 ? 224 THR B CB  1 
ATOM   3982 O OG1 . THR B 1 224 ? 17.77762  37.55316  5.70370   1.000 32.70194 ? 224 THR B OG1 1 
ATOM   3983 C CG2 . THR B 1 224 ? 18.77882  39.73830  5.73653   1.000 30.78466 ? 224 THR B CG2 1 
ATOM   3984 N N   . THR B 1 225 ? 19.02121  37.34626  8.30111   1.000 33.64999 ? 225 THR B N   1 
ATOM   3985 C CA  . THR B 1 225 ? 20.22119  36.92534  9.00765   1.000 33.69602 ? 225 THR B CA  1 
ATOM   3986 C C   . THR B 1 225 ? 21.06162  36.06741  8.07666   1.000 33.00777 ? 225 THR B C   1 
ATOM   3987 O O   . THR B 1 225 ? 20.65190  35.73242  6.96259   1.000 32.37390 ? 225 THR B O   1 
ATOM   3988 C CB  . THR B 1 225 ? 19.89585  36.15082  10.30073  1.000 39.87471 ? 225 THR B CB  1 
ATOM   3989 O OG1 . THR B 1 225 ? 21.11687  35.74398  10.93376  1.000 33.60916 ? 225 THR B OG1 1 
ATOM   3990 C CG2 . THR B 1 225 ? 19.06770  34.90041  9.99511   1.000 32.04265 ? 225 THR B CG2 1 
ATOM   3991 N N   . THR B 1 226 ? 22.25739  35.71908  8.53339   1.000 32.05140 ? 226 THR B N   1 
ATOM   3992 C CA  . THR B 1 226 ? 23.05116  34.73032  7.82036   1.000 37.10656 ? 226 THR B CA  1 
ATOM   3993 C C   . THR B 1 226 ? 22.75285  33.34683  8.38531   1.000 34.31335 ? 226 THR B C   1 
ATOM   3994 O O   . THR B 1 226 ? 22.42444  33.19922  9.56610   1.000 28.90212 ? 226 THR B O   1 
ATOM   3995 C CB  . THR B 1 226 ? 24.55083  35.02616  7.92475   1.000 28.19365 ? 226 THR B CB  1 
ATOM   3996 O OG1 . THR B 1 226 ? 24.97774  34.87649  9.28678   1.000 38.32068 ? 226 THR B OG1 1 
ATOM   3997 C CG2 . THR B 1 226 ? 24.85060  36.44462  7.45068   1.000 41.16357 ? 226 THR B CG2 1 
ATOM   3998 N N   . LEU B 1 227 ? 22.85263  32.33111  7.52011   1.000 32.19590 ? 227 LEU B N   1 
ATOM   3999 C CA  . LEU B 1 227 ? 22.63171  30.96339  7.97564   1.000 31.65003 ? 227 LEU B CA  1 
ATOM   4000 C C   . LEU B 1 227 ? 23.57155  30.62341  9.11409   1.000 29.39729 ? 227 LEU B C   1 
ATOM   4001 O O   . LEU B 1 227 ? 23.16361  30.02802  10.11685  1.000 35.88008 ? 227 LEU B O   1 
ATOM   4002 C CB  . LEU B 1 227 ? 22.82156  29.97693  6.82580   1.000 35.77494 ? 227 LEU B CB  1 
ATOM   4003 C CG  . LEU B 1 227 ? 22.39224  28.53373  7.11635   1.000 36.20603 ? 227 LEU B CG  1 
ATOM   4004 C CD1 . LEU B 1 227 ? 20.91082  28.47551  7.47537   1.000 37.85065 ? 227 LEU B CD1 1 
ATOM   4005 C CD2 . LEU B 1 227 ? 22.68489  27.61744  5.93433   1.000 41.37175 ? 227 LEU B CD2 1 
ATOM   4006 N N   . ASN B 1 228 ? 24.83425  30.99917  8.98509   1.000 30.46938 ? 228 ASN B N   1 
ATOM   4007 C CA  . ASN B 1 228 ? 25.78417  30.64568  10.02849  1.000 34.18106 ? 228 ASN B CA  1 
ATOM   4008 C C   . ASN B 1 228 ? 25.45647  31.37376  11.32517  1.000 38.73432 ? 228 ASN B C   1 
ATOM   4009 O O   . ASN B 1 228 ? 25.53120  30.78760  12.41218  1.000 33.88055 ? 228 ASN B O   1 
ATOM   4010 C CB  . ASN B 1 228 ? 27.20956  30.94784  9.56589   1.000 35.91556 ? 228 ASN B CB  1 
ATOM   4011 C CG  . ASN B 1 228 ? 28.26664  30.40115  10.53021  1.000 39.03319 ? 228 ASN B CG  1 
ATOM   4012 O OD1 . ASN B 1 228 ? 28.90979  31.16923  11.25794  1.000 39.96947 ? 228 ASN B OD1 1 
ATOM   4013 N ND2 . ASN B 1 228 ? 28.42776  29.06196  10.55754  1.000 29.10803 ? 228 ASN B ND2 1 
ATOM   4014 N N   . ASP B 1 229 ? 25.06329  32.64379  11.23628  1.000 33.36795 ? 229 ASP B N   1 
ATOM   4015 C CA  . ASP B 1 229 ? 24.69576  33.35793  12.45158  1.000 29.86278 ? 229 ASP B CA  1 
ATOM   4016 C C   . ASP B 1 229 ? 23.44651  32.75688  13.07834  1.000 32.39252 ? 229 ASP B C   1 
ATOM   4017 O O   . ASP B 1 229 ? 23.37522  32.59538  14.30235  1.000 29.46861 ? 229 ASP B O   1 
ATOM   4018 C CB  . ASP B 1 229 ? 24.47914  34.84064  12.15868  1.000 39.37167 ? 229 ASP B CB  1 
ATOM   4019 C CG  . ASP B 1 229 ? 24.26187  35.65105  13.42200  1.000 48.03804 ? 229 ASP B CG  1 
ATOM   4020 O OD1 . ASP B 1 229 ? 25.27271  35.98396  14.08188  1.000 55.99077 ? 229 ASP B OD1 1 
ATOM   4021 O OD2 . ASP B 1 229 ? 23.08909  35.93401  13.77143  1.000 51.66534 ? 229 ASP B OD2 1 
ATOM   4022 N N   . PHE B 1 230 ? 22.44657  32.43085  12.25669  1.000 25.59076 ? 230 PHE B N   1 
ATOM   4023 C CA  . PHE B 1 230 ? 21.23323  31.81307  12.78282  1.000 27.36356 ? 230 PHE B CA  1 
ATOM   4024 C C   . PHE B 1 230 ? 21.53043  30.47181  13.45888  1.000 27.25897 ? 230 PHE B C   1 
ATOM   4025 O O   . PHE B 1 230 ? 20.98473  30.16395  14.52850  1.000 24.30563 ? 230 PHE B O   1 
ATOM   4026 C CB  . PHE B 1 230 ? 20.21185  31.62886  11.65651  1.000 26.46978 ? 230 PHE B CB  1 
ATOM   4027 C CG  . PHE B 1 230 ? 18.97507  30.93537  12.10291  1.000 23.56981 ? 230 PHE B CG  1 
ATOM   4028 C CD1 . PHE B 1 230 ? 17.99326  31.62461  12.79058  1.000 26.56515 ? 230 PHE B CD1 1 
ATOM   4029 C CD2 . PHE B 1 230 ? 18.82168  29.56959  11.90500  1.000 32.30366 ? 230 PHE B CD2 1 
ATOM   4030 C CE1 . PHE B 1 230 ? 16.85143  30.97862  13.23919  1.000 29.28324 ? 230 PHE B CE1 1 
ATOM   4031 C CE2 . PHE B 1 230 ? 17.69154  28.91231  12.35054  1.000 30.93249 ? 230 PHE B CE2 1 
ATOM   4032 C CZ  . PHE B 1 230 ? 16.70416  29.61484  13.02770  1.000 27.26207 ? 230 PHE B CZ  1 
ATOM   4033 N N   . ASN B 1 231 ? 22.38688  29.65479  12.84901  1.000 25.05629 ? 231 ASN B N   1 
ATOM   4034 C CA  . ASN B 1 231 ? 22.63546  28.32604  13.39917  1.000 26.86921 ? 231 ASN B CA  1 
ATOM   4035 C C   . ASN B 1 231 ? 23.30880  28.40376  14.76014  1.000 28.50846 ? 231 ASN B C   1 
ATOM   4036 O O   . ASN B 1 231 ? 23.01202  27.59307  15.64297  1.000 28.19631 ? 231 ASN B O   1 
ATOM   4037 C CB  . ASN B 1 231 ? 23.49115  27.50454  12.44066  1.000 28.91566 ? 231 ASN B CB  1 
ATOM   4038 C CG  . ASN B 1 231 ? 22.67368  26.84120  11.36237  1.000 26.61009 ? 231 ASN B CG  1 
ATOM   4039 O OD1 . ASN B 1 231 ? 21.44733  27.01878  11.29048  1.000 26.88971 ? 231 ASN B OD1 1 
ATOM   4040 N ND2 . ASN B 1 231 ? 23.34482  26.06254  10.51054  1.000 22.64129 ? 231 ASN B ND2 1 
ATOM   4041 N N   . LEU B 1 232 ? 24.22806  29.35933  14.94429  1.000 28.80918 ? 232 LEU B N   1 
ATOM   4042 C CA  . LEU B 1 232 ? 24.91800  29.47487  16.22873  1.000 29.62012 ? 232 LEU B CA  1 
ATOM   4043 C C   . LEU B 1 232 ? 23.97318  29.97007  17.31438  1.000 31.98779 ? 232 LEU B C   1 
ATOM   4044 O O   . LEU B 1 232 ? 24.03908  29.50915  18.46035  1.000 33.73804 ? 232 LEU B O   1 
ATOM   4045 C CB  . LEU B 1 232 ? 26.12856  30.39672  16.10516  1.000 31.76211 ? 232 LEU B CB  1 
ATOM   4046 C CG  . LEU B 1 232 ? 27.24733  29.90145  15.18914  1.000 35.29162 ? 232 LEU B CG  1 
ATOM   4047 C CD1 . LEU B 1 232 ? 28.40541  30.89391  15.19469  1.000 36.20139 ? 232 LEU B CD1 1 
ATOM   4048 C CD2 . LEU B 1 232 ? 27.72475  28.52512  15.62241  1.000 32.96899 ? 232 LEU B CD2 1 
ATOM   4049 N N   . VAL B 1 233 ? 23.07101  30.89215  16.97353  1.000 32.07224 ? 233 VAL B N   1 
ATOM   4050 C CA  . VAL B 1 233 ? 22.11193  31.36023  17.97197  1.000 30.36513 ? 233 VAL B CA  1 
ATOM   4051 C C   . VAL B 1 233 ? 21.08935  30.27750  18.27571  1.000 30.93849 ? 233 VAL B C   1 
ATOM   4052 O O   . VAL B 1 233 ? 20.71852  30.06167  19.43663  1.000 29.01455 ? 233 VAL B O   1 
ATOM   4053 C CB  . VAL B 1 233 ? 21.42830  32.65807  17.51102  1.000 37.45503 ? 233 VAL B CB  1 
ATOM   4054 C CG1 . VAL B 1 233 ? 20.44864  33.13230  18.57527  1.000 40.44004 ? 233 VAL B CG1 1 
ATOM   4055 C CG2 . VAL B 1 233 ? 22.46929  33.71813  17.23372  1.000 38.87661 ? 233 VAL B CG2 1 
ATOM   4056 N N   . ALA B 1 234 ? 20.61529  29.58067  17.23953  1.000 33.82332 ? 234 ALA B N   1 
ATOM   4057 C CA  . ALA B 1 234 ? 19.60770  28.54497  17.44359  1.000 30.26226 ? 234 ALA B CA  1 
ATOM   4058 C C   . ALA B 1 234 ? 20.07224  27.51633  18.46830  1.000 29.16519 ? 234 ALA B C   1 
ATOM   4059 O O   . ALA B 1 234 ? 19.30523  27.11287  19.35071  1.000 28.24229 ? 234 ALA B O   1 
ATOM   4060 C CB  . ALA B 1 234 ? 19.27623  27.86853  16.11419  1.000 31.00339 ? 234 ALA B CB  1 
ATOM   4061 N N   . MET B 1 235 ? 21.32889  27.08615  18.37661  1.000 23.50972 ? 235 MET B N   1 
ATOM   4062 C CA  . MET B 1 235 ? 21.80804  26.07456  19.31137  1.000 29.07632 ? 235 MET B CA  1 
ATOM   4063 C C   . MET B 1 235 ? 21.73923  26.55805  20.75304  1.000 27.41552 ? 235 MET B C   1 
ATOM   4064 O O   . MET B 1 235 ? 21.56464  25.74360  21.66870  1.000 29.57434 ? 235 MET B O   1 
ATOM   4065 C CB  . MET B 1 235 ? 23.22609  25.65985  18.93409  1.000 28.96272 ? 235 MET B CB  1 
ATOM   4066 C CG  . MET B 1 235 ? 23.26319  25.07383  17.52212  1.000 34.77376 ? 235 MET B CG  1 
ATOM   4067 S SD  . MET B 1 235 ? 24.77777  24.22059  17.11539  1.000 40.60000 ? 235 MET B SD  1 
ATOM   4068 C CE  . MET B 1 235 ? 26.01632  25.36526  17.71499  1.000 43.88284 ? 235 MET B CE  1 
ATOM   4069 N N   . LYS B 1 236 ? 21.85098  27.87347  20.97552  1.000 29.50795 ? 236 LYS B N   1 
ATOM   4070 C CA  . LYS B 1 236 ? 21.77727  28.41696  22.33170  1.000 31.94719 ? 236 LYS B CA  1 
ATOM   4071 C C   . LYS B 1 236 ? 20.40329  28.25429  22.94939  1.000 32.51267 ? 236 LYS B C   1 
ATOM   4072 O O   . LYS B 1 236 ? 20.28223  28.28637  24.17823  1.000 32.82600 ? 236 LYS B O   1 
ATOM   4073 C CB  . LYS B 1 236 ? 22.14156  29.90220  22.34184  1.000 32.83968 ? 236 LYS B CB  1 
ATOM   4074 C CG  . LYS B 1 236 ? 23.59790  30.20531  22.07626  1.000 30.87636 ? 236 LYS B CG  1 
ATOM   4075 C CD  . LYS B 1 236 ? 23.77875  31.71940  21.87829  1.000 39.84076 ? 236 LYS B CD  1 
ATOM   4076 C CE  . LYS B 1 236 ? 25.24540  32.12492  21.92913  1.000 48.66210 ? 236 LYS B CE  1 
ATOM   4077 N NZ  . LYS B 1 236 ? 26.05345  31.28718  21.01568  1.000 54.72982 ? 236 LYS B NZ  1 
ATOM   4078 N N   . TYR B 1 237 ? 19.36593  28.12222  22.13305  1.000 24.65151 ? 237 TYR B N   1 
ATOM   4079 C CA  . TYR B 1 237 ? 18.01340  27.89100  22.60738  1.000 25.71109 ? 237 TYR B CA  1 
ATOM   4080 C C   . TYR B 1 237 ? 17.60789  26.42705  22.47767  1.000 27.58816 ? 237 TYR B C   1 
ATOM   4081 O O   . TYR B 1 237 ? 16.41686  26.11625  22.53571  1.000 33.03436 ? 237 TYR B O   1 
ATOM   4082 C CB  . TYR B 1 237 ? 17.03765  28.79660  21.84825  1.000 23.95544 ? 237 TYR B CB  1 
ATOM   4083 C CG  . TYR B 1 237 ? 17.23146  30.27449  22.14959  1.000 34.61352 ? 237 TYR B CG  1 
ATOM   4084 C CD1 . TYR B 1 237 ? 18.20547  31.02065  21.49434  1.000 33.25262 ? 237 TYR B CD1 1 
ATOM   4085 C CD2 . TYR B 1 237 ? 16.45379  30.91273  23.10905  1.000 36.55517 ? 237 TYR B CD2 1 
ATOM   4086 C CE1 . TYR B 1 237 ? 18.39078  32.37332  21.78032  1.000 37.56970 ? 237 TYR B CE1 1 
ATOM   4087 C CE2 . TYR B 1 237 ? 16.63469  32.25439  23.40452  1.000 38.28940 ? 237 TYR B CE2 1 
ATOM   4088 C CZ  . TYR B 1 237 ? 17.60129  32.97768  22.74133  1.000 39.16118 ? 237 TYR B CZ  1 
ATOM   4089 O OH  . TYR B 1 237 ? 17.77506  34.30961  23.03538  1.000 39.39048 ? 237 TYR B OH  1 
ATOM   4090 N N   . ASN B 1 238 ? 18.57621  25.52730  22.29746  1.000 25.47937 ? 238 ASN B N   1 
ATOM   4091 C CA  . ASN B 1 238 ? 18.30874  24.09712  22.10587  1.000 27.71559 ? 238 ASN B CA  1 
ATOM   4092 C C   . ASN B 1 238 ? 17.42712  23.84976  20.88344  1.000 31.76868 ? 238 ASN B C   1 
ATOM   4093 O O   . ASN B 1 238 ? 16.54389  22.98566  20.88632  1.000 27.91713 ? 238 ASN B O   1 
ATOM   4094 C CB  . ASN B 1 238 ? 17.70453  23.47197  23.35944  1.000 33.87910 ? 238 ASN B CB  1 
ATOM   4095 C CG  . ASN B 1 238 ? 18.76704  23.08335  24.36047  1.000 52.61332 ? 238 ASN B CG  1 
ATOM   4096 O OD1 . ASN B 1 238 ? 19.84541  22.59858  23.98351  1.000 50.06306 ? 238 ASN B OD1 1 
ATOM   4097 N ND2 . ASN B 1 238 ? 18.48851  23.31314  25.63946  1.000 61.37104 ? 238 ASN B ND2 1 
ATOM   4098 N N   . TYR B 1 239 ? 17.68359  24.61420  19.83141  1.000 26.57430 ? 239 TYR B N   1 
ATOM   4099 C CA  . TYR B 1 239 ? 17.09113  24.41314  18.51802  1.000 25.19523 ? 239 TYR B CA  1 
ATOM   4100 C C   . TYR B 1 239 ? 18.12905  23.76217  17.61305  1.000 28.05860 ? 239 TYR B C   1 
ATOM   4101 O O   . TYR B 1 239 ? 19.31939  24.06270  17.71934  1.000 25.22346 ? 239 TYR B O   1 
ATOM   4102 C CB  . TYR B 1 239 ? 16.63915  25.75228  17.92190  1.000 23.83193 ? 239 TYR B CB  1 
ATOM   4103 C CG  . TYR B 1 239 ? 15.18759  26.09568  18.19345  1.000 28.17370 ? 239 TYR B CG  1 
ATOM   4104 C CD1 . TYR B 1 239 ? 14.72353  26.27652  19.49199  1.000 28.84322 ? 239 TYR B CD1 1 
ATOM   4105 C CD2 . TYR B 1 239 ? 14.28345  26.23518  17.14954  1.000 29.18961 ? 239 TYR B CD2 1 
ATOM   4106 C CE1 . TYR B 1 239 ? 13.39291  26.57625  19.74193  1.000 30.61437 ? 239 TYR B CE1 1 
ATOM   4107 C CE2 . TYR B 1 239 ? 12.94614  26.54564  17.38932  1.000 30.18597 ? 239 TYR B CE2 1 
ATOM   4108 C CZ  . TYR B 1 239 ? 12.51229  26.71702  18.68538  1.000 35.80740 ? 239 TYR B CZ  1 
ATOM   4109 O OH  . TYR B 1 239 ? 11.19014  27.02405  18.93562  1.000 35.90698 ? 239 TYR B OH  1 
ATOM   4110 N N   . GLU B 1 240 ? 17.67724  22.86415  16.73112  1.000 26.56716 ? 240 GLU B N   1 
ATOM   4111 C CA  . GLU B 1 240 ? 18.56934  22.24583  15.75706  1.000 28.61582 ? 240 GLU B CA  1 
ATOM   4112 C C   . GLU B 1 240 ? 19.08330  23.27840  14.76099  1.000 30.06121 ? 240 GLU B C   1 
ATOM   4113 O O   . GLU B 1 240 ? 18.32428  24.15218  14.32243  1.000 24.98557 ? 240 GLU B O   1 
ATOM   4114 C CB  . GLU B 1 240 ? 17.84671  21.15220  14.97611  1.000 28.35635 ? 240 GLU B CB  1 
ATOM   4115 C CG  . GLU B 1 240 ? 17.69985  19.85518  15.71690  1.000 31.56179 ? 240 GLU B CG  1 
ATOM   4116 C CD  . GLU B 1 240 ? 19.04395  19.22384  16.02770  1.000 40.71361 ? 240 GLU B CD  1 
ATOM   4117 O OE1 . GLU B 1 240 ? 19.80800  18.94887  15.07589  1.000 43.24745 ? 240 GLU B OE1 1 
ATOM   4118 O OE2 . GLU B 1 240 ? 19.33756  19.02101  17.22259  1.000 37.30151 ? 240 GLU B OE2 1 
ATOM   4119 N N   . PRO B 1 241 ? 20.34198  23.17861  14.34744  1.000 25.81279 ? 241 PRO B N   1 
ATOM   4120 C CA  . PRO B 1 241 ? 20.80900  23.99186  13.22966  1.000 24.98963 ? 241 PRO B CA  1 
ATOM   4121 C C   . PRO B 1 241 ? 20.24750  23.47432  11.91476  1.000 30.69603 ? 241 PRO B C   1 
ATOM   4122 O O   . PRO B 1 241 ? 19.88390  22.30303  11.76745  1.000 28.26486 ? 241 PRO B O   1 
ATOM   4123 C CB  . PRO B 1 241 ? 22.33234  23.83477  13.28243  1.000 25.92428 ? 241 PRO B CB  1 
ATOM   4124 C CG  . PRO B 1 241 ? 22.54451  22.50480  13.93462  1.000 29.36623 ? 241 PRO B CG  1 
ATOM   4125 C CD  . PRO B 1 241 ? 21.38921  22.27929  14.86038  1.000 27.93118 ? 241 PRO B CD  1 
ATOM   4126 N N   . LEU B 1 242 ? 20.20308  24.37536  10.94433  1.000 22.78359 ? 242 LEU B N   1 
ATOM   4127 C CA  . LEU B 1 242 ? 19.74655  24.02968  9.60932   1.000 22.68105 ? 242 LEU B CA  1 
ATOM   4128 C C   . LEU B 1 242 ? 20.86226  23.40466  8.78762   1.000 24.69218 ? 242 LEU B C   1 
ATOM   4129 O O   . LEU B 1 242 ? 22.01741  23.83027  8.86388   1.000 27.51836 ? 242 LEU B O   1 
ATOM   4130 C CB  . LEU B 1 242 ? 19.24220  25.27917  8.90277   1.000 23.15038 ? 242 LEU B CB  1 
ATOM   4131 C CG  . LEU B 1 242 ? 18.05044  25.88973  9.63492   1.000 27.46461 ? 242 LEU B CG  1 
ATOM   4132 C CD1 . LEU B 1 242 ? 17.73357  27.26855  9.05574   1.000 32.34607 ? 242 LEU B CD1 1 
ATOM   4133 C CD2 . LEU B 1 242 ? 16.85482  24.94885  9.54864   1.000 24.75369 ? 242 LEU B CD2 1 
ATOM   4134 N N   . THR B 1 243 ? 20.50107  22.40721  7.98152   1.000 26.77988 ? 243 THR B N   1 
ATOM   4135 C CA  . THR B 1 243 ? 21.35419  21.90936  6.91049   1.000 26.34690 ? 243 THR B CA  1 
ATOM   4136 C C   . THR B 1 243 ? 20.99045  22.56248  5.57345   1.000 28.91514 ? 243 THR B C   1 
ATOM   4137 O O   . THR B 1 243 ? 19.93936  23.20068  5.41322   1.000 25.63318 ? 243 THR B O   1 
ATOM   4138 C CB  . THR B 1 243 ? 21.21979  20.39312  6.77787   1.000 27.70425 ? 243 THR B CB  1 
ATOM   4139 O OG1 . THR B 1 243 ? 19.86986  20.08796  6.41478   1.000 23.93864 ? 243 THR B OG1 1 
ATOM   4140 C CG2 . THR B 1 243 ? 21.54010  19.69152  8.09223   1.000 21.91460 ? 243 THR B CG2 1 
ATOM   4141 N N   . GLN B 1 244 ? 21.87071  22.37298  4.58374   1.000 26.76938 ? 244 GLN B N   1 
ATOM   4142 C CA  . GLN B 1 244 ? 21.53776  22.81108  3.23189   1.000 24.91994 ? 244 GLN B CA  1 
ATOM   4143 C C   . GLN B 1 244 ? 20.24299  22.15488  2.75742   1.000 29.65784 ? 244 GLN B C   1 
ATOM   4144 O O   . GLN B 1 244 ? 19.42130  22.79167  2.08108   1.000 27.51540 ? 244 GLN B O   1 
ATOM   4145 C CB  . GLN B 1 244 ? 22.69961  22.49502  2.28631   1.000 26.48631 ? 244 GLN B CB  1 
ATOM   4146 C CG  . GLN B 1 244 ? 22.53340  23.06000  0.87372   1.000 28.18220 ? 244 GLN B CG  1 
ATOM   4147 C CD  . GLN B 1 244 ? 22.27363  24.54361  0.88926   1.000 33.44298 ? 244 GLN B CD  1 
ATOM   4148 O OE1 . GLN B 1 244 ? 22.95991  25.29667  1.58568   1.000 34.51676 ? 244 GLN B OE1 1 
ATOM   4149 N NE2 . GLN B 1 244 ? 21.26665  24.97730  0.13402   1.000 41.77495 ? 244 GLN B NE2 1 
ATOM   4150 N N   . ASP B 1 245 ? 20.03962  20.88021  3.11363   1.000 26.29487 ? 245 ASP B N   1 
ATOM   4151 C CA  . ASP B 1 245 ? 18.82984  20.16948  2.70005   1.000 27.85369 ? 245 ASP B CA  1 
ATOM   4152 C C   . ASP B 1 245 ? 17.58404  20.79784  3.31111   1.000 30.25006 ? 245 ASP B C   1 
ATOM   4153 O O   . ASP B 1 245 ? 16.52451  20.84023  2.67525   1.000 24.60558 ? 245 ASP B O   1 
ATOM   4154 C CB  . ASP B 1 245 ? 18.91441  18.69173  3.09931   1.000 31.83856 ? 245 ASP B CB  1 
ATOM   4155 C CG  . ASP B 1 245 ? 19.81535  17.87512  2.18383   1.000 32.26895 ? 245 ASP B CG  1 
ATOM   4156 O OD1 . ASP B 1 245 ? 20.33982  18.43633  1.19355   1.000 32.25231 ? 245 ASP B OD1 1 
ATOM   4157 O OD2 . ASP B 1 245 ? 19.99055  16.65880  2.45603   1.000 36.61182 ? 245 ASP B OD2 1 
ATOM   4158 N N   . HIS B 1 246 ? 17.67892  21.24991  4.56452   1.000 26.14735 ? 246 HIS B N   1 
ATOM   4159 C CA  . HIS B 1 246 ? 16.55632  21.94821  5.18338   1.000 23.09518 ? 246 HIS B CA  1 
ATOM   4160 C C   . HIS B 1 246 ? 16.20731  23.22124  4.42154   1.000 26.40695 ? 246 HIS B C   1 
ATOM   4161 O O   . HIS B 1 246 ? 15.02662  23.52668  4.20522   1.000 25.35092 ? 246 HIS B O   1 
ATOM   4162 C CB  . HIS B 1 246 ? 16.88611  22.30484  6.63579   1.000 24.29738 ? 246 HIS B CB  1 
ATOM   4163 C CG  . HIS B 1 246 ? 17.00162  21.12053  7.54213   1.000 29.10239 ? 246 HIS B CG  1 
ATOM   4164 N ND1 . HIS B 1 246 ? 17.70966  21.16123  8.72427   1.000 23.21520 ? 246 HIS B ND1 1 
ATOM   4165 C CD2 . HIS B 1 246 ? 16.49805  19.86853  7.44490   1.000 28.19172 ? 246 HIS B CD2 1 
ATOM   4166 C CE1 . HIS B 1 246 ? 17.64338  19.98034  9.31372   1.000 29.84517 ? 246 HIS B CE1 1 
ATOM   4167 N NE2 . HIS B 1 246 ? 16.91249  19.17724  8.55743   1.000 26.19565 ? 246 HIS B NE2 1 
ATOM   4168 N N   . VAL B 1 247 ? 17.22250  24.00128  4.04523   1.000 24.69172 ? 247 VAL B N   1 
ATOM   4169 C CA  . VAL B 1 247 ? 16.96101  25.24377  3.33307   1.000 27.18484 ? 247 VAL B CA  1 
ATOM   4170 C C   . VAL B 1 247 ? 16.32121  24.93699  1.98851   1.000 28.78309 ? 247 VAL B C   1 
ATOM   4171 O O   . VAL B 1 247 ? 15.42740  25.65563  1.52834   1.000 25.09032 ? 247 VAL B O   1 
ATOM   4172 C CB  . VAL B 1 247 ? 18.26245  26.05933  3.18445   1.000 28.71900 ? 247 VAL B CB  1 
ATOM   4173 C CG1 . VAL B 1 247 ? 18.03384  27.25538  2.26801   1.000 29.80687 ? 247 VAL B CG1 1 
ATOM   4174 C CG2 . VAL B 1 247 ? 18.75608  26.52827  4.56323   1.000 25.95793 ? 247 VAL B CG2 1 
ATOM   4175 N N   . ASP B 1 248 ? 16.73029  23.83210  1.36722   1.000 25.56131 ? 248 ASP B N   1 
ATOM   4176 C CA  . ASP B 1 248 ? 16.17481  23.44681  0.07004   1.000 28.68463 ? 248 ASP B CA  1 
ATOM   4177 C C   . ASP B 1 248 ? 14.71855  23.00946  0.17898   1.000 32.15854 ? 248 ASP B C   1 
ATOM   4178 O O   . ASP B 1 248 ? 13.89253  23.38721  -0.65970  1.000 31.95067 ? 248 ASP B O   1 
ATOM   4179 C CB  . ASP B 1 248 ? 17.00247  22.32333  -0.55191  1.000 29.37427 ? 248 ASP B CB  1 
ATOM   4180 C CG  . ASP B 1 248 ? 18.39908  22.77284  -0.95866  1.000 44.09070 ? 248 ASP B CG  1 
ATOM   4181 O OD1 . ASP B 1 248 ? 18.62412  23.99785  -1.07419  1.000 49.52064 ? 248 ASP B OD1 1 
ATOM   4182 O OD2 . ASP B 1 248 ? 19.26938  21.89625  -1.17540  1.000 49.02077 ? 248 ASP B OD2 1 
ATOM   4183 N N   . ILE B 1 249 ? 14.37734  22.18728  1.17511   1.000 23.35602 ? 249 ILE B N   1 
ATOM   4184 C CA  . ILE B 1 249 ? 12.99487  21.71914  1.25503   1.000 20.83762 ? 249 ILE B CA  1 
ATOM   4185 C C   . ILE B 1 249 ? 12.03218  22.81341  1.68521   1.000 27.37245 ? 249 ILE B C   1 
ATOM   4186 O O   . ILE B 1 249 ? 10.82021  22.66281  1.49385   1.000 28.55070 ? 249 ILE B O   1 
ATOM   4187 C CB  . ILE B 1 249 ? 12.81504  20.49891  2.18326   1.000 30.79855 ? 249 ILE B CB  1 
ATOM   4188 C CG1 . ILE B 1 249 ? 13.19866  20.82729  3.61811   1.000 29.50925 ? 249 ILE B CG1 1 
ATOM   4189 C CG2 . ILE B 1 249 ? 13.61518  19.30194  1.68469   1.000 30.61071 ? 249 ILE B CG2 1 
ATOM   4190 C CD1 . ILE B 1 249 ? 12.86911  19.66883  4.58252   1.000 28.59756 ? 249 ILE B CD1 1 
ATOM   4191 N N   . LEU B 1 250 ? 12.53297  23.92492  2.22378   1.000 26.03616 ? 250 LEU B N   1 
ATOM   4192 C CA  . LEU B 1 250 ? 11.68879  25.08345  2.48318   1.000 29.02041 ? 250 LEU B CA  1 
ATOM   4193 C C   . LEU B 1 250 ? 11.47856  25.95782  1.25388   1.000 30.55712 ? 250 LEU B C   1 
ATOM   4194 O O   . LEU B 1 250 ? 10.73248  26.93560  1.34199   1.000 27.48182 ? 250 LEU B O   1 
ATOM   4195 C CB  . LEU B 1 250 ? 12.28610  25.93950  3.60112   1.000 27.41867 ? 250 LEU B CB  1 
ATOM   4196 C CG  . LEU B 1 250 ? 12.15486  25.38500  5.01747   1.000 29.74620 ? 250 LEU B CG  1 
ATOM   4197 C CD1 . LEU B 1 250 ? 13.06693  26.15724  5.96999   1.000 23.41070 ? 250 LEU B CD1 1 
ATOM   4198 C CD2 . LEU B 1 250 ? 10.69709  25.46993  5.46734   1.000 24.95380 ? 250 LEU B CD2 1 
ATOM   4199 N N   . GLY B 1 251 ? 12.12614  25.65203  0.12864   1.000 29.08418 ? 251 GLY B N   1 
ATOM   4200 C CA  . GLY B 1 251 ? 12.06187  26.49162  -1.04682  1.000 28.26207 ? 251 GLY B CA  1 
ATOM   4201 C C   . GLY B 1 251 ? 10.64776  26.74291  -1.53689  1.000 29.39078 ? 251 GLY B C   1 
ATOM   4202 O O   . GLY B 1 251 ? 10.24223  27.88758  -1.78034  1.000 29.37462 ? 251 GLY B O   1 
ATOM   4203 N N   . PRO B 1 252 ? 9.88070   25.66381  -1.72945  1.000 32.55499 ? 252 PRO B N   1 
ATOM   4204 C CA  . PRO B 1 252 ? 8.50064   25.82895  -2.20820  1.000 27.46609 ? 252 PRO B CA  1 
ATOM   4205 C C   . PRO B 1 252 ? 7.64741   26.73544  -1.33586  1.000 28.98818 ? 252 PRO B C   1 
ATOM   4206 O O   . PRO B 1 252 ? 6.85936   27.52184  -1.86779  1.000 27.72770 ? 252 PRO B O   1 
ATOM   4207 C CB  . PRO B 1 252 ? 7.97964   24.38741  -2.22770  1.000 27.54754 ? 252 PRO B CB  1 
ATOM   4208 C CG  . PRO B 1 252 ? 9.19655   23.58245  -2.54011  1.000 27.96211 ? 252 PRO B CG  1 
ATOM   4209 C CD  . PRO B 1 252 ? 10.31936  24.25739  -1.80862  1.000 31.92967 ? 252 PRO B CD  1 
ATOM   4210 N N   . LEU B 1 253 ? 7.74940   26.62672  -0.00858  1.000 23.41753 ? 253 LEU B N   1 
ATOM   4211 C CA  . LEU B 1 253 ? 6.99015   27.51990  0.86129   1.000 24.76636 ? 253 LEU B CA  1 
ATOM   4212 C C   . LEU B 1 253 ? 7.54989   28.93363  0.80259   1.000 27.82187 ? 253 LEU B C   1 
ATOM   4213 O O   . LEU B 1 253 ? 6.80223   29.91265  0.90630   1.000 24.66388 ? 253 LEU B O   1 
ATOM   4214 C CB  . LEU B 1 253 ? 6.99779   26.99157  2.30625   1.000 25.70319 ? 253 LEU B CB  1 
ATOM   4215 C CG  . LEU B 1 253 ? 6.29146   25.64408  2.51159   1.000 26.10640 ? 253 LEU B CG  1 
ATOM   4216 C CD1 . LEU B 1 253 ? 6.61204   25.06514  3.88071   1.000 26.22472 ? 253 LEU B CD1 1 
ATOM   4217 C CD2 . LEU B 1 253 ? 4.76891   25.74741  2.34055   1.000 32.02576 ? 253 LEU B CD2 1 
ATOM   4218 N N   . SER B 1 254 ? 8.87162   29.07085  0.66783   1.000 22.44480 ? 254 SER B N   1 
ATOM   4219 C CA  . SER B 1 254 ? 9.41005   30.41150  0.50522   1.000 25.02243 ? 254 SER B CA  1 
ATOM   4220 C C   . SER B 1 254 ? 8.86225   31.04888  -0.77010  1.000 27.33904 ? 254 SER B C   1 
ATOM   4221 O O   . SER B 1 254 ? 8.53386   32.24377  -0.79975  1.000 24.96551 ? 254 SER B O   1 
ATOM   4222 C CB  . SER B 1 254 ? 10.93821  30.35763  0.48452   1.000 26.18404 ? 254 SER B CB  1 
ATOM   4223 O OG  . SER B 1 254 ? 11.47202  31.66096  0.32964   1.000 37.13016 ? 254 SER B OG  1 
ATOM   4224 N N   . ALA B 1 255 ? 8.73391   30.25406  -1.83178  1.000 24.93717 ? 255 ALA B N   1 
ATOM   4225 C CA  . ALA B 1 255 ? 8.25365   30.79173  -3.10277  1.000 20.64944 ? 255 ALA B CA  1 
ATOM   4226 C C   . ALA B 1 255 ? 6.77609   31.16957  -3.01839  1.000 25.79456 ? 255 ALA B C   1 
ATOM   4227 O O   . ALA B 1 255 ? 6.37145   32.23118  -3.50313  1.000 30.97365 ? 255 ALA B O   1 
ATOM   4228 C CB  . ALA B 1 255 ? 8.48597   29.76564  -4.21028  1.000 21.15924 ? 255 ALA B CB  1 
ATOM   4229 N N   . GLN B 1 256 ? 5.96391   30.30956  -2.40010  1.000 24.08855 ? 256 GLN B N   1 
ATOM   4230 C CA  . GLN B 1 256 ? 4.53460   30.56348  -2.23710  1.000 23.40701 ? 256 GLN B CA  1 
ATOM   4231 C C   . GLN B 1 256 ? 4.25770   31.87153  -1.50048  1.000 30.02350 ? 256 GLN B C   1 
ATOM   4232 O O   . GLN B 1 256 ? 3.30237   32.58420  -1.83189  1.000 32.70915 ? 256 GLN B O   1 
ATOM   4233 C CB  . GLN B 1 256 ? 3.88661   29.39884  -1.48414  1.000 26.56818 ? 256 GLN B CB  1 
ATOM   4234 C CG  . GLN B 1 256 ? 2.38344   29.33343  -1.63733  1.000 28.95497 ? 256 GLN B CG  1 
ATOM   4235 C CD  . GLN B 1 256 ? 2.00009   28.96552  -3.05244  1.000 46.28605 ? 256 GLN B CD  1 
ATOM   4236 O OE1 . GLN B 1 256 ? 2.79676   28.35511  -3.77745  1.000 47.73763 ? 256 GLN B OE1 1 
ATOM   4237 N NE2 . GLN B 1 256 ? 0.78966   29.34593  -3.46777  1.000 46.48903 ? 256 GLN B NE2 1 
ATOM   4238 N N   . THR B 1 257 ? 5.04248   32.17884  -0.46195  1.000 29.60135 ? 257 THR B N   1 
ATOM   4239 C CA  . THR B 1 257 ? 4.82408   33.37517  0.34209   1.000 30.07392 ? 257 THR B CA  1 
ATOM   4240 C C   . THR B 1 257 ? 5.71910   34.54196  -0.04735  1.000 32.36315 ? 257 THR B C   1 
ATOM   4241 O O   . THR B 1 257 ? 5.48420   35.65401  0.42449   1.000 32.41370 ? 257 THR B O   1 
ATOM   4242 C CB  . THR B 1 257 ? 5.04747   33.07021  1.82751   1.000 28.44135 ? 257 THR B CB  1 
ATOM   4243 O OG1 . THR B 1 257 ? 6.39511   32.59471  2.01544   1.000 24.70039 ? 257 THR B OG1 1 
ATOM   4244 C CG2 . THR B 1 257 ? 4.05635   32.02843  2.30990   1.000 27.08966 ? 257 THR B CG2 1 
ATOM   4245 N N   . GLY B 1 258 ? 6.74610   34.32285  -0.86854  1.000 31.87869 ? 258 GLY B N   1 
ATOM   4246 C CA  . GLY B 1 258 ? 7.67540   35.39928  -1.16959  1.000 28.31595 ? 258 GLY B CA  1 
ATOM   4247 C C   . GLY B 1 258 ? 8.54928   35.83315  -0.01238  1.000 33.20925 ? 258 GLY B C   1 
ATOM   4248 O O   . GLY B 1 258 ? 9.11093   36.93162  -0.04114  1.000 32.04112 ? 258 GLY B O   1 
ATOM   4249 N N   . ILE B 1 259 ? 8.68970   34.99856  1.00879   1.000 29.29156 ? 259 ILE B N   1 
ATOM   4250 C CA  . ILE B 1 259 ? 9.48475   35.30958  2.19134   1.000 30.62791 ? 259 ILE B CA  1 
ATOM   4251 C C   . ILE B 1 259 ? 10.73772  34.44762  2.15801   1.000 29.67687 ? 259 ILE B C   1 
ATOM   4252 O O   . ILE B 1 259 ? 10.64706  33.21356  2.22082   1.000 27.50844 ? 259 ILE B O   1 
ATOM   4253 C CB  . ILE B 1 259 ? 8.67214   35.07060  3.46727   1.000 29.97396 ? 259 ILE B CB  1 
ATOM   4254 C CG1 . ILE B 1 259 ? 7.43902   35.97626  3.45120   1.000 31.13353 ? 259 ILE B CG1 1 
ATOM   4255 C CG2 . ILE B 1 259 ? 9.53500   35.28730  4.72169   1.000 27.74335 ? 259 ILE B CG2 1 
ATOM   4256 C CD1 . ILE B 1 259 ? 6.31714   35.48074  4.30489   1.000 34.79262 ? 259 ILE B CD1 1 
ATOM   4257 N N   . ALA B 1 260 ? 11.90770  35.08831  2.05213   1.000 27.25014 ? 260 ALA B N   1 
ATOM   4258 C CA  . ALA B 1 260 ? 13.15447  34.33332  1.97336   1.000 29.57692 ? 260 ALA B CA  1 
ATOM   4259 C C   . ALA B 1 260 ? 13.34045  33.46970  3.21805   1.000 28.73520 ? 260 ALA B C   1 
ATOM   4260 O O   . ALA B 1 260 ? 12.92612  33.83158  4.32345   1.000 26.66775 ? 260 ALA B O   1 
ATOM   4261 C CB  . ALA B 1 260 ? 14.35072  35.27302  1.80507   1.000 27.53025 ? 260 ALA B CB  1 
ATOM   4262 N N   . VAL B 1 261 ? 13.98571  32.31602  3.03750   1.000 27.90102 ? 261 VAL B N   1 
ATOM   4263 C CA  . VAL B 1 261 ? 14.19922  31.41519  4.17399   1.000 25.83863 ? 261 VAL B CA  1 
ATOM   4264 C C   . VAL B 1 261 ? 14.90281  32.14694  5.31248   1.000 29.38287 ? 261 VAL B C   1 
ATOM   4265 O O   . VAL B 1 261 ? 14.48958  32.06485  6.47475   1.000 27.72883 ? 261 VAL B O   1 
ATOM   4266 C CB  . VAL B 1 261 ? 14.98551  30.16701  3.73177   1.000 26.62146 ? 261 VAL B CB  1 
ATOM   4267 C CG1 . VAL B 1 261 ? 15.40451  29.34260  4.93912   1.000 25.34095 ? 261 VAL B CG1 1 
ATOM   4268 C CG2 . VAL B 1 261 ? 14.13751  29.33460  2.81779   1.000 27.32056 ? 261 VAL B CG2 1 
ATOM   4269 N N   . LEU B 1 262 ? 15.97992  32.87776  4.99501   1.000 31.05060 ? 262 LEU B N   1 
ATOM   4270 C CA  . LEU B 1 262 ? 16.73663  33.59383  6.01751   1.000 29.77298 ? 262 LEU B CA  1 
ATOM   4271 C C   . LEU B 1 262 ? 15.95942  34.75827  6.62531   1.000 29.05606 ? 262 LEU B C   1 
ATOM   4272 O O   . LEU B 1 262 ? 16.25892  35.15620  7.75518   1.000 29.85891 ? 262 LEU B O   1 
ATOM   4273 C CB  . LEU B 1 262 ? 18.05804  34.09267  5.43383   1.000 29.22414 ? 262 LEU B CB  1 
ATOM   4274 C CG  . LEU B 1 262 ? 19.03973  32.97921  5.07681   1.000 30.76805 ? 262 LEU B CG  1 
ATOM   4275 C CD1 . LEU B 1 262 ? 20.30660  33.56041  4.49262   1.000 38.23502 ? 262 LEU B CD1 1 
ATOM   4276 C CD2 . LEU B 1 262 ? 19.36367  32.11876  6.29447   1.000 31.68930 ? 262 LEU B CD2 1 
ATOM   4277 N N   . ASP B 1 263 ? 14.96569  35.30797  5.92109   1.000 28.69173 ? 263 ASP B N   1 
ATOM   4278 C CA  . ASP B 1 263 ? 14.09062  36.29890  6.55298   1.000 29.46473 ? 263 ASP B CA  1 
ATOM   4279 C C   . ASP B 1 263 ? 13.18169  35.64018  7.57576   1.000 29.23516 ? 263 ASP B C   1 
ATOM   4280 O O   . ASP B 1 263 ? 12.97676  36.17450  8.67174   1.000 30.66529 ? 263 ASP B O   1 
ATOM   4281 C CB  . ASP B 1 263 ? 13.23276  37.03751  5.51884   1.000 30.39724 ? 263 ASP B CB  1 
ATOM   4282 C CG  . ASP B 1 263 ? 14.04814  37.77586  4.50110   1.000 37.25354 ? 263 ASP B CG  1 
ATOM   4283 O OD1 . ASP B 1 263 ? 15.28782  37.71611  4.56961   1.000 39.75926 ? 263 ASP B OD1 1 
ATOM   4284 O OD2 . ASP B 1 263 ? 13.44797  38.42658  3.62354   1.000 43.81850 ? 263 ASP B OD2 1 
ATOM   4285 N N   . MET B 1 264 ? 12.62370  34.47635  7.23911   1.000 28.12479 ? 264 MET B N   1 
ATOM   4286 C CA  . MET B 1 264 ? 11.84955  33.75052  8.23702   1.000 30.04516 ? 264 MET B CA  1 
ATOM   4287 C C   . MET B 1 264 ? 12.72387  33.32777  9.40965   1.000 27.09186 ? 264 MET B C   1 
ATOM   4288 O O   . MET B 1 264 ? 12.25209  33.27971  10.55290  1.000 26.12192 ? 264 MET B O   1 
ATOM   4289 C CB  . MET B 1 264 ? 11.18456  32.53196  7.61570   1.000 27.85990 ? 264 MET B CB  1 
ATOM   4290 C CG  . MET B 1 264 ? 10.14398  31.91856  8.52099   1.000 23.39588 ? 264 MET B CG  1 
ATOM   4291 S SD  . MET B 1 264 ? 8.69385   32.98782  8.73397   1.000 29.69178 ? 264 MET B SD  1 
ATOM   4292 C CE  . MET B 1 264 ? 7.70901   32.58104  7.26943   1.000 26.05197 ? 264 MET B CE  1 
ATOM   4293 N N   . CYS B 1 265 ? 13.99082  32.97319  9.14555   1.000 24.84157 ? 265 CYS B N   1 
ATOM   4294 C CA  . CYS B 1 265 ? 14.89505  32.65054  10.24929  1.000 28.92068 ? 265 CYS B CA  1 
ATOM   4295 C C   . CYS B 1 265 ? 15.06470  33.84530  11.17559  1.000 30.50798 ? 265 CYS B C   1 
ATOM   4296 O O   . CYS B 1 265 ? 15.11305  33.68840  12.40388  1.000 25.50346 ? 265 CYS B O   1 
ATOM   4297 C CB  . CYS B 1 265 ? 16.26634  32.19589  9.72725   1.000 31.25597 ? 265 CYS B CB  1 
ATOM   4298 S SG  . CYS B 1 265 ? 16.30475  30.55635  8.90882   1.000 28.58096 ? 265 CYS B SG  1 
ATOM   4299 N N   . ALA B 1 266 ? 15.17571  35.04726  10.60166  1.000 25.71668 ? 266 ALA B N   1 
ATOM   4300 C CA  . ALA B 1 266 ? 15.31021  36.24226  11.42352  1.000 28.82536 ? 266 ALA B CA  1 
ATOM   4301 C C   . ALA B 1 266 ? 14.06081  36.46507  12.26117  1.000 28.53427 ? 266 ALA B C   1 
ATOM   4302 O O   . ALA B 1 266 ? 14.15071  36.80007  13.44780  1.000 30.45356 ? 266 ALA B O   1 
ATOM   4303 C CB  . ALA B 1 266 ? 15.61440  37.45332  10.53812  1.000 26.00201 ? 266 ALA B CB  1 
ATOM   4304 N N   . SER B 1 267 ? 12.88424  36.23486  11.67752  1.000 28.18163 ? 267 SER B N   1 
ATOM   4305 C CA  . SER B 1 267 ? 11.65046  36.34919  12.45279  1.000 28.84743 ? 267 SER B CA  1 
ATOM   4306 C C   . SER B 1 267 ? 11.59141  35.31016  13.56969  1.000 27.06588 ? 267 SER B C   1 
ATOM   4307 O O   . SER B 1 267 ? 11.15224  35.61433  14.68414  1.000 32.05591 ? 267 SER B O   1 
ATOM   4308 C CB  . SER B 1 267 ? 10.43444  36.21671  11.53313  1.000 31.72838 ? 267 SER B CB  1 
ATOM   4309 O OG  . SER B 1 267 ? 10.45070  37.21257  10.51902  1.000 34.76292 ? 267 SER B OG  1 
ATOM   4310 N N   . LEU B 1 268 ? 11.99784  34.07125  13.28737  1.000 25.89457 ? 268 LEU B N   1 
ATOM   4311 C CA  . LEU B 1 268 ? 12.04283  33.05417  14.34339  1.000 27.52367 ? 268 LEU B CA  1 
ATOM   4312 C C   . LEU B 1 268 ? 13.00595  33.45334  15.45941  1.000 31.39061 ? 268 LEU B C   1 
ATOM   4313 O O   . LEU B 1 268 ? 12.69568  33.30026  16.64934  1.000 27.47190 ? 268 LEU B O   1 
ATOM   4314 C CB  . LEU B 1 268 ? 12.44120  31.69689  13.75900  1.000 25.64670 ? 268 LEU B CB  1 
ATOM   4315 C CG  . LEU B 1 268 ? 12.62386  30.58417  14.80081  1.000 29.84179 ? 268 LEU B CG  1 
ATOM   4316 C CD1 . LEU B 1 268 ? 11.34612  30.37623  15.63536  1.000 26.65794 ? 268 LEU B CD1 1 
ATOM   4317 C CD2 . LEU B 1 268 ? 13.05346  29.28232  14.14725  1.000 31.64266 ? 268 LEU B CD2 1 
ATOM   4318 N N   . LYS B 1 269 ? 14.18554  33.95546  15.09557  1.000 27.95243 ? 269 LYS B N   1 
ATOM   4319 C CA  . LYS B 1 269 ? 15.15939  34.35666  16.10455  1.000 30.84184 ? 269 LYS B CA  1 
ATOM   4320 C C   . LYS B 1 269 ? 14.58239  35.40086  17.05792  1.000 38.53318 ? 269 LYS B C   1 
ATOM   4321 O O   . LYS B 1 269 ? 14.78679  35.31814  18.27605  1.000 34.03599 ? 269 LYS B O   1 
ATOM   4322 C CB  . LYS B 1 269 ? 16.42107  34.88453  15.42438  1.000 35.88002 ? 269 LYS B CB  1 
ATOM   4323 C CG  . LYS B 1 269 ? 17.52963  35.27039  16.37817  1.000 38.22486 ? 269 LYS B CG  1 
ATOM   4324 C CD  . LYS B 1 269 ? 18.86362  35.43907  15.64432  1.000 43.81079 ? 269 LYS B CD  1 
ATOM   4325 C CE  . LYS B 1 269 ? 19.16324  36.90272  15.34547  1.000 47.72366 ? 269 LYS B CE  1 
ATOM   4326 N NZ  . LYS B 1 269 ? 20.59963  37.13264  14.97291  1.000 52.26754 ? 269 LYS B NZ  1 
ATOM   4327 N N   . GLU B 1 270 ? 13.85558  36.38970  16.52676  1.000 34.19813 ? 270 GLU B N   1 
ATOM   4328 C CA  . GLU B 1 270 ? 13.25094  37.39493  17.39606  1.000 39.62620 ? 270 GLU B CA  1 
ATOM   4329 C C   . GLU B 1 270 ? 12.22424  36.76265  18.32253  1.000 39.55905 ? 270 GLU B C   1 
ATOM   4330 O O   . GLU B 1 270 ? 12.13418  37.12290  19.50248  1.000 37.15938 ? 270 GLU B O   1 
ATOM   4331 C CB  . GLU B 1 270 ? 12.60458  38.51835  16.57573  1.000 31.33802 ? 270 GLU B CB  1 
ATOM   4332 C CG  . GLU B 1 270 ? 12.38643  39.76990  17.43125  1.000 48.65605 ? 270 GLU B CG  1 
ATOM   4333 C CD  . GLU B 1 270 ? 11.35206  40.72618  16.87211  1.000 65.33111 ? 270 GLU B CD  1 
ATOM   4334 O OE1 . GLU B 1 270 ? 11.45342  41.11035  15.68309  1.000 58.29296 ? 270 GLU B OE1 1 
ATOM   4335 O OE2 . GLU B 1 270 ? 10.43480  41.09752  17.63747  1.000 68.53224 ? 270 GLU B OE2 1 
ATOM   4336 N N   . LEU B 1 271 ? 11.44072  35.81429  17.80652  1.000 34.86902 ? 271 LEU B N   1 
ATOM   4337 C CA  . LEU B 1 271 ? 10.52379  35.07741  18.66704  1.000 32.56055 ? 271 LEU B CA  1 
ATOM   4338 C C   . LEU B 1 271 ? 11.27946  34.38700  19.79951  1.000 39.86737 ? 271 LEU B C   1 
ATOM   4339 O O   . LEU B 1 271 ? 10.90221  34.49409  20.97257  1.000 41.04840 ? 271 LEU B O   1 
ATOM   4340 C CB  . LEU B 1 271 ? 9.72978   34.06325  17.84523  1.000 34.36405 ? 271 LEU B CB  1 
ATOM   4341 C CG  . LEU B 1 271 ? 8.60563   34.60450  16.95922  1.000 38.68798 ? 271 LEU B CG  1 
ATOM   4342 C CD1 . LEU B 1 271 ? 7.87836   33.45123  16.27347  1.000 34.43537 ? 271 LEU B CD1 1 
ATOM   4343 C CD2 . LEU B 1 271 ? 7.62225   35.44848  17.75006  1.000 42.77252 ? 271 LEU B CD2 1 
ATOM   4344 N N   . LEU B 1 272 ? 12.36363  33.68552  19.46817  1.000 34.59069 ? 272 LEU B N   1 
ATOM   4345 C CA  . LEU B 1 272 ? 13.13239  32.99379  20.49538  1.000 40.19161 ? 272 LEU B CA  1 
ATOM   4346 C C   . LEU B 1 272 ? 13.70273  33.97029  21.51485  1.000 42.70554 ? 272 LEU B C   1 
ATOM   4347 O O   . LEU B 1 272 ? 13.79855  33.64243  22.70365  1.000 38.76728 ? 272 LEU B O   1 
ATOM   4348 C CB  . LEU B 1 272 ? 14.26085  32.18127  19.85410  1.000 37.02062 ? 272 LEU B CB  1 
ATOM   4349 C CG  . LEU B 1 272 ? 13.86175  31.00665  18.95281  1.000 35.13894 ? 272 LEU B CG  1 
ATOM   4350 C CD1 . LEU B 1 272 ? 15.06937  30.12158  18.67379  1.000 40.37283 ? 272 LEU B CD1 1 
ATOM   4351 C CD2 . LEU B 1 272 ? 12.72489  30.19293  19.56910  1.000 34.63143 ? 272 LEU B CD2 1 
ATOM   4352 N N   . GLN B 1 273 ? 14.08244  35.17057  21.07581  1.000 33.09185 ? 273 GLN B N   1 
ATOM   4353 C CA  . GLN B 1 273 ? 14.72296  36.10487  21.98878  1.000 42.26550 ? 273 GLN B CA  1 
ATOM   4354 C C   . GLN B 1 273 ? 13.70942  36.85868  22.84775  1.000 47.85589 ? 273 GLN B C   1 
ATOM   4355 O O   . GLN B 1 273 ? 14.00156  37.17012  24.01184  1.000 55.25959 ? 273 GLN B O   1 
ATOM   4356 C CB  . GLN B 1 273 ? 15.62264  37.06664  21.19875  1.000 37.43794 ? 273 GLN B CB  1 
ATOM   4357 C CG  . GLN B 1 273 ? 16.83361  36.35099  20.57702  1.000 37.91732 ? 273 GLN B CG  1 
ATOM   4358 C CD  . GLN B 1 273 ? 17.78295  37.26565  19.81526  1.000 46.10674 ? 273 GLN B CD  1 
ATOM   4359 O OE1 . GLN B 1 273 ? 17.36748  38.21974  19.16063  1.000 46.37846 ? 273 GLN B OE1 1 
ATOM   4360 N NE2 . GLN B 1 273 ? 19.06998  36.95457  19.87910  1.000 43.23787 ? 273 GLN B NE2 1 
ATOM   4361 N N   . ASN B 1 274 ? 12.51435  37.13430  22.32476  1.000 42.85201 ? 274 ASN B N   1 
ATOM   4362 C CA  . ASN B 1 274 ? 11.53128  37.92211  23.06158  1.000 45.94766 ? 274 ASN B CA  1 
ATOM   4363 C C   . ASN B 1 274 ? 10.22947  37.19237  23.35756  1.000 45.55005 ? 274 ASN B C   1 
ATOM   4364 O O   . ASN B 1 274 ? 9.31998   37.80246  23.92685  1.000 52.65822 ? 274 ASN B O   1 
ATOM   4365 C CB  . ASN B 1 274 ? 11.19999  39.21671  22.30495  1.000 47.03530 ? 274 ASN B CB  1 
ATOM   4366 C CG  . ASN B 1 274 ? 12.43109  39.94719  21.82806  1.000 52.62714 ? 274 ASN B CG  1 
ATOM   4367 O OD1 . ASN B 1 274 ? 12.76483  39.91244  20.64364  1.000 59.97521 ? 274 ASN B OD1 1 
ATOM   4368 N ND2 . ASN B 1 274 ? 13.11898  40.60964  22.74389  1.000 58.69831 ? 274 ASN B ND2 1 
ATOM   4369 N N   . GLY B 1 275 ? 10.10533  35.92509  22.98993  1.000 40.38965 ? 275 GLY B N   1 
ATOM   4370 C CA  . GLY B 1 275 ? 8.87436   35.18341  23.19160  1.000 38.46336 ? 275 GLY B CA  1 
ATOM   4371 C C   . GLY B 1 275 ? 7.72249   35.79738  22.41761  1.000 47.55698 ? 275 GLY B C   1 
ATOM   4372 O O   . GLY B 1 275 ? 7.88146   36.71985  21.62679  1.000 49.25033 ? 275 GLY B O   1 
ATOM   4373 N N   . MET B 1 276 ? 6.53705   35.24309  22.64295  1.000 49.88247 ? 276 MET B N   1 
ATOM   4374 C CA  . MET B 1 276 ? 5.31204   35.72808  22.02164  1.000 55.21725 ? 276 MET B CA  1 
ATOM   4375 C C   . MET B 1 276 ? 4.55559   36.53641  23.06352  1.000 65.21121 ? 276 MET B C   1 
ATOM   4376 O O   . MET B 1 276 ? 4.04833   35.97742  24.04064  1.000 72.95754 ? 276 MET B O   1 
ATOM   4377 C CB  . MET B 1 276 ? 4.46700   34.57009  21.50090  1.000 57.51153 ? 276 MET B CB  1 
ATOM   4378 C CG  . MET B 1 276 ? 4.97781   33.97380  20.19970  1.000 56.55743 ? 276 MET B CG  1 
ATOM   4379 S SD  . MET B 1 276 ? 4.11738   32.44957  19.75612  1.000 66.35992 ? 276 MET B SD  1 
ATOM   4380 C CE  . MET B 1 276 ? 5.16452   31.26023  20.59836  1.000 57.70503 ? 276 MET B CE  1 
ATOM   4381 N N   . ASN B 1 277 ? 4.49463   37.85316  22.86416  1.000 65.74055 ? 277 ASN B N   1 
ATOM   4382 C CA  . ASN B 1 277 ? 3.89016   38.76073  23.83945  1.000 65.17764 ? 277 ASN B CA  1 
ATOM   4383 C C   . ASN B 1 277 ? 2.39361   38.47004  23.91600  1.000 63.08200 ? 277 ASN B C   1 
ATOM   4384 O O   . ASN B 1 277 ? 1.55855   39.14781  23.31130  1.000 63.43252 ? 277 ASN B O   1 
ATOM   4385 C CB  . ASN B 1 277 ? 4.16390   40.21257  23.46227  1.000 64.60150 ? 277 ASN B CB  1 
ATOM   4386 N N   . GLY B 1 278 ? 2.05457   37.42861  24.67542  1.000 61.02271 ? 278 GLY B N   1 
ATOM   4387 C CA  . GLY B 1 278 ? 0.67310   37.02908  24.86397  1.000 53.06629 ? 278 GLY B CA  1 
ATOM   4388 C C   . GLY B 1 278 ? -0.07958  36.87326  23.56052  1.000 62.01161 ? 278 GLY B C   1 
ATOM   4389 O O   . GLY B 1 278 ? -1.29702  37.07344  23.50195  1.000 58.63952 ? 278 GLY B O   1 
ATOM   4390 N N   . ARG B 1 279 ? 0.63647   36.52391  22.50110  1.000 55.17508 ? 279 ARG B N   1 
ATOM   4391 C CA  . ARG B 1 279 ? 0.03754   36.37199  21.18885  1.000 53.98776 ? 279 ARG B CA  1 
ATOM   4392 C C   . ARG B 1 279 ? 0.17946   34.92328  20.74662  1.000 44.51390 ? 279 ARG B C   1 
ATOM   4393 O O   . ARG B 1 279 ? 1.02296   34.17807  21.25240  1.000 53.74033 ? 279 ARG B O   1 
ATOM   4394 C CB  . ARG B 1 279 ? 0.68018   37.32768  20.17070  1.000 51.88799 ? 279 ARG B CB  1 
ATOM   4395 N N   . THR B 1 280 ? -0.66994  34.52002  19.80738  1.000 48.58145 ? 280 THR B N   1 
ATOM   4396 C CA  . THR B 1 280 ? -0.67397  33.15338  19.31297  1.000 42.79515 ? 280 THR B CA  1 
ATOM   4397 C C   . THR B 1 280 ? -0.39194  33.12731  17.81632  1.000 43.96376 ? 280 THR B C   1 
ATOM   4398 O O   . THR B 1 280 ? -0.51357  34.13648  17.11551  1.000 45.44911 ? 280 THR B O   1 
ATOM   4399 C CB  . THR B 1 280 ? -2.00804  32.44895  19.60188  1.000 45.71398 ? 280 THR B CB  1 
ATOM   4400 O OG1 . THR B 1 280 ? -3.05483  33.04839  18.82824  1.000 43.89165 ? 280 THR B OG1 1 
ATOM   4401 C CG2 . THR B 1 280 ? -2.35108  32.55846  21.07522  1.000 45.34087 ? 280 THR B CG2 1 
ATOM   4402 N N   . ILE B 1 281 ? 0.00716   31.95144  17.34228  1.000 37.89922 ? 281 ILE B N   1 
ATOM   4403 C CA  . ILE B 1 281 ? 0.22820   31.68932  15.92747  1.000 39.43320 ? 281 ILE B CA  1 
ATOM   4404 C C   . ILE B 1 281 ? -0.58596  30.45640  15.57124  1.000 41.15915 ? 281 ILE B C   1 
ATOM   4405 O O   . ILE B 1 281 ? -0.39870  29.39325  16.17297  1.000 43.08290 ? 281 ILE B O   1 
ATOM   4406 C CB  . ILE B 1 281 ? 1.71572   31.47618  15.60237  1.000 31.99442 ? 281 ILE B CB  1 
ATOM   4407 C CG1 . ILE B 1 281 ? 2.50867   32.74711  15.89683  1.000 32.42113 ? 281 ILE B CG1 1 
ATOM   4408 C CG2 . ILE B 1 281 ? 1.88401   31.03664  14.15675  1.000 38.67953 ? 281 ILE B CG2 1 
ATOM   4409 C CD1 . ILE B 1 281 ? 4.02133   32.59171  15.70853  1.000 35.81812 ? 281 ILE B CD1 1 
ATOM   4410 N N   . LEU B 1 282 ? -1.49996  30.60162  14.61323  1.000 37.54867 ? 282 LEU B N   1 
ATOM   4411 C CA  . LEU B 1 282 ? -2.43158  29.53466  14.26225  1.000 35.71028 ? 282 LEU B CA  1 
ATOM   4412 C C   . LEU B 1 282 ? -3.19937  29.05559  15.49378  1.000 39.95080 ? 282 LEU B C   1 
ATOM   4413 O O   . LEU B 1 282 ? -3.48896  27.86983  15.65406  1.000 36.95994 ? 282 LEU B O   1 
ATOM   4414 C CB  . LEU B 1 282 ? -1.70618  28.37836  13.57454  1.000 41.55484 ? 282 LEU B CB  1 
ATOM   4415 C CG  . LEU B 1 282 ? -1.24413  28.64645  12.13906  1.000 38.88196 ? 282 LEU B CG  1 
ATOM   4416 C CD1 . LEU B 1 282 ? -0.55368  27.43014  11.52348  1.000 36.99595 ? 282 LEU B CD1 1 
ATOM   4417 C CD2 . LEU B 1 282 ? -2.44090  29.04051  11.30343  1.000 34.78631 ? 282 LEU B CD2 1 
ATOM   4418 N N   . GLY B 1 283 ? -3.53633  29.99619  16.37268  1.000 40.06723 ? 283 GLY B N   1 
ATOM   4419 C CA  . GLY B 1 283 ? -4.34324  29.68362  17.53415  1.000 40.68042 ? 283 GLY B CA  1 
ATOM   4420 C C   . GLY B 1 283 ? -3.58867  29.04844  18.67512  1.000 52.40650 ? 283 GLY B C   1 
ATOM   4421 O O   . GLY B 1 283 ? -4.21532  28.47542  19.57486  1.000 48.48804 ? 283 GLY B O   1 
ATOM   4422 N N   . SER B 1 284 ? -2.25932  29.14679  18.67816  1.000 45.00465 ? 284 SER B N   1 
ATOM   4423 C CA  . SER B 1 284 ? -1.43097  28.43628  19.63842  1.000 43.25019 ? 284 SER B CA  1 
ATOM   4424 C C   . SER B 1 284 ? -0.36214  29.35109  20.21191  1.000 46.44342 ? 284 SER B C   1 
ATOM   4425 O O   . SER B 1 284 ? 0.17148   30.21945  19.51304  1.000 45.13359 ? 284 SER B O   1 
ATOM   4426 C CB  . SER B 1 284 ? -0.76433  27.22451  18.99161  1.000 43.76665 ? 284 SER B CB  1 
ATOM   4427 O OG  . SER B 1 284 ? 0.16808   26.64316  19.87775  1.000 42.93492 ? 284 SER B OG  1 
ATOM   4428 N N   . ALA B 1 285 ? -0.05411  29.14397  21.49443  1.000 48.60107 ? 285 ALA B N   1 
ATOM   4429 C CA  . ALA B 1 285 ? 1.05261   29.82288  22.15015  1.000 43.20378 ? 285 ALA B CA  1 
ATOM   4430 C C   . ALA B 1 285 ? 2.36549   29.06660  22.02256  1.000 35.38119 ? 285 ALA B C   1 
ATOM   4431 O O   . ALA B 1 285 ? 3.42385   29.64909  22.27994  1.000 40.17313 ? 285 ALA B O   1 
ATOM   4432 C CB  . ALA B 1 285 ? 0.73719   30.03285  23.63482  1.000 43.70078 ? 285 ALA B CB  1 
ATOM   4433 N N   . LEU B 1 286 ? 2.31954   27.79279  21.63868  1.000 38.82110 ? 286 LEU B N   1 
ATOM   4434 C CA  . LEU B 1 286 ? 3.50698   26.96779  21.45561  1.000 35.82569 ? 286 LEU B CA  1 
ATOM   4435 C C   . LEU B 1 286 ? 3.85406   26.86471  19.97565  1.000 33.76791 ? 286 LEU B C   1 
ATOM   4436 O O   . LEU B 1 286 ? 2.96673   26.76718  19.12561  1.000 38.89638 ? 286 LEU B O   1 
ATOM   4437 C CB  . LEU B 1 286 ? 3.29418   25.55827  22.01179  1.000 41.42530 ? 286 LEU B CB  1 
ATOM   4438 C CG  . LEU B 1 286 ? 2.68383   25.41776  23.40223  1.000 44.86118 ? 286 LEU B CG  1 
ATOM   4439 C CD1 . LEU B 1 286 ? 2.71994   23.96302  23.83426  1.000 42.93662 ? 286 LEU B CD1 1 
ATOM   4440 C CD2 . LEU B 1 286 ? 3.41208   26.30966  24.39592  1.000 38.55963 ? 286 LEU B CD2 1 
ATOM   4441 N N   . LEU B 1 287 ? 5.14980   26.86152  19.67326  1.000 33.97103 ? 287 LEU B N   1 
ATOM   4442 C CA  . LEU B 1 287 ? 5.60508   26.67858  18.30005  1.000 31.89899 ? 287 LEU B CA  1 
ATOM   4443 C C   . LEU B 1 287 ? 5.63461   25.18722  17.97436  1.000 33.48639 ? 287 LEU B C   1 
ATOM   4444 O O   . LEU B 1 287 ? 6.35453   24.42191  18.62472  1.000 41.07442 ? 287 LEU B O   1 
ATOM   4445 C CB  . LEU B 1 287 ? 6.98602   27.30532  18.11649  1.000 31.55185 ? 287 LEU B CB  1 
ATOM   4446 C CG  . LEU B 1 287 ? 7.03784   28.81797  18.37766  1.000 32.48407 ? 287 LEU B CG  1 
ATOM   4447 C CD1 . LEU B 1 287 ? 8.46270   29.29569  18.56946  1.000 33.92593 ? 287 LEU B CD1 1 
ATOM   4448 C CD2 . LEU B 1 287 ? 6.36321   29.56351  17.22981  1.000 34.03270 ? 287 LEU B CD2 1 
ATOM   4449 N N   . GLU B 1 288 ? 4.86819   24.78183  16.96857  1.000 30.90949 ? 288 GLU B N   1 
ATOM   4450 C CA  . GLU B 1 288 ? 4.74229   23.37402  16.60909  1.000 30.18350 ? 288 GLU B CA  1 
ATOM   4451 C C   . GLU B 1 288 ? 5.96739   22.92942  15.82659  1.000 28.82042 ? 288 GLU B C   1 
ATOM   4452 O O   . GLU B 1 288 ? 6.37887   23.62195  14.89822  1.000 26.83135 ? 288 GLU B O   1 
ATOM   4453 C CB  . GLU B 1 288 ? 3.48298   23.16904  15.77225  1.000 27.75468 ? 288 GLU B CB  1 
ATOM   4454 C CG  . GLU B 1 288 ? 3.32925   21.77243  15.18168  1.000 31.10630 ? 288 GLU B CG  1 
ATOM   4455 C CD  . GLU B 1 288 ? 3.07757   20.72223  16.24125  1.000 42.44623 ? 288 GLU B CD  1 
ATOM   4456 O OE1 . GLU B 1 288 ? 2.25185   20.98159  17.14923  1.000 36.99338 ? 288 GLU B OE1 1 
ATOM   4457 O OE2 . GLU B 1 288 ? 3.71694   19.64680  16.16529  1.000 33.93787 ? 288 GLU B OE2 1 
ATOM   4458 N N   . ASP B 1 289 ? 6.54145   21.76595  16.17087  1.000 30.67516 ? 289 ASP B N   1 
ATOM   4459 C CA  . ASP B 1 289 ? 7.71191   21.28286  15.43812  1.000 29.66892 ? 289 ASP B CA  1 
ATOM   4460 C C   . ASP B 1 289 ? 7.55689   19.86341  14.88243  1.000 25.02515 ? 289 ASP B C   1 
ATOM   4461 O O   . ASP B 1 289 ? 8.54560   19.27216  14.45251  1.000 26.89141 ? 289 ASP B O   1 
ATOM   4462 C CB  . ASP B 1 289 ? 8.97623   21.41762  16.29810  1.000 23.90533 ? 289 ASP B CB  1 
ATOM   4463 C CG  . ASP B 1 289 ? 9.18178   20.27211  17.30456  1.000 29.49572 ? 289 ASP B CG  1 
ATOM   4464 O OD1 . ASP B 1 289 ? 8.21301   19.62387  17.74863  1.000 22.28630 ? 289 ASP B OD1 1 
ATOM   4465 O OD2 . ASP B 1 289 ? 10.36362  20.06431  17.67865  1.000 26.38360 ? 289 ASP B OD2 1 
ATOM   4466 N N   . GLU B 1 290 ? 6.34009   19.31925  14.80250  1.000 19.66822 ? 290 GLU B N   1 
ATOM   4467 C CA  . GLU B 1 290 ? 6.14939   18.03268  14.13216  1.000 26.95306 ? 290 GLU B CA  1 
ATOM   4468 C C   . GLU B 1 290 ? 5.29357   18.12137  12.85703  1.000 28.85759 ? 290 GLU B C   1 
ATOM   4469 O O   . GLU B 1 290 ? 4.67019   17.13318  12.45539  1.000 20.70810 ? 290 GLU B O   1 
ATOM   4470 C CB  . GLU B 1 290 ? 5.59401   17.00310  15.12013  1.000 29.61895 ? 290 GLU B CB  1 
ATOM   4471 C CG  . GLU B 1 290 ? 6.60359   16.74415  16.26690  1.000 24.18342 ? 290 GLU B CG  1 
ATOM   4472 C CD  . GLU B 1 290 ? 6.47320   15.37121  16.95230  1.000 32.63502 ? 290 GLU B CD  1 
ATOM   4473 O OE1 . GLU B 1 290 ? 5.40272   14.73126  16.83278  1.000 33.59649 ? 290 GLU B OE1 1 
ATOM   4474 O OE2 . GLU B 1 290 ? 7.45385   14.94100  17.62707  1.000 29.08444 ? 290 GLU B OE2 1 
ATOM   4475 N N   . PHE B 1 291 ? 5.30742   19.27476  12.18100  1.000 24.07821 ? 291 PHE B N   1 
ATOM   4476 C CA  . PHE B 1 291 ? 4.79009   19.45065  10.81922  1.000 28.31641 ? 291 PHE B CA  1 
ATOM   4477 C C   . PHE B 1 291 ? 5.94559   19.81676  9.89667   1.000 28.89815 ? 291 PHE B C   1 
ATOM   4478 O O   . PHE B 1 291 ? 6.52450   20.89443  10.04766  1.000 26.55501 ? 291 PHE B O   1 
ATOM   4479 C CB  . PHE B 1 291 ? 3.75963   20.57925  10.74377  1.000 32.40953 ? 291 PHE B CB  1 
ATOM   4480 C CG  . PHE B 1 291 ? 2.38186   20.18662  11.13968  1.000 39.69264 ? 291 PHE B CG  1 
ATOM   4481 C CD1 . PHE B 1 291 ? 1.61455   19.39151  10.30908  1.000 37.13234 ? 291 PHE B CD1 1 
ATOM   4482 C CD2 . PHE B 1 291 ? 1.83696   20.62941  12.33782  1.000 45.00808 ? 291 PHE B CD2 1 
ATOM   4483 C CE1 . PHE B 1 291 ? 0.32883   19.02417  10.66798  1.000 49.65607 ? 291 PHE B CE1 1 
ATOM   4484 C CE2 . PHE B 1 291 ? 0.54224   20.26651  12.70527  1.000 48.25634 ? 291 PHE B CE2 1 
ATOM   4485 C CZ  . PHE B 1 291 ? -0.20581  19.45969  11.87063  1.000 50.86809 ? 291 PHE B CZ  1 
ATOM   4486 N N   . THR B 1 292 ? 6.23911   18.97224  8.91487   1.000 28.62158 ? 292 THR B N   1 
ATOM   4487 C CA  . THR B 1 292 ? 7.33953   19.23384  7.99242   1.000 27.10803 ? 292 THR B CA  1 
ATOM   4488 C C   . THR B 1 292 ? 6.86658   20.06325  6.80774   1.000 30.38643 ? 292 THR B C   1 
ATOM   4489 O O   . THR B 1 292 ? 5.66975   20.24124  6.55962   1.000 29.90278 ? 292 THR B O   1 
ATOM   4490 C CB  . THR B 1 292 ? 7.93843   17.91855  7.50288   1.000 32.03997 ? 292 THR B CB  1 
ATOM   4491 O OG1 . THR B 1 292 ? 7.12193   17.38288  6.45919   1.000 27.85336 ? 292 THR B OG1 1 
ATOM   4492 C CG2 . THR B 1 292 ? 8.03163   16.91289  8.63713   1.000 35.87683 ? 292 THR B CG2 1 
ATOM   4493 N N   . PRO B 1 293 ? 7.80121   20.60997  6.04100   1.000 25.99873 ? 293 PRO B N   1 
ATOM   4494 C CA  . PRO B 1 293 ? 7.38827   21.37857  4.86394   1.000 32.03147 ? 293 PRO B CA  1 
ATOM   4495 C C   . PRO B 1 293 ? 6.56587   20.54494  3.90230   1.000 35.28382 ? 293 PRO B C   1 
ATOM   4496 O O   . PRO B 1 293 ? 5.56834   21.04221  3.36489   1.000 34.14911 ? 293 PRO B O   1 
ATOM   4497 C CB  . PRO B 1 293 ? 8.71641   21.85376  4.25394   1.000 30.40055 ? 293 PRO B CB  1 
ATOM   4498 C CG  . PRO B 1 293 ? 9.78895   21.07543  4.94421   1.000 40.43917 ? 293 PRO B CG  1 
ATOM   4499 C CD  . PRO B 1 293 ? 9.25514   20.64344  6.26900   1.000 30.42572 ? 293 PRO B CD  1 
ATOM   4500 N N   . PHE B 1 294 ? 6.92541   19.27055  3.71429   1.000 32.85965 ? 294 PHE B N   1 
ATOM   4501 C CA  . PHE B 1 294 ? 6.09297   18.38057  2.90824   1.000 37.25316 ? 294 PHE B CA  1 
ATOM   4502 C C   . PHE B 1 294 ? 4.69280   18.25774  3.48991   1.000 35.54020 ? 294 PHE B C   1 
ATOM   4503 O O   . PHE B 1 294 ? 3.70274   18.27399  2.75360   1.000 44.07726 ? 294 PHE B O   1 
ATOM   4504 C CB  . PHE B 1 294 ? 6.74037   17.00154  2.80134   1.000 43.34396 ? 294 PHE B CB  1 
ATOM   4505 C CG  . PHE B 1 294 ? 8.10089   17.02315  2.17532   1.000 45.02042 ? 294 PHE B CG  1 
ATOM   4506 C CD1 . PHE B 1 294 ? 8.24402   17.16845  0.80239   1.000 48.84899 ? 294 PHE B CD1 1 
ATOM   4507 C CD2 . PHE B 1 294 ? 9.23848   16.89372  2.95649   1.000 49.15942 ? 294 PHE B CD2 1 
ATOM   4508 C CE1 . PHE B 1 294 ? 9.50011   17.19199  0.22253   1.000 54.60372 ? 294 PHE B CE1 1 
ATOM   4509 C CE2 . PHE B 1 294 ? 10.49722  16.91185  2.38386   1.000 47.94531 ? 294 PHE B CE2 1 
ATOM   4510 C CZ  . PHE B 1 294 ? 10.63083  17.06542  1.01887   1.000 49.93808 ? 294 PHE B CZ  1 
ATOM   4511 N N   . ASP B 1 295 ? 4.58557   18.12687  4.81063   1.000 32.55810 ? 295 ASP B N   1 
ATOM   4512 C CA  . ASP B 1 295 ? 3.26269   18.04678  5.41585   1.000 37.94192 ? 295 ASP B CA  1 
ATOM   4513 C C   . ASP B 1 295 ? 2.44099   19.29087  5.09890   1.000 41.66784 ? 295 ASP B C   1 
ATOM   4514 O O   . ASP B 1 295 ? 1.25963   19.18707  4.75665   1.000 44.48785 ? 295 ASP B O   1 
ATOM   4515 C CB  . ASP B 1 295 ? 3.38064   17.84145  6.92790   1.000 35.33265 ? 295 ASP B CB  1 
ATOM   4516 C CG  . ASP B 1 295 ? 4.01993   16.49968  7.29213   1.000 42.30380 ? 295 ASP B CG  1 
ATOM   4517 O OD1 . ASP B 1 295 ? 3.92631   15.54448  6.48077   1.000 42.80206 ? 295 ASP B OD1 1 
ATOM   4518 O OD2 . ASP B 1 295 ? 4.61367   16.39377  8.39088   1.000 29.79000 ? 295 ASP B OD2 1 
ATOM   4519 N N   . VAL B 1 296 ? 3.05052   20.47731  5.20147   1.000 41.28042 ? 296 VAL B N   1 
ATOM   4520 C CA  . VAL B 1 296 ? 2.31784   21.71532  4.94580   1.000 43.76033 ? 296 VAL B CA  1 
ATOM   4521 C C   . VAL B 1 296 ? 1.77908   21.72522  3.51928   1.000 46.17789 ? 296 VAL B C   1 
ATOM   4522 O O   . VAL B 1 296 ? 0.59354   21.98479  3.28396   1.000 55.19393 ? 296 VAL B O   1 
ATOM   4523 C CB  . VAL B 1 296 ? 3.21060   22.93820  5.22695   1.000 36.36627 ? 296 VAL B CB  1 
ATOM   4524 C CG1 . VAL B 1 296 ? 2.48914   24.22184  4.83158   1.000 42.33203 ? 296 VAL B CG1 1 
ATOM   4525 C CG2 . VAL B 1 296 ? 3.61299   22.98506  6.70719   1.000 32.89498 ? 296 VAL B CG2 1 
ATOM   4526 N N   . VAL B 1 297 ? 2.63706   21.41317  2.54856   1.000 41.74852 ? 297 VAL B N   1 
ATOM   4527 C CA  . VAL B 1 297 ? 2.20163   21.34744  1.15261   1.000 45.77284 ? 297 VAL B CA  1 
ATOM   4528 C C   . VAL B 1 297 ? 1.11211   20.29320  0.97121   1.000 51.22861 ? 297 VAL B C   1 
ATOM   4529 O O   . VAL B 1 297 ? 0.03372   20.57276  0.43188   1.000 59.37953 ? 297 VAL B O   1 
ATOM   4530 C CB  . VAL B 1 297 ? 3.40419   21.07784  0.23236   1.000 42.98913 ? 297 VAL B CB  1 
ATOM   4531 C CG1 . VAL B 1 297 ? 2.93454   20.60914  -1.13275  1.000 47.34182 ? 297 VAL B CG1 1 
ATOM   4532 C CG2 . VAL B 1 297 ? 4.26601   22.33522  0.10904   1.000 37.93323 ? 297 VAL B CG2 1 
ATOM   4533 N N   . ARG B 1 298 ? 1.37469   19.06569  1.42097   1.000 49.67906 ? 298 ARG B N   1 
ATOM   4534 C CA  A ARG B 1 298 ? 0.41682   17.98353  1.21262   0.500 49.35279 ? 298 ARG B CA  1 
ATOM   4535 C CA  B ARG B 1 298 ? 0.41780   17.97768  1.22119   0.500 49.34943 ? 298 ARG B CA  1 
ATOM   4536 C C   . ARG B 1 298 ? -0.94674  18.32680  1.80311   1.000 52.78883 ? 298 ARG B C   1 
ATOM   4537 O O   . ARG B 1 298 ? -1.97967  18.16002  1.14329   1.000 55.11092 ? 298 ARG B O   1 
ATOM   4538 C CB  A ARG B 1 298 ? 0.96368   16.69461  1.81734   0.500 44.44678 ? 298 ARG B CB  1 
ATOM   4539 C CB  B ARG B 1 298 ? 0.95515   16.68893  1.84628   0.500 44.44896 ? 298 ARG B CB  1 
ATOM   4540 C CG  A ARG B 1 298 ? 0.39481   15.42388  1.23563   0.500 44.31928 ? 298 ARG B CG  1 
ATOM   4541 C CG  B ARG B 1 298 ? -0.00830  15.51038  1.80433   0.500 45.38641 ? 298 ARG B CG  1 
ATOM   4542 C CD  A ARG B 1 298 ? 1.41844   14.31641  1.40322   0.500 40.58644 ? 298 ARG B CD  1 
ATOM   4543 C CD  B ARG B 1 298 ? 0.52998   14.32521  2.61817   0.500 42.60257 ? 298 ARG B CD  1 
ATOM   4544 N NE  A ARG B 1 298 ? 2.10861   14.44554  2.68013   0.500 38.69216 ? 298 ARG B NE  1 
ATOM   4545 N NE  B ARG B 1 298 ? 0.39033   14.52013  4.05902   0.500 44.95062 ? 298 ARG B NE  1 
ATOM   4546 C CZ  A ARG B 1 298 ? 3.34181   14.02041  2.91391   0.500 37.69916 ? 298 ARG B CZ  1 
ATOM   4547 C CZ  B ARG B 1 298 ? -0.44158  13.83791  4.83669   0.500 32.14336 ? 298 ARG B CZ  1 
ATOM   4548 N NH1 A ARG B 1 298 ? 4.06273   13.43615  1.97193   0.500 42.14860 ? 298 ARG B NH1 1 
ATOM   4549 N NH1 B ARG B 1 298 ? -1.22097  12.88537  4.35238   0.500 29.58826 ? 298 ARG B NH1 1 
ATOM   4550 N NH2 A ARG B 1 298 ? 3.86531   14.18752  4.12280   0.500 40.33741 ? 298 ARG B NH2 1 
ATOM   4551 N NH2 B ARG B 1 298 ? -0.48428  14.11117  6.13464   0.500 30.10554 ? 298 ARG B NH2 1 
ATOM   4552 N N   . GLN B 1 299 ? -0.97060  18.81639  3.04683   1.000 55.01633 ? 299 GLN B N   1 
ATOM   4553 C CA  . GLN B 1 299 ? -2.22682  19.09065  3.73665   1.000 55.11579 ? 299 GLN B CA  1 
ATOM   4554 C C   . GLN B 1 299 ? -2.88054  20.39666  3.30362   1.000 60.84147 ? 299 GLN B C   1 
ATOM   4555 O O   . GLN B 1 299 ? -4.08271  20.57398  3.53404   1.000 63.19369 ? 299 GLN B O   1 
ATOM   4556 C CB  . GLN B 1 299 ? -2.00819  19.10884  5.25339   1.000 46.68344 ? 299 GLN B CB  1 
ATOM   4557 N N   . CYS B 1 300 ? -2.13024  21.31426  2.69475   1.000 59.32468 ? 300 CYS B N   1 
ATOM   4558 C CA  . CYS B 1 300 ? -2.70256  22.56431  2.21170   1.000 58.95758 ? 300 CYS B CA  1 
ATOM   4559 C C   . CYS B 1 300 ? -3.05987  22.52293  0.73068   1.000 67.73963 ? 300 CYS B C   1 
ATOM   4560 O O   . CYS B 1 300 ? -3.65901  23.47979  0.22880   1.000 72.04503 ? 300 CYS B O   1 
ATOM   4561 C CB  . CYS B 1 300 ? -1.74274  23.73685  2.47990   1.000 61.16091 ? 300 CYS B CB  1 
ATOM   4562 S SG  . CYS B 1 300 ? -1.42476  24.11623  4.25919   1.000 75.46402 ? 300 CYS B SG  1 
ATOM   4563 N N   . SER B 1 301 ? -2.72260  21.44061  0.02305   1.000 65.87157 ? 301 SER B N   1 
ATOM   4564 C CA  . SER B 1 301 ? -3.08035  21.29501  -1.37980  1.000 59.83175 ? 301 SER B CA  1 
ATOM   4565 C C   . SER B 1 301 ? -3.92212  20.06305  -1.67788  1.000 63.23803 ? 301 SER B C   1 
ATOM   4566 O O   . SER B 1 301 ? -4.55445  20.01791  -2.73831  1.000 66.96324 ? 301 SER B O   1 
ATOM   4567 C CB  . SER B 1 301 ? -1.81808  21.25540  -2.25974  1.000 63.32755 ? 301 SER B CB  1 
ATOM   4568 O OG  . SER B 1 301 ? -1.21514  19.97406  -2.24605  1.000 63.65926 ? 301 SER B OG  1 
ATOM   4569 N N   . GLY B 1 302 ? -3.95020  19.07250  -0.78924  1.000 62.40218 ? 302 GLY B N   1 
ATOM   4570 C CA  . GLY B 1 302 ? -4.78971  17.90154  -0.97113  1.000 49.66854 ? 302 GLY B CA  1 
ATOM   4571 C C   . GLY B 1 302 ? -4.18647  16.83897  -1.86930  1.000 68.28944 ? 302 GLY B C   1 
ATOM   4572 O O   . GLY B 1 302 ? -4.90973  16.08778  -2.52807  1.000 67.20788 ? 302 GLY B O   1 
HETATM 4573 C C8  . 4WI C 2 .   ? -15.37077 22.26869  2.70272   1.000 29.74682 ? 401 4WI A C8  1 
HETATM 4574 C C3  . 4WI C 2 .   ? -17.78331 19.61954  -0.55913  1.000 25.42704 ? 401 4WI A C3  1 
HETATM 4575 C C1  . 4WI C 2 .   ? -19.47713 22.61998  -0.31967  1.000 28.47899 ? 401 4WI A C1  1 
HETATM 4576 C C13 . 4WI C 2 .   ? -19.88647 25.09590  1.37214   1.000 30.99291 ? 401 4WI A C13 1 
HETATM 4577 C C21 . 4WI C 2 .   ? -21.45796 27.68905  2.97802   1.000 34.28738 ? 401 4WI A C21 1 
HETATM 4578 C C6  . 4WI C 2 .   ? -15.26260 23.03623  0.42861   1.000 26.90007 ? 401 4WI A C6  1 
HETATM 4579 C C7  . 4WI C 2 .   ? -14.38802 23.90797  1.30949   1.000 26.86802 ? 401 4WI A C7  1 
HETATM 4580 C C10 . 4WI C 2 .   ? -21.54519 25.25875  -0.53148  1.000 30.98635 ? 401 4WI A C10 1 
HETATM 4581 C C5  . 4WI C 2 .   ? -16.20514 22.37456  1.42267   1.000 24.77947 ? 401 4WI A C5  1 
HETATM 4582 C C9  . 4WI C 2 .   ? -20.81853 23.08450  0.20156   1.000 27.33504 ? 401 4WI A C9  1 
HETATM 4583 C C11 . 4WI C 2 .   ? -22.27838 24.19080  -1.35324  1.000 27.29304 ? 401 4WI A C11 1 
HETATM 4584 C C12 . 4WI C 2 .   ? -21.95277 22.82989  -0.79851  1.000 24.17636 ? 401 4WI A C12 1 
HETATM 4585 C C18 . 4WI C 2 .   ? -23.24074 23.52529  -0.38259  1.000 27.49467 ? 401 4WI A C18 1 
HETATM 4586 C C19 . 4WI C 2 .   ? -24.49988 23.00648  -0.98676  1.000 26.36134 ? 401 4WI A C19 1 
HETATM 4587 C C20 . 4WI C 2 .   ? -23.46920 23.93736  1.03945   1.000 26.81095 ? 401 4WI A C20 1 
HETATM 4588 C C16 . 4WI C 2 .   ? -17.48943 26.60404  2.17119   1.000 32.58588 ? 401 4WI A C16 1 
HETATM 4589 C C17 . 4WI C 2 .   ? -18.64986 28.70958  1.31741   1.000 31.53888 ? 401 4WI A C17 1 
HETATM 4590 C C23 . 4WI C 2 .   ? -18.17676 26.80844  -0.26152  1.000 34.01078 ? 401 4WI A C23 1 
HETATM 4591 C C4  . 4WI C 2 .   ? -16.63852 20.99656  1.04792   1.000 26.59310 ? 401 4WI A C4  1 
HETATM 4592 C C2  . 4WI C 2 .   ? -17.61918 21.03647  -0.08850  1.000 27.01982 ? 401 4WI A C2  1 
HETATM 4593 C C14 . 4WI C 2 .   ? -19.87256 26.60828  1.43594   1.000 30.55419 ? 401 4WI A C14 1 
HETATM 4594 C C22 . 4WI C 2 .   ? -21.80500 27.93128  4.42091   1.000 37.70703 ? 401 4WI A C22 1 
HETATM 4595 C C15 . 4WI C 2 .   ? -18.51494 27.18131  1.18327   1.000 35.32610 ? 401 4WI A C15 1 
HETATM 4596 N N5  . 4WI C 2 .   ? -17.09395 19.05170  -1.60902  1.000 32.13657 ? 401 4WI A N5  1 
HETATM 4597 N N2  . 4WI C 2 .   ? -14.35958 23.14058  2.55319   1.000 34.57769 ? 401 4WI A N2  1 
HETATM 4598 N N3  . 4WI C 2 .   ? -20.69056 24.53541  0.41749   1.000 24.98846 ? 401 4WI A N3  1 
HETATM 4599 N N1  . 4WI C 2 .   ? -18.92311 21.57312  0.30362   1.000 26.60536 ? 401 4WI A N1  1 
HETATM 4600 N N4  . 4WI C 2 .   ? -20.34716 26.97987  2.77027   1.000 27.88770 ? 401 4WI A N4  1 
HETATM 4601 O O1  . 4WI C 2 .   ? -15.53698 21.49625  3.64103   1.000 27.10326 ? 401 4WI A O1  1 
HETATM 4602 O O2  . 4WI C 2 .   ? -18.88549 23.17922  -1.25077  1.000 30.72543 ? 401 4WI A O2  1 
HETATM 4603 O O3  . 4WI C 2 .   ? -19.21899 24.40139  2.15008   1.000 24.72297 ? 401 4WI A O3  1 
HETATM 4604 O O4  . 4WI C 2 .   ? -22.11971 28.09188  2.02922   1.000 32.48320 ? 401 4WI A O4  1 
HETATM 4605 F F1  . 4WI C 2 .   ? -21.20418 27.05252  5.21957   1.000 41.17536 ? 401 4WI A F1  1 
HETATM 4606 F F2  . 4WI C 2 .   ? -23.12467 27.76927  4.52385   1.000 43.82217 ? 401 4WI A F2  1 
HETATM 4607 F F3  . 4WI C 2 .   ? -21.45457 29.15950  4.77018   1.000 47.98521 ? 401 4WI A F3  1 
HETATM 4608 H H5  . 4WI C 2 .   ? -14.66236 22.28785  -0.08671  1.000 32.29795 ? 401 4WI A H5  1 
HETATM 4609 H H6  . 4WI C 2 .   ? -15.82036 23.64577  -0.28081  1.000 32.29795 ? 401 4WI A H6  1 
HETATM 4610 H H7  . 4WI C 2 .   ? -14.84632 24.88341  1.46569   1.000 32.25948 ? 401 4WI A H7  1 
HETATM 4611 H H8  . 4WI C 2 .   ? -13.38794 24.00294  0.88908   1.000 32.25948 ? 401 4WI A H8  1 
HETATM 4612 H H11 . 4WI C 2 .   ? -22.26674 25.86916  0.00952   1.000 37.20148 ? 401 4WI A H11 1 
HETATM 4613 H H12 . 4WI C 2 .   ? -20.93235 25.87456  -1.18809  1.000 37.20148 ? 401 4WI A H12 1 
HETATM 4614 H H4  . 4WI C 2 .   ? -17.07608 23.01408  1.53163   1.000 29.75323 ? 401 4WI A H4  1 
HETATM 4615 H H10 . 4WI C 2 .   ? -21.15478 22.58745  1.11269   1.000 32.81992 ? 401 4WI A H10 1 
HETATM 4616 H H14 . 4WI C 2 .   ? -22.19076 21.87276  -1.26024  1.000 29.02950 ? 401 4WI A H14 1 
HETATM 4617 H H23 . 4WI C 2 .   ? -25.25717 23.77884  -0.96020  1.000 31.65147 ? 401 4WI A H23 1 
HETATM 4618 H H24 . 4WI C 2 .   ? -24.84123 22.14671  -0.42552  1.000 31.65147 ? 401 4WI A H24 1 
HETATM 4619 H H25 . 4WI C 2 .   ? -24.31475 22.71751  -2.01289  1.000 31.65147 ? 401 4WI A H25 1 
HETATM 4620 H H26 . 4WI C 2 .   ? -22.60113 23.67010  1.64025   1.000 32.19100 ? 401 4WI A H26 1 
HETATM 4621 H H27 . 4WI C 2 .   ? -23.62377 25.01431  1.08644   1.000 32.19100 ? 401 4WI A H27 1 
HETATM 4622 H H28 . 4WI C 2 .   ? -24.34942 23.42838  1.42943   1.000 32.19100 ? 401 4WI A H28 1 
HETATM 4623 H H17 . 4WI C 2 .   ? -17.23050 25.59166  1.87184   1.000 39.12092 ? 401 4WI A H17 1 
HETATM 4624 H H19 . 4WI C 2 .   ? -17.91890 26.58975  3.16965   1.000 39.12092 ? 401 4WI A H19 1 
HETATM 4625 H H18 . 4WI C 2 .   ? -16.59668 27.22416  2.16782   1.000 39.12092 ? 401 4WI A H18 1 
HETATM 4626 H H20 . 4WI C 2 .   ? -19.55870 29.03997  0.81447   1.000 37.86452 ? 401 4WI A H20 1 
HETATM 4627 H H21 . 4WI C 2 .   ? -18.70037 28.97900  2.37238   1.000 37.86452 ? 401 4WI A H21 1 
HETATM 4628 H H22 . 4WI C 2 .   ? -17.78609 29.19243  0.86040   1.000 37.86452 ? 401 4WI A H22 1 
HETATM 4629 H H29 . 4WI C 2 .   ? -17.92103 25.75328  -0.31454  1.000 40.83080 ? 401 4WI A H29 1 
HETATM 4630 H H30 . 4WI C 2 .   ? -17.33230 27.40204  -0.60224  1.000 40.83080 ? 401 4WI A H30 1 
HETATM 4631 H H31 . 4WI C 2 .   ? -19.03575 27.00406  -0.89826  1.000 40.83080 ? 401 4WI A H31 1 
HETATM 4632 H H2  . 4WI C 2 .   ? -15.76772 20.41671  0.74558   1.000 31.92959 ? 401 4WI A H2  1 
HETATM 4633 H H3  . 4WI C 2 .   ? -17.11006 20.52285  1.90766   1.000 31.92959 ? 401 4WI A H3  1 
HETATM 4634 H H32 . 4WI C 2 .   ? -17.23794 21.69604  -0.86527  1.000 32.44165 ? 401 4WI A H32 1 
HETATM 4635 H H15 . 4WI C 2 .   ? -20.51409 27.01046  0.65464   1.000 36.68289 ? 401 4WI A H15 1 
HETATM 4636 H H9  . 4WI C 2 .   ? -13.63801 23.25631  3.24455   1.000 41.51109 ? 401 4WI A H9  1 
HETATM 4637 H H1  . 4WI C 2 .   ? -19.41922 21.14141  1.06621   1.000 31.94429 ? 401 4WI A H1  1 
HETATM 4638 H H16 . 4WI C 2 .   ? -19.81073 26.68684  3.56801   1.000 33.48311 ? 401 4WI A H16 1 
HETATM 4639 C C8  . 4WI D 2 .   ? 6.96100   -0.59976  24.42741  1.000 25.85734 ? 401 4WI B C8  1 
HETATM 4640 C C3  . 4WI D 2 .   ? 7.88614   -5.02406  22.27907  1.000 26.81525 ? 401 4WI B C3  1 
HETATM 4641 C C1  . 4WI D 2 .   ? 10.22946  -4.61458  24.72382  1.000 28.55270 ? 401 4WI B C1  1 
HETATM 4642 C C13 . 4WI D 2 .   ? 11.76108  -2.81389  26.52624  1.000 27.92792 ? 401 4WI B C13 1 
HETATM 4643 C C21 . 4WI D 2 .   ? 14.33777  -1.23816  28.10136  1.000 36.47880 ? 401 4WI B C21 1 
HETATM 4644 C C6  . 4WI D 2 .   ? 6.69404   -2.61891  25.74281  1.000 27.29130 ? 401 4WI B C6  1 
HETATM 4645 C C7  . 4WI D 2 .   ? 6.03599   -1.45428  26.44653  1.000 30.48938 ? 401 4WI B C7  1 
HETATM 4646 C C10 . 4WI D 2 .   ? 12.89534  -5.10081  26.72865  1.000 28.33795 ? 401 4WI B C10 1 
HETATM 4647 C C5  . 4WI D 2 .   ? 7.50999   -2.00397  24.60263  1.000 24.77485 ? 401 4WI B C5  1 
HETATM 4648 C C9  . 4WI D 2 .   ? 11.74385  -4.49524  24.69813  1.000 21.63008 ? 401 4WI B C9  1 
HETATM 4649 C C11 . 4WI D 2 .   ? 13.11278  -6.22794  25.69362  1.000 28.60394 ? 401 4WI B C11 1 
HETATM 4650 C C12 . 4WI D 2 .   ? 12.42810  -5.83452  24.41093  1.000 24.87474 ? 401 4WI B C12 1 
HETATM 4651 C C18 . 4WI D 2 .   ? 13.93091  -5.65948  24.52339  1.000 26.92746 ? 401 4WI B C18 1 
HETATM 4652 C C19 . 4WI D 2 .   ? 14.74513  -6.60715  23.69810  1.000 28.00092 ? 401 4WI B C19 1 
HETATM 4653 C C20 . 4WI D 2 .   ? 14.57045  -4.30194  24.55865  1.000 28.62475 ? 401 4WI B C20 1 
HETATM 4654 C C16 . 4WI D 2 .   ? 10.18381  -1.09899  28.39252  1.000 32.38419 ? 401 4WI B C16 1 
HETATM 4655 C C17 . 4WI D 2 .   ? 11.63234  -2.05773  30.26734  1.000 28.49888 ? 401 4WI B C17 1 
HETATM 4656 C C23 . 4WI D 2 .   ? 10.24513  -3.59412  28.81212  1.000 24.57737 ? 401 4WI B C23 1 
HETATM 4657 C C4  . 4WI D 2 .   ? 7.49430   -2.76701  23.29452  1.000 23.13413 ? 401 4WI B C4  1 
HETATM 4658 C C2  . 4WI D 2 .   ? 8.10903   -4.12637  23.48714  1.000 24.16274 ? 401 4WI B C2  1 
HETATM 4659 C C14 . 4WI D 2 .   ? 12.20164  -2.48392  27.93488  1.000 26.52289 ? 401 4WI B C14 1 
HETATM 4660 C C22 . 4WI D 2 .   ? 14.96080  0.12792   27.93949  1.000 37.98686 ? 401 4WI B C22 1 
HETATM 4661 C C15 . 4WI D 2 .   ? 11.03516  -2.28478  28.86124  1.000 30.71819 ? 401 4WI B C15 1 
HETATM 4662 N N5  . 4WI D 2 .   ? 6.68390   -5.65320  22.04551  1.000 23.49208 ? 401 4WI B N5  1 
HETATM 4663 N N2  . 4WI D 2 .   ? 6.16739   -0.37900  25.47306  1.000 30.10176 ? 401 4WI B N2  1 
HETATM 4664 N N3  . 4WI D 2 .   ? 12.12217  -4.04200  26.04093  1.000 32.33050 ? 401 4WI B N3  1 
HETATM 4665 N N1  . 4WI D 2 .   ? 9.57340   -4.10271  23.67299  1.000 26.41792 ? 401 4WI B N1  1 
HETATM 4666 N N4  . 4WI D 2 .   ? 13.02474  -1.27774  27.86821  1.000 28.94389 ? 401 4WI B N4  1 
HETATM 4667 O O1  . 4WI D 2 .   ? 7.19354   0.19218   23.52426  1.000 24.42645 ? 401 4WI B O1  1 
HETATM 4668 O O2  . 4WI D 2 .   ? 9.59994   -5.11310  25.65933  1.000 26.14335 ? 401 4WI B O2  1 
HETATM 4669 O O3  . 4WI D 2 .   ? 11.11210  -2.00809  25.83262  1.000 26.77468 ? 401 4WI B O3  1 
HETATM 4670 O O4  . 4WI D 2 .   ? 14.95314  -2.24734  28.42510  1.000 33.60519 ? 401 4WI B O4  1 
HETATM 4671 F F1  . 4WI D 2 .   ? 14.49384  0.76080   26.86549  1.000 37.16575 ? 401 4WI B F1  1 
HETATM 4672 F F2  . 4WI D 2 .   ? 16.27839  -0.02613  27.78856  1.000 45.72039 ? 401 4WI B F2  1 
HETATM 4673 F F3  . 4WI D 2 .   ? 14.66627  0.85012   29.00713  1.000 41.00170 ? 401 4WI B F3  1 
HETATM 4674 H H5  . 4WI D 2 .   ? 5.93628   -3.28742  25.33951  1.000 32.76743 ? 401 4WI B H5  1 
HETATM 4675 H H6  . 4WI D 2 .   ? 7.35300   -3.14573  26.42980  1.000 32.76743 ? 401 4WI B H6  1 
HETATM 4676 H H7  . 4WI D 2 .   ? 6.56963   -1.20994  27.36502  1.000 36.60512 ? 401 4WI B H7  1 
HETATM 4677 H H8  . 4WI D 2 .   ? 4.98578   -1.66917  26.64398  1.000 36.60512 ? 401 4WI B H8  1 
HETATM 4678 H H11 . 4WI D 2 .   ? 13.85707  -4.70565  27.05244  1.000 34.02340 ? 401 4WI B H11 1 
HETATM 4679 H H12 . 4WI D 2 .   ? 12.32798  -5.48186  27.57648  1.000 34.02340 ? 401 4WI B H12 1 
HETATM 4680 H H10 . 4WI D 2 .   ? 12.14589  -3.83065  23.93342  1.000 25.97396 ? 401 4WI B H10 1 
HETATM 4681 H H14 . 4WI D 2 .   ? 12.16887  -6.52494  23.60966  1.000 29.86755 ? 401 4WI B H14 1 
HETATM 4682 H H23 . 4WI D 2 .   ? 14.83510  -6.22133  22.69016  1.000 33.61897 ? 401 4WI B H23 1 
HETATM 4683 H H24 . 4WI D 2 .   ? 14.25739  -7.57379  23.67322  1.000 33.61897 ? 401 4WI B H24 1 
HETATM 4684 H H25 . 4WI D 2 .   ? 15.73060  -6.71038  24.13522  1.000 33.61897 ? 401 4WI B H25 1 
HETATM 4685 H H26 . 4WI D 2 .   ? 15.62569  -4.38872  24.30397  1.000 34.36757 ? 401 4WI B H26 1 
HETATM 4686 H H27 . 4WI D 2 .   ? 14.07847  -3.64778  23.84035  1.000 34.36757 ? 401 4WI B H27 1 
HETATM 4687 H H28 . 4WI D 2 .   ? 14.47389  -3.87866  25.55737  1.000 34.36757 ? 401 4WI B H28 1 
HETATM 4688 H H17 . 4WI D 2 .   ? 10.04728  -0.40506  29.21798  1.000 38.87889 ? 401 4WI B H17 1 
HETATM 4689 H H19 . 4WI D 2 .   ? 9.21546   -1.46123  28.05688  1.000 38.87889 ? 401 4WI B H19 1 
HETATM 4690 H H18 . 4WI D 2 .   ? 10.68872  -0.59501  27.57237  1.000 38.87889 ? 401 4WI B H18 1 
HETATM 4691 H H20 . 4WI D 2 .   ? 12.17327  -1.11158  30.28467  1.000 34.21652 ? 401 4WI B H20 1 
HETATM 4692 H H21 . 4WI D 2 .   ? 10.82922  -2.02983  31.00377  1.000 34.21652 ? 401 4WI B H21 1 
HETATM 4693 H H22 . 4WI D 2 .   ? 12.31680  -2.87122  30.50785  1.000 34.21652 ? 401 4WI B H22 1 
HETATM 4694 H H29 . 4WI D 2 .   ? 9.53632   -3.62343  29.63571  1.000 29.51071 ? 401 4WI B H29 1 
HETATM 4695 H H30 . 4WI D 2 .   ? 10.92831  -4.43554  28.89498  1.000 29.51071 ? 401 4WI B H30 1 
HETATM 4696 H H31 . 4WI D 2 .   ? 9.70592   -3.65955  27.87055  1.000 29.51071 ? 401 4WI B H31 1 
HETATM 4697 H H2  . 4WI D 2 .   ? 6.46520   -2.88248  22.95435  1.000 27.77882 ? 401 4WI B H2  1 
HETATM 4698 H H3  . 4WI D 2 .   ? 8.06530   -2.21663  22.54676  1.000 27.77882 ? 401 4WI B H3  1 
HETATM 4699 H H32 . 4WI D 2 .   ? 7.61613   -4.49708  24.38466  1.000 29.01315 ? 401 4WI B H32 1 
HETATM 4700 H H15 . 4WI D 2 .   ? 12.77067  -3.31757  28.34104  1.000 31.84534 ? 401 4WI B H15 1 
HETATM 4701 H H9  . 4WI D 2 .   ? 5.67933   0.49342   25.58583  1.000 36.13998 ? 401 4WI B H9  1 
HETATM 4702 H H1  . 4WI D 2 .   ? 10.12475  -3.66608  22.95089  1.000 31.71937 ? 401 4WI B H1  1 
HETATM 4703 H H16 . 4WI D 2 .   ? 12.56827  -0.41486  27.62924  1.000 34.75053 ? 401 4WI B H16 1 
HETATM 4704 O O   . HOH E 3 .   ? -13.59195 15.12761  -4.87152  1.000 30.22678 ? 501 HOH A O   1 
HETATM 4705 O O   . HOH E 3 .   ? -31.04085 10.11914  11.35289  1.000 32.04886 ? 502 HOH A O   1 
HETATM 4706 O O   . HOH E 3 .   ? -25.08152 19.70474  22.51845  1.000 41.57944 ? 503 HOH A O   1 
HETATM 4707 O O   . HOH E 3 .   ? -26.48089 10.17227  34.99466  1.000 42.81793 ? 504 HOH A O   1 
HETATM 4708 O O   . HOH E 3 .   ? -35.047   27.931    -0.462    1.000 38.42445 ? 505 HOH A O   1 
HETATM 4709 O O   . HOH E 3 .   ? -23.78089 22.34792  45.90055  1.000 42.42179 ? 506 HOH A O   1 
HETATM 4710 O O   . HOH E 3 .   ? -8.50053  10.50505  45.23618  1.000 35.14524 ? 507 HOH A O   1 
HETATM 4711 O O   . HOH E 3 .   ? -34.516   7.729     11.013    1.000 42.12165 ? 508 HOH A O   1 
HETATM 4712 O O   . HOH E 3 .   ? -14.35014 18.10747  16.29752  1.000 28.09568 ? 509 HOH A O   1 
HETATM 4713 O O   . HOH E 3 .   ? -14.13231 8.76633   3.60129   1.000 30.61039 ? 510 HOH A O   1 
HETATM 4714 O O   . HOH E 3 .   ? -17.87610 27.81808  14.65615  1.000 39.32961 ? 511 HOH A O   1 
HETATM 4715 O O   . HOH E 3 .   ? -13.06638 -2.41938  2.64812   1.000 31.44328 ? 512 HOH A O   1 
HETATM 4716 O O   . HOH E 3 .   ? -15.04695 6.61237   22.22879  1.000 35.04290 ? 513 HOH A O   1 
HETATM 4717 O O   . HOH E 3 .   ? -21.07357 5.58855   -14.14407 1.000 31.39403 ? 514 HOH A O   1 
HETATM 4718 O O   . HOH E 3 .   ? -10.06544 10.20656  20.56522  1.000 29.42047 ? 515 HOH A O   1 
HETATM 4719 O O   . HOH E 3 .   ? -29.48882 5.44060   4.40699   1.000 39.24707 ? 516 HOH A O   1 
HETATM 4720 O O   . HOH E 3 .   ? -25.65939 7.12464   10.28821  1.000 33.80444 ? 517 HOH A O   1 
HETATM 4721 O O   . HOH E 3 .   ? 3.46447   18.16608  29.00422  1.000 40.98264 ? 518 HOH A O   1 
HETATM 4722 O O   . HOH E 3 .   ? -25.10118 24.83253  16.46672  1.000 32.18287 ? 519 HOH A O   1 
HETATM 4723 O O   . HOH E 3 .   ? 3.27489   0.90861   28.85644  1.000 36.19361 ? 520 HOH A O   1 
HETATM 4724 O O   . HOH E 3 .   ? -13.53447 7.09286   18.48416  1.000 29.34200 ? 521 HOH A O   1 
HETATM 4725 O O   . HOH E 3 .   ? -15.65731 -6.48097  8.38720   1.000 34.50925 ? 522 HOH A O   1 
HETATM 4726 O O   . HOH E 3 .   ? -22.83723 19.02232  11.38183  1.000 21.99438 ? 523 HOH A O   1 
HETATM 4727 O O   . HOH E 3 .   ? -12.04248 23.10131  11.54793  1.000 34.45949 ? 524 HOH A O   1 
HETATM 4728 O O   . HOH E 3 .   ? -1.72495  7.93638   40.92725  1.000 39.97490 ? 525 HOH A O   1 
HETATM 4729 O O   . HOH E 3 .   ? -10.77600 22.88813  43.38093  1.000 40.75800 ? 526 HOH A O   1 
HETATM 4730 O O   . HOH E 3 .   ? -1.03656  2.81879   23.35764  1.000 34.58430 ? 527 HOH A O   1 
HETATM 4731 O O   . HOH E 3 .   ? -27.08166 13.45126  18.15130  1.000 35.01629 ? 528 HOH A O   1 
HETATM 4732 O O   . HOH E 3 .   ? -7.25530  6.90012   22.06011  1.000 32.44524 ? 529 HOH A O   1 
HETATM 4733 O O   . HOH E 3 .   ? -26.45238 12.74435  36.90981  1.000 39.03793 ? 530 HOH A O   1 
HETATM 4734 O O   . HOH E 3 .   ? -16.97386 10.02919  -11.38861 1.000 34.18193 ? 531 HOH A O   1 
HETATM 4735 O O   . HOH E 3 .   ? -17.80718 11.69580  25.81746  1.000 34.04078 ? 532 HOH A O   1 
HETATM 4736 O O   . HOH E 3 .   ? 1.26445   8.93708   37.71252  1.000 35.95692 ? 533 HOH A O   1 
HETATM 4737 O O   . HOH E 3 .   ? -18.748   -6.877    -8.228    1.000 32.79865 ? 534 HOH A O   1 
HETATM 4738 O O   . HOH E 3 .   ? -16.00766 26.44529  26.51996  1.000 40.58278 ? 535 HOH A O   1 
HETATM 4739 O O   . HOH E 3 .   ? -17.99390 25.33151  16.34469  1.000 34.85404 ? 536 HOH A O   1 
HETATM 4740 O O   . HOH E 3 .   ? -17.11993 7.83887   20.33272  1.000 37.23537 ? 537 HOH A O   1 
HETATM 4741 O O   . HOH E 3 .   ? -13.84076 -2.82215  -4.37596  1.000 34.34205 ? 538 HOH A O   1 
HETATM 4742 O O   . HOH E 3 .   ? -23.68921 17.00651  30.05509  1.000 34.61316 ? 539 HOH A O   1 
HETATM 4743 O O   . HOH E 3 .   ? -14.60760 30.76380  39.38628  1.000 40.16179 ? 540 HOH A O   1 
HETATM 4744 O O   . HOH E 3 .   ? -8.20287  16.93276  3.92130   1.000 39.90716 ? 541 HOH A O   1 
HETATM 4745 O O   . HOH E 3 .   ? -31.27231 20.46053  4.35717   1.000 27.96569 ? 542 HOH A O   1 
HETATM 4746 O O   . HOH E 3 .   ? -25.86817 -0.69778  0.85698   1.000 39.12369 ? 543 HOH A O   1 
HETATM 4747 O O   . HOH E 3 .   ? -27.41915 0.20654   10.26515  1.000 40.49148 ? 544 HOH A O   1 
HETATM 4748 O O   . HOH E 3 .   ? -31.09208 20.23485  7.02078   1.000 22.96764 ? 545 HOH A O   1 
HETATM 4749 O O   . HOH E 3 .   ? -9.99553  14.56355  25.91215  1.000 29.01358 ? 546 HOH A O   1 
HETATM 4750 O O   . HOH E 3 .   ? -20.22521 29.45115  13.15637  1.000 43.10372 ? 547 HOH A O   1 
HETATM 4751 O O   . HOH E 3 .   ? -19.63997 5.68123   14.57289  1.000 30.39208 ? 548 HOH A O   1 
HETATM 4752 O O   . HOH E 3 .   ? -33.00880 16.33689  7.10377   1.000 35.41604 ? 549 HOH A O   1 
HETATM 4753 O O   . HOH E 3 .   ? -3.49953  2.93406   2.35393   1.000 27.95201 ? 550 HOH A O   1 
HETATM 4754 O O   . HOH E 3 .   ? -21.48929 -6.62545  5.03644   1.000 43.27393 ? 551 HOH A O   1 
HETATM 4755 O O   . HOH E 3 .   ? -21.37272 14.84972  45.05698  1.000 35.28592 ? 552 HOH A O   1 
HETATM 4756 O O   . HOH E 3 .   ? -11.35575 18.33070  50.08970  1.000 43.11307 ? 553 HOH A O   1 
HETATM 4757 O O   . HOH E 3 .   ? -23.22857 16.94429  44.56275  1.000 34.71561 ? 554 HOH A O   1 
HETATM 4758 O O   . HOH E 3 .   ? 4.83991   22.16000  31.95301  1.000 44.39266 ? 555 HOH A O   1 
HETATM 4759 O O   . HOH E 3 .   ? -7.76352  8.98009   20.02079  1.000 24.18808 ? 556 HOH A O   1 
HETATM 4760 O O   . HOH E 3 .   ? -10.59111 22.64413  6.49198   1.000 35.18041 ? 557 HOH A O   1 
HETATM 4761 O O   . HOH E 3 .   ? -17.49968 20.92104  47.06432  1.000 37.69462 ? 558 HOH A O   1 
HETATM 4762 O O   . HOH E 3 .   ? -19.24506 16.33499  30.18810  1.000 26.13343 ? 559 HOH A O   1 
HETATM 4763 O O   . HOH E 3 .   ? -32.79090 4.43723   6.95697   1.000 37.71019 ? 560 HOH A O   1 
HETATM 4764 O O   . HOH E 3 .   ? -29.04688 15.85100  16.84089  1.000 44.90869 ? 561 HOH A O   1 
HETATM 4765 O O   . HOH E 3 .   ? -36.31636 9.69166   -4.07349  1.000 38.87783 ? 562 HOH A O   1 
HETATM 4766 O O   . HOH E 3 .   ? -25.94453 17.80006  0.11249   1.000 23.37493 ? 563 HOH A O   1 
HETATM 4767 O O   . HOH E 3 .   ? -31.32444 17.55741  8.11648   1.000 22.48199 ? 564 HOH A O   1 
HETATM 4768 O O   . HOH E 3 .   ? -20.74537 11.34170  42.27690  1.000 37.62688 ? 565 HOH A O   1 
HETATM 4769 O O   . HOH E 3 .   ? -1.22688  23.51401  22.71320  1.000 31.12353 ? 566 HOH A O   1 
HETATM 4770 O O   . HOH E 3 .   ? -9.95682  -2.71168  10.70543  1.000 37.56856 ? 567 HOH A O   1 
HETATM 4771 O O   . HOH E 3 .   ? 3.83052   14.60337  29.40609  1.000 44.15016 ? 568 HOH A O   1 
HETATM 4772 O O   . HOH E 3 .   ? -1.21435  11.59754  15.98898  1.000 38.75964 ? 569 HOH A O   1 
HETATM 4773 O O   . HOH E 3 .   ? -18.14653 2.53179   37.54495  1.000 41.77879 ? 570 HOH A O   1 
HETATM 4774 O O   . HOH E 3 .   ? -17.21696 15.02572  47.52340  1.000 37.47202 ? 571 HOH A O   1 
HETATM 4775 O O   . HOH E 3 .   ? -28.87041 17.79643  15.57382  1.000 33.35514 ? 572 HOH A O   1 
HETATM 4776 O O   . HOH E 3 .   ? -27.82109 5.43002   16.26582  1.000 35.36160 ? 573 HOH A O   1 
HETATM 4777 O O   . HOH E 3 .   ? -36.29579 11.92467  1.72880   1.000 37.83954 ? 574 HOH A O   1 
HETATM 4778 O O   . HOH E 3 .   ? -15.63144 10.38693  43.15733  1.000 33.20206 ? 575 HOH A O   1 
HETATM 4779 O O   . HOH E 3 .   ? -7.75023  25.35588  28.04534  1.000 37.89369 ? 576 HOH A O   1 
HETATM 4780 O O   . HOH E 3 .   ? -22.48572 12.29951  26.92311  1.000 41.51704 ? 577 HOH A O   1 
HETATM 4781 O O   . HOH E 3 .   ? -14.51839 7.80892   41.90856  1.000 40.67977 ? 578 HOH A O   1 
HETATM 4782 O O   . HOH E 3 .   ? -10.05713 24.26545  -0.06345  1.000 38.44922 ? 579 HOH A O   1 
HETATM 4783 O O   . HOH E 3 .   ? -15.04452 28.76208  4.31998   1.000 45.11775 ? 580 HOH A O   1 
HETATM 4784 O O   . HOH E 3 .   ? -23.21279 -5.60232  7.53369   1.000 31.26386 ? 581 HOH A O   1 
HETATM 4785 O O   . HOH E 3 .   ? -9.27675  19.86398  21.95656  1.000 41.03736 ? 582 HOH A O   1 
HETATM 4786 O O   . HOH E 3 .   ? -31.50119 17.67088  10.59959  1.000 37.05799 ? 583 HOH A O   1 
HETATM 4787 O O   . HOH E 3 .   ? -15.97801 21.59422  -3.47666  1.000 31.49293 ? 584 HOH A O   1 
HETATM 4788 O O   . HOH E 3 .   ? -23.39168 20.13730  46.96516  1.000 42.73642 ? 585 HOH A O   1 
HETATM 4789 O O   . HOH E 3 .   ? -34.90418 5.15957   -9.92794  1.000 39.68419 ? 586 HOH A O   1 
HETATM 4790 O O   . HOH E 3 .   ? -32.02518 20.05398  11.63802  1.000 35.85602 ? 587 HOH A O   1 
HETATM 4791 O O   . HOH E 3 .   ? -11.27355 6.62320   -7.80448  1.000 40.46309 ? 588 HOH A O   1 
HETATM 4792 O O   . HOH E 3 .   ? -31.96931 11.42706  13.62555  1.000 38.18747 ? 589 HOH A O   1 
HETATM 4793 O O   . HOH E 3 .   ? -28.24511 6.65936   11.13469  1.000 38.93893 ? 590 HOH A O   1 
HETATM 4794 O O   . HOH E 3 .   ? -10.80478 -3.52496  2.52899   1.000 39.82489 ? 591 HOH A O   1 
HETATM 4795 O O   . HOH E 3 .   ? -21.62143 31.62828  1.97711   1.000 41.83455 ? 592 HOH A O   1 
HETATM 4796 O O   . HOH E 3 .   ? -34.206   29.930    2.978     1.000 49.74718 ? 593 HOH A O   1 
HETATM 4797 O O   . HOH E 3 .   ? -19.24424 20.31471  -4.41880  1.000 38.25465 ? 594 HOH A O   1 
HETATM 4798 O O   . HOH E 3 .   ? -20.38380 13.81138  26.44780  1.000 38.15812 ? 595 HOH A O   1 
HETATM 4799 O O   . HOH E 3 .   ? -26.76963 24.90623  18.40554  1.000 47.67673 ? 596 HOH A O   1 
HETATM 4800 O O   . HOH E 3 .   ? -19.76956 -9.50539  -1.47221  1.000 47.26957 ? 597 HOH A O   1 
HETATM 4801 O O   . HOH E 3 .   ? -3.33452  4.56915   0.19376   1.000 33.30906 ? 598 HOH A O   1 
HETATM 4802 O O   . HOH E 3 .   ? -31.019   6.241     14.444    1.000 41.60659 ? 599 HOH A O   1 
HETATM 4803 O O   . HOH E 3 .   ? -20.80714 16.06352  27.67539  1.000 41.32667 ? 600 HOH A O   1 
HETATM 4804 O O   . HOH E 3 .   ? -32.87390 14.05518  13.09713  1.000 39.56862 ? 601 HOH A O   1 
HETATM 4805 O O   . HOH E 3 .   ? -21.79282 12.59548  44.04663  1.000 40.51487 ? 602 HOH A O   1 
HETATM 4806 O O   . HOH E 3 .   ? -18.15442 9.36939   26.21864  1.000 38.57792 ? 603 HOH A O   1 
HETATM 4807 O O   . HOH E 3 .   ? -31.846   8.558     14.997    1.000 40.59636 ? 604 HOH A O   1 
HETATM 4808 O O   . HOH E 3 .   ? -18.40624 9.87758   42.87727  1.000 47.17081 ? 605 HOH A O   1 
HETATM 4809 O O   . HOH F 3 .   ? 1.33009   24.88056  18.91574  1.000 40.70045 ? 501 HOH B O   1 
HETATM 4810 O O   . HOH F 3 .   ? 11.91829  37.72329  1.98411   1.000 35.77889 ? 502 HOH B O   1 
HETATM 4811 O O   . HOH F 3 .   ? 20.03082  1.26771   7.11333   1.000 38.68390 ? 503 HOH B O   1 
HETATM 4812 O O   . HOH F 3 .   ? 10.19026  27.06721  21.09808  1.000 41.18429 ? 504 HOH B O   1 
HETATM 4813 O O   . HOH F 3 .   ? 5.97783   20.20588  18.56051  1.000 37.90077 ? 505 HOH B O   1 
HETATM 4814 O O   . HOH F 3 .   ? 3.27129   14.80445  15.57248  1.000 36.70881 ? 506 HOH B O   1 
HETATM 4815 O O   . HOH F 3 .   ? 19.12940  -21.21768 12.39387  1.000 38.06956 ? 507 HOH B O   1 
HETATM 4816 O O   . HOH F 3 .   ? 15.58460  -25.98327 15.67369  1.000 39.27178 ? 508 HOH B O   1 
HETATM 4817 O O   . HOH F 3 .   ? -0.84978  -6.22249  -4.47993  1.000 34.91316 ? 509 HOH B O   1 
HETATM 4818 O O   . HOH F 3 .   ? -1.10109  -5.18727  24.67888  1.000 41.18724 ? 510 HOH B O   1 
HETATM 4819 O O   . HOH F 3 .   ? 17.44977  -20.66868 20.22675  1.000 38.99058 ? 511 HOH B O   1 
HETATM 4820 O O   . HOH F 3 .   ? 21.11535  9.91442   9.58814   1.000 41.31444 ? 512 HOH B O   1 
HETATM 4821 O O   . HOH F 3 .   ? 5.406     38.203    0.043     1.000 36.50433 ? 513 HOH B O   1 
HETATM 4822 O O   . HOH F 3 .   ? 4.50239   -20.55804 10.36491  1.000 25.73752 ? 514 HOH B O   1 
HETATM 4823 O O   . HOH F 3 .   ? 15.28449  27.15007  -0.58031  1.000 35.32585 ? 515 HOH B O   1 
HETATM 4824 O O   . HOH F 3 .   ? 8.97376   2.73930   30.22795  1.000 40.90770 ? 516 HOH B O   1 
HETATM 4825 O O   . HOH F 3 .   ? 19.46053  16.27821  8.94983   1.000 34.33972 ? 517 HOH B O   1 
HETATM 4826 O O   . HOH F 3 .   ? 2.97999   15.29000  10.10570  1.000 41.15162 ? 518 HOH B O   1 
HETATM 4827 O O   . HOH F 3 .   ? 1.68836   -8.79129  19.60770  1.000 26.44307 ? 519 HOH B O   1 
HETATM 4828 O O   . HOH F 3 .   ? 7.78218   11.99382  17.93827  1.000 26.17752 ? 520 HOH B O   1 
HETATM 4829 O O   . HOH F 3 .   ? 20.32573  15.80139  4.91571   1.000 37.91896 ? 521 HOH B O   1 
HETATM 4830 O O   . HOH F 3 .   ? -3.23645  33.06318  16.20399  1.000 41.76294 ? 522 HOH B O   1 
HETATM 4831 O O   . HOH F 3 .   ? 0.83266   42.02284  7.12026   1.000 45.00706 ? 523 HOH B O   1 
HETATM 4832 O O   . HOH F 3 .   ? 25.92782  28.13054  19.67955  1.000 35.88268 ? 524 HOH B O   1 
HETATM 4833 O O   . HOH F 3 .   ? 22.73982  -8.90917  13.33896  1.000 37.90713 ? 525 HOH B O   1 
HETATM 4834 O O   . HOH F 3 .   ? -3.14128  -21.04077 12.55911  1.000 41.60737 ? 526 HOH B O   1 
HETATM 4835 O O   . HOH F 3 .   ? -1.98207  -3.87507  1.27830   1.000 29.64155 ? 527 HOH B O   1 
HETATM 4836 O O   . HOH F 3 .   ? 26.82153  27.39019  9.28528   1.000 31.18286 ? 528 HOH B O   1 
HETATM 4837 O O   . HOH F 3 .   ? 15.25515  4.73235   17.67469  1.000 23.32936 ? 529 HOH B O   1 
HETATM 4838 O O   . HOH F 3 .   ? -2.92042  -10.71392 2.35411   1.000 29.26822 ? 530 HOH B O   1 
HETATM 4839 O O   . HOH F 3 .   ? 19.04118  17.56221  6.48873   1.000 30.89945 ? 531 HOH B O   1 
HETATM 4840 O O   . HOH F 3 .   ? -4.77358  38.19335  7.64390   1.000 43.98702 ? 532 HOH B O   1 
HETATM 4841 O O   . HOH F 3 .   ? 20.63200  19.76852  12.12928  1.000 29.29249 ? 533 HOH B O   1 
HETATM 4842 O O   . HOH F 3 .   ? 4.95034   -7.26049  -5.52053  1.000 39.07123 ? 534 HOH B O   1 
HETATM 4843 O O   . HOH F 3 .   ? 20.802    14.889    0.625     1.000 27.85827 ? 535 HOH B O   1 
HETATM 4844 O O   . HOH F 3 .   ? 2.31264   -1.71236  11.73576  1.000 28.30761 ? 536 HOH B O   1 
HETATM 4845 O O   . HOH F 3 .   ? 15.61952  -5.85108  5.27620   1.000 29.13770 ? 537 HOH B O   1 
HETATM 4846 O O   . HOH F 3 .   ? -0.33440  36.21173  4.23111   1.000 28.10733 ? 538 HOH B O   1 
HETATM 4847 O O   . HOH F 3 .   ? 13.72304  1.12126   6.31140   1.000 26.30994 ? 539 HOH B O   1 
HETATM 4848 O O   . HOH F 3 .   ? 11.96077  1.86174   29.76653  1.000 39.68828 ? 540 HOH B O   1 
HETATM 4849 O O   . HOH F 3 .   ? 15.04120  -6.79817  18.56293  1.000 24.11428 ? 541 HOH B O   1 
HETATM 4850 O O   . HOH F 3 .   ? 2.11706   -16.17212 15.43318  1.000 27.21899 ? 542 HOH B O   1 
HETATM 4851 O O   . HOH F 3 .   ? 15.15599  -19.20456 21.27725  1.000 33.65543 ? 543 HOH B O   1 
HETATM 4852 O O   . HOH F 3 .   ? 5.88603   21.89811  12.62869  1.000 23.68039 ? 544 HOH B O   1 
HETATM 4853 O O   . HOH F 3 .   ? 12.15810  10.06914  3.27807   1.000 40.81757 ? 545 HOH B O   1 
HETATM 4854 O O   . HOH F 3 .   ? 20.08651  -6.64765  32.13480  1.000 38.82251 ? 546 HOH B O   1 
HETATM 4855 O O   . HOH F 3 .   ? -2.55251  -10.54061 10.68402  1.000 34.27935 ? 547 HOH B O   1 
HETATM 4856 O O   . HOH F 3 .   ? 19.80935  -1.91764  33.83920  1.000 45.19667 ? 548 HOH B O   1 
HETATM 4857 O O   . HOH F 3 .   ? 15.86889  -24.41112 9.37029   1.000 41.09830 ? 549 HOH B O   1 
HETATM 4858 O O   . HOH F 3 .   ? -4.419    38.210    4.911     1.000 37.96472 ? 550 HOH B O   1 
HETATM 4859 O O   . HOH F 3 .   ? -4.45483  1.26718   20.62574  1.000 39.40463 ? 551 HOH B O   1 
HETATM 4860 O O   . HOH F 3 .   ? 14.88893  7.69118   28.58604  1.000 35.11073 ? 552 HOH B O   1 
HETATM 4861 O O   . HOH F 3 .   ? 22.451    27.947    2.205     1.000 35.72341 ? 553 HOH B O   1 
HETATM 4862 O O   . HOH F 3 .   ? -0.63717  1.75221   20.81080  1.000 33.90847 ? 554 HOH B O   1 
HETATM 4863 O O   . HOH F 3 .   ? 24.014    22.248    10.027    1.000 25.31860 ? 555 HOH B O   1 
HETATM 4864 O O   . HOH F 3 .   ? 15.04282  31.81956  0.48064   1.000 35.87811 ? 556 HOH B O   1 
HETATM 4865 O O   . HOH F 3 .   ? 6.97216   -22.50615 9.99536   1.000 33.84988 ? 557 HOH B O   1 
HETATM 4866 O O   . HOH F 3 .   ? -9.63566  -0.90690  8.87844   1.000 27.18817 ? 558 HOH B O   1 
HETATM 4867 O O   . HOH F 3 .   ? 19.61476  9.54113   22.30814  1.000 39.40598 ? 559 HOH B O   1 
HETATM 4868 O O   . HOH F 3 .   ? 9.88216   -8.61678  0.54798   1.000 25.68753 ? 560 HOH B O   1 
HETATM 4869 O O   . HOH F 3 .   ? 16.90468  5.55315   2.62744   1.000 34.45084 ? 561 HOH B O   1 
HETATM 4870 O O   . HOH F 3 .   ? -7.01312  -4.28915  9.42807   1.000 36.70008 ? 562 HOH B O   1 
HETATM 4871 O O   . HOH F 3 .   ? 16.69384  -8.89640  1.74646   1.000 44.86705 ? 563 HOH B O   1 
HETATM 4872 O O   . HOH F 3 .   ? 8.99005   7.01637   5.08020   1.000 23.50115 ? 564 HOH B O   1 
HETATM 4873 O O   . HOH F 3 .   ? 21.34325  6.56121   14.24623  1.000 38.59467 ? 565 HOH B O   1 
HETATM 4874 O O   . HOH F 3 .   ? 18.865    19.391    -2.460    1.000 48.34808 ? 566 HOH B O   1 
HETATM 4875 O O   . HOH F 3 .   ? 21.96620  18.90984  3.83855   1.000 24.62096 ? 567 HOH B O   1 
HETATM 4876 O O   . HOH F 3 .   ? 21.83529  4.87589   26.95160  1.000 42.13211 ? 568 HOH B O   1 
HETATM 4877 O O   . HOH F 3 .   ? 21.37412  -3.84007  19.11870  1.000 31.36390 ? 569 HOH B O   1 
HETATM 4878 O O   . HOH F 3 .   ? 12.88127  11.49696  26.33562  1.000 38.50785 ? 570 HOH B O   1 
HETATM 4879 O O   . HOH F 3 .   ? 7.19850   26.96275  21.68036  1.000 39.33150 ? 571 HOH B O   1 
HETATM 4880 O O   . HOH F 3 .   ? 0.48822   -0.02156  -4.21712  1.000 30.28372 ? 572 HOH B O   1 
HETATM 4881 O O   . HOH F 3 .   ? 22.06555  -1.58826  17.87575  1.000 29.42960 ? 573 HOH B O   1 
HETATM 4882 O O   . HOH F 3 .   ? 13.01149  11.81205  23.80831  1.000 30.05784 ? 574 HOH B O   1 
HETATM 4883 O O   . HOH F 3 .   ? 7.62669   -21.97159 18.53796  1.000 32.57588 ? 575 HOH B O   1 
HETATM 4884 O O   . HOH F 3 .   ? 21.51647  -1.33209  15.23341  1.000 27.56566 ? 576 HOH B O   1 
HETATM 4885 O O   . HOH F 3 .   ? 13.64269  -0.86039  -0.89716  1.000 38.21224 ? 577 HOH B O   1 
HETATM 4886 O O   . HOH F 3 .   ? 21.48435  -14.96405 9.51625   1.000 39.65303 ? 578 HOH B O   1 
HETATM 4887 O O   . HOH F 3 .   ? -1.871    -23.636   12.046    1.000 41.96096 ? 579 HOH B O   1 
HETATM 4888 O O   . HOH F 3 .   ? 22.00635  2.79352   24.76766  1.000 43.73954 ? 580 HOH B O   1 
HETATM 4889 O O   . HOH F 3 .   ? 5.13254   -21.43097 19.30328  1.000 25.68486 ? 581 HOH B O   1 
HETATM 4890 O O   . HOH F 3 .   ? 21.95478  22.82050  21.55725  1.000 37.48524 ? 582 HOH B O   1 
HETATM 4891 O O   . HOH F 3 .   ? 5.99360   8.90833   23.91551  1.000 33.32482 ? 583 HOH B O   1 
HETATM 4892 O O   . HOH F 3 .   ? 21.21734  22.22989  19.08217  1.000 38.62483 ? 584 HOH B O   1 
HETATM 4893 O O   . HOH F 3 .   ? 6.01692   -6.67294  24.82019  1.000 31.44222 ? 585 HOH B O   1 
HETATM 4894 O O   . HOH F 3 .   ? 19.07324  8.77860   10.52467  1.000 39.81403 ? 586 HOH B O   1 
HETATM 4895 O O   . HOH F 3 .   ? 20.12012  14.67658  15.05246  1.000 29.48182 ? 587 HOH B O   1 
HETATM 4896 O O   . HOH F 3 .   ? 22.69510  2.09058   14.19959  1.000 39.65372 ? 588 HOH B O   1 
HETATM 4897 O O   . HOH F 3 .   ? 16.28589  21.76232  11.74085  1.000 29.42558 ? 589 HOH B O   1 
HETATM 4898 O O   . HOH F 3 .   ? 15.05729  -18.58868 30.02561  1.000 43.01746 ? 590 HOH B O   1 
HETATM 4899 O O   . HOH F 3 .   ? 23.50273  -9.28469  10.77042  1.000 49.09187 ? 591 HOH B O   1 
HETATM 4900 O O   . HOH F 3 .   ? 17.23824  32.81850  2.20248   1.000 34.24605 ? 592 HOH B O   1 
HETATM 4901 O O   . HOH F 3 .   ? 23.96199  32.64757  4.66077   1.000 42.59320 ? 593 HOH B O   1 
HETATM 4902 O O   . HOH F 3 .   ? 24.12962  -10.74814 20.76458  1.000 46.99695 ? 594 HOH B O   1 
HETATM 4903 O O   . HOH F 3 .   ? 11.89523  17.80528  8.19166   1.000 34.84462 ? 595 HOH B O   1 
HETATM 4904 O O   . HOH F 3 .   ? 17.46303  -20.56229 6.05666   1.000 35.27187 ? 596 HOH B O   1 
HETATM 4905 O O   . HOH F 3 .   ? 1.59552   -2.40275  28.55516  1.000 41.47881 ? 597 HOH B O   1 
HETATM 4906 O O   . HOH F 3 .   ? -3.835    -22.441   8.441     1.000 36.06863 ? 598 HOH B O   1 
HETATM 4907 O O   . HOH F 3 .   ? 5.25235   -4.93783  -5.18199  1.000 44.79810 ? 599 HOH B O   1 
HETATM 4908 O O   . HOH F 3 .   ? -4.46095  -3.72623  1.11584   1.000 32.36050 ? 600 HOH B O   1 
HETATM 4909 O O   . HOH F 3 .   ? 15.58624  -15.39150 4.12381   1.000 43.14934 ? 601 HOH B O   1 
HETATM 4910 O O   . HOH F 3 .   ? 16.44842  19.08846  12.34849  1.000 39.93093 ? 602 HOH B O   1 
HETATM 4911 O O   . HOH F 3 .   ? 9.92504   8.69453   3.08144   1.000 41.25169 ? 603 HOH B O   1 
HETATM 4912 O O   . HOH F 3 .   ? 13.43708  -5.19143  -0.33553  1.000 43.47626 ? 604 HOH B O   1 
HETATM 4913 O O   . HOH F 3 .   ? 8.73980   30.91719  21.81705  1.000 48.98791 ? 605 HOH B O   1 
HETATM 4914 O O   . HOH F 3 .   ? 6.81452   -2.11141  30.63742  1.000 50.15361 ? 606 HOH B O   1 
HETATM 4915 O O   . HOH F 3 .   ? 8.36864   -9.70450  23.91452  1.000 39.30057 ? 607 HOH B O   1 
HETATM 4916 O O   . HOH F 3 .   ? 18.38051  35.22027  1.59447   1.000 38.49830 ? 608 HOH B O   1 
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