data_9N7R
# 
_entry.id   9N7R 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9N7R         pdb_00009n7r 10.2210/pdb9n7r/pdb 
WWPDB D_1000292681 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9N7R 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-06 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              kiefer.james@gene.com 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_last          Kiefer 
_pdbx_contact_author.name_mi            R 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6317-0902 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Walters, B.T.' 1 0000-0001-5400-0696 
'Kiefer, J.R.'  2 0000-0001-6317-0902 
'Hsu, P.L.'     3 0000-0002-9381-6564 
'Wang, W.'      4 ?                   
'Wu, P.'        5 ?                   
# 
_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            J.Chem.Inf.Model. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1549-960X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Integrating Hydrogen Exchange with Molecular Dynamics for Improved Ligand Binding Predictions.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jcim.5c00397 
_citation.pdbx_database_id_PubMed   40495786 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Walters, B.T.'  1 ? 
primary 'Patapoff, A.W.' 2 ? 
primary 'Kiefer, J.R.'   3 ? 
primary 'Wu, P.'         4 ? 
primary 'Wang, W.'       5 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Mitogen-activated protein kinase kinase kinase kinase 1' 35018.434 2   2.7.11.1 ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL 62.068    9   ?        ? ? ? 
3 non-polymer syn GLYCEROL 92.094    1   ?        ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    2   ?        ? ? ? 
5 non-polymer syn 
"N-(3,5-difluoro-4-{[3-(trifluoromethyl)-1H-pyrrolo[2,3-b]pyridin-4-yl]oxy}phenyl)-N'-[3-(morpholin-4-yl)propyl]urea" 499.434   5 
?        ? ? ? 
6 water       nat water 18.015    232 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Hematopoietic progenitor kinase,MAPK/ERK kinase kinase kinase 1,MEK kinase kinase 1,MEKKK 1' 
# 
_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       
;MHHHHHHGENLYFQGSDVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILI
LKTCRHANIVAYHGSYLWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILI
NDAGEVRLADFGISAQIGAELARRLEFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLF
LMTKSGYQPPRLKEKGKWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKNGNS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGENLYFQGSDVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILI
LKTCRHANIVAYHGSYLWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILI
NDAGEVRLADFGISAQIGAELARRLEFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLF
LMTKSGYQPPRLKEKGKWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKNGNS
;
_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 1,2-ETHANEDIOL                                                                                                        EDO   
3 GLYCEROL                                                                                                              GOL   
4 'DIMETHYL SULFOXIDE'                                                                                                  DMS   
5 "N-(3,5-difluoro-4-{[3-(trifluoromethyl)-1H-pyrrolo[2,3-b]pyridin-4-yl]oxy}phenyl)-N'-[3-(morpholin-4-yl)propyl]urea" A1BWC 
6 water                                                                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLY n 
1 9   GLU n 
1 10  ASN n 
1 11  LEU n 
1 12  TYR n 
1 13  PHE n 
1 14  GLN n 
1 15  GLY n 
1 16  SER n 
1 17  ASP n 
1 18  VAL n 
1 19  VAL n 
1 20  ASP n 
1 21  PRO n 
1 22  ASP n 
1 23  ILE n 
1 24  PHE n 
1 25  ASN n 
1 26  ARG n 
1 27  ASP n 
1 28  PRO n 
1 29  ARG n 
1 30  ASP n 
1 31  HIS n 
1 32  TYR n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  GLN n 
1 37  ARG n 
1 38  LEU n 
1 39  GLY n 
1 40  GLY n 
1 41  GLY n 
1 42  THR n 
1 43  TYR n 
1 44  GLY n 
1 45  GLU n 
1 46  VAL n 
1 47  PHE n 
1 48  LYS n 
1 49  ALA n 
1 50  ARG n 
1 51  ASP n 
1 52  LYS n 
1 53  VAL n 
1 54  SER n 
1 55  GLY n 
1 56  ASP n 
1 57  LEU n 
1 58  VAL n 
1 59  ALA n 
1 60  LEU n 
1 61  LYS n 
1 62  MET n 
1 63  VAL n 
1 64  LYS n 
1 65  MET n 
1 66  GLU n 
1 67  PRO n 
1 68  ASP n 
1 69  ASP n 
1 70  ASP n 
1 71  VAL n 
1 72  SER n 
1 73  THR n 
1 74  LEU n 
1 75  GLN n 
1 76  LYS n 
1 77  GLU n 
1 78  ILE n 
1 79  LEU n 
1 80  ILE n 
1 81  LEU n 
1 82  LYS n 
1 83  THR n 
1 84  CYS n 
1 85  ARG n 
1 86  HIS n 
1 87  ALA n 
1 88  ASN n 
1 89  ILE n 
1 90  VAL n 
1 91  ALA n 
1 92  TYR n 
1 93  HIS n 
1 94  GLY n 
1 95  SER n 
1 96  TYR n 
1 97  LEU n 
1 98  TRP n 
1 99  LEU n 
1 100 GLN n 
1 101 LYS n 
1 102 LEU n 
1 103 TRP n 
1 104 ILE n 
1 105 CYS n 
1 106 MET n 
1 107 GLU n 
1 108 PHE n 
1 109 CYS n 
1 110 GLY n 
1 111 ALA n 
1 112 GLY n 
1 113 SER n 
1 114 LEU n 
1 115 GLN n 
1 116 ASP n 
1 117 ILE n 
1 118 TYR n 
1 119 GLN n 
1 120 VAL n 
1 121 THR n 
1 122 GLY n 
1 123 SER n 
1 124 LEU n 
1 125 SER n 
1 126 GLU n 
1 127 LEU n 
1 128 GLN n 
1 129 ILE n 
1 130 SER n 
1 131 TYR n 
1 132 VAL n 
1 133 CYS n 
1 134 ARG n 
1 135 GLU n 
1 136 VAL n 
1 137 LEU n 
1 138 GLN n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 TYR n 
1 143 LEU n 
1 144 HIS n 
1 145 SER n 
1 146 GLN n 
1 147 LYS n 
1 148 LYS n 
1 149 ILE n 
1 150 HIS n 
1 151 ARG n 
1 152 ASP n 
1 153 ILE n 
1 154 LYS n 
1 155 GLY n 
1 156 ALA n 
1 157 ASN n 
1 158 ILE n 
1 159 LEU n 
1 160 ILE n 
1 161 ASN n 
1 162 ASP n 
1 163 ALA n 
1 164 GLY n 
1 165 GLU n 
1 166 VAL n 
1 167 ARG n 
1 168 LEU n 
1 169 ALA n 
1 170 ASP n 
1 171 PHE n 
1 172 GLY n 
1 173 ILE n 
1 174 SER n 
1 175 ALA n 
1 176 GLN n 
1 177 ILE n 
1 178 GLY n 
1 179 ALA n 
1 180 GLU n 
1 181 LEU n 
1 182 ALA n 
1 183 ARG n 
1 184 ARG n 
1 185 LEU n 
1 186 GLU n 
1 187 PHE n 
1 188 ILE n 
1 189 GLY n 
1 190 THR n 
1 191 PRO n 
1 192 TYR n 
1 193 TRP n 
1 194 MET n 
1 195 ALA n 
1 196 PRO n 
1 197 GLU n 
1 198 VAL n 
1 199 ALA n 
1 200 ALA n 
1 201 VAL n 
1 202 ALA n 
1 203 LEU n 
1 204 LYS n 
1 205 GLY n 
1 206 GLY n 
1 207 TYR n 
1 208 ASN n 
1 209 GLU n 
1 210 LEU n 
1 211 CYS n 
1 212 ASP n 
1 213 ILE n 
1 214 TRP n 
1 215 SER n 
1 216 LEU n 
1 217 GLY n 
1 218 ILE n 
1 219 THR n 
1 220 ALA n 
1 221 ILE n 
1 222 GLU n 
1 223 LEU n 
1 224 ALA n 
1 225 GLU n 
1 226 LEU n 
1 227 GLN n 
1 228 PRO n 
1 229 PRO n 
1 230 LEU n 
1 231 PHE n 
1 232 ASP n 
1 233 VAL n 
1 234 HIS n 
1 235 PRO n 
1 236 LEU n 
1 237 ARG n 
1 238 VAL n 
1 239 LEU n 
1 240 PHE n 
1 241 LEU n 
1 242 MET n 
1 243 THR n 
1 244 LYS n 
1 245 SER n 
1 246 GLY n 
1 247 TYR n 
1 248 GLN n 
1 249 PRO n 
1 250 PRO n 
1 251 ARG n 
1 252 LEU n 
1 253 LYS n 
1 254 GLU n 
1 255 LYS n 
1 256 GLY n 
1 257 LYS n 
1 258 TRP n 
1 259 SER n 
1 260 ALA n 
1 261 ALA n 
1 262 PHE n 
1 263 HIS n 
1 264 ASN n 
1 265 PHE n 
1 266 ILE n 
1 267 LYS n 
1 268 VAL n 
1 269 THR n 
1 270 LEU n 
1 271 THR n 
1 272 LYS n 
1 273 SER n 
1 274 PRO n 
1 275 LYS n 
1 276 LYS n 
1 277 ARG n 
1 278 PRO n 
1 279 SER n 
1 280 ALA n 
1 281 THR n 
1 282 LYS n 
1 283 MET n 
1 284 LEU n 
1 285 SER n 
1 286 HIS n 
1 287 GLN n 
1 288 LEU n 
1 289 VAL n 
1 290 SER n 
1 291 GLN n 
1 292 PRO n 
1 293 GLY n 
1 294 LEU n 
1 295 ASN n 
1 296 ARG n 
1 297 GLY n 
1 298 LEU n 
1 299 ILE n 
1 300 LEU n 
1 301 ASP n 
1 302 LEU n 
1 303 LEU n 
1 304 ASP n 
1 305 LYS n 
1 306 LEU n 
1 307 LYS n 
1 308 ASN n 
1 309 GLY n 
1 310 ASN n 
1 311 SER 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                   311 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MAP4K1, HPK1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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               'fall armyworm' 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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 
A1BWC non-polymer         . 
"N-(3,5-difluoro-4-{[3-(trifluoromethyl)-1H-pyrrolo[2,3-b]pyridin-4-yl]oxy}phenyl)-N'-[3-(morpholin-4-yl)propyl]urea" ? 
'C22 H22 F5 N5 O3' 499.434 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ?                               'C2 H6 O S'        78.133  
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL'               'C2 H6 O2'         62.068  
GLN   'L-peptide linking' y GLUTAMINE ?                               'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ?                               'C2 H5 N O2'       75.067  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
HIS   'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER ?                               'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'    149.211 
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   MET 1   -14 ?   ?   ?   A . n 
A 1 2   HIS 2   -13 ?   ?   ?   A . n 
A 1 3   HIS 3   -12 ?   ?   ?   A . n 
A 1 4   HIS 4   -11 ?   ?   ?   A . n 
A 1 5   HIS 5   -10 ?   ?   ?   A . n 
A 1 6   HIS 6   -9  ?   ?   ?   A . n 
A 1 7   HIS 7   -8  ?   ?   ?   A . n 
A 1 8   GLY 8   -7  ?   ?   ?   A . n 
A 1 9   GLU 9   -6  ?   ?   ?   A . n 
A 1 10  ASN 10  -5  ?   ?   ?   A . n 
A 1 11  LEU 11  -4  ?   ?   ?   A . n 
A 1 12  TYR 12  -3  ?   ?   ?   A . n 
A 1 13  PHE 13  -2  ?   ?   ?   A . n 
A 1 14  GLN 14  -1  ?   ?   ?   A . n 
A 1 15  GLY 15  0   ?   ?   ?   A . n 
A 1 16  SER 16  1   ?   ?   ?   A . n 
A 1 17  ASP 17  2   ?   ?   ?   A . n 
A 1 18  VAL 18  3   ?   ?   ?   A . n 
A 1 19  VAL 19  4   ?   ?   ?   A . n 
A 1 20  ASP 20  5   ?   ?   ?   A . n 
A 1 21  PRO 21  6   6   PRO PRO A . n 
A 1 22  ASP 22  7   7   ASP ASP A . n 
A 1 23  ILE 23  8   8   ILE ILE A . n 
A 1 24  PHE 24  9   9   PHE PHE A . n 
A 1 25  ASN 25  10  10  ASN ASN A . n 
A 1 26  ARG 26  11  11  ARG ARG A . n 
A 1 27  ASP 27  12  12  ASP ASP A . n 
A 1 28  PRO 28  13  13  PRO PRO A . n 
A 1 29  ARG 29  14  14  ARG ARG A . n 
A 1 30  ASP 30  15  15  ASP ASP A . n 
A 1 31  HIS 31  16  16  HIS HIS A . n 
A 1 32  TYR 32  17  17  TYR TYR A . n 
A 1 33  ASP 33  18  18  ASP ASP A . n 
A 1 34  LEU 34  19  19  LEU LEU A . n 
A 1 35  LEU 35  20  20  LEU LEU A . n 
A 1 36  GLN 36  21  21  GLN GLN A . n 
A 1 37  ARG 37  22  22  ARG ARG A . n 
A 1 38  LEU 38  23  23  LEU LEU A . n 
A 1 39  GLY 39  24  24  GLY GLY A . n 
A 1 40  GLY 40  25  25  GLY GLY A . n 
A 1 41  GLY 41  26  26  GLY GLY A . n 
A 1 42  THR 42  27  27  THR THR A . n 
A 1 43  TYR 43  28  28  TYR TYR A . n 
A 1 44  GLY 44  29  29  GLY GLY A . n 
A 1 45  GLU 45  30  30  GLU GLU A . n 
A 1 46  VAL 46  31  31  VAL VAL A . n 
A 1 47  PHE 47  32  32  PHE PHE A . n 
A 1 48  LYS 48  33  33  LYS LYS A . n 
A 1 49  ALA 49  34  34  ALA ALA A . n 
A 1 50  ARG 50  35  35  ARG ARG A . n 
A 1 51  ASP 51  36  36  ASP ASP A . n 
A 1 52  LYS 52  37  37  LYS LYS A . n 
A 1 53  VAL 53  38  38  VAL VAL A . n 
A 1 54  SER 54  39  39  SER SER A . n 
A 1 55  GLY 55  40  40  GLY GLY A . n 
A 1 56  ASP 56  41  41  ASP ASP A . n 
A 1 57  LEU 57  42  42  LEU LEU A . n 
A 1 58  VAL 58  43  43  VAL VAL A . n 
A 1 59  ALA 59  44  44  ALA ALA A . n 
A 1 60  LEU 60  45  45  LEU LEU A . n 
A 1 61  LYS 61  46  46  LYS LYS A . n 
A 1 62  MET 62  47  47  MET MET A . n 
A 1 63  VAL 63  48  48  VAL VAL A . n 
A 1 64  LYS 64  49  49  LYS LYS A . n 
A 1 65  MET 65  50  50  MET MET A . n 
A 1 66  GLU 66  51  51  GLU GLU A . n 
A 1 67  PRO 67  52  52  PRO PRO A . n 
A 1 68  ASP 68  53  53  ASP ASP A . n 
A 1 69  ASP 69  54  54  ASP ASP A . n 
A 1 70  ASP 70  55  55  ASP ASP A . n 
A 1 71  VAL 71  56  56  VAL VAL A . n 
A 1 72  SER 72  57  57  SER SER A . n 
A 1 73  THR 73  58  58  THR THR A . n 
A 1 74  LEU 74  59  59  LEU LEU A . n 
A 1 75  GLN 75  60  60  GLN GLN A . n 
A 1 76  LYS 76  61  61  LYS LYS A . n 
A 1 77  GLU 77  62  62  GLU GLU A . n 
A 1 78  ILE 78  63  63  ILE ILE A . n 
A 1 79  LEU 79  64  64  LEU LEU A . n 
A 1 80  ILE 80  65  65  ILE ILE A . n 
A 1 81  LEU 81  66  66  LEU LEU A . n 
A 1 82  LYS 82  67  67  LYS LYS A . n 
A 1 83  THR 83  68  68  THR THR A . n 
A 1 84  CYS 84  69  69  CYS CYS A . n 
A 1 85  ARG 85  70  70  ARG ARG A . n 
A 1 86  HIS 86  71  71  HIS HIS A . n 
A 1 87  ALA 87  72  72  ALA ALA A . n 
A 1 88  ASN 88  73  73  ASN ASN A . n 
A 1 89  ILE 89  74  74  ILE ILE A . n 
A 1 90  VAL 90  75  75  VAL VAL A . n 
A 1 91  ALA 91  76  76  ALA ALA A . n 
A 1 92  TYR 92  77  77  TYR TYR A . n 
A 1 93  HIS 93  78  78  HIS HIS A . n 
A 1 94  GLY 94  79  79  GLY GLY A . n 
A 1 95  SER 95  80  80  SER SER A . n 
A 1 96  TYR 96  81  81  TYR TYR A . n 
A 1 97  LEU 97  82  82  LEU LEU A . n 
A 1 98  TRP 98  83  83  TRP TRP A . n 
A 1 99  LEU 99  84  84  LEU LEU A . n 
A 1 100 GLN 100 85  85  GLN GLN A . n 
A 1 101 LYS 101 86  86  LYS LYS A . n 
A 1 102 LEU 102 87  87  LEU LEU A . n 
A 1 103 TRP 103 88  88  TRP TRP A . n 
A 1 104 ILE 104 89  89  ILE ILE A . n 
A 1 105 CYS 105 90  90  CYS CYS A . n 
A 1 106 MET 106 91  91  MET MET A . n 
A 1 107 GLU 107 92  92  GLU GLU A . n 
A 1 108 PHE 108 93  93  PHE PHE A . n 
A 1 109 CYS 109 94  94  CYS CYS A . n 
A 1 110 GLY 110 95  95  GLY GLY A . n 
A 1 111 ALA 111 96  96  ALA ALA A . n 
A 1 112 GLY 112 97  97  GLY GLY A . n 
A 1 113 SER 113 98  98  SER SER A . n 
A 1 114 LEU 114 99  99  LEU LEU A . n 
A 1 115 GLN 115 100 100 GLN GLN A . n 
A 1 116 ASP 116 101 101 ASP ASP A . n 
A 1 117 ILE 117 102 102 ILE ILE A . n 
A 1 118 TYR 118 103 103 TYR TYR A . n 
A 1 119 GLN 119 104 104 GLN GLN A . n 
A 1 120 VAL 120 105 105 VAL VAL A . n 
A 1 121 THR 121 106 106 THR THR A . n 
A 1 122 GLY 122 107 107 GLY GLY A . n 
A 1 123 SER 123 108 108 SER SER A . n 
A 1 124 LEU 124 109 109 LEU LEU A . n 
A 1 125 SER 125 110 110 SER SER A . n 
A 1 126 GLU 126 111 111 GLU GLU A . n 
A 1 127 LEU 127 112 112 LEU LEU A . n 
A 1 128 GLN 128 113 113 GLN GLN A . n 
A 1 129 ILE 129 114 114 ILE ILE A . n 
A 1 130 SER 130 115 115 SER SER A . n 
A 1 131 TYR 131 116 116 TYR TYR A . n 
A 1 132 VAL 132 117 117 VAL VAL A . n 
A 1 133 CYS 133 118 118 CYS CYS A . n 
A 1 134 ARG 134 119 119 ARG ARG A . n 
A 1 135 GLU 135 120 120 GLU GLU A . n 
A 1 136 VAL 136 121 121 VAL VAL A . n 
A 1 137 LEU 137 122 122 LEU LEU A . n 
A 1 138 GLN 138 123 123 GLN GLN A . n 
A 1 139 GLY 139 124 124 GLY GLY A . n 
A 1 140 LEU 140 125 125 LEU LEU A . n 
A 1 141 ALA 141 126 126 ALA ALA A . n 
A 1 142 TYR 142 127 127 TYR TYR A . n 
A 1 143 LEU 143 128 128 LEU LEU A . n 
A 1 144 HIS 144 129 129 HIS HIS A . n 
A 1 145 SER 145 130 130 SER SER A . n 
A 1 146 GLN 146 131 131 GLN GLN A . n 
A 1 147 LYS 147 132 132 LYS LYS A . n 
A 1 148 LYS 148 133 133 LYS LYS A . n 
A 1 149 ILE 149 134 134 ILE ILE A . n 
A 1 150 HIS 150 135 135 HIS HIS A . n 
A 1 151 ARG 151 136 136 ARG ARG A . n 
A 1 152 ASP 152 137 137 ASP ASP A . n 
A 1 153 ILE 153 138 138 ILE ILE A . n 
A 1 154 LYS 154 139 139 LYS LYS A . n 
A 1 155 GLY 155 140 140 GLY GLY A . n 
A 1 156 ALA 156 141 141 ALA ALA A . n 
A 1 157 ASN 157 142 142 ASN ASN A . n 
A 1 158 ILE 158 143 143 ILE ILE A . n 
A 1 159 LEU 159 144 144 LEU LEU A . n 
A 1 160 ILE 160 145 145 ILE ILE A . n 
A 1 161 ASN 161 146 146 ASN ASN A . n 
A 1 162 ASP 162 147 147 ASP ASP A . n 
A 1 163 ALA 163 148 148 ALA ALA A . n 
A 1 164 GLY 164 149 149 GLY GLY A . n 
A 1 165 GLU 165 150 150 GLU GLU A . n 
A 1 166 VAL 166 151 151 VAL VAL A . n 
A 1 167 ARG 167 152 152 ARG ARG A . n 
A 1 168 LEU 168 153 153 LEU LEU A . n 
A 1 169 ALA 169 154 154 ALA ALA A . n 
A 1 170 ASP 170 155 155 ASP ASP A . n 
A 1 171 PHE 171 156 156 PHE PHE A . n 
A 1 172 GLY 172 157 157 GLY GLY A . n 
A 1 173 ILE 173 158 158 ILE ILE A . n 
A 1 174 SER 174 159 159 SER SER A . n 
A 1 175 ALA 175 160 160 ALA ALA A . n 
A 1 176 GLN 176 161 161 GLN GLN A . n 
A 1 177 ILE 177 162 162 ILE ILE A . n 
A 1 178 GLY 178 163 163 GLY GLY A . n 
A 1 179 ALA 179 164 164 ALA ALA A . n 
A 1 180 GLU 180 165 165 GLU GLU A . n 
A 1 181 LEU 181 166 166 LEU LEU A . n 
A 1 182 ALA 182 167 167 ALA ALA A . n 
A 1 183 ARG 183 168 168 ARG ARG A . n 
A 1 184 ARG 184 169 169 ARG ARG A . n 
A 1 185 LEU 185 170 170 LEU LEU A . n 
A 1 186 GLU 186 171 171 GLU GLU A . n 
A 1 187 PHE 187 172 172 PHE PHE A . n 
A 1 188 ILE 188 173 173 ILE ILE A . n 
A 1 189 GLY 189 174 174 GLY GLY A . n 
A 1 190 THR 190 175 175 THR THR A . n 
A 1 191 PRO 191 176 176 PRO PRO A . n 
A 1 192 TYR 192 177 177 TYR TYR A . n 
A 1 193 TRP 193 178 178 TRP TRP A . n 
A 1 194 MET 194 179 179 MET MET A . n 
A 1 195 ALA 195 180 180 ALA ALA A . n 
A 1 196 PRO 196 181 181 PRO PRO A . n 
A 1 197 GLU 197 182 182 GLU GLU A . n 
A 1 198 VAL 198 183 183 VAL VAL A . n 
A 1 199 ALA 199 184 184 ALA ALA A . n 
A 1 200 ALA 200 185 185 ALA ALA A . n 
A 1 201 VAL 201 186 186 VAL VAL A . n 
A 1 202 ALA 202 187 187 ALA ALA A . n 
A 1 203 LEU 203 188 188 LEU LEU A . n 
A 1 204 LYS 204 189 189 LYS LYS A . n 
A 1 205 GLY 205 190 190 GLY GLY A . n 
A 1 206 GLY 206 191 191 GLY GLY A . n 
A 1 207 TYR 207 192 192 TYR TYR A . n 
A 1 208 ASN 208 193 193 ASN ASN A . n 
A 1 209 GLU 209 194 194 GLU GLU A . n 
A 1 210 LEU 210 195 195 LEU LEU A . n 
A 1 211 CYS 211 196 196 CYS CYS A . n 
A 1 212 ASP 212 197 197 ASP ASP A . n 
A 1 213 ILE 213 198 198 ILE ILE A . n 
A 1 214 TRP 214 199 199 TRP TRP A . n 
A 1 215 SER 215 200 200 SER SER A . n 
A 1 216 LEU 216 201 201 LEU LEU A . n 
A 1 217 GLY 217 202 202 GLY GLY A . n 
A 1 218 ILE 218 203 203 ILE ILE A . n 
A 1 219 THR 219 204 204 THR THR A . n 
A 1 220 ALA 220 205 205 ALA ALA A . n 
A 1 221 ILE 221 206 206 ILE ILE A . n 
A 1 222 GLU 222 207 207 GLU GLU A . n 
A 1 223 LEU 223 208 208 LEU LEU A . n 
A 1 224 ALA 224 209 209 ALA ALA A . n 
A 1 225 GLU 225 210 210 GLU GLU A . n 
A 1 226 LEU 226 211 211 LEU LEU A . n 
A 1 227 GLN 227 212 212 GLN GLN A . n 
A 1 228 PRO 228 213 213 PRO PRO A . n 
A 1 229 PRO 229 214 214 PRO PRO A . n 
A 1 230 LEU 230 215 215 LEU LEU A . n 
A 1 231 PHE 231 216 216 PHE PHE A . n 
A 1 232 ASP 232 217 217 ASP ASP A . n 
A 1 233 VAL 233 218 218 VAL VAL A . n 
A 1 234 HIS 234 219 219 HIS HIS A . n 
A 1 235 PRO 235 220 220 PRO PRO A . n 
A 1 236 LEU 236 221 221 LEU LEU A . n 
A 1 237 ARG 237 222 222 ARG ARG A . n 
A 1 238 VAL 238 223 223 VAL VAL A . n 
A 1 239 LEU 239 224 224 LEU LEU A . n 
A 1 240 PHE 240 225 225 PHE PHE A . n 
A 1 241 LEU 241 226 226 LEU LEU A . n 
A 1 242 MET 242 227 227 MET MET A . n 
A 1 243 THR 243 228 228 THR THR A . n 
A 1 244 LYS 244 229 229 LYS LYS A . n 
A 1 245 SER 245 230 230 SER SER A . n 
A 1 246 GLY 246 231 231 GLY GLY A . n 
A 1 247 TYR 247 232 232 TYR TYR A . n 
A 1 248 GLN 248 233 233 GLN GLN A . n 
A 1 249 PRO 249 234 234 PRO PRO A . n 
A 1 250 PRO 250 235 235 PRO PRO A . n 
A 1 251 ARG 251 236 236 ARG ARG A . n 
A 1 252 LEU 252 237 237 LEU LEU A . n 
A 1 253 LYS 253 238 238 LYS LYS A . n 
A 1 254 GLU 254 239 239 GLU GLU A . n 
A 1 255 LYS 255 240 240 LYS LYS A . n 
A 1 256 GLY 256 241 241 GLY GLY A . n 
A 1 257 LYS 257 242 242 LYS LYS A . n 
A 1 258 TRP 258 243 243 TRP TRP A . n 
A 1 259 SER 259 244 244 SER SER A . n 
A 1 260 ALA 260 245 245 ALA ALA A . n 
A 1 261 ALA 261 246 246 ALA ALA A . n 
A 1 262 PHE 262 247 247 PHE PHE A . n 
A 1 263 HIS 263 248 248 HIS HIS A . n 
A 1 264 ASN 264 249 249 ASN ASN A . n 
A 1 265 PHE 265 250 250 PHE PHE A . n 
A 1 266 ILE 266 251 251 ILE ILE A . n 
A 1 267 LYS 267 252 252 LYS LYS A . n 
A 1 268 VAL 268 253 253 VAL VAL A . n 
A 1 269 THR 269 254 254 THR THR A . n 
A 1 270 LEU 270 255 255 LEU LEU A . n 
A 1 271 THR 271 256 256 THR THR A . n 
A 1 272 LYS 272 257 257 LYS LYS A . n 
A 1 273 SER 273 258 258 SER SER A . n 
A 1 274 PRO 274 259 259 PRO PRO A . n 
A 1 275 LYS 275 260 260 LYS LYS A . n 
A 1 276 LYS 276 261 261 LYS LYS A . n 
A 1 277 ARG 277 262 262 ARG ARG A . n 
A 1 278 PRO 278 263 263 PRO PRO A . n 
A 1 279 SER 279 264 264 SER SER A . n 
A 1 280 ALA 280 265 265 ALA ALA A . n 
A 1 281 THR 281 266 266 THR THR A . n 
A 1 282 LYS 282 267 267 LYS LYS A . n 
A 1 283 MET 283 268 268 MET MET A . n 
A 1 284 LEU 284 269 269 LEU LEU A . n 
A 1 285 SER 285 270 270 SER SER A . n 
A 1 286 HIS 286 271 271 HIS HIS A . n 
A 1 287 GLN 287 272 272 GLN GLN A . n 
A 1 288 LEU 288 273 273 LEU LEU A . n 
A 1 289 VAL 289 274 274 VAL VAL A . n 
A 1 290 SER 290 275 275 SER SER A . n 
A 1 291 GLN 291 276 276 GLN GLN A . n 
A 1 292 PRO 292 277 277 PRO PRO A . n 
A 1 293 GLY 293 278 278 GLY GLY A . n 
A 1 294 LEU 294 279 279 LEU LEU A . n 
A 1 295 ASN 295 280 280 ASN ASN A . n 
A 1 296 ARG 296 281 281 ARG ARG A . n 
A 1 297 GLY 297 282 282 GLY GLY A . n 
A 1 298 LEU 298 283 283 LEU LEU A . n 
A 1 299 ILE 299 284 284 ILE ILE A . n 
A 1 300 LEU 300 285 285 LEU LEU A . n 
A 1 301 ASP 301 286 286 ASP ASP A . n 
A 1 302 LEU 302 287 287 LEU LEU A . n 
A 1 303 LEU 303 288 288 LEU LEU A . n 
A 1 304 ASP 304 289 289 ASP ASP A . n 
A 1 305 LYS 305 290 290 LYS LYS A . n 
A 1 306 LEU 306 291 291 LEU LEU A . n 
A 1 307 LYS 307 292 292 LYS LYS A . n 
A 1 308 ASN 308 293 293 ASN ASN A . n 
A 1 309 GLY 309 294 294 GLY GLY A . n 
A 1 310 ASN 310 295 295 ASN ASN A . n 
A 1 311 SER 311 296 296 SER SER A . n 
B 1 1   MET 1   -14 ?   ?   ?   B . n 
B 1 2   HIS 2   -13 ?   ?   ?   B . n 
B 1 3   HIS 3   -12 ?   ?   ?   B . n 
B 1 4   HIS 4   -11 ?   ?   ?   B . n 
B 1 5   HIS 5   -10 ?   ?   ?   B . n 
B 1 6   HIS 6   -9  ?   ?   ?   B . n 
B 1 7   HIS 7   -8  ?   ?   ?   B . n 
B 1 8   GLY 8   -7  ?   ?   ?   B . n 
B 1 9   GLU 9   -6  ?   ?   ?   B . n 
B 1 10  ASN 10  -5  ?   ?   ?   B . n 
B 1 11  LEU 11  -4  ?   ?   ?   B . n 
B 1 12  TYR 12  -3  ?   ?   ?   B . n 
B 1 13  PHE 13  -2  ?   ?   ?   B . n 
B 1 14  GLN 14  -1  ?   ?   ?   B . n 
B 1 15  GLY 15  0   ?   ?   ?   B . n 
B 1 16  SER 16  1   ?   ?   ?   B . n 
B 1 17  ASP 17  2   ?   ?   ?   B . n 
B 1 18  VAL 18  3   ?   ?   ?   B . n 
B 1 19  VAL 19  4   ?   ?   ?   B . n 
B 1 20  ASP 20  5   ?   ?   ?   B . n 
B 1 21  PRO 21  6   ?   ?   ?   B . n 
B 1 22  ASP 22  7   ?   ?   ?   B . n 
B 1 23  ILE 23  8   8   ILE ILE B . n 
B 1 24  PHE 24  9   9   PHE PHE B . n 
B 1 25  ASN 25  10  10  ASN ASN B . n 
B 1 26  ARG 26  11  11  ARG ARG B . n 
B 1 27  ASP 27  12  12  ASP ASP B . n 
B 1 28  PRO 28  13  13  PRO PRO B . n 
B 1 29  ARG 29  14  14  ARG ARG B . n 
B 1 30  ASP 30  15  15  ASP ASP B . n 
B 1 31  HIS 31  16  16  HIS HIS B . n 
B 1 32  TYR 32  17  17  TYR TYR B . n 
B 1 33  ASP 33  18  18  ASP ASP B . n 
B 1 34  LEU 34  19  19  LEU LEU B . n 
B 1 35  LEU 35  20  20  LEU LEU B . n 
B 1 36  GLN 36  21  21  GLN GLN B . n 
B 1 37  ARG 37  22  22  ARG ARG B . n 
B 1 38  LEU 38  23  23  LEU LEU B . n 
B 1 39  GLY 39  24  24  GLY GLY B . n 
B 1 40  GLY 40  25  25  GLY GLY B . n 
B 1 41  GLY 41  26  26  GLY GLY B . n 
B 1 42  THR 42  27  27  THR THR B . n 
B 1 43  TYR 43  28  28  TYR TYR B . n 
B 1 44  GLY 44  29  29  GLY GLY B . n 
B 1 45  GLU 45  30  30  GLU GLU B . n 
B 1 46  VAL 46  31  31  VAL VAL B . n 
B 1 47  PHE 47  32  32  PHE PHE B . n 
B 1 48  LYS 48  33  33  LYS LYS B . n 
B 1 49  ALA 49  34  34  ALA ALA B . n 
B 1 50  ARG 50  35  35  ARG ARG B . n 
B 1 51  ASP 51  36  36  ASP ASP B . n 
B 1 52  LYS 52  37  37  LYS LYS B . n 
B 1 53  VAL 53  38  38  VAL VAL B . n 
B 1 54  SER 54  39  39  SER SER B . n 
B 1 55  GLY 55  40  40  GLY GLY B . n 
B 1 56  ASP 56  41  41  ASP ASP B . n 
B 1 57  LEU 57  42  42  LEU LEU B . n 
B 1 58  VAL 58  43  43  VAL VAL B . n 
B 1 59  ALA 59  44  44  ALA ALA B . n 
B 1 60  LEU 60  45  45  LEU LEU B . n 
B 1 61  LYS 61  46  46  LYS LYS B . n 
B 1 62  MET 62  47  47  MET MET B . n 
B 1 63  VAL 63  48  48  VAL VAL B . n 
B 1 64  LYS 64  49  49  LYS LYS B . n 
B 1 65  MET 65  50  50  MET MET B . n 
B 1 66  GLU 66  51  51  GLU GLU B . n 
B 1 67  PRO 67  52  52  PRO PRO B . n 
B 1 68  ASP 68  53  53  ASP ASP B . n 
B 1 69  ASP 69  54  54  ASP ASP B . n 
B 1 70  ASP 70  55  55  ASP ASP B . n 
B 1 71  VAL 71  56  56  VAL VAL B . n 
B 1 72  SER 72  57  57  SER SER B . n 
B 1 73  THR 73  58  58  THR THR B . n 
B 1 74  LEU 74  59  59  LEU LEU B . n 
B 1 75  GLN 75  60  60  GLN GLN B . n 
B 1 76  LYS 76  61  61  LYS LYS B . n 
B 1 77  GLU 77  62  62  GLU GLU B . n 
B 1 78  ILE 78  63  63  ILE ILE B . n 
B 1 79  LEU 79  64  64  LEU LEU B . n 
B 1 80  ILE 80  65  65  ILE ILE B . n 
B 1 81  LEU 81  66  66  LEU LEU B . n 
B 1 82  LYS 82  67  67  LYS LYS B . n 
B 1 83  THR 83  68  68  THR THR B . n 
B 1 84  CYS 84  69  69  CYS CYS B . n 
B 1 85  ARG 85  70  70  ARG ARG B . n 
B 1 86  HIS 86  71  71  HIS HIS B . n 
B 1 87  ALA 87  72  72  ALA ALA B . n 
B 1 88  ASN 88  73  73  ASN ASN B . n 
B 1 89  ILE 89  74  74  ILE ILE B . n 
B 1 90  VAL 90  75  75  VAL VAL B . n 
B 1 91  ALA 91  76  76  ALA ALA B . n 
B 1 92  TYR 92  77  77  TYR TYR B . n 
B 1 93  HIS 93  78  78  HIS HIS B . n 
B 1 94  GLY 94  79  79  GLY GLY B . n 
B 1 95  SER 95  80  80  SER SER B . n 
B 1 96  TYR 96  81  81  TYR TYR B . n 
B 1 97  LEU 97  82  82  LEU LEU B . n 
B 1 98  TRP 98  83  83  TRP TRP B . n 
B 1 99  LEU 99  84  84  LEU LEU B . n 
B 1 100 GLN 100 85  85  GLN GLN B . n 
B 1 101 LYS 101 86  86  LYS LYS B . n 
B 1 102 LEU 102 87  87  LEU LEU B . n 
B 1 103 TRP 103 88  88  TRP TRP B . n 
B 1 104 ILE 104 89  89  ILE ILE B . n 
B 1 105 CYS 105 90  90  CYS CYS B . n 
B 1 106 MET 106 91  91  MET MET B . n 
B 1 107 GLU 107 92  92  GLU GLU B . n 
B 1 108 PHE 108 93  93  PHE PHE B . n 
B 1 109 CYS 109 94  94  CYS CYS B . n 
B 1 110 GLY 110 95  95  GLY GLY B . n 
B 1 111 ALA 111 96  96  ALA ALA B . n 
B 1 112 GLY 112 97  97  GLY GLY B . n 
B 1 113 SER 113 98  98  SER SER B . n 
B 1 114 LEU 114 99  99  LEU LEU B . n 
B 1 115 GLN 115 100 100 GLN GLN B . n 
B 1 116 ASP 116 101 101 ASP ASP B . n 
B 1 117 ILE 117 102 102 ILE ILE B . n 
B 1 118 TYR 118 103 103 TYR TYR B . n 
B 1 119 GLN 119 104 104 GLN GLN B . n 
B 1 120 VAL 120 105 105 VAL VAL B . n 
B 1 121 THR 121 106 106 THR THR B . n 
B 1 122 GLY 122 107 107 GLY GLY B . n 
B 1 123 SER 123 108 108 SER SER B . n 
B 1 124 LEU 124 109 109 LEU LEU B . n 
B 1 125 SER 125 110 110 SER SER B . n 
B 1 126 GLU 126 111 111 GLU GLU B . n 
B 1 127 LEU 127 112 112 LEU LEU B . n 
B 1 128 GLN 128 113 113 GLN GLN B . n 
B 1 129 ILE 129 114 114 ILE ILE B . n 
B 1 130 SER 130 115 115 SER SER B . n 
B 1 131 TYR 131 116 116 TYR TYR B . n 
B 1 132 VAL 132 117 117 VAL VAL B . n 
B 1 133 CYS 133 118 118 CYS CYS B . n 
B 1 134 ARG 134 119 119 ARG ARG B . n 
B 1 135 GLU 135 120 120 GLU GLU B . n 
B 1 136 VAL 136 121 121 VAL VAL B . n 
B 1 137 LEU 137 122 122 LEU LEU B . n 
B 1 138 GLN 138 123 123 GLN GLN B . n 
B 1 139 GLY 139 124 124 GLY GLY B . n 
B 1 140 LEU 140 125 125 LEU LEU B . n 
B 1 141 ALA 141 126 126 ALA ALA B . n 
B 1 142 TYR 142 127 127 TYR TYR B . n 
B 1 143 LEU 143 128 128 LEU LEU B . n 
B 1 144 HIS 144 129 129 HIS HIS B . n 
B 1 145 SER 145 130 130 SER SER B . n 
B 1 146 GLN 146 131 131 GLN GLN B . n 
B 1 147 LYS 147 132 132 LYS LYS B . n 
B 1 148 LYS 148 133 133 LYS LYS B . n 
B 1 149 ILE 149 134 134 ILE ILE B . n 
B 1 150 HIS 150 135 135 HIS HIS B . n 
B 1 151 ARG 151 136 136 ARG ARG B . n 
B 1 152 ASP 152 137 137 ASP ASP B . n 
B 1 153 ILE 153 138 138 ILE ILE B . n 
B 1 154 LYS 154 139 139 LYS LYS B . n 
B 1 155 GLY 155 140 140 GLY GLY B . n 
B 1 156 ALA 156 141 141 ALA ALA B . n 
B 1 157 ASN 157 142 142 ASN ASN B . n 
B 1 158 ILE 158 143 143 ILE ILE B . n 
B 1 159 LEU 159 144 144 LEU LEU B . n 
B 1 160 ILE 160 145 145 ILE ILE B . n 
B 1 161 ASN 161 146 146 ASN ASN B . n 
B 1 162 ASP 162 147 147 ASP ASP B . n 
B 1 163 ALA 163 148 148 ALA ALA B . n 
B 1 164 GLY 164 149 149 GLY GLY B . n 
B 1 165 GLU 165 150 150 GLU GLU B . n 
B 1 166 VAL 166 151 151 VAL VAL B . n 
B 1 167 ARG 167 152 152 ARG ARG B . n 
B 1 168 LEU 168 153 153 LEU LEU B . n 
B 1 169 ALA 169 154 154 ALA ALA B . n 
B 1 170 ASP 170 155 155 ASP ASP B . n 
B 1 171 PHE 171 156 156 PHE PHE B . n 
B 1 172 GLY 172 157 157 GLY GLY B . n 
B 1 173 ILE 173 158 158 ILE ILE B . n 
B 1 174 SER 174 159 159 SER SER B . n 
B 1 175 ALA 175 160 160 ALA ALA B . n 
B 1 176 GLN 176 161 161 GLN GLN B . n 
B 1 177 ILE 177 162 162 ILE ILE B . n 
B 1 178 GLY 178 163 163 GLY GLY B . n 
B 1 179 ALA 179 164 164 ALA ALA B . n 
B 1 180 GLU 180 165 165 GLU GLU B . n 
B 1 181 LEU 181 166 166 LEU LEU B . n 
B 1 182 ALA 182 167 167 ALA ALA B . n 
B 1 183 ARG 183 168 168 ARG ARG B . n 
B 1 184 ARG 184 169 169 ARG ARG B . n 
B 1 185 LEU 185 170 170 LEU LEU B . n 
B 1 186 GLU 186 171 171 GLU GLU B . n 
B 1 187 PHE 187 172 172 PHE PHE B . n 
B 1 188 ILE 188 173 173 ILE ILE B . n 
B 1 189 GLY 189 174 174 GLY GLY B . n 
B 1 190 THR 190 175 175 THR THR B . n 
B 1 191 PRO 191 176 176 PRO PRO B . n 
B 1 192 TYR 192 177 177 TYR TYR B . n 
B 1 193 TRP 193 178 178 TRP TRP B . n 
B 1 194 MET 194 179 179 MET MET B . n 
B 1 195 ALA 195 180 180 ALA ALA B . n 
B 1 196 PRO 196 181 181 PRO PRO B . n 
B 1 197 GLU 197 182 182 GLU GLU B . n 
B 1 198 VAL 198 183 183 VAL VAL B . n 
B 1 199 ALA 199 184 184 ALA ALA B . n 
B 1 200 ALA 200 185 185 ALA ALA B . n 
B 1 201 VAL 201 186 186 VAL VAL B . n 
B 1 202 ALA 202 187 187 ALA ALA B . n 
B 1 203 LEU 203 188 188 LEU LEU B . n 
B 1 204 LYS 204 189 189 LYS LYS B . n 
B 1 205 GLY 205 190 190 GLY GLY B . n 
B 1 206 GLY 206 191 191 GLY GLY B . n 
B 1 207 TYR 207 192 192 TYR TYR B . n 
B 1 208 ASN 208 193 193 ASN ASN B . n 
B 1 209 GLU 209 194 194 GLU GLU B . n 
B 1 210 LEU 210 195 195 LEU LEU B . n 
B 1 211 CYS 211 196 196 CYS CYS B . n 
B 1 212 ASP 212 197 197 ASP ASP B . n 
B 1 213 ILE 213 198 198 ILE ILE B . n 
B 1 214 TRP 214 199 199 TRP TRP B . n 
B 1 215 SER 215 200 200 SER SER B . n 
B 1 216 LEU 216 201 201 LEU LEU B . n 
B 1 217 GLY 217 202 202 GLY GLY B . n 
B 1 218 ILE 218 203 203 ILE ILE B . n 
B 1 219 THR 219 204 204 THR THR B . n 
B 1 220 ALA 220 205 205 ALA ALA B . n 
B 1 221 ILE 221 206 206 ILE ILE B . n 
B 1 222 GLU 222 207 207 GLU GLU B . n 
B 1 223 LEU 223 208 208 LEU LEU B . n 
B 1 224 ALA 224 209 209 ALA ALA B . n 
B 1 225 GLU 225 210 210 GLU GLU B . n 
B 1 226 LEU 226 211 211 LEU LEU B . n 
B 1 227 GLN 227 212 212 GLN GLN B . n 
B 1 228 PRO 228 213 213 PRO PRO B . n 
B 1 229 PRO 229 214 214 PRO PRO B . n 
B 1 230 LEU 230 215 215 LEU LEU B . n 
B 1 231 PHE 231 216 216 PHE PHE B . n 
B 1 232 ASP 232 217 217 ASP ASP B . n 
B 1 233 VAL 233 218 218 VAL VAL B . n 
B 1 234 HIS 234 219 219 HIS HIS B . n 
B 1 235 PRO 235 220 220 PRO PRO B . n 
B 1 236 LEU 236 221 221 LEU LEU B . n 
B 1 237 ARG 237 222 222 ARG ARG B . n 
B 1 238 VAL 238 223 223 VAL VAL B . n 
B 1 239 LEU 239 224 224 LEU LEU B . n 
B 1 240 PHE 240 225 225 PHE PHE B . n 
B 1 241 LEU 241 226 226 LEU LEU B . n 
B 1 242 MET 242 227 227 MET MET B . n 
B 1 243 THR 243 228 228 THR THR B . n 
B 1 244 LYS 244 229 229 LYS LYS B . n 
B 1 245 SER 245 230 230 SER SER B . n 
B 1 246 GLY 246 231 231 GLY GLY B . n 
B 1 247 TYR 247 232 232 TYR TYR B . n 
B 1 248 GLN 248 233 233 GLN GLN B . n 
B 1 249 PRO 249 234 234 PRO PRO B . n 
B 1 250 PRO 250 235 235 PRO PRO B . n 
B 1 251 ARG 251 236 236 ARG ARG B . n 
B 1 252 LEU 252 237 237 LEU LEU B . n 
B 1 253 LYS 253 238 238 LYS LYS B . n 
B 1 254 GLU 254 239 239 GLU GLU B . n 
B 1 255 LYS 255 240 240 LYS LYS B . n 
B 1 256 GLY 256 241 241 GLY GLY B . n 
B 1 257 LYS 257 242 242 LYS LYS B . n 
B 1 258 TRP 258 243 243 TRP TRP B . n 
B 1 259 SER 259 244 244 SER SER B . n 
B 1 260 ALA 260 245 245 ALA ALA B . n 
B 1 261 ALA 261 246 246 ALA ALA B . n 
B 1 262 PHE 262 247 247 PHE PHE B . n 
B 1 263 HIS 263 248 248 HIS HIS B . n 
B 1 264 ASN 264 249 249 ASN ASN B . n 
B 1 265 PHE 265 250 250 PHE PHE B . n 
B 1 266 ILE 266 251 251 ILE ILE B . n 
B 1 267 LYS 267 252 252 LYS LYS B . n 
B 1 268 VAL 268 253 253 VAL VAL B . n 
B 1 269 THR 269 254 254 THR THR B . n 
B 1 270 LEU 270 255 255 LEU LEU B . n 
B 1 271 THR 271 256 256 THR THR B . n 
B 1 272 LYS 272 257 257 LYS LYS B . n 
B 1 273 SER 273 258 258 SER SER B . n 
B 1 274 PRO 274 259 259 PRO PRO B . n 
B 1 275 LYS 275 260 260 LYS LYS B . n 
B 1 276 LYS 276 261 261 LYS LYS B . n 
B 1 277 ARG 277 262 262 ARG ARG B . n 
B 1 278 PRO 278 263 263 PRO PRO B . n 
B 1 279 SER 279 264 264 SER SER B . n 
B 1 280 ALA 280 265 265 ALA ALA B . n 
B 1 281 THR 281 266 266 THR THR B . n 
B 1 282 LYS 282 267 267 LYS LYS B . n 
B 1 283 MET 283 268 268 MET MET B . n 
B 1 284 LEU 284 269 269 LEU LEU B . n 
B 1 285 SER 285 270 270 SER SER B . n 
B 1 286 HIS 286 271 271 HIS HIS B . n 
B 1 287 GLN 287 272 272 GLN GLN B . n 
B 1 288 LEU 288 273 273 LEU LEU B . n 
B 1 289 VAL 289 274 274 VAL VAL B . n 
B 1 290 SER 290 275 275 SER SER B . n 
B 1 291 GLN 291 276 276 GLN GLN B . n 
B 1 292 PRO 292 277 277 PRO PRO B . n 
B 1 293 GLY 293 278 278 GLY GLY B . n 
B 1 294 LEU 294 279 279 LEU LEU B . n 
B 1 295 ASN 295 280 280 ASN ASN B . n 
B 1 296 ARG 296 281 281 ARG ARG B . n 
B 1 297 GLY 297 282 282 GLY GLY B . n 
B 1 298 LEU 298 283 283 LEU LEU B . n 
B 1 299 ILE 299 284 284 ILE ILE B . n 
B 1 300 LEU 300 285 285 LEU LEU B . n 
B 1 301 ASP 301 286 286 ASP ASP B . n 
B 1 302 LEU 302 287 287 LEU LEU B . n 
B 1 303 LEU 303 288 288 LEU LEU B . n 
B 1 304 ASP 304 289 289 ASP ASP B . n 
B 1 305 LYS 305 290 290 LYS LYS B . n 
B 1 306 LEU 306 291 291 LEU LEU B . n 
B 1 307 LYS 307 292 292 LYS LYS B . n 
B 1 308 ASN 308 293 293 ASN ASN B . n 
B 1 309 GLY 309 294 294 GLY GLY B . n 
B 1 310 ASN 310 295 ?   ?   ?   B . n 
B 1 311 SER 311 296 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BWC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BWC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 EDO   1   301 249 EDO   EDO A . 
D 2 EDO   1   302 250 EDO   EDO A . 
E 2 EDO   1   303 251 EDO   EDO A . 
F 2 EDO   1   304 252 EDO   EDO A . 
G 2 EDO   1   305 254 EDO   EDO A . 
H 2 EDO   1   306 255 EDO   EDO A . 
I 2 EDO   1   307 257 EDO   EDO A . 
J 3 GOL   1   308 258 GOL   GOL A . 
K 4 DMS   1   309 260 DMS   DMS A . 
L 4 DMS   1   310 261 DMS   DMS A . 
M 5 A1BWC 1   311 2   A1BWC LIG A . 
N 5 A1BWC 1   312 3   A1BWC LIG A . 
O 5 A1BWC 1   313 1   A1BWC LIG A . 
P 5 A1BWC 1   314 2   A1BWC LIG A . 
Q 2 EDO   1   301 253 EDO   EDO B . 
R 2 EDO   1   302 256 EDO   EDO B . 
S 5 A1BWC 1   303 1   A1BWC LIG B . 
T 6 HOH   1   401 153 HOH   HOH A . 
T 6 HOH   2   402 135 HOH   HOH A . 
T 6 HOH   3   403 211 HOH   HOH A . 
T 6 HOH   4   404 35  HOH   HOH A . 
T 6 HOH   5   405 97  HOH   HOH A . 
T 6 HOH   6   406 189 HOH   HOH A . 
T 6 HOH   7   407 222 HOH   HOH A . 
T 6 HOH   8   408 177 HOH   HOH A . 
T 6 HOH   9   409 141 HOH   HOH A . 
T 6 HOH   10  410 188 HOH   HOH A . 
T 6 HOH   11  411 1   HOH   HOH A . 
T 6 HOH   12  412 91  HOH   HOH A . 
T 6 HOH   13  413 126 HOH   HOH A . 
T 6 HOH   14  414 48  HOH   HOH A . 
T 6 HOH   15  415 95  HOH   HOH A . 
T 6 HOH   16  416 130 HOH   HOH A . 
T 6 HOH   17  417 46  HOH   HOH A . 
T 6 HOH   18  418 23  HOH   HOH A . 
T 6 HOH   19  419 76  HOH   HOH A . 
T 6 HOH   20  420 110 HOH   HOH A . 
T 6 HOH   21  421 111 HOH   HOH A . 
T 6 HOH   22  422 4   HOH   HOH A . 
T 6 HOH   23  423 38  HOH   HOH A . 
T 6 HOH   24  424 121 HOH   HOH A . 
T 6 HOH   25  425 21  HOH   HOH A . 
T 6 HOH   26  426 22  HOH   HOH A . 
T 6 HOH   27  427 128 HOH   HOH A . 
T 6 HOH   28  428 137 HOH   HOH A . 
T 6 HOH   29  429 107 HOH   HOH A . 
T 6 HOH   30  430 109 HOH   HOH A . 
T 6 HOH   31  431 51  HOH   HOH A . 
T 6 HOH   32  432 218 HOH   HOH A . 
T 6 HOH   33  433 179 HOH   HOH A . 
T 6 HOH   34  434 246 HOH   HOH A . 
T 6 HOH   35  435 34  HOH   HOH A . 
T 6 HOH   36  436 124 HOH   HOH A . 
T 6 HOH   37  437 17  HOH   HOH A . 
T 6 HOH   38  438 59  HOH   HOH A . 
T 6 HOH   39  439 49  HOH   HOH A . 
T 6 HOH   40  440 82  HOH   HOH A . 
T 6 HOH   41  441 67  HOH   HOH A . 
T 6 HOH   42  442 93  HOH   HOH A . 
T 6 HOH   43  443 89  HOH   HOH A . 
T 6 HOH   44  444 214 HOH   HOH A . 
T 6 HOH   45  445 213 HOH   HOH A . 
T 6 HOH   46  446 103 HOH   HOH A . 
T 6 HOH   47  447 28  HOH   HOH A . 
T 6 HOH   48  448 3   HOH   HOH A . 
T 6 HOH   49  449 33  HOH   HOH A . 
T 6 HOH   50  450 205 HOH   HOH A . 
T 6 HOH   51  451 190 HOH   HOH A . 
T 6 HOH   52  452 13  HOH   HOH A . 
T 6 HOH   53  453 170 HOH   HOH A . 
T 6 HOH   54  454 77  HOH   HOH A . 
T 6 HOH   55  455 197 HOH   HOH A . 
T 6 HOH   56  456 56  HOH   HOH A . 
T 6 HOH   57  457 37  HOH   HOH A . 
T 6 HOH   58  458 54  HOH   HOH A . 
T 6 HOH   59  459 227 HOH   HOH A . 
T 6 HOH   60  460 15  HOH   HOH A . 
T 6 HOH   61  461 120 HOH   HOH A . 
T 6 HOH   62  462 167 HOH   HOH A . 
T 6 HOH   63  463 217 HOH   HOH A . 
T 6 HOH   64  464 50  HOH   HOH A . 
T 6 HOH   65  465 178 HOH   HOH A . 
T 6 HOH   66  466 72  HOH   HOH A . 
T 6 HOH   67  467 185 HOH   HOH A . 
T 6 HOH   68  468 68  HOH   HOH A . 
T 6 HOH   69  469 45  HOH   HOH A . 
T 6 HOH   70  470 156 HOH   HOH A . 
T 6 HOH   71  471 40  HOH   HOH A . 
T 6 HOH   72  472 207 HOH   HOH A . 
T 6 HOH   73  473 173 HOH   HOH A . 
T 6 HOH   74  474 16  HOH   HOH A . 
T 6 HOH   75  475 125 HOH   HOH A . 
T 6 HOH   76  476 19  HOH   HOH A . 
T 6 HOH   77  477 180 HOH   HOH A . 
T 6 HOH   78  478 26  HOH   HOH A . 
T 6 HOH   79  479 186 HOH   HOH A . 
T 6 HOH   80  480 30  HOH   HOH A . 
T 6 HOH   81  481 202 HOH   HOH A . 
T 6 HOH   82  482 87  HOH   HOH A . 
T 6 HOH   83  483 248 HOH   HOH A . 
T 6 HOH   84  484 225 HOH   HOH A . 
T 6 HOH   85  485 80  HOH   HOH A . 
T 6 HOH   86  486 6   HOH   HOH A . 
T 6 HOH   87  487 105 HOH   HOH A . 
T 6 HOH   88  488 24  HOH   HOH A . 
T 6 HOH   89  489 83  HOH   HOH A . 
T 6 HOH   90  490 134 HOH   HOH A . 
T 6 HOH   91  491 193 HOH   HOH A . 
T 6 HOH   92  492 119 HOH   HOH A . 
T 6 HOH   93  493 139 HOH   HOH A . 
T 6 HOH   94  494 88  HOH   HOH A . 
T 6 HOH   95  495 29  HOH   HOH A . 
T 6 HOH   96  496 39  HOH   HOH A . 
T 6 HOH   97  497 195 HOH   HOH A . 
T 6 HOH   98  498 42  HOH   HOH A . 
T 6 HOH   99  499 78  HOH   HOH A . 
T 6 HOH   100 500 140 HOH   HOH A . 
T 6 HOH   101 501 61  HOH   HOH A . 
T 6 HOH   102 502 81  HOH   HOH A . 
T 6 HOH   103 503 70  HOH   HOH A . 
T 6 HOH   104 504 157 HOH   HOH A . 
T 6 HOH   105 505 32  HOH   HOH A . 
T 6 HOH   106 506 8   HOH   HOH A . 
T 6 HOH   107 507 2   HOH   HOH A . 
T 6 HOH   108 508 229 HOH   HOH A . 
T 6 HOH   109 509 237 HOH   HOH A . 
T 6 HOH   110 510 224 HOH   HOH A . 
T 6 HOH   111 511 209 HOH   HOH A . 
T 6 HOH   112 512 131 HOH   HOH A . 
T 6 HOH   113 513 43  HOH   HOH A . 
T 6 HOH   114 514 36  HOH   HOH A . 
T 6 HOH   115 515 63  HOH   HOH A . 
T 6 HOH   116 516 86  HOH   HOH A . 
T 6 HOH   117 517 168 HOH   HOH A . 
T 6 HOH   118 518 75  HOH   HOH A . 
T 6 HOH   119 519 216 HOH   HOH A . 
T 6 HOH   120 520 57  HOH   HOH A . 
T 6 HOH   121 521 144 HOH   HOH A . 
T 6 HOH   122 522 147 HOH   HOH A . 
T 6 HOH   123 523 98  HOH   HOH A . 
T 6 HOH   124 524 79  HOH   HOH A . 
T 6 HOH   125 525 152 HOH   HOH A . 
T 6 HOH   126 526 123 HOH   HOH A . 
T 6 HOH   127 527 18  HOH   HOH A . 
T 6 HOH   128 528 187 HOH   HOH A . 
T 6 HOH   129 529 99  HOH   HOH A . 
T 6 HOH   130 530 145 HOH   HOH A . 
T 6 HOH   131 531 176 HOH   HOH A . 
T 6 HOH   132 532 47  HOH   HOH A . 
T 6 HOH   133 533 198 HOH   HOH A . 
T 6 HOH   134 534 85  HOH   HOH A . 
T 6 HOH   135 535 94  HOH   HOH A . 
T 6 HOH   136 536 52  HOH   HOH A . 
T 6 HOH   137 537 108 HOH   HOH A . 
T 6 HOH   138 538 92  HOH   HOH A . 
T 6 HOH   139 539 162 HOH   HOH A . 
T 6 HOH   140 540 106 HOH   HOH A . 
T 6 HOH   141 541 73  HOH   HOH A . 
T 6 HOH   142 542 206 HOH   HOH A . 
T 6 HOH   143 543 163 HOH   HOH A . 
T 6 HOH   144 544 181 HOH   HOH A . 
T 6 HOH   145 545 117 HOH   HOH A . 
T 6 HOH   146 546 96  HOH   HOH A . 
T 6 HOH   147 547 245 HOH   HOH A . 
T 6 HOH   148 548 244 HOH   HOH A . 
T 6 HOH   149 549 174 HOH   HOH A . 
T 6 HOH   150 550 90  HOH   HOH A . 
T 6 HOH   151 551 172 HOH   HOH A . 
T 6 HOH   152 552 243 HOH   HOH A . 
T 6 HOH   153 553 182 HOH   HOH A . 
T 6 HOH   154 554 161 HOH   HOH A . 
T 6 HOH   155 555 242 HOH   HOH A . 
T 6 HOH   156 556 71  HOH   HOH A . 
T 6 HOH   157 557 148 HOH   HOH A . 
T 6 HOH   158 558 165 HOH   HOH A . 
U 6 HOH   1   401 208 HOH   HOH B . 
U 6 HOH   2   402 194 HOH   HOH B . 
U 6 HOH   3   403 112 HOH   HOH B . 
U 6 HOH   4   404 132 HOH   HOH B . 
U 6 HOH   5   405 14  HOH   HOH B . 
U 6 HOH   6   406 192 HOH   HOH B . 
U 6 HOH   7   407 138 HOH   HOH B . 
U 6 HOH   8   408 25  HOH   HOH B . 
U 6 HOH   9   409 115 HOH   HOH B . 
U 6 HOH   10  410 239 HOH   HOH B . 
U 6 HOH   11  411 12  HOH   HOH B . 
U 6 HOH   12  412 104 HOH   HOH B . 
U 6 HOH   13  413 233 HOH   HOH B . 
U 6 HOH   14  414 113 HOH   HOH B . 
U 6 HOH   15  415 7   HOH   HOH B . 
U 6 HOH   16  416 133 HOH   HOH B . 
U 6 HOH   17  417 169 HOH   HOH B . 
U 6 HOH   18  418 127 HOH   HOH B . 
U 6 HOH   19  419 200 HOH   HOH B . 
U 6 HOH   20  420 149 HOH   HOH B . 
U 6 HOH   21  421 62  HOH   HOH B . 
U 6 HOH   22  422 223 HOH   HOH B . 
U 6 HOH   23  423 20  HOH   HOH B . 
U 6 HOH   24  424 199 HOH   HOH B . 
U 6 HOH   25  425 10  HOH   HOH B . 
U 6 HOH   26  426 203 HOH   HOH B . 
U 6 HOH   27  427 60  HOH   HOH B . 
U 6 HOH   28  428 236 HOH   HOH B . 
U 6 HOH   29  429 11  HOH   HOH B . 
U 6 HOH   30  430 64  HOH   HOH B . 
U 6 HOH   31  431 136 HOH   HOH B . 
U 6 HOH   32  432 230 HOH   HOH B . 
U 6 HOH   33  433 235 HOH   HOH B . 
U 6 HOH   34  434 142 HOH   HOH B . 
U 6 HOH   35  435 240 HOH   HOH B . 
U 6 HOH   36  436 116 HOH   HOH B . 
U 6 HOH   37  437 129 HOH   HOH B . 
U 6 HOH   38  438 5   HOH   HOH B . 
U 6 HOH   39  439 69  HOH   HOH B . 
U 6 HOH   40  440 234 HOH   HOH B . 
U 6 HOH   41  441 122 HOH   HOH B . 
U 6 HOH   42  442 100 HOH   HOH B . 
U 6 HOH   43  443 102 HOH   HOH B . 
U 6 HOH   44  444 171 HOH   HOH B . 
U 6 HOH   45  445 146 HOH   HOH B . 
U 6 HOH   46  446 226 HOH   HOH B . 
U 6 HOH   47  447 210 HOH   HOH B . 
U 6 HOH   48  448 219 HOH   HOH B . 
U 6 HOH   49  449 65  HOH   HOH B . 
U 6 HOH   50  450 9   HOH   HOH B . 
U 6 HOH   51  451 118 HOH   HOH B . 
U 6 HOH   52  452 238 HOH   HOH B . 
U 6 HOH   53  453 66  HOH   HOH B . 
U 6 HOH   54  454 55  HOH   HOH B . 
U 6 HOH   55  455 53  HOH   HOH B . 
U 6 HOH   56  456 143 HOH   HOH B . 
U 6 HOH   57  457 164 HOH   HOH B . 
U 6 HOH   58  458 212 HOH   HOH B . 
U 6 HOH   59  459 101 HOH   HOH B . 
U 6 HOH   60  460 31  HOH   HOH B . 
U 6 HOH   61  461 154 HOH   HOH B . 
U 6 HOH   62  462 151 HOH   HOH B . 
U 6 HOH   63  463 150 HOH   HOH B . 
U 6 HOH   64  464 201 HOH   HOH B . 
U 6 HOH   65  465 114 HOH   HOH B . 
U 6 HOH   66  466 241 HOH   HOH B . 
U 6 HOH   67  467 196 HOH   HOH B . 
U 6 HOH   68  468 27  HOH   HOH B . 
U 6 HOH   69  469 204 HOH   HOH B . 
U 6 HOH   70  470 160 HOH   HOH B . 
U 6 HOH   71  471 58  HOH   HOH B . 
U 6 HOH   72  472 166 HOH   HOH B . 
U 6 HOH   73  473 158 HOH   HOH B . 
U 6 HOH   74  474 159 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 B LYS   189 ? CG  ? B LYS   204 CG  
2  1 Y 1 B LYS   189 ? CD  ? B LYS   204 CD  
3  1 Y 1 B LYS   189 ? CE  ? B LYS   204 CE  
4  1 Y 1 B LYS   189 ? NZ  ? B LYS   204 NZ  
5  1 N 1 A A1BWC 312 ? C21 ? N A1BWC 1   C21 
6  1 N 1 A A1BWC 312 ? C24 ? N A1BWC 1   C24 
7  1 N 1 A A1BWC 312 ? C26 ? N A1BWC 1   C26 
8  1 N 1 A A1BWC 312 ? C28 ? N A1BWC 1   C28 
9  1 N 1 A A1BWC 312 ? C25 ? N A1BWC 1   C25 
10 1 N 1 A A1BWC 312 ? C29 ? N A1BWC 1   C29 
11 1 N 1 A A1BWC 312 ? C30 ? N A1BWC 1   C30 
12 1 N 1 A A1BWC 312 ? C32 ? N A1BWC 1   C32 
13 1 N 1 A A1BWC 312 ? N22 ? N A1BWC 1   N22 
14 1 N 1 A A1BWC 312 ? N27 ? N A1BWC 1   N27 
15 1 N 1 A A1BWC 312 ? N8  ? N A1BWC 1   N8  
16 1 N 1 A A1BWC 312 ? O23 ? N A1BWC 1   O23 
17 1 N 1 A A1BWC 312 ? O31 ? N A1BWC 1   O31 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487           1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? '0.7.4 (CCP4 7.0.71)' 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                     3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.82 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9N7R 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.190 
_cell.length_a_esd                 ? 
_cell.length_b                     76.690 
_cell.length_b_esd                 ? 
_cell.length_c                     85.870 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9N7R 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9N7R 
_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             2.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.43 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '12% PEG8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     93 
_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 PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-03-16 
_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                    M 
_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   1.11583 
_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                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.11583 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9N7R 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.13 
_reflns.d_resolution_low                               47.94 
_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                                     34882 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.05 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.095 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       233514 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.088 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.13 
_reflns_shell.d_res_low                                     2.19 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           19926 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2879 
_reflns_shell.percent_possible_obs                          99.8 
_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                               6.9 
_reflns_shell.pdbx_chi_squared                              1.01 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.7 
_reflns_shell.pdbx_Rrim_I_all                               0.878 
_reflns_shell.pdbx_Rpim_I_all                               0.332 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.817 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.811 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9N7R 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.13 
_refine.ls_d_res_low                             47.94 
_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                     34675 
_refine.ls_number_reflns_R_free                  1699 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.29 
_refine.ls_percent_reflns_R_free                 4.90 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1807 
_refine.ls_R_factor_R_free                       0.2268 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1783 
_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                          1.36 
_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       ML 
_refine.pdbx_R_Free_selection_details            4.90% 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.78 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.27 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4555 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         212 
_refine_hist.number_atoms_solvent             232 
_refine_hist.number_atoms_total               4999 
_refine_hist.d_res_high                       2.13 
_refine_hist.d_res_low                        47.94 
# 
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' ? 0.005  ? 4873 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.774  ? 6579 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.680 ? 1800 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 703  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 812  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.13 2.19  . . 156 2757 100.00 . . . . 0.2509 . . . . . . . . . . . 0.3167 
'X-RAY DIFFRACTION' 2.19 2.26  . . 137 2717 100.00 . . . . 0.2374 . . . . . . . . . . . 0.2958 
'X-RAY DIFFRACTION' 2.26 2.34  . . 118 2743 99.00  . . . . 0.2210 . . . . . . . . . . . 0.2876 
'X-RAY DIFFRACTION' 2.34 2.44  . . 135 2756 99.00  . . . . 0.2194 . . . . . . . . . . . 0.2638 
'X-RAY DIFFRACTION' 2.44 2.55  . . 150 2752 99.00  . . . . 0.2016 . . . . . . . . . . . 0.2701 
'X-RAY DIFFRACTION' 2.55 2.68  . . 131 2761 100.00 . . . . 0.1912 . . . . . . . . . . . 0.2700 
'X-RAY DIFFRACTION' 2.68 2.85  . . 151 2731 100.00 . . . . 0.1899 . . . . . . . . . . . 0.2443 
'X-RAY DIFFRACTION' 2.85 3.07  . . 150 2713 99.00  . . . . 0.2056 . . . . . . . . . . . 0.2726 
'X-RAY DIFFRACTION' 3.07 3.38  . . 145 2748 99.00  . . . . 0.1806 . . . . . . . . . . . 0.2475 
'X-RAY DIFFRACTION' 3.38 3.87  . . 148 2735 99.00  . . . . 0.1618 . . . . . . . . . . . 0.1946 
'X-RAY DIFFRACTION' 3.87 4.87  . . 128 2768 98.00  . . . . 0.1345 . . . . . . . . . . . 0.1877 
'X-RAY DIFFRACTION' 4.88 47.94 . . 150 2795 99.00  . . . . 0.1711 . . . . . . . . . . . 0.1893 
# 
_struct.entry_id                     9N7R 
_struct.title                        
;Crystal structure of HPK1 bound to N-(3,5-difluoro-4-{[3-(trifluoromethyl)-1H-pyrrolo[2,3-b]pyridin-4-yl]oxy}phenyl)-N'-[3-(morpholin-4-yl)propyl]urea (compound C6)
;
_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        9N7R 
_struct_keywords.text            
'nucleotide binding, MAP4K1, Mitogen-activated protein kinase kinase kinase kinase 1, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING 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 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 2 ? 
R N N 2 ? 
S N N 5 ? 
T N N 6 ? 
U N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    M4K1_HUMAN 
_struct_ref.pdbx_db_accession          Q92918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILILKTCRHANIVAYHGSY
LWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGISAQ
IGATLARRLSFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLFLMTKSGYQPPRLKEKG
KWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKN
;
_struct_ref.pdbx_align_begin           2 
# 
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 9N7R A 17 ? 308 ? Q92918 2 ? 293 ? 2 293 
2 1 9N7R B 17 ? 308 ? Q92918 2 ? 293 ? 2 293 
# 
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 9N7R MET A 1   ? UNP Q92918 ?   ?   'initiating methionine' -14 1  
1 9N7R HIS A 2   ? UNP Q92918 ?   ?   'expression tag'        -13 2  
1 9N7R HIS A 3   ? UNP Q92918 ?   ?   'expression tag'        -12 3  
1 9N7R HIS A 4   ? UNP Q92918 ?   ?   'expression tag'        -11 4  
1 9N7R HIS A 5   ? UNP Q92918 ?   ?   'expression tag'        -10 5  
1 9N7R HIS A 6   ? UNP Q92918 ?   ?   'expression tag'        -9  6  
1 9N7R HIS A 7   ? UNP Q92918 ?   ?   'expression tag'        -8  7  
1 9N7R GLY A 8   ? UNP Q92918 ?   ?   'expression tag'        -7  8  
1 9N7R GLU A 9   ? UNP Q92918 ?   ?   'expression tag'        -6  9  
1 9N7R ASN A 10  ? UNP Q92918 ?   ?   'expression tag'        -5  10 
1 9N7R LEU A 11  ? UNP Q92918 ?   ?   'expression tag'        -4  11 
1 9N7R TYR A 12  ? UNP Q92918 ?   ?   'expression tag'        -3  12 
1 9N7R PHE A 13  ? UNP Q92918 ?   ?   'expression tag'        -2  13 
1 9N7R GLN A 14  ? UNP Q92918 ?   ?   'expression tag'        -1  14 
1 9N7R GLY A 15  ? UNP Q92918 ?   ?   'expression tag'        0   15 
1 9N7R SER A 16  ? UNP Q92918 ?   ?   'expression tag'        1   16 
1 9N7R GLU A 180 ? UNP Q92918 THR 165 conflict                165 17 
1 9N7R GLU A 186 ? UNP Q92918 SER 171 conflict                171 18 
1 9N7R GLY A 309 ? UNP Q92918 ?   ?   'expression tag'        294 19 
1 9N7R ASN A 310 ? UNP Q92918 ?   ?   'expression tag'        295 20 
1 9N7R SER A 311 ? UNP Q92918 ?   ?   'expression tag'        296 21 
2 9N7R MET B 1   ? UNP Q92918 ?   ?   'initiating methionine' -14 22 
2 9N7R HIS B 2   ? UNP Q92918 ?   ?   'expression tag'        -13 23 
2 9N7R HIS B 3   ? UNP Q92918 ?   ?   'expression tag'        -12 24 
2 9N7R HIS B 4   ? UNP Q92918 ?   ?   'expression tag'        -11 25 
2 9N7R HIS B 5   ? UNP Q92918 ?   ?   'expression tag'        -10 26 
2 9N7R HIS B 6   ? UNP Q92918 ?   ?   'expression tag'        -9  27 
2 9N7R HIS B 7   ? UNP Q92918 ?   ?   'expression tag'        -8  28 
2 9N7R GLY B 8   ? UNP Q92918 ?   ?   'expression tag'        -7  29 
2 9N7R GLU B 9   ? UNP Q92918 ?   ?   'expression tag'        -6  30 
2 9N7R ASN B 10  ? UNP Q92918 ?   ?   'expression tag'        -5  31 
2 9N7R LEU B 11  ? UNP Q92918 ?   ?   'expression tag'        -4  32 
2 9N7R TYR B 12  ? UNP Q92918 ?   ?   'expression tag'        -3  33 
2 9N7R PHE B 13  ? UNP Q92918 ?   ?   'expression tag'        -2  34 
2 9N7R GLN B 14  ? UNP Q92918 ?   ?   'expression tag'        -1  35 
2 9N7R GLY B 15  ? UNP Q92918 ?   ?   'expression tag'        0   36 
2 9N7R SER B 16  ? UNP Q92918 ?   ?   'expression tag'        1   37 
2 9N7R GLU B 180 ? UNP Q92918 THR 165 conflict                165 38 
2 9N7R GLU B 186 ? UNP Q92918 SER 171 conflict                171 39 
2 9N7R GLY B 309 ? UNP Q92918 ?   ?   'expression tag'        294 40 
2 9N7R ASN B 310 ? UNP Q92918 ?   ?   'expression tag'        295 41 
2 9N7R SER B 311 ? UNP Q92918 ?   ?   'expression tag'        296 42 
# 
_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)' 8230  ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  26190 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 27  ? ASP A 30  ? ASP A 12  ASP A 15  5 ? 4  
HELX_P HELX_P2  AA2 ASP A 70  ? THR A 73  ? ASP A 55  THR A 58  5 ? 4  
HELX_P HELX_P3  AA3 LEU A 74  ? CYS A 84  ? LEU A 59  CYS A 69  1 ? 11 
HELX_P HELX_P4  AA4 SER A 113 ? GLY A 122 ? SER A 98  GLY A 107 1 ? 10 
HELX_P HELX_P5  AA5 SER A 125 ? GLN A 146 ? SER A 110 GLN A 131 1 ? 22 
HELX_P HELX_P6  AA6 LYS A 154 ? ALA A 156 ? LYS A 139 ALA A 141 5 ? 3  
HELX_P HELX_P7  AA7 GLY A 172 ? GLN A 176 ? GLY A 157 GLN A 161 5 ? 5  
HELX_P HELX_P8  AA8 ILE A 177 ? GLY A 189 ? ILE A 162 GLY A 174 1 ? 13 
HELX_P HELX_P9  AA9 ALA A 195 ? LEU A 203 ? ALA A 180 LEU A 188 1 ? 9  
HELX_P HELX_P10 AB1 LEU A 210 ? LEU A 226 ? LEU A 195 LEU A 211 1 ? 17 
HELX_P HELX_P11 AB2 HIS A 234 ? THR A 243 ? HIS A 219 THR A 228 1 ? 10 
HELX_P HELX_P12 AB3 SER A 259 ? LEU A 270 ? SER A 244 LEU A 255 1 ? 12 
HELX_P HELX_P13 AB4 SER A 273 ? ARG A 277 ? SER A 258 ARG A 262 5 ? 5  
HELX_P HELX_P14 AB5 SER A 279 ? SER A 285 ? SER A 264 SER A 270 1 ? 7  
HELX_P HELX_P15 AB6 HIS A 286 ? GLN A 291 ? HIS A 271 GLN A 276 1 ? 6  
HELX_P HELX_P16 AB7 ARG A 296 ? GLY A 309 ? ARG A 281 GLY A 294 1 ? 14 
HELX_P HELX_P17 AB8 ASP B 27  ? ASP B 30  ? ASP B 12  ASP B 15  5 ? 4  
HELX_P HELX_P18 AB9 ASP B 70  ? CYS B 84  ? ASP B 55  CYS B 69  1 ? 15 
HELX_P HELX_P19 AC1 SER B 113 ? GLY B 122 ? SER B 98  GLY B 107 1 ? 10 
HELX_P HELX_P20 AC2 SER B 125 ? GLN B 146 ? SER B 110 GLN B 131 1 ? 22 
HELX_P HELX_P21 AC3 ILE B 173 ? GLN B 176 ? ILE B 158 GLN B 161 5 ? 4  
HELX_P HELX_P22 AC4 ILE B 177 ? GLY B 189 ? ILE B 162 GLY B 174 1 ? 13 
HELX_P HELX_P23 AC5 ALA B 195 ? GLY B 205 ? ALA B 180 GLY B 190 1 ? 11 
HELX_P HELX_P24 AC6 LEU B 210 ? LEU B 226 ? LEU B 195 LEU B 211 1 ? 17 
HELX_P HELX_P25 AC7 HIS B 234 ? LYS B 244 ? HIS B 219 LYS B 229 1 ? 11 
HELX_P HELX_P26 AC8 SER B 259 ? LEU B 270 ? SER B 244 LEU B 255 1 ? 12 
HELX_P HELX_P27 AC9 SER B 273 ? ARG B 277 ? SER B 258 ARG B 262 5 ? 5  
HELX_P HELX_P28 AD1 SER B 279 ? LEU B 284 ? SER B 264 LEU B 269 1 ? 6  
HELX_P HELX_P29 AD2 HIS B 286 ? GLN B 291 ? HIS B 271 GLN B 276 1 ? 6  
HELX_P HELX_P30 AD3 ARG B 296 ? ASN B 308 ? ARG B 281 ASN B 293 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 5 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 32  ? GLY A 41  ? TYR A 17  GLY A 26  
AA1 2 GLY A 44  ? ASP A 51  ? GLY A 29  ASP A 36  
AA1 3 LEU A 57  ? LYS A 64  ? LEU A 42  LYS A 49  
AA1 4 LYS A 101 ? GLU A 107 ? LYS A 86  GLU A 92  
AA1 5 TYR A 92  ? TRP A 98  ? TYR A 77  TRP A 83  
AA2 1 ILE A 158 ? ILE A 160 ? ILE A 143 ILE A 145 
AA2 2 VAL A 166 ? LEU A 168 ? VAL A 151 LEU A 153 
AA3 1 TYR B 32  ? GLY B 39  ? TYR B 17  GLY B 24  
AA3 2 GLU B 45  ? ASP B 51  ? GLU B 30  ASP B 36  
AA3 3 LEU B 57  ? LYS B 64  ? LEU B 42  LYS B 49  
AA3 4 LYS B 101 ? GLU B 107 ? LYS B 86  GLU B 92  
AA3 5 TYR B 92  ? TRP B 98  ? TYR B 77  TRP B 83  
AA4 1 ILE B 158 ? ILE B 160 ? ILE B 143 ILE B 145 
AA4 2 VAL B 166 ? LEU B 168 ? VAL B 151 LEU B 153 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 36  ? N GLN A 21  O LYS A 48  ? O LYS A 33  
AA1 2 3 N GLU A 45  ? N GLU A 30  O MET A 62  ? O MET A 47  
AA1 3 4 N VAL A 63  ? N VAL A 48  O LEU A 102 ? O LEU A 87  
AA1 4 5 O CYS A 105 ? O CYS A 90  N GLY A 94  ? N GLY A 79  
AA2 1 2 N LEU A 159 ? N LEU A 144 O ARG A 167 ? O ARG A 152 
AA3 1 2 N GLY B 39  ? N GLY B 24  O VAL B 46  ? O VAL B 31  
AA3 2 3 N GLU B 45  ? N GLU B 30  O MET B 62  ? O MET B 47  
AA3 3 4 N VAL B 63  ? N VAL B 48  O LEU B 102 ? O LEU B 87  
AA3 4 5 O CYS B 105 ? O CYS B 90  N GLY B 94  ? N GLY B 79  
AA4 1 2 N LEU B 159 ? N LEU B 144 O ARG B 167 ? O ARG B 152 
# 
_pdbx_entry_details.entry_id                   9N7R 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    527 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    555 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
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 ARG A 136 ? ? 86.93   -14.11 
2  1 ASP A 137 ? ? -144.79 48.35  
3  1 THR A 175 ? ? 64.18   169.47 
4  1 LYS A 189 ? ? 75.95   43.22  
5  1 LEU A 255 ? ? -86.32  49.12  
6  1 ASP B 53  ? ? -65.13  0.36   
7  1 ARG B 136 ? ? 77.61   -10.23 
8  1 ASP B 137 ? ? -142.39 47.81  
9  1 LEU B 211 ? ? 77.81   -1.12  
10 1 LEU B 255 ? ? -91.48  47.17  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 1.5018  22.2715  10.8102 0.3184 ? 0.0104  ? -0.0059 ? 0.3880 ? -0.0186 ? 0.3910 ? 2.2062 ? 
-0.5436 ? -0.8695 ? 1.8211  ? -1.1174 ? 1.6638 ? 0.1522  ? -0.0043 ? 0.3755  ? 0.1524  ? 0.0532  ? 0.1397  ? -0.2446 ? -0.2069 ? 
0.0000  ? 
2  'X-RAY DIFFRACTION' ? refined 7.5497  17.9812  21.9746 0.3419 ? -0.0014 ? -0.0075 ? 0.4110 ? -0.0412 ? 0.3377 ? 0.5799 ? 0.3160 
? 0.5823  ? 0.7513  ? -0.3269 ? 0.8860 ? 0.0108  ? -0.4749 ? -0.0044 ? 0.3765  ? 0.0039  ? -0.0725 ? -0.1277 ? -0.1333 ? -0.0000 ? 
3  'X-RAY DIFFRACTION' ? refined 18.7094 13.4122  8.1306  0.2118 ? -0.0123 ? -0.0212 ? 0.2275 ? -0.0076 ? 0.2512 ? 1.7958 ? 
-0.4598 ? -0.0613 ? 1.1298  ? -0.2839 ? 0.6932 ? 0.0411  ? -0.0936 ? 0.1394  ? -0.0095 ? -0.0650 ? -0.0149 ? -0.0349 ? -0.0440 ? 
0.0000  ? 
4  'X-RAY DIFFRACTION' ? refined 13.9724 2.3369   19.7189 0.3827 ? -0.0072 ? 0.0216  ? 0.3992 ? 0.0174  ? 0.3688 ? 0.8906 ? 0.6144 
? -1.9525 ? -0.1331 ? -0.6571 ? 0.5155 ? -0.0272 ? -0.1110 ? -0.0373 ? 0.2278  ? -0.0911 ? 0.0948  ? 0.0375  ? 0.0514  ? -0.0002 ? 
5  'X-RAY DIFFRACTION' ? refined 30.8687 -0.7181  7.8207  0.2312 ? 0.0412  ? -0.0073 ? 0.2768 ? 0.0242  ? 0.3023 ? 1.4803 ? 
-0.2529 ? -0.5634 ? 2.3322  ? 1.0159  ? 1.9226 ? -0.1165 ? -0.1119 ? -0.1888 ? 0.0765  ? -0.0293 ? -0.1401 ? 0.3549  ? 0.1351  ? 
-0.0001 ? 
6  'X-RAY DIFFRACTION' ? refined 20.8031 16.6494  -8.6898 0.4500 ? 0.0215  ? 0.0243  ? 0.3616 ? 0.0114  ? 0.4432 ? 0.7593 ? 
-0.0372 ? -0.0872 ? 0.4864  ? -0.0251 ? 0.0755 ? -0.1514 ? 0.6518  ? -0.2789 ? -0.8684 ? -0.0999 ? 0.1454  ? -0.0909 ? -0.1942 ? 
0.0083  ? 
7  'X-RAY DIFFRACTION' ? refined -0.7702 -26.8961 17.2662 0.7014 ? -0.0434 ? -0.0666 ? 0.6821 ? -0.0535 ? 0.5885 ? 0.6058 ? 0.2183 
? 0.1039  ? 1.4189  ? -0.6044 ? 3.1941 ? -0.0322 ? 0.5509  ? 0.0181  ? -0.5007 ? 0.3061  ? -0.2639 ? 0.7139  ? -0.0023 ? -0.0000 ? 
8  'X-RAY DIFFRACTION' ? refined -0.4912 -20.9085 34.0370 0.4414 ? 0.0245  ? 0.0012  ? 0.3323 ? 0.0060  ? 0.2624 ? 1.8683 ? 0.7233 
? 0.6025  ? 2.5929  ? -0.5138 ? 2.3193 ? 0.0827  ? 0.2872  ? -0.0847 ? -0.0420 ? 0.0624  ? 0.0944  ? 0.2493  ? -0.0054 ? -0.0025 ? 
9  'X-RAY DIFFRACTION' ? refined 12.1229 -10.5504 19.6633 0.4987 ? -0.0475 ? 0.0390  ? 0.4444 ? 0.0208  ? 0.4570 ? 0.1354 ? 0.8227 
? -1.2100 ? 0.1794  ? -1.0704 ? 0.3942 ? -0.0681 ? -0.0830 ? -0.3493 ? 0.1800  ? -0.0878 ? -0.0789 ? 0.0991  ? -0.2178 ? 0.0003  ? 
10 'X-RAY DIFFRACTION' ? refined 3.4915  -10.5759 44.1582 0.4351 ? 0.0116  ? 0.0224  ? 0.3405 ? -0.0028 ? 0.2649 ? 0.9048 ? 0.4713 
? 0.0844  ? 3.5502  ? -0.3028 ? 1.9785 ? 0.1846  ? -0.0925 ? 0.0733  ? 0.4611  ? -0.1266 ? -0.1179 ? -0.0886 ? 0.1449  ? -0.0000 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 6 through 49 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 50 through 83 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 84 through 150 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 151 through 210 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 211 through 280 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 281 through 296 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 8 through 83 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 84 through 150 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 151 through 193 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 194 through 294 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -14 ? A MET 1   
2  1 Y 1 A HIS -13 ? A HIS 2   
3  1 Y 1 A HIS -12 ? A HIS 3   
4  1 Y 1 A HIS -11 ? A HIS 4   
5  1 Y 1 A HIS -10 ? A HIS 5   
6  1 Y 1 A HIS -9  ? A HIS 6   
7  1 Y 1 A HIS -8  ? A HIS 7   
8  1 Y 1 A GLY -7  ? A GLY 8   
9  1 Y 1 A GLU -6  ? A GLU 9   
10 1 Y 1 A ASN -5  ? A ASN 10  
11 1 Y 1 A LEU -4  ? A LEU 11  
12 1 Y 1 A TYR -3  ? A TYR 12  
13 1 Y 1 A PHE -2  ? A PHE 13  
14 1 Y 1 A GLN -1  ? A GLN 14  
15 1 Y 1 A GLY 0   ? A GLY 15  
16 1 Y 1 A SER 1   ? A SER 16  
17 1 Y 1 A ASP 2   ? A ASP 17  
18 1 Y 1 A VAL 3   ? A VAL 18  
19 1 Y 1 A VAL 4   ? A VAL 19  
20 1 Y 1 A ASP 5   ? A ASP 20  
21 1 Y 1 B MET -14 ? B MET 1   
22 1 Y 1 B HIS -13 ? B HIS 2   
23 1 Y 1 B HIS -12 ? B HIS 3   
24 1 Y 1 B HIS -11 ? B HIS 4   
25 1 Y 1 B HIS -10 ? B HIS 5   
26 1 Y 1 B HIS -9  ? B HIS 6   
27 1 Y 1 B HIS -8  ? B HIS 7   
28 1 Y 1 B GLY -7  ? B GLY 8   
29 1 Y 1 B GLU -6  ? B GLU 9   
30 1 Y 1 B ASN -5  ? B ASN 10  
31 1 Y 1 B LEU -4  ? B LEU 11  
32 1 Y 1 B TYR -3  ? B TYR 12  
33 1 Y 1 B PHE -2  ? B PHE 13  
34 1 Y 1 B GLN -1  ? B GLN 14  
35 1 Y 1 B GLY 0   ? B GLY 15  
36 1 Y 1 B SER 1   ? B SER 16  
37 1 Y 1 B ASP 2   ? B ASP 17  
38 1 Y 1 B VAL 3   ? B VAL 18  
39 1 Y 1 B VAL 4   ? B VAL 19  
40 1 Y 1 B ASP 5   ? B ASP 20  
41 1 Y 1 B PRO 6   ? B PRO 21  
42 1 Y 1 B ASP 7   ? B ASP 22  
43 1 Y 1 B ASN 295 ? B ASN 310 
44 1 Y 1 B SER 296 ? B SER 311 
# 
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 
A1BWC C4   C Y N 1   
A1BWC C5   C Y N 2   
A1BWC C6   C Y N 3   
A1BWC C7   C Y N 4   
A1BWC C10  C Y N 5   
A1BWC C13  C Y N 6   
A1BWC C20  C N N 7   
A1BWC C21  C N N 8   
A1BWC C24  C N N 9   
A1BWC C26  C N N 10  
A1BWC C28  C N N 11  
A1BWC C1   C Y N 12  
A1BWC C14  C Y N 13  
A1BWC C16  C Y N 14  
A1BWC C18  C Y N 15  
A1BWC C19  C Y N 16  
A1BWC C2   C Y N 17  
A1BWC C25  C N N 18  
A1BWC C29  C N N 19  
A1BWC C30  C N N 20  
A1BWC C32  C N N 21  
A1BWC C9   C Y N 22  
A1BWC F11  F N N 23  
A1BWC F12  F N N 24  
A1BWC F33  F N N 25  
A1BWC F34  F N N 26  
A1BWC F35  F N N 27  
A1BWC N15  N Y N 28  
A1BWC N17  N Y N 29  
A1BWC N22  N N N 30  
A1BWC N27  N N N 31  
A1BWC N8   N N N 32  
A1BWC O23  O N N 33  
A1BWC O3   O N N 34  
A1BWC O31  O N N 35  
A1BWC H61  H N N 36  
A1BWC H131 H N N 37  
A1BWC H242 H N N 38  
A1BWC H241 H N N 39  
A1BWC H262 H N N 40  
A1BWC H261 H N N 41  
A1BWC H281 H N N 42  
A1BWC H282 H N N 43  
A1BWC H141 H N N 44  
A1BWC H181 H N N 45  
A1BWC H251 H N N 46  
A1BWC H252 H N N 47  
A1BWC H292 H N N 48  
A1BWC H291 H N N 49  
A1BWC H301 H N N 50  
A1BWC H302 H N N 51  
A1BWC H321 H N N 52  
A1BWC H322 H N N 53  
A1BWC H91  H N N 54  
A1BWC H171 H N N 55  
A1BWC H221 H N N 56  
A1BWC H81  H N N 57  
ALA   N    N N N 58  
ALA   CA   C N S 59  
ALA   C    C N N 60  
ALA   O    O N N 61  
ALA   CB   C N N 62  
ALA   OXT  O N N 63  
ALA   H    H N N 64  
ALA   H2   H N N 65  
ALA   HA   H N N 66  
ALA   HB1  H N N 67  
ALA   HB2  H N N 68  
ALA   HB3  H N N 69  
ALA   HXT  H N N 70  
ARG   N    N N N 71  
ARG   CA   C N S 72  
ARG   C    C N N 73  
ARG   O    O N N 74  
ARG   CB   C N N 75  
ARG   CG   C N N 76  
ARG   CD   C N N 77  
ARG   NE   N N N 78  
ARG   CZ   C N N 79  
ARG   NH1  N N N 80  
ARG   NH2  N N N 81  
ARG   OXT  O N N 82  
ARG   H    H N N 83  
ARG   H2   H N N 84  
ARG   HA   H N N 85  
ARG   HB2  H N N 86  
ARG   HB3  H N N 87  
ARG   HG2  H N N 88  
ARG   HG3  H N N 89  
ARG   HD2  H N N 90  
ARG   HD3  H N N 91  
ARG   HE   H N N 92  
ARG   HH11 H N N 93  
ARG   HH12 H N N 94  
ARG   HH21 H N N 95  
ARG   HH22 H N N 96  
ARG   HXT  H N N 97  
ASN   N    N N N 98  
ASN   CA   C N S 99  
ASN   C    C N N 100 
ASN   O    O N N 101 
ASN   CB   C N N 102 
ASN   CG   C N N 103 
ASN   OD1  O N N 104 
ASN   ND2  N N N 105 
ASN   OXT  O N N 106 
ASN   H    H N N 107 
ASN   H2   H N N 108 
ASN   HA   H N N 109 
ASN   HB2  H N N 110 
ASN   HB3  H N N 111 
ASN   HD21 H N N 112 
ASN   HD22 H N N 113 
ASN   HXT  H N N 114 
ASP   N    N N N 115 
ASP   CA   C N S 116 
ASP   C    C N N 117 
ASP   O    O N N 118 
ASP   CB   C N N 119 
ASP   CG   C N N 120 
ASP   OD1  O N N 121 
ASP   OD2  O N N 122 
ASP   OXT  O N N 123 
ASP   H    H N N 124 
ASP   H2   H N N 125 
ASP   HA   H N N 126 
ASP   HB2  H N N 127 
ASP   HB3  H N N 128 
ASP   HD2  H N N 129 
ASP   HXT  H N N 130 
CYS   N    N N N 131 
CYS   CA   C N R 132 
CYS   C    C N N 133 
CYS   O    O N N 134 
CYS   CB   C N N 135 
CYS   SG   S N N 136 
CYS   OXT  O N N 137 
CYS   H    H N N 138 
CYS   H2   H N N 139 
CYS   HA   H N N 140 
CYS   HB2  H N N 141 
CYS   HB3  H N N 142 
CYS   HG   H N N 143 
CYS   HXT  H N N 144 
DMS   S    S N N 145 
DMS   O    O N N 146 
DMS   C1   C N N 147 
DMS   C2   C N N 148 
DMS   H11  H N N 149 
DMS   H12  H N N 150 
DMS   H13  H N N 151 
DMS   H21  H N N 152 
DMS   H22  H N N 153 
DMS   H23  H N N 154 
EDO   C1   C N N 155 
EDO   O1   O N N 156 
EDO   C2   C N N 157 
EDO   O2   O N N 158 
EDO   H11  H N N 159 
EDO   H12  H N N 160 
EDO   HO1  H N N 161 
EDO   H21  H N N 162 
EDO   H22  H N N 163 
EDO   HO2  H N N 164 
GLN   N    N N N 165 
GLN   CA   C N S 166 
GLN   C    C N N 167 
GLN   O    O N N 168 
GLN   CB   C N N 169 
GLN   CG   C N N 170 
GLN   CD   C N N 171 
GLN   OE1  O N N 172 
GLN   NE2  N N N 173 
GLN   OXT  O N N 174 
GLN   H    H N N 175 
GLN   H2   H N N 176 
GLN   HA   H N N 177 
GLN   HB2  H N N 178 
GLN   HB3  H N N 179 
GLN   HG2  H N N 180 
GLN   HG3  H N N 181 
GLN   HE21 H N N 182 
GLN   HE22 H N N 183 
GLN   HXT  H N N 184 
GLU   N    N N N 185 
GLU   CA   C N S 186 
GLU   C    C N N 187 
GLU   O    O N N 188 
GLU   CB   C N N 189 
GLU   CG   C N N 190 
GLU   CD   C N N 191 
GLU   OE1  O N N 192 
GLU   OE2  O N N 193 
GLU   OXT  O N N 194 
GLU   H    H N N 195 
GLU   H2   H N N 196 
GLU   HA   H N N 197 
GLU   HB2  H N N 198 
GLU   HB3  H N N 199 
GLU   HG2  H N N 200 
GLU   HG3  H N N 201 
GLU   HE2  H N N 202 
GLU   HXT  H N N 203 
GLY   N    N N N 204 
GLY   CA   C N N 205 
GLY   C    C N N 206 
GLY   O    O N N 207 
GLY   OXT  O N N 208 
GLY   H    H N N 209 
GLY   H2   H N N 210 
GLY   HA2  H N N 211 
GLY   HA3  H N N 212 
GLY   HXT  H N N 213 
GOL   C1   C N N 214 
GOL   O1   O N N 215 
GOL   C2   C N N 216 
GOL   O2   O N N 217 
GOL   C3   C N N 218 
GOL   O3   O N N 219 
GOL   H11  H N N 220 
GOL   H12  H N N 221 
GOL   HO1  H N N 222 
GOL   H2   H N N 223 
GOL   HO2  H N N 224 
GOL   H31  H N N 225 
GOL   H32  H N N 226 
GOL   HO3  H N N 227 
HIS   N    N N N 228 
HIS   CA   C N S 229 
HIS   C    C N N 230 
HIS   O    O N N 231 
HIS   CB   C N N 232 
HIS   CG   C Y N 233 
HIS   ND1  N Y N 234 
HIS   CD2  C Y N 235 
HIS   CE1  C Y N 236 
HIS   NE2  N Y N 237 
HIS   OXT  O N N 238 
HIS   H    H N N 239 
HIS   H2   H N N 240 
HIS   HA   H N N 241 
HIS   HB2  H N N 242 
HIS   HB3  H N N 243 
HIS   HD1  H N N 244 
HIS   HD2  H N N 245 
HIS   HE1  H N N 246 
HIS   HE2  H N N 247 
HIS   HXT  H N N 248 
HOH   O    O N N 249 
HOH   H1   H N N 250 
HOH   H2   H N N 251 
ILE   N    N N N 252 
ILE   CA   C N S 253 
ILE   C    C N N 254 
ILE   O    O N N 255 
ILE   CB   C N S 256 
ILE   CG1  C N N 257 
ILE   CG2  C N N 258 
ILE   CD1  C N N 259 
ILE   OXT  O N N 260 
ILE   H    H N N 261 
ILE   H2   H N N 262 
ILE   HA   H N N 263 
ILE   HB   H N N 264 
ILE   HG12 H N N 265 
ILE   HG13 H N N 266 
ILE   HG21 H N N 267 
ILE   HG22 H N N 268 
ILE   HG23 H N N 269 
ILE   HD11 H N N 270 
ILE   HD12 H N N 271 
ILE   HD13 H N N 272 
ILE   HXT  H N N 273 
LEU   N    N N N 274 
LEU   CA   C N S 275 
LEU   C    C N N 276 
LEU   O    O N N 277 
LEU   CB   C N N 278 
LEU   CG   C N N 279 
LEU   CD1  C N N 280 
LEU   CD2  C N N 281 
LEU   OXT  O N N 282 
LEU   H    H N N 283 
LEU   H2   H N N 284 
LEU   HA   H N N 285 
LEU   HB2  H N N 286 
LEU   HB3  H N N 287 
LEU   HG   H N N 288 
LEU   HD11 H N N 289 
LEU   HD12 H N N 290 
LEU   HD13 H N N 291 
LEU   HD21 H N N 292 
LEU   HD22 H N N 293 
LEU   HD23 H N N 294 
LEU   HXT  H N N 295 
LYS   N    N N N 296 
LYS   CA   C N S 297 
LYS   C    C N N 298 
LYS   O    O N N 299 
LYS   CB   C N N 300 
LYS   CG   C N N 301 
LYS   CD   C N N 302 
LYS   CE   C N N 303 
LYS   NZ   N N N 304 
LYS   OXT  O N N 305 
LYS   H    H N N 306 
LYS   H2   H N N 307 
LYS   HA   H N N 308 
LYS   HB2  H N N 309 
LYS   HB3  H N N 310 
LYS   HG2  H N N 311 
LYS   HG3  H N N 312 
LYS   HD2  H N N 313 
LYS   HD3  H N N 314 
LYS   HE2  H N N 315 
LYS   HE3  H N N 316 
LYS   HZ1  H N N 317 
LYS   HZ2  H N N 318 
LYS   HZ3  H N N 319 
LYS   HXT  H N N 320 
MET   N    N N N 321 
MET   CA   C N S 322 
MET   C    C N N 323 
MET   O    O N N 324 
MET   CB   C N N 325 
MET   CG   C N N 326 
MET   SD   S N N 327 
MET   CE   C N N 328 
MET   OXT  O N N 329 
MET   H    H N N 330 
MET   H2   H N N 331 
MET   HA   H N N 332 
MET   HB2  H N N 333 
MET   HB3  H N N 334 
MET   HG2  H N N 335 
MET   HG3  H N N 336 
MET   HE1  H N N 337 
MET   HE2  H N N 338 
MET   HE3  H N N 339 
MET   HXT  H N N 340 
PHE   N    N N N 341 
PHE   CA   C N S 342 
PHE   C    C N N 343 
PHE   O    O N N 344 
PHE   CB   C N N 345 
PHE   CG   C Y N 346 
PHE   CD1  C Y N 347 
PHE   CD2  C Y N 348 
PHE   CE1  C Y N 349 
PHE   CE2  C Y N 350 
PHE   CZ   C Y N 351 
PHE   OXT  O N N 352 
PHE   H    H N N 353 
PHE   H2   H N N 354 
PHE   HA   H N N 355 
PHE   HB2  H N N 356 
PHE   HB3  H N N 357 
PHE   HD1  H N N 358 
PHE   HD2  H N N 359 
PHE   HE1  H N N 360 
PHE   HE2  H N N 361 
PHE   HZ   H N N 362 
PHE   HXT  H N N 363 
PRO   N    N N N 364 
PRO   CA   C N S 365 
PRO   C    C N N 366 
PRO   O    O N N 367 
PRO   CB   C N N 368 
PRO   CG   C N N 369 
PRO   CD   C N N 370 
PRO   OXT  O N N 371 
PRO   H    H N N 372 
PRO   HA   H N N 373 
PRO   HB2  H N N 374 
PRO   HB3  H N N 375 
PRO   HG2  H N N 376 
PRO   HG3  H N N 377 
PRO   HD2  H N N 378 
PRO   HD3  H N N 379 
PRO   HXT  H N N 380 
SER   N    N N N 381 
SER   CA   C N S 382 
SER   C    C N N 383 
SER   O    O N N 384 
SER   CB   C N N 385 
SER   OG   O N N 386 
SER   OXT  O N N 387 
SER   H    H N N 388 
SER   H2   H N N 389 
SER   HA   H N N 390 
SER   HB2  H N N 391 
SER   HB3  H N N 392 
SER   HG   H N N 393 
SER   HXT  H N N 394 
THR   N    N N N 395 
THR   CA   C N S 396 
THR   C    C N N 397 
THR   O    O N N 398 
THR   CB   C N R 399 
THR   OG1  O N N 400 
THR   CG2  C N N 401 
THR   OXT  O N N 402 
THR   H    H N N 403 
THR   H2   H N N 404 
THR   HA   H N N 405 
THR   HB   H N N 406 
THR   HG1  H N N 407 
THR   HG21 H N N 408 
THR   HG22 H N N 409 
THR   HG23 H N N 410 
THR   HXT  H N N 411 
TRP   N    N N N 412 
TRP   CA   C N S 413 
TRP   C    C N N 414 
TRP   O    O N N 415 
TRP   CB   C N N 416 
TRP   CG   C Y N 417 
TRP   CD1  C Y N 418 
TRP   CD2  C Y N 419 
TRP   NE1  N Y N 420 
TRP   CE2  C Y N 421 
TRP   CE3  C Y N 422 
TRP   CZ2  C Y N 423 
TRP   CZ3  C Y N 424 
TRP   CH2  C Y N 425 
TRP   OXT  O N N 426 
TRP   H    H N N 427 
TRP   H2   H N N 428 
TRP   HA   H N N 429 
TRP   HB2  H N N 430 
TRP   HB3  H N N 431 
TRP   HD1  H N N 432 
TRP   HE1  H N N 433 
TRP   HE3  H N N 434 
TRP   HZ2  H N N 435 
TRP   HZ3  H N N 436 
TRP   HH2  H N N 437 
TRP   HXT  H N N 438 
TYR   N    N N N 439 
TYR   CA   C N S 440 
TYR   C    C N N 441 
TYR   O    O N N 442 
TYR   CB   C N N 443 
TYR   CG   C Y N 444 
TYR   CD1  C Y N 445 
TYR   CD2  C Y N 446 
TYR   CE1  C Y N 447 
TYR   CE2  C Y N 448 
TYR   CZ   C Y N 449 
TYR   OH   O N N 450 
TYR   OXT  O N N 451 
TYR   H    H N N 452 
TYR   H2   H N N 453 
TYR   HA   H N N 454 
TYR   HB2  H N N 455 
TYR   HB3  H N N 456 
TYR   HD1  H N N 457 
TYR   HD2  H N N 458 
TYR   HE1  H N N 459 
TYR   HE2  H N N 460 
TYR   HH   H N N 461 
TYR   HXT  H N N 462 
VAL   N    N N N 463 
VAL   CA   C N S 464 
VAL   C    C N N 465 
VAL   O    O N N 466 
VAL   CB   C N N 467 
VAL   CG1  C N N 468 
VAL   CG2  C N N 469 
VAL   OXT  O N N 470 
VAL   H    H N N 471 
VAL   H2   H N N 472 
VAL   HA   H N N 473 
VAL   HB   H N N 474 
VAL   HG11 H N N 475 
VAL   HG12 H N N 476 
VAL   HG13 H N N 477 
VAL   HG21 H N N 478 
VAL   HG22 H N N 479 
VAL   HG23 H N N 480 
VAL   HXT  H N N 481 
# 
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 
A1BWC N17 C18  sing Y N 1   
A1BWC N17 C16  sing Y N 2   
A1BWC C18 C19  doub Y N 3   
A1BWC F33 C20  sing N N 4   
A1BWC F34 C20  sing N N 5   
A1BWC C16 N15  doub Y N 6   
A1BWC C16 C1   sing Y N 7   
A1BWC C19 C20  sing N N 8   
A1BWC C19 C1   sing Y N 9   
A1BWC F12 C5   sing N N 10  
A1BWC N15 C14  sing Y N 11  
A1BWC C30 O31  sing N N 12  
A1BWC C30 C29  sing N N 13  
A1BWC C20 F35  sing N N 14  
A1BWC C1  C2   doub Y N 15  
A1BWC O31 C32  sing N N 16  
A1BWC C14 C13  doub Y N 17  
A1BWC C32 C28  sing N N 18  
A1BWC C2  C13  sing Y N 19  
A1BWC C2  O3   sing N N 20  
A1BWC C5  C6   doub Y N 21  
A1BWC C5  C4   sing Y N 22  
A1BWC C29 N27  sing N N 23  
A1BWC O3  C4   sing N N 24  
A1BWC N27 C28  sing N N 25  
A1BWC N27 C26  sing N N 26  
A1BWC C6  C7   sing Y N 27  
A1BWC O23 C21  doub N N 28  
A1BWC C4  C10  doub Y N 29  
A1BWC C25 C26  sing N N 30  
A1BWC C25 C24  sing N N 31  
A1BWC C21 N8   sing N N 32  
A1BWC C21 N22  sing N N 33  
A1BWC C7  N8   sing N N 34  
A1BWC C7  C9   doub Y N 35  
A1BWC C24 N22  sing N N 36  
A1BWC C10 C9   sing Y N 37  
A1BWC C10 F11  sing N N 38  
A1BWC C6  H61  sing N N 39  
A1BWC C13 H131 sing N N 40  
A1BWC C24 H242 sing N N 41  
A1BWC C24 H241 sing N N 42  
A1BWC C26 H262 sing N N 43  
A1BWC C26 H261 sing N N 44  
A1BWC C28 H281 sing N N 45  
A1BWC C28 H282 sing N N 46  
A1BWC C14 H141 sing N N 47  
A1BWC C18 H181 sing N N 48  
A1BWC C25 H251 sing N N 49  
A1BWC C25 H252 sing N N 50  
A1BWC C29 H292 sing N N 51  
A1BWC C29 H291 sing N N 52  
A1BWC C30 H301 sing N N 53  
A1BWC C30 H302 sing N N 54  
A1BWC C32 H321 sing N N 55  
A1BWC C32 H322 sing N N 56  
A1BWC C9  H91  sing N N 57  
A1BWC N17 H171 sing N N 58  
A1BWC N22 H221 sing N N 59  
A1BWC N8  H81  sing N N 60  
ALA   N   CA   sing N N 61  
ALA   N   H    sing N N 62  
ALA   N   H2   sing N N 63  
ALA   CA  C    sing N N 64  
ALA   CA  CB   sing N N 65  
ALA   CA  HA   sing N N 66  
ALA   C   O    doub N N 67  
ALA   C   OXT  sing N N 68  
ALA   CB  HB1  sing N N 69  
ALA   CB  HB2  sing N N 70  
ALA   CB  HB3  sing N N 71  
ALA   OXT HXT  sing N N 72  
ARG   N   CA   sing N N 73  
ARG   N   H    sing N N 74  
ARG   N   H2   sing N N 75  
ARG   CA  C    sing N N 76  
ARG   CA  CB   sing N N 77  
ARG   CA  HA   sing N N 78  
ARG   C   O    doub N N 79  
ARG   C   OXT  sing N N 80  
ARG   CB  CG   sing N N 81  
ARG   CB  HB2  sing N N 82  
ARG   CB  HB3  sing N N 83  
ARG   CG  CD   sing N N 84  
ARG   CG  HG2  sing N N 85  
ARG   CG  HG3  sing N N 86  
ARG   CD  NE   sing N N 87  
ARG   CD  HD2  sing N N 88  
ARG   CD  HD3  sing N N 89  
ARG   NE  CZ   sing N N 90  
ARG   NE  HE   sing N N 91  
ARG   CZ  NH1  sing N N 92  
ARG   CZ  NH2  doub N N 93  
ARG   NH1 HH11 sing N N 94  
ARG   NH1 HH12 sing N N 95  
ARG   NH2 HH21 sing N N 96  
ARG   NH2 HH22 sing N N 97  
ARG   OXT HXT  sing N N 98  
ASN   N   CA   sing N N 99  
ASN   N   H    sing N N 100 
ASN   N   H2   sing N N 101 
ASN   CA  C    sing N N 102 
ASN   CA  CB   sing N N 103 
ASN   CA  HA   sing N N 104 
ASN   C   O    doub N N 105 
ASN   C   OXT  sing N N 106 
ASN   CB  CG   sing N N 107 
ASN   CB  HB2  sing N N 108 
ASN   CB  HB3  sing N N 109 
ASN   CG  OD1  doub N N 110 
ASN   CG  ND2  sing N N 111 
ASN   ND2 HD21 sing N N 112 
ASN   ND2 HD22 sing N N 113 
ASN   OXT HXT  sing N N 114 
ASP   N   CA   sing N N 115 
ASP   N   H    sing N N 116 
ASP   N   H2   sing N N 117 
ASP   CA  C    sing N N 118 
ASP   CA  CB   sing N N 119 
ASP   CA  HA   sing N N 120 
ASP   C   O    doub N N 121 
ASP   C   OXT  sing N N 122 
ASP   CB  CG   sing N N 123 
ASP   CB  HB2  sing N N 124 
ASP   CB  HB3  sing N N 125 
ASP   CG  OD1  doub N N 126 
ASP   CG  OD2  sing N N 127 
ASP   OD2 HD2  sing N N 128 
ASP   OXT HXT  sing N N 129 
CYS   N   CA   sing N N 130 
CYS   N   H    sing N N 131 
CYS   N   H2   sing N N 132 
CYS   CA  C    sing N N 133 
CYS   CA  CB   sing N N 134 
CYS   CA  HA   sing N N 135 
CYS   C   O    doub N N 136 
CYS   C   OXT  sing N N 137 
CYS   CB  SG   sing N N 138 
CYS   CB  HB2  sing N N 139 
CYS   CB  HB3  sing N N 140 
CYS   SG  HG   sing N N 141 
CYS   OXT HXT  sing N N 142 
DMS   S   O    doub N N 143 
DMS   S   C1   sing N N 144 
DMS   S   C2   sing N N 145 
DMS   C1  H11  sing N N 146 
DMS   C1  H12  sing N N 147 
DMS   C1  H13  sing N N 148 
DMS   C2  H21  sing N N 149 
DMS   C2  H22  sing N N 150 
DMS   C2  H23  sing N N 151 
EDO   C1  O1   sing N N 152 
EDO   C1  C2   sing N N 153 
EDO   C1  H11  sing N N 154 
EDO   C1  H12  sing N N 155 
EDO   O1  HO1  sing N N 156 
EDO   C2  O2   sing N N 157 
EDO   C2  H21  sing N N 158 
EDO   C2  H22  sing N N 159 
EDO   O2  HO2  sing N N 160 
GLN   N   CA   sing N N 161 
GLN   N   H    sing N N 162 
GLN   N   H2   sing N N 163 
GLN   CA  C    sing N N 164 
GLN   CA  CB   sing N N 165 
GLN   CA  HA   sing N N 166 
GLN   C   O    doub N N 167 
GLN   C   OXT  sing N N 168 
GLN   CB  CG   sing N N 169 
GLN   CB  HB2  sing N N 170 
GLN   CB  HB3  sing N N 171 
GLN   CG  CD   sing N N 172 
GLN   CG  HG2  sing N N 173 
GLN   CG  HG3  sing N N 174 
GLN   CD  OE1  doub N N 175 
GLN   CD  NE2  sing N N 176 
GLN   NE2 HE21 sing N N 177 
GLN   NE2 HE22 sing N N 178 
GLN   OXT HXT  sing N N 179 
GLU   N   CA   sing N N 180 
GLU   N   H    sing N N 181 
GLU   N   H2   sing N N 182 
GLU   CA  C    sing N N 183 
GLU   CA  CB   sing N N 184 
GLU   CA  HA   sing N N 185 
GLU   C   O    doub N N 186 
GLU   C   OXT  sing N N 187 
GLU   CB  CG   sing N N 188 
GLU   CB  HB2  sing N N 189 
GLU   CB  HB3  sing N N 190 
GLU   CG  CD   sing N N 191 
GLU   CG  HG2  sing N N 192 
GLU   CG  HG3  sing N N 193 
GLU   CD  OE1  doub N N 194 
GLU   CD  OE2  sing N N 195 
GLU   OE2 HE2  sing N N 196 
GLU   OXT HXT  sing N N 197 
GLY   N   CA   sing N N 198 
GLY   N   H    sing N N 199 
GLY   N   H2   sing N N 200 
GLY   CA  C    sing N N 201 
GLY   CA  HA2  sing N N 202 
GLY   CA  HA3  sing N N 203 
GLY   C   O    doub N N 204 
GLY   C   OXT  sing N N 205 
GLY   OXT HXT  sing N N 206 
GOL   C1  O1   sing N N 207 
GOL   C1  C2   sing N N 208 
GOL   C1  H11  sing N N 209 
GOL   C1  H12  sing N N 210 
GOL   O1  HO1  sing N N 211 
GOL   C2  O2   sing N N 212 
GOL   C2  C3   sing N N 213 
GOL   C2  H2   sing N N 214 
GOL   O2  HO2  sing N N 215 
GOL   C3  O3   sing N N 216 
GOL   C3  H31  sing N N 217 
GOL   C3  H32  sing N N 218 
GOL   O3  HO3  sing N N 219 
HIS   N   CA   sing N N 220 
HIS   N   H    sing N N 221 
HIS   N   H2   sing N N 222 
HIS   CA  C    sing N N 223 
HIS   CA  CB   sing N N 224 
HIS   CA  HA   sing N N 225 
HIS   C   O    doub N N 226 
HIS   C   OXT  sing N N 227 
HIS   CB  CG   sing N N 228 
HIS   CB  HB2  sing N N 229 
HIS   CB  HB3  sing N N 230 
HIS   CG  ND1  sing Y N 231 
HIS   CG  CD2  doub Y N 232 
HIS   ND1 CE1  doub Y N 233 
HIS   ND1 HD1  sing N N 234 
HIS   CD2 NE2  sing Y N 235 
HIS   CD2 HD2  sing N N 236 
HIS   CE1 NE2  sing Y N 237 
HIS   CE1 HE1  sing N N 238 
HIS   NE2 HE2  sing N N 239 
HIS   OXT HXT  sing N N 240 
HOH   O   H1   sing N N 241 
HOH   O   H2   sing N N 242 
ILE   N   CA   sing N N 243 
ILE   N   H    sing N N 244 
ILE   N   H2   sing N N 245 
ILE   CA  C    sing N N 246 
ILE   CA  CB   sing N N 247 
ILE   CA  HA   sing N N 248 
ILE   C   O    doub N N 249 
ILE   C   OXT  sing N N 250 
ILE   CB  CG1  sing N N 251 
ILE   CB  CG2  sing N N 252 
ILE   CB  HB   sing N N 253 
ILE   CG1 CD1  sing N N 254 
ILE   CG1 HG12 sing N N 255 
ILE   CG1 HG13 sing N N 256 
ILE   CG2 HG21 sing N N 257 
ILE   CG2 HG22 sing N N 258 
ILE   CG2 HG23 sing N N 259 
ILE   CD1 HD11 sing N N 260 
ILE   CD1 HD12 sing N N 261 
ILE   CD1 HD13 sing N N 262 
ILE   OXT HXT  sing N N 263 
LEU   N   CA   sing N N 264 
LEU   N   H    sing N N 265 
LEU   N   H2   sing N N 266 
LEU   CA  C    sing N N 267 
LEU   CA  CB   sing N N 268 
LEU   CA  HA   sing N N 269 
LEU   C   O    doub N N 270 
LEU   C   OXT  sing N N 271 
LEU   CB  CG   sing N N 272 
LEU   CB  HB2  sing N N 273 
LEU   CB  HB3  sing N N 274 
LEU   CG  CD1  sing N N 275 
LEU   CG  CD2  sing N N 276 
LEU   CG  HG   sing N N 277 
LEU   CD1 HD11 sing N N 278 
LEU   CD1 HD12 sing N N 279 
LEU   CD1 HD13 sing N N 280 
LEU   CD2 HD21 sing N N 281 
LEU   CD2 HD22 sing N N 282 
LEU   CD2 HD23 sing N N 283 
LEU   OXT HXT  sing N N 284 
LYS   N   CA   sing N N 285 
LYS   N   H    sing N N 286 
LYS   N   H2   sing N N 287 
LYS   CA  C    sing N N 288 
LYS   CA  CB   sing N N 289 
LYS   CA  HA   sing N N 290 
LYS   C   O    doub N N 291 
LYS   C   OXT  sing N N 292 
LYS   CB  CG   sing N N 293 
LYS   CB  HB2  sing N N 294 
LYS   CB  HB3  sing N N 295 
LYS   CG  CD   sing N N 296 
LYS   CG  HG2  sing N N 297 
LYS   CG  HG3  sing N N 298 
LYS   CD  CE   sing N N 299 
LYS   CD  HD2  sing N N 300 
LYS   CD  HD3  sing N N 301 
LYS   CE  NZ   sing N N 302 
LYS   CE  HE2  sing N N 303 
LYS   CE  HE3  sing N N 304 
LYS   NZ  HZ1  sing N N 305 
LYS   NZ  HZ2  sing N N 306 
LYS   NZ  HZ3  sing N N 307 
LYS   OXT HXT  sing N N 308 
MET   N   CA   sing N N 309 
MET   N   H    sing N N 310 
MET   N   H2   sing N N 311 
MET   CA  C    sing N N 312 
MET   CA  CB   sing N N 313 
MET   CA  HA   sing N N 314 
MET   C   O    doub N N 315 
MET   C   OXT  sing N N 316 
MET   CB  CG   sing N N 317 
MET   CB  HB2  sing N N 318 
MET   CB  HB3  sing N N 319 
MET   CG  SD   sing N N 320 
MET   CG  HG2  sing N N 321 
MET   CG  HG3  sing N N 322 
MET   SD  CE   sing N N 323 
MET   CE  HE1  sing N N 324 
MET   CE  HE2  sing N N 325 
MET   CE  HE3  sing N N 326 
MET   OXT HXT  sing N N 327 
PHE   N   CA   sing N N 328 
PHE   N   H    sing N N 329 
PHE   N   H2   sing N N 330 
PHE   CA  C    sing N N 331 
PHE   CA  CB   sing N N 332 
PHE   CA  HA   sing N N 333 
PHE   C   O    doub N N 334 
PHE   C   OXT  sing N N 335 
PHE   CB  CG   sing N N 336 
PHE   CB  HB2  sing N N 337 
PHE   CB  HB3  sing N N 338 
PHE   CG  CD1  doub Y N 339 
PHE   CG  CD2  sing Y N 340 
PHE   CD1 CE1  sing Y N 341 
PHE   CD1 HD1  sing N N 342 
PHE   CD2 CE2  doub Y N 343 
PHE   CD2 HD2  sing N N 344 
PHE   CE1 CZ   doub Y N 345 
PHE   CE1 HE1  sing N N 346 
PHE   CE2 CZ   sing Y N 347 
PHE   CE2 HE2  sing N N 348 
PHE   CZ  HZ   sing N N 349 
PHE   OXT HXT  sing N N 350 
PRO   N   CA   sing N N 351 
PRO   N   CD   sing N N 352 
PRO   N   H    sing N N 353 
PRO   CA  C    sing N N 354 
PRO   CA  CB   sing N N 355 
PRO   CA  HA   sing N N 356 
PRO   C   O    doub N N 357 
PRO   C   OXT  sing N N 358 
PRO   CB  CG   sing N N 359 
PRO   CB  HB2  sing N N 360 
PRO   CB  HB3  sing N N 361 
PRO   CG  CD   sing N N 362 
PRO   CG  HG2  sing N N 363 
PRO   CG  HG3  sing N N 364 
PRO   CD  HD2  sing N N 365 
PRO   CD  HD3  sing N N 366 
PRO   OXT HXT  sing N N 367 
SER   N   CA   sing N N 368 
SER   N   H    sing N N 369 
SER   N   H2   sing N N 370 
SER   CA  C    sing N N 371 
SER   CA  CB   sing N N 372 
SER   CA  HA   sing N N 373 
SER   C   O    doub N N 374 
SER   C   OXT  sing N N 375 
SER   CB  OG   sing N N 376 
SER   CB  HB2  sing N N 377 
SER   CB  HB3  sing N N 378 
SER   OG  HG   sing N N 379 
SER   OXT HXT  sing N N 380 
THR   N   CA   sing N N 381 
THR   N   H    sing N N 382 
THR   N   H2   sing N N 383 
THR   CA  C    sing N N 384 
THR   CA  CB   sing N N 385 
THR   CA  HA   sing N N 386 
THR   C   O    doub N N 387 
THR   C   OXT  sing N N 388 
THR   CB  OG1  sing N N 389 
THR   CB  CG2  sing N N 390 
THR   CB  HB   sing N N 391 
THR   OG1 HG1  sing N N 392 
THR   CG2 HG21 sing N N 393 
THR   CG2 HG22 sing N N 394 
THR   CG2 HG23 sing N N 395 
THR   OXT HXT  sing N N 396 
TRP   N   CA   sing N N 397 
TRP   N   H    sing N N 398 
TRP   N   H2   sing N N 399 
TRP   CA  C    sing N N 400 
TRP   CA  CB   sing N N 401 
TRP   CA  HA   sing N N 402 
TRP   C   O    doub N N 403 
TRP   C   OXT  sing N N 404 
TRP   CB  CG   sing N N 405 
TRP   CB  HB2  sing N N 406 
TRP   CB  HB3  sing N N 407 
TRP   CG  CD1  doub Y N 408 
TRP   CG  CD2  sing Y N 409 
TRP   CD1 NE1  sing Y N 410 
TRP   CD1 HD1  sing N N 411 
TRP   CD2 CE2  doub Y N 412 
TRP   CD2 CE3  sing Y N 413 
TRP   NE1 CE2  sing Y N 414 
TRP   NE1 HE1  sing N N 415 
TRP   CE2 CZ2  sing Y N 416 
TRP   CE3 CZ3  doub Y N 417 
TRP   CE3 HE3  sing N N 418 
TRP   CZ2 CH2  doub Y N 419 
TRP   CZ2 HZ2  sing N N 420 
TRP   CZ3 CH2  sing Y N 421 
TRP   CZ3 HZ3  sing N N 422 
TRP   CH2 HH2  sing N N 423 
TRP   OXT HXT  sing N N 424 
TYR   N   CA   sing N N 425 
TYR   N   H    sing N N 426 
TYR   N   H2   sing N N 427 
TYR   CA  C    sing N N 428 
TYR   CA  CB   sing N N 429 
TYR   CA  HA   sing N N 430 
TYR   C   O    doub N N 431 
TYR   C   OXT  sing N N 432 
TYR   CB  CG   sing N N 433 
TYR   CB  HB2  sing N N 434 
TYR   CB  HB3  sing N N 435 
TYR   CG  CD1  doub Y N 436 
TYR   CG  CD2  sing Y N 437 
TYR   CD1 CE1  sing Y N 438 
TYR   CD1 HD1  sing N N 439 
TYR   CD2 CE2  doub Y N 440 
TYR   CD2 HD2  sing N N 441 
TYR   CE1 CZ   doub Y N 442 
TYR   CE1 HE1  sing N N 443 
TYR   CE2 CZ   sing Y N 444 
TYR   CE2 HE2  sing N N 445 
TYR   CZ  OH   sing N N 446 
TYR   OH  HH   sing N N 447 
TYR   OXT HXT  sing N N 448 
VAL   N   CA   sing N N 449 
VAL   N   H    sing N N 450 
VAL   N   H2   sing N N 451 
VAL   CA  C    sing N N 452 
VAL   CA  CB   sing N N 453 
VAL   CA  HA   sing N N 454 
VAL   C   O    doub N N 455 
VAL   C   OXT  sing N N 456 
VAL   CB  CG1  sing N N 457 
VAL   CB  CG2  sing N N 458 
VAL   CB  HB   sing N N 459 
VAL   CG1 HG11 sing N N 460 
VAL   CG1 HG12 sing N N 461 
VAL   CG1 HG13 sing N N 462 
VAL   CG2 HG21 sing N N 463 
VAL   CG2 HG22 sing N N 464 
VAL   CG2 HG23 sing N N 465 
VAL   OXT HXT  sing N N 466 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Internal Model' 
# 
_atom_sites.entry_id                    9N7R 
_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]   0.020751 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002115 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013040 
_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]   0.011706 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
F 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . PRO   A 1 21  ? 5.094   28.006  28.438  1.00 66.85  ? 6   PRO   A N    1 
ATOM   2    C CA   . PRO   A 1 21  ? 4.311   27.455  27.328  1.00 65.49  ? 6   PRO   A CA   1 
ATOM   3    C C    . PRO   A 1 21  ? 4.993   26.255  26.685  1.00 63.28  ? 6   PRO   A C    1 
ATOM   4    O O    . PRO   A 1 21  ? 5.531   26.369  25.586  1.00 63.21  ? 6   PRO   A O    1 
ATOM   5    C CB   . PRO   A 1 21  ? 4.223   28.626  26.349  1.00 71.00  ? 6   PRO   A CB   1 
ATOM   6    C CG   . PRO   A 1 21  ? 5.478   29.400  26.594  1.00 77.31  ? 6   PRO   A CG   1 
ATOM   7    C CD   . PRO   A 1 21  ? 5.753   29.274  28.071  1.00 76.58  ? 6   PRO   A CD   1 
ATOM   8    H HA   . PRO   A 1 21  ? 3.418   27.206  27.614  1.00 78.59  ? 6   PRO   A HA   1 
ATOM   9    H HB2  . PRO   A 1 21  ? 4.187   28.297  25.437  1.00 85.20  ? 6   PRO   A HB2  1 
ATOM   10   H HB3  . PRO   A 1 21  ? 3.437   29.162  26.539  1.00 85.20  ? 6   PRO   A HB3  1 
ATOM   11   H HG2  . PRO   A 1 21  ? 6.204   29.020  26.075  1.00 92.77  ? 6   PRO   A HG2  1 
ATOM   12   H HG3  . PRO   A 1 21  ? 5.344   30.328  26.347  1.00 92.77  ? 6   PRO   A HG3  1 
ATOM   13   H HD2  . PRO   A 1 21  ? 6.707   29.228  28.240  1.00 91.90  ? 6   PRO   A HD2  1 
ATOM   14   H HD3  . PRO   A 1 21  ? 5.365   30.018  28.558  1.00 91.90  ? 6   PRO   A HD3  1 
ATOM   15   N N    . ASP   A 1 22  ? 4.975   25.119  27.383  1.00 66.33  ? 7   ASP   A N    1 
ATOM   16   C CA   . ASP   A 1 22  ? 5.561   23.894  26.846  1.00 63.80  ? 7   ASP   A CA   1 
ATOM   17   C C    . ASP   A 1 22  ? 4.903   23.516  25.521  1.00 61.16  ? 7   ASP   A C    1 
ATOM   18   O O    . ASP   A 1 22  ? 5.563   23.442  24.478  1.00 57.96  ? 7   ASP   A O    1 
ATOM   19   C CB   . ASP   A 1 22  ? 5.411   22.774  27.879  1.00 71.86  ? 7   ASP   A CB   1 
ATOM   20   C CG   . ASP   A 1 22  ? 6.577   21.808  27.875  1.00 79.15  ? 7   ASP   A CG   1 
ATOM   21   O OD1  . ASP   A 1 22  ? 7.732   22.271  28.003  1.00 79.07  ? 7   ASP   A OD1  1 
ATOM   22   O OD2  . ASP   A 1 22  ? 6.334   20.585  27.769  1.00 78.14  ? 7   ASP   A OD2  1 
ATOM   23   H H    . ASP   A 1 22  ? 4.632   25.033  28.167  1.00 79.59  ? 7   ASP   A H    1 
ATOM   24   H HA   . ASP   A 1 22  ? 6.506   24.030  26.678  1.00 76.56  ? 7   ASP   A HA   1 
ATOM   25   H HB2  . ASP   A 1 22  ? 5.351   23.167  28.764  1.00 86.23  ? 7   ASP   A HB2  1 
ATOM   26   H HB3  . ASP   A 1 22  ? 4.605   22.271  27.684  1.00 86.23  ? 7   ASP   A HB3  1 
ATOM   27   N N    . ILE   A 1 23  ? 3.595   23.280  25.549  1.00 47.58  ? 8   ILE   A N    1 
ATOM   28   C CA   . ILE   A 1 23  ? 2.793   23.002  24.365  1.00 37.26  ? 8   ILE   A CA   1 
ATOM   29   C C    . ILE   A 1 23  ? 1.779   24.128  24.227  1.00 41.11  ? 8   ILE   A C    1 
ATOM   30   O O    . ILE   A 1 23  ? 1.207   24.578  25.224  1.00 39.77  ? 8   ILE   A O    1 
ATOM   31   C CB   . ILE   A 1 23  ? 2.080   21.638  24.467  1.00 38.14  ? 8   ILE   A CB   1 
ATOM   32   C CG1  . ILE   A 1 23  ? 3.102   20.505  24.623  1.00 47.55  ? 8   ILE   A CG1  1 
ATOM   33   C CG2  . ILE   A 1 23  ? 1.188   21.406  23.252  1.00 35.06  ? 8   ILE   A CG2  1 
ATOM   34   C CD1  . ILE   A 1 23  ? 2.483   19.160  24.996  1.00 39.06  ? 8   ILE   A CD1  1 
ATOM   35   H H    . ILE   A 1 23  ? 3.132   23.276  26.274  1.00 57.09  ? 8   ILE   A H    1 
ATOM   36   H HA   . ILE   A 1 23  ? 3.360   22.983  23.579  1.00 44.72  ? 8   ILE   A HA   1 
ATOM   37   H HB   . ILE   A 1 23  ? 1.519   21.648  25.258  1.00 45.76  ? 8   ILE   A HB   1 
ATOM   38   H HG12 . ILE   A 1 23  ? 3.571   20.391  23.782  1.00 57.06  ? 8   ILE   A HG12 1 
ATOM   39   H HG13 . ILE   A 1 23  ? 3.729   20.746  25.323  1.00 57.06  ? 8   ILE   A HG13 1 
ATOM   40   H HG21 . ILE   A 1 23  ? 0.858   20.494  23.272  1.00 42.07  ? 8   ILE   A HG21 1 
ATOM   41   H HG22 . ILE   A 1 23  ? 0.445   22.028  23.282  1.00 42.07  ? 8   ILE   A HG22 1 
ATOM   42   H HG23 . ILE   A 1 23  ? 1.708   21.552  22.446  1.00 42.07  ? 8   ILE   A HG23 1 
ATOM   43   H HD11 . ILE   A 1 23  ? 3.191   18.541  25.233  1.00 46.87  ? 8   ILE   A HD11 1 
ATOM   44   H HD12 . ILE   A 1 23  ? 1.887   19.285  25.752  1.00 46.87  ? 8   ILE   A HD12 1 
ATOM   45   H HD13 . ILE   A 1 23  ? 1.986   18.820  24.236  1.00 46.87  ? 8   ILE   A HD13 1 
ATOM   46   N N    . PHE   A 1 24  ? 1.562   24.590  22.998  1.00 40.40  ? 9   PHE   A N    1 
ATOM   47   C CA   . PHE   A 1 24  ? 0.642   25.695  22.764  1.00 38.47  ? 9   PHE   A CA   1 
ATOM   48   C C    . PHE   A 1 24  ? -0.800  25.207  22.826  1.00 38.28  ? 9   PHE   A C    1 
ATOM   49   O O    . PHE   A 1 24  ? -1.175  24.257  22.134  1.00 36.89  ? 9   PHE   A O    1 
ATOM   50   C CB   . PHE   A 1 24  ? 0.913   26.350  21.411  1.00 37.74  ? 9   PHE   A CB   1 
ATOM   51   C CG   . PHE   A 1 24  ? 2.155   27.194  21.380  1.00 38.43  ? 9   PHE   A CG   1 
ATOM   52   C CD1  . PHE   A 1 24  ? 2.386   28.146  22.357  1.00 43.60  ? 9   PHE   A CD1  1 
ATOM   53   C CD2  . PHE   A 1 24  ? 3.097   27.031  20.379  1.00 41.98  ? 9   PHE   A CD2  1 
ATOM   54   C CE1  . PHE   A 1 24  ? 3.530   28.920  22.333  1.00 49.14  ? 9   PHE   A CE1  1 
ATOM   55   C CE2  . PHE   A 1 24  ? 4.240   27.802  20.354  1.00 48.51  ? 9   PHE   A CE2  1 
ATOM   56   C CZ   . PHE   A 1 24  ? 4.454   28.748  21.334  1.00 40.09  ? 9   PHE   A CZ   1 
ATOM   57   H H    . PHE   A 1 24  ? 1.935   24.281  22.287  1.00 48.48  ? 9   PHE   A H    1 
ATOM   58   H HA   . PHE   A 1 24  ? 0.773   26.361  23.456  1.00 46.16  ? 9   PHE   A HA   1 
ATOM   59   H HB2  . PHE   A 1 24  ? 1.011   25.655  20.742  1.00 45.29  ? 9   PHE   A HB2  1 
ATOM   60   H HB3  . PHE   A 1 24  ? 0.162   26.922  21.186  1.00 45.29  ? 9   PHE   A HB3  1 
ATOM   61   H HD1  . PHE   A 1 24  ? 1.764   28.266  23.038  1.00 52.31  ? 9   PHE   A HD1  1 
ATOM   62   H HD2  . PHE   A 1 24  ? 2.957   26.393  19.717  1.00 50.38  ? 9   PHE   A HD2  1 
ATOM   63   H HE1  . PHE   A 1 24  ? 3.674   29.558  22.994  1.00 58.97  ? 9   PHE   A HE1  1 
ATOM   64   H HE2  . PHE   A 1 24  ? 4.866   27.684  19.676  1.00 58.21  ? 9   PHE   A HE2  1 
ATOM   65   H HZ   . PHE   A 1 24  ? 5.224   29.269  21.318  1.00 48.10  ? 9   PHE   A HZ   1 
ATOM   66   N N    . ASN   A 1 25  ? -1.603  25.864  23.665  1.00 39.95  ? 10  ASN   A N    1 
ATOM   67   C CA   . ASN   A 1 25  ? -3.050  25.657  23.697  1.00 40.83  ? 10  ASN   A CA   1 
ATOM   68   C C    . ASN   A 1 25  ? -3.707  26.494  22.596  1.00 43.79  ? 10  ASN   A C    1 
ATOM   69   O O    . ASN   A 1 25  ? -4.494  27.410  22.843  1.00 41.78  ? 10  ASN   A O    1 
ATOM   70   C CB   . ASN   A 1 25  ? -3.599  26.016  25.072  1.00 43.02  ? 10  ASN   A CB   1 
ATOM   71   C CG   . ASN   A 1 25  ? -5.090  25.775  25.186  1.00 42.69  ? 10  ASN   A CG   1 
ATOM   72   O OD1  . ASN   A 1 25  ? -5.617  24.802  24.646  1.00 41.68  ? 10  ASN   A OD1  1 
ATOM   73   N ND2  . ASN   A 1 25  ? -5.780  26.666  25.886  1.00 44.67  ? 10  ASN   A ND2  1 
ATOM   74   H H    . ASN   A 1 25  ? -1.327  26.445  24.236  1.00 47.94  ? 10  ASN   A H    1 
ATOM   75   H HA   . ASN   A 1 25  ? -3.247  24.721  23.536  1.00 48.99  ? 10  ASN   A HA   1 
ATOM   76   H HB2  . ASN   A 1 25  ? -3.155  25.473  25.742  1.00 51.62  ? 10  ASN   A HB2  1 
ATOM   77   H HB3  . ASN   A 1 25  ? -3.433  26.956  25.244  1.00 51.62  ? 10  ASN   A HB3  1 
ATOM   78   H HD21 . ASN   A 1 25  ? -6.630  26.574  25.980  1.00 53.60  ? 10  ASN   A HD21 1 
ATOM   79   H HD22 . ASN   A 1 25  ? -5.377  27.336  26.245  1.00 53.60  ? 10  ASN   A HD22 1 
ATOM   80   N N    . ARG   A 1 26  ? -3.349  26.157  21.357  1.00 42.47  ? 11  ARG   A N    1 
ATOM   81   C CA   . ARG   A 1 26  ? -3.711  26.930  20.182  1.00 41.51  ? 11  ARG   A CA   1 
ATOM   82   C C    . ARG   A 1 26  ? -3.877  26.003  18.988  1.00 41.13  ? 11  ARG   A C    1 
ATOM   83   O O    . ARG   A 1 26  ? -3.166  25.003  18.859  1.00 35.77  ? 11  ARG   A O    1 
ATOM   84   C CB   . ARG   A 1 26  ? -2.640  27.961  19.815  1.00 47.53  ? 11  ARG   A CB   1 
ATOM   85   C CG   . ARG   A 1 26  ? -2.733  29.282  20.524  1.00 56.84  ? 11  ARG   A CG   1 
ATOM   86   C CD   . ARG   A 1 26  ? -1.709  30.248  19.952  1.00 60.57  ? 11  ARG   A CD   1 
ATOM   87   N NE   . ARG   A 1 26  ? -2.219  31.613  19.892  1.00 73.83  ? 11  ARG   A NE   1 
ATOM   88   C CZ   . ARG   A 1 26  ? -3.051  32.059  18.960  1.00 66.16  ? 11  ARG   A CZ   1 
ATOM   89   N NH1  . ARG   A 1 26  ? -3.506  31.266  18.002  1.00 66.55  ? 11  ARG   A NH1  1 
ATOM   90   N NH2  . ARG   A 1 26  ? -3.441  33.330  18.993  1.00 70.03  ? 11  ARG   A NH2  1 
ATOM   91   H H    . ARG   A 1 26  ? -2.881  25.460  21.170  1.00 50.96  ? 11  ARG   A H    1 
ATOM   92   H HA   . ARG   A 1 26  ? -4.550  27.377  20.373  1.00 49.81  ? 11  ARG   A HA   1 
ATOM   93   H HB2  . ARG   A 1 26  ? -1.771  27.584  20.023  1.00 57.03  ? 11  ARG   A HB2  1 
ATOM   94   H HB3  . ARG   A 1 26  ? -2.705  28.141  18.864  1.00 57.03  ? 11  ARG   A HB3  1 
ATOM   95   H HG2  . ARG   A 1 26  ? -3.619  29.658  20.401  1.00 68.20  ? 11  ARG   A HG2  1 
ATOM   96   H HG3  . ARG   A 1 26  ? -2.553  29.160  21.469  1.00 68.20  ? 11  ARG   A HG3  1 
ATOM   97   H HD2  . ARG   A 1 26  ? -0.918  30.244  20.514  1.00 72.68  ? 11  ARG   A HD2  1 
ATOM   98   H HD3  . ARG   A 1 26  ? -1.477  29.971  19.052  1.00 72.68  ? 11  ARG   A HD3  1 
ATOM   99   H HE   . ARG   A 1 26  ? -1.964  32.164  20.500  1.00 88.59  ? 11  ARG   A HE   1 
ATOM   100  H HH11 . ARG   A 1 26  ? -3.262  30.441  17.975  1.00 79.86  ? 11  ARG   A HH11 1 
ATOM   101  H HH12 . ARG   A 1 26  ? -4.045  31.575  17.408  1.00 79.86  ? 11  ARG   A HH12 1 
ATOM   102  H HH21 . ARG   A 1 26  ? -3.154  33.851  19.614  1.00 84.04  ? 11  ARG   A HH21 1 
ATOM   103  H HH22 . ARG   A 1 26  ? -3.981  33.630  18.395  1.00 84.04  ? 11  ARG   A HH22 1 
ATOM   104  N N    . ASP   A 1 27  ? -4.786  26.374  18.104  1.00 38.87  ? 12  ASP   A N    1 
ATOM   105  C CA   . ASP   A 1 27  ? -4.882  25.728  16.800  1.00 41.26  ? 12  ASP   A CA   1 
ATOM   106  C C    . ASP   A 1 27  ? -3.725  26.191  15.919  1.00 37.15  ? 12  ASP   A C    1 
ATOM   107  O O    . ASP   A 1 27  ? -3.614  27.394  15.644  1.00 37.02  ? 12  ASP   A O    1 
ATOM   108  C CB   . ASP   A 1 27  ? -6.220  26.080  16.157  1.00 49.22  ? 12  ASP   A CB   1 
ATOM   109  C CG   . ASP   A 1 27  ? -6.428  25.392  14.825  1.00 45.80  ? 12  ASP   A CG   1 
ATOM   110  O OD1  . ASP   A 1 27  ? -5.536  24.636  14.398  1.00 42.49  ? 12  ASP   A OD1  1 
ATOM   111  O OD2  . ASP   A 1 27  ? -7.492  25.611  14.209  1.00 54.59  ? 12  ASP   A OD2  1 
ATOM   112  H H    . ASP   A 1 27  ? -5.363  26.999  18.231  1.00 46.64  ? 12  ASP   A H    1 
ATOM   113  H HA   . ASP   A 1 27  ? -4.831  24.765  16.896  1.00 49.51  ? 12  ASP   A HA   1 
ATOM   114  H HB2  . ASP   A 1 27  ? -6.938  25.806  16.751  1.00 59.07  ? 12  ASP   A HB2  1 
ATOM   115  H HB3  . ASP   A 1 27  ? -6.259  27.037  16.010  1.00 59.07  ? 12  ASP   A HB3  1 
ATOM   116  N N    . PRO   A 1 28  ? -2.850  25.294  15.452  1.00 34.57  ? 13  PRO   A N    1 
ATOM   117  C CA   . PRO   A 1 28  ? -1.729  25.755  14.614  1.00 37.31  ? 13  PRO   A CA   1 
ATOM   118  C C    . PRO   A 1 28  ? -2.171  26.446  13.339  1.00 33.84  ? 13  PRO   A C    1 
ATOM   119  O O    . PRO   A 1 28  ? -1.413  27.254  12.789  1.00 34.04  ? 13  PRO   A O    1 
ATOM   120  C CB   . PRO   A 1 28  ? -0.961  24.460  14.309  1.00 32.10  ? 13  PRO   A CB   1 
ATOM   121  C CG   . PRO   A 1 28  ? -1.963  23.393  14.448  1.00 32.19  ? 13  PRO   A CG   1 
ATOM   122  C CD   . PRO   A 1 28  ? -2.872  23.826  15.566  1.00 33.94  ? 13  PRO   A CD   1 
ATOM   123  H HA   . PRO   A 1 28  ? -1.164  26.355  15.126  1.00 44.78  ? 13  PRO   A HA   1 
ATOM   124  H HB2  . PRO   A 1 28  ? -0.606  24.490  13.406  1.00 38.52  ? 13  PRO   A HB2  1 
ATOM   125  H HB3  . PRO   A 1 28  ? -0.238  24.346  14.945  1.00 38.52  ? 13  PRO   A HB3  1 
ATOM   126  H HG2  . PRO   A 1 28  ? -2.458  23.299  13.620  1.00 38.63  ? 13  PRO   A HG2  1 
ATOM   127  H HG3  . PRO   A 1 28  ? -1.522  22.557  14.668  1.00 38.63  ? 13  PRO   A HG3  1 
ATOM   128  H HD2  . PRO   A 1 28  ? -3.770  23.481  15.437  1.00 40.72  ? 13  PRO   A HD2  1 
ATOM   129  H HD3  . PRO   A 1 28  ? -2.527  23.539  16.426  1.00 40.72  ? 13  PRO   A HD3  1 
ATOM   130  N N    . ARG   A 1 29  ? -3.370  26.134  12.844  1.00 34.03  ? 14  ARG   A N    1 
ATOM   131  C CA   . ARG   A 1 29  ? -3.905  26.797  11.664  1.00 36.17  ? 14  ARG   A CA   1 
ATOM   132  C C    . ARG   A 1 29  ? -4.093  28.293  11.880  1.00 36.35  ? 14  ARG   A C    1 
ATOM   133  O O    . ARG   A 1 29  ? -4.294  29.024  10.906  1.00 37.44  ? 14  ARG   A O    1 
ATOM   134  C CB   . ARG   A 1 29  ? -5.246  26.179  11.269  1.00 43.17  ? 14  ARG   A CB   1 
ATOM   135  C CG   . ARG   A 1 29  ? -5.205  24.685  11.001  1.00 52.83  ? 14  ARG   A CG   1 
ATOM   136  C CD   . ARG   A 1 29  ? -5.457  24.367  9.536   1.00 54.54  ? 14  ARG   A CD   1 
ATOM   137  N NE   . ARG   A 1 29  ? -6.341  23.218  9.370   1.00 68.15  ? 14  ARG   A NE   1 
ATOM   138  C CZ   . ARG   A 1 29  ? -6.856  22.835  8.209   1.00 65.80  ? 14  ARG   A CZ   1 
ATOM   139  N NH1  . ARG   A 1 29  ? -6.596  23.490  7.088   1.00 58.13  ? 14  ARG   A NH1  1 
ATOM   140  N NH2  . ARG   A 1 29  ? -7.651  21.769  8.171   1.00 61.14  ? 14  ARG   A NH2  1 
ATOM   141  H H    . ARG   A 1 29  ? -3.894  25.539  13.178  1.00 40.83  ? 14  ARG   A H    1 
ATOM   142  H HA   . ARG   A 1 29  ? -3.285  26.663  10.930  1.00 43.40  ? 14  ARG   A HA   1 
ATOM   143  H HB2  . ARG   A 1 29  ? -5.878  26.329  11.989  1.00 51.80  ? 14  ARG   A HB2  1 
ATOM   144  H HB3  . ARG   A 1 29  ? -5.558  26.612  10.459  1.00 51.80  ? 14  ARG   A HB3  1 
ATOM   145  H HG2  . ARG   A 1 29  ? -4.330  24.341  11.240  1.00 63.39  ? 14  ARG   A HG2  1 
ATOM   146  H HG3  . ARG   A 1 29  ? -5.889  24.246  11.529  1.00 63.39  ? 14  ARG   A HG3  1 
ATOM   147  H HD2  . ARG   A 1 29  ? -5.872  25.133  9.110   1.00 65.45  ? 14  ARG   A HD2  1 
ATOM   148  H HD3  . ARG   A 1 29  ? -4.613  24.164  9.104   1.00 65.45  ? 14  ARG   A HD3  1 
ATOM   149  H HE   . ARG   A 1 29  ? -6.542  22.760  10.070  1.00 81.78  ? 14  ARG   A HE   1 
ATOM   150  H HH11 . ARG   A 1 29  ? -6.083  24.180  7.102   1.00 69.76  ? 14  ARG   A HH11 1 
ATOM   151  H HH12 . ARG   A 1 29  ? -6.940  23.225  6.345   1.00 69.76  ? 14  ARG   A HH12 1 
ATOM   152  H HH21 . ARG   A 1 29  ? -7.826  21.337  8.894   1.00 73.37  ? 14  ARG   A HH21 1 
ATOM   153  H HH22 . ARG   A 1 29  ? -7.990  21.512  7.424   1.00 73.37  ? 14  ARG   A HH22 1 
ATOM   154  N N    . ASP   A 1 30  ? -4.055  28.757  13.128  1.00 38.16  ? 15  ASP   A N    1 
ATOM   155  C CA   . ASP   A 1 30  ? -4.040  30.192  13.377  1.00 40.78  ? 15  ASP   A CA   1 
ATOM   156  C C    . ASP   A 1 30  ? -2.728  30.828  12.935  1.00 43.84  ? 15  ASP   A C    1 
ATOM   157  O O    . ASP   A 1 30  ? -2.700  32.020  12.606  1.00 42.63  ? 15  ASP   A O    1 
ATOM   158  C CB   . ASP   A 1 30  ? -4.270  30.469  14.859  1.00 49.72  ? 15  ASP   A CB   1 
ATOM   159  C CG   . ASP   A 1 30  ? -5.619  29.993  15.331  1.00 55.06  ? 15  ASP   A CG   1 
ATOM   160  O OD1  . ASP   A 1 30  ? -6.528  29.865  14.484  1.00 61.62  ? 15  ASP   A OD1  1 
ATOM   161  O OD2  . ASP   A 1 30  ? -5.766  29.753  16.547  1.00 56.74  ? 15  ASP   A OD2  1 
ATOM   162  H H    . ASP   A 1 30  ? -4.037  28.269  13.836  1.00 45.79  ? 15  ASP   A H    1 
ATOM   163  H HA   . ASP   A 1 30  ? -4.762  30.599  12.872  1.00 48.94  ? 15  ASP   A HA   1 
ATOM   164  H HB2  . ASP   A 1 30  ? -3.590  30.010  15.377  1.00 59.67  ? 15  ASP   A HB2  1 
ATOM   165  H HB3  . ASP   A 1 30  ? -4.217  31.425  15.016  1.00 59.67  ? 15  ASP   A HB3  1 
ATOM   166  N N    . HIS   A 1 31  ? -1.635  30.056  12.935  1.00 36.91  ? 16  HIS   A N    1 
ATOM   167  C CA   . HIS   A 1 31  ? -0.320  30.556  12.568  1.00 36.99  ? 16  HIS   A CA   1 
ATOM   168  C C    . HIS   A 1 31  ? 0.175   30.064  11.213  1.00 36.96  ? 16  HIS   A C    1 
ATOM   169  O O    . HIS   A 1 31  ? 1.046   30.711  10.628  1.00 38.94  ? 16  HIS   A O    1 
ATOM   170  C CB   . HIS   A 1 31  ? 0.722   30.150  13.622  1.00 39.61  ? 16  HIS   A CB   1 
ATOM   171  C CG   . HIS   A 1 31  ? 0.524   30.788  14.958  1.00 44.40  ? 16  HIS   A CG   1 
ATOM   172  N ND1  . HIS   A 1 31  ? 1.295   30.463  16.053  1.00 52.65  ? 16  HIS   A ND1  1 
ATOM   173  C CD2  . HIS   A 1 31  ? -0.350  31.732  15.380  1.00 52.69  ? 16  HIS   A CD2  1 
ATOM   174  C CE1  . HIS   A 1 31  ? 0.903   31.178  17.093  1.00 56.42  ? 16  HIS   A CE1  1 
ATOM   175  N NE2  . HIS   A 1 31  ? -0.094  31.956  16.712  1.00 51.70  ? 16  HIS   A NE2  1 
ATOM   176  H H    . HIS   A 1 31  ? -1.637  29.223  13.150  1.00 44.30  ? 16  HIS   A H    1 
ATOM   177  H HA   . HIS   A 1 31  ? -0.367  31.524  12.539  1.00 44.39  ? 16  HIS   A HA   1 
ATOM   178  H HB2  . HIS   A 1 31  ? 0.680   29.189  13.746  1.00 47.53  ? 16  HIS   A HB2  1 
ATOM   179  H HB3  . HIS   A 1 31  ? 1.602   30.405  13.302  1.00 47.53  ? 16  HIS   A HB3  1 
ATOM   180  H HD2  . HIS   A 1 31  ? -1.002  32.150  14.865  1.00 63.23  ? 16  HIS   A HD2  1 
ATOM   181  H HE1  . HIS   A 1 31  ? 1.268   31.140  17.948  1.00 67.71  ? 16  HIS   A HE1  1 
ATOM   182  H HE2  . HIS   A 1 31  ? -0.515  32.512  17.215  1.00 62.04  ? 16  HIS   A HE2  1 
ATOM   183  N N    . TYR   A 1 32  ? -0.345  28.949  10.705  1.00 34.62  ? 17  TYR   A N    1 
ATOM   184  C CA   . TYR   A 1 32  ? 0.185   28.332  9.498   1.00 33.62  ? 17  TYR   A CA   1 
ATOM   185  C C    . TYR   A 1 32  ? -0.933  28.015  8.519   1.00 33.68  ? 17  TYR   A C    1 
ATOM   186  O O    . TYR   A 1 32  ? -2.066  27.732  8.912   1.00 33.99  ? 17  TYR   A O    1 
ATOM   187  C CB   . TYR   A 1 32  ? 0.958   27.051  9.825   1.00 32.28  ? 17  TYR   A CB   1 
ATOM   188  C CG   . TYR   A 1 32  ? 2.135   27.277  10.733  1.00 32.33  ? 17  TYR   A CG   1 
ATOM   189  C CD1  . TYR   A 1 32  ? 3.358   27.690  10.226  1.00 32.33  ? 17  TYR   A CD1  1 
ATOM   190  C CD2  . TYR   A 1 32  ? 2.026   27.084  12.095  1.00 32.56  ? 17  TYR   A CD2  1 
ATOM   191  C CE1  . TYR   A 1 32  ? 4.432   27.901  11.051  1.00 32.59  ? 17  TYR   A CE1  1 
ATOM   192  C CE2  . TYR   A 1 32  ? 3.097   27.294  12.927  1.00 36.59  ? 17  TYR   A CE2  1 
ATOM   193  C CZ   . TYR   A 1 32  ? 4.295   27.705  12.400  1.00 32.88  ? 17  TYR   A CZ   1 
ATOM   194  O OH   . TYR   A 1 32  ? 5.360   27.917  13.235  1.00 42.08  ? 17  TYR   A OH   1 
ATOM   195  H H    . TYR   A 1 32  ? -1.012  28.528  11.047  1.00 41.54  ? 17  TYR   A H    1 
ATOM   196  H HA   . TYR   A 1 32  ? 0.783   28.959  9.062   1.00 40.34  ? 17  TYR   A HA   1 
ATOM   197  H HB2  . TYR   A 1 32  ? 0.359   26.427  10.265  1.00 38.74  ? 17  TYR   A HB2  1 
ATOM   198  H HB3  . TYR   A 1 32  ? 1.290   26.665  8.999   1.00 38.74  ? 17  TYR   A HB3  1 
ATOM   199  H HD1  . TYR   A 1 32  ? 3.452   27.825  9.310   1.00 38.79  ? 17  TYR   A HD1  1 
ATOM   200  H HD2  . TYR   A 1 32  ? 1.214   26.807  12.454  1.00 39.08  ? 17  TYR   A HD2  1 
ATOM   201  H HE1  . TYR   A 1 32  ? 5.247   28.175  10.698  1.00 39.11  ? 17  TYR   A HE1  1 
ATOM   202  H HE2  . TYR   A 1 32  ? 3.011   27.158  13.843  1.00 43.91  ? 17  TYR   A HE2  1 
ATOM   203  H HH   . TYR   A 1 32  ? 6.079   27.764  12.828  1.00 50.49  ? 17  TYR   A HH   1 
ATOM   204  N N    . ASP   A 1 33  ? -0.598  28.089  7.233   1.00 36.84  ? 18  ASP   A N    1 
ATOM   205  C CA   . ASP   A 1 33  ? -1.452  27.608  6.154   1.00 38.47  ? 18  ASP   A CA   1 
ATOM   206  C C    . ASP   A 1 33  ? -0.930  26.250  5.704   1.00 34.27  ? 18  ASP   A C    1 
ATOM   207  O O    . ASP   A 1 33  ? 0.225   26.145  5.276   1.00 31.87  ? 18  ASP   A O    1 
ATOM   208  C CB   . ASP   A 1 33  ? -1.445  28.583  4.978   1.00 34.57  ? 18  ASP   A CB   1 
ATOM   209  C CG   . ASP   A 1 33  ? -2.021  29.927  5.338   1.00 42.92  ? 18  ASP   A CG   1 
ATOM   210  O OD1  . ASP   A 1 33  ? -3.189  29.970  5.777   1.00 46.58  ? 18  ASP   A OD1  1 
ATOM   211  O OD2  . ASP   A 1 33  ? -1.299  30.937  5.198   1.00 45.06  ? 18  ASP   A OD2  1 
ATOM   212  H H    . ASP   A 1 33  ? 0.143   28.424  6.954   1.00 44.21  ? 18  ASP   A H    1 
ATOM   213  H HA   . ASP   A 1 33  ? -2.363  27.517  6.473   1.00 46.16  ? 18  ASP   A HA   1 
ATOM   214  H HB2  . ASP   A 1 33  ? -0.531  28.716  4.682   1.00 41.49  ? 18  ASP   A HB2  1 
ATOM   215  H HB3  . ASP   A 1 33  ? -1.977  28.212  4.256   1.00 41.49  ? 18  ASP   A HB3  1 
ATOM   216  N N    . LEU   A 1 34  ? -1.770  25.220  5.806   1.00 36.91  ? 19  LEU   A N    1 
ATOM   217  C CA   . LEU   A 1 34  ? -1.409  23.894  5.318   1.00 35.95  ? 19  LEU   A CA   1 
ATOM   218  C C    . LEU   A 1 34  ? -1.409  23.893  3.795   1.00 31.67  ? 19  LEU   A C    1 
ATOM   219  O O    . LEU   A 1 34  ? -2.421  24.214  3.168   1.00 33.37  ? 19  LEU   A O    1 
ATOM   220  C CB   . LEU   A 1 34  ? -2.384  22.842  5.842   1.00 33.09  ? 19  LEU   A CB   1 
ATOM   221  C CG   . LEU   A 1 34  ? -2.475  22.639  7.355   1.00 40.34  ? 19  LEU   A CG   1 
ATOM   222  C CD1  . LEU   A 1 34  ? -3.309  21.401  7.657   1.00 38.08  ? 19  LEU   A CD1  1 
ATOM   223  C CD2  . LEU   A 1 34  ? -1.106  22.519  7.991   1.00 37.33  ? 19  LEU   A CD2  1 
ATOM   224  H H    . LEU   A 1 34  ? -2.555  25.265  6.155   1.00 44.29  ? 19  LEU   A H    1 
ATOM   225  H HA   . LEU   A 1 34  ? -0.521  23.670  5.638   1.00 43.14  ? 19  LEU   A HA   1 
ATOM   226  H HB2  . LEU   A 1 34  ? -3.272  23.086  5.540   1.00 39.71  ? 19  LEU   A HB2  1 
ATOM   227  H HB3  . LEU   A 1 34  ? -2.127  21.987  5.462   1.00 39.71  ? 19  LEU   A HB3  1 
ATOM   228  H HG   . LEU   A 1 34  ? -2.902  23.417  7.746   1.00 48.41  ? 19  LEU   A HG   1 
ATOM   229  H HD11 . LEU   A 1 34  ? -3.373  21.290  8.618   1.00 45.70  ? 19  LEU   A HD11 1 
ATOM   230  H HD12 . LEU   A 1 34  ? -4.194  21.516  7.278   1.00 45.70  ? 19  LEU   A HD12 1 
ATOM   231  H HD13 . LEU   A 1 34  ? -2.879  20.626  7.262   1.00 45.70  ? 19  LEU   A HD13 1 
ATOM   232  H HD21 . LEU   A 1 34  ? -1.211  22.273  8.923   1.00 44.79  ? 19  LEU   A HD21 1 
ATOM   233  H HD22 . LEU   A 1 34  ? -0.599  21.836  7.524   1.00 44.79  ? 19  LEU   A HD22 1 
ATOM   234  H HD23 . LEU   A 1 34  ? -0.650  23.373  7.924   1.00 44.79  ? 19  LEU   A HD23 1 
ATOM   235  N N    . LEU   A 1 35  ? -0.288  23.513  3.197   1.00 31.07  ? 20  LEU   A N    1 
ATOM   236  C CA   . LEU   A 1 35  ? -0.158  23.525  1.745   1.00 38.03  ? 20  LEU   A CA   1 
ATOM   237  C C    . LEU   A 1 35  ? -0.359  22.157  1.119   1.00 36.84  ? 20  LEU   A C    1 
ATOM   238  O O    . LEU   A 1 35  ? -0.950  22.057  0.041   1.00 38.83  ? 20  LEU   A O    1 
ATOM   239  C CB   . LEU   A 1 35  ? 1.217   24.057  1.335   1.00 35.11  ? 20  LEU   A CB   1 
ATOM   240  C CG   . LEU   A 1 35  ? 1.517   25.517  1.694   1.00 42.60  ? 20  LEU   A CG   1 
ATOM   241  C CD1  . LEU   A 1 35  ? 2.853   25.938  1.096   1.00 31.88  ? 20  LEU   A CD1  1 
ATOM   242  C CD2  . LEU   A 1 35  ? 0.401   26.438  1.234   1.00 37.42  ? 20  LEU   A CD2  1 
ATOM   243  H H    . LEU   A 1 35  ? 0.416   23.243  3.613   1.00 37.29  ? 20  LEU   A H    1 
ATOM   244  H HA   . LEU   A 1 35  ? -0.832  24.123  1.386   1.00 45.64  ? 20  LEU   A HA   1 
ATOM   245  H HB2  . LEU   A 1 35  ? 1.892   23.512  1.769   1.00 42.13  ? 20  LEU   A HB2  1 
ATOM   246  H HB3  . LEU   A 1 35  ? 1.295   23.978  0.372   1.00 42.13  ? 20  LEU   A HB3  1 
ATOM   247  H HG   . LEU   A 1 35  ? 1.575   25.599  2.659   1.00 51.12  ? 20  LEU   A HG   1 
ATOM   248  H HD11 . LEU   A 1 35  ? 3.029   26.861  1.334   1.00 38.26  ? 20  LEU   A HD11 1 
ATOM   249  H HD12 . LEU   A 1 35  ? 3.551   25.366  1.450   1.00 38.26  ? 20  LEU   A HD12 1 
ATOM   250  H HD13 . LEU   A 1 35  ? 2.809   25.848  0.131   1.00 38.26  ? 20  LEU   A HD13 1 
ATOM   251  H HD21 . LEU   A 1 35  ? 0.703   27.358  1.299   1.00 44.90  ? 20  LEU   A HD21 1 
ATOM   252  H HD22 . LEU   A 1 35  ? 0.177   26.228  0.314   1.00 44.90  ? 20  LEU   A HD22 1 
ATOM   253  H HD23 . LEU   A 1 35  ? -0.374  26.304  1.803   1.00 44.90  ? 20  LEU   A HD23 1 
ATOM   254  N N    . GLN   A 1 36  ? 0.097   21.097  1.780   1.00 40.42  ? 21  GLN   A N    1 
ATOM   255  C CA   . GLN   A 1 36  ? 0.221   19.809  1.115   1.00 35.23  ? 21  GLN   A CA   1 
ATOM   256  C C    . GLN   A 1 36  ? 0.467   18.732  2.157   1.00 31.23  ? 21  GLN   A C    1 
ATOM   257  O O    . GLN   A 1 36  ? 1.259   18.927  3.079   1.00 28.72  ? 21  GLN   A O    1 
ATOM   258  C CB   . GLN   A 1 36  ? 1.374   19.859  0.104   1.00 35.90  ? 21  GLN   A CB   1 
ATOM   259  C CG   . GLN   A 1 36  ? 1.464   18.713  -0.864  1.00 49.46  ? 21  GLN   A CG   1 
ATOM   260  C CD   . GLN   A 1 36  ? 2.607   18.898  -1.862  1.00 56.99  ? 21  GLN   A CD   1 
ATOM   261  O OE1  . GLN   A 1 36  ? 3.778   18.989  -1.486  1.00 51.85  ? 21  GLN   A OE1  1 
ATOM   262  N NE2  . GLN   A 1 36  ? 2.263   18.975  -3.140  1.00 69.94  ? 21  GLN   A NE2  1 
ATOM   263  H H    . GLN   A 1 36  ? 0.339   21.101  2.606   1.00 48.50  ? 21  GLN   A H    1 
ATOM   264  H HA   . GLN   A 1 36  ? -0.601  19.582  0.653   1.00 42.28  ? 21  GLN   A HA   1 
ATOM   265  H HB2  . GLN   A 1 36  ? 1.278   20.669  -0.421  1.00 43.07  ? 21  GLN   A HB2  1 
ATOM   266  H HB3  . GLN   A 1 36  ? 2.208   19.881  0.599   1.00 43.07  ? 21  GLN   A HB3  1 
ATOM   267  H HG2  . GLN   A 1 36  ? 1.621   17.891  -0.372  1.00 59.35  ? 21  GLN   A HG2  1 
ATOM   268  H HG3  . GLN   A 1 36  ? 0.634   18.648  -1.361  1.00 59.35  ? 21  GLN   A HG3  1 
ATOM   269  H HE21 . GLN   A 1 36  ? 1.435   18.921  -3.367  1.00 83.93  ? 21  GLN   A HE21 1 
ATOM   270  H HE22 . GLN   A 1 36  ? 2.868   19.079  -3.743  1.00 83.93  ? 21  GLN   A HE22 1 
ATOM   271  N N    . ARG   A 1 37  ? -0.226  17.608  2.011   1.00 31.80  ? 22  ARG   A N    1 
ATOM   272  C CA   . ARG   A 1 37  ? 0.072   16.423  2.804   1.00 33.20  ? 22  ARG   A CA   1 
ATOM   273  C C    . ARG   A 1 37  ? 1.255   15.698  2.177   1.00 28.78  ? 22  ARG   A C    1 
ATOM   274  O O    . ARG   A 1 37  ? 1.164   15.243  1.038   1.00 30.75  ? 22  ARG   A O    1 
ATOM   275  C CB   . ARG   A 1 37  ? -1.140  15.500  2.873   1.00 35.82  ? 22  ARG   A CB   1 
ATOM   276  C CG   . ARG   A 1 37  ? -0.978  14.307  3.816   1.00 31.83  ? 22  ARG   A CG   1 
ATOM   277  C CD   . ARG   A 1 37  ? -2.263  13.503  3.820   1.00 32.42  ? 22  ARG   A CD   1 
ATOM   278  N NE   . ARG   A 1 37  ? -2.278  12.394  4.765   1.00 43.10  ? 22  ARG   A NE   1 
ATOM   279  C CZ   . ARG   A 1 37  ? -1.878  11.164  4.482   1.00 41.26  ? 22  ARG   A CZ   1 
ATOM   280  N NH1  . ARG   A 1 37  ? -1.357  10.859  3.304   1.00 39.08  ? 22  ARG   A NH1  1 
ATOM   281  N NH2  . ARG   A 1 37  ? -1.995  10.219  5.411   1.00 39.13  ? 22  ARG   A NH2  1 
ATOM   282  H H    . ARG   A 1 37  ? -0.876  17.507  1.457   1.00 38.15  ? 22  ARG   A H    1 
ATOM   283  H HA   . ARG   A 1 37  ? 0.299   16.687  3.710   1.00 39.84  ? 22  ARG   A HA   1 
ATOM   284  H HB2  . ARG   A 1 37  ? -1.903  16.014  3.180   1.00 42.99  ? 22  ARG   A HB2  1 
ATOM   285  H HB3  . ARG   A 1 37  ? -1.312  15.149  1.985   1.00 42.99  ? 22  ARG   A HB3  1 
ATOM   286  H HG2  . ARG   A 1 37  ? -0.252  13.740  3.511   1.00 38.19  ? 22  ARG   A HG2  1 
ATOM   287  H HG3  . ARG   A 1 37  ? -0.799  14.619  4.717   1.00 38.19  ? 22  ARG   A HG3  1 
ATOM   288  H HD2  . ARG   A 1 37  ? -2.997  14.094  4.050   1.00 38.90  ? 22  ARG   A HD2  1 
ATOM   289  H HD3  . ARG   A 1 37  ? -2.399  13.133  2.934   1.00 38.90  ? 22  ARG   A HD3  1 
ATOM   290  H HE   . ARG   A 1 37  ? -2.566  12.549  5.561   1.00 51.72  ? 22  ARG   A HE   1 
ATOM   291  H HH11 . ARG   A 1 37  ? -1.272  11.467  2.701   1.00 46.90  ? 22  ARG   A HH11 1 
ATOM   292  H HH12 . ARG   A 1 37  ? -1.104  10.054  3.141   1.00 46.90  ? 22  ARG   A HH12 1 
ATOM   293  H HH21 . ARG   A 1 37  ? -2.326  10.411  6.181   1.00 46.96  ? 22  ARG   A HH21 1 
ATOM   294  H HH22 . ARG   A 1 37  ? -1.739  9.416   5.241   1.00 46.96  ? 22  ARG   A HH22 1 
ATOM   295  N N    . LEU   A 1 38  ? 2.358   15.597  2.914   1.00 27.89  ? 23  LEU   A N    1 
ATOM   296  C CA   . LEU   A 1 38  ? 3.578   14.994  2.397   1.00 27.64  ? 23  LEU   A CA   1 
ATOM   297  C C    . LEU   A 1 38  ? 3.620   13.484  2.590   1.00 29.40  ? 23  LEU   A C    1 
ATOM   298  O O    . LEU   A 1 38  ? 4.271   12.786  1.811   1.00 27.88  ? 23  LEU   A O    1 
ATOM   299  C CB   . LEU   A 1 38  ? 4.799   15.608  3.078   1.00 26.91  ? 23  LEU   A CB   1 
ATOM   300  C CG   . LEU   A 1 38  ? 4.974   17.112  2.886   1.00 27.95  ? 23  LEU   A CG   1 
ATOM   301  C CD1  . LEU   A 1 38  ? 6.188   17.586  3.642   1.00 32.32  ? 23  LEU   A CD1  1 
ATOM   302  C CD2  . LEU   A 1 38  ? 5.085   17.454  1.423   1.00 28.41  ? 23  LEU   A CD2  1 
ATOM   303  H H    . LEU   A 1 38  ? 2.424   15.874  3.726   1.00 33.46  ? 23  LEU   A H    1 
ATOM   304  H HA   . LEU   A 1 38  ? 3.631   15.180  1.446   1.00 33.16  ? 23  LEU   A HA   1 
ATOM   305  H HB2  . LEU   A 1 38  ? 4.730   15.445  4.032   1.00 32.29  ? 23  LEU   A HB2  1 
ATOM   306  H HB3  . LEU   A 1 38  ? 5.594   15.177  2.725   1.00 32.29  ? 23  LEU   A HB3  1 
ATOM   307  H HG   . LEU   A 1 38  ? 4.196   17.574  3.235   1.00 33.54  ? 23  LEU   A HG   1 
ATOM   308  H HD11 . LEU   A 1 38  ? 6.278   18.545  3.525   1.00 38.78  ? 23  LEU   A HD11 1 
ATOM   309  H HD12 . LEU   A 1 38  ? 6.076   17.377  4.582   1.00 38.78  ? 23  LEU   A HD12 1 
ATOM   310  H HD13 . LEU   A 1 38  ? 6.973   17.135  3.294   1.00 38.78  ? 23  LEU   A HD13 1 
ATOM   311  H HD21 . LEU   A 1 38  ? 5.369   18.378  1.336   1.00 34.10  ? 23  LEU   A HD21 1 
ATOM   312  H HD22 . LEU   A 1 38  ? 5.737   16.867  1.010   1.00 34.10  ? 23  LEU   A HD22 1 
ATOM   313  H HD23 . LEU   A 1 38  ? 4.219   17.333  1.004   1.00 34.10  ? 23  LEU   A HD23 1 
ATOM   314  N N    . GLY   A 1 39  ? 2.968   12.976  3.622   1.00 32.20  ? 24  GLY   A N    1 
ATOM   315  C CA   . GLY   A 1 39  ? 2.975   11.553  3.884   1.00 33.06  ? 24  GLY   A CA   1 
ATOM   316  C C    . GLY   A 1 39  ? 2.218   11.285  5.162   1.00 35.77  ? 24  GLY   A C    1 
ATOM   317  O O    . GLY   A 1 39  ? 1.839   12.207  5.896   1.00 28.12  ? 24  GLY   A O    1 
ATOM   318  H H    . GLY   A 1 39  ? 2.511   13.437  4.187   1.00 38.64  ? 24  GLY   A H    1 
ATOM   319  H HA2  . GLY   A 1 39  ? 2.549   11.076  3.155   1.00 39.67  ? 24  GLY   A HA2  1 
ATOM   320  H HA3  . GLY   A 1 39  ? 3.886   11.235  3.980   1.00 39.67  ? 24  GLY   A HA3  1 
ATOM   321  N N    . GLY   A 1 40  ? 2.010   10.005  5.418   1.00 32.07  ? 25  GLY   A N    1 
ATOM   322  C CA   . GLY   A 1 40  ? 1.309   9.581   6.611   1.00 29.15  ? 25  GLY   A CA   1 
ATOM   323  C C    . GLY   A 1 40  ? 1.609   8.130   6.886   1.00 36.10  ? 25  GLY   A C    1 
ATOM   324  O O    . GLY   A 1 40  ? 1.816   7.335   5.963   1.00 33.32  ? 25  GLY   A O    1 
ATOM   325  H H    . GLY   A 1 40  ? 2.267   9.359   4.911   1.00 38.48  ? 25  GLY   A H    1 
ATOM   326  H HA2  . GLY   A 1 40  ? 1.594   10.113  7.371   1.00 34.98  ? 25  GLY   A HA2  1 
ATOM   327  H HA3  . GLY   A 1 40  ? 0.353   9.689   6.491   1.00 34.98  ? 25  GLY   A HA3  1 
ATOM   328  N N    . GLY   A 1 41  ? 1.650   7.789   8.167   1.00 31.55  ? 26  GLY   A N    1 
ATOM   329  C CA   . GLY   A 1 41  ? 1.908   6.424   8.568   1.00 34.89  ? 26  GLY   A CA   1 
ATOM   330  C C    . GLY   A 1 41  ? 1.798   6.299   10.068  1.00 38.03  ? 26  GLY   A C    1 
ATOM   331  O O    . GLY   A 1 41  ? 1.144   7.116   10.723  1.00 37.53  ? 26  GLY   A O    1 
ATOM   332  H H    . GLY   A 1 41  ? 1.532   8.334   8.822   1.00 37.86  ? 26  GLY   A H    1 
ATOM   333  H HA2  . GLY   A 1 41  ? 1.262   5.830   8.154   1.00 41.86  ? 26  GLY   A HA2  1 
ATOM   334  H HA3  . GLY   A 1 41  ? 2.800   6.161   8.294   1.00 41.86  ? 26  GLY   A HA3  1 
ATOM   335  N N    . THR   A 1 42  ? 2.453   5.267   10.613  1.00 32.56  ? 27  THR   A N    1 
ATOM   336  C CA   . THR   A 1 42  ? 2.464   5.073   12.056  1.00 34.48  ? 27  THR   A CA   1 
ATOM   337  C C    . THR   A 1 42  ? 3.162   6.220   12.770  1.00 30.04  ? 27  THR   A C    1 
ATOM   338  O O    . THR   A 1 42  ? 2.902   6.454   13.956  1.00 32.64  ? 27  THR   A O    1 
ATOM   339  C CB   . THR   A 1 42  ? 3.145   3.746   12.422  1.00 36.38  ? 27  THR   A CB   1 
ATOM   340  O OG1  . THR   A 1 42  ? 4.514   3.756   11.997  1.00 33.90  ? 27  THR   A OG1  1 
ATOM   341  C CG2  . THR   A 1 42  ? 2.421   2.576   11.772  1.00 35.74  ? 27  THR   A CG2  1 
ATOM   342  H H    . THR   A 1 42  ? 2.891   4.674   10.169  1.00 39.08  ? 27  THR   A H    1 
ATOM   343  H HA   . THR   A 1 42  ? 1.547   5.025   12.367  1.00 41.38  ? 27  THR   A HA   1 
ATOM   344  H HB   . THR   A 1 42  ? 3.114   3.631   13.385  1.00 43.65  ? 27  THR   A HB   1 
ATOM   345  H HG1  . THR   A 1 42  ? 4.934   4.363   12.398  1.00 40.68  ? 27  THR   A HG1  1 
ATOM   346  H HG21 . THR   A 1 42  ? 2.831   1.740   12.044  1.00 42.88  ? 27  THR   A HG21 1 
ATOM   347  H HG22 . THR   A 1 42  ? 1.489   2.571   12.040  1.00 42.88  ? 27  THR   A HG22 1 
ATOM   348  H HG23 . THR   A 1 42  ? 2.471   2.650   10.806  1.00 42.88  ? 27  THR   A HG23 1 
ATOM   349  N N    . TYR   A 1 43  ? 4.040   6.935   12.076  1.00 31.96  ? 28  TYR   A N    1 
ATOM   350  C CA   . TYR   A 1 43  ? 4.712   8.106   12.624  1.00 37.19  ? 28  TYR   A CA   1 
ATOM   351  C C    . TYR   A 1 43  ? 3.819   9.338   12.704  1.00 34.86  ? 28  TYR   A C    1 
ATOM   352  O O    . TYR   A 1 43  ? 4.265   10.371  13.218  1.00 37.86  ? 28  TYR   A O    1 
ATOM   353  C CB   . TYR   A 1 43  ? 5.939   8.446   11.773  1.00 33.73  ? 28  TYR   A CB   1 
ATOM   354  C CG   . TYR   A 1 43  ? 5.621   8.681   10.305  1.00 36.30  ? 28  TYR   A CG   1 
ATOM   355  C CD1  . TYR   A 1 43  ? 5.215   9.930   9.846   1.00 38.48  ? 28  TYR   A CD1  1 
ATOM   356  C CD2  . TYR   A 1 43  ? 5.736   7.652   9.378   1.00 37.19  ? 28  TYR   A CD2  1 
ATOM   357  C CE1  . TYR   A 1 43  ? 4.926   10.141  8.505   1.00 40.22  ? 28  TYR   A CE1  1 
ATOM   358  C CE2  . TYR   A 1 43  ? 5.448   7.852   8.037   1.00 36.86  ? 28  TYR   A CE2  1 
ATOM   359  C CZ   . TYR   A 1 43  ? 5.046   9.096   7.603   1.00 45.01  ? 28  TYR   A CZ   1 
ATOM   360  O OH   . TYR   A 1 43  ? 4.763   9.290   6.264   1.00 44.90  ? 28  TYR   A OH   1 
ATOM   361  H H    . TYR   A 1 43  ? 4.268   6.759   11.266  1.00 38.35  ? 28  TYR   A H    1 
ATOM   362  H HA   . TYR   A 1 43  ? 5.002   7.889   13.524  1.00 44.63  ? 28  TYR   A HA   1 
ATOM   363  H HB2  . TYR   A 1 43  ? 6.345   9.256   12.121  1.00 40.48  ? 28  TYR   A HB2  1 
ATOM   364  H HB3  . TYR   A 1 43  ? 6.569   7.710   11.826  1.00 40.48  ? 28  TYR   A HB3  1 
ATOM   365  H HD1  . TYR   A 1 43  ? 5.136   10.635  10.448  1.00 46.18  ? 28  TYR   A HD1  1 
ATOM   366  H HD2  . TYR   A 1 43  ? 6.013   6.811   9.663   1.00 44.63  ? 28  TYR   A HD2  1 
ATOM   367  H HE1  . TYR   A 1 43  ? 4.652   10.981  8.213   1.00 48.27  ? 28  TYR   A HE1  1 
ATOM   368  H HE2  . TYR   A 1 43  ? 5.525   7.150   7.433   1.00 44.23  ? 28  TYR   A HE2  1 
ATOM   369  H HH   . TYR   A 1 43  ? 4.854   8.568   5.844   1.00 53.88  ? 28  TYR   A HH   1 
ATOM   370  N N    . GLY   A 1 44  ? 2.589   9.260   12.220  1.00 36.19  ? 29  GLY   A N    1 
ATOM   371  C CA   . GLY   A 1 44  ? 1.710   10.413  12.140  1.00 37.50  ? 29  GLY   A CA   1 
ATOM   372  C C    . GLY   A 1 44  ? 1.484   10.845  10.695  1.00 38.20  ? 29  GLY   A C    1 
ATOM   373  O O    . GLY   A 1 44  ? 1.766   10.121  9.742   1.00 35.16  ? 29  GLY   A O    1 
ATOM   374  H H    . GLY   A 1 44  ? 2.233   8.535   11.925  1.00 43.43  ? 29  GLY   A H    1 
ATOM   375  H HA2  . GLY   A 1 44  ? 0.852   10.195  12.535  1.00 45.00  ? 29  GLY   A HA2  1 
ATOM   376  H HA3  . GLY   A 1 44  ? 2.103   11.155  12.626  1.00 45.00  ? 29  GLY   A HA3  1 
ATOM   377  N N    . GLU   A 1 45  ? 0.941   12.051  10.559  1.00 26.55  ? 30  GLU   A N    1 
ATOM   378  C CA   . GLU   A 1 45  ? 0.707   12.661  9.253   1.00 29.91  ? 30  GLU   A CA   1 
ATOM   379  C C    . GLU   A 1 45  ? 1.490   13.963  9.166   1.00 26.39  ? 30  GLU   A C    1 
ATOM   380  O O    . GLU   A 1 45  ? 1.441   14.778  10.092  1.00 27.50  ? 30  GLU   A O    1 
ATOM   381  C CB   . GLU   A 1 45  ? -0.788  12.891  9.029   1.00 28.79  ? 30  GLU   A CB   1 
ATOM   382  C CG   . GLU   A 1 45  ? -1.494  11.646  8.493   1.00 44.51  ? 30  GLU   A CG   1 
ATOM   383  C CD   . GLU   A 1 45  ? -2.990  11.645  8.732   1.00 59.79  ? 30  GLU   A CD   1 
ATOM   384  O OE1  . GLU   A 1 45  ? -3.450  12.355  9.652   1.00 55.29  ? 30  GLU   A OE1  1 
ATOM   385  O OE2  . GLU   A 1 45  ? -3.705  10.917  8.006   1.00 57.46  ? 30  GLU   A OE2  1 
ATOM   386  H H    . GLU   A 1 45  ? 0.696   12.544  11.219  1.00 31.86  ? 30  GLU   A H    1 
ATOM   387  H HA   . GLU   A 1 45  ? 1.028   12.081  8.545   1.00 35.89  ? 30  GLU   A HA   1 
ATOM   388  H HB2  . GLU   A 1 45  ? -1.202  13.132  9.873   1.00 34.55  ? 30  GLU   A HB2  1 
ATOM   389  H HB3  . GLU   A 1 45  ? -0.906  13.606  8.385   1.00 34.55  ? 30  GLU   A HB3  1 
ATOM   390  H HG2  . GLU   A 1 45  ? -1.348  11.591  7.535   1.00 53.41  ? 30  GLU   A HG2  1 
ATOM   391  H HG3  . GLU   A 1 45  ? -1.124  10.863  8.930   1.00 53.41  ? 30  GLU   A HG3  1 
ATOM   392  N N    . VAL   A 1 46  ? 2.231   14.143  8.068   1.00 26.25  ? 31  VAL   A N    1 
ATOM   393  C CA   . VAL   A 1 46  ? 3.174   15.245  7.908   1.00 26.01  ? 31  VAL   A CA   1 
ATOM   394  C C    . VAL   A 1 46  ? 2.698   16.145  6.775   1.00 29.27  ? 31  VAL   A C    1 
ATOM   395  O O    . VAL   A 1 46  ? 2.431   15.667  5.666   1.00 26.80  ? 31  VAL   A O    1 
ATOM   396  C CB   . VAL   A 1 46  ? 4.600   14.739  7.626   1.00 27.43  ? 31  VAL   A CB   1 
ATOM   397  C CG1  . VAL   A 1 46  ? 5.525   15.895  7.339   1.00 26.70  ? 31  VAL   A CG1  1 
ATOM   398  C CG2  . VAL   A 1 46  ? 5.123   13.919  8.798   1.00 30.23  ? 31  VAL   A CG2  1 
ATOM   399  H H    . VAL   A 1 46  ? 2.201   13.622  7.384   1.00 31.50  ? 31  VAL   A H    1 
ATOM   400  H HA   . VAL   A 1 46  ? 3.182   15.766  8.727   1.00 31.21  ? 31  VAL   A HA   1 
ATOM   401  H HB   . VAL   A 1 46  ? 4.575   14.167  6.843   1.00 32.91  ? 31  VAL   A HB   1 
ATOM   402  H HG11 . VAL   A 1 46  ? 6.443   15.593  7.421   1.00 32.04  ? 31  VAL   A HG11 1 
ATOM   403  H HG12 . VAL   A 1 46  ? 5.361   16.215  6.439   1.00 32.04  ? 31  VAL   A HG12 1 
ATOM   404  H HG13 . VAL   A 1 46  ? 5.352   16.604  7.979   1.00 32.04  ? 31  VAL   A HG13 1 
ATOM   405  H HG21 . VAL   A 1 46  ? 6.024   13.619  8.597   1.00 36.28  ? 31  VAL   A HG21 1 
ATOM   406  H HG22 . VAL   A 1 46  ? 5.129   14.473  9.594   1.00 36.28  ? 31  VAL   A HG22 1 
ATOM   407  H HG23 . VAL   A 1 46  ? 4.542   13.153  8.932   1.00 36.28  ? 31  VAL   A HG23 1 
ATOM   408  N N    . PHE   A 1 47  ? 2.641   17.448  7.046   1.00 26.66  ? 32  PHE   A N    1 
ATOM   409  C CA   . PHE   A 1 47  ? 2.138   18.437  6.107   1.00 27.26  ? 32  PHE   A CA   1 
ATOM   410  C C    . PHE   A 1 47  ? 3.200   19.481  5.807   1.00 27.25  ? 32  PHE   A C    1 
ATOM   411  O O    . PHE   A 1 47  ? 3.941   19.907  6.698   1.00 28.70  ? 32  PHE   A O    1 
ATOM   412  C CB   . PHE   A 1 47  ? 0.890   19.155  6.651   1.00 27.86  ? 32  PHE   A CB   1 
ATOM   413  C CG   . PHE   A 1 47  ? -0.293  18.259  6.818   1.00 28.15  ? 32  PHE   A CG   1 
ATOM   414  C CD1  . PHE   A 1 47  ? -0.454  17.514  7.971   1.00 27.86  ? 32  PHE   A CD1  1 
ATOM   415  C CD2  . PHE   A 1 47  ? -1.238  18.145  5.817   1.00 29.25  ? 32  PHE   A CD2  1 
ATOM   416  C CE1  . PHE   A 1 47  ? -1.530  16.678  8.121   1.00 31.25  ? 32  PHE   A CE1  1 
ATOM   417  C CE2  . PHE   A 1 47  ? -2.330  17.307  5.976   1.00 33.78  ? 32  PHE   A CE2  1 
ATOM   418  C CZ   . PHE   A 1 47  ? -2.469  16.578  7.122   1.00 29.04  ? 32  PHE   A CZ   1 
ATOM   419  H H    . PHE   A 1 47  ? 2.896   17.790  7.792   1.00 32.00  ? 32  PHE   A H    1 
ATOM   420  H HA   . PHE   A 1 47  ? 1.910   17.979  5.283   1.00 32.71  ? 32  PHE   A HA   1 
ATOM   421  H HB2  . PHE   A 1 47  ? 1.101   19.532  7.519   1.00 33.43  ? 32  PHE   A HB2  1 
ATOM   422  H HB3  . PHE   A 1 47  ? 0.642   19.861  6.034   1.00 33.43  ? 32  PHE   A HB3  1 
ATOM   423  H HD1  . PHE   A 1 47  ? 0.175   17.582  8.653   1.00 33.43  ? 32  PHE   A HD1  1 
ATOM   424  H HD2  . PHE   A 1 47  ? -1.140  18.634  5.032   1.00 35.10  ? 32  PHE   A HD2  1 
ATOM   425  H HE1  . PHE   A 1 47  ? -1.624  16.177  8.898   1.00 37.50  ? 32  PHE   A HE1  1 
ATOM   426  H HE2  . PHE   A 1 47  ? -2.968  17.240  5.302   1.00 40.54  ? 32  PHE   A HE2  1 
ATOM   427  H HZ   . PHE   A 1 47  ? -3.201  16.014  7.228   1.00 34.84  ? 32  PHE   A HZ   1 
ATOM   428  N N    . LYS   A 1 48  ? 3.260   19.890  4.548   1.00 27.67  ? 33  LYS   A N    1 
ATOM   429  C CA   . LYS   A 1 48  ? 3.965   21.104  4.172   1.00 28.00  ? 33  LYS   A CA   1 
ATOM   430  C C    . LYS   A 1 48  ? 3.070   22.280  4.528   1.00 28.69  ? 33  LYS   A C    1 
ATOM   431  O O    . LYS   A 1 48  ? 1.860   22.243  4.276   1.00 29.16  ? 33  LYS   A O    1 
ATOM   432  C CB   . LYS   A 1 48  ? 4.288   21.074  2.681   1.00 32.43  ? 33  LYS   A CB   1 
ATOM   433  C CG   . LYS   A 1 48  ? 4.992   22.304  2.140   1.00 28.88  ? 33  LYS   A CG   1 
ATOM   434  C CD   . LYS   A 1 48  ? 5.245   22.164  0.641   1.00 29.38  ? 33  LYS   A CD   1 
ATOM   435  C CE   . LYS   A 1 48  ? 6.068   23.316  0.091   1.00 37.89  ? 33  LYS   A CE   1 
ATOM   436  N NZ   . LYS   A 1 48  ? 6.180   23.273  -1.398  1.00 49.16  ? 33  LYS   A NZ   1 
ATOM   437  H H    . LYS   A 1 48  ? 2.896   19.479  3.887   1.00 33.20  ? 33  LYS   A H    1 
ATOM   438  H HA   . LYS   A 1 48  ? 4.809   21.193  4.641   1.00 33.60  ? 33  LYS   A HA   1 
ATOM   439  H HB2  . LYS   A 1 48  ? 4.864   20.313  2.509   1.00 38.91  ? 33  LYS   A HB2  1 
ATOM   440  H HB3  . LYS   A 1 48  ? 3.457   20.979  2.190   1.00 38.91  ? 33  LYS   A HB3  1 
ATOM   441  H HG2  . LYS   A 1 48  ? 4.438   23.086  2.287   1.00 34.66  ? 33  LYS   A HG2  1 
ATOM   442  H HG3  . LYS   A 1 48  ? 5.846   22.412  2.588   1.00 34.66  ? 33  LYS   A HG3  1 
ATOM   443  H HD2  . LYS   A 1 48  ? 5.729   21.340  0.474   1.00 35.26  ? 33  LYS   A HD2  1 
ATOM   444  H HD3  . LYS   A 1 48  ? 4.395   22.150  0.174   1.00 35.26  ? 33  LYS   A HD3  1 
ATOM   445  H HE2  . LYS   A 1 48  ? 5.647   24.154  0.338   1.00 45.47  ? 33  LYS   A HE2  1 
ATOM   446  H HE3  . LYS   A 1 48  ? 6.964   23.272  0.461   1.00 45.47  ? 33  LYS   A HE3  1 
ATOM   447  H HZ1  . LYS   A 1 48  ? 6.667   23.960  -1.686  1.00 58.99  ? 33  LYS   A HZ1  1 
ATOM   448  H HZ2  . LYS   A 1 48  ? 6.570   22.515  -1.653  1.00 58.99  ? 33  LYS   A HZ2  1 
ATOM   449  H HZ3  . LYS   A 1 48  ? 5.370   23.319  -1.765  1.00 58.99  ? 33  LYS   A HZ3  1 
ATOM   450  N N    . ALA   A 1 49  ? 3.651   23.306  5.146   1.00 28.91  ? 34  ALA   A N    1 
ATOM   451  C CA   . ALA   A 1 49  ? 2.884   24.452  5.620   1.00 31.00  ? 34  ALA   A CA   1 
ATOM   452  C C    . ALA   A 1 49  ? 3.723   25.723  5.519   1.00 30.37  ? 34  ALA   A C    1 
ATOM   453  O O    . ALA   A 1 49  ? 4.955   25.678  5.500   1.00 30.09  ? 34  ALA   A O    1 
ATOM   454  C CB   . ALA   A 1 49  ? 2.415   24.235  7.065   1.00 29.60  ? 34  ALA   A CB   1 
ATOM   455  H H    . ALA   A 1 49  ? 4.495   23.362  5.303   1.00 34.70  ? 34  ALA   A H    1 
ATOM   456  H HA   . ALA   A 1 49  ? 2.109   24.572  5.048   1.00 37.21  ? 34  ALA   A HA   1 
ATOM   457  H HB1  . ALA   A 1 49  ? 1.911   25.012  7.354   1.00 35.52  ? 34  ALA   A HB1  1 
ATOM   458  H HB2  . ALA   A 1 49  ? 1.853   23.445  7.100   1.00 35.52  ? 34  ALA   A HB2  1 
ATOM   459  H HB3  . ALA   A 1 49  ? 3.191   24.114  7.635   1.00 35.52  ? 34  ALA   A HB3  1 
ATOM   460  N N    . ARG   A 1 50  ? 3.030   26.866  5.463   1.00 31.39  ? 35  ARG   A N    1 
ATOM   461  C CA   . ARG   A 1 50  ? 3.656   28.178  5.368   1.00 32.32  ? 35  ARG   A CA   1 
ATOM   462  C C    . ARG   A 1 50  ? 3.264   29.053  6.556   1.00 33.15  ? 35  ARG   A C    1 
ATOM   463  O O    . ARG   A 1 50  ? 2.075   29.233  6.839   1.00 33.62  ? 35  ARG   A O    1 
ATOM   464  C CB   . ARG   A 1 50  ? 3.268   28.903  4.074   1.00 33.18  ? 35  ARG   A CB   1 
ATOM   465  C CG   . ARG   A 1 50  ? 3.886   30.295  3.968   1.00 39.74  ? 35  ARG   A CG   1 
ATOM   466  C CD   . ARG   A 1 50  ? 3.436   31.057  2.735   1.00 41.66  ? 35  ARG   A CD   1 
ATOM   467  N NE   . ARG   A 1 50  ? 3.841   30.408  1.494   1.00 53.73  ? 35  ARG   A NE   1 
ATOM   468  C CZ   . ARG   A 1 50  ? 3.012   29.845  0.622   1.00 54.64  ? 35  ARG   A CZ   1 
ATOM   469  N NH1  . ARG   A 1 50  ? 1.702   29.822  0.820   1.00 55.61  ? 35  ARG   A NH1  1 
ATOM   470  N NH2  . ARG   A 1 50  ? 3.512   29.299  -0.483  1.00 54.62  ? 35  ARG   A NH2  1 
ATOM   471  H H    . ARG   A 1 50  ? 2.171   26.901  5.478   1.00 37.67  ? 35  ARG   A H    1 
ATOM   472  H HA   . ARG   A 1 50  ? 4.617   28.045  5.387   1.00 38.78  ? 35  ARG   A HA   1 
ATOM   473  H HB2  . ARG   A 1 50  ? 3.574   28.380  3.316   1.00 39.82  ? 35  ARG   A HB2  1 
ATOM   474  H HB3  . ARG   A 1 50  ? 2.304   28.999  4.043   1.00 39.82  ? 35  ARG   A HB3  1 
ATOM   475  H HG2  . ARG   A 1 50  ? 3.631   30.813  4.747   1.00 47.69  ? 35  ARG   A HG2  1 
ATOM   476  H HG3  . ARG   A 1 50  ? 4.852   30.209  3.928   1.00 47.69  ? 35  ARG   A HG3  1 
ATOM   477  H HD2  . ARG   A 1 50  ? 2.468   31.120  2.738   1.00 49.99  ? 35  ARG   A HD2  1 
ATOM   478  H HD3  . ARG   A 1 50  ? 3.826   31.945  2.751   1.00 49.99  ? 35  ARG   A HD3  1 
ATOM   479  H HE   . ARG   A 1 50  ? 4.682   30.389  1.313   1.00 64.47  ? 35  ARG   A HE   1 
ATOM   480  H HH11 . ARG   A 1 50  ? 1.368   30.177  1.528   1.00 66.74  ? 35  ARG   A HH11 1 
ATOM   481  H HH12 . ARG   A 1 50  ? 1.186   29.450  0.241   1.00 66.74  ? 35  ARG   A HH12 1 
ATOM   482  H HH21 . ARG   A 1 50  ? 4.360   29.314  -0.625  1.00 65.54  ? 35  ARG   A HH21 1 
ATOM   483  H HH22 . ARG   A 1 50  ? 2.987   28.931  -1.056  1.00 65.54  ? 35  ARG   A HH22 1 
ATOM   484  N N    . ASP   A 1 51  ? 4.268   29.604  7.228   1.00 33.53  ? 36  ASP   A N    1 
ATOM   485  C CA   . ASP   A 1 51  ? 4.036   30.586  8.276   1.00 35.39  ? 36  ASP   A CA   1 
ATOM   486  C C    . ASP   A 1 51  ? 3.286   31.782  7.700   1.00 37.49  ? 36  ASP   A C    1 
ATOM   487  O O    . ASP   A 1 51  ? 3.659   32.317  6.654   1.00 36.45  ? 36  ASP   A O    1 
ATOM   488  C CB   . ASP   A 1 51  ? 5.377   31.017  8.873   1.00 40.20  ? 36  ASP   A CB   1 
ATOM   489  C CG   . ASP   A 1 51  ? 5.227   31.863  10.119  1.00 41.10  ? 36  ASP   A CG   1 
ATOM   490  O OD1  . ASP   A 1 51  ? 4.352   32.748  10.136  1.00 50.55  ? 36  ASP   A OD1  1 
ATOM   491  O OD2  . ASP   A 1 51  ? 5.993   31.644  11.079  1.00 49.25  ? 36  ASP   A OD2  1 
ATOM   492  H H    . ASP   A 1 51  ? 5.099   29.425  7.096   1.00 40.23  ? 36  ASP   A H    1 
ATOM   493  H HA   . ASP   A 1 51  ? 3.498   30.206  8.988   1.00 42.47  ? 36  ASP   A HA   1 
ATOM   494  H HB2  . ASP   A 1 51  ? 5.886   30.226  9.109   1.00 48.24  ? 36  ASP   A HB2  1 
ATOM   495  H HB3  . ASP   A 1 51  ? 5.862   31.539  8.215   1.00 48.24  ? 36  ASP   A HB3  1 
ATOM   496  N N    . LYS   A 1 52  ? 2.209   32.184  8.381   1.00 36.81  ? 37  LYS   A N    1 
ATOM   497  C CA   . LYS   A 1 52  ? 1.372   33.273  7.889   1.00 40.24  ? 37  LYS   A CA   1 
ATOM   498  C C    . LYS   A 1 52  ? 2.063   34.626  8.012   1.00 40.05  ? 37  LYS   A C    1 
ATOM   499  O O    . LYS   A 1 52  ? 1.752   35.548  7.251   1.00 43.55  ? 37  LYS   A O    1 
ATOM   500  C CB   . LYS   A 1 52  ? 0.045   33.304  8.651   1.00 38.78  ? 37  LYS   A CB   1 
ATOM   501  C CG   . LYS   A 1 52  ? -1.023  32.374  8.114   1.00 38.02  ? 37  LYS   A CG   1 
ATOM   502  C CD   . LYS   A 1 52  ? -2.255  32.338  9.031   1.00 44.44  ? 37  LYS   A CD   1 
ATOM   503  C CE   . LYS   A 1 52  ? -3.354  31.468  8.438   1.00 53.78  ? 37  LYS   A CE   1 
ATOM   504  N NZ   . LYS   A 1 52  ? -4.523  31.299  9.343   1.00 50.72  ? 37  LYS   A NZ   1 
ATOM   505  H H    . LYS   A 1 52  ? 1.945   31.843  9.126   1.00 44.18  ? 37  LYS   A H    1 
ATOM   506  H HA   . LYS   A 1 52  ? 1.188   33.110  6.951   1.00 48.29  ? 37  LYS   A HA   1 
ATOM   507  H HB2  . LYS   A 1 52  ? 0.214   33.052  9.572   1.00 46.54  ? 37  LYS   A HB2  1 
ATOM   508  H HB3  . LYS   A 1 52  ? -0.309  34.206  8.613   1.00 46.54  ? 37  LYS   A HB3  1 
ATOM   509  H HG2  . LYS   A 1 52  ? -1.305  32.680  7.238   1.00 45.62  ? 37  LYS   A HG2  1 
ATOM   510  H HG3  . LYS   A 1 52  ? -0.664  31.475  8.051   1.00 45.62  ? 37  LYS   A HG3  1 
ATOM   511  H HD2  . LYS   A 1 52  ? -2.006  31.971  9.893   1.00 53.33  ? 37  LYS   A HD2  1 
ATOM   512  H HD3  . LYS   A 1 52  ? -2.602  33.237  9.141   1.00 53.33  ? 37  LYS   A HD3  1 
ATOM   513  H HE2  . LYS   A 1 52  ? -3.670  31.876  7.617   1.00 64.53  ? 37  LYS   A HE2  1 
ATOM   514  H HE3  . LYS   A 1 52  ? -2.992  30.587  8.252   1.00 64.53  ? 37  LYS   A HE3  1 
ATOM   515  H HZ1  . LYS   A 1 52  ? -5.136  30.783  8.955   1.00 60.87  ? 37  LYS   A HZ1  1 
ATOM   516  H HZ2  . LYS   A 1 52  ? -4.266  30.919  10.105  1.00 60.87  ? 37  LYS   A HZ2  1 
ATOM   517  H HZ3  . LYS   A 1 52  ? -4.886  32.091  9.523   1.00 60.87  ? 37  LYS   A HZ3  1 
ATOM   518  N N    . VAL   A 1 53  ? 2.987   34.773  8.958   1.00 42.66  ? 38  VAL   A N    1 
ATOM   519  C CA   . VAL   A 1 53  ? 3.657   36.050  9.169   1.00 49.14  ? 38  VAL   A CA   1 
ATOM   520  C C    . VAL   A 1 53  ? 4.932   36.120  8.338   1.00 41.56  ? 38  VAL   A C    1 
ATOM   521  O O    . VAL   A 1 53  ? 5.076   37.001  7.485   1.00 50.45  ? 38  VAL   A O    1 
ATOM   522  C CB   . VAL   A 1 53  ? 3.964   36.276  10.662  1.00 52.94  ? 38  VAL   A CB   1 
ATOM   523  C CG1  . VAL   A 1 53  ? 4.876   37.491  10.848  1.00 55.26  ? 38  VAL   A CG1  1 
ATOM   524  C CG2  . VAL   A 1 53  ? 2.670   36.460  11.440  1.00 53.51  ? 38  VAL   A CG2  1 
ATOM   525  H H    . VAL   A 1 53  ? 3.243   34.147  9.490   1.00 51.19  ? 38  VAL   A H    1 
ATOM   526  H HA   . VAL   A 1 53  ? 3.067   36.756  8.863   1.00 58.96  ? 38  VAL   A HA   1 
ATOM   527  H HB   . VAL   A 1 53  ? 4.427   35.497  11.010  1.00 63.53  ? 38  VAL   A HB   1 
ATOM   528  H HG11 . VAL   A 1 53  ? 4.828   37.783  11.772  1.00 66.32  ? 38  VAL   A HG11 1 
ATOM   529  H HG12 . VAL   A 1 53  ? 5.786   37.239  10.628  1.00 66.32  ? 38  VAL   A HG12 1 
ATOM   530  H HG13 . VAL   A 1 53  ? 4.577   38.202  10.260  1.00 66.32  ? 38  VAL   A HG13 1 
ATOM   531  H HG21 . VAL   A 1 53  ? 2.881   36.595  12.377  1.00 64.22  ? 38  VAL   A HG21 1 
ATOM   532  H HG22 . VAL   A 1 53  ? 2.200   37.233  11.091  1.00 64.22  ? 38  VAL   A HG22 1 
ATOM   533  H HG23 . VAL   A 1 53  ? 2.123   35.665  11.335  1.00 64.22  ? 38  VAL   A HG23 1 
ATOM   534  N N    . SER   A 1 54  ? 5.855   35.184  8.577   1.00 49.41  ? 39  SER   A N    1 
ATOM   535  C CA   . SER   A 1 54  ? 7.176   35.239  7.962   1.00 46.72  ? 39  SER   A CA   1 
ATOM   536  C C    . SER   A 1 54  ? 7.192   34.717  6.530   1.00 46.15  ? 39  SER   A C    1 
ATOM   537  O O    . SER   A 1 54  ? 8.063   35.108  5.746   1.00 51.88  ? 39  SER   A O    1 
ATOM   538  C CB   . SER   A 1 54  ? 8.172   34.432  8.800   1.00 43.93  ? 39  SER   A CB   1 
ATOM   539  O OG   . SER   A 1 54  ? 7.857   33.050  8.781   1.00 50.50  ? 39  SER   A OG   1 
ATOM   540  H H    . SER   A 1 54  ? 5.739   34.506  9.093   1.00 59.29  ? 39  SER   A H    1 
ATOM   541  H HA   . SER   A 1 54  ? 7.455   36.168  7.941   1.00 56.07  ? 39  SER   A HA   1 
ATOM   542  H HB2  . SER   A 1 54  ? 9.063   34.556  8.436   1.00 52.72  ? 39  SER   A HB2  1 
ATOM   543  H HB3  . SER   A 1 54  ? 8.142   34.748  9.716   1.00 52.72  ? 39  SER   A HB3  1 
ATOM   544  H HG   . SER   A 1 54  ? 8.418   32.622  9.236   1.00 60.60  ? 39  SER   A HG   1 
ATOM   545  N N    . GLY   A 1 55  ? 6.267   33.833  6.171   1.00 45.21  ? 40  GLY   A N    1 
ATOM   546  C CA   . GLY   A 1 55  ? 6.323   33.178  4.884   1.00 37.29  ? 40  GLY   A CA   1 
ATOM   547  C C    . GLY   A 1 55  ? 7.247   31.979  4.823   1.00 37.93  ? 40  GLY   A C    1 
ATOM   548  O O    . GLY   A 1 55  ? 7.371   31.371  3.752   1.00 37.46  ? 40  GLY   A O    1 
ATOM   549  H H    . GLY   A 1 55  ? 5.600   33.600  6.660   1.00 54.25  ? 40  GLY   A H    1 
ATOM   550  H HA2  . GLY   A 1 55  ? 5.431   32.876  4.649   1.00 44.75  ? 40  GLY   A HA2  1 
ATOM   551  H HA3  . GLY   A 1 55  ? 6.625   33.818  4.221   1.00 44.75  ? 40  GLY   A HA3  1 
ATOM   552  N N    . ASP   A 1 56  ? 7.907   31.632  5.931   1.00 38.46  ? 41  ASP   A N    1 
ATOM   553  C CA   . ASP   A 1 56  ? 8.756   30.451  5.978   1.00 36.64  ? 41  ASP   A CA   1 
ATOM   554  C C    . ASP   A 1 56  ? 7.942   29.182  5.767   1.00 36.19  ? 41  ASP   A C    1 
ATOM   555  O O    . ASP   A 1 56  ? 6.825   29.044  6.271   1.00 32.70  ? 41  ASP   A O    1 
ATOM   556  C CB   . ASP   A 1 56  ? 9.463   30.354  7.333   1.00 44.39  ? 41  ASP   A CB   1 
ATOM   557  C CG   . ASP   A 1 56  ? 10.673  31.249  7.435   1.00 47.91  ? 41  ASP   A CG   1 
ATOM   558  O OD1  . ASP   A 1 56  ? 11.584  31.142  6.585   1.00 61.76  ? 41  ASP   A OD1  1 
ATOM   559  O OD2  . ASP   A 1 56  ? 10.715  32.053  8.385   1.00 57.03  ? 41  ASP   A OD2  1 
ATOM   560  H H    . ASP   A 1 56  ? 7.878   32.070  6.671   1.00 46.15  ? 41  ASP   A H    1 
ATOM   561  H HA   . ASP   A 1 56  ? 9.418   30.526  5.274   1.00 43.97  ? 41  ASP   A HA   1 
ATOM   562  H HB2  . ASP   A 1 56  ? 8.842   30.611  8.032   1.00 53.27  ? 41  ASP   A HB2  1 
ATOM   563  H HB3  . ASP   A 1 56  ? 9.756   29.439  7.469   1.00 53.27  ? 41  ASP   A HB3  1 
ATOM   564  N N    . LEU   A 1 57  ? 8.521   28.238  5.036   1.00 33.34  ? 42  LEU   A N    1 
ATOM   565  C CA   . LEU   A 1 57  ? 7.972   26.896  4.972   1.00 33.87  ? 42  LEU   A CA   1 
ATOM   566  C C    . LEU   A 1 57  ? 8.386   26.104  6.207   1.00 30.33  ? 42  LEU   A C    1 
ATOM   567  O O    . LEU   A 1 57  ? 9.484   26.280  6.743   1.00 30.38  ? 42  LEU   A O    1 
ATOM   568  C CB   . LEU   A 1 57  ? 8.439   26.187  3.703   1.00 31.46  ? 42  LEU   A CB   1 
ATOM   569  C CG   . LEU   A 1 57  ? 7.963   26.824  2.391   1.00 38.61  ? 42  LEU   A CG   1 
ATOM   570  C CD1  . LEU   A 1 57  ? 8.408   25.994  1.196   1.00 37.23  ? 42  LEU   A CD1  1 
ATOM   571  C CD2  . LEU   A 1 57  ? 6.450   26.988  2.391   1.00 37.62  ? 42  LEU   A CD2  1 
ATOM   572  H H    . LEU   A 1 57  ? 9.234   28.352  4.568   1.00 40.01  ? 42  LEU   A H    1 
ATOM   573  H HA   . LEU   A 1 57  ? 7.003   26.939  4.947   1.00 40.64  ? 42  LEU   A HA   1 
ATOM   574  H HB2  . LEU   A 1 57  ? 9.409   26.188  3.691   1.00 37.75  ? 42  LEU   A HB2  1 
ATOM   575  H HB3  . LEU   A 1 57  ? 8.108   25.276  3.721   1.00 37.75  ? 42  LEU   A HB3  1 
ATOM   576  H HG   . LEU   A 1 57  ? 8.361   27.705  2.311   1.00 46.33  ? 42  LEU   A HG   1 
ATOM   577  H HD11 . LEU   A 1 57  ? 8.064   26.400  0.384   1.00 44.68  ? 42  LEU   A HD11 1 
ATOM   578  H HD12 . LEU   A 1 57  ? 9.378   25.973  1.170   1.00 44.68  ? 42  LEU   A HD12 1 
ATOM   579  H HD13 . LEU   A 1 57  ? 8.060   25.094  1.289   1.00 44.68  ? 42  LEU   A HD13 1 
ATOM   580  H HD21 . LEU   A 1 57  ? 6.153   27.179  1.487   1.00 45.15  ? 42  LEU   A HD21 1 
ATOM   581  H HD22 . LEU   A 1 57  ? 6.043   26.166  2.706   1.00 45.15  ? 42  LEU   A HD22 1 
ATOM   582  H HD23 . LEU   A 1 57  ? 6.211   27.722  2.979   1.00 45.15  ? 42  LEU   A HD23 1 
ATOM   583  N N    . VAL   A 1 58  ? 7.478   25.249  6.674   1.00 29.49  ? 43  VAL   A N    1 
ATOM   584  C CA   . VAL   A 1 58  ? 7.741   24.332  7.771   1.00 28.88  ? 43  VAL   A CA   1 
ATOM   585  C C    . VAL   A 1 58  ? 7.095   22.994  7.433   1.00 28.01  ? 43  VAL   A C    1 
ATOM   586  O O    . VAL   A 1 58  ? 6.317   22.868  6.484   1.00 28.02  ? 43  VAL   A O    1 
ATOM   587  C CB   . VAL   A 1 58  ? 7.203   24.838  9.131   1.00 29.88  ? 43  VAL   A CB   1 
ATOM   588  C CG1  . VAL   A 1 58  ? 7.802   26.181  9.498   1.00 30.56  ? 43  VAL   A CG1  1 
ATOM   589  C CG2  . VAL   A 1 58  ? 5.684   24.919  9.106   1.00 29.53  ? 43  VAL   A CG2  1 
ATOM   590  H H    . VAL   A 1 58  ? 6.681   25.183  6.359   1.00 35.39  ? 43  VAL   A H    1 
ATOM   591  H HA   . VAL   A 1 58  ? 8.700   24.218  7.852   1.00 34.66  ? 43  VAL   A HA   1 
ATOM   592  H HB   . VAL   A 1 58  ? 7.465   24.203  9.816   1.00 35.85  ? 43  VAL   A HB   1 
ATOM   593  H HG11 . VAL   A 1 58  ? 7.430   26.472  10.346  1.00 36.67  ? 43  VAL   A HG11 1 
ATOM   594  H HG12 . VAL   A 1 58  ? 8.765   26.087  9.575   1.00 36.67  ? 43  VAL   A HG12 1 
ATOM   595  H HG13 . VAL   A 1 58  ? 7.587   26.823  8.804   1.00 36.67  ? 43  VAL   A HG13 1 
ATOM   596  H HG21 . VAL   A 1 58  ? 5.383   25.443  9.865   1.00 35.44  ? 43  VAL   A HG21 1 
ATOM   597  H HG22 . VAL   A 1 58  ? 5.404   25.343  8.279   1.00 35.44  ? 43  VAL   A HG22 1 
ATOM   598  H HG23 . VAL   A 1 58  ? 5.318   24.022  9.157   1.00 35.44  ? 43  VAL   A HG23 1 
ATOM   599  N N    . ALA   A 1 59  ? 7.419   21.996  8.240   1.00 27.45  ? 44  ALA   A N    1 
ATOM   600  C CA   . ALA   A 1 59  ? 6.711   20.728  8.239   1.00 26.83  ? 44  ALA   A CA   1 
ATOM   601  C C    . ALA   A 1 59  ? 5.933   20.636  9.540   1.00 28.24  ? 44  ALA   A C    1 
ATOM   602  O O    . ALA   A 1 59  ? 6.470   20.942  10.608  1.00 28.73  ? 44  ALA   A O    1 
ATOM   603  C CB   . ALA   A 1 59  ? 7.674   19.549  8.097   1.00 30.10  ? 44  ALA   A CB   1 
ATOM   604  H H    . ALA   A 1 59  ? 8.061   22.032  8.810   1.00 32.94  ? 44  ALA   A H    1 
ATOM   605  H HA   . ALA   A 1 59  ? 6.095   20.681  7.491   1.00 32.20  ? 44  ALA   A HA   1 
ATOM   606  H HB1  . ALA   A 1 59  ? 7.166   18.723  8.101   1.00 36.12  ? 44  ALA   A HB1  1 
ATOM   607  H HB2  . ALA   A 1 59  ? 8.158   19.636  7.260   1.00 36.12  ? 44  ALA   A HB2  1 
ATOM   608  H HB3  . ALA   A 1 59  ? 8.296   19.559  8.841   1.00 36.12  ? 44  ALA   A HB3  1 
ATOM   609  N N    . LEU   A 1 60  ? 4.663   20.259  9.441   1.00 26.93  ? 45  LEU   A N    1 
ATOM   610  C CA   . LEU   A 1 60  ? 3.809   20.014  10.593  1.00 27.09  ? 45  LEU   A CA   1 
ATOM   611  C C    . LEU   A 1 60  ? 3.500   18.523  10.646  1.00 26.77  ? 45  LEU   A C    1 
ATOM   612  O O    . LEU   A 1 60  ? 2.914   17.977  9.706   1.00 26.50  ? 45  LEU   A O    1 
ATOM   613  C CB   . LEU   A 1 60  ? 2.519   20.829  10.502  1.00 27.78  ? 45  LEU   A CB   1 
ATOM   614  C CG   . LEU   A 1 60  ? 2.633   22.313  10.853  1.00 32.17  ? 45  LEU   A CG   1 
ATOM   615  C CD1  . LEU   A 1 60  ? 1.324   23.035  10.545  1.00 29.35  ? 45  LEU   A CD1  1 
ATOM   616  C CD2  . LEU   A 1 60  ? 2.995   22.483  12.320  1.00 38.64  ? 45  LEU   A CD2  1 
ATOM   617  H H    . LEU   A 1 60  ? 4.261   20.135  8.690   1.00 32.32  ? 45  LEU   A H    1 
ATOM   618  H HA   . LEU   A 1 60  ? 4.270   20.268  11.407  1.00 32.51  ? 45  LEU   A HA   1 
ATOM   619  H HB2  . LEU   A 1 60  ? 2.191   20.775  9.591   1.00 33.34  ? 45  LEU   A HB2  1 
ATOM   620  H HB3  . LEU   A 1 60  ? 1.873   20.440  11.111  1.00 33.34  ? 45  LEU   A HB3  1 
ATOM   621  H HG   . LEU   A 1 60  ? 3.336   22.713  10.317  1.00 38.61  ? 45  LEU   A HG   1 
ATOM   622  H HD11 . LEU   A 1 60  ? 1.414   23.969  10.791  1.00 35.22  ? 45  LEU   A HD11 1 
ATOM   623  H HD12 . LEU   A 1 60  ? 1.138   22.959  9.596   1.00 35.22  ? 45  LEU   A HD12 1 
ATOM   624  H HD13 . LEU   A 1 60  ? 0.609   22.626  11.057  1.00 35.22  ? 45  LEU   A HD13 1 
ATOM   625  H HD21 . LEU   A 1 60  ? 2.915   23.420  12.558  1.00 46.37  ? 45  LEU   A HD21 1 
ATOM   626  H HD22 . LEU   A 1 60  ? 2.388   21.952  12.859  1.00 46.37  ? 45  LEU   A HD22 1 
ATOM   627  H HD23 . LEU   A 1 60  ? 3.907   22.184  12.457  1.00 46.37  ? 45  LEU   A HD23 1 
ATOM   628  N N    . LYS   A 1 61  ? 3.906   17.871  11.734  1.00 26.40  ? 46  LYS   A N    1 
ATOM   629  C CA   . LYS   A 1 61  ? 3.553   16.482  11.989  1.00 29.03  ? 46  LYS   A CA   1 
ATOM   630  C C    . LYS   A 1 61  ? 2.415   16.446  12.997  1.00 30.09  ? 46  LYS   A C    1 
ATOM   631  O O    . LYS   A 1 61  ? 2.524   17.020  14.085  1.00 29.91  ? 46  LYS   A O    1 
ATOM   632  C CB   . LYS   A 1 61  ? 4.737   15.674  12.517  1.00 30.74  ? 46  LYS   A CB   1 
ATOM   633  C CG   . LYS   A 1 61  ? 4.390   14.196  12.745  1.00 37.49  ? 46  LYS   A CG   1 
ATOM   634  C CD   . LYS   A 1 61  ? 5.496   13.457  13.450  1.00 35.24  ? 46  LYS   A CD   1 
ATOM   635  C CE   . LYS   A 1 61  ? 6.681   13.226  12.543  1.00 30.23  ? 46  LYS   A CE   1 
ATOM   636  N NZ   . LYS   A 1 61  ? 7.770   12.531  13.279  1.00 45.83  ? 46  LYS   A NZ   1 
ATOM   637  H H    . LYS   A 1 61  ? 4.395   18.221  12.349  1.00 31.68  ? 46  LYS   A H    1 
ATOM   638  H HA   . LYS   A 1 61  ? 3.269   16.070  11.158  1.00 34.84  ? 46  LYS   A HA   1 
ATOM   639  H HB2  . LYS   A 1 61  ? 5.461   15.717  11.873  1.00 36.88  ? 46  LYS   A HB2  1 
ATOM   640  H HB3  . LYS   A 1 61  ? 5.024   16.050  13.364  1.00 36.88  ? 46  LYS   A HB3  1 
ATOM   641  H HG2  . LYS   A 1 61  ? 3.591   14.137  13.292  1.00 44.98  ? 46  LYS   A HG2  1 
ATOM   642  H HG3  . LYS   A 1 61  ? 4.238   13.768  11.888  1.00 44.98  ? 46  LYS   A HG3  1 
ATOM   643  H HD2  . LYS   A 1 61  ? 5.794   13.977  14.212  1.00 42.28  ? 46  LYS   A HD2  1 
ATOM   644  H HD3  . LYS   A 1 61  ? 5.167   12.594  13.745  1.00 42.28  ? 46  LYS   A HD3  1 
ATOM   645  H HE2  . LYS   A 1 61  ? 6.414   12.674  11.792  1.00 36.28  ? 46  LYS   A HE2  1 
ATOM   646  H HE3  . LYS   A 1 61  ? 7.018   14.078  12.225  1.00 36.28  ? 46  LYS   A HE3  1 
ATOM   647  H HZ1  . LYS   A 1 61  ? 8.466   12.401  12.740  1.00 54.99  ? 46  LYS   A HZ1  1 
ATOM   648  H HZ2  . LYS   A 1 61  ? 8.030   13.023  13.973  1.00 54.99  ? 46  LYS   A HZ2  1 
ATOM   649  H HZ3  . LYS   A 1 61  ? 7.482   11.742  13.574  1.00 54.99  ? 46  LYS   A HZ3  1 
ATOM   650  N N    . MET   A 1 62  ? 1.332   15.774  12.631  1.00 26.71  ? 47  MET   A N    1 
ATOM   651  C CA   . MET   A 1 62  ? 0.131   15.696  13.448  1.00 28.41  ? 47  MET   A CA   1 
ATOM   652  C C    . MET   A 1 62  ? -0.046  14.270  13.954  1.00 27.23  ? 47  MET   A C    1 
ATOM   653  O O    . MET   A 1 62  ? 0.086   13.310  13.184  1.00 26.98  ? 47  MET   A O    1 
ATOM   654  C CB   . MET   A 1 62  ? -1.090  16.139  12.640  1.00 27.93  ? 47  MET   A CB   1 
ATOM   655  C CG   . MET   A 1 62  ? -2.345  16.295  13.473  1.00 33.56  ? 47  MET   A CG   1 
ATOM   656  S SD   . MET   A 1 62  ? -3.239  14.742  13.689  1.00 34.11  ? 47  MET   A SD   1 
ATOM   657  C CE   . MET   A 1 62  ? -4.182  14.696  12.165  1.00 29.40  ? 47  MET   A CE   1 
ATOM   658  H H    . MET   A 1 62  ? 1.268   15.342  11.890  1.00 32.05  ? 47  MET   A H    1 
ATOM   659  H HA   . MET   A 1 62  ? 0.217   16.285  14.214  1.00 34.10  ? 47  MET   A HA   1 
ATOM   660  H HB2  . MET   A 1 62  ? -0.898  16.997  12.229  1.00 33.52  ? 47  MET   A HB2  1 
ATOM   661  H HB3  . MET   A 1 62  ? -1.269  15.476  11.955  1.00 33.52  ? 47  MET   A HB3  1 
ATOM   662  H HG2  . MET   A 1 62  ? -2.101  16.625  14.352  1.00 40.28  ? 47  MET   A HG2  1 
ATOM   663  H HG3  . MET   A 1 62  ? -2.939  16.924  13.035  1.00 40.28  ? 47  MET   A HG3  1 
ATOM   664  H HE1  . MET   A 1 62  ? -4.722  13.890  12.152  1.00 35.28  ? 47  MET   A HE1  1 
ATOM   665  H HE2  . MET   A 1 62  ? -4.754  15.478  12.124  1.00 35.28  ? 47  MET   A HE2  1 
ATOM   666  H HE3  . MET   A 1 62  ? -3.568  14.695  11.414  1.00 35.28  ? 47  MET   A HE3  1 
ATOM   667  N N    . VAL   A 1 63  ? -0.325  14.141  15.250  1.00 27.62  ? 48  VAL   A N    1 
ATOM   668  C CA   . VAL   A 1 63  ? -0.583  12.863  15.905  1.00 27.79  ? 48  VAL   A CA   1 
ATOM   669  C C    . VAL   A 1 63  ? -1.949  12.933  16.570  1.00 28.64  ? 48  VAL   A C    1 
ATOM   670  O O    . VAL   A 1 63  ? -2.222  13.863  17.338  1.00 29.13  ? 48  VAL   A O    1 
ATOM   671  C CB   . VAL   A 1 63  ? 0.499   12.526  16.948  1.00 27.65  ? 48  VAL   A CB   1 
ATOM   672  C CG1  . VAL   A 1 63  ? 0.221   11.172  17.605  1.00 27.96  ? 48  VAL   A CG1  1 
ATOM   673  C CG2  . VAL   A 1 63  ? 1.874   12.546  16.308  1.00 34.52  ? 48  VAL   A CG2  1 
ATOM   674  H H    . VAL   A 1 63  ? -0.373  14.808  15.791  1.00 33.15  ? 48  VAL   A H    1 
ATOM   675  H HA   . VAL   A 1 63  ? -0.595  12.162  15.235  1.00 33.35  ? 48  VAL   A HA   1 
ATOM   676  H HB   . VAL   A 1 63  ? 0.481   13.200  17.646  1.00 33.18  ? 48  VAL   A HB   1 
ATOM   677  H HG11 . VAL   A 1 63  ? 0.991   10.914  18.135  1.00 33.55  ? 48  VAL   A HG11 1 
ATOM   678  H HG12 . VAL   A 1 63  ? -0.560  11.253  18.175  1.00 33.55  ? 48  VAL   A HG12 1 
ATOM   679  H HG13 . VAL   A 1 63  ? 0.059   10.512  16.913  1.00 33.55  ? 48  VAL   A HG13 1 
ATOM   680  H HG21 . VAL   A 1 63  ? 2.529   12.246  16.957  1.00 41.42  ? 48  VAL   A HG21 1 
ATOM   681  H HG22 . VAL   A 1 63  ? 1.874   11.954  15.540  1.00 41.42  ? 48  VAL   A HG22 1 
ATOM   682  H HG23 . VAL   A 1 63  ? 2.079   13.452  16.027  1.00 41.42  ? 48  VAL   A HG23 1 
ATOM   683  N N    . LYS   A 1 64  ? -2.797  11.948  16.288  1.00 29.00  ? 49  LYS   A N    1 
ATOM   684  C CA   . LYS   A 1 64  ? -4.135  11.906  16.865  1.00 29.96  ? 49  LYS   A CA   1 
ATOM   685  C C    . LYS   A 1 64  ? -4.097  11.338  18.285  1.00 30.39  ? 49  LYS   A C    1 
ATOM   686  O O    . LYS   A 1 64  ? -3.439  10.322  18.542  1.00 30.13  ? 49  LYS   A O    1 
ATOM   687  C CB   . LYS   A 1 64  ? -5.060  11.073  15.986  1.00 30.56  ? 49  LYS   A CB   1 
ATOM   688  C CG   . LYS   A 1 64  ? -4.959  11.390  14.507  1.00 30.11  ? 49  LYS   A CG   1 
ATOM   689  C CD   . LYS   A 1 64  ? -5.881  10.509  13.676  1.00 30.88  ? 49  LYS   A CD   1 
ATOM   690  C CE   . LYS   A 1 64  ? -5.484  10.524  12.207  1.00 33.47  ? 49  LYS   A CE   1 
ATOM   691  N NZ   . LYS   A 1 64  ? -6.328  9.620   11.380  1.00 37.67  ? 49  LYS   A NZ   1 
ATOM   692  H H    . LYS   A 1 64  ? -2.620  11.290  15.763  1.00 34.80  ? 49  LYS   A H    1 
ATOM   693  H HA   . LYS   A 1 64  ? -4.485  12.809  16.918  1.00 35.95  ? 49  LYS   A HA   1 
ATOM   694  H HB2  . LYS   A 1 64  ? -4.839  10.136  16.102  1.00 36.68  ? 49  LYS   A HB2  1 
ATOM   695  H HB3  . LYS   A 1 64  ? -5.977  11.234  16.259  1.00 36.68  ? 49  LYS   A HB3  1 
ATOM   696  H HG2  . LYS   A 1 64  ? -5.209  12.316  14.359  1.00 36.14  ? 49  LYS   A HG2  1 
ATOM   697  H HG3  . LYS   A 1 64  ? -4.048  11.242  14.209  1.00 36.14  ? 49  LYS   A HG3  1 
ATOM   698  H HD2  . LYS   A 1 64  ? -5.829  9.596   13.997  1.00 37.06  ? 49  LYS   A HD2  1 
ATOM   699  H HD3  . LYS   A 1 64  ? -6.791  10.836  13.750  1.00 37.06  ? 49  LYS   A HD3  1 
ATOM   700  H HE2  . LYS   A 1 64  ? -5.580  11.425  11.861  1.00 40.16  ? 49  LYS   A HE2  1 
ATOM   701  H HE3  . LYS   A 1 64  ? -4.562  10.234  12.124  1.00 40.16  ? 49  LYS   A HE3  1 
ATOM   702  H HZ1  . LYS   A 1 64  ? -6.074  9.660   10.528  1.00 45.20  ? 49  LYS   A HZ1  1 
ATOM   703  H HZ2  . LYS   A 1 64  ? -6.246  8.781   11.667  1.00 45.20  ? 49  LYS   A HZ2  1 
ATOM   704  H HZ3  . LYS   A 1 64  ? -7.182  9.863   11.439  1.00 45.20  ? 49  LYS   A HZ3  1 
ATOM   705  N N    . MET   A 1 65  ? -4.812  11.996  19.199  1.00 28.45  ? 50  MET   A N    1 
ATOM   706  C CA   . MET   A 1 65  ? -4.832  11.585  20.601  1.00 31.89  ? 50  MET   A CA   1 
ATOM   707  C C    . MET   A 1 65  ? -5.869  10.491  20.841  1.00 35.18  ? 50  MET   A C    1 
ATOM   708  O O    . MET   A 1 65  ? -6.948  10.485  20.239  1.00 30.04  ? 50  MET   A O    1 
ATOM   709  C CB   . MET   A 1 65  ? -5.136  12.782  21.514  1.00 31.90  ? 50  MET   A CB   1 
ATOM   710  C CG   . MET   A 1 65  ? -4.101  13.903  21.473  1.00 32.56  ? 50  MET   A CG   1 
ATOM   711  S SD   . MET   A 1 65  ? -2.492  13.460  22.177  1.00 32.47  ? 50  MET   A SD   1 
ATOM   712  C CE   . MET   A 1 65  ? -1.633  12.810  20.739  1.00 28.79  ? 50  MET   A CE   1 
ATOM   713  H H    . MET   A 1 65  ? -5.296  12.687  19.031  1.00 34.14  ? 50  MET   A H    1 
ATOM   714  H HA   . MET   A 1 65  ? -3.953  11.242  20.826  1.00 38.27  ? 50  MET   A HA   1 
ATOM   715  H HB2  . MET   A 1 65  ? -5.988  13.162  21.249  1.00 38.28  ? 50  MET   A HB2  1 
ATOM   716  H HB3  . MET   A 1 65  ? -5.185  12.465  22.430  1.00 38.28  ? 50  MET   A HB3  1 
ATOM   717  H HG2  . MET   A 1 65  ? -3.956  14.158  20.548  1.00 39.07  ? 50  MET   A HG2  1 
ATOM   718  H HG3  . MET   A 1 65  ? -4.443  14.659  21.976  1.00 39.07  ? 50  MET   A HG3  1 
ATOM   719  H HE1  . MET   A 1 65  ? -0.679  12.815  20.912  1.00 34.55  ? 50  MET   A HE1  1 
ATOM   720  H HE2  . MET   A 1 65  ? -1.935  11.903  20.574  1.00 34.55  ? 50  MET   A HE2  1 
ATOM   721  H HE3  . MET   A 1 65  ? -1.833  13.370  19.972  1.00 34.55  ? 50  MET   A HE3  1 
ATOM   722  N N    . GLU   A 1 66  ? -5.528  9.556   21.732  1.00 35.01  ? 51  GLU   A N    1 
ATOM   723  C CA   . GLU   A 1 66  ? -6.465  8.558   22.217  1.00 31.58  ? 51  GLU   A CA   1 
ATOM   724  C C    . GLU   A 1 66  ? -7.201  9.098   23.433  1.00 36.30  ? 51  GLU   A C    1 
ATOM   725  O O    . GLU   A 1 66  ? -6.761  10.063  24.061  1.00 35.32  ? 51  GLU   A O    1 
ATOM   726  C CB   . GLU   A 1 66  ? -5.726  7.275   22.580  1.00 40.54  ? 51  GLU   A CB   1 
ATOM   727  C CG   . GLU   A 1 66  ? -4.851  6.710   21.469  1.00 39.15  ? 51  GLU   A CG   1 
ATOM   728  C CD   . GLU   A 1 66  ? -5.633  6.381   20.211  1.00 42.33  ? 51  GLU   A CD   1 
ATOM   729  O OE1  . GLU   A 1 66  ? -6.624  5.630   20.303  1.00 50.27  ? 51  GLU   A OE1  1 
ATOM   730  O OE2  . GLU   A 1 66  ? -5.257  6.881   19.130  1.00 50.47  ? 51  GLU   A OE2  1 
ATOM   731  H H    . GLU   A 1 66  ? -4.742  9.482   22.074  1.00 42.02  ? 51  GLU   A H    1 
ATOM   732  H HA   . GLU   A 1 66  ? -7.112  8.343   21.527  1.00 37.90  ? 51  GLU   A HA   1 
ATOM   733  H HB2  . GLU   A 1 66  ? -5.152  7.454   23.342  1.00 48.65  ? 51  GLU   A HB2  1 
ATOM   734  H HB3  . GLU   A 1 66  ? -6.380  6.596   22.811  1.00 48.65  ? 51  GLU   A HB3  1 
ATOM   735  H HG2  . GLU   A 1 66  ? -4.173  7.364   21.237  1.00 46.98  ? 51  GLU   A HG2  1 
ATOM   736  H HG3  . GLU   A 1 66  ? -4.430  5.894   21.782  1.00 46.98  ? 51  GLU   A HG3  1 
ATOM   737  N N    . PRO   A 1 67  ? -8.331  8.492   23.806  1.00 42.86  ? 52  PRO   A N    1 
ATOM   738  C CA   . PRO   A 1 67  ? -9.075  9.005   24.969  1.00 47.06  ? 52  PRO   A CA   1 
ATOM   739  C C    . PRO   A 1 67  ? -8.271  9.014   26.261  1.00 41.02  ? 52  PRO   A C    1 
ATOM   740  O O    . PRO   A 1 67  ? -8.494  9.891   27.104  1.00 48.12  ? 52  PRO   A O    1 
ATOM   741  C CB   . PRO   A 1 67  ? -10.278 8.056   25.059  1.00 43.00  ? 52  PRO   A CB   1 
ATOM   742  C CG   . PRO   A 1 67  ? -10.424 7.493   23.681  1.00 42.42  ? 52  PRO   A CG   1 
ATOM   743  C CD   . PRO   A 1 67  ? -9.036  7.386   23.138  1.00 40.54  ? 52  PRO   A CD   1 
ATOM   744  H HA   . PRO   A 1 67  ? -9.385  9.905   24.786  1.00 56.47  ? 52  PRO   A HA   1 
ATOM   745  H HB2  . PRO   A 1 67  ? -10.099 7.354   25.704  1.00 51.60  ? 52  PRO   A HB2  1 
ATOM   746  H HB3  . PRO   A 1 67  ? -11.071 8.551   25.319  1.00 51.60  ? 52  PRO   A HB3  1 
ATOM   747  H HG2  . PRO   A 1 67  ? -10.844 6.620   23.727  1.00 50.90  ? 52  PRO   A HG2  1 
ATOM   748  H HG3  . PRO   A 1 67  ? -10.960 8.092   23.138  1.00 50.90  ? 52  PRO   A HG3  1 
ATOM   749  H HD2  . PRO   A 1 67  ? -8.639  6.532   23.370  1.00 48.65  ? 52  PRO   A HD2  1 
ATOM   750  H HD3  . PRO   A 1 67  ? -9.032  7.503   22.175  1.00 48.65  ? 52  PRO   A HD3  1 
ATOM   751  N N    . ASP   A 1 68  ? -7.336  8.082   26.442  1.00 43.61  ? 53  ASP   A N    1 
ATOM   752  C CA   . ASP   A 1 68  ? -6.542  8.004   27.661  1.00 47.07  ? 53  ASP   A CA   1 
ATOM   753  C C    . ASP   A 1 68  ? -5.191  8.704   27.566  1.00 44.98  ? 53  ASP   A C    1 
ATOM   754  O O    . ASP   A 1 68  ? -4.423  8.660   28.533  1.00 38.76  ? 53  ASP   A O    1 
ATOM   755  C CB   . ASP   A 1 68  ? -6.303  6.539   28.047  1.00 51.73  ? 53  ASP   A CB   1 
ATOM   756  C CG   . ASP   A 1 68  ? -7.537  5.874   28.603  1.00 58.64  ? 53  ASP   A CG   1 
ATOM   757  O OD1  . ASP   A 1 68  ? -8.429  6.593   29.104  1.00 57.07  ? 53  ASP   A OD1  1 
ATOM   758  O OD2  . ASP   A 1 68  ? -7.611  4.627   28.547  1.00 70.28  ? 53  ASP   A OD2  1 
ATOM   759  H H    . ASP   A 1 68  ? -7.143  7.476   25.863  1.00 52.33  ? 53  ASP   A H    1 
ATOM   760  H HA   . ASP   A 1 68  ? -7.052  8.435   28.365  1.00 56.48  ? 53  ASP   A HA   1 
ATOM   761  H HB2  . ASP   A 1 68  ? -6.026  6.046   27.259  1.00 62.07  ? 53  ASP   A HB2  1 
ATOM   762  H HB3  . ASP   A 1 68  ? -5.610  6.500   28.724  1.00 62.07  ? 53  ASP   A HB3  1 
ATOM   763  N N    . ASP   A 1 69  ? -4.871  9.338   26.443  1.00 36.29  ? 54  ASP   A N    1 
ATOM   764  C CA   . ASP   A 1 69  ? -3.544  9.918   26.300  1.00 34.19  ? 54  ASP   A CA   1 
ATOM   765  C C    . ASP   A 1 69  ? -3.358  11.090  27.256  1.00 40.73  ? 54  ASP   A C    1 
ATOM   766  O O    . ASP   A 1 69  ? -4.287  11.846  27.546  1.00 39.43  ? 54  ASP   A O    1 
ATOM   767  C CB   . ASP   A 1 69  ? -3.300  10.359  24.861  1.00 36.40  ? 54  ASP   A CB   1 
ATOM   768  C CG   . ASP   A 1 69  ? -2.748  9.229   23.994  1.00 38.26  ? 54  ASP   A CG   1 
ATOM   769  O OD1  . ASP   A 1 69  ? -2.016  8.367   24.531  1.00 34.72  ? 54  ASP   A OD1  1 
ATOM   770  O OD2  . ASP   A 1 69  ? -3.039  9.205   22.779  1.00 35.01  ? 54  ASP   A OD2  1 
ATOM   771  H H    . ASP   A 1 69  ? -5.392  9.443   25.766  1.00 43.55  ? 54  ASP   A H    1 
ATOM   772  H HA   . ASP   A 1 69  ? -2.878  9.248   26.520  1.00 41.02  ? 54  ASP   A HA   1 
ATOM   773  H HB2  . ASP   A 1 69  ? -4.138  10.655  24.473  1.00 43.68  ? 54  ASP   A HB2  1 
ATOM   774  H HB3  . ASP   A 1 69  ? -2.657  11.086  24.856  1.00 43.68  ? 54  ASP   A HB3  1 
ATOM   775  N N    . ASP   A 1 70  ? -2.128  11.229  27.745  1.00 41.82  ? 55  ASP   A N    1 
ATOM   776  C CA   . ASP   A 1 70  ? -1.761  12.224  28.750  1.00 40.28  ? 55  ASP   A CA   1 
ATOM   777  C C    . ASP   A 1 70  ? -0.504  12.929  28.251  1.00 36.31  ? 55  ASP   A C    1 
ATOM   778  O O    . ASP   A 1 70  ? 0.597   12.380  28.350  1.00 36.23  ? 55  ASP   A O    1 
ATOM   779  C CB   . ASP   A 1 70  ? -1.539  11.559  30.105  1.00 37.24  ? 55  ASP   A CB   1 
ATOM   780  C CG   . ASP   A 1 70  ? -1.151  12.546  31.188  1.00 47.63  ? 55  ASP   A CG   1 
ATOM   781  O OD1  . ASP   A 1 70  ? -1.075  13.759  30.892  1.00 41.79  ? 55  ASP   A OD1  1 
ATOM   782  O OD2  . ASP   A 1 70  ? -0.915  12.110  32.339  1.00 41.70  ? 55  ASP   A OD2  1 
ATOM   783  H H    . ASP   A 1 70  ? -1.464  10.740  27.500  1.00 50.18  ? 55  ASP   A H    1 
ATOM   784  H HA   . ASP   A 1 70  ? -2.466  12.884  28.846  1.00 48.33  ? 55  ASP   A HA   1 
ATOM   785  H HB2  . ASP   A 1 70  ? -2.359  11.120  30.380  1.00 44.69  ? 55  ASP   A HB2  1 
ATOM   786  H HB3  . ASP   A 1 70  ? -0.825  10.907  30.024  1.00 44.69  ? 55  ASP   A HB3  1 
ATOM   787  N N    . VAL   A 1 71  ? -0.667  14.143  27.706  1.00 37.87  ? 56  VAL   A N    1 
ATOM   788  C CA   . VAL   A 1 71  ? 0.464   14.863  27.133  1.00 33.98  ? 56  VAL   A CA   1 
ATOM   789  C C    . VAL   A 1 71  ? 1.510   15.229  28.173  1.00 34.73  ? 56  VAL   A C    1 
ATOM   790  O O    . VAL   A 1 71  ? 2.665   15.483  27.821  1.00 34.15  ? 56  VAL   A O    1 
ATOM   791  C CB   . VAL   A 1 71  ? 0.011   16.145  26.397  1.00 38.10  ? 56  VAL   A CB   1 
ATOM   792  C CG1  . VAL   A 1 71  ? -0.679  15.797  25.091  1.00 38.49  ? 56  VAL   A CG1  1 
ATOM   793  C CG2  . VAL   A 1 71  ? -0.898  16.998  27.287  1.00 41.37  ? 56  VAL   A CG2  1 
ATOM   794  H H    . VAL   A 1 71  ? -1.416  14.562  27.660  1.00 45.45  ? 56  VAL   A H    1 
ATOM   795  H HA   . VAL   A 1 71  ? 0.863   14.260  26.486  1.00 40.78  ? 56  VAL   A HA   1 
ATOM   796  H HB   . VAL   A 1 71  ? 0.796   16.675  26.189  1.00 45.72  ? 56  VAL   A HB   1 
ATOM   797  H HG11 . VAL   A 1 71  ? -0.960  16.616  24.654  1.00 46.18  ? 56  VAL   A HG11 1 
ATOM   798  H HG12 . VAL   A 1 71  ? -0.057  15.316  24.524  1.00 46.18  ? 56  VAL   A HG12 1 
ATOM   799  H HG13 . VAL   A 1 71  ? -1.452  15.242  25.280  1.00 46.18  ? 56  VAL   A HG13 1 
ATOM   800  H HG21 . VAL   A 1 71  ? -1.003  17.874  26.883  1.00 49.64  ? 56  VAL   A HG21 1 
ATOM   801  H HG22 . VAL   A 1 71  ? -1.761  16.564  27.365  1.00 49.64  ? 56  VAL   A HG22 1 
ATOM   802  H HG23 . VAL   A 1 71  ? -0.490  17.084  28.163  1.00 49.64  ? 56  VAL   A HG23 1 
ATOM   803  N N    . SER   A 1 72  ? 1.132   15.282  29.455  1.00 36.09  ? 57  SER   A N    1 
ATOM   804  C CA   . SER   A 1 72  ? 2.110   15.604  30.488  1.00 36.89  ? 57  SER   A CA   1 
ATOM   805  C C    . SER   A 1 72  ? 3.192   14.541  30.589  1.00 36.77  ? 57  SER   A C    1 
ATOM   806  O O    . SER   A 1 72  ? 4.296   14.833  31.063  1.00 36.85  ? 57  SER   A O    1 
ATOM   807  C CB   . SER   A 1 72  ? 1.420   15.783  31.844  1.00 40.80  ? 57  SER   A CB   1 
ATOM   808  O OG   . SER   A 1 72  ? 0.860   14.567  32.318  1.00 40.10  ? 57  SER   A OG   1 
ATOM   809  H H    . SER   A 1 72  ? 0.334   15.139  29.743  1.00 43.30  ? 57  SER   A H    1 
ATOM   810  H HA   . SER   A 1 72  ? 2.534   16.448  30.264  1.00 44.26  ? 57  SER   A HA   1 
ATOM   811  H HB2  . SER   A 1 72  ? 2.074   16.097  32.488  1.00 48.96  ? 57  SER   A HB2  1 
ATOM   812  H HB3  . SER   A 1 72  ? 0.709   16.436  31.748  1.00 48.96  ? 57  SER   A HB3  1 
ATOM   813  H HG   . SER   A 1 72  ? 0.055   14.511  32.086  1.00 48.12  ? 57  SER   A HG   1 
ATOM   814  N N    . THR   A 1 73  ? 2.911   13.316  30.138  1.00 36.11  ? 58  THR   A N    1 
ATOM   815  C CA   . THR   A 1 73  ? 3.933   12.281  30.108  1.00 35.81  ? 58  THR   A CA   1 
ATOM   816  C C    . THR   A 1 73  ? 5.005   12.553  29.061  1.00 36.82  ? 58  THR   A C    1 
ATOM   817  O O    . THR   A 1 73  ? 5.989   11.810  29.009  1.00 34.43  ? 58  THR   A O    1 
ATOM   818  C CB   . THR   A 1 73  ? 3.304   10.913  29.832  1.00 36.35  ? 58  THR   A CB   1 
ATOM   819  O OG1  . THR   A 1 73  ? 2.734   10.908  28.518  1.00 34.52  ? 58  THR   A OG1  1 
ATOM   820  C CG2  . THR   A 1 73  ? 2.225   10.598  30.852  1.00 36.86  ? 58  THR   A CG2  1 
ATOM   821  H H    . THR   A 1 73  ? 2.141   13.066  29.848  1.00 43.34  ? 58  THR   A H    1 
ATOM   822  H HA   . THR   A 1 73  ? 4.355   12.247  30.981  1.00 42.97  ? 58  THR   A HA   1 
ATOM   823  H HB   . THR   A 1 73  ? 3.986   10.227  29.894  1.00 43.63  ? 58  THR   A HB   1 
ATOM   824  H HG1  . THR   A 1 73  ? 2.143   11.502  28.458  1.00 41.42  ? 58  THR   A HG1  1 
ATOM   825  H HG21 . THR   A 1 73  ? 1.899   9.694   30.722  1.00 44.23  ? 58  THR   A HG21 1 
ATOM   826  H HG22 . THR   A 1 73  ? 2.583   10.678  31.750  1.00 44.23  ? 58  THR   A HG22 1 
ATOM   827  H HG23 . THR   A 1 73  ? 1.484   11.216  30.753  1.00 44.23  ? 58  THR   A HG23 1 
ATOM   828  N N    . LEU   A 1 74  ? 4.824   13.579  28.227  1.00 36.63  ? 59  LEU   A N    1 
ATOM   829  C CA   . LEU   A 1 74  ? 5.780   13.965  27.199  1.00 32.90  ? 59  LEU   A CA   1 
ATOM   830  C C    . LEU   A 1 74  ? 6.680   15.114  27.638  1.00 36.60  ? 59  LEU   A C    1 
ATOM   831  O O    . LEU   A 1 74  ? 7.461   15.621  26.825  1.00 37.60  ? 59  LEU   A O    1 
ATOM   832  C CB   . LEU   A 1 74  ? 5.045   14.374  25.920  1.00 37.60  ? 59  LEU   A CB   1 
ATOM   833  C CG   . LEU   A 1 74  ? 4.150   13.346  25.230  1.00 43.14  ? 59  LEU   A CG   1 
ATOM   834  C CD1  . LEU   A 1 74  ? 3.406   13.997  24.074  1.00 44.42  ? 59  LEU   A CD1  1 
ATOM   835  C CD2  . LEU   A 1 74  ? 4.968   12.171  24.733  1.00 38.98  ? 59  LEU   A CD2  1 
ATOM   836  H H    . LEU   A 1 74  ? 4.127   14.084  28.240  1.00 43.95  ? 59  LEU   A H    1 
ATOM   837  H HA   . LEU   A 1 74  ? 6.337   13.195  27.005  1.00 39.48  ? 59  LEU   A HA   1 
ATOM   838  H HB2  . LEU   A 1 74  ? 4.479   15.131  26.137  1.00 45.12  ? 59  LEU   A HB2  1 
ATOM   839  H HB3  . LEU   A 1 74  ? 5.715   14.637  25.269  1.00 45.12  ? 59  LEU   A HB3  1 
ATOM   840  H HG   . LEU   A 1 74  ? 3.501   13.011  25.868  1.00 51.77  ? 59  LEU   A HG   1 
ATOM   841  H HD11 . LEU   A 1 74  ? 2.914   13.314  23.591  1.00 53.30  ? 59  LEU   A HD11 1 
ATOM   842  H HD12 . LEU   A 1 74  ? 2.793   14.660  24.427  1.00 53.30  ? 59  LEU   A HD12 1 
ATOM   843  H HD13 . LEU   A 1 74  ? 4.049   14.421  23.484  1.00 53.30  ? 59  LEU   A HD13 1 
ATOM   844  H HD21 . LEU   A 1 74  ? 4.385   11.559  24.258  1.00 46.78  ? 59  LEU   A HD21 1 
ATOM   845  H HD22 . LEU   A 1 74  ? 5.661   12.498  24.138  1.00 46.78  ? 59  LEU   A HD22 1 
ATOM   846  H HD23 . LEU   A 1 74  ? 5.370   11.722  25.494  1.00 46.78  ? 59  LEU   A HD23 1 
ATOM   847  N N    . GLN   A 1 75  ? 6.588   15.532  28.901  1.00 37.49  ? 60  GLN   A N    1 
ATOM   848  C CA   . GLN   A 1 75  ? 7.232   16.772  29.324  1.00 43.53  ? 60  GLN   A CA   1 
ATOM   849  C C    . GLN   A 1 75  ? 8.743   16.708  29.145  1.00 41.05  ? 60  GLN   A C    1 
ATOM   850  O O    . GLN   A 1 75  ? 9.367   17.681  28.702  1.00 34.24  ? 60  GLN   A O    1 
ATOM   851  C CB   . GLN   A 1 75  ? 6.878   17.067  30.782  1.00 46.47  ? 60  GLN   A CB   1 
ATOM   852  C CG   . GLN   A 1 75  ? 7.204   18.486  31.227  1.00 54.66  ? 60  GLN   A CG   1 
ATOM   853  C CD   . GLN   A 1 75  ? 6.830   18.728  32.677  1.00 64.75  ? 60  GLN   A CD   1 
ATOM   854  O OE1  . GLN   A 1 75  ? 6.909   17.816  33.501  1.00 66.32  ? 60  GLN   A OE1  1 
ATOM   855  N NE2  . GLN   A 1 75  ? 6.407   19.953  32.995  1.00 62.84  ? 60  GLN   A NE2  1 
ATOM   856  H H    . GLN   A 1 75  ? 6.164   15.121  29.526  1.00 44.99  ? 60  GLN   A H    1 
ATOM   857  H HA   . GLN   A 1 75  ? 6.900   17.499  28.774  1.00 52.24  ? 60  GLN   A HA   1 
ATOM   858  H HB2  . GLN   A 1 75  ? 5.925   16.932  30.903  1.00 55.76  ? 60  GLN   A HB2  1 
ATOM   859  H HB3  . GLN   A 1 75  ? 7.374   16.458  31.351  1.00 55.76  ? 60  GLN   A HB3  1 
ATOM   860  H HG2  . GLN   A 1 75  ? 8.157   18.639  31.131  1.00 65.59  ? 60  GLN   A HG2  1 
ATOM   861  H HG3  . GLN   A 1 75  ? 6.709   19.114  30.678  1.00 65.59  ? 60  GLN   A HG3  1 
ATOM   862  H HE21 . GLN   A 1 75  ? 6.357   20.562  32.389  1.00 75.40  ? 60  GLN   A HE21 1 
ATOM   863  H HE22 . GLN   A 1 75  ? 6.185   20.135  33.806  1.00 75.40  ? 60  GLN   A HE22 1 
ATOM   864  N N    . LYS   A 1 76  ? 9.353   15.570  29.478  1.00 40.86  ? 61  LYS   A N    1 
ATOM   865  C CA   . LYS   A 1 76  ? 10.806  15.474  29.383  1.00 45.31  ? 61  LYS   A CA   1 
ATOM   866  C C    . LYS   A 1 76  ? 11.275  15.360  27.938  1.00 42.77  ? 61  LYS   A C    1 
ATOM   867  O O    . LYS   A 1 76  ? 12.341  15.885  27.595  1.00 39.79  ? 61  LYS   A O    1 
ATOM   868  C CB   . LYS   A 1 76  ? 11.309  14.298  30.221  1.00 47.51  ? 61  LYS   A CB   1 
ATOM   869  C CG   . LYS   A 1 76  ? 11.692  14.713  31.643  1.00 56.18  ? 61  LYS   A CG   1 
ATOM   870  C CD   . LYS   A 1 76  ? 11.509  13.594  32.658  1.00 59.42  ? 61  LYS   A CD   1 
ATOM   871  C CE   . LYS   A 1 76  ? 11.732  14.102  34.082  1.00 57.99  ? 61  LYS   A CE   1 
ATOM   872  N NZ   . LYS   A 1 76  ? 11.166  13.182  35.112  1.00 65.28  ? 61  LYS   A NZ   1 
ATOM   873  H H    . LYS   A 1 76  ? 8.958   14.858  29.753  1.00 49.03  ? 61  LYS   A H    1 
ATOM   874  H HA   . LYS   A 1 76  ? 11.198  16.282  29.750  1.00 54.37  ? 61  LYS   A HA   1 
ATOM   875  H HB2  . LYS   A 1 76  ? 10.609  13.629  30.280  1.00 57.01  ? 61  LYS   A HB2  1 
ATOM   876  H HB3  . LYS   A 1 76  ? 12.094  13.919  29.795  1.00 57.01  ? 61  LYS   A HB3  1 
ATOM   877  H HG2  . LYS   A 1 76  ? 12.626  14.977  31.654  1.00 67.41  ? 61  LYS   A HG2  1 
ATOM   878  H HG3  . LYS   A 1 76  ? 11.134  15.458  31.916  1.00 67.41  ? 61  LYS   A HG3  1 
ATOM   879  H HD2  . LYS   A 1 76  ? 10.606  13.245  32.594  1.00 71.31  ? 61  LYS   A HD2  1 
ATOM   880  H HD3  . LYS   A 1 76  ? 12.150  12.888  32.480  1.00 71.31  ? 61  LYS   A HD3  1 
ATOM   881  H HE2  . LYS   A 1 76  ? 12.685  14.185  34.244  1.00 69.59  ? 61  LYS   A HE2  1 
ATOM   882  H HE3  . LYS   A 1 76  ? 11.302  14.966  34.182  1.00 69.59  ? 61  LYS   A HE3  1 
ATOM   883  H HZ1  . LYS   A 1 76  ? 11.312  13.509  35.927  1.00 78.34  ? 61  LYS   A HZ1  1 
ATOM   884  H HZ2  . LYS   A 1 76  ? 10.288  13.092  34.991  1.00 78.34  ? 61  LYS   A HZ2  1 
ATOM   885  H HZ3  . LYS   A 1 76  ? 11.550  12.381  35.049  1.00 78.34  ? 61  LYS   A HZ3  1 
ATOM   886  N N    . GLU   A 1 77  ? 10.501  14.707  27.069  1.00 39.07  ? 62  GLU   A N    1 
ATOM   887  C CA   . GLU   A 1 77  ? 10.888  14.657  25.661  1.00 39.94  ? 62  GLU   A CA   1 
ATOM   888  C C    . GLU   A 1 77  ? 10.764  16.033  25.015  1.00 37.31  ? 62  GLU   A C    1 
ATOM   889  O O    . GLU   A 1 77  ? 11.574  16.399  24.158  1.00 35.56  ? 62  GLU   A O    1 
ATOM   890  C CB   . GLU   A 1 77  ? 10.041  13.631  24.908  1.00 42.29  ? 62  GLU   A CB   1 
ATOM   891  C CG   . GLU   A 1 77  ? 10.282  12.179  25.329  1.00 46.60  ? 62  GLU   A CG   1 
ATOM   892  C CD   . GLU   A 1 77  ? 11.597  11.619  24.811  1.00 49.61  ? 62  GLU   A CD   1 
ATOM   893  O OE1  . GLU   A 1 77  ? 12.021  12.010  23.698  1.00 40.81  ? 62  GLU   A OE1  1 
ATOM   894  O OE2  . GLU   A 1 77  ? 12.209  10.787  25.516  1.00 44.80  ? 62  GLU   A OE2  1 
ATOM   895  H H    . GLU   A 1 77  ? 9.770   14.298  27.264  1.00 46.89  ? 62  GLU   A H    1 
ATOM   896  H HA   . GLU   A 1 77  ? 11.814  14.372  25.602  1.00 47.93  ? 62  GLU   A HA   1 
ATOM   897  H HB2  . GLU   A 1 77  ? 9.104   13.830  25.064  1.00 50.75  ? 62  GLU   A HB2  1 
ATOM   898  H HB3  . GLU   A 1 77  ? 10.242  13.699  23.962  1.00 50.75  ? 62  GLU   A HB3  1 
ATOM   899  H HG2  . GLU   A 1 77  ? 10.297  12.130  26.297  1.00 55.92  ? 62  GLU   A HG2  1 
ATOM   900  H HG3  . GLU   A 1 77  ? 9.564   11.627  24.980  1.00 55.92  ? 62  GLU   A HG3  1 
ATOM   901  N N    . ILE   A 1 78  ? 9.762   16.814  25.426  1.00 39.36  ? 63  ILE   A N    1 
ATOM   902  C CA   . ILE   A 1 78  ? 9.577   18.149  24.868  1.00 31.64  ? 63  ILE   A CA   1 
ATOM   903  C C    . ILE   A 1 78  ? 10.708  19.070  25.310  1.00 37.00  ? 63  ILE   A C    1 
ATOM   904  O O    . ILE   A 1 78  ? 11.176  19.916  24.540  1.00 33.56  ? 63  ILE   A O    1 
ATOM   905  C CB   . ILE   A 1 78  ? 8.201   18.706  25.275  1.00 38.43  ? 63  ILE   A CB   1 
ATOM   906  C CG1  . ILE   A 1 78  ? 7.076   17.913  24.605  1.00 39.69  ? 63  ILE   A CG1  1 
ATOM   907  C CG2  . ILE   A 1 78  ? 8.098   20.188  24.938  1.00 46.82  ? 63  ILE   A CG2  1 
ATOM   908  C CD1  . ILE   A 1 78  ? 6.922   18.171  23.139  1.00 45.53  ? 63  ILE   A CD1  1 
ATOM   909  H H    . ILE   A 1 78  ? 9.182   16.595  26.022  1.00 47.23  ? 63  ILE   A H    1 
ATOM   910  H HA   . ILE   A 1 78  ? 9.603   18.088  23.900  1.00 37.96  ? 63  ILE   A HA   1 
ATOM   911  H HB   . ILE   A 1 78  ? 8.108   18.607  26.236  1.00 46.12  ? 63  ILE   A HB   1 
ATOM   912  H HG12 . ILE   A 1 78  ? 7.256   16.966  24.718  1.00 47.63  ? 63  ILE   A HG12 1 
ATOM   913  H HG13 . ILE   A 1 78  ? 6.237   18.145  25.032  1.00 47.63  ? 63  ILE   A HG13 1 
ATOM   914  H HG21 . ILE   A 1 78  ? 7.163   20.447  24.932  1.00 56.18  ? 63  ILE   A HG21 1 
ATOM   915  H HG22 . ILE   A 1 78  ? 8.578   20.699  25.609  1.00 56.18  ? 63  ILE   A HG22 1 
ATOM   916  H HG23 . ILE   A 1 78  ? 8.489   20.341  24.064  1.00 56.18  ? 63  ILE   A HG23 1 
ATOM   917  H HD11 . ILE   A 1 78  ? 6.269   17.553  22.776  1.00 54.63  ? 63  ILE   A HD11 1 
ATOM   918  H HD12 . ILE   A 1 78  ? 6.622   19.084  23.009  1.00 54.63  ? 63  ILE   A HD12 1 
ATOM   919  H HD13 . ILE   A 1 78  ? 7.779   18.039  22.703  1.00 54.63  ? 63  ILE   A HD13 1 
ATOM   920  N N    . LEU   A 1 79  ? 11.165  18.924  26.553  1.00 38.89  ? 64  LEU   A N    1 
ATOM   921  C CA   . LEU   A 1 79  ? 12.286  19.730  27.020  1.00 41.04  ? 64  LEU   A CA   1 
ATOM   922  C C    . LEU   A 1 79  ? 13.543  19.456  26.203  1.00 45.11  ? 64  LEU   A C    1 
ATOM   923  O O    . LEU   A 1 79  ? 14.313  20.378  25.907  1.00 40.76  ? 64  LEU   A O    1 
ATOM   924  C CB   . LEU   A 1 79  ? 12.543  19.456  28.498  1.00 45.17  ? 64  LEU   A CB   1 
ATOM   925  C CG   . LEU   A 1 79  ? 13.607  20.340  29.149  1.00 58.63  ? 64  LEU   A CG   1 
ATOM   926  C CD1  . LEU   A 1 79  ? 13.163  21.800  29.147  1.00 54.56  ? 64  LEU   A CD1  1 
ATOM   927  C CD2  . LEU   A 1 79  ? 13.909  19.860  30.566  1.00 53.24  ? 64  LEU   A CD2  1 
ATOM   928  H H    . LEU   A 1 79  ? 10.849  18.375  27.134  1.00 46.67  ? 64  LEU   A H    1 
ATOM   929  H HA   . LEU   A 1 79  ? 12.059  20.668  26.919  1.00 49.25  ? 64  LEU   A HA   1 
ATOM   930  H HB2  . LEU   A 1 79  ? 11.714  19.593  28.983  1.00 54.21  ? 64  LEU   A HB2  1 
ATOM   931  H HB3  . LEU   A 1 79  ? 12.834  18.535  28.591  1.00 54.21  ? 64  LEU   A HB3  1 
ATOM   932  H HG   . LEU   A 1 79  ? 14.428  20.280  28.636  1.00 70.35  ? 64  LEU   A HG   1 
ATOM   933  H HD11 . LEU   A 1 79  ? 13.782  22.318  29.686  1.00 65.48  ? 64  LEU   A HD11 1 
ATOM   934  H HD12 . LEU   A 1 79  ? 13.163  22.129  28.235  1.00 65.48  ? 64  LEU   A HD12 1 
ATOM   935  H HD13 . LEU   A 1 79  ? 12.270  21.859  29.520  1.00 65.48  ? 64  LEU   A HD13 1 
ATOM   936  H HD21 . LEU   A 1 79  ? 14.587  20.434  30.955  1.00 63.88  ? 64  LEU   A HD21 1 
ATOM   937  H HD22 . LEU   A 1 79  ? 13.096  19.902  31.093  1.00 63.88  ? 64  LEU   A HD22 1 
ATOM   938  H HD23 . LEU   A 1 79  ? 14.232  18.946  30.527  1.00 63.88  ? 64  LEU   A HD23 1 
ATOM   939  N N    . ILE   A 1 80  ? 13.777  18.189  25.844  1.00 31.85  ? 65  ILE   A N    1 
ATOM   940  C CA   . ILE   A 1 80  ? 14.925  17.842  25.011  1.00 37.54  ? 65  ILE   A CA   1 
ATOM   941  C C    . ILE   A 1 80  ? 14.801  18.480  23.631  1.00 36.13  ? 65  ILE   A C    1 
ATOM   942  O O    . ILE   A 1 80  ? 15.776  19.013  23.089  1.00 40.66  ? 65  ILE   A O    1 
ATOM   943  C CB   . ILE   A 1 80  ? 15.071  16.309  24.907  1.00 34.27  ? 65  ILE   A CB   1 
ATOM   944  C CG1  . ILE   A 1 80  ? 15.616  15.734  26.218  1.00 32.15  ? 65  ILE   A CG1  1 
ATOM   945  C CG2  . ILE   A 1 80  ? 15.952  15.931  23.710  1.00 39.32  ? 65  ILE   A CG2  1 
ATOM   946  C CD1  . ILE   A 1 80  ? 15.625  14.216  26.258  1.00 40.18  ? 65  ILE   A CD1  1 
ATOM   947  H H    . ILE   A 1 80  ? 13.289  17.518  26.070  1.00 38.22  ? 65  ILE   A H    1 
ATOM   948  H HA   . ILE   A 1 80  ? 15.723  18.195  25.434  1.00 45.05  ? 65  ILE   A HA   1 
ATOM   949  H HB   . ILE   A 1 80  ? 14.193  15.923  24.758  1.00 41.12  ? 65  ILE   A HB   1 
ATOM   950  H HG12 . ILE   A 1 80  ? 16.529  16.039  26.337  1.00 38.58  ? 65  ILE   A HG12 1 
ATOM   951  H HG13 . ILE   A 1 80  ? 15.063  16.048  26.951  1.00 38.58  ? 65  ILE   A HG13 1 
ATOM   952  H HG21 . ILE   A 1 80  ? 16.222  15.003  23.797  1.00 47.18  ? 65  ILE   A HG21 1 
ATOM   953  H HG22 . ILE   A 1 80  ? 15.444  16.052  22.892  1.00 47.18  ? 65  ILE   A HG22 1 
ATOM   954  H HG23 . ILE   A 1 80  ? 16.735  16.504  23.700  1.00 47.18  ? 65  ILE   A HG23 1 
ATOM   955  H HD11 . ILE   A 1 80  ? 15.805  13.925  27.166  1.00 48.22  ? 65  ILE   A HD11 1 
ATOM   956  H HD12 . ILE   A 1 80  ? 14.758  13.888  25.972  1.00 48.22  ? 65  ILE   A HD12 1 
ATOM   957  H HD13 . ILE   A 1 80  ? 16.316  13.888  25.662  1.00 48.22  ? 65  ILE   A HD13 1 
ATOM   958  N N    . LEU   A 1 81  ? 13.608  18.413  23.029  1.00 30.82  ? 66  LEU   A N    1 
ATOM   959  C CA   . LEU   A 1 81  ? 13.390  19.050  21.735  1.00 28.83  ? 66  LEU   A CA   1 
ATOM   960  C C    . LEU   A 1 81  ? 13.641  20.550  21.789  1.00 30.72  ? 66  LEU   A C    1 
ATOM   961  O O    . LEU   A 1 81  ? 14.076  21.141  20.792  1.00 31.24  ? 66  LEU   A O    1 
ATOM   962  C CB   . LEU   A 1 81  ? 11.967  18.782  21.250  1.00 28.26  ? 66  LEU   A CB   1 
ATOM   963  C CG   . LEU   A 1 81  ? 11.730  17.399  20.644  1.00 33.07  ? 66  LEU   A CG   1 
ATOM   964  C CD1  . LEU   A 1 81  ? 10.249  17.145  20.424  1.00 32.15  ? 66  LEU   A CD1  1 
ATOM   965  C CD2  . LEU   A 1 81  ? 12.494  17.255  19.330  1.00 37.10  ? 66  LEU   A CD2  1 
ATOM   966  H H    . LEU   A 1 81  ? 12.918  18.010  23.347  1.00 36.99  ? 66  LEU   A H    1 
ATOM   967  H HA   . LEU   A 1 81  ? 14.011  18.664  21.098  1.00 34.60  ? 66  LEU   A HA   1 
ATOM   968  H HB2  . LEU   A 1 81  ? 11.365  18.874  22.005  1.00 33.91  ? 66  LEU   A HB2  1 
ATOM   969  H HB3  . LEU   A 1 81  ? 11.748  19.438  20.570  1.00 33.91  ? 66  LEU   A HB3  1 
ATOM   970  H HG   . LEU   A 1 81  ? 12.056  16.729  21.264  1.00 39.68  ? 66  LEU   A HG   1 
ATOM   971  H HD11 . LEU   A 1 81  ? 10.133  16.259  20.046  1.00 38.58  ? 66  LEU   A HD11 1 
ATOM   972  H HD12 . LEU   A 1 81  ? 9.789   17.204  21.276  1.00 38.58  ? 66  LEU   A HD12 1 
ATOM   973  H HD13 . LEU   A 1 81  ? 9.902   17.813  19.813  1.00 38.58  ? 66  LEU   A HD13 1 
ATOM   974  H HD21 . LEU   A 1 81  ? 12.180  16.463  18.867  1.00 44.52  ? 66  LEU   A HD21 1 
ATOM   975  H HD22 . LEU   A 1 81  ? 12.335  18.042  18.785  1.00 44.52  ? 66  LEU   A HD22 1 
ATOM   976  H HD23 . LEU   A 1 81  ? 13.441  17.172  19.524  1.00 44.52  ? 66  LEU   A HD23 1 
ATOM   977  N N    . LYS   A 1 82  ? 13.360  21.187  22.929  1.00 30.30  ? 67  LYS   A N    1 
ATOM   978  C CA   . LYS   A 1 82  ? 13.565  22.624  23.061  1.00 30.31  ? 67  LYS   A CA   1 
ATOM   979  C C    . LYS   A 1 82  ? 15.042  22.968  23.220  1.00 38.75  ? 67  LYS   A C    1 
ATOM   980  O O    . LYS   A 1 82  ? 15.502  23.995  22.714  1.00 44.61  ? 67  LYS   A O    1 
ATOM   981  C CB   . LYS   A 1 82  ? 12.797  23.171  24.269  1.00 42.45  ? 67  LYS   A CB   1 
ATOM   982  C CG   . LYS   A 1 82  ? 11.299  23.331  24.084  1.00 47.12  ? 67  LYS   A CG   1 
ATOM   983  C CD   . LYS   A 1 82  ? 10.711  24.158  25.231  1.00 49.57  ? 67  LYS   A CD   1 
ATOM   984  C CE   . LYS   A 1 82  ? 9.250   24.508  24.998  1.00 63.00  ? 67  LYS   A CE   1 
ATOM   985  N NZ   . LYS   A 1 82  ? 8.751   25.476  26.020  1.00 72.56  ? 67  LYS   A NZ   1 
ATOM   986  H H    . LYS   A 1 82  ? 13.050  20.809  23.637  1.00 36.36  ? 67  LYS   A H    1 
ATOM   987  H HA   . LYS   A 1 82  ? 13.224  23.046  22.257  1.00 36.37  ? 67  LYS   A HA   1 
ATOM   988  H HB2  . LYS   A 1 82  ? 12.931  22.565  25.015  1.00 50.94  ? 67  LYS   A HB2  1 
ATOM   989  H HB3  . LYS   A 1 82  ? 13.154  24.047  24.485  1.00 50.94  ? 67  LYS   A HB3  1 
ATOM   990  H HG2  . LYS   A 1 82  ? 11.120  23.788  23.248  1.00 56.55  ? 67  LYS   A HG2  1 
ATOM   991  H HG3  . LYS   A 1 82  ? 10.875  22.458  24.082  1.00 56.55  ? 67  LYS   A HG3  1 
ATOM   992  H HD2  . LYS   A 1 82  ? 10.772  23.649  26.055  1.00 59.48  ? 67  LYS   A HD2  1 
ATOM   993  H HD3  . LYS   A 1 82  ? 11.210  24.986  25.315  1.00 59.48  ? 67  LYS   A HD3  1 
ATOM   994  H HE2  . LYS   A 1 82  ? 9.152   24.913  24.122  1.00 75.60  ? 67  LYS   A HE2  1 
ATOM   995  H HE3  . LYS   A 1 82  ? 8.713   23.702  25.054  1.00 75.60  ? 67  LYS   A HE3  1 
ATOM   996  H HZ1  . LYS   A 1 82  ? 7.896   25.668  25.866  1.00 87.08  ? 67  LYS   A HZ1  1 
ATOM   997  H HZ2  . LYS   A 1 82  ? 8.825   25.124  26.834  1.00 87.08  ? 67  LYS   A HZ2  1 
ATOM   998  H HZ3  . LYS   A 1 82  ? 9.227   26.227  25.986  1.00 87.08  ? 67  LYS   A HZ3  1 
ATOM   999  N N    . THR   A 1 83  ? 15.789  22.130  23.938  1.00 35.14  ? 68  THR   A N    1 
ATOM   1000 C CA   . THR   A 1 83  ? 17.146  22.471  24.342  1.00 40.03  ? 68  THR   A CA   1 
ATOM   1001 C C    . THR   A 1 83  ? 18.210  21.944  23.386  1.00 42.27  ? 68  THR   A C    1 
ATOM   1002 O O    . THR   A 1 83  ? 19.290  22.539  23.296  1.00 49.53  ? 68  THR   A O    1 
ATOM   1003 C CB   . THR   A 1 83  ? 17.421  21.942  25.758  1.00 43.35  ? 68  THR   A CB   1 
ATOM   1004 O OG1  . THR   A 1 83  ? 17.209  20.526  25.807  1.00 54.64  ? 68  THR   A OG1  1 
ATOM   1005 C CG2  . THR   A 1 83  ? 16.498  22.596  26.762  1.00 50.62  ? 68  THR   A CG2  1 
ATOM   1006 H H    . THR   A 1 83  ? 15.529  21.355  24.203  1.00 42.17  ? 68  THR   A H    1 
ATOM   1007 H HA   . THR   A 1 83  ? 17.226  23.437  24.361  1.00 48.04  ? 68  THR   A HA   1 
ATOM   1008 H HB   . THR   A 1 83  ? 18.341  22.144  25.991  1.00 52.02  ? 68  THR   A HB   1 
ATOM   1009 H HG1  . THR   A 1 83  ? 16.404  20.351  25.644  1.00 65.56  ? 68  THR   A HG1  1 
ATOM   1010 H HG21 . THR   A 1 83  ? 16.685  22.261  27.653  1.00 60.75  ? 68  THR   A HG21 1 
ATOM   1011 H HG22 . THR   A 1 83  ? 16.627  23.557  26.754  1.00 60.75  ? 68  THR   A HG22 1 
ATOM   1012 H HG23 . THR   A 1 83  ? 15.574  22.400  26.540  1.00 60.75  ? 68  THR   A HG23 1 
ATOM   1013 N N    . CYS   A 1 84  ? 17.939  20.854  22.670  1.00 38.99  ? 69  CYS   A N    1 
ATOM   1014 C CA   . CYS   A 1 84  ? 18.882  20.313  21.698  1.00 33.66  ? 69  CYS   A CA   1 
ATOM   1015 C C    . CYS   A 1 84  ? 18.691  21.025  20.366  1.00 34.92  ? 69  CYS   A C    1 
ATOM   1016 O O    . CYS   A 1 84  ? 17.612  20.954  19.765  1.00 38.68  ? 69  CYS   A O    1 
ATOM   1017 C CB   . CYS   A 1 84  ? 18.701  18.807  21.525  1.00 39.53  ? 69  CYS   A CB   1 
ATOM   1018 S SG   . CYS   A 1 84  ? 19.652  17.819  22.703  1.00 48.83  ? 69  CYS   A SG   1 
ATOM   1019 H H    . CYS   A 1 84  ? 17.207  20.407  22.731  1.00 46.79  ? 69  CYS   A H    1 
ATOM   1020 H HA   . CYS   A 1 84  ? 19.785  20.472  22.015  1.00 40.39  ? 69  CYS   A HA   1 
ATOM   1021 H HB2  . CYS   A 1 84  ? 17.763  18.590  21.646  1.00 47.43  ? 69  CYS   A HB2  1 
ATOM   1022 H HB3  . CYS   A 1 84  ? 18.987  18.560  20.632  1.00 47.43  ? 69  CYS   A HB3  1 
ATOM   1023 H HG   . CYS   A 1 84  ? 19.441  16.655  22.496  1.00 58.59  ? 69  CYS   A HG   1 
ATOM   1024 N N    . ARG   A 1 85  ? 19.735  21.700  19.904  1.00 28.95  ? 70  ARG   A N    1 
ATOM   1025 C CA   . ARG   A 1 85  ? 19.659  22.453  18.657  1.00 31.58  ? 70  ARG   A CA   1 
ATOM   1026 C C    . ARG   A 1 85  ? 21.011  22.379  17.969  1.00 28.21  ? 70  ARG   A C    1 
ATOM   1027 O O    . ARG   A 1 85  ? 22.045  22.552  18.618  1.00 28.95  ? 70  ARG   A O    1 
ATOM   1028 C CB   . ARG   A 1 85  ? 19.251  23.908  18.922  1.00 28.86  ? 70  ARG   A CB   1 
ATOM   1029 C CG   . ARG   A 1 85  ? 18.545  24.572  17.751  1.00 36.28  ? 70  ARG   A CG   1 
ATOM   1030 C CD   . ARG   A 1 85  ? 17.794  25.813  18.196  1.00 34.88  ? 70  ARG   A CD   1 
ATOM   1031 N NE   . ARG   A 1 85  ? 16.906  26.318  17.154  1.00 40.37  ? 70  ARG   A NE   1 
ATOM   1032 C CZ   . ARG   A 1 85  ? 15.671  25.880  16.939  1.00 46.83  ? 70  ARG   A CZ   1 
ATOM   1033 N NH1  . ARG   A 1 85  ? 15.142  24.908  17.668  1.00 41.38  ? 70  ARG   A NH1  1 
ATOM   1034 N NH2  . ARG   A 1 85  ? 14.954  26.424  15.960  1.00 46.87  ? 70  ARG   A NH2  1 
ATOM   1035 H H    . ARG   A 1 85  ? 20.501  21.738  20.293  1.00 34.74  ? 70  ARG   A H    1 
ATOM   1036 H HA   . ARG   A 1 85  ? 18.997  22.061  18.066  1.00 37.89  ? 70  ARG   A HA   1 
ATOM   1037 H HB2  . ARG   A 1 85  ? 18.648  23.929  19.681  1.00 34.63  ? 70  ARG   A HB2  1 
ATOM   1038 H HB3  . ARG   A 1 85  ? 20.049  24.424  19.118  1.00 34.63  ? 70  ARG   A HB3  1 
ATOM   1039 H HG2  . ARG   A 1 85  ? 19.201  24.833  17.085  1.00 43.53  ? 70  ARG   A HG2  1 
ATOM   1040 H HG3  . ARG   A 1 85  ? 17.909  23.951  17.363  1.00 43.53  ? 70  ARG   A HG3  1 
ATOM   1041 H HD2  . ARG   A 1 85  ? 17.256  25.598  18.974  1.00 41.85  ? 70  ARG   A HD2  1 
ATOM   1042 H HD3  . ARG   A 1 85  ? 18.431  26.510  18.415  1.00 41.85  ? 70  ARG   A HD3  1 
ATOM   1043 H HE   . ARG   A 1 85  ? 17.204  26.943  16.644  1.00 48.45  ? 70  ARG   A HE   1 
ATOM   1044 H HH11 . ARG   A 1 85  ? 15.600  24.544  18.299  1.00 49.66  ? 70  ARG   A HH11 1 
ATOM   1045 H HH12 . ARG   A 1 85  ? 14.339  24.640  17.511  1.00 49.66  ? 70  ARG   A HH12 1 
ATOM   1046 H HH21 . ARG   A 1 85  ? 15.291  27.050  15.476  1.00 56.24  ? 70  ARG   A HH21 1 
ATOM   1047 H HH22 . ARG   A 1 85  ? 14.152  26.149  15.810  1.00 56.24  ? 70  ARG   A HH22 1 
ATOM   1048 N N    . HIS   A 1 86  ? 20.997  22.084  16.669  1.00 28.44  ? 71  HIS   A N    1 
ATOM   1049 C CA   . HIS   A 1 86  ? 22.208  22.014  15.859  1.00 27.38  ? 71  HIS   A CA   1 
ATOM   1050 C C    . HIS   A 1 86  ? 21.811  22.050  14.389  1.00 26.47  ? 71  HIS   A C    1 
ATOM   1051 O O    . HIS   A 1 86  ? 20.752  21.548  14.010  1.00 25.85  ? 71  HIS   A O    1 
ATOM   1052 C CB   . HIS   A 1 86  ? 23.018  20.747  16.169  1.00 30.00  ? 71  HIS   A CB   1 
ATOM   1053 C CG   . HIS   A 1 86  ? 24.326  20.666  15.443  1.00 28.66  ? 71  HIS   A CG   1 
ATOM   1054 N ND1  . HIS   A 1 86  ? 24.462  20.043  14.222  1.00 27.34  ? 71  HIS   A ND1  1 
ATOM   1055 C CD2  . HIS   A 1 86  ? 25.562  21.122  15.772  1.00 30.53  ? 71  HIS   A CD2  1 
ATOM   1056 C CE1  . HIS   A 1 86  ? 25.719  20.126  13.822  1.00 27.75  ? 71  HIS   A CE1  1 
ATOM   1057 N NE2  . HIS   A 1 86  ? 26.409  20.773  14.745  1.00 28.53  ? 71  HIS   A NE2  1 
ATOM   1058 H H    . HIS   A 1 86  ? 20.280  21.917  16.224  1.00 34.12  ? 71  HIS   A H    1 
ATOM   1059 H HA   . HIS   A 1 86  ? 22.769  22.783  16.043  1.00 32.85  ? 71  HIS   A HA   1 
ATOM   1060 H HB2  . HIS   A 1 86  ? 23.207  20.723  17.120  1.00 36.00  ? 71  HIS   A HB2  1 
ATOM   1061 H HB3  . HIS   A 1 86  ? 22.493  19.972  15.916  1.00 36.00  ? 71  HIS   A HB3  1 
ATOM   1062 H HD2  . HIS   A 1 86  ? 25.793  21.583  16.545  1.00 36.63  ? 71  HIS   A HD2  1 
ATOM   1063 H HE1  . HIS   A 1 86  ? 26.061  19.786  13.027  1.00 33.30  ? 71  HIS   A HE1  1 
ATOM   1064 H HE2  . HIS   A 1 86  ? 27.250  20.947  14.710  1.00 34.24  ? 71  HIS   A HE2  1 
ATOM   1065 N N    . ALA   A 1 87  ? 22.672  22.654  13.563  1.00 26.45  ? 72  ALA   A N    1 
ATOM   1066 C CA   . ALA   A 1 87  ? 22.347  22.820  12.146  1.00 28.28  ? 72  ALA   A CA   1 
ATOM   1067 C C    . ALA   A 1 87  ? 21.982  21.486  11.489  1.00 25.11  ? 72  ALA   A C    1 
ATOM   1068 O O    . ALA   A 1 87  ? 21.077  21.429  10.647  1.00 24.38  ? 72  ALA   A O    1 
ATOM   1069 C CB   . ALA   A 1 87  ? 23.521  23.479  11.408  1.00 29.08  ? 72  ALA   A CB   1 
ATOM   1070 H H    . ALA   A 1 87  ? 23.438  22.970  13.795  1.00 31.74  ? 72  ALA   A H    1 
ATOM   1071 H HA   . ALA   A 1 87  ? 21.577  23.406  12.075  1.00 33.93  ? 72  ALA   A HA   1 
ATOM   1072 H HB1  . ALA   A 1 87  ? 23.288  23.583  10.472  1.00 34.90  ? 72  ALA   A HB1  1 
ATOM   1073 H HB2  . ALA   A 1 87  ? 23.694  24.348  11.804  1.00 34.90  ? 72  ALA   A HB2  1 
ATOM   1074 H HB3  . ALA   A 1 87  ? 24.305  22.915  11.493  1.00 34.90  ? 72  ALA   A HB3  1 
ATOM   1075 N N    . ASN   A 1 88  ? 22.652  20.402  11.877  1.00 25.50  ? 73  ASN   A N    1 
ATOM   1076 C CA   . ASN   A 1 88  ? 22.510  19.116  11.200  1.00 26.00  ? 73  ASN   A CA   1 
ATOM   1077 C C    . ASN   A 1 88  ? 21.468  18.193  11.831  1.00 26.62  ? 73  ASN   A C    1 
ATOM   1078 O O    . ASN   A 1 88  ? 21.460  16.989  11.539  1.00 25.12  ? 73  ASN   A O    1 
ATOM   1079 C CB   . ASN   A 1 88  ? 23.868  18.407  11.151  1.00 30.59  ? 73  ASN   A CB   1 
ATOM   1080 C CG   . ASN   A 1 88  ? 24.837  19.078  10.195  1.00 25.80  ? 73  ASN   A CG   1 
ATOM   1081 O OD1  . ASN   A 1 88  ? 25.906  19.514  10.592  1.00 26.50  ? 73  ASN   A OD1  1 
ATOM   1082 N ND2  . ASN   A 1 88  ? 24.455  19.160  8.927   1.00 28.12  ? 73  ASN   A ND2  1 
ATOM   1083 H H    . ASN   A 1 88  ? 23.201  20.387  12.539  1.00 30.60  ? 73  ASN   A H    1 
ATOM   1084 H HA   . ASN   A 1 88  ? 22.218  19.290  10.292  1.00 31.19  ? 73  ASN   A HA   1 
ATOM   1085 H HB2  . ASN   A 1 88  ? 24.263  18.416  12.037  1.00 36.70  ? 73  ASN   A HB2  1 
ATOM   1086 H HB3  . ASN   A 1 88  ? 23.738  17.492  10.856  1.00 36.70  ? 73  ASN   A HB3  1 
ATOM   1087 H HD21 . ASN   A 1 88  ? 24.970  19.532  8.346   1.00 33.74  ? 73  ASN   A HD21 1 
ATOM   1088 H HD22 . ASN   A 1 88  ? 23.694  18.842  8.686   1.00 33.74  ? 73  ASN   A HD22 1 
ATOM   1089 N N    . ILE   A 1 89  ? 20.595  18.716  12.692  1.00 26.53  ? 74  ILE   A N    1 
ATOM   1090 C CA   . ILE   A 1 89  ? 19.425  17.979  13.160  1.00 24.80  ? 74  ILE   A CA   1 
ATOM   1091 C C    . ILE   A 1 89  ? 18.194  18.828  12.890  1.00 25.08  ? 74  ILE   A C    1 
ATOM   1092 O O    . ILE   A 1 89  ? 18.219  20.052  13.085  1.00 25.31  ? 74  ILE   A O    1 
ATOM   1093 C CB   . ILE   A 1 89  ? 19.523  17.597  14.651  1.00 25.58  ? 74  ILE   A CB   1 
ATOM   1094 C CG1  . ILE   A 1 89  ? 19.436  18.832  15.556  1.00 26.05  ? 74  ILE   A CG1  1 
ATOM   1095 C CG2  . ILE   A 1 89  ? 20.820  16.827  14.913  1.00 26.16  ? 74  ILE   A CG2  1 
ATOM   1096 C CD1  . ILE   A 1 89  ? 19.507  18.485  17.018  1.00 28.87  ? 74  ILE   A CD1  1 
ATOM   1097 H H    . ILE   A 1 89  ? 20.661  19.507  13.022  1.00 31.84  ? 74  ILE   A H    1 
ATOM   1098 H HA   . ILE   A 1 89  ? 19.348  17.152  12.658  1.00 29.76  ? 74  ILE   A HA   1 
ATOM   1099 H HB   . ILE   A 1 89  ? 18.767  17.028  14.862  1.00 30.69  ? 74  ILE   A HB   1 
ATOM   1100 H HG12 . ILE   A 1 89  ? 20.176  19.426  15.352  1.00 31.26  ? 74  ILE   A HG12 1 
ATOM   1101 H HG13 . ILE   A 1 89  ? 18.593  19.284  15.394  1.00 31.26  ? 74  ILE   A HG13 1 
ATOM   1102 H HG21 . ILE   A 1 89  ? 20.776  16.424  15.794  1.00 31.40  ? 74  ILE   A HG21 1 
ATOM   1103 H HG22 . ILE   A 1 89  ? 20.920  16.138  14.238  1.00 31.40  ? 74  ILE   A HG22 1 
ATOM   1104 H HG23 . ILE   A 1 89  ? 21.568  17.444  14.868  1.00 31.40  ? 74  ILE   A HG23 1 
ATOM   1105 H HD11 . ILE   A 1 89  ? 19.245  19.259  17.539  1.00 34.64  ? 74  ILE   A HD11 1 
ATOM   1106 H HD12 . ILE   A 1 89  ? 18.903  17.746  17.196  1.00 34.64  ? 74  ILE   A HD12 1 
ATOM   1107 H HD13 . ILE   A 1 89  ? 20.416  18.229  17.238  1.00 34.64  ? 74  ILE   A HD13 1 
ATOM   1108 N N    . VAL   A 1 90  ? 17.121  18.179  12.434  1.00 23.74  ? 75  VAL   A N    1 
ATOM   1109 C CA   . VAL   A 1 90  ? 15.910  18.896  12.053  1.00 23.25  ? 75  VAL   A CA   1 
ATOM   1110 C C    . VAL   A 1 90  ? 15.506  19.846  13.169  1.00 25.67  ? 75  VAL   A C    1 
ATOM   1111 O O    . VAL   A 1 90  ? 15.399  19.451  14.334  1.00 24.36  ? 75  VAL   A O    1 
ATOM   1112 C CB   . VAL   A 1 90  ? 14.789  17.894  11.726  1.00 25.75  ? 75  VAL   A CB   1 
ATOM   1113 C CG1  . VAL   A 1 90  ? 13.457  18.601  11.630  1.00 35.91  ? 75  VAL   A CG1  1 
ATOM   1114 C CG2  . VAL   A 1 90  ? 15.097  17.175  10.427  1.00 38.03  ? 75  VAL   A CG2  1 
ATOM   1115 H H    . VAL   A 1 90  ? 17.070  17.326  12.337  1.00 28.48  ? 75  VAL   A H    1 
ATOM   1116 H HA   . VAL   A 1 90  ? 16.092  19.425  11.260  1.00 27.90  ? 75  VAL   A HA   1 
ATOM   1117 H HB   . VAL   A 1 90  ? 14.733  17.239  12.440  1.00 30.90  ? 75  VAL   A HB   1 
ATOM   1118 H HG11 . VAL   A 1 90  ? 12.830  18.031  11.158  1.00 43.09  ? 75  VAL   A HG11 1 
ATOM   1119 H HG12 . VAL   A 1 90  ? 13.130  18.782  12.525  1.00 43.09  ? 75  VAL   A HG12 1 
ATOM   1120 H HG13 . VAL   A 1 90  ? 13.575  19.434  11.147  1.00 43.09  ? 75  VAL   A HG13 1 
ATOM   1121 H HG21 . VAL   A 1 90  ? 14.432  16.484  10.282  1.00 45.64  ? 75  VAL   A HG21 1 
ATOM   1122 H HG22 . VAL   A 1 90  ? 15.073  17.815  9.698   1.00 45.64  ? 75  VAL   A HG22 1 
ATOM   1123 H HG23 . VAL   A 1 90  ? 15.979  16.776  10.488  1.00 45.64  ? 75  VAL   A HG23 1 
ATOM   1124 N N    . ALA   A 1 91  ? 15.279  21.107  12.818  1.00 25.90  ? 76  ALA   A N    1 
ATOM   1125 C CA   . ALA   A 1 91  ? 15.011  22.130  13.817  1.00 24.25  ? 76  ALA   A CA   1 
ATOM   1126 C C    . ALA   A 1 91  ? 13.585  22.005  14.356  1.00 24.30  ? 76  ALA   A C    1 
ATOM   1127 O O    . ALA   A 1 91  ? 12.628  21.879  13.588  1.00 24.94  ? 76  ALA   A O    1 
ATOM   1128 C CB   . ALA   A 1 91  ? 15.237  23.520  13.220  1.00 29.08  ? 76  ALA   A CB   1 
ATOM   1129 H H    . ALA   A 1 91  ? 15.275  21.395  12.007  1.00 31.08  ? 76  ALA   A H    1 
ATOM   1130 H HA   . ALA   A 1 91  ? 15.618  22.011  14.564  1.00 29.10  ? 76  ALA   A HA   1 
ATOM   1131 H HB1  . ALA   A 1 91  ? 15.255  24.172  13.937  1.00 34.89  ? 76  ALA   A HB1  1 
ATOM   1132 H HB2  . ALA   A 1 91  ? 16.083  23.526  12.746  1.00 34.89  ? 76  ALA   A HB2  1 
ATOM   1133 H HB3  . ALA   A 1 91  ? 14.513  23.722  12.607  1.00 34.89  ? 76  ALA   A HB3  1 
ATOM   1134 N N    . TYR   A 1 92  ? 13.455  22.028  15.680  1.00 33.03  ? 77  TYR   A N    1 
ATOM   1135 C CA   . TYR   A 1 92  ? 12.163  22.020  16.357  1.00 29.77  ? 77  TYR   A CA   1 
ATOM   1136 C C    . TYR   A 1 92  ? 11.693  23.450  16.592  1.00 25.71  ? 77  TYR   A C    1 
ATOM   1137 O O    . TYR   A 1 92  ? 12.433  24.261  17.153  1.00 31.95  ? 77  TYR   A O    1 
ATOM   1138 C CB   . TYR   A 1 92  ? 12.287  21.270  17.689  1.00 32.34  ? 77  TYR   A CB   1 
ATOM   1139 C CG   . TYR   A 1 92  ? 11.096  21.384  18.610  1.00 26.67  ? 77  TYR   A CG   1 
ATOM   1140 C CD1  . TYR   A 1 92  ? 9.977   20.584  18.432  1.00 34.90  ? 77  TYR   A CD1  1 
ATOM   1141 C CD2  . TYR   A 1 92  ? 11.094  22.283  19.668  1.00 37.94  ? 77  TYR   A CD2  1 
ATOM   1142 C CE1  . TYR   A 1 92  ? 8.879   20.680  19.276  1.00 30.44  ? 77  TYR   A CE1  1 
ATOM   1143 C CE2  . TYR   A 1 92  ? 9.995   22.389  20.525  1.00 33.52  ? 77  TYR   A CE2  1 
ATOM   1144 C CZ   . TYR   A 1 92  ? 8.892   21.578  20.319  1.00 32.28  ? 77  TYR   A CZ   1 
ATOM   1145 O OH   . TYR   A 1 92  ? 7.799   21.665  21.146  1.00 32.92  ? 77  TYR   A OH   1 
ATOM   1146 H H    . TYR   A 1 92  ? 14.121  22.049  16.224  1.00 39.64  ? 77  TYR   A H    1 
ATOM   1147 H HA   . TYR   A 1 92  ? 11.499  21.575  15.807  1.00 35.72  ? 77  TYR   A HA   1 
ATOM   1148 H HB2  . TYR   A 1 92  ? 12.415  20.328  17.499  1.00 38.81  ? 77  TYR   A HB2  1 
ATOM   1149 H HB3  . TYR   A 1 92  ? 13.055  21.620  18.167  1.00 38.81  ? 77  TYR   A HB3  1 
ATOM   1150 H HD1  . TYR   A 1 92  ? 9.962   19.971  17.733  1.00 41.88  ? 77  TYR   A HD1  1 
ATOM   1151 H HD2  . TYR   A 1 92  ? 11.837  22.825  19.808  1.00 45.53  ? 77  TYR   A HD2  1 
ATOM   1152 H HE1  . TYR   A 1 92  ? 8.135   20.139  19.136  1.00 36.53  ? 77  TYR   A HE1  1 
ATOM   1153 H HE2  . TYR   A 1 92  ? 10.004  22.999  21.227  1.00 40.22  ? 77  TYR   A HE2  1 
ATOM   1154 H HH   . TYR   A 1 92  ? 7.197   21.142  20.883  1.00 39.51  ? 77  TYR   A HH   1 
ATOM   1155 N N    . HIS   A 1 93  ? 10.452  23.754  16.181  1.00 28.43  ? 78  HIS   A N    1 
ATOM   1156 C CA   . HIS   A 1 93  ? 9.916   25.105  16.315  1.00 27.30  ? 78  HIS   A CA   1 
ATOM   1157 C C    . HIS   A 1 93  ? 8.804   25.241  17.345  1.00 35.32  ? 78  HIS   A C    1 
ATOM   1158 O O    . HIS   A 1 93  ? 8.532   26.365  17.778  1.00 46.05  ? 78  HIS   A O    1 
ATOM   1159 C CB   . HIS   A 1 93  ? 9.391   25.619  14.964  1.00 33.66  ? 78  HIS   A CB   1 
ATOM   1160 C CG   . HIS   A 1 93  ? 10.453  25.762  13.917  1.00 25.98  ? 78  HIS   A CG   1 
ATOM   1161 N ND1  . HIS   A 1 93  ? 11.605  26.487  14.123  1.00 35.35  ? 78  HIS   A ND1  1 
ATOM   1162 C CD2  . HIS   A 1 93  ? 10.543  25.261  12.664  1.00 30.08  ? 78  HIS   A CD2  1 
ATOM   1163 C CE1  . HIS   A 1 93  ? 12.355  26.436  13.037  1.00 31.14  ? 78  HIS   A CE1  1 
ATOM   1164 N NE2  . HIS   A 1 93  ? 11.735  25.696  12.138  1.00 31.95  ? 78  HIS   A NE2  1 
ATOM   1165 H H    . HIS   A 1 93  ? 9.908   23.193  15.822  1.00 34.12  ? 78  HIS   A H    1 
ATOM   1166 H HA   . HIS   A 1 93  ? 10.644  25.684  16.592  1.00 32.76  ? 78  HIS   A HA   1 
ATOM   1167 H HB2  . HIS   A 1 93  ? 8.727   24.995  14.630  1.00 40.39  ? 78  HIS   A HB2  1 
ATOM   1168 H HB3  . HIS   A 1 93  ? 8.988   26.491  15.098  1.00 40.39  ? 78  HIS   A HB3  1 
ATOM   1169 H HD1  . HIS   A 1 93  ? 11.805  26.907  14.846  1.00 42.42  ? 78  HIS   A HD1  1 
ATOM   1170 H HD2  . HIS   A 1 93  ? 9.915   24.723  12.238  1.00 36.09  ? 78  HIS   A HD2  1 
ATOM   1171 H HE1  . HIS   A 1 93  ? 13.180  26.851  12.926  1.00 37.37  ? 78  HIS   A HE1  1 
ATOM   1172 N N    . GLY   A 1 94  ? 8.160   24.158  17.743  1.00 35.24  ? 79  GLY   A N    1 
ATOM   1173 C CA   . GLY   A 1 94  ? 7.137   24.222  18.772  1.00 28.64  ? 79  GLY   A CA   1 
ATOM   1174 C C    . GLY   A 1 94  ? 6.107   23.126  18.596  1.00 28.33  ? 79  GLY   A C    1 
ATOM   1175 O O    . GLY   A 1 94  ? 6.054   22.439  17.581  1.00 27.52  ? 79  GLY   A O    1 
ATOM   1176 H H    . GLY   A 1 94  ? 8.297   23.368  17.431  1.00 42.28  ? 79  GLY   A H    1 
ATOM   1177 H HA2  . GLY   A 1 94  ? 7.548   24.124  19.645  1.00 34.37  ? 79  GLY   A HA2  1 
ATOM   1178 H HA3  . GLY   A 1 94  ? 6.687   25.080  18.729  1.00 34.37  ? 79  GLY   A HA3  1 
ATOM   1179 N N    . SER   A 1 95  ? 5.273   22.977  19.625  1.00 27.93  ? 80  SER   A N    1 
ATOM   1180 C CA   . SER   A 1 95  ? 4.213   21.980  19.646  1.00 28.73  ? 80  SER   A CA   1 
ATOM   1181 C C    . SER   A 1 95  ? 2.875   22.635  19.956  1.00 30.61  ? 80  SER   A C    1 
ATOM   1182 O O    . SER   A 1 95  ? 2.802   23.624  20.693  1.00 29.33  ? 80  SER   A O    1 
ATOM   1183 C CB   . SER   A 1 95  ? 4.491   20.898  20.681  1.00 28.42  ? 80  SER   A CB   1 
ATOM   1184 O OG   . SER   A 1 95  ? 5.770   20.340  20.492  1.00 44.16  ? 80  SER   A OG   1 
ATOM   1185 H H    . SER   A 1 95  ? 5.305   23.455  20.339  1.00 33.51  ? 80  SER   A H    1 
ATOM   1186 H HA   . SER   A 1 95  ? 4.151   21.569  18.769  1.00 34.48  ? 80  SER   A HA   1 
ATOM   1187 H HB2  . SER   A 1 95  ? 4.445   21.289  21.567  1.00 34.11  ? 80  SER   A HB2  1 
ATOM   1188 H HB3  . SER   A 1 95  ? 3.825   20.198  20.593  1.00 34.11  ? 80  SER   A HB3  1 
ATOM   1189 H HG   . SER   A 1 95  ? 5.894   19.713  21.036  1.00 53.00  ? 80  SER   A HG   1 
ATOM   1190 N N    . TYR   A 1 96  ? 1.811   22.063  19.391  1.00 28.09  ? 81  TYR   A N    1 
ATOM   1191 C CA   . TYR   A 1 96  ? 0.452   22.550  19.585  1.00 33.83  ? 81  TYR   A CA   1 
ATOM   1192 C C    . TYR   A 1 96  ? -0.466  21.391  19.956  1.00 31.35  ? 81  TYR   A C    1 
ATOM   1193 O O    . TYR   A 1 96  ? -0.339  20.290  19.406  1.00 28.22  ? 81  TYR   A O    1 
ATOM   1194 C CB   . TYR   A 1 96  ? -0.106  23.218  18.319  1.00 30.51  ? 81  TYR   A CB   1 
ATOM   1195 C CG   . TYR   A 1 96  ? 0.652   24.433  17.840  1.00 30.67  ? 81  TYR   A CG   1 
ATOM   1196 C CD1  . TYR   A 1 96  ? 1.873   24.303  17.200  1.00 32.65  ? 81  TYR   A CD1  1 
ATOM   1197 C CD2  . TYR   A 1 96  ? 0.137   25.714  18.015  1.00 34.50  ? 81  TYR   A CD2  1 
ATOM   1198 C CE1  . TYR   A 1 96  ? 2.562   25.405  16.756  1.00 35.00  ? 81  TYR   A CE1  1 
ATOM   1199 C CE2  . TYR   A 1 96  ? 0.819   26.818  17.577  1.00 35.39  ? 81  TYR   A CE2  1 
ATOM   1200 C CZ   . TYR   A 1 96  ? 2.033   26.661  16.943  1.00 39.84  ? 81  TYR   A CZ   1 
ATOM   1201 O OH   . TYR   A 1 96  ? 2.730   27.765  16.494  1.00 45.45  ? 81  TYR   A OH   1 
ATOM   1202 H H    . TYR   A 1 96  ? 1.856   21.373  18.879  1.00 33.71  ? 81  TYR   A H    1 
ATOM   1203 H HA   . TYR   A 1 96  ? 0.461   23.198  20.307  1.00 40.59  ? 81  TYR   A HA   1 
ATOM   1204 H HB2  . TYR   A 1 96  ? -0.093  22.567  17.600  1.00 36.62  ? 81  TYR   A HB2  1 
ATOM   1205 H HB3  . TYR   A 1 96  ? -1.017  23.497  18.498  1.00 36.62  ? 81  TYR   A HB3  1 
ATOM   1206 H HD1  . TYR   A 1 96  ? 2.233   23.455  17.069  1.00 39.18  ? 81  TYR   A HD1  1 
ATOM   1207 H HD2  . TYR   A 1 96  ? -0.685  25.822  18.436  1.00 41.40  ? 81  TYR   A HD2  1 
ATOM   1208 H HE1  . TYR   A 1 96  ? 3.382   25.303  16.330  1.00 42.00  ? 81  TYR   A HE1  1 
ATOM   1209 H HE2  . TYR   A 1 96  ? 0.465   27.668  17.706  1.00 42.46  ? 81  TYR   A HE2  1 
ATOM   1210 H HH   . TYR   A 1 96  ? 2.372   28.468  16.783  1.00 54.54  ? 81  TYR   A HH   1 
ATOM   1211 N N    . LEU   A 1 97  ? -1.392  21.639  20.875  1.00 30.03  ? 82  LEU   A N    1 
ATOM   1212 C CA   . LEU   A 1 97  ? -2.468  20.701  21.169  1.00 30.40  ? 82  LEU   A CA   1 
ATOM   1213 C C    . LEU   A 1 97  ? -3.797  21.403  20.946  1.00 30.83  ? 82  LEU   A C    1 
ATOM   1214 O O    . LEU   A 1 97  ? -4.042  22.468  21.520  1.00 32.58  ? 82  LEU   A O    1 
ATOM   1215 C CB   . LEU   A 1 97  ? -2.384  20.163  22.599  1.00 31.52  ? 82  LEU   A CB   1 
ATOM   1216 C CG   . LEU   A 1 97  ? -3.508  19.180  22.973  1.00 32.94  ? 82  LEU   A CG   1 
ATOM   1217 C CD1  . LEU   A 1 97  ? -3.450  17.917  22.116  1.00 31.02  ? 82  LEU   A CD1  1 
ATOM   1218 C CD2  . LEU   A 1 97  ? -3.481  18.829  24.466  1.00 33.35  ? 82  LEU   A CD2  1 
ATOM   1219 H H    . LEU   A 1 97  ? -1.419  22.356  21.349  1.00 36.04  ? 82  LEU   A H    1 
ATOM   1220 H HA   . LEU   A 1 97  ? -2.406  19.941  20.569  1.00 36.48  ? 82  LEU   A HA   1 
ATOM   1221 H HB2  . LEU   A 1 97  ? -1.539  19.698  22.706  1.00 37.83  ? 82  LEU   A HB2  1 
ATOM   1222 H HB3  . LEU   A 1 97  ? -2.431  20.911  23.214  1.00 37.83  ? 82  LEU   A HB3  1 
ATOM   1223 H HG   . LEU   A 1 97  ? -4.354  19.619  22.794  1.00 39.53  ? 82  LEU   A HG   1 
ATOM   1224 H HD11 . LEU   A 1 97  ? -4.103  17.280  22.447  1.00 37.23  ? 82  LEU   A HD11 1 
ATOM   1225 H HD12 . LEU   A 1 97  ? -3.653  18.149  21.196  1.00 37.23  ? 82  LEU   A HD12 1 
ATOM   1226 H HD13 . LEU   A 1 97  ? -2.560  17.537  22.173  1.00 37.23  ? 82  LEU   A HD13 1 
ATOM   1227 H HD21 . LEU   A 1 97  ? -4.205  18.212  24.659  1.00 40.02  ? 82  LEU   A HD21 1 
ATOM   1228 H HD22 . LEU   A 1 97  ? -2.629  18.415  24.678  1.00 40.02  ? 82  LEU   A HD22 1 
ATOM   1229 H HD23 . LEU   A 1 97  ? -3.592  19.641  24.984  1.00 40.02  ? 82  LEU   A HD23 1 
ATOM   1230 N N    . TRP   A 1 98  ? -4.653  20.808  20.122  1.00 30.28  ? 83  TRP   A N    1 
ATOM   1231 C CA   . TRP   A 1 98  ? -5.955  21.408  19.857  1.00 30.70  ? 83  TRP   A CA   1 
ATOM   1232 C C    . TRP   A 1 98  ? -6.911  20.340  19.344  1.00 30.39  ? 83  TRP   A C    1 
ATOM   1233 O O    . TRP   A 1 98  ? -6.607  19.644  18.369  1.00 30.45  ? 83  TRP   A O    1 
ATOM   1234 C CB   . TRP   A 1 98  ? -5.814  22.559  18.850  1.00 35.91  ? 83  TRP   A CB   1 
ATOM   1235 C CG   . TRP   A 1 98  ? -7.033  23.416  18.750  1.00 36.54  ? 83  TRP   A CG   1 
ATOM   1236 C CD1  . TRP   A 1 98  ? -7.953  23.417  17.742  1.00 44.32  ? 83  TRP   A CD1  1 
ATOM   1237 C CD2  . TRP   A 1 98  ? -7.477  24.399  19.698  1.00 45.35  ? 83  TRP   A CD2  1 
ATOM   1238 N NE1  . TRP   A 1 98  ? -8.944  24.334  18.004  1.00 47.34  ? 83  TRP   A NE1  1 
ATOM   1239 C CE2  . TRP   A 1 98  ? -8.674  24.952  19.198  1.00 44.67  ? 83  TRP   A CE2  1 
ATOM   1240 C CE3  . TRP   A 1 98  ? -6.977  24.865  20.920  1.00 44.54  ? 83  TRP   A CE3  1 
ATOM   1241 C CZ2  . TRP   A 1 98  ? -9.379  25.949  19.877  1.00 45.53  ? 83  TRP   A CZ2  1 
ATOM   1242 C CZ3  . TRP   A 1 98  ? -7.679  25.852  21.593  1.00 43.50  ? 83  TRP   A CZ3  1 
ATOM   1243 C CH2  . TRP   A 1 98  ? -8.869  26.383  21.070  1.00 39.42  ? 83  TRP   A CH2  1 
ATOM   1244 H H    . TRP   A 1 98  ? -4.505  20.068  19.710  1.00 36.33  ? 83  TRP   A H    1 
ATOM   1245 H HA   . TRP   A 1 98  ? -6.332  21.758  20.679  1.00 36.84  ? 83  TRP   A HA   1 
ATOM   1246 H HB2  . TRP   A 1 98  ? -5.074  23.124  19.122  1.00 43.09  ? 83  TRP   A HB2  1 
ATOM   1247 H HB3  . TRP   A 1 98  ? -5.640  22.186  17.971  1.00 43.09  ? 83  TRP   A HB3  1 
ATOM   1248 H HD1  . TRP   A 1 98  ? -7.915  22.876  16.986  1.00 53.19  ? 83  TRP   A HD1  1 
ATOM   1249 H HE1  . TRP   A 1 98  ? -9.623  24.493  17.501  1.00 56.81  ? 83  TRP   A HE1  1 
ATOM   1250 H HE3  . TRP   A 1 98  ? -6.189  24.520  21.274  1.00 53.45  ? 83  TRP   A HE3  1 
ATOM   1251 H HZ2  . TRP   A 1 98  ? -10.166 26.304  19.531  1.00 54.64  ? 83  TRP   A HZ2  1 
ATOM   1252 H HZ3  . TRP   A 1 98  ? -7.357  26.168  22.407  1.00 52.20  ? 83  TRP   A HZ3  1 
ATOM   1253 H HH2  . TRP   A 1 98  ? -9.320  27.044  21.544  1.00 47.31  ? 83  TRP   A HH2  1 
ATOM   1254 N N    . LEU   A 1 99  ? -8.057  20.203  20.008  1.00 34.92  ? 84  LEU   A N    1 
ATOM   1255 C CA   . LEU   A 1 99  ? -9.105  19.276  19.584  1.00 37.13  ? 84  LEU   A CA   1 
ATOM   1256 C C    . LEU   A 1 99  ? -8.544  17.877  19.330  1.00 33.71  ? 84  LEU   A C    1 
ATOM   1257 O O    . LEU   A 1 99  ? -8.791  17.259  18.293  1.00 37.01  ? 84  LEU   A O    1 
ATOM   1258 C CB   . LEU   A 1 99  ? -9.819  19.802  18.337  1.00 36.69  ? 84  LEU   A CB   1 
ATOM   1259 C CG   . LEU   A 1 99  ? -10.545 21.143  18.475  1.00 50.38  ? 84  LEU   A CG   1 
ATOM   1260 C CD1  . LEU   A 1 99  ? -11.299 21.470  17.198  1.00 40.35  ? 84  LEU   A CD1  1 
ATOM   1261 C CD2  . LEU   A 1 99  ? -11.485 21.146  19.689  1.00 37.52  ? 84  LEU   A CD2  1 
ATOM   1262 H H    . LEU   A 1 99  ? -8.254  20.644  20.720  1.00 41.91  ? 84  LEU   A H    1 
ATOM   1263 H HA   . LEU   A 1 99  ? -9.751  19.205  20.304  1.00 44.56  ? 84  LEU   A HA   1 
ATOM   1264 H HB2  . LEU   A 1 99  ? -9.158  19.907  17.635  1.00 44.03  ? 84  LEU   A HB2  1 
ATOM   1265 H HB3  . LEU   A 1 99  ? -10.483 19.146  18.072  1.00 44.03  ? 84  LEU   A HB3  1 
ATOM   1266 H HG   . LEU   A 1 99  ? -9.887  21.840  18.623  1.00 60.46  ? 84  LEU   A HG   1 
ATOM   1267 H HD11 . LEU   A 1 99  ? -11.745 22.325  17.305  1.00 48.42  ? 84  LEU   A HD11 1 
ATOM   1268 H HD12 . LEU   A 1 99  ? -10.669 21.515  16.462  1.00 48.42  ? 84  LEU   A HD12 1 
ATOM   1269 H HD13 . LEU   A 1 99  ? -11.954 20.774  17.031  1.00 48.42  ? 84  LEU   A HD13 1 
ATOM   1270 H HD21 . LEU   A 1 99  ? -12.041 21.940  19.656  1.00 45.02  ? 84  LEU   A HD21 1 
ATOM   1271 H HD22 . LEU   A 1 99  ? -12.042 20.352  19.660  1.00 45.02  ? 84  LEU   A HD22 1 
ATOM   1272 H HD23 . LEU   A 1 99  ? -10.953 21.147  20.500  1.00 45.02  ? 84  LEU   A HD23 1 
ATOM   1273 N N    . GLN   A 1 100 ? -7.756  17.384  20.285  1.00 33.60  ? 85  GLN   A N    1 
ATOM   1274 C CA   . GLN   A 1 100 ? -7.266  16.010  20.296  1.00 34.46  ? 85  GLN   A CA   1 
ATOM   1275 C C    . GLN   A 1 100 ? -6.299  15.711  19.161  1.00 32.99  ? 85  GLN   A C    1 
ATOM   1276 O O    . GLN   A 1 100 ? -6.129  14.546  18.780  1.00 31.13  ? 85  GLN   A O    1 
ATOM   1277 C CB   . GLN   A 1 100 ? -8.429  15.013  20.248  1.00 33.82  ? 85  GLN   A CB   1 
ATOM   1278 C CG   . GLN   A 1 100 ? -9.471  15.238  21.328  1.00 35.36  ? 85  GLN   A CG   1 
ATOM   1279 C CD   . GLN   A 1 100 ? -10.550 14.177  21.303  1.00 43.04  ? 85  GLN   A CD   1 
ATOM   1280 O OE1  . GLN   A 1 100 ? -10.340 13.069  20.803  1.00 47.61  ? 85  GLN   A OE1  1 
ATOM   1281 N NE2  . GLN   A 1 100 ? -11.712 14.510  21.836  1.00 46.91  ? 85  GLN   A NE2  1 
ATOM   1282 H H    . GLN   A 1 100 ? -7.484  17.845  20.958  1.00 40.32  ? 85  GLN   A H    1 
ATOM   1283 H HA   . GLN   A 1 100 ? -6.778  15.880  21.124  1.00 41.35  ? 85  GLN   A HA   1 
ATOM   1284 H HB2  . GLN   A 1 100 ? -8.873  15.093  19.389  1.00 40.58  ? 85  GLN   A HB2  1 
ATOM   1285 H HB3  . GLN   A 1 100 ? -8.077  14.117  20.358  1.00 40.58  ? 85  GLN   A HB3  1 
ATOM   1286 H HG2  . GLN   A 1 100 ? -9.040  15.211  22.197  1.00 42.44  ? 85  GLN   A HG2  1 
ATOM   1287 H HG3  . GLN   A 1 100 ? -9.891  16.101  21.193  1.00 42.44  ? 85  GLN   A HG3  1 
ATOM   1288 H HE21 . GLN   A 1 100 ? -11.822 15.294  22.173  1.00 56.29  ? 85  GLN   A HE21 1 
ATOM   1289 H HE22 . GLN   A 1 100 ? -12.359 13.943  21.847  1.00 56.29  ? 85  GLN   A HE22 1 
ATOM   1290 N N    . LYS   A 1 101 ? -5.666  16.742  18.609  1.00 30.96  ? 86  LYS   A N    1 
ATOM   1291 C CA   . LYS   A 1 101 ? -4.596  16.593  17.631  1.00 29.67  ? 86  LYS   A CA   1 
ATOM   1292 C C    . LYS   A 1 101 ? -3.359  17.279  18.195  1.00 31.51  ? 86  LYS   A C    1 
ATOM   1293 O O    . LYS   A 1 101 ? -3.409  18.458  18.566  1.00 29.78  ? 86  LYS   A O    1 
ATOM   1294 C CB   . LYS   A 1 101 ? -4.994  17.185  16.274  1.00 33.77  ? 86  LYS   A CB   1 
ATOM   1295 C CG   . LYS   A 1 101 ? -6.067  16.379  15.540  1.00 34.87  ? 86  LYS   A CG   1 
ATOM   1296 C CD   . LYS   A 1 101 ? -7.128  17.267  14.863  1.00 38.24  ? 86  LYS   A CD   1 
ATOM   1297 C CE   . LYS   A 1 101 ? -6.638  17.818  13.536  1.00 46.79  ? 86  LYS   A CE   1 
ATOM   1298 N NZ   . LYS   A 1 101 ? -7.722  18.555  12.823  1.00 58.23  ? 86  LYS   A NZ   1 
ATOM   1299 H H    . LYS   A 1 101 ? -5.846  17.563  18.791  1.00 37.15  ? 86  LYS   A H    1 
ATOM   1300 H HA   . LYS   A 1 101 ? -4.395  15.655  17.488  1.00 35.61  ? 86  LYS   A HA   1 
ATOM   1301 H HB2  . LYS   A 1 101 ? -5.341  18.080  16.414  1.00 40.53  ? 86  LYS   A HB2  1 
ATOM   1302 H HB3  . LYS   A 1 101 ? -4.209  17.219  15.706  1.00 40.53  ? 86  LYS   A HB3  1 
ATOM   1303 H HG2  . LYS   A 1 101 ? -5.643  15.843  14.852  1.00 41.85  ? 86  LYS   A HG2  1 
ATOM   1304 H HG3  . LYS   A 1 101 ? -6.520  15.804  16.176  1.00 41.85  ? 86  LYS   A HG3  1 
ATOM   1305 H HD2  . LYS   A 1 101 ? -7.927  16.742  14.697  1.00 45.89  ? 86  LYS   A HD2  1 
ATOM   1306 H HD3  . LYS   A 1 101 ? -7.337  18.015  15.444  1.00 45.89  ? 86  LYS   A HD3  1 
ATOM   1307 H HE2  . LYS   A 1 101 ? -5.903  18.431  13.693  1.00 56.15  ? 86  LYS   A HE2  1 
ATOM   1308 H HE3  . LYS   A 1 101 ? -6.344  17.086  12.972  1.00 56.15  ? 86  LYS   A HE3  1 
ATOM   1309 H HZ1  . LYS   A 1 101 ? -7.416  18.873  12.050  1.00 69.88  ? 86  LYS   A HZ1  1 
ATOM   1310 H HZ2  . LYS   A 1 101 ? -8.405  18.009  12.660  1.00 69.88  ? 86  LYS   A HZ2  1 
ATOM   1311 H HZ3  . LYS   A 1 101 ? -8.007  19.235  13.322  1.00 69.88  ? 86  LYS   A HZ3  1 
ATOM   1312 N N    . LEU   A 1 102 ? -2.266  16.532  18.287  1.00 28.52  ? 87  LEU   A N    1 
ATOM   1313 C CA   . LEU   A 1 102 ? -0.985  17.059  18.726  1.00 28.67  ? 87  LEU   A CA   1 
ATOM   1314 C C    . LEU   A 1 102 ? -0.142  17.340  17.490  1.00 27.04  ? 87  LEU   A C    1 
ATOM   1315 O O    . LEU   A 1 102 ? 0.098   16.436  16.685  1.00 28.50  ? 87  LEU   A O    1 
ATOM   1316 C CB   . LEU   A 1 102 ? -0.281  16.070  19.647  1.00 28.07  ? 87  LEU   A CB   1 
ATOM   1317 C CG   . LEU   A 1 102 ? 1.106   16.535  20.088  1.00 31.10  ? 87  LEU   A CG   1 
ATOM   1318 C CD1  . LEU   A 1 102 ? 0.983   17.669  21.079  1.00 28.69  ? 87  LEU   A CD1  1 
ATOM   1319 C CD2  . LEU   A 1 102 ? 1.903   15.380  20.667  1.00 32.74  ? 87  LEU   A CD2  1 
ATOM   1320 H H    . LEU   A 1 102 ? -2.243  15.694  18.095  1.00 34.22  ? 87  LEU   A H    1 
ATOM   1321 H HA   . LEU   A 1 102 ? -1.113  17.887  19.216  1.00 34.41  ? 87  LEU   A HA   1 
ATOM   1322 H HB2  . LEU   A 1 102 ? -0.821  15.945  20.443  1.00 33.69  ? 87  LEU   A HB2  1 
ATOM   1323 H HB3  . LEU   A 1 102 ? -0.178  15.226  19.180  1.00 33.69  ? 87  LEU   A HB3  1 
ATOM   1324 H HG   . LEU   A 1 102 ? 1.596   16.863  19.317  1.00 37.32  ? 87  LEU   A HG   1 
ATOM   1325 H HD11 . LEU   A 1 102 ? 1.868   17.907  21.398  1.00 34.42  ? 87  LEU   A HD11 1 
ATOM   1326 H HD12 . LEU   A 1 102 ? 0.574   18.431  20.638  1.00 34.42  ? 87  LEU   A HD12 1 
ATOM   1327 H HD13 . LEU   A 1 102 ? 0.430   17.381  21.822  1.00 34.42  ? 87  LEU   A HD13 1 
ATOM   1328 H HD21 . LEU   A 1 102 ? 2.777   15.703  20.937  1.00 39.29  ? 87  LEU   A HD21 1 
ATOM   1329 H HD22 . LEU   A 1 102 ? 1.430   15.023  21.435  1.00 39.29  ? 87  LEU   A HD22 1 
ATOM   1330 H HD23 . LEU   A 1 102 ? 2.000   14.692  19.989  1.00 39.29  ? 87  LEU   A HD23 1 
ATOM   1331 N N    . TRP   A 1 103 ? 0.301   18.590  17.338  1.00 27.03  ? 88  TRP   A N    1 
ATOM   1332 C CA   . TRP   A 1 103 ? 1.092   19.016  16.194  1.00 26.19  ? 88  TRP   A CA   1 
ATOM   1333 C C    . TRP   A 1 103 ? 2.503   19.381  16.638  1.00 25.85  ? 88  TRP   A C    1 
ATOM   1334 O O    . TRP   A 1 103 ? 2.686   20.083  17.639  1.00 30.43  ? 88  TRP   A O    1 
ATOM   1335 C CB   . TRP   A 1 103 ? 0.479   20.237  15.506  1.00 26.57  ? 88  TRP   A CB   1 
ATOM   1336 C CG   . TRP   A 1 103 ? -0.910  20.094  15.004  1.00 27.04  ? 88  TRP   A CG   1 
ATOM   1337 C CD1  . TRP   A 1 103 ? -2.055  20.152  15.739  1.00 28.01  ? 88  TRP   A CD1  1 
ATOM   1338 C CD2  . TRP   A 1 103 ? -1.316  19.931  13.641  1.00 26.69  ? 88  TRP   A CD2  1 
ATOM   1339 N NE1  . TRP   A 1 103 ? -3.148  20.019  14.922  1.00 28.27  ? 88  TRP   A NE1  1 
ATOM   1340 C CE2  . TRP   A 1 103 ? -2.719  19.876  13.628  1.00 27.49  ? 88  TRP   A CE2  1 
ATOM   1341 C CE3  . TRP   A 1 103 ? -0.627  19.805  12.433  1.00 30.43  ? 88  TRP   A CE3  1 
ATOM   1342 C CZ2  . TRP   A 1 103 ? -3.446  19.707  12.453  1.00 34.93  ? 88  TRP   A CZ2  1 
ATOM   1343 C CZ3  . TRP   A 1 103 ? -1.353  19.636  11.269  1.00 25.94  ? 88  TRP   A CZ3  1 
ATOM   1344 C CH2  . TRP   A 1 103 ? -2.742  19.592  11.285  1.00 26.75  ? 88  TRP   A CH2  1 
ATOM   1345 H H    . TRP   A 1 103 ? 0.149   19.221  17.902  1.00 32.44  ? 88  TRP   A H    1 
ATOM   1346 H HA   . TRP   A 1 103 ? 1.131   18.282  15.561  1.00 31.43  ? 88  TRP   A HA   1 
ATOM   1347 H HB2  . TRP   A 1 103 ? 0.476   20.970  16.142  1.00 31.88  ? 88  TRP   A HB2  1 
ATOM   1348 H HB3  . TRP   A 1 103 ? 1.034   20.462  14.743  1.00 31.88  ? 88  TRP   A HB3  1 
ATOM   1349 H HD1  . TRP   A 1 103 ? -2.091  20.266  16.661  1.00 33.61  ? 88  TRP   A HD1  1 
ATOM   1350 H HE1  . TRP   A 1 103 ? -3.969  20.025  15.180  1.00 33.93  ? 88  TRP   A HE1  1 
ATOM   1351 H HE3  . TRP   A 1 103 ? 0.302   19.834  12.412  1.00 36.52  ? 88  TRP   A HE3  1 
ATOM   1352 H HZ2  . TRP   A 1 103 ? -4.376  19.672  12.462  1.00 41.91  ? 88  TRP   A HZ2  1 
ATOM   1353 H HZ3  . TRP   A 1 103 ? -0.903  19.550  10.459  1.00 31.13  ? 88  TRP   A HZ3  1 
ATOM   1354 H HH2  . TRP   A 1 103 ? -3.203  19.482  10.485  1.00 32.10  ? 88  TRP   A HH2  1 
ATOM   1355 N N    . ILE   A 1 104 ? 3.497   18.928  15.881  1.00 25.98  ? 89  ILE   A N    1 
ATOM   1356 C CA   . ILE   A 1 104 ? 4.890   19.298  16.096  1.00 26.00  ? 89  ILE   A CA   1 
ATOM   1357 C C    . ILE   A 1 104 ? 5.368   20.071  14.872  1.00 24.13  ? 89  ILE   A C    1 
ATOM   1358 O O    . ILE   A 1 104 ? 5.283   19.570  13.744  1.00 28.14  ? 89  ILE   A O    1 
ATOM   1359 C CB   . ILE   A 1 104 ? 5.787   18.066  16.331  1.00 30.93  ? 89  ILE   A CB   1 
ATOM   1360 C CG1  . ILE   A 1 104 ? 5.284   17.239  17.513  1.00 39.27  ? 89  ILE   A CG1  1 
ATOM   1361 C CG2  . ILE   A 1 104 ? 7.221   18.512  16.576  1.00 31.19  ? 89  ILE   A CG2  1 
ATOM   1362 C CD1  . ILE   A 1 104 ? 4.315   16.136  17.122  1.00 42.06  ? 89  ILE   A CD1  1 
ATOM   1363 H H    . ILE   A 1 104 ? 3.385   18.391  15.218  1.00 31.18  ? 89  ILE   A H    1 
ATOM   1364 H HA   . ILE   A 1 104 ? 4.947   19.871  16.876  1.00 31.20  ? 89  ILE   A HA   1 
ATOM   1365 H HB   . ILE   A 1 104 ? 5.752   17.510  15.537  1.00 37.12  ? 89  ILE   A HB   1 
ATOM   1366 H HG12 . ILE   A 1 104 ? 6.044   16.824  17.949  1.00 47.12  ? 89  ILE   A HG12 1 
ATOM   1367 H HG13 . ILE   A 1 104 ? 4.827   17.829  18.133  1.00 47.12  ? 89  ILE   A HG13 1 
ATOM   1368 H HG21 . ILE   A 1 104 ? 7.748   17.744  16.850  1.00 37.43  ? 89  ILE   A HG21 1 
ATOM   1369 H HG22 . ILE   A 1 104 ? 7.581   18.884  15.755  1.00 37.43  ? 89  ILE   A HG22 1 
ATOM   1370 H HG23 . ILE   A 1 104 ? 7.228   19.184  17.275  1.00 37.43  ? 89  ILE   A HG23 1 
ATOM   1371 H HD11 . ILE   A 1 104 ? 3.696   15.985  17.853  1.00 50.47  ? 89  ILE   A HD11 1 
ATOM   1372 H HD12 . ILE   A 1 104 ? 3.828   16.410  16.328  1.00 50.47  ? 89  ILE   A HD12 1 
ATOM   1373 H HD13 . ILE   A 1 104 ? 4.815   15.326  16.939  1.00 50.47  ? 89  ILE   A HD13 1 
ATOM   1374 N N    . CYS   A 1 105 ? 5.897   21.266  15.092  1.00 27.80  ? 90  CYS   A N    1 
ATOM   1375 C CA   . CYS   A 1 105 ? 6.354   22.124  14.005  1.00 25.35  ? 90  CYS   A CA   1 
ATOM   1376 C C    . CYS   A 1 105 ? 7.864   22.010  13.854  1.00 25.79  ? 90  CYS   A C    1 
ATOM   1377 O O    . CYS   A 1 105 ? 8.609   22.241  14.811  1.00 26.50  ? 90  CYS   A O    1 
ATOM   1378 C CB   . CYS   A 1 105 ? 5.966   23.580  14.256  1.00 26.25  ? 90  CYS   A CB   1 
ATOM   1379 S SG   . CYS   A 1 105 ? 6.381   24.624  12.860  1.00 32.69  ? 90  CYS   A SG   1 
ATOM   1380 H H    . CYS   A 1 105 ? 6.004   21.608  15.874  1.00 33.36  ? 90  CYS   A H    1 
ATOM   1381 H HA   . CYS   A 1 105 ? 5.939   21.832  13.178  1.00 30.42  ? 90  CYS   A HA   1 
ATOM   1382 H HB2  . CYS   A 1 105 ? 5.010   23.635  14.405  1.00 31.50  ? 90  CYS   A HB2  1 
ATOM   1383 H HB3  . CYS   A 1 105 ? 6.443   23.908  15.035  1.00 31.50  ? 90  CYS   A HB3  1 
ATOM   1384 H HG   . CYS   A 1 105 ? 6.184   25.770  13.157  1.00 39.23  ? 90  CYS   A HG   1 
ATOM   1385 N N    . MET   A 1 106 ? 8.310   21.686  12.642  1.00 25.24  ? 91  MET   A N    1 
ATOM   1386 C CA   . MET   A 1 106 ? 9.707   21.397  12.382  1.00 27.39  ? 91  MET   A CA   1 
ATOM   1387 C C    . MET   A 1 106 ? 10.162  22.069  11.096  1.00 26.09  ? 91  MET   A C    1 
ATOM   1388 O O    . MET   A 1 106 ? 9.358   22.441  10.236  1.00 23.09  ? 91  MET   A O    1 
ATOM   1389 C CB   . MET   A 1 106 ? 9.960   19.887  12.252  1.00 21.79  ? 91  MET   A CB   1 
ATOM   1390 C CG   . MET   A 1 106 ? 9.634   19.096  13.483  1.00 29.80  ? 91  MET   A CG   1 
ATOM   1391 S SD   . MET   A 1 106 ? 9.697   17.322  13.132  1.00 41.06  ? 91  MET   A SD   1 
ATOM   1392 C CE   . MET   A 1 106 ? 8.257   17.132  12.073  1.00 30.41  ? 91  MET   A CE   1 
ATOM   1393 H H    . MET   A 1 106 ? 7.809   21.629  11.945  1.00 30.29  ? 91  MET   A H    1 
ATOM   1394 H HA   . MET   A 1 106 ? 10.220  21.750  13.125  1.00 32.87  ? 91  MET   A HA   1 
ATOM   1395 H HB2  . MET   A 1 106 ? 9.413   19.543  11.529  1.00 26.14  ? 91  MET   A HB2  1 
ATOM   1396 H HB3  . MET   A 1 106 ? 10.899  19.746  12.053  1.00 26.14  ? 91  MET   A HB3  1 
ATOM   1397 H HG2  . MET   A 1 106 ? 10.279  19.298  14.178  1.00 35.76  ? 91  MET   A HG2  1 
ATOM   1398 H HG3  . MET   A 1 106 ? 8.739   19.320  13.785  1.00 35.76  ? 91  MET   A HG3  1 
ATOM   1399 H HE1  . MET   A 1 106 ? 8.068   16.187  11.964  1.00 36.50  ? 91  MET   A HE1  1 
ATOM   1400 H HE2  . MET   A 1 106 ? 7.500   17.576  12.486  1.00 36.50  ? 91  MET   A HE2  1 
ATOM   1401 H HE3  . MET   A 1 106 ? 8.445   17.533  11.209  1.00 36.50  ? 91  MET   A HE3  1 
ATOM   1402 N N    . GLU   A 1 107 ? 11.483  22.194  10.986  1.00 27.58  ? 92  GLU   A N    1 
ATOM   1403 C CA   . GLU   A 1 107 ? 12.140  22.602  9.754   1.00 31.84  ? 92  GLU   A CA   1 
ATOM   1404 C C    . GLU   A 1 107 ? 11.652  21.763  8.581   1.00 31.29  ? 92  GLU   A C    1 
ATOM   1405 O O    . GLU   A 1 107 ? 11.391  20.566  8.719   1.00 27.76  ? 92  GLU   A O    1 
ATOM   1406 C CB   . GLU   A 1 107 ? 13.654  22.443  9.935   1.00 37.02  ? 92  GLU   A CB   1 
ATOM   1407 C CG   . GLU   A 1 107 ? 14.520  22.941  8.809   1.00 34.42  ? 92  GLU   A CG   1 
ATOM   1408 C CD   . GLU   A 1 107 ? 16.009  22.687  9.067   1.00 37.02  ? 92  GLU   A CD   1 
ATOM   1409 O OE1  . GLU   A 1 107 ? 16.364  22.186  10.162  1.00 29.37  ? 92  GLU   A OE1  1 
ATOM   1410 O OE2  . GLU   A 1 107 ? 16.826  22.987  8.170   1.00 34.66  ? 92  GLU   A OE2  1 
ATOM   1411 H H    . GLU   A 1 107 ? 12.034  22.044  11.629  1.00 33.10  ? 92  GLU   A H    1 
ATOM   1412 H HA   . GLU   A 1 107 ? 11.939  23.529  9.552   1.00 38.20  ? 92  GLU   A HA   1 
ATOM   1413 H HB2  . GLU   A 1 107 ? 13.915  22.930  10.732  1.00 44.43  ? 92  GLU   A HB2  1 
ATOM   1414 H HB3  . GLU   A 1 107 ? 13.846  21.499  10.045  1.00 44.43  ? 92  GLU   A HB3  1 
ATOM   1415 H HG2  . GLU   A 1 107 ? 14.272  22.483  7.991   1.00 41.30  ? 92  GLU   A HG2  1 
ATOM   1416 H HG3  . GLU   A 1 107 ? 14.390  23.897  8.707   1.00 41.30  ? 92  GLU   A HG3  1 
ATOM   1417 N N    . PHE   A 1 108 ? 11.536  22.402  7.416   1.00 24.04  ? 93  PHE   A N    1 
ATOM   1418 C CA   . PHE   A 1 108 ? 11.076  21.744  6.199   1.00 32.49  ? 93  PHE   A CA   1 
ATOM   1419 C C    . PHE   A 1 108 ? 12.260  21.301  5.351   1.00 25.21  ? 93  PHE   A C    1 
ATOM   1420 O O    . PHE   A 1 108 ? 13.174  22.089  5.096   1.00 28.27  ? 93  PHE   A O    1 
ATOM   1421 C CB   . PHE   A 1 108 ? 10.183  22.680  5.391   1.00 24.41  ? 93  PHE   A CB   1 
ATOM   1422 C CG   . PHE   A 1 108 ? 9.737   22.114  4.077   1.00 25.36  ? 93  PHE   A CG   1 
ATOM   1423 C CD1  . PHE   A 1 108 ? 8.897   21.020  4.032   1.00 24.71  ? 93  PHE   A CD1  1 
ATOM   1424 C CD2  . PHE   A 1 108 ? 10.138  22.691  2.885   1.00 24.08  ? 93  PHE   A CD2  1 
ATOM   1425 C CE1  . PHE   A 1 108 ? 8.472   20.511  2.829   1.00 22.04  ? 93  PHE   A CE1  1 
ATOM   1426 C CE2  . PHE   A 1 108 ? 9.715   22.176  1.679   1.00 22.23  ? 93  PHE   A CE2  1 
ATOM   1427 C CZ   . PHE   A 1 108 ? 8.882   21.091  1.652   1.00 23.10  ? 93  PHE   A CZ   1 
ATOM   1428 H H    . PHE   A 1 108 ? 11.722  23.234  7.306   1.00 28.85  ? 93  PHE   A H    1 
ATOM   1429 H HA   . PHE   A 1 108 ? 10.570  20.953  6.442   1.00 38.99  ? 93  PHE   A HA   1 
ATOM   1430 H HB2  . PHE   A 1 108 ? 9.388   22.879  5.911   1.00 29.29  ? 93  PHE   A HB2  1 
ATOM   1431 H HB3  . PHE   A 1 108 ? 10.672  23.498  5.209   1.00 29.29  ? 93  PHE   A HB3  1 
ATOM   1432 H HD1  . PHE   A 1 108 ? 8.615   20.624  4.824   1.00 29.65  ? 93  PHE   A HD1  1 
ATOM   1433 H HD2  . PHE   A 1 108 ? 10.698  23.433  2.897   1.00 28.90  ? 93  PHE   A HD2  1 
ATOM   1434 H HE1  . PHE   A 1 108 ? 7.906   19.772  2.810   1.00 26.45  ? 93  PHE   A HE1  1 
ATOM   1435 H HE2  . PHE   A 1 108 ? 9.995   22.566  0.883   1.00 26.68  ? 93  PHE   A HE2  1 
ATOM   1436 H HZ   . PHE   A 1 108 ? 8.594   20.747  0.838   1.00 27.72  ? 93  PHE   A HZ   1 
ATOM   1437 N N    . CYS   A 1 109 ? 12.227  20.048  4.905   1.00 27.34  ? 94  CYS   A N    1 
ATOM   1438 C CA   . CYS   A 1 109 ? 13.269  19.459  4.065   1.00 27.69  ? 94  CYS   A CA   1 
ATOM   1439 C C    . CYS   A 1 109 ? 12.611  18.932  2.795   1.00 24.26  ? 94  CYS   A C    1 
ATOM   1440 O O    . CYS   A 1 109 ? 12.107  17.804  2.766   1.00 25.92  ? 94  CYS   A O    1 
ATOM   1441 C CB   . CYS   A 1 109 ? 14.002  18.359  4.823   1.00 29.20  ? 94  CYS   A CB   1 
ATOM   1442 S SG   . CYS   A 1 109 ? 14.834  18.951  6.327   1.00 32.04  ? 94  CYS   A SG   1 
ATOM   1443 H H    . CYS   A 1 109 ? 11.588  19.500  5.081   1.00 32.81  ? 94  CYS   A H    1 
ATOM   1444 H HA   . CYS   A 1 109 ? 13.910  20.140  3.809   1.00 33.23  ? 94  CYS   A HA   1 
ATOM   1445 H HB2  . CYS   A 1 109 ? 13.361  17.679  5.084   1.00 35.04  ? 94  CYS   A HB2  1 
ATOM   1446 H HB3  . CYS   A 1 109 ? 14.676  17.974  4.241   1.00 35.04  ? 94  CYS   A HB3  1 
ATOM   1447 H HG   . CYS   A 1 109 ? 15.402  18.030  6.846   1.00 38.45  ? 94  CYS   A HG   1 
ATOM   1448 N N    . GLY   A 1 110 ? 12.670  19.738  1.733   1.00 21.76  ? 95  GLY   A N    1 
ATOM   1449 C CA   . GLY   A 1 110 ? 11.796  19.558  0.586   1.00 22.78  ? 95  GLY   A CA   1 
ATOM   1450 C C    . GLY   A 1 110 ? 12.108  18.355  -0.281  1.00 29.66  ? 95  GLY   A C    1 
ATOM   1451 O O    . GLY   A 1 110 ? 11.263  17.960  -1.094  1.00 31.40  ? 95  GLY   A O    1 
ATOM   1452 H H    . GLY   A 1 110 ? 13.213  20.400  1.655   1.00 26.11  ? 95  GLY   A H    1 
ATOM   1453 H HA2  . GLY   A 1 110 ? 10.884  19.463  0.904   1.00 27.33  ? 95  GLY   A HA2  1 
ATOM   1454 H HA3  . GLY   A 1 110 ? 11.854  20.348  0.026   1.00 27.33  ? 95  GLY   A HA3  1 
ATOM   1455 N N    . ALA   A 1 111 ? 13.293  17.769  -0.143  1.00 20.98  ? 96  ALA   A N    1 
ATOM   1456 C CA   . ALA   A 1 111 ? 13.676  16.621  -0.958  1.00 24.83  ? 96  ALA   A CA   1 
ATOM   1457 C C    . ALA   A 1 111 ? 13.467  15.288  -0.249  1.00 21.84  ? 96  ALA   A C    1 
ATOM   1458 O O    . ALA   A 1 111 ? 13.770  14.243  -0.829  1.00 31.84  ? 96  ALA   A O    1 
ATOM   1459 C CB   . ALA   A 1 111 ? 15.140  16.740  -1.387  1.00 26.76  ? 96  ALA   A CB   1 
ATOM   1460 H H    . ALA   A 1 111 ? 13.894  18.019  0.419   1.00 25.17  ? 96  ALA   A H    1 
ATOM   1461 H HA   . ALA   A 1 111 ? 13.127  16.623  -1.758  1.00 29.79  ? 96  ALA   A HA   1 
ATOM   1462 H HB1  . ALA   A 1 111 ? 15.374  15.969  -1.927  1.00 32.12  ? 96  ALA   A HB1  1 
ATOM   1463 H HB2  . ALA   A 1 111 ? 15.252  17.553  -1.904  1.00 32.12  ? 96  ALA   A HB2  1 
ATOM   1464 H HB3  . ALA   A 1 111 ? 15.699  16.771  -0.595  1.00 32.12  ? 96  ALA   A HB3  1 
ATOM   1465 N N    . GLY   A 1 112 ? 12.977  15.295  0.990   1.00 23.37  ? 97  GLY   A N    1 
ATOM   1466 C CA   . GLY   A 1 112 ? 12.680  14.053  1.681   1.00 31.17  ? 97  GLY   A CA   1 
ATOM   1467 C C    . GLY   A 1 112 ? 13.928  13.386  2.239   1.00 26.62  ? 97  GLY   A C    1 
ATOM   1468 O O    . GLY   A 1 112 ? 14.934  14.034  2.521   1.00 23.66  ? 97  GLY   A O    1 
ATOM   1469 H H    . GLY   A 1 112 ? 12.809  16.005  1.447   1.00 28.05  ? 97  GLY   A H    1 
ATOM   1470 H HA2  . GLY   A 1 112 ? 12.074  14.232  2.417   1.00 37.41  ? 97  GLY   A HA2  1 
ATOM   1471 H HA3  . GLY   A 1 112 ? 12.255  13.437  1.064   1.00 37.41  ? 97  GLY   A HA3  1 
ATOM   1472 N N    . SER   A 1 113 ? 13.851  12.068  2.391   1.00 24.88  ? 98  SER   A N    1 
ATOM   1473 C CA   . SER   A 1 113 ? 14.946  11.289  2.943   1.00 19.90  ? 98  SER   A CA   1 
ATOM   1474 C C    . SER   A 1 113 ? 15.876  10.826  1.828   1.00 18.68  ? 98  SER   A C    1 
ATOM   1475 O O    . SER   A 1 113 ? 15.498  10.766  0.661   1.00 20.86  ? 98  SER   A O    1 
ATOM   1476 C CB   . SER   A 1 113 ? 14.421  10.072  3.709   1.00 23.18  ? 98  SER   A CB   1 
ATOM   1477 O OG   . SER   A 1 113 ? 14.105  9.014   2.815   1.00 26.80  ? 98  SER   A OG   1 
ATOM   1478 H H    . SER   A 1 113 ? 13.163  11.598  2.177   1.00 29.85  ? 98  SER   A H    1 
ATOM   1479 H HA   . SER   A 1 113 ? 15.448  11.841  3.562   1.00 23.88  ? 98  SER   A HA   1 
ATOM   1480 H HB2  . SER   A 1 113 ? 15.103  9.770   4.329   1.00 27.82  ? 98  SER   A HB2  1 
ATOM   1481 H HB3  . SER   A 1 113 ? 13.620  10.326  4.194   1.00 27.82  ? 98  SER   A HB3  1 
ATOM   1482 H HG   . SER   A 1 113 ? 13.819  8.351   3.244   1.00 32.16  ? 98  SER   A HG   1 
ATOM   1483 N N    . LEU   A 1 114 ? 17.118  10.521  2.207   1.00 18.84  ? 99  LEU   A N    1 
ATOM   1484 C CA   . LEU   A 1 114 ? 18.061  9.947   1.257   1.00 23.96  ? 99  LEU   A CA   1 
ATOM   1485 C C    . LEU   A 1 114 ? 17.555  8.627   0.680   1.00 19.92  ? 99  LEU   A C    1 
ATOM   1486 O O    . LEU   A 1 114 ? 17.849  8.305   -0.478  1.00 21.51  ? 99  LEU   A O    1 
ATOM   1487 C CB   . LEU   A 1 114 ? 19.421  9.757   1.935   1.00 23.09  ? 99  LEU   A CB   1 
ATOM   1488 C CG   . LEU   A 1 114 ? 20.307  11.006  1.979   1.00 21.70  ? 99  LEU   A CG   1 
ATOM   1489 C CD1  . LEU   A 1 114 ? 21.588  10.763  2.746   1.00 25.07  ? 99  LEU   A CD1  1 
ATOM   1490 C CD2  . LEU   A 1 114 ? 20.636  11.441  0.574   1.00 19.88  ? 99  LEU   A CD2  1 
ATOM   1491 H H    . LEU   A 1 114 ? 17.433  10.636  2.999   1.00 22.61  ? 99  LEU   A H    1 
ATOM   1492 H HA   . LEU   A 1 114 ? 18.176  10.561  0.516   1.00 28.75  ? 99  LEU   A HA   1 
ATOM   1493 H HB2  . LEU   A 1 114 ? 19.270  9.476   2.851   1.00 27.71  ? 99  LEU   A HB2  1 
ATOM   1494 H HB3  . LEU   A 1 114 ? 19.909  9.071   1.453   1.00 27.71  ? 99  LEU   A HB3  1 
ATOM   1495 H HG   . LEU   A 1 114 ? 19.822  11.709  2.438   1.00 26.04  ? 99  LEU   A HG   1 
ATOM   1496 H HD11 . LEU   A 1 114 ? 22.095  11.589  2.784   1.00 30.08  ? 99  LEU   A HD11 1 
ATOM   1497 H HD12 . LEU   A 1 114 ? 21.368  10.468  3.643   1.00 30.08  ? 99  LEU   A HD12 1 
ATOM   1498 H HD13 . LEU   A 1 114 ? 22.104  10.079  2.290   1.00 30.08  ? 99  LEU   A HD13 1 
ATOM   1499 H HD21 . LEU   A 1 114 ? 21.423  12.008  0.594   1.00 23.85  ? 99  LEU   A HD21 1 
ATOM   1500 H HD22 . LEU   A 1 114 ? 20.808  10.655  0.032   1.00 23.85  ? 99  LEU   A HD22 1 
ATOM   1501 H HD23 . LEU   A 1 114 ? 19.883  11.934  0.212   1.00 23.85  ? 99  LEU   A HD23 1 
ATOM   1502 N N    . GLN   A 1 115 ? 16.799  7.846   1.459   1.00 19.00  ? 100 GLN   A N    1 
ATOM   1503 C CA   . GLN   A 1 115 ? 16.176  6.648   0.899   1.00 22.13  ? 100 GLN   A CA   1 
ATOM   1504 C C    . GLN   A 1 115 ? 15.192  7.012   -0.209  1.00 28.49  ? 100 GLN   A C    1 
ATOM   1505 O O    . GLN   A 1 115 ? 15.174  6.371   -1.266  1.00 25.01  ? 100 GLN   A O    1 
ATOM   1506 C CB   . GLN   A 1 115 ? 15.475  5.839   1.992   1.00 20.60  ? 100 GLN   A CB   1 
ATOM   1507 C CG   . GLN   A 1 115 ? 14.838  4.543   1.490   1.00 27.24  ? 100 GLN   A CG   1 
ATOM   1508 C CD   . GLN   A 1 115 ? 14.217  3.722   2.613   1.00 30.23  ? 100 GLN   A CD   1 
ATOM   1509 O OE1  . GLN   A 1 115 ? 14.924  3.092   3.402   1.00 29.80  ? 100 GLN   A OE1  1 
ATOM   1510 N NE2  . GLN   A 1 115 ? 12.893  3.741   2.695   1.00 33.71  ? 100 GLN   A NE2  1 
ATOM   1511 H H    . GLN   A 1 115 ? 16.637  7.985   2.292   1.00 22.80  ? 100 GLN   A H    1 
ATOM   1512 H HA   . GLN   A 1 115 ? 16.872  6.087   0.522   1.00 26.56  ? 100 GLN   A HA   1 
ATOM   1513 H HB2  . GLN   A 1 115 ? 16.125  5.605   2.672   1.00 24.72  ? 100 GLN   A HB2  1 
ATOM   1514 H HB3  . GLN   A 1 115 ? 14.771  6.383   2.379   1.00 24.72  ? 100 GLN   A HB3  1 
ATOM   1515 H HG2  . GLN   A 1 115 ? 14.138  4.759   0.854   1.00 32.69  ? 100 GLN   A HG2  1 
ATOM   1516 H HG3  . GLN   A 1 115 ? 15.519  4.000   1.063   1.00 32.69  ? 100 GLN   A HG3  1 
ATOM   1517 H HE21 . GLN   A 1 115 ? 12.434  4.201   2.131   1.00 40.45  ? 100 GLN   A HE21 1 
ATOM   1518 H HE22 . GLN   A 1 115 ? 12.494  3.294   3.311   1.00 40.45  ? 100 GLN   A HE22 1 
ATOM   1519 N N    . ASP   A 1 116 ? 14.377  8.051   0.007   1.00 22.62  ? 101 ASP   A N    1 
ATOM   1520 C CA   . ASP   A 1 116 ? 13.471  8.498   -1.044  1.00 26.61  ? 101 ASP   A CA   1 
ATOM   1521 C C    . ASP   A 1 116 ? 14.249  8.886   -2.292  1.00 27.60  ? 101 ASP   A C    1 
ATOM   1522 O O    . ASP   A 1 116 ? 13.776  8.684   -3.415  1.00 29.06  ? 101 ASP   A O    1 
ATOM   1523 C CB   . ASP   A 1 116 ? 12.639  9.701   -0.586  1.00 32.42  ? 101 ASP   A CB   1 
ATOM   1524 C CG   . ASP   A 1 116 ? 11.737  9.399   0.602   1.00 34.84  ? 101 ASP   A CG   1 
ATOM   1525 O OD1  . ASP   A 1 116 ? 11.299  8.243   0.782   1.00 30.17  ? 101 ASP   A OD1  1 
ATOM   1526 O OD2  . ASP   A 1 116 ? 11.445  10.357  1.354   1.00 30.68  ? 101 ASP   A OD2  1 
ATOM   1527 H H    . ASP   A 1 116 ? 14.332  8.502   0.739   1.00 27.14  ? 101 ASP   A H    1 
ATOM   1528 H HA   . ASP   A 1 116 ? 12.861  7.772   -1.244  1.00 31.93  ? 101 ASP   A HA   1 
ATOM   1529 H HB2  . ASP   A 1 116 ? 13.240  10.418  -0.327  1.00 38.90  ? 101 ASP   A HB2  1 
ATOM   1530 H HB3  . ASP   A 1 116 ? 12.076  9.990   -1.321  1.00 38.90  ? 101 ASP   A HB3  1 
ATOM   1531 N N    . ILE   A 1 117 ? 15.443  9.441   -2.109  1.00 24.80  ? 102 ILE   A N    1 
ATOM   1532 C CA   . ILE   A 1 117 ? 16.201  9.966   -3.235  1.00 20.44  ? 102 ILE   A CA   1 
ATOM   1533 C C    . ILE   A 1 117 ? 16.898  8.839   -3.995  1.00 22.12  ? 102 ILE   A C    1 
ATOM   1534 O O    . ILE   A 1 117 ? 16.765  8.737   -5.219  1.00 29.20  ? 102 ILE   A O    1 
ATOM   1535 C CB   . ILE   A 1 117 ? 17.195  11.031  -2.736  1.00 22.40  ? 102 ILE   A CB   1 
ATOM   1536 C CG1  . ILE   A 1 117 ? 16.447  12.196  -2.066  1.00 27.14  ? 102 ILE   A CG1  1 
ATOM   1537 C CG2  . ILE   A 1 117 ? 18.000  11.564  -3.869  1.00 25.08  ? 102 ILE   A CG2  1 
ATOM   1538 C CD1  . ILE   A 1 117 ? 17.343  13.170  -1.357  1.00 20.91  ? 102 ILE   A CD1  1 
ATOM   1539 H H    . ILE   A 1 117 ? 15.833  9.526   -1.348  1.00 29.76  ? 102 ILE   A H    1 
ATOM   1540 H HA   . ILE   A 1 117 ? 15.590  10.393  -3.856  1.00 24.53  ? 102 ILE   A HA   1 
ATOM   1541 H HB   . ILE   A 1 117 ? 17.781  10.606  -2.090  1.00 26.87  ? 102 ILE   A HB   1 
ATOM   1542 H HG12 . ILE   A 1 117 ? 15.959  12.685  -2.747  1.00 32.57  ? 102 ILE   A HG12 1 
ATOM   1543 H HG13 . ILE   A 1 117 ? 15.829  11.833  -1.412  1.00 32.57  ? 102 ILE   A HG13 1 
ATOM   1544 H HG21 . ILE   A 1 117 ? 18.558  12.289  -3.546  1.00 30.09  ? 102 ILE   A HG21 1 
ATOM   1545 H HG22 . ILE   A 1 117 ? 18.555  10.853  -4.225  1.00 30.09  ? 102 ILE   A HG22 1 
ATOM   1546 H HG23 . ILE   A 1 117 ? 17.399  11.891  -4.557  1.00 30.09  ? 102 ILE   A HG23 1 
ATOM   1547 H HD11 . ILE   A 1 117 ? 16.804  13.735  -0.781  1.00 25.09  ? 102 ILE   A HD11 1 
ATOM   1548 H HD12 . ILE   A 1 117 ? 17.989  12.677  -0.826  1.00 25.09  ? 102 ILE   A HD12 1 
ATOM   1549 H HD13 . ILE   A 1 117 ? 17.803  13.714  -2.016  1.00 25.09  ? 102 ILE   A HD13 1 
ATOM   1550 N N    . TYR   A 1 118 ? 17.649  7.972   -3.308  1.00 24.51  ? 103 TYR   A N    1 
ATOM   1551 C CA   . TYR   A 1 118 ? 18.411  6.981   -4.064  1.00 20.90  ? 103 TYR   A CA   1 
ATOM   1552 C C    . TYR   A 1 118 ? 17.517  5.922   -4.692  1.00 21.64  ? 103 TYR   A C    1 
ATOM   1553 O O    . TYR   A 1 118 ? 17.925  5.293   -5.672  1.00 24.66  ? 103 TYR   A O    1 
ATOM   1554 C CB   . TYR   A 1 118 ? 19.520  6.335   -3.218  1.00 20.49  ? 103 TYR   A CB   1 
ATOM   1555 C CG   . TYR   A 1 118 ? 19.124  5.428   -2.065  1.00 25.38  ? 103 TYR   A CG   1 
ATOM   1556 C CD1  . TYR   A 1 118 ? 18.423  4.255   -2.275  1.00 20.92  ? 103 TYR   A CD1  1 
ATOM   1557 C CD2  . TYR   A 1 118 ? 19.516  5.720   -0.767  1.00 23.14  ? 103 TYR   A CD2  1 
ATOM   1558 C CE1  . TYR   A 1 118 ? 18.089  3.426   -1.224  1.00 23.56  ? 103 TYR   A CE1  1 
ATOM   1559 C CE2  . TYR   A 1 118 ? 19.194  4.891   0.280   1.00 19.74  ? 103 TYR   A CE2  1 
ATOM   1560 C CZ   . TYR   A 1 118 ? 18.478  3.753   0.046   1.00 20.96  ? 103 TYR   A CZ   1 
ATOM   1561 O OH   . TYR   A 1 118 ? 18.153  2.940   1.098   1.00 23.01  ? 103 TYR   A OH   1 
ATOM   1562 H H    . TYR   A 1 118 ? 17.728  7.941   -2.453  1.00 29.41  ? 103 TYR   A H    1 
ATOM   1563 H HA   . TYR   A 1 118 ? 18.869  7.447   -4.781  1.00 25.08  ? 103 TYR   A HA   1 
ATOM   1564 H HB2  . TYR   A 1 118 ? 20.067  5.799   -3.813  1.00 24.58  ? 103 TYR   A HB2  1 
ATOM   1565 H HB3  . TYR   A 1 118 ? 20.050  7.051   -2.834  1.00 24.58  ? 103 TYR   A HB3  1 
ATOM   1566 H HD1  . TYR   A 1 118 ? 18.173  4.020   -3.140  1.00 25.11  ? 103 TYR   A HD1  1 
ATOM   1567 H HD2  . TYR   A 1 118 ? 20.008  6.492   -0.603  1.00 27.76  ? 103 TYR   A HD2  1 
ATOM   1568 H HE1  . TYR   A 1 118 ? 17.603  2.649   -1.378  1.00 28.27  ? 103 TYR   A HE1  1 
ATOM   1569 H HE2  . TYR   A 1 118 ? 19.462  5.105   1.144   1.00 23.69  ? 103 TYR   A HE2  1 
ATOM   1570 H HH   . TYR   A 1 118 ? 18.421  3.280   1.818   1.00 27.61  ? 103 TYR   A HH   1 
ATOM   1571 N N    . GLN   A 1 119 ? 16.291  5.744   -4.199  1.00 26.18  ? 104 GLN   A N    1 
ATOM   1572 C CA   . GLN   A 1 119 ? 15.367  4.848   -4.890  1.00 29.23  ? 104 GLN   A CA   1 
ATOM   1573 C C    . GLN   A 1 119 ? 15.013  5.366   -6.279  1.00 27.28  ? 104 GLN   A C    1 
ATOM   1574 O O    . GLN   A 1 119 ? 14.580  4.582   -7.128  1.00 29.77  ? 104 GLN   A O    1 
ATOM   1575 C CB   . GLN   A 1 119 ? 14.100  4.639   -4.054  1.00 25.06  ? 104 GLN   A CB   1 
ATOM   1576 C CG   . GLN   A 1 119 ? 14.329  3.770   -2.817  1.00 29.57  ? 104 GLN   A CG   1 
ATOM   1577 C CD   . GLN   A 1 119 ? 13.109  3.645   -1.900  1.00 33.68  ? 104 GLN   A CD   1 
ATOM   1578 O OE1  . GLN   A 1 119 ? 12.202  4.477   -1.910  1.00 38.37  ? 104 GLN   A OE1  1 
ATOM   1579 N NE2  . GLN   A 1 119 ? 13.099  2.594   -1.095  1.00 33.41  ? 104 GLN   A NE2  1 
ATOM   1580 H H    . GLN   A 1 119 ? 15.980  6.119   -3.490  1.00 31.42  ? 104 GLN   A H    1 
ATOM   1581 H HA   . GLN   A 1 119 ? 15.787  3.980   -4.993  1.00 35.08  ? 104 GLN   A HA   1 
ATOM   1582 H HB2  . GLN   A 1 119 ? 13.775  5.503   -3.756  1.00 30.08  ? 104 GLN   A HB2  1 
ATOM   1583 H HB3  . GLN   A 1 119 ? 13.430  4.204   -4.605  1.00 30.08  ? 104 GLN   A HB3  1 
ATOM   1584 H HG2  . GLN   A 1 119 ? 14.571  2.876   -3.107  1.00 35.48  ? 104 GLN   A HG2  1 
ATOM   1585 H HG3  . GLN   A 1 119 ? 15.049  4.156   -2.296  1.00 35.48  ? 104 GLN   A HG3  1 
ATOM   1586 H HE21 . GLN   A 1 119 ? 13.752  2.035   -1.109  1.00 40.09  ? 104 GLN   A HE21 1 
ATOM   1587 H HE22 . GLN   A 1 119 ? 12.439  2.471   -0.557  1.00 40.09  ? 104 GLN   A HE22 1 
ATOM   1588 N N    . VAL   A 1 120 ? 15.203  6.657   -6.531  1.00 28.46  ? 105 VAL   A N    1 
ATOM   1589 C CA   . VAL   A 1 120 ? 14.971  7.241   -7.846  1.00 30.01  ? 105 VAL   A CA   1 
ATOM   1590 C C    . VAL   A 1 120 ? 16.272  7.447   -8.612  1.00 28.02  ? 105 VAL   A C    1 
ATOM   1591 O O    . VAL   A 1 120 ? 16.334  7.181   -9.809  1.00 36.58  ? 105 VAL   A O    1 
ATOM   1592 C CB   . VAL   A 1 120 ? 14.207  8.575   -7.707  1.00 32.16  ? 105 VAL   A CB   1 
ATOM   1593 C CG1  . VAL   A 1 120 ? 14.202  9.320   -9.038  1.00 32.17  ? 105 VAL   A CG1  1 
ATOM   1594 C CG2  . VAL   A 1 120 ? 12.793  8.332   -7.204  1.00 34.52  ? 105 VAL   A CG2  1 
ATOM   1595 H H    . VAL   A 1 120 ? 15.472  7.226   -5.945  1.00 34.15  ? 105 VAL   A H    1 
ATOM   1596 H HA   . VAL   A 1 120 ? 14.423  6.626   -8.358  1.00 36.01  ? 105 VAL   A HA   1 
ATOM   1597 H HB   . VAL   A 1 120 ? 14.657  9.135   -7.055  1.00 38.59  ? 105 VAL   A HB   1 
ATOM   1598 H HG11 . VAL   A 1 120 ? 13.547  10.035  -8.997  1.00 38.60  ? 105 VAL   A HG11 1 
ATOM   1599 H HG12 . VAL   A 1 120 ? 15.084  9.689   -9.197  1.00 38.60  ? 105 VAL   A HG12 1 
ATOM   1600 H HG13 . VAL   A 1 120 ? 13.970  8.699   -9.746  1.00 38.60  ? 105 VAL   A HG13 1 
ATOM   1601 H HG21 . VAL   A 1 120 ? 12.333  9.183   -7.132  1.00 41.42  ? 105 VAL   A HG21 1 
ATOM   1602 H HG22 . VAL   A 1 120 ? 12.329  7.757   -7.832  1.00 41.42  ? 105 VAL   A HG22 1 
ATOM   1603 H HG23 . VAL   A 1 120 ? 12.836  7.905   -6.334  1.00 41.42  ? 105 VAL   A HG23 1 
ATOM   1604 N N    . THR   A 1 121 ? 17.312  7.935   -7.943  1.00 30.17  ? 106 THR   A N    1 
ATOM   1605 C CA   . THR   A 1 121 ? 18.541  8.311   -8.618  1.00 28.83  ? 106 THR   A CA   1 
ATOM   1606 C C    . THR   A 1 121 ? 19.525  7.162   -8.788  1.00 26.90  ? 106 THR   A C    1 
ATOM   1607 O O    . THR   A 1 121 ? 20.373  7.220   -9.684  1.00 24.41  ? 106 THR   A O    1 
ATOM   1608 C CB   . THR   A 1 121 ? 19.247  9.416   -7.836  1.00 26.86  ? 106 THR   A CB   1 
ATOM   1609 O OG1  . THR   A 1 121 ? 19.685  8.878   -6.586  1.00 28.46  ? 106 THR   A OG1  1 
ATOM   1610 C CG2  . THR   A 1 121 ? 18.319  10.573  -7.580  1.00 29.59  ? 106 THR   A CG2  1 
ATOM   1611 H H    . THR   A 1 121 ? 17.328  8.057   -7.092  1.00 36.20  ? 106 THR   A H    1 
ATOM   1612 H HA   . THR   A 1 121 ? 18.306  8.641   -9.499  1.00 34.59  ? 106 THR   A HA   1 
ATOM   1613 H HB   . THR   A 1 121 ? 20.003  9.749   -8.344  1.00 32.23  ? 106 THR   A HB   1 
ATOM   1614 H HG1  . THR   A 1 121 ? 20.032  9.484   -6.118  1.00 34.15  ? 106 THR   A HG1  1 
ATOM   1615 H HG21 . THR   A 1 121 ? 18.811  11.315  -7.197  1.00 35.51  ? 106 THR   A HG21 1 
ATOM   1616 H HG22 . THR   A 1 121 ? 17.911  10.861  -8.412  1.00 35.51  ? 106 THR   A HG22 1 
ATOM   1617 H HG23 . THR   A 1 121 ? 17.620  10.307  -6.962  1.00 35.51  ? 106 THR   A HG23 1 
ATOM   1618 N N    . GLY   A 1 122 ? 19.445  6.140   -7.950  1.00 28.81  ? 107 GLY   A N    1 
ATOM   1619 C CA   . GLY   A 1 122 ? 20.499  5.146   -7.888  1.00 30.17  ? 107 GLY   A CA   1 
ATOM   1620 C C    . GLY   A 1 122 ? 21.580  5.556   -6.905  1.00 26.30  ? 107 GLY   A C    1 
ATOM   1621 O O    . GLY   A 1 122 ? 21.485  6.573   -6.212  1.00 25.70  ? 107 GLY   A O    1 
ATOM   1622 H H    . GLY   A 1 122 ? 18.792  6.002   -7.408  1.00 34.57  ? 107 GLY   A H    1 
ATOM   1623 H HA2  . GLY   A 1 122 ? 20.128  4.295   -7.606  1.00 36.20  ? 107 GLY   A HA2  1 
ATOM   1624 H HA3  . GLY   A 1 122 ? 20.900  5.041   -8.765  1.00 36.20  ? 107 GLY   A HA3  1 
ATOM   1625 N N    . SER   A 1 123 ? 22.642  4.761   -6.870  1.00 22.97  ? 108 SER   A N    1 
ATOM   1626 C CA   . SER   A 1 123 ? 23.628  4.899   -5.805  1.00 28.86  ? 108 SER   A CA   1 
ATOM   1627 C C    . SER   A 1 123 ? 24.337  6.247   -5.879  1.00 25.49  ? 108 SER   A C    1 
ATOM   1628 O O    . SER   A 1 123 ? 24.565  6.803   -6.953  1.00 28.06  ? 108 SER   A O    1 
ATOM   1629 C CB   . SER   A 1 123 ? 24.653  3.767   -5.870  1.00 31.36  ? 108 SER   A CB   1 
ATOM   1630 O OG   . SER   A 1 123 ? 25.331  3.754   -7.116  1.00 31.63  ? 108 SER   A OG   1 
ATOM   1631 H H    . SER   A 1 123 ? 22.814  4.142   -7.442  1.00 27.57  ? 108 SER   A H    1 
ATOM   1632 H HA   . SER   A 1 123 ? 23.172  4.847   -4.951  1.00 34.63  ? 108 SER   A HA   1 
ATOM   1633 H HB2  . SER   A 1 123 ? 25.303  3.891   -5.161  1.00 37.63  ? 108 SER   A HB2  1 
ATOM   1634 H HB3  . SER   A 1 123 ? 24.194  2.921   -5.755  1.00 37.63  ? 108 SER   A HB3  1 
ATOM   1635 H HG   . SER   A 1 123 ? 24.783  3.633   -7.741  1.00 37.95  ? 108 SER   A HG   1 
ATOM   1636 N N    . LEU   A 1 124 ? 24.692  6.769   -4.711  1.00 26.13  ? 109 LEU   A N    1 
ATOM   1637 C CA   . LEU   A 1 124 ? 25.429  8.016   -4.639  1.00 29.53  ? 109 LEU   A CA   1 
ATOM   1638 C C    . LEU   A 1 124 ? 26.900  7.789   -4.961  1.00 28.81  ? 109 LEU   A C    1 
ATOM   1639 O O    . LEU   A 1 124 ? 27.441  6.691   -4.805  1.00 28.52  ? 109 LEU   A O    1 
ATOM   1640 C CB   . LEU   A 1 124 ? 25.304  8.641   -3.249  1.00 25.43  ? 109 LEU   A CB   1 
ATOM   1641 C CG   . LEU   A 1 124 ? 24.026  9.421   -2.966  1.00 25.78  ? 109 LEU   A CG   1 
ATOM   1642 C CD1  . LEU   A 1 124 ? 22.796  8.529   -3.091  1.00 26.69  ? 109 LEU   A CD1  1 
ATOM   1643 C CD2  . LEU   A 1 124 ? 24.124  10.052  -1.587  1.00 23.63  ? 109 LEU   A CD2  1 
ATOM   1644 H H    . LEU   A 1 124 ? 24.517  6.418   -3.946  1.00 31.35  ? 109 LEU   A H    1 
ATOM   1645 H HA   . LEU   A 1 124 ? 25.062  8.637   -5.288  1.00 35.44  ? 109 LEU   A HA   1 
ATOM   1646 H HB2  . LEU   A 1 124 ? 25.354  7.928   -2.594  1.00 30.52  ? 109 LEU   A HB2  1 
ATOM   1647 H HB3  . LEU   A 1 124 ? 26.046  9.255   -3.128  1.00 30.52  ? 109 LEU   A HB3  1 
ATOM   1648 H HG   . LEU   A 1 124 ? 23.918  10.128  -3.622  1.00 30.94  ? 109 LEU   A HG   1 
ATOM   1649 H HD11 . LEU   A 1 124 ? 22.014  9.025   -2.802  1.00 32.02  ? 109 LEU   A HD11 1 
ATOM   1650 H HD12 . LEU   A 1 124 ? 22.692  8.261   -4.018  1.00 32.02  ? 109 LEU   A HD12 1 
ATOM   1651 H HD13 . LEU   A 1 124 ? 22.916  7.745   -2.532  1.00 32.02  ? 109 LEU   A HD13 1 
ATOM   1652 H HD21 . LEU   A 1 124 ? 23.311  10.551  -1.410  1.00 28.36  ? 109 LEU   A HD21 1 
ATOM   1653 H HD22 . LEU   A 1 124 ? 24.233  9.350   -0.926  1.00 28.36  ? 109 LEU   A HD22 1 
ATOM   1654 H HD23 . LEU   A 1 124 ? 24.889  10.648  -1.566  1.00 28.36  ? 109 LEU   A HD23 1 
ATOM   1655 N N    . SER   A 1 125 ? 27.547  8.852   -5.419  1.00 27.67  ? 110 SER   A N    1 
ATOM   1656 C CA   . SER   A 1 125 ? 28.980  8.818   -5.631  1.00 22.31  ? 110 SER   A CA   1 
ATOM   1657 C C    . SER   A 1 125 ? 29.712  8.884   -4.297  1.00 21.75  ? 110 SER   A C    1 
ATOM   1658 O O    . SER   A 1 125 ? 29.159  9.289   -3.273  1.00 21.94  ? 110 SER   A O    1 
ATOM   1659 C CB   . SER   A 1 125 ? 29.411  9.989   -6.500  1.00 28.17  ? 110 SER   A CB   1 
ATOM   1660 O OG   . SER   A 1 125 ? 29.270  11.184  -5.761  1.00 25.13  ? 110 SER   A OG   1 
ATOM   1661 H H    . SER   A 1 125 ? 27.177  9.603   -5.613  1.00 33.20  ? 110 SER   A H    1 
ATOM   1662 H HA   . SER   A 1 125 ? 29.222  7.993   -6.081  1.00 26.77  ? 110 SER   A HA   1 
ATOM   1663 H HB2  . SER   A 1 125 ? 30.339  9.877   -6.758  1.00 33.80  ? 110 SER   A HB2  1 
ATOM   1664 H HB3  . SER   A 1 125 ? 28.850  10.030  -7.290  1.00 33.80  ? 110 SER   A HB3  1 
ATOM   1665 H HG   . SER   A 1 125 ? 29.509  11.840  -6.227  1.00 30.15  ? 110 SER   A HG   1 
ATOM   1666 N N    . GLU   A 1 126 ? 30.987  8.495   -4.320  1.00 22.59  ? 111 GLU   A N    1 
ATOM   1667 C CA   . GLU   A 1 126 ? 31.765  8.504   -3.086  1.00 22.49  ? 111 GLU   A CA   1 
ATOM   1668 C C    . GLU   A 1 126 ? 31.795  9.895   -2.458  1.00 23.56  ? 111 GLU   A C    1 
ATOM   1669 O O    . GLU   A 1 126 ? 31.683  10.033  -1.233  1.00 23.86  ? 111 GLU   A O    1 
ATOM   1670 C CB   . GLU   A 1 126 ? 33.185  8.007   -3.344  1.00 22.31  ? 111 GLU   A CB   1 
ATOM   1671 C CG   . GLU   A 1 126 ? 34.053  7.997   -2.104  1.00 22.93  ? 111 GLU   A CG   1 
ATOM   1672 C CD   . GLU   A 1 126 ? 35.397  7.334   -2.318  1.00 30.13  ? 111 GLU   A CD   1 
ATOM   1673 O OE1  . GLU   A 1 126 ? 35.481  6.390   -3.139  1.00 32.40  ? 111 GLU   A OE1  1 
ATOM   1674 O OE2  . GLU   A 1 126 ? 36.376  7.761   -1.668  1.00 27.02  ? 111 GLU   A OE2  1 
ATOM   1675 H H    . GLU   A 1 126 ? 31.412  8.229   -5.018  1.00 27.11  ? 111 GLU   A H    1 
ATOM   1676 H HA   . GLU   A 1 126 ? 31.347  7.896   -2.457  1.00 26.99  ? 111 GLU   A HA   1 
ATOM   1677 H HB2  . GLU   A 1 126 ? 33.143  7.100   -3.685  1.00 26.77  ? 111 GLU   A HB2  1 
ATOM   1678 H HB3  . GLU   A 1 126 ? 33.606  8.588   -3.997  1.00 26.77  ? 111 GLU   A HB3  1 
ATOM   1679 H HG2  . GLU   A 1 126 ? 34.213  8.913   -1.826  1.00 27.51  ? 111 GLU   A HG2  1 
ATOM   1680 H HG3  . GLU   A 1 126 ? 33.591  7.514   -1.402  1.00 27.51  ? 111 GLU   A HG3  1 
ATOM   1681 N N    . LEU   A 1 127 ? 31.939  10.941  -3.275  1.00 25.46  ? 112 LEU   A N    1 
ATOM   1682 C CA   . LEU   A 1 127 ? 32.048  12.290  -2.722  1.00 25.45  ? 112 LEU   A CA   1 
ATOM   1683 C C    . LEU   A 1 127 ? 30.725  12.763  -2.132  1.00 21.40  ? 112 LEU   A C    1 
ATOM   1684 O O    . LEU   A 1 127 ? 30.712  13.454  -1.111  1.00 25.18  ? 112 LEU   A O    1 
ATOM   1685 C CB   . LEU   A 1 127 ? 32.534  13.262  -3.794  1.00 24.85  ? 112 LEU   A CB   1 
ATOM   1686 C CG   . LEU   A 1 127 ? 34.028  13.186  -4.105  1.00 27.43  ? 112 LEU   A CG   1 
ATOM   1687 C CD1  . LEU   A 1 127 ? 34.350  14.003  -5.346  1.00 36.54  ? 112 LEU   A CD1  1 
ATOM   1688 C CD2  . LEU   A 1 127 ? 34.834  13.673  -2.914  1.00 29.48  ? 112 LEU   A CD2  1 
ATOM   1689 H H    . LEU   A 1 127 ? 31.975  10.897  -4.133  1.00 30.55  ? 112 LEU   A H    1 
ATOM   1690 H HA   . LEU   A 1 127 ? 32.705  12.275  -2.008  1.00 30.55  ? 112 LEU   A HA   1 
ATOM   1691 H HB2  . LEU   A 1 127 ? 32.055  13.075  -4.617  1.00 29.83  ? 112 LEU   A HB2  1 
ATOM   1692 H HB3  . LEU   A 1 127 ? 32.343  14.166  -3.498  1.00 29.83  ? 112 LEU   A HB3  1 
ATOM   1693 H HG   . LEU   A 1 127 ? 34.276  12.265  -4.281  1.00 32.92  ? 112 LEU   A HG   1 
ATOM   1694 H HD11 . LEU   A 1 127 ? 35.305  13.965  -5.510  1.00 43.84  ? 112 LEU   A HD11 1 
ATOM   1695 H HD12 . LEU   A 1 127 ? 33.870  13.630  -6.103  1.00 43.84  ? 112 LEU   A HD12 1 
ATOM   1696 H HD13 . LEU   A 1 127 ? 34.075  14.921  -5.200  1.00 43.84  ? 112 LEU   A HD13 1 
ATOM   1697 H HD21 . LEU   A 1 127 ? 35.757  13.796  -3.186  1.00 35.38  ? 112 LEU   A HD21 1 
ATOM   1698 H HD22 . LEU   A 1 127 ? 34.465  14.515  -2.605  1.00 35.38  ? 112 LEU   A HD22 1 
ATOM   1699 H HD23 . LEU   A 1 127 ? 34.784  13.011  -2.206  1.00 35.38  ? 112 LEU   A HD23 1 
ATOM   1700 N N    . GLN   A 1 128 ? 29.605  12.422  -2.772  1.00 25.20  ? 113 GLN   A N    1 
ATOM   1701 C CA   . GLN   A 1 128 ? 28.310  12.703  -2.167  1.00 21.46  ? 113 GLN   A CA   1 
ATOM   1702 C C    . GLN   A 1 128 ? 28.161  11.959  -0.845  1.00 23.59  ? 113 GLN   A C    1 
ATOM   1703 O O    . GLN   A 1 128 ? 27.707  12.534  0.158   1.00 22.01  ? 113 GLN   A O    1 
ATOM   1704 C CB   . GLN   A 1 128 ? 27.191  12.328  -3.140  1.00 26.33  ? 113 GLN   A CB   1 
ATOM   1705 C CG   . GLN   A 1 128 ? 27.166  13.163  -4.412  1.00 27.10  ? 113 GLN   A CG   1 
ATOM   1706 C CD   . GLN   A 1 128 ? 26.264  12.581  -5.488  1.00 30.86  ? 113 GLN   A CD   1 
ATOM   1707 O OE1  . GLN   A 1 128 ? 26.085  11.366  -5.580  1.00 30.18  ? 113 GLN   A OE1  1 
ATOM   1708 N NE2  . GLN   A 1 128 ? 25.707  13.448  -6.321  1.00 30.56  ? 113 GLN   A NE2  1 
ATOM   1709 H H    . GLN   A 1 128 ? 29.571  12.036  -3.540  1.00 30.24  ? 113 GLN   A H    1 
ATOM   1710 H HA   . GLN   A 1 128 ? 28.236  13.653  -1.986  1.00 25.75  ? 113 GLN   A HA   1 
ATOM   1711 H HB2  . GLN   A 1 128 ? 27.303  11.400  -3.399  1.00 31.60  ? 113 GLN   A HB2  1 
ATOM   1712 H HB3  . GLN   A 1 128 ? 26.338  12.447  -2.692  1.00 31.60  ? 113 GLN   A HB3  1 
ATOM   1713 H HG2  . GLN   A 1 128 ? 26.841  14.052  -4.200  1.00 32.52  ? 113 GLN   A HG2  1 
ATOM   1714 H HG3  . GLN   A 1 128 ? 28.065  13.215  -4.772  1.00 32.52  ? 113 GLN   A HG3  1 
ATOM   1715 H HE21 . GLN   A 1 128 ? 25.864  14.289  -6.234  1.00 36.67  ? 113 GLN   A HE21 1 
ATOM   1716 H HE22 . GLN   A 1 128 ? 25.188  13.169  -6.948  1.00 36.67  ? 113 GLN   A HE22 1 
ATOM   1717 N N    . ILE   A 1 129 ? 28.552  10.682  -0.816  1.00 20.05  ? 114 ILE   A N    1 
ATOM   1718 C CA   . ILE   A 1 129 ? 28.501  9.912   0.423   1.00 19.59  ? 114 ILE   A CA   1 
ATOM   1719 C C    . ILE   A 1 129 ? 29.420  10.524  1.473   1.00 25.22  ? 114 ILE   A C    1 
ATOM   1720 O O    . ILE   A 1 129 ? 29.070  10.582  2.661   1.00 23.71  ? 114 ILE   A O    1 
ATOM   1721 C CB   . ILE   A 1 129 ? 28.860  8.437   0.155   1.00 19.71  ? 114 ILE   A CB   1 
ATOM   1722 C CG1  . ILE   A 1 129 ? 27.811  7.800   -0.761  1.00 27.37  ? 114 ILE   A CG1  1 
ATOM   1723 C CG2  . ILE   A 1 129 ? 28.961  7.653   1.472   1.00 21.66  ? 114 ILE   A CG2  1 
ATOM   1724 C CD1  . ILE   A 1 129 ? 28.090  6.316   -1.131  1.00 22.77  ? 114 ILE   A CD1  1 
ATOM   1725 H H    . ILE   A 1 129 ? 28.847  10.245  -1.495  1.00 24.06  ? 114 ILE   A H    1 
ATOM   1726 H HA   . ILE   A 1 129 ? 27.593  9.945   0.762   1.00 23.51  ? 114 ILE   A HA   1 
ATOM   1727 H HB   . ILE   A 1 129 ? 29.724  8.408   -0.285  1.00 23.65  ? 114 ILE   A HB   1 
ATOM   1728 H HG12 . ILE   A 1 129 ? 26.951  7.834   -0.314  1.00 32.85  ? 114 ILE   A HG12 1 
ATOM   1729 H HG13 . ILE   A 1 129 ? 27.776  8.306   -1.588  1.00 32.85  ? 114 ILE   A HG13 1 
ATOM   1730 H HG21 . ILE   A 1 129 ? 29.070  6.710   1.271   1.00 25.99  ? 114 ILE   A HG21 1 
ATOM   1731 H HG22 . ILE   A 1 129 ? 29.728  7.975   1.972   1.00 25.99  ? 114 ILE   A HG22 1 
ATOM   1732 H HG23 . ILE   A 1 129 ? 28.150  7.791   1.985   1.00 25.99  ? 114 ILE   A HG23 1 
ATOM   1733 H HD11 . ILE   A 1 129 ? 27.534  6.069   -1.887  1.00 27.32  ? 114 ILE   A HD11 1 
ATOM   1734 H HD12 . ILE   A 1 129 ? 29.027  6.219   -1.364  1.00 27.32  ? 114 ILE   A HD12 1 
ATOM   1735 H HD13 . ILE   A 1 129 ? 27.879  5.755   -0.369  1.00 27.32  ? 114 ILE   A HD13 1 
ATOM   1736 N N    . SER   A 1 130 ? 30.616  10.976  1.059   1.00 20.06  ? 115 SER   A N    1 
ATOM   1737 C CA   . SER   A 1 130 ? 31.544  11.590  2.007   1.00 25.22  ? 115 SER   A CA   1 
ATOM   1738 C C    . SER   A 1 130 ? 30.957  12.863  2.606   1.00 22.73  ? 115 SER   A C    1 
ATOM   1739 O O    . SER   A 1 130 ? 31.100  13.126  3.805   1.00 21.64  ? 115 SER   A O    1 
ATOM   1740 C CB   . SER   A 1 130 ? 32.880  11.906  1.325   1.00 22.49  ? 115 SER   A CB   1 
ATOM   1741 O OG   . SER   A 1 130 ? 33.394  10.788  0.621   1.00 29.34  ? 115 SER   A OG   1 
ATOM   1742 H H    . SER   A 1 130 ? 30.904  10.938  0.250   1.00 24.08  ? 115 SER   A H    1 
ATOM   1743 H HA   . SER   A 1 130 ? 31.711  10.955  2.722   1.00 30.27  ? 115 SER   A HA   1 
ATOM   1744 H HB2  . SER   A 1 130 ? 32.744  12.633  0.697   1.00 26.98  ? 115 SER   A HB2  1 
ATOM   1745 H HB3  . SER   A 1 130 ? 33.521  12.169  2.003   1.00 26.98  ? 115 SER   A HB3  1 
ATOM   1746 H HG   . SER   A 1 130 ? 32.859  10.560  0.014   1.00 35.21  ? 115 SER   A HG   1 
ATOM   1747 N N    . TYR   A 1 131 ? 30.294  13.672  1.785   1.00 22.92  ? 116 TYR   A N    1 
ATOM   1748 C CA   . TYR   A 1 131 ? 29.655  14.873  2.314   1.00 28.20  ? 116 TYR   A CA   1 
ATOM   1749 C C    . TYR   A 1 131 ? 28.553  14.527  3.307   1.00 23.54  ? 116 TYR   A C    1 
ATOM   1750 O O    . TYR   A 1 131 ? 28.442  15.155  4.364   1.00 20.11  ? 116 TYR   A O    1 
ATOM   1751 C CB   . TYR   A 1 131 ? 29.085  15.692  1.169   1.00 23.15  ? 116 TYR   A CB   1 
ATOM   1752 C CG   . TYR   A 1 131 ? 28.183  16.812  1.602   1.00 26.79  ? 116 TYR   A CG   1 
ATOM   1753 C CD1  . TYR   A 1 131 ? 28.685  17.921  2.269   1.00 21.94  ? 116 TYR   A CD1  1 
ATOM   1754 C CD2  . TYR   A 1 131 ? 26.830  16.777  1.316   1.00 22.91  ? 116 TYR   A CD2  1 
ATOM   1755 C CE1  . TYR   A 1 131 ? 27.858  18.963  2.649   1.00 29.58  ? 116 TYR   A CE1  1 
ATOM   1756 C CE2  . TYR   A 1 131 ? 26.001  17.808  1.688   1.00 24.40  ? 116 TYR   A CE2  1 
ATOM   1757 C CZ   . TYR   A 1 131 ? 26.522  18.899  2.350   1.00 26.11  ? 116 TYR   A CZ   1 
ATOM   1758 O OH   . TYR   A 1 131 ? 25.692  19.914  2.725   1.00 27.81  ? 116 TYR   A OH   1 
ATOM   1759 H H    . TYR   A 1 131 ? 30.202  13.552  0.938   1.00 27.50  ? 116 TYR   A H    1 
ATOM   1760 H HA   . TYR   A 1 131 ? 30.322  15.404  2.777   1.00 33.84  ? 116 TYR   A HA   1 
ATOM   1761 H HB2  . TYR   A 1 131 ? 29.821  16.082  0.672   1.00 27.78  ? 116 TYR   A HB2  1 
ATOM   1762 H HB3  . TYR   A 1 131 ? 28.570  15.105  0.594   1.00 27.78  ? 116 TYR   A HB3  1 
ATOM   1763 H HD1  . TYR   A 1 131 ? 29.593  17.965  2.463   1.00 26.33  ? 116 TYR   A HD1  1 
ATOM   1764 H HD2  . TYR   A 1 131 ? 26.476  16.045  0.866   1.00 27.49  ? 116 TYR   A HD2  1 
ATOM   1765 H HE1  . TYR   A 1 131 ? 28.204  19.698  3.102   1.00 35.50  ? 116 TYR   A HE1  1 
ATOM   1766 H HE2  . TYR   A 1 131 ? 25.092  17.770  1.494   1.00 29.28  ? 116 TYR   A HE2  1 
ATOM   1767 H HH   . TYR   A 1 131 ? 24.911  19.758  2.460   1.00 33.38  ? 116 TYR   A HH   1 
ATOM   1768 N N    . VAL   A 1 132 ? 27.732  13.524  2.982   1.00 19.32  ? 117 VAL   A N    1 
ATOM   1769 C CA   . VAL   A 1 132 ? 26.635  13.144  3.866   1.00 22.46  ? 117 VAL   A CA   1 
ATOM   1770 C C    . VAL   A 1 132 ? 27.177  12.672  5.207   1.00 22.65  ? 117 VAL   A C    1 
ATOM   1771 O O    . VAL   A 1 132 ? 26.692  13.074  6.273   1.00 21.33  ? 117 VAL   A O    1 
ATOM   1772 C CB   . VAL   A 1 132 ? 25.756  12.063  3.211   1.00 21.79  ? 117 VAL   A CB   1 
ATOM   1773 C CG1  . VAL   A 1 132 ? 24.785  11.479  4.235   1.00 23.64  ? 117 VAL   A CG1  1 
ATOM   1774 C CG2  . VAL   A 1 132 ? 24.970  12.645  2.051   1.00 21.38  ? 117 VAL   A CG2  1 
ATOM   1775 H H    . VAL   A 1 132 ? 27.790  13.055  2.264   1.00 23.19  ? 117 VAL   A H    1 
ATOM   1776 H HA   . VAL   A 1 132 ? 26.084  13.927  4.019   1.00 26.96  ? 117 VAL   A HA   1 
ATOM   1777 H HB   . VAL   A 1 132 ? 26.332  11.358  2.878   1.00 26.15  ? 117 VAL   A HB   1 
ATOM   1778 H HG11 . VAL   A 1 132 ? 24.091  10.987  3.767   1.00 28.37  ? 117 VAL   A HG11 1 
ATOM   1779 H HG12 . VAL   A 1 132 ? 25.270  10.884  4.827   1.00 28.37  ? 117 VAL   A HG12 1 
ATOM   1780 H HG13 . VAL   A 1 132 ? 24.390  12.203  4.745   1.00 28.37  ? 117 VAL   A HG13 1 
ATOM   1781 H HG21 . VAL   A 1 132 ? 24.441  11.942  1.643   1.00 25.66  ? 117 VAL   A HG21 1 
ATOM   1782 H HG22 . VAL   A 1 132 ? 24.388  13.346  2.384   1.00 25.66  ? 117 VAL   A HG22 1 
ATOM   1783 H HG23 . VAL   A 1 132 ? 25.591  13.011  1.401   1.00 25.66  ? 117 VAL   A HG23 1 
ATOM   1784 N N    . CYS   A 1 133 ? 28.178  11.798  5.176   1.00 23.03  ? 118 CYS   A N    1 
ATOM   1785 C CA   . CYS   A 1 133 ? 28.738  11.286  6.417   1.00 22.06  ? 118 CYS   A CA   1 
ATOM   1786 C C    . CYS   A 1 133 ? 29.303  12.409  7.274   1.00 23.15  ? 118 CYS   A C    1 
ATOM   1787 O O    . CYS   A 1 133 ? 29.097  12.425  8.491   1.00 22.85  ? 118 CYS   A O    1 
ATOM   1788 C CB   . CYS   A 1 133 ? 29.810  10.246  6.109   1.00 19.95  ? 118 CYS   A CB   1 
ATOM   1789 S SG   . CYS   A 1 133 ? 29.138  8.704   5.401   1.00 31.03  ? 118 CYS   A SG   1 
ATOM   1790 H H    . CYS   A 1 133 ? 28.545  11.491  4.460   1.00 27.63  ? 118 CYS   A H    1 
ATOM   1791 H HA   . CYS   A 1 133 ? 28.036  10.853  6.926   1.00 26.48  ? 118 CYS   A HA   1 
ATOM   1792 H HB2  . CYS   A 1 133 ? 30.435  10.620  5.469   1.00 23.94  ? 118 CYS   A HB2  1 
ATOM   1793 H HB3  . CYS   A 1 133 ? 30.272  10.019  6.931   1.00 23.94  ? 118 CYS   A HB3  1 
ATOM   1794 H HG   . CYS   A 1 133 ? 28.539  8.965   4.394   1.00 37.24  ? 118 CYS   A HG   1 
ATOM   1795 N N    . ARG   A 1 134 ? 30.031  13.348  6.672   1.00 21.63  ? 119 ARG   A N    1 
ATOM   1796 C CA   . ARG   A 1 134 ? 30.554  14.461  7.454   1.00 20.14  ? 119 ARG   A CA   1 
ATOM   1797 C C    . ARG   A 1 134 ? 29.422  15.196  8.174   1.00 23.72  ? 119 ARG   A C    1 
ATOM   1798 O O    . ARG   A 1 134 ? 29.495  15.446  9.382   1.00 23.14  ? 119 ARG   A O    1 
ATOM   1799 C CB   . ARG   A 1 134 ? 31.332  15.425  6.558   1.00 22.26  ? 119 ARG   A CB   1 
ATOM   1800 C CG   . ARG   A 1 134 ? 32.059  16.540  7.352   1.00 23.02  ? 119 ARG   A CG   1 
ATOM   1801 C CD   . ARG   A 1 134 ? 32.607  17.626  6.447   1.00 28.86  ? 119 ARG   A CD   1 
ATOM   1802 N NE   . ARG   A 1 134 ? 31.538  18.401  5.835   1.00 27.93  ? 119 ARG   A NE   1 
ATOM   1803 C CZ   . ARG   A 1 134 ? 31.721  19.371  4.950   1.00 25.23  ? 119 ARG   A CZ   1 
ATOM   1804 N NH1  . ARG   A 1 134 ? 32.928  19.700  4.520   1.00 28.08  ? 119 ARG   A NH1  1 
ATOM   1805 N NH2  . ARG   A 1 134 ? 30.663  20.022  4.479   1.00 32.09  ? 119 ARG   A NH2  1 
ATOM   1806 H H    . ARG   A 1 134 ? 30.231  13.362  5.836   1.00 25.95  ? 119 ARG   A H    1 
ATOM   1807 H HA   . ARG   A 1 134 ? 31.168  14.111  8.118   1.00 24.16  ? 119 ARG   A HA   1 
ATOM   1808 H HB2  . ARG   A 1 134 ? 32.001  14.926  6.065   1.00 26.71  ? 119 ARG   A HB2  1 
ATOM   1809 H HB3  . ARG   A 1 134 ? 30.714  15.851  5.943   1.00 26.71  ? 119 ARG   A HB3  1 
ATOM   1810 H HG2  . ARG   A 1 134 ? 31.433  16.950  7.970   1.00 27.62  ? 119 ARG   A HG2  1 
ATOM   1811 H HG3  . ARG   A 1 134 ? 32.801  16.151  7.840   1.00 27.62  ? 119 ARG   A HG3  1 
ATOM   1812 H HD2  . ARG   A 1 134 ? 33.161  18.229  6.968   1.00 34.64  ? 119 ARG   A HD2  1 
ATOM   1813 H HD3  . ARG   A 1 134 ? 33.133  17.220  5.741   1.00 34.64  ? 119 ARG   A HD3  1 
ATOM   1814 H HE   . ARG   A 1 134 ? 30.729  18.216  6.064   1.00 33.51  ? 119 ARG   A HE   1 
ATOM   1815 H HH11 . ARG   A 1 134 ? 33.618  19.281  4.815   1.00 33.69  ? 119 ARG   A HH11 1 
ATOM   1816 H HH12 . ARG   A 1 134 ? 33.022  20.333  3.946   1.00 33.69  ? 119 ARG   A HH12 1 
ATOM   1817 H HH21 . ARG   A 1 134 ? 29.874  19.812  4.749   1.00 38.51  ? 119 ARG   A HH21 1 
ATOM   1818 H HH22 . ARG   A 1 134 ? 30.767  20.654  3.905   1.00 38.51  ? 119 ARG   A HH22 1 
ATOM   1819 N N    . GLU   A 1 135 ? 28.357  15.531  7.441   1.00 22.09  ? 120 GLU   A N    1 
ATOM   1820 C CA   . GLU   A 1 135 ? 27.248  16.279  8.027   1.00 23.65  ? 120 GLU   A CA   1 
ATOM   1821 C C    . GLU   A 1 135 ? 26.526  15.482  9.108   1.00 19.51  ? 120 GLU   A C    1 
ATOM   1822 O O    . GLU   A 1 135 ? 26.066  16.045  10.107  1.00 22.33  ? 120 GLU   A O    1 
ATOM   1823 C CB   . GLU   A 1 135 ? 26.266  16.679  6.929   1.00 23.66  ? 120 GLU   A CB   1 
ATOM   1824 C CG   . GLU   A 1 135 ? 26.870  17.610  5.882   1.00 24.29  ? 120 GLU   A CG   1 
ATOM   1825 C CD   . GLU   A 1 135 ? 27.379  18.880  6.500   1.00 24.82  ? 120 GLU   A CD   1 
ATOM   1826 O OE1  . GLU   A 1 135 ? 26.546  19.689  6.954   1.00 29.72  ? 120 GLU   A OE1  1 
ATOM   1827 O OE2  . GLU   A 1 135 ? 28.611  19.053  6.560   1.00 30.95  ? 120 GLU   A OE2  1 
ATOM   1828 H H    . GLU   A 1 135 ? 28.253  15.338  6.610   1.00 26.51  ? 120 GLU   A H    1 
ATOM   1829 H HA   . GLU   A 1 135 ? 27.605  17.080  8.442   1.00 28.38  ? 120 GLU   A HA   1 
ATOM   1830 H HB2  . GLU   A 1 135 ? 25.962  15.878  6.474   1.00 28.39  ? 120 GLU   A HB2  1 
ATOM   1831 H HB3  . GLU   A 1 135 ? 25.512  17.136  7.334   1.00 28.39  ? 120 GLU   A HB3  1 
ATOM   1832 H HG2  . GLU   A 1 135 ? 27.614  17.164  5.447   1.00 29.15  ? 120 GLU   A HG2  1 
ATOM   1833 H HG3  . GLU   A 1 135 ? 26.192  17.840  5.227   1.00 29.15  ? 120 GLU   A HG3  1 
ATOM   1834 N N    . VAL   A 1 136 ? 26.386  14.169  8.908   1.00 21.73  ? 121 VAL   A N    1 
ATOM   1835 C CA   . VAL   A 1 136 ? 25.754  13.315  9.907   1.00 19.00  ? 121 VAL   A CA   1 
ATOM   1836 C C    . VAL   A 1 136 ? 26.623  13.207  11.154  1.00 22.60  ? 121 VAL   A C    1 
ATOM   1837 O O    . VAL   A 1 136 ? 26.113  13.216  12.284  1.00 23.95  ? 121 VAL   A O    1 
ATOM   1838 C CB   . VAL   A 1 136 ? 25.454  11.927  9.309   1.00 23.38  ? 121 VAL   A CB   1 
ATOM   1839 C CG1  . VAL   A 1 136 ? 25.059  10.939  10.420  1.00 22.83  ? 121 VAL   A CG1  1 
ATOM   1840 C CG2  . VAL   A 1 136 ? 24.359  12.032  8.256   1.00 25.42  ? 121 VAL   A CG2  1 
ATOM   1841 H H    . VAL   A 1 136 ? 26.648  13.751  8.203   1.00 26.07  ? 121 VAL   A H    1 
ATOM   1842 H HA   . VAL   A 1 136 ? 24.912  13.723  10.165  1.00 22.80  ? 121 VAL   A HA   1 
ATOM   1843 H HB   . VAL   A 1 136 ? 26.253  11.586  8.877   1.00 28.06  ? 121 VAL   A HB   1 
ATOM   1844 H HG11 . VAL   A 1 136 ? 24.573  10.198  10.025  1.00 27.39  ? 121 VAL   A HG11 1 
ATOM   1845 H HG12 . VAL   A 1 136 ? 25.863  10.614  10.854  1.00 27.39  ? 121 VAL   A HG12 1 
ATOM   1846 H HG13 . VAL   A 1 136 ? 24.496  11.397  11.064  1.00 27.39  ? 121 VAL   A HG13 1 
ATOM   1847 H HG21 . VAL   A 1 136 ? 24.224  11.159  7.854   1.00 30.51  ? 121 VAL   A HG21 1 
ATOM   1848 H HG22 . VAL   A 1 136 ? 23.540  12.330  8.681   1.00 30.51  ? 121 VAL   A HG22 1 
ATOM   1849 H HG23 . VAL   A 1 136 ? 24.632  12.670  7.579   1.00 30.51  ? 121 VAL   A HG23 1 
ATOM   1850 N N    . LEU   A 1 137 ? 27.943  13.089  10.972  1.00 19.53  ? 122 LEU   A N    1 
ATOM   1851 C CA   . LEU   A 1 137 ? 28.851  13.033  12.112  1.00 20.03  ? 122 LEU   A CA   1 
ATOM   1852 C C    . LEU   A 1 137 ? 28.839  14.328  12.906  1.00 23.63  ? 122 LEU   A C    1 
ATOM   1853 O O    . LEU   A 1 137 ? 28.997  14.301  14.132  1.00 23.16  ? 122 LEU   A O    1 
ATOM   1854 C CB   . LEU   A 1 137 ? 30.269  12.726  11.640  1.00 20.25  ? 122 LEU   A CB   1 
ATOM   1855 C CG   . LEU   A 1 137 ? 30.523  11.245  11.318  1.00 26.78  ? 122 LEU   A CG   1 
ATOM   1856 C CD1  . LEU   A 1 137 ? 31.822  11.063  10.571  1.00 28.52  ? 122 LEU   A CD1  1 
ATOM   1857 C CD2  . LEU   A 1 137 ? 30.536  10.439  12.601  1.00 23.86  ? 122 LEU   A CD2  1 
ATOM   1858 H H    . LEU   A 1 137 ? 28.331  13.040  10.206  1.00 23.44  ? 122 LEU   A H    1 
ATOM   1859 H HA   . LEU   A 1 137 ? 28.563  12.316  12.699  1.00 24.04  ? 122 LEU   A HA   1 
ATOM   1860 H HB2  . LEU   A 1 137 ? 30.443  13.237  10.834  1.00 24.30  ? 122 LEU   A HB2  1 
ATOM   1861 H HB3  . LEU   A 1 137 ? 30.890  12.986  12.339  1.00 24.30  ? 122 LEU   A HB3  1 
ATOM   1862 H HG   . LEU   A 1 137 ? 29.811  10.920  10.745  1.00 32.14  ? 122 LEU   A HG   1 
ATOM   1863 H HD11 . LEU   A 1 137 ? 31.949  10.120  10.384  1.00 34.22  ? 122 LEU   A HD11 1 
ATOM   1864 H HD12 . LEU   A 1 137 ? 31.781  11.562  9.740   1.00 34.22  ? 122 LEU   A HD12 1 
ATOM   1865 H HD13 . LEU   A 1 137 ? 32.551  11.392  11.119  1.00 34.22  ? 122 LEU   A HD13 1 
ATOM   1866 H HD21 . LEU   A 1 137 ? 30.876  9.550   12.413  1.00 28.63  ? 122 LEU   A HD21 1 
ATOM   1867 H HD22 . LEU   A 1 137 ? 31.109  10.882  13.247  1.00 28.63  ? 122 LEU   A HD22 1 
ATOM   1868 H HD23 . LEU   A 1 137 ? 29.632  10.381  12.947  1.00 28.63  ? 122 LEU   A HD23 1 
ATOM   1869 N N    . GLN   A 1 138 ? 28.670  15.469  12.239  1.00 21.32  ? 123 GLN   A N    1 
ATOM   1870 C CA   . GLN   A 1 138 ? 28.566  16.722  12.973  1.00 21.36  ? 123 GLN   A CA   1 
ATOM   1871 C C    . GLN   A 1 138 ? 27.335  16.698  13.874  1.00 21.33  ? 123 GLN   A C    1 
ATOM   1872 O O    . GLN   A 1 138 ? 27.423  17.002  15.065  1.00 23.31  ? 123 GLN   A O    1 
ATOM   1873 C CB   . GLN   A 1 138 ? 28.533  17.891  11.993  1.00 25.82  ? 123 GLN   A CB   1 
ATOM   1874 C CG   . GLN   A 1 138 ? 29.880  18.157  11.365  1.00 26.32  ? 123 GLN   A CG   1 
ATOM   1875 C CD   . GLN   A 1 138 ? 29.797  18.960  10.087  1.00 28.67  ? 123 GLN   A CD   1 
ATOM   1876 O OE1  . GLN   A 1 138 ? 28.727  19.431  9.687   1.00 26.06  ? 123 GLN   A OE1  1 
ATOM   1877 N NE2  . GLN   A 1 138 ? 30.932  19.109  9.428   1.00 23.65  ? 123 GLN   A NE2  1 
ATOM   1878 H H    . GLN   A 1 138 ? 28.615  15.541  11.384  1.00 25.58  ? 123 GLN   A H    1 
ATOM   1879 H HA   . GLN   A 1 138 ? 29.345  16.845  13.538  1.00 25.64  ? 123 GLN   A HA   1 
ATOM   1880 H HB2  . GLN   A 1 138 ? 27.904  17.691  11.283  1.00 30.99  ? 123 GLN   A HB2  1 
ATOM   1881 H HB3  . GLN   A 1 138 ? 28.257  18.692  12.465  1.00 30.99  ? 123 GLN   A HB3  1 
ATOM   1882 H HG2  . GLN   A 1 138 ? 30.426  18.655  11.994  1.00 31.59  ? 123 GLN   A HG2  1 
ATOM   1883 H HG3  . GLN   A 1 138 ? 30.302  17.309  11.158  1.00 31.59  ? 123 GLN   A HG3  1 
ATOM   1884 H HE21 . GLN   A 1 138 ? 31.656  18.759  9.733   1.00 28.39  ? 123 GLN   A HE21 1 
ATOM   1885 H HE22 . GLN   A 1 138 ? 30.946  19.556  8.693   1.00 28.39  ? 123 GLN   A HE22 1 
ATOM   1886 N N    . GLY   A 1 139 ? 26.188  16.297  13.324  1.00 21.59  ? 124 GLY   A N    1 
ATOM   1887 C CA   . GLY   A 1 139 ? 24.998  16.142  14.139  1.00 25.45  ? 124 GLY   A CA   1 
ATOM   1888 C C    . GLY   A 1 139 ? 25.201  15.174  15.289  1.00 27.41  ? 124 GLY   A C    1 
ATOM   1889 O O    . GLY   A 1 139 ? 24.831  15.459  16.431  1.00 21.84  ? 124 GLY   A O    1 
ATOM   1890 H H    . GLY   A 1 139 ? 26.079  16.112  12.492  1.00 25.91  ? 124 GLY   A H    1 
ATOM   1891 H HA2  . GLY   A 1 139 ? 24.747  17.004  14.507  1.00 30.53  ? 124 GLY   A HA2  1 
ATOM   1892 H HA3  . GLY   A 1 139 ? 24.273  15.811  13.587  1.00 30.53  ? 124 GLY   A HA3  1 
ATOM   1893 N N    . LEU   A 1 140 ? 25.807  14.017  15.003  1.00 20.73  ? 125 LEU   A N    1 
ATOM   1894 C CA   . LEU   A 1 140 ? 25.995  12.999  16.032  1.00 23.28  ? 125 LEU   A CA   1 
ATOM   1895 C C    . LEU   A 1 140 ? 26.984  13.457  17.094  1.00 23.15  ? 125 LEU   A C    1 
ATOM   1896 O O    . LEU   A 1 140 ? 26.811  13.162  18.285  1.00 28.56  ? 125 LEU   A O    1 
ATOM   1897 C CB   . LEU   A 1 140 ? 26.475  11.691  15.407  1.00 20.34  ? 125 LEU   A CB   1 
ATOM   1898 C CG   . LEU   A 1 140 ? 25.452  10.868  14.634  1.00 23.62  ? 125 LEU   A CG   1 
ATOM   1899 C CD1  . LEU   A 1 140 ? 26.137  9.636   14.001  1.00 27.85  ? 125 LEU   A CD1  1 
ATOM   1900 C CD2  . LEU   A 1 140 ? 24.313  10.442  15.523  1.00 19.85  ? 125 LEU   A CD2  1 
ATOM   1901 H H    . LEU   A 1 140 ? 26.114  13.802  14.229  1.00 24.88  ? 125 LEU   A H    1 
ATOM   1902 H HA   . LEU   A 1 140 ? 25.138  12.838  16.458  1.00 27.93  ? 125 LEU   A HA   1 
ATOM   1903 H HB2  . LEU   A 1 140 ? 27.192  11.903  14.789  1.00 24.40  ? 125 LEU   A HB2  1 
ATOM   1904 H HB3  . LEU   A 1 140 ? 26.810  11.126  16.121  1.00 24.40  ? 125 LEU   A HB3  1 
ATOM   1905 H HG   . LEU   A 1 140 ? 25.079  11.414  13.924  1.00 28.34  ? 125 LEU   A HG   1 
ATOM   1906 H HD11 . LEU   A 1 140 ? 25.473  9.120   13.517  1.00 33.42  ? 125 LEU   A HD11 1 
ATOM   1907 H HD12 . LEU   A 1 140 ? 26.830  9.937   13.393  1.00 33.42  ? 125 LEU   A HD12 1 
ATOM   1908 H HD13 . LEU   A 1 140 ? 26.527  9.095   14.706  1.00 33.42  ? 125 LEU   A HD13 1 
ATOM   1909 H HD21 . LEU   A 1 140 ? 23.772  9.788   15.053  1.00 23.83  ? 125 LEU   A HD21 1 
ATOM   1910 H HD22 . LEU   A 1 140 ? 24.674  10.051  16.334  1.00 23.83  ? 125 LEU   A HD22 1 
ATOM   1911 H HD23 . LEU   A 1 140 ? 23.776  11.219  15.742  1.00 23.83  ? 125 LEU   A HD23 1 
ATOM   1912 N N    . ALA   A 1 141 ? 28.045  14.149  16.687  1.00 22.84  ? 126 ALA   A N    1 
ATOM   1913 C CA   . ALA   A 1 141 ? 28.971  14.693  17.670  1.00 26.84  ? 126 ALA   A CA   1 
ATOM   1914 C C    . ALA   A 1 141 ? 28.248  15.622  18.639  1.00 25.54  ? 126 ALA   A C    1 
ATOM   1915 O O    . ALA   A 1 141 ? 28.493  15.582  19.851  1.00 24.27  ? 126 ALA   A O    1 
ATOM   1916 C CB   . ALA   A 1 141 ? 30.109  15.430  16.970  1.00 25.93  ? 126 ALA   A CB   1 
ATOM   1917 H H    . ALA   A 1 141 ? 28.246  14.313  15.867  1.00 27.41  ? 126 ALA   A H    1 
ATOM   1918 H HA   . ALA   A 1 141 ? 29.358  13.963  18.178  1.00 32.21  ? 126 ALA   A HA   1 
ATOM   1919 H HB1  . ALA   A 1 141 ? 30.716  15.784  17.639  1.00 31.12  ? 126 ALA   A HB1  1 
ATOM   1920 H HB2  . ALA   A 1 141 ? 30.580  14.809  16.392  1.00 31.12  ? 126 ALA   A HB2  1 
ATOM   1921 H HB3  . ALA   A 1 141 ? 29.738  16.156  16.443  1.00 31.12  ? 126 ALA   A HB3  1 
ATOM   1922 N N    . TYR   A 1 142 ? 27.338  16.458  18.125  1.00 25.42  ? 127 TYR   A N    1 
ATOM   1923 C CA   . TYR   A 1 142 ? 26.575  17.334  19.010  1.00 28.08  ? 127 TYR   A CA   1 
ATOM   1924 C C    . TYR   A 1 142 ? 25.652  16.527  19.921  1.00 26.34  ? 127 TYR   A C    1 
ATOM   1925 O O    . TYR   A 1 142 ? 25.640  16.729  21.141  1.00 28.75  ? 127 TYR   A O    1 
ATOM   1926 C CB   . TYR   A 1 142 ? 25.754  18.342  18.207  1.00 29.17  ? 127 TYR   A CB   1 
ATOM   1927 C CG   . TYR   A 1 142 ? 24.812  19.141  19.092  1.00 24.82  ? 127 TYR   A CG   1 
ATOM   1928 C CD1  . TYR   A 1 142 ? 25.243  20.289  19.753  1.00 30.70  ? 127 TYR   A CD1  1 
ATOM   1929 C CD2  . TYR   A 1 142 ? 23.501  18.733  19.283  1.00 25.32  ? 127 TYR   A CD2  1 
ATOM   1930 C CE1  . TYR   A 1 142 ? 24.376  21.008  20.571  1.00 29.63  ? 127 TYR   A CE1  1 
ATOM   1931 C CE2  . TYR   A 1 142 ? 22.645  19.435  20.092  1.00 31.97  ? 127 TYR   A CE2  1 
ATOM   1932 C CZ   . TYR   A 1 142 ? 23.079  20.562  20.735  1.00 27.27  ? 127 TYR   A CZ   1 
ATOM   1933 O OH   . TYR   A 1 142 ? 22.186  21.235  21.528  1.00 33.46  ? 127 TYR   A OH   1 
ATOM   1934 H H    . TYR   A 1 142 ? 27.151  16.533  17.289  1.00 30.50  ? 127 TYR   A H    1 
ATOM   1935 H HA   . TYR   A 1 142 ? 27.207  17.827  19.556  1.00 33.70  ? 127 TYR   A HA   1 
ATOM   1936 H HB2  . TYR   A 1 142 ? 26.355  18.962  17.765  1.00 35.00  ? 127 TYR   A HB2  1 
ATOM   1937 H HB3  . TYR   A 1 142 ? 25.223  17.868  17.548  1.00 35.00  ? 127 TYR   A HB3  1 
ATOM   1938 H HD1  . TYR   A 1 142 ? 26.120  20.578  19.648  1.00 36.84  ? 127 TYR   A HD1  1 
ATOM   1939 H HD2  . TYR   A 1 142 ? 23.195  17.967  18.854  1.00 30.39  ? 127 TYR   A HD2  1 
ATOM   1940 H HE1  . TYR   A 1 142 ? 24.667  21.779  21.001  1.00 35.55  ? 127 TYR   A HE1  1 
ATOM   1941 H HE2  . TYR   A 1 142 ? 21.768  19.145  20.204  1.00 38.36  ? 127 TYR   A HE2  1 
ATOM   1942 H HH   . TYR   A 1 142 ? 22.535  21.942  21.816  1.00 40.16  ? 127 TYR   A HH   1 
ATOM   1943 N N    . LEU   A 1 143 ? 24.846  15.634  19.343  1.00 26.96  ? 128 LEU   A N    1 
ATOM   1944 C CA   . LEU   A 1 143 ? 23.945  14.824  20.161  1.00 31.75  ? 128 LEU   A CA   1 
ATOM   1945 C C    . LEU   A 1 143 ? 24.706  14.135  21.284  1.00 25.53  ? 128 LEU   A C    1 
ATOM   1946 O O    . LEU   A 1 143 ? 24.311  14.200  22.455  1.00 29.76  ? 128 LEU   A O    1 
ATOM   1947 C CB   . LEU   A 1 143 ? 23.220  13.798  19.287  1.00 24.94  ? 128 LEU   A CB   1 
ATOM   1948 C CG   . LEU   A 1 143 ? 22.166  14.401  18.358  1.00 23.06  ? 128 LEU   A CG   1 
ATOM   1949 C CD1  . LEU   A 1 143 ? 21.550  13.325  17.516  1.00 21.01  ? 128 LEU   A CD1  1 
ATOM   1950 C CD2  . LEU   A 1 143 ? 21.095  15.139  19.148  1.00 27.63  ? 128 LEU   A CD2  1 
ATOM   1951 H H    . LEU   A 1 143 ? 24.803  15.481  18.498  1.00 32.36  ? 128 LEU   A H    1 
ATOM   1952 H HA   . LEU   A 1 143 ? 23.274  15.401  20.558  1.00 38.11  ? 128 LEU   A HA   1 
ATOM   1953 H HB2  . LEU   A 1 143 ? 23.875  13.345  18.734  1.00 29.93  ? 128 LEU   A HB2  1 
ATOM   1954 H HB3  . LEU   A 1 143 ? 22.774  13.160  19.864  1.00 29.93  ? 128 LEU   A HB3  1 
ATOM   1955 H HG   . LEU   A 1 143 ? 22.593  15.048  17.774  1.00 27.67  ? 128 LEU   A HG   1 
ATOM   1956 H HD11 . LEU   A 1 143 ? 20.894  13.724  16.923  1.00 25.22  ? 128 LEU   A HD11 1 
ATOM   1957 H HD12 . LEU   A 1 143 ? 22.247  12.894  16.996  1.00 25.22  ? 128 LEU   A HD12 1 
ATOM   1958 H HD13 . LEU   A 1 143 ? 21.121  12.677  18.096  1.00 25.22  ? 128 LEU   A HD13 1 
ATOM   1959 H HD21 . LEU   A 1 143 ? 20.324  15.283  18.577  1.00 33.16  ? 128 LEU   A HD21 1 
ATOM   1960 H HD22 . LEU   A 1 143 ? 20.843  14.602  19.915  1.00 33.16  ? 128 LEU   A HD22 1 
ATOM   1961 H HD23 . LEU   A 1 143 ? 21.452  15.992  19.443  1.00 33.16  ? 128 LEU   A HD23 1 
ATOM   1962 N N    . HIS   A 1 144 ? 25.823  13.492  20.944  1.00 23.68  ? 129 HIS   A N    1 
ATOM   1963 C CA   . HIS   A 1 144 ? 26.595  12.760  21.946  1.00 26.36  ? 129 HIS   A CA   1 
ATOM   1964 C C    . HIS   A 1 144 ? 27.149  13.698  23.012  1.00 30.48  ? 129 HIS   A C    1 
ATOM   1965 O O    . HIS   A 1 144 ? 27.217  13.333  24.191  1.00 30.71  ? 129 HIS   A O    1 
ATOM   1966 C CB   . HIS   A 1 144 ? 27.719  11.982  21.259  1.00 30.94  ? 129 HIS   A CB   1 
ATOM   1967 C CG   . HIS   A 1 144 ? 27.228  10.917  20.328  1.00 25.20  ? 129 HIS   A CG   1 
ATOM   1968 N ND1  . HIS   A 1 144 ? 28.080  10.124  19.586  1.00 27.58  ? 129 HIS   A ND1  1 
ATOM   1969 C CD2  . HIS   A 1 144 ? 25.973  10.508  20.022  1.00 26.13  ? 129 HIS   A CD2  1 
ATOM   1970 C CE1  . HIS   A 1 144 ? 27.369  9.275   18.862  1.00 31.98  ? 129 HIS   A CE1  1 
ATOM   1971 N NE2  . HIS   A 1 144 ? 26.087  9.484   19.112  1.00 26.90  ? 129 HIS   A NE2  1 
ATOM   1972 H H    . HIS   A 1 144 ? 26.152  13.464  20.150  1.00 28.41  ? 129 HIS   A H    1 
ATOM   1973 H HA   . HIS   A 1 144 ? 26.017  12.122  22.393  1.00 31.64  ? 129 HIS   A HA   1 
ATOM   1974 H HB2  . HIS   A 1 144 ? 28.258  12.601  20.743  1.00 37.13  ? 129 HIS   A HB2  1 
ATOM   1975 H HB3  . HIS   A 1 144 ? 28.264  11.554  21.938  1.00 37.13  ? 129 HIS   A HB3  1 
ATOM   1976 H HD2  . HIS   A 1 144 ? 25.181  10.856  20.364  1.00 31.36  ? 129 HIS   A HD2  1 
ATOM   1977 H HE1  . HIS   A 1 144 ? 27.712  8.639   18.277  1.00 38.38  ? 129 HIS   A HE1  1 
ATOM   1978 H HE2  . HIS   A 1 144 ? 25.432  9.050   18.763  1.00 32.28  ? 129 HIS   A HE2  1 
ATOM   1979 N N    . SER   A 1 145 ? 27.535  14.920  22.623  1.00 26.50  ? 130 SER   A N    1 
ATOM   1980 C CA   . SER   A 1 145 ? 28.029  15.865  23.618  1.00 28.71  ? 130 SER   A CA   1 
ATOM   1981 C C    . SER   A 1 145 ? 26.943  16.208  24.629  1.00 27.72  ? 130 SER   A C    1 
ATOM   1982 O O    . SER   A 1 145 ? 27.243  16.477  25.795  1.00 33.17  ? 130 SER   A O    1 
ATOM   1983 C CB   . SER   A 1 145 ? 28.552  17.140  22.948  1.00 32.18  ? 130 SER   A CB   1 
ATOM   1984 O OG   . SER   A 1 145 ? 27.501  17.893  22.367  1.00 32.17  ? 130 SER   A OG   1 
ATOM   1985 H H    . SER   A 1 145 ? 27.520  15.213  21.815  1.00 31.80  ? 130 SER   A H    1 
ATOM   1986 H HA   . SER   A 1 145 ? 28.776  15.460  24.086  1.00 34.46  ? 130 SER   A HA   1 
ATOM   1987 H HB2  . SER   A 1 145 ? 28.995  17.686  23.617  1.00 38.62  ? 130 SER   A HB2  1 
ATOM   1988 H HB3  . SER   A 1 145 ? 29.181  16.892  22.253  1.00 38.62  ? 130 SER   A HB3  1 
ATOM   1989 H HG   . SER   A 1 145 ? 27.120  17.441  21.770  1.00 38.61  ? 130 SER   A HG   1 
ATOM   1990 N N    . GLN   A 1 146 ? 25.684  16.204  24.197  1.00 29.75  ? 131 GLN   A N    1 
ATOM   1991 C CA   . GLN   A 1 146 ? 24.531  16.384  25.065  1.00 30.46  ? 131 GLN   A CA   1 
ATOM   1992 C C    . GLN   A 1 146 ? 24.097  15.087  25.750  1.00 36.38  ? 131 GLN   A C    1 
ATOM   1993 O O    . GLN   A 1 146 ? 23.028  15.060  26.369  1.00 32.89  ? 131 GLN   A O    1 
ATOM   1994 C CB   . GLN   A 1 146 ? 23.362  16.949  24.255  1.00 30.17  ? 131 GLN   A CB   1 
ATOM   1995 C CG   . GLN   A 1 146 ? 23.700  18.215  23.483  1.00 34.44  ? 131 GLN   A CG   1 
ATOM   1996 C CD   . GLN   A 1 146 ? 24.011  19.381  24.396  1.00 37.62  ? 131 GLN   A CD   1 
ATOM   1997 O OE1  . GLN   A 1 146 ? 23.157  19.828  25.162  1.00 41.38  ? 131 GLN   A OE1  1 
ATOM   1998 N NE2  . GLN   A 1 146 ? 25.244  19.866  24.335  1.00 40.26  ? 131 GLN   A NE2  1 
ATOM   1999 H H    . GLN   A 1 146 ? 25.467  16.094  23.372  1.00 35.70  ? 131 GLN   A H    1 
ATOM   2000 H HA   . GLN   A 1 146 ? 24.760  17.024  25.757  1.00 36.55  ? 131 GLN   A HA   1 
ATOM   2001 H HB2  . GLN   A 1 146 ? 23.076  16.280  23.613  1.00 36.20  ? 131 GLN   A HB2  1 
ATOM   2002 H HB3  . GLN   A 1 146 ? 22.636  17.159  24.862  1.00 36.20  ? 131 GLN   A HB3  1 
ATOM   2003 H HG2  . GLN   A 1 146 ? 24.479  18.051  22.928  1.00 41.33  ? 131 GLN   A HG2  1 
ATOM   2004 H HG3  . GLN   A 1 146 ? 22.944  18.460  22.928  1.00 41.33  ? 131 GLN   A HG3  1 
ATOM   2005 H HE21 . GLN   A 1 146 ? 25.816  19.519  23.796  1.00 48.31  ? 131 GLN   A HE21 1 
ATOM   2006 H HE22 . GLN   A 1 146 ? 25.470  20.529  24.834  1.00 48.31  ? 131 GLN   A HE22 1 
ATOM   2007 N N    . LYS   A 1 147 ? 24.885  14.016  25.631  1.00 30.26  ? 132 LYS   A N    1 
ATOM   2008 C CA   . LYS   A 1 147 ? 24.614  12.737  26.283  1.00 28.43  ? 132 LYS   A CA   1 
ATOM   2009 C C    . LYS   A 1 147 ? 23.337  12.088  25.755  1.00 29.52  ? 132 LYS   A C    1 
ATOM   2010 O O    . LYS   A 1 147 ? 22.636  11.377  26.484  1.00 33.59  ? 132 LYS   A O    1 
ATOM   2011 C CB   . LYS   A 1 147 ? 24.548  12.907  27.805  1.00 35.17  ? 132 LYS   A CB   1 
ATOM   2012 C CG   . LYS   A 1 147 ? 25.697  13.733  28.374  1.00 40.88  ? 132 LYS   A CG   1 
ATOM   2013 C CD   . LYS   A 1 147 ? 26.877  12.879  28.819  1.00 52.00  ? 132 LYS   A CD   1 
ATOM   2014 C CE   . LYS   A 1 147 ? 26.696  12.384  30.267  1.00 62.37  ? 132 LYS   A CE   1 
ATOM   2015 N NZ   . LYS   A 1 147 ? 27.982  12.382  31.042  1.00 64.40  ? 132 LYS   A NZ   1 
ATOM   2016 H H    . LYS   A 1 147 ? 25.606  14.008  25.162  1.00 36.31  ? 132 LYS   A H    1 
ATOM   2017 H HA   . LYS   A 1 147 ? 25.341  12.126  26.084  1.00 34.12  ? 132 LYS   A HA   1 
ATOM   2018 H HB2  . LYS   A 1 147 ? 23.718  13.355  28.034  1.00 42.21  ? 132 LYS   A HB2  1 
ATOM   2019 H HB3  . LYS   A 1 147 ? 24.577  12.031  28.220  1.00 42.21  ? 132 LYS   A HB3  1 
ATOM   2020 H HG2  . LYS   A 1 147 ? 26.013  14.346  27.692  1.00 49.06  ? 132 LYS   A HG2  1 
ATOM   2021 H HG3  . LYS   A 1 147 ? 25.379  14.228  29.144  1.00 49.06  ? 132 LYS   A HG3  1 
ATOM   2022 H HD2  . LYS   A 1 147 ? 26.952  12.106  28.238  1.00 62.40  ? 132 LYS   A HD2  1 
ATOM   2023 H HD3  . LYS   A 1 147 ? 27.690  13.407  28.775  1.00 62.40  ? 132 LYS   A HD3  1 
ATOM   2024 H HE2  . LYS   A 1 147 ? 26.070  12.966  30.725  1.00 74.85  ? 132 LYS   A HE2  1 
ATOM   2025 H HE3  . LYS   A 1 147 ? 26.354  11.476  30.251  1.00 74.85  ? 132 LYS   A HE3  1 
ATOM   2026 H HZ1  . LYS   A 1 147 ? 27.837  12.093  31.871  1.00 77.28  ? 132 LYS   A HZ1  1 
ATOM   2027 H HZ2  . LYS   A 1 147 ? 28.573  11.845  30.649  1.00 77.28  ? 132 LYS   A HZ2  1 
ATOM   2028 H HZ3  . LYS   A 1 147 ? 28.318  13.205  31.077  1.00 77.28  ? 132 LYS   A HZ3  1 
ATOM   2029 N N    . LYS   A 1 148 ? 23.032  12.329  24.482  1.00 27.54  ? 133 LYS   A N    1 
ATOM   2030 C CA   . LYS   A 1 148 ? 21.908  11.721  23.787  1.00 24.87  ? 133 LYS   A CA   1 
ATOM   2031 C C    . LYS   A 1 148 ? 22.413  10.709  22.765  1.00 27.63  ? 133 LYS   A C    1 
ATOM   2032 O O    . LYS   A 1 148 ? 23.564  10.764  22.323  1.00 33.79  ? 133 LYS   A O    1 
ATOM   2033 C CB   . LYS   A 1 148 ? 21.063  12.784  23.078  1.00 24.48  ? 133 LYS   A CB   1 
ATOM   2034 C CG   . LYS   A 1 148 ? 20.706  14.004  23.943  1.00 33.54  ? 133 LYS   A CG   1 
ATOM   2035 C CD   . LYS   A 1 148 ? 19.691  13.656  25.021  1.00 37.41  ? 133 LYS   A CD   1 
ATOM   2036 C CE   . LYS   A 1 148 ? 19.182  14.909  25.749  1.00 38.96  ? 133 LYS   A CE   1 
ATOM   2037 N NZ   . LYS   A 1 148 ? 20.120  15.378  26.808  1.00 46.86  ? 133 LYS   A NZ   1 
ATOM   2038 H H    . LYS   A 1 148 ? 23.483  12.865  23.982  1.00 33.04  ? 133 LYS   A H    1 
ATOM   2039 H HA   . LYS   A 1 148 ? 21.345  11.260  24.429  1.00 29.85  ? 133 LYS   A HA   1 
ATOM   2040 H HB2  . LYS   A 1 148 ? 21.556  13.107  22.308  1.00 29.37  ? 133 LYS   A HB2  1 
ATOM   2041 H HB3  . LYS   A 1 148 ? 20.230  12.376  22.792  1.00 29.37  ? 133 LYS   A HB3  1 
ATOM   2042 H HG2  . LYS   A 1 148 ? 21.508  14.334  24.377  1.00 40.25  ? 133 LYS   A HG2  1 
ATOM   2043 H HG3  . LYS   A 1 148 ? 20.325  14.696  23.380  1.00 40.25  ? 133 LYS   A HG3  1 
ATOM   2044 H HD2  . LYS   A 1 148 ? 18.931  13.212  24.614  1.00 44.89  ? 133 LYS   A HD2  1 
ATOM   2045 H HD3  . LYS   A 1 148 ? 20.106  13.072  25.675  1.00 44.89  ? 133 LYS   A HD3  1 
ATOM   2046 H HE2  . LYS   A 1 148 ? 19.073  15.627  25.105  1.00 46.76  ? 133 LYS   A HE2  1 
ATOM   2047 H HE3  . LYS   A 1 148 ? 18.331  14.708  26.169  1.00 46.76  ? 133 LYS   A HE3  1 
ATOM   2048 H HZ1  . LYS   A 1 148 ? 19.794  16.107  27.201  1.00 56.23  ? 133 LYS   A HZ1  1 
ATOM   2049 H HZ2  . LYS   A 1 148 ? 20.228  14.743  27.422  1.00 56.23  ? 133 LYS   A HZ2  1 
ATOM   2050 H HZ3  . LYS   A 1 148 ? 20.911  15.572  26.450  1.00 56.23  ? 133 LYS   A HZ3  1 
ATOM   2051 N N    . ILE   A 1 149 ? 21.532  9.788   22.381  1.00 32.13  ? 134 ILE   A N    1 
ATOM   2052 C CA   . ILE   A 1 149 ? 21.817  8.796   21.352  1.00 23.54  ? 134 ILE   A CA   1 
ATOM   2053 C C    . ILE   A 1 149 ? 20.718  8.877   20.302  1.00 24.70  ? 134 ILE   A C    1 
ATOM   2054 O O    . ILE   A 1 149 ? 19.536  8.980   20.649  1.00 28.18  ? 134 ILE   A O    1 
ATOM   2055 C CB   . ILE   A 1 149 ? 21.898  7.361   21.921  1.00 28.76  ? 134 ILE   A CB   1 
ATOM   2056 C CG1  . ILE   A 1 149 ? 22.749  7.324   23.192  1.00 33.11  ? 134 ILE   A CG1  1 
ATOM   2057 C CG2  . ILE   A 1 149 ? 22.470  6.407   20.860  1.00 22.37  ? 134 ILE   A CG2  1 
ATOM   2058 C CD1  . ILE   A 1 149 ? 22.718  5.986   23.931  1.00 33.89  ? 134 ILE   A CD1  1 
ATOM   2059 H H    . ILE   A 1 149 ? 20.741  9.718   22.711  1.00 38.56  ? 134 ILE   A H    1 
ATOM   2060 H HA   . ILE   A 1 149 ? 22.671  9.006   20.943  1.00 28.25  ? 134 ILE   A HA   1 
ATOM   2061 H HB   . ILE   A 1 149 ? 21.002  7.074   22.155  1.00 34.51  ? 134 ILE   A HB   1 
ATOM   2062 H HG12 . ILE   A 1 149 ? 23.671  7.506   22.953  1.00 39.73  ? 134 ILE   A HG12 1 
ATOM   2063 H HG13 . ILE   A 1 149 ? 22.424  8.004   23.803  1.00 39.73  ? 134 ILE   A HG13 1 
ATOM   2064 H HG21 . ILE   A 1 149 ? 22.595  5.531   21.257  1.00 26.84  ? 134 ILE   A HG21 1 
ATOM   2065 H HG22 . ILE   A 1 149 ? 21.846  6.348   20.120  1.00 26.84  ? 134 ILE   A HG22 1 
ATOM   2066 H HG23 . ILE   A 1 149 ? 23.321  6.754   20.549  1.00 26.84  ? 134 ILE   A HG23 1 
ATOM   2067 H HD11 . ILE   A 1 149 ? 23.142  6.094   24.797  1.00 40.67  ? 134 ILE   A HD11 1 
ATOM   2068 H HD12 . ILE   A 1 149 ? 21.796  5.710   24.047  1.00 40.67  ? 134 ILE   A HD12 1 
ATOM   2069 H HD13 . ILE   A 1 149 ? 23.198  5.325   23.408  1.00 40.67  ? 134 ILE   A HD13 1 
ATOM   2070 N N    . HIS   A 1 150 ? 21.096  8.805   19.018  1.00 23.21  ? 135 HIS   A N    1 
ATOM   2071 C CA   . HIS   A 1 150 ? 20.082  8.838   17.969  1.00 24.19  ? 135 HIS   A CA   1 
ATOM   2072 C C    . HIS   A 1 150 ? 19.317  7.522   17.911  1.00 25.31  ? 135 HIS   A C    1 
ATOM   2073 O O    . HIS   A 1 150 ? 18.083  7.508   17.918  1.00 25.08  ? 135 HIS   A O    1 
ATOM   2074 C CB   . HIS   A 1 150 ? 20.709  9.141   16.604  1.00 24.47  ? 135 HIS   A CB   1 
ATOM   2075 C CG   . HIS   A 1 150 ? 19.696  9.340   15.519  1.00 19.53  ? 135 HIS   A CG   1 
ATOM   2076 N ND1  . HIS   A 1 150 ? 19.048  8.293   14.897  1.00 26.16  ? 135 HIS   A ND1  1 
ATOM   2077 C CD2  . HIS   A 1 150 ? 19.185  10.470  14.979  1.00 19.67  ? 135 HIS   A CD2  1 
ATOM   2078 C CE1  . HIS   A 1 150 ? 18.196  8.770   14.006  1.00 20.79  ? 135 HIS   A CE1  1 
ATOM   2079 N NE2  . HIS   A 1 150 ? 18.261  10.089  14.034  1.00 21.09  ? 135 HIS   A NE2  1 
ATOM   2080 H H    . HIS   A 1 150 ? 21.908  8.740   18.742  1.00 27.85  ? 135 HIS   A H    1 
ATOM   2081 H HA   . HIS   A 1 150 ? 19.463  9.555   18.174  1.00 29.03  ? 135 HIS   A HA   1 
ATOM   2082 H HB2  . HIS   A 1 150 ? 21.235  9.952   16.674  1.00 29.37  ? 135 HIS   A HB2  1 
ATOM   2083 H HB3  . HIS   A 1 150 ? 21.277  8.398   16.348  1.00 29.37  ? 135 HIS   A HB3  1 
ATOM   2084 H HD2  . HIS   A 1 150 ? 19.416  11.342  15.204  1.00 23.60  ? 135 HIS   A HD2  1 
ATOM   2085 H HE1  . HIS   A 1 150 ? 17.645  8.264   13.454  1.00 24.94  ? 135 HIS   A HE1  1 
ATOM   2086 H HE2  . HIS   A 1 150 ? 17.801  10.623  13.542  1.00 25.31  ? 135 HIS   A HE2  1 
ATOM   2087 N N    . ARG   A 1 151 ? 20.048  6.409   17.799  1.00 28.80  ? 136 ARG   A N    1 
ATOM   2088 C CA   . ARG   A 1 151 ? 19.614  5.011   17.873  1.00 26.04  ? 136 ARG   A CA   1 
ATOM   2089 C C    . ARG   A 1 151 ? 19.144  4.448   16.534  1.00 30.15  ? 136 ARG   A C    1 
ATOM   2090 O O    . ARG   A 1 151 ? 19.023  3.230   16.412  1.00 26.00  ? 136 ARG   A O    1 
ATOM   2091 C CB   . ARG   A 1 151 ? 18.516  4.776   18.927  1.00 26.38  ? 136 ARG   A CB   1 
ATOM   2092 C CG   . ARG   A 1 151 ? 18.990  5.010   20.356  1.00 28.92  ? 136 ARG   A CG   1 
ATOM   2093 C CD   . ARG   A 1 151 ? 17.920  4.650   21.371  1.00 39.21  ? 136 ARG   A CD   1 
ATOM   2094 N NE   . ARG   A 1 151 ? 18.417  4.748   22.737  1.00 38.39  ? 136 ARG   A NE   1 
ATOM   2095 C CZ   . ARG   A 1 151 ? 18.470  5.878   23.429  1.00 41.33  ? 136 ARG   A CZ   1 
ATOM   2096 N NH1  . ARG   A 1 151 ? 18.053  7.023   22.913  1.00 40.40  ? 136 ARG   A NH1  1 
ATOM   2097 N NH2  . ARG   A 1 151 ? 18.960  5.861   24.665  1.00 49.42  ? 136 ARG   A NH2  1 
ATOM   2098 H H    . ARG   A 1 151 ? 20.896  6.449   17.664  1.00 34.56  ? 136 ARG   A H    1 
ATOM   2099 H HA   . ARG   A 1 151 ? 20.386  4.485   18.134  1.00 31.24  ? 136 ARG   A HA   1 
ATOM   2100 H HB2  . ARG   A 1 151 ? 17.780  5.383   18.753  1.00 31.66  ? 136 ARG   A HB2  1 
ATOM   2101 H HB3  . ARG   A 1 151 ? 18.210  3.857   18.861  1.00 31.66  ? 136 ARG   A HB3  1 
ATOM   2102 H HG2  . ARG   A 1 151 ? 19.770  4.461   20.530  1.00 34.71  ? 136 ARG   A HG2  1 
ATOM   2103 H HG3  . ARG   A 1 151 ? 19.213  5.948   20.470  1.00 34.71  ? 136 ARG   A HG3  1 
ATOM   2104 H HD2  . ARG   A 1 151 ? 17.170  5.258   21.276  1.00 47.06  ? 136 ARG   A HD2  1 
ATOM   2105 H HD3  . ARG   A 1 151 ? 17.628  3.737   21.218  1.00 47.06  ? 136 ARG   A HD3  1 
ATOM   2106 H HE   . ARG   A 1 151 ? 18.694  4.029   23.118  1.00 46.06  ? 136 ARG   A HE   1 
ATOM   2107 H HH11 . ARG   A 1 151 ? 17.739  7.045   22.113  1.00 48.48  ? 136 ARG   A HH11 1 
ATOM   2108 H HH12 . ARG   A 1 151 ? 18.095  7.745   23.378  1.00 48.48  ? 136 ARG   A HH12 1 
ATOM   2109 H HH21 . ARG   A 1 151 ? 19.238  5.122   25.007  1.00 59.31  ? 136 ARG   A HH21 1 
ATOM   2110 H HH22 . ARG   A 1 151 ? 18.998  6.588   25.122  1.00 59.31  ? 136 ARG   A HH22 1 
ATOM   2111 N N    . ASP   A 1 152 ? 18.890  5.279   15.522  1.00 25.97  ? 137 ASP   A N    1 
ATOM   2112 C CA   . ASP   A 1 152 ? 18.270  4.796   14.287  1.00 22.96  ? 137 ASP   A CA   1 
ATOM   2113 C C    . ASP   A 1 152 ? 18.813  5.532   13.069  1.00 22.81  ? 137 ASP   A C    1 
ATOM   2114 O O    . ASP   A 1 152 ? 18.067  5.985   12.199  1.00 21.53  ? 137 ASP   A O    1 
ATOM   2115 C CB   . ASP   A 1 152 ? 16.749  4.941   14.372  1.00 31.51  ? 137 ASP   A CB   1 
ATOM   2116 C CG   . ASP   A 1 152 ? 16.011  4.043   13.392  1.00 29.57  ? 137 ASP   A CG   1 
ATOM   2117 O OD1  . ASP   A 1 152 ? 16.635  3.121   12.833  1.00 36.67  ? 137 ASP   A OD1  1 
ATOM   2118 O OD2  . ASP   A 1 152 ? 14.799  4.268   13.178  1.00 44.90  ? 137 ASP   A OD2  1 
ATOM   2119 H H    . ASP   A 1 152 ? 19.066  6.121   15.528  1.00 31.17  ? 137 ASP   A H    1 
ATOM   2120 H HA   . ASP   A 1 152 ? 18.504  3.861   14.179  1.00 27.55  ? 137 ASP   A HA   1 
ATOM   2121 H HB2  . ASP   A 1 152 ? 16.459  4.707   15.268  1.00 37.81  ? 137 ASP   A HB2  1 
ATOM   2122 H HB3  . ASP   A 1 152 ? 16.508  5.860   14.176  1.00 37.81  ? 137 ASP   A HB3  1 
ATOM   2123 N N    . ILE   A 1 153 ? 20.137  5.634   12.987  1.00 18.81  ? 138 ILE   A N    1 
ATOM   2124 C CA   . ILE   A 1 153 ? 20.782  6.243   11.831  1.00 22.36  ? 138 ILE   A CA   1 
ATOM   2125 C C    . ILE   A 1 153 ? 20.623  5.314   10.635  1.00 21.74  ? 138 ILE   A C    1 
ATOM   2126 O O    . ILE   A 1 153 ? 21.012  4.140   10.685  1.00 21.79  ? 138 ILE   A O    1 
ATOM   2127 C CB   . ILE   A 1 153 ? 22.264  6.519   12.114  1.00 22.68  ? 138 ILE   A CB   1 
ATOM   2128 C CG1  . ILE   A 1 153 ? 22.425  7.654   13.130  1.00 26.31  ? 138 ILE   A CG1  1 
ATOM   2129 C CG2  . ILE   A 1 153 ? 23.018  6.800   10.819  1.00 25.05  ? 138 ILE   A CG2  1 
ATOM   2130 C CD1  . ILE   A 1 153 ? 21.880  8.991   12.673  1.00 21.93  ? 138 ILE   A CD1  1 
ATOM   2131 H H    . ILE   A 1 153 ? 20.684  5.356   13.589  1.00 22.57  ? 138 ILE   A H    1 
ATOM   2132 H HA   . ILE   A 1 153 ? 20.344  7.085   11.631  1.00 26.84  ? 138 ILE   A HA   1 
ATOM   2133 H HB   . ILE   A 1 153 ? 22.651  5.723   12.510  1.00 27.21  ? 138 ILE   A HB   1 
ATOM   2134 H HG12 . ILE   A 1 153 ? 21.955  7.409   13.943  1.00 31.57  ? 138 ILE   A HG12 1 
ATOM   2135 H HG13 . ILE   A 1 153 ? 23.370  7.771   13.316  1.00 31.57  ? 138 ILE   A HG13 1 
ATOM   2136 H HG21 . ILE   A 1 153 ? 23.852  7.248   11.030  1.00 30.06  ? 138 ILE   A HG21 1 
ATOM   2137 H HG22 . ILE   A 1 153 ? 23.198  5.960   10.370  1.00 30.06  ? 138 ILE   A HG22 1 
ATOM   2138 H HG23 . ILE   A 1 153 ? 22.472  7.368   10.252  1.00 30.06  ? 138 ILE   A HG23 1 
ATOM   2139 H HD11 . ILE   A 1 153 ? 22.174  9.680   13.289  1.00 26.32  ? 138 ILE   A HD11 1 
ATOM   2140 H HD12 . ILE   A 1 153 ? 22.214  9.180   11.782  1.00 26.32  ? 138 ILE   A HD12 1 
ATOM   2141 H HD13 . ILE   A 1 153 ? 20.911  8.950   12.660  1.00 26.32  ? 138 ILE   A HD13 1 
ATOM   2142 N N    . LYS   A 1 154 ? 20.056  5.838   9.557   1.00 25.18  ? 139 LYS   A N    1 
ATOM   2143 C CA   . LYS   A 1 154 ? 19.853  5.097   8.323   1.00 22.30  ? 139 LYS   A CA   1 
ATOM   2144 C C    . LYS   A 1 154 ? 19.397  6.094   7.268   1.00 22.15  ? 139 LYS   A C    1 
ATOM   2145 O O    . LYS   A 1 154 ? 19.075  7.246   7.571   1.00 22.51  ? 139 LYS   A O    1 
ATOM   2146 C CB   . LYS   A 1 154 ? 18.833  3.974   8.502   1.00 23.19  ? 139 LYS   A CB   1 
ATOM   2147 C CG   . LYS   A 1 154 ? 17.452  4.464   8.883   1.00 20.84  ? 139 LYS   A CG   1 
ATOM   2148 C CD   . LYS   A 1 154 ? 16.562  3.351   9.438   1.00 24.21  ? 139 LYS   A CD   1 
ATOM   2149 C CE   . LYS   A 1 154 ? 16.059  2.436   8.335   1.00 30.74  ? 139 LYS   A CE   1 
ATOM   2150 N NZ   . LYS   A 1 154 ? 15.357  1.248   8.883   1.00 37.39  ? 139 LYS   A NZ   1 
ATOM   2151 H H    . LYS   A 1 154 ? 19.771  6.648   9.515   1.00 30.21  ? 139 LYS   A H    1 
ATOM   2152 H HA   . LYS   A 1 154 ? 20.689  4.698   8.035   1.00 26.76  ? 139 LYS   A HA   1 
ATOM   2153 H HB2  . LYS   A 1 154 ? 18.754  3.487   7.666   1.00 27.82  ? 139 LYS   A HB2  1 
ATOM   2154 H HB3  . LYS   A 1 154 ? 19.141  3.380   9.204   1.00 27.82  ? 139 LYS   A HB3  1 
ATOM   2155 H HG2  . LYS   A 1 154 ? 17.537  5.149   9.566   1.00 25.01  ? 139 LYS   A HG2  1 
ATOM   2156 H HG3  . LYS   A 1 154 ? 17.018  4.832   8.097   1.00 25.01  ? 139 LYS   A HG3  1 
ATOM   2157 H HD2  . LYS   A 1 154 ? 17.072  2.816   10.068  1.00 29.05  ? 139 LYS   A HD2  1 
ATOM   2158 H HD3  . LYS   A 1 154 ? 15.795  3.744   9.882   1.00 29.05  ? 139 LYS   A HD3  1 
ATOM   2159 H HE2  . LYS   A 1 154 ? 15.436  2.924   7.774   1.00 36.89  ? 139 LYS   A HE2  1 
ATOM   2160 H HE3  . LYS   A 1 154 ? 16.811  2.127   7.806   1.00 36.89  ? 139 LYS   A HE3  1 
ATOM   2161 H HZ1  . LYS   A 1 154 ? 15.071  0.730   8.219   1.00 44.87  ? 139 LYS   A HZ1  1 
ATOM   2162 H HZ2  . LYS   A 1 154 ? 15.911  0.778   9.398   1.00 44.87  ? 139 LYS   A HZ2  1 
ATOM   2163 H HZ3  . LYS   A 1 154 ? 14.658  1.505   9.371   1.00 44.87  ? 139 LYS   A HZ3  1 
ATOM   2164 N N    . GLY   A 1 155 ? 19.387  5.632   6.015   1.00 22.57  ? 140 GLY   A N    1 
ATOM   2165 C CA   . GLY   A 1 155 ? 19.017  6.502   4.912   1.00 21.59  ? 140 GLY   A CA   1 
ATOM   2166 C C    . GLY   A 1 155 ? 17.654  7.151   5.080   1.00 25.59  ? 140 GLY   A C    1 
ATOM   2167 O O    . GLY   A 1 155 ? 17.469  8.324   4.735   1.00 18.60  ? 140 GLY   A O    1 
ATOM   2168 H H    . GLY   A 1 155 ? 19.588  4.828   5.785   1.00 27.09  ? 140 GLY   A H    1 
ATOM   2169 H HA2  . GLY   A 1 155 ? 19.678  7.208   4.831   1.00 25.91  ? 140 GLY   A HA2  1 
ATOM   2170 H HA3  . GLY   A 1 155 ? 19.005  5.985   4.092   1.00 25.91  ? 140 GLY   A HA3  1 
ATOM   2171 N N    . ALA   A 1 156 ? 16.680  6.398   5.600   1.00 19.37  ? 141 ALA   A N    1 
ATOM   2172 C CA   . ALA   A 1 156 ? 15.323  6.921   5.752   1.00 25.01  ? 141 ALA   A CA   1 
ATOM   2173 C C    . ALA   A 1 156 ? 15.221  8.030   6.795   1.00 21.68  ? 141 ALA   A C    1 
ATOM   2174 O O    . ALA   A 1 156 ? 14.216  8.751   6.815   1.00 20.40  ? 141 ALA   A O    1 
ATOM   2175 C CB   . ALA   A 1 156 ? 14.362  5.791   6.127   1.00 23.94  ? 141 ALA   A CB   1 
ATOM   2176 H H    . ALA   A 1 156 ? 16.780  5.588   5.870   1.00 23.24  ? 141 ALA   A H    1 
ATOM   2177 H HA   . ALA   A 1 156 ? 15.052  7.291   4.897   1.00 30.01  ? 141 ALA   A HA   1 
ATOM   2178 H HB1  . ALA   A 1 156 ? 13.468  6.155   6.222   1.00 28.72  ? 141 ALA   A HB1  1 
ATOM   2179 H HB2  . ALA   A 1 156 ? 14.374  5.121   5.426   1.00 28.72  ? 141 ALA   A HB2  1 
ATOM   2180 H HB3  . ALA   A 1 156 ? 14.650  5.397   6.965   1.00 28.72  ? 141 ALA   A HB3  1 
ATOM   2181 N N    . ASN   A 1 157 ? 16.225  8.180   7.661   1.00 18.96  ? 142 ASN   A N    1 
ATOM   2182 C CA   . ASN   A 1 157 ? 16.203  9.174   8.726   1.00 23.40  ? 142 ASN   A CA   1 
ATOM   2183 C C    . ASN   A 1 157 ? 17.188  10.312  8.484   1.00 27.10  ? 142 ASN   A C    1 
ATOM   2184 O O    . ASN   A 1 157 ? 17.447  11.102  9.401   1.00 23.06  ? 142 ASN   A O    1 
ATOM   2185 C CB   . ASN   A 1 157 ? 16.497  8.523   10.083  1.00 19.13  ? 142 ASN   A CB   1 
ATOM   2186 C CG   . ASN   A 1 157 ? 15.320  7.766   10.626  1.00 25.39  ? 142 ASN   A CG   1 
ATOM   2187 O OD1  . ASN   A 1 157 ? 14.176  8.120   10.358  1.00 29.05  ? 142 ASN   A OD1  1 
ATOM   2188 N ND2  . ASN   A 1 157 ? 15.590  6.705   11.387  1.00 23.57  ? 142 ASN   A ND2  1 
ATOM   2189 H H    . ASN   A 1 157 ? 16.943  7.707   7.648   1.00 22.76  ? 142 ASN   A H    1 
ATOM   2190 H HA   . ASN   A 1 157 ? 15.310  9.549   8.763   1.00 28.08  ? 142 ASN   A HA   1 
ATOM   2191 H HB2  . ASN   A 1 157 ? 17.234  7.901   9.983   1.00 22.96  ? 142 ASN   A HB2  1 
ATOM   2192 H HB3  . ASN   A 1 157 ? 16.731  9.214   10.723  1.00 22.96  ? 142 ASN   A HB3  1 
ATOM   2193 H HD21 . ASN   A 1 157 ? 14.948  6.240   11.720  1.00 28.28  ? 142 ASN   A HD21 1 
ATOM   2194 H HD22 . ASN   A 1 157 ? 16.407  6.485   11.544  1.00 28.28  ? 142 ASN   A HD22 1 
ATOM   2195 N N    . ILE   A 1 158 ? 17.740  10.418  7.282   1.00 21.77  ? 143 ILE   A N    1 
ATOM   2196 C CA   . ILE   A 1 158 ? 18.623  11.516  6.916   1.00 24.34  ? 143 ILE   A CA   1 
ATOM   2197 C C    . ILE   A 1 158 ? 17.899  12.311  5.847   1.00 20.87  ? 143 ILE   A C    1 
ATOM   2198 O O    . ILE   A 1 158 ? 17.706  11.827  4.726   1.00 23.79  ? 143 ILE   A O    1 
ATOM   2199 C CB   . ILE   A 1 158 ? 19.985  11.022  6.427   1.00 22.83  ? 143 ILE   A CB   1 
ATOM   2200 C CG1  . ILE   A 1 158 ? 20.672  10.210  7.521   1.00 20.69  ? 143 ILE   A CG1  1 
ATOM   2201 C CG2  . ILE   A 1 158 ? 20.847  12.209  6.004   1.00 19.40  ? 143 ILE   A CG2  1 
ATOM   2202 C CD1  . ILE   A 1 158 ? 21.883  9.399   7.015   1.00 19.70  ? 143 ILE   A CD1  1 
ATOM   2203 H H    . ILE   A 1 158 ? 17.615  9.851   6.647   1.00 26.13  ? 143 ILE   A H    1 
ATOM   2204 H HA   . ILE   A 1 158 ? 18.777  12.087  7.685   1.00 29.20  ? 143 ILE   A HA   1 
ATOM   2205 H HB   . ILE   A 1 158 ? 19.856  10.445  5.658   1.00 27.40  ? 143 ILE   A HB   1 
ATOM   2206 H HG12 . ILE   A 1 158 ? 20.987  10.816  8.210   1.00 24.83  ? 143 ILE   A HG12 1 
ATOM   2207 H HG13 . ILE   A 1 158 ? 20.032  9.585   7.897   1.00 24.83  ? 143 ILE   A HG13 1 
ATOM   2208 H HG21 . ILE   A 1 158 ? 21.750  11.899  5.834   1.00 23.28  ? 143 ILE   A HG21 1 
ATOM   2209 H HG22 . ILE   A 1 158 ? 20.474  12.599  5.198   1.00 23.28  ? 143 ILE   A HG22 1 
ATOM   2210 H HG23 . ILE   A 1 158 ? 20.852  12.866  6.717   1.00 23.28  ? 143 ILE   A HG23 1 
ATOM   2211 H HD11 . ILE   A 1 158 ? 22.217  8.846   7.738   1.00 23.64  ? 143 ILE   A HD11 1 
ATOM   2212 H HD12 . ILE   A 1 158 ? 21.602  8.841   6.274   1.00 23.64  ? 143 ILE   A HD12 1 
ATOM   2213 H HD13 . ILE   A 1 158 ? 22.575  10.014  6.723   1.00 23.64  ? 143 ILE   A HD13 1 
ATOM   2214 N N    . LEU   A 1 159 ? 17.456  13.513  6.206   1.00 27.41  ? 144 LEU   A N    1 
ATOM   2215 C CA   . LEU   A 1 159 ? 16.654  14.346  5.326   1.00 24.47  ? 144 LEU   A CA   1 
ATOM   2216 C C    . LEU   A 1 159 ? 17.535  15.349  4.593   1.00 22.66  ? 144 LEU   A C    1 
ATOM   2217 O O    . LEU   A 1 159 ? 18.607  15.733  5.069   1.00 23.20  ? 144 LEU   A O    1 
ATOM   2218 C CB   . LEU   A 1 159 ? 15.567  15.077  6.124   1.00 21.98  ? 144 LEU   A CB   1 
ATOM   2219 C CG   . LEU   A 1 159 ? 14.679  14.169  6.975   1.00 22.74  ? 144 LEU   A CG   1 
ATOM   2220 C CD1  . LEU   A 1 159 ? 13.526  14.937  7.588   1.00 25.89  ? 144 LEU   A CD1  1 
ATOM   2221 C CD2  . LEU   A 1 159 ? 14.169  12.989  6.147   1.00 22.23  ? 144 LEU   A CD2  1 
ATOM   2222 H H    . LEU   A 1 159 ? 17.611  13.872  6.972   1.00 32.89  ? 144 LEU   A H    1 
ATOM   2223 H HA   . LEU   A 1 159 ? 16.220  13.792  4.659   1.00 29.37  ? 144 LEU   A HA   1 
ATOM   2224 H HB2  . LEU   A 1 159 ? 15.997  15.709  6.722   1.00 26.38  ? 144 LEU   A HB2  1 
ATOM   2225 H HB3  . LEU   A 1 159 ? 14.992  15.548  5.501   1.00 26.38  ? 144 LEU   A HB3  1 
ATOM   2226 H HG   . LEU   A 1 159 ? 15.210  13.817  7.706   1.00 27.29  ? 144 LEU   A HG   1 
ATOM   2227 H HD11 . LEU   A 1 159 ? 12.994  14.332  8.128   1.00 31.07  ? 144 LEU   A HD11 1 
ATOM   2228 H HD12 . LEU   A 1 159 ? 13.880  15.650  8.141   1.00 31.07  ? 144 LEU   A HD12 1 
ATOM   2229 H HD13 . LEU   A 1 159 ? 12.981  15.310  6.877   1.00 31.07  ? 144 LEU   A HD13 1 
ATOM   2230 H HD21 . LEU   A 1 159 ? 13.449  12.553  6.629   1.00 26.68  ? 144 LEU   A HD21 1 
ATOM   2231 H HD22 . LEU   A 1 159 ? 13.845  13.319  5.295   1.00 26.68  ? 144 LEU   A HD22 1 
ATOM   2232 H HD23 . LEU   A 1 159 ? 14.898  12.365  6.005   1.00 26.68  ? 144 LEU   A HD23 1 
ATOM   2233 N N    . ILE   A 1 160 ? 17.056  15.781  3.427   1.00 24.45  ? 145 ILE   A N    1 
ATOM   2234 C CA   . ILE   A 1 160 ? 17.763  16.708  2.550   1.00 24.02  ? 145 ILE   A CA   1 
ATOM   2235 C C    . ILE   A 1 160 ? 16.809  17.838  2.187   1.00 23.91  ? 145 ILE   A C    1 
ATOM   2236 O O    . ILE   A 1 160 ? 15.676  17.572  1.768   1.00 23.91  ? 145 ILE   A O    1 
ATOM   2237 C CB   . ILE   A 1 160 ? 18.252  15.999  1.267   1.00 19.58  ? 145 ILE   A CB   1 
ATOM   2238 C CG1  . ILE   A 1 160 ? 19.070  14.753  1.613   1.00 18.87  ? 145 ILE   A CG1  1 
ATOM   2239 C CG2  . ILE   A 1 160 ? 19.055  16.958  0.375   1.00 21.45  ? 145 ILE   A CG2  1 
ATOM   2240 C CD1  . ILE   A 1 160 ? 20.339  15.050  2.399   1.00 23.27  ? 145 ILE   A CD1  1 
ATOM   2241 H H    . ILE   A 1 160 ? 16.293  15.541  3.112   1.00 29.34  ? 145 ILE   A H    1 
ATOM   2242 H HA   . ILE   A 1 160 ? 18.527  17.083  3.017   1.00 28.82  ? 145 ILE   A HA   1 
ATOM   2243 H HB   . ILE   A 1 160 ? 17.469  15.715  0.769   1.00 23.49  ? 145 ILE   A HB   1 
ATOM   2244 H HG12 . ILE   A 1 160 ? 18.522  14.160  2.150   1.00 22.65  ? 145 ILE   A HG12 1 
ATOM   2245 H HG13 . ILE   A 1 160 ? 19.329  14.312  0.789   1.00 22.65  ? 145 ILE   A HG13 1 
ATOM   2246 H HG21 . ILE   A 1 160 ? 19.470  16.450  -0.340  1.00 25.73  ? 145 ILE   A HG21 1 
ATOM   2247 H HG22 . ILE   A 1 160 ? 18.453  17.622  0.003   1.00 25.73  ? 145 ILE   A HG22 1 
ATOM   2248 H HG23 . ILE   A 1 160 ? 19.736  17.392  0.912   1.00 25.73  ? 145 ILE   A HG23 1 
ATOM   2249 H HD11 . ILE   A 1 160 ? 20.802  14.216  2.578   1.00 27.93  ? 145 ILE   A HD11 1 
ATOM   2250 H HD12 . ILE   A 1 160 ? 20.906  15.636  1.873   1.00 27.93  ? 145 ILE   A HD12 1 
ATOM   2251 H HD13 . ILE   A 1 160 ? 20.100  15.482  3.234   1.00 27.93  ? 145 ILE   A HD13 1 
ATOM   2252 N N    . ASN   A 1 161 ? 17.257  19.090  2.322   1.00 24.84  ? 146 ASN   A N    1 
ATOM   2253 C CA   . ASN   A 1 161 ? 16.439  20.219  1.900   1.00 26.26  ? 146 ASN   A CA   1 
ATOM   2254 C C    . ASN   A 1 161 ? 16.848  20.656  0.497   1.00 26.18  ? 146 ASN   A C    1 
ATOM   2255 O O    . ASN   A 1 161 ? 17.799  20.138  -0.092  1.00 25.55  ? 146 ASN   A O    1 
ATOM   2256 C CB   . ASN   A 1 161 ? 16.497  21.393  2.900   1.00 24.48  ? 146 ASN   A CB   1 
ATOM   2257 C CG   . ASN   A 1 161 ? 17.845  22.096  2.965   1.00 25.84  ? 146 ASN   A CG   1 
ATOM   2258 O OD1  . ASN   A 1 161 ? 18.719  21.927  2.107   1.00 27.82  ? 146 ASN   A OD1  1 
ATOM   2259 N ND2  . ASN   A 1 161 ? 18.007  22.921  3.998   1.00 25.54  ? 146 ASN   A ND2  1 
ATOM   2260 H H    . ASN   A 1 161 ? 18.023  19.303  2.652   1.00 29.80  ? 146 ASN   A H    1 
ATOM   2261 H HA   . ASN   A 1 161 ? 15.510  19.939  1.876   1.00 31.52  ? 146 ASN   A HA   1 
ATOM   2262 H HB2  . ASN   A 1 161 ? 15.834  22.053  2.643   1.00 29.38  ? 146 ASN   A HB2  1 
ATOM   2263 H HB3  . ASN   A 1 161 ? 16.300  21.054  3.788   1.00 29.38  ? 146 ASN   A HB3  1 
ATOM   2264 H HD21 . ASN   A 1 161 ? 18.747  23.350  4.093   1.00 30.65  ? 146 ASN   A HD21 1 
ATOM   2265 H HD22 . ASN   A 1 161 ? 17.373  23.025  4.569   1.00 30.65  ? 146 ASN   A HD22 1 
ATOM   2266 N N    . ASP   A 1 162 ? 16.083  21.592  -0.056  1.00 26.96  ? 147 ASP   A N    1 
ATOM   2267 C CA   . ASP   A 1 162 ? 16.287  21.967  -1.450  1.00 32.12  ? 147 ASP   A CA   1 
ATOM   2268 C C    . ASP   A 1 162 ? 17.587  22.723  -1.673  1.00 31.05  ? 147 ASP   A C    1 
ATOM   2269 O O    . ASP   A 1 162 ? 18.007  22.862  -2.828  1.00 29.33  ? 147 ASP   A O    1 
ATOM   2270 C CB   . ASP   A 1 162 ? 15.094  22.782  -1.935  1.00 31.87  ? 147 ASP   A CB   1 
ATOM   2271 C CG   . ASP   A 1 162 ? 13.815  21.967  -1.940  1.00 37.34  ? 147 ASP   A CG   1 
ATOM   2272 O OD1  . ASP   A 1 162 ? 13.846  20.832  -2.464  1.00 40.59  ? 147 ASP   A OD1  1 
ATOM   2273 O OD2  . ASP   A 1 162 ? 12.792  22.436  -1.395  1.00 45.16  ? 147 ASP   A OD2  1 
ATOM   2274 H H    . ASP   A 1 162 ? 15.453  22.017  0.347   1.00 32.35  ? 147 ASP   A H    1 
ATOM   2275 H HA   . ASP   A 1 162 ? 16.335  21.166  -1.994  1.00 38.55  ? 147 ASP   A HA   1 
ATOM   2276 H HB2  . ASP   A 1 162 ? 14.966  23.542  -1.346  1.00 38.24  ? 147 ASP   A HB2  1 
ATOM   2277 H HB3  . ASP   A 1 162 ? 15.263  23.088  -2.840  1.00 38.24  ? 147 ASP   A HB3  1 
ATOM   2278 N N    . ALA   A 1 163 ? 18.237  23.188  -0.609  1.00 24.19  ? 148 ALA   A N    1 
ATOM   2279 C CA   . ALA   A 1 163 ? 19.561  23.780  -0.697  1.00 22.75  ? 148 ALA   A CA   1 
ATOM   2280 C C    . ALA   A 1 163 ? 20.675  22.742  -0.679  1.00 23.39  ? 148 ALA   A C    1 
ATOM   2281 O O    . ALA   A 1 163 ? 21.845  23.115  -0.791  1.00 25.79  ? 148 ALA   A O    1 
ATOM   2282 C CB   . ALA   A 1 163 ? 19.760  24.778  0.449   1.00 35.44  ? 148 ALA   A CB   1 
ATOM   2283 H H    . ALA   A 1 163 ? 17.923  23.169  0.191   1.00 29.03  ? 148 ALA   A H    1 
ATOM   2284 H HA   . ALA   A 1 163 ? 19.630  24.269  -1.532  1.00 27.31  ? 148 ALA   A HA   1 
ATOM   2285 H HB1  . ALA   A 1 163 ? 20.645  25.169  0.377   1.00 42.53  ? 148 ALA   A HB1  1 
ATOM   2286 H HB2  . ALA   A 1 163 ? 19.085  25.471  0.385   1.00 42.53  ? 148 ALA   A HB2  1 
ATOM   2287 H HB3  . ALA   A 1 163 ? 19.674  24.309  1.294   1.00 42.53  ? 148 ALA   A HB3  1 
ATOM   2288 N N    . GLY   A 1 164 ? 20.343  21.454  -0.565  1.00 26.02  ? 149 GLY   A N    1 
ATOM   2289 C CA   . GLY   A 1 164 ? 21.348  20.410  -0.533  1.00 25.94  ? 149 GLY   A CA   1 
ATOM   2290 C C    . GLY   A 1 164 ? 21.947  20.133  0.826   1.00 26.40  ? 149 GLY   A C    1 
ATOM   2291 O O    . GLY   A 1 164 ? 22.967  19.436  0.906   1.00 20.64  ? 149 GLY   A O    1 
ATOM   2292 H H    . GLY   A 1 164 ? 19.535  21.164  -0.505  1.00 31.23  ? 149 GLY   A H    1 
ATOM   2293 H HA2  . GLY   A 1 164 ? 20.948  19.585  -0.851  1.00 31.13  ? 149 GLY   A HA2  1 
ATOM   2294 H HA3  . GLY   A 1 164 ? 22.072  20.659  -1.128  1.00 31.13  ? 149 GLY   A HA3  1 
ATOM   2295 N N    . GLU   A 1 165 ? 21.345  20.652  1.891   1.00 22.79  ? 150 GLU   A N    1 
ATOM   2296 C CA   . GLU   A 1 165 ? 21.836  20.485  3.249   1.00 25.05  ? 150 GLU   A CA   1 
ATOM   2297 C C    . GLU   A 1 165 ? 21.204  19.268  3.908   1.00 20.19  ? 150 GLU   A C    1 
ATOM   2298 O O    . GLU   A 1 165 ? 20.108  18.836  3.549   1.00 22.19  ? 150 GLU   A O    1 
ATOM   2299 C CB   . GLU   A 1 165 ? 21.543  21.744  4.063   1.00 21.02  ? 150 GLU   A CB   1 
ATOM   2300 C CG   . GLU   A 1 165 ? 22.291  22.939  3.539   1.00 31.40  ? 150 GLU   A CG   1 
ATOM   2301 C CD   . GLU   A 1 165 ? 21.785  24.244  4.111   1.00 33.48  ? 150 GLU   A CD   1 
ATOM   2302 O OE1  . GLU   A 1 165 ? 20.552  24.422  4.191   1.00 35.34  ? 150 GLU   A OE1  1 
ATOM   2303 O OE2  . GLU   A 1 165 ? 22.627  25.086  4.481   1.00 50.40  ? 150 GLU   A OE2  1 
ATOM   2304 H H    . GLU   A 1 165 ? 20.625  21.121  1.849   1.00 27.35  ? 150 GLU   A H    1 
ATOM   2305 H HA   . GLU   A 1 165 ? 22.796  20.344  3.234   1.00 30.07  ? 150 GLU   A HA   1 
ATOM   2306 H HB2  . GLU   A 1 165 ? 20.594  21.937  4.021   1.00 25.22  ? 150 GLU   A HB2  1 
ATOM   2307 H HB3  . GLU   A 1 165 ? 21.812  21.597  4.984   1.00 25.22  ? 150 GLU   A HB3  1 
ATOM   2308 H HG2  . GLU   A 1 165 ? 23.228  22.853  3.773   1.00 37.68  ? 150 GLU   A HG2  1 
ATOM   2309 H HG3  . GLU   A 1 165 ? 22.192  22.976  2.575   1.00 37.68  ? 150 GLU   A HG3  1 
ATOM   2310 N N    . VAL   A 1 166 ? 21.903  18.743  4.918   1.00 27.60  ? 151 VAL   A N    1 
ATOM   2311 C CA   . VAL   A 1 166 ? 21.641  17.431  5.499   1.00 21.68  ? 151 VAL   A CA   1 
ATOM   2312 C C    . VAL   A 1 166 ? 21.158  17.590  6.938   1.00 24.97  ? 151 VAL   A C    1 
ATOM   2313 O O    . VAL   A 1 166 ? 21.796  18.285  7.736   1.00 24.82  ? 151 VAL   A O    1 
ATOM   2314 C CB   . VAL   A 1 166 ? 22.913  16.564  5.458   1.00 26.80  ? 151 VAL   A CB   1 
ATOM   2315 C CG1  . VAL   A 1 166 ? 22.654  15.200  6.087   1.00 32.07  ? 151 VAL   A CG1  1 
ATOM   2316 C CG2  . VAL   A 1 166 ? 23.408  16.411  4.036   1.00 29.83  ? 151 VAL   A CG2  1 
ATOM   2317 H H    . VAL   A 1 166 ? 22.561  19.149  5.297   1.00 33.12  ? 151 VAL   A H    1 
ATOM   2318 H HA   . VAL   A 1 166 ? 20.930  17.003  4.997   1.00 26.01  ? 151 VAL   A HA   1 
ATOM   2319 H HB   . VAL   A 1 166 ? 23.606  17.005  5.973   1.00 32.16  ? 151 VAL   A HB   1 
ATOM   2320 H HG11 . VAL   A 1 166 ? 23.384  14.603  5.859   1.00 38.48  ? 151 VAL   A HG11 1 
ATOM   2321 H HG12 . VAL   A 1 166 ? 22.598  15.301  7.050   1.00 38.48  ? 151 VAL   A HG12 1 
ATOM   2322 H HG13 . VAL   A 1 166 ? 21.819  14.846  5.742   1.00 38.48  ? 151 VAL   A HG13 1 
ATOM   2323 H HG21 . VAL   A 1 166 ? 24.174  15.816  4.030   1.00 35.80  ? 151 VAL   A HG21 1 
ATOM   2324 H HG22 . VAL   A 1 166 ? 22.696  16.040  3.492   1.00 35.80  ? 151 VAL   A HG22 1 
ATOM   2325 H HG23 . VAL   A 1 166 ? 23.664  17.283  3.696   1.00 35.80  ? 151 VAL   A HG23 1 
ATOM   2326 N N    . ARG   A 1 167 ? 20.061  16.898  7.281   1.00 24.60  ? 152 ARG   A N    1 
ATOM   2327 C CA   . ARG   A 1 167 ? 19.406  17.026  8.585   1.00 24.47  ? 152 ARG   A CA   1 
ATOM   2328 C C    . ARG   A 1 167 ? 18.971  15.667  9.117   1.00 24.83  ? 152 ARG   A C    1 
ATOM   2329 O O    . ARG   A 1 167 ? 18.160  14.989  8.483   1.00 25.88  ? 152 ARG   A O    1 
ATOM   2330 C CB   . ARG   A 1 167 ? 18.166  17.925  8.495   1.00 28.00  ? 152 ARG   A CB   1 
ATOM   2331 C CG   . ARG   A 1 167 ? 18.391  19.287  7.874   1.00 34.46  ? 152 ARG   A CG   1 
ATOM   2332 C CD   . ARG   A 1 167 ? 19.003  20.239  8.856   1.00 31.12  ? 152 ARG   A CD   1 
ATOM   2333 N NE   . ARG   A 1 167 ? 19.162  21.570  8.281   1.00 32.78  ? 152 ARG   A NE   1 
ATOM   2334 C CZ   . ARG   A 1 167 ? 20.290  22.053  7.775   1.00 29.09  ? 152 ARG   A CZ   1 
ATOM   2335 N NH1  . ARG   A 1 167 ? 21.394  21.322  7.712   1.00 25.59  ? 152 ARG   A NH1  1 
ATOM   2336 N NH2  . ARG   A 1 167 ? 20.316  23.308  7.338   1.00 32.04  ? 152 ARG   A NH2  1 
ATOM   2337 H H    . ARG   A 1 167 ? 19.671  16.335  6.761   1.00 29.52  ? 152 ARG   A H    1 
ATOM   2338 H HA   . ARG   A 1 167 ? 20.061  17.399  9.195   1.00 29.36  ? 152 ARG   A HA   1 
ATOM   2339 H HB2  . ARG   A 1 167 ? 17.497  17.470  7.959   1.00 33.60  ? 152 ARG   A HB2  1 
ATOM   2340 H HB3  . ARG   A 1 167 ? 17.828  18.070  9.393   1.00 33.60  ? 152 ARG   A HB3  1 
ATOM   2341 H HG2  . ARG   A 1 167 ? 18.992  19.200  7.117   1.00 41.35  ? 152 ARG   A HG2  1 
ATOM   2342 H HG3  . ARG   A 1 167 ? 17.541  19.652  7.582   1.00 41.35  ? 152 ARG   A HG3  1 
ATOM   2343 H HD2  . ARG   A 1 167 ? 18.429  20.310  9.635   1.00 37.35  ? 152 ARG   A HD2  1 
ATOM   2344 H HD3  . ARG   A 1 167 ? 19.878  19.913  9.117   1.00 37.35  ? 152 ARG   A HD3  1 
ATOM   2345 H HE   . ARG   A 1 167 ? 18.471  22.082  8.269   1.00 39.33  ? 152 ARG   A HE   1 
ATOM   2346 H HH11 . ARG   A 1 167 ? 21.391  20.513  8.004   1.00 30.70  ? 152 ARG   A HH11 1 
ATOM   2347 H HH12 . ARG   A 1 167 ? 22.113  21.657  7.380   1.00 30.70  ? 152 ARG   A HH12 1 
ATOM   2348 H HH21 . ARG   A 1 167 ? 19.608  23.795  7.386   1.00 38.45  ? 152 ARG   A HH21 1 
ATOM   2349 H HH22 . ARG   A 1 167 ? 21.040  23.633  7.008   1.00 38.45  ? 152 ARG   A HH22 1 
ATOM   2350 N N    . LEU   A 1 168 ? 19.427  15.313  10.317  1.00 29.43  ? 153 LEU   A N    1 
ATOM   2351 C CA   . LEU   A 1 168 ? 18.960  14.096  10.967  1.00 26.22  ? 153 LEU   A CA   1 
ATOM   2352 C C    . LEU   A 1 168 ? 17.529  14.252  11.468  1.00 26.44  ? 153 LEU   A C    1 
ATOM   2353 O O    . LEU   A 1 168 ? 17.152  15.291  12.014  1.00 26.93  ? 153 LEU   A O    1 
ATOM   2354 C CB   . LEU   A 1 168 ? 19.848  13.738  12.153  1.00 25.87  ? 153 LEU   A CB   1 
ATOM   2355 C CG   . LEU   A 1 168 ? 21.301  13.445  11.855  1.00 25.19  ? 153 LEU   A CG   1 
ATOM   2356 C CD1  . LEU   A 1 168 ? 22.062  13.192  13.139  1.00 27.46  ? 153 LEU   A CD1  1 
ATOM   2357 C CD2  . LEU   A 1 168 ? 21.384  12.252  10.928  1.00 29.65  ? 153 LEU   A CD2  1 
ATOM   2358 H H    . LEU   A 1 168 ? 20.005  15.759  10.772  1.00 35.32  ? 153 LEU   A H    1 
ATOM   2359 H HA   . LEU   A 1 168 ? 18.994  13.377  10.316  1.00 31.47  ? 153 LEU   A HA   1 
ATOM   2360 H HB2  . LEU   A 1 168 ? 19.831  14.482  12.775  1.00 31.05  ? 153 LEU   A HB2  1 
ATOM   2361 H HB3  . LEU   A 1 168 ? 19.479  12.946  12.574  1.00 31.05  ? 153 LEU   A HB3  1 
ATOM   2362 H HG   . LEU   A 1 168 ? 21.715  14.206  11.419  1.00 30.22  ? 153 LEU   A HG   1 
ATOM   2363 H HD11 . LEU   A 1 168 ? 22.988  13.001  12.925  1.00 32.95  ? 153 LEU   A HD11 1 
ATOM   2364 H HD12 . LEU   A 1 168 ? 22.008  13.982  13.699  1.00 32.95  ? 153 LEU   A HD12 1 
ATOM   2365 H HD13 . LEU   A 1 168 ? 21.665  12.434  13.597  1.00 32.95  ? 153 LEU   A HD13 1 
ATOM   2366 H HD21 . LEU   A 1 168 ? 22.308  11.964  10.867  1.00 35.58  ? 153 LEU   A HD21 1 
ATOM   2367 H HD22 . LEU   A 1 168 ? 20.837  11.535  11.287  1.00 35.58  ? 153 LEU   A HD22 1 
ATOM   2368 H HD23 . LEU   A 1 168 ? 21.059  12.510  10.052  1.00 35.58  ? 153 LEU   A HD23 1 
ATOM   2369 N N    . ALA   A 1 169 ? 16.739  13.199  11.287  1.00 26.60  ? 154 ALA   A N    1 
ATOM   2370 C CA   . ALA   A 1 169 ? 15.393  13.083  11.816  1.00 27.32  ? 154 ALA   A CA   1 
ATOM   2371 C C    . ALA   A 1 169 ? 15.274  11.751  12.551  1.00 31.12  ? 154 ALA   A C    1 
ATOM   2372 O O    . ALA   A 1 169 ? 16.218  10.955  12.591  1.00 27.21  ? 154 ALA   A O    1 
ATOM   2373 C CB   . ALA   A 1 169 ? 14.346  13.180  10.701  1.00 27.36  ? 154 ALA   A CB   1 
ATOM   2374 H H    . ALA   A 1 169 ? 16.977  12.505  10.837  1.00 31.92  ? 154 ALA   A H    1 
ATOM   2375 H HA   . ALA   A 1 169 ? 15.233  13.804  12.444  1.00 32.79  ? 154 ALA   A HA   1 
ATOM   2376 H HB1  . ALA   A 1 169 ? 13.462  13.095  11.091  1.00 32.84  ? 154 ALA   A HB1  1 
ATOM   2377 H HB2  . ALA   A 1 169 ? 14.432  14.039  10.260  1.00 32.84  ? 154 ALA   A HB2  1 
ATOM   2378 H HB3  . ALA   A 1 169 ? 14.496  12.464  10.064  1.00 32.84  ? 154 ALA   A HB3  1 
ATOM   2379 N N    . ASP   A 1 170 ? 14.098  11.507  13.132  1.00 35.34  ? 155 ASP   A N    1 
ATOM   2380 C CA   . ASP   A 1 170 ? 13.822  10.261  13.835  1.00 33.72  ? 155 ASP   A CA   1 
ATOM   2381 C C    . ASP   A 1 170 ? 12.357  9.886   13.621  1.00 37.27  ? 155 ASP   A C    1 
ATOM   2382 O O    . ASP   A 1 170 ? 11.594  10.613  12.980  1.00 37.56  ? 155 ASP   A O    1 
ATOM   2383 C CB   . ASP   A 1 170 ? 14.147  10.382  15.328  1.00 40.48  ? 155 ASP   A CB   1 
ATOM   2384 C CG   . ASP   A 1 170 ? 13.267  11.403  16.047  1.00 41.51  ? 155 ASP   A CG   1 
ATOM   2385 O OD1  . ASP   A 1 170 ? 13.055  12.519  15.519  1.00 49.40  ? 155 ASP   A OD1  1 
ATOM   2386 O OD2  . ASP   A 1 170 ? 12.792  11.083  17.157  1.00 55.58  ? 155 ASP   A OD2  1 
ATOM   2387 H H    . ASP   A 1 170 ? 13.437  12.058  13.131  1.00 42.41  ? 155 ASP   A H    1 
ATOM   2388 H HA   . ASP   A 1 170 ? 14.377  9.563   13.453  1.00 40.47  ? 155 ASP   A HA   1 
ATOM   2389 H HB2  . ASP   A 1 170 ? 14.012  9.519   15.751  1.00 48.58  ? 155 ASP   A HB2  1 
ATOM   2390 H HB3  . ASP   A 1 170 ? 15.071  10.660  15.428  1.00 48.58  ? 155 ASP   A HB3  1 
ATOM   2391 N N    . PHE   A 1 171 ? 11.973  8.731   14.170  1.00 47.96  ? 156 PHE   A N    1 
ATOM   2392 C CA   . PHE   A 1 171 ? 10.580  8.301   14.089  1.00 33.44  ? 156 PHE   A CA   1 
ATOM   2393 C C    . PHE   A 1 171 ? 9.655   9.300   14.779  1.00 35.34  ? 156 PHE   A C    1 
ATOM   2394 O O    . PHE   A 1 171 ? 8.553   9.578   14.290  1.00 33.16  ? 156 PHE   A O    1 
ATOM   2395 C CB   . PHE   A 1 171 ? 10.440  6.906   14.700  1.00 32.69  ? 156 PHE   A CB   1 
ATOM   2396 C CG   . PHE   A 1 171 ? 9.064   6.342   14.595  1.00 37.77  ? 156 PHE   A CG   1 
ATOM   2397 C CD1  . PHE   A 1 171 ? 8.650   5.715   13.439  1.00 32.97  ? 156 PHE   A CD1  1 
ATOM   2398 C CD2  . PHE   A 1 171 ? 8.176   6.447   15.651  1.00 40.71  ? 156 PHE   A CD2  1 
ATOM   2399 C CE1  . PHE   A 1 171 ? 7.376   5.202   13.336  1.00 38.18  ? 156 PHE   A CE1  1 
ATOM   2400 C CE2  . PHE   A 1 171 ? 6.904   5.933   15.551  1.00 44.79  ? 156 PHE   A CE2  1 
ATOM   2401 C CZ   . PHE   A 1 171 ? 6.506   5.312   14.389  1.00 36.94  ? 156 PHE   A CZ   1 
ATOM   2402 H H    . PHE   A 1 171 ? 12.492  8.188   14.589  1.00 57.56  ? 156 PHE   A H    1 
ATOM   2403 H HA   . PHE   A 1 171 ? 10.312  8.249   13.159  1.00 40.13  ? 156 PHE   A HA   1 
ATOM   2404 H HB2  . PHE   A 1 171 ? 11.044  6.302   14.240  1.00 39.22  ? 156 PHE   A HB2  1 
ATOM   2405 H HB3  . PHE   A 1 171 ? 10.670  6.953   15.641  1.00 39.22  ? 156 PHE   A HB3  1 
ATOM   2406 H HD1  . PHE   A 1 171 ? 9.237   5.638   12.722  1.00 39.57  ? 156 PHE   A HD1  1 
ATOM   2407 H HD2  . PHE   A 1 171 ? 8.442   6.870   16.436  1.00 48.85  ? 156 PHE   A HD2  1 
ATOM   2408 H HE1  . PHE   A 1 171 ? 7.106   4.781   12.552  1.00 45.81  ? 156 PHE   A HE1  1 
ATOM   2409 H HE2  . PHE   A 1 171 ? 6.314   6.004   16.267  1.00 53.74  ? 156 PHE   A HE2  1 
ATOM   2410 H HZ   . PHE   A 1 171 ? 5.646   4.967   14.318  1.00 44.33  ? 156 PHE   A HZ   1 
ATOM   2411 N N    . GLY   A 1 172 ? 10.079  9.846   15.916  1.00 41.89  ? 157 GLY   A N    1 
ATOM   2412 C CA   . GLY   A 1 172 ? 9.385   10.952  16.550  1.00 42.85  ? 157 GLY   A CA   1 
ATOM   2413 C C    . GLY   A 1 172 ? 8.538   10.531  17.736  1.00 44.35  ? 157 GLY   A C    1 
ATOM   2414 O O    . GLY   A 1 172 ? 8.440   9.357   18.105  1.00 41.45  ? 157 GLY   A O    1 
ATOM   2415 H H    . GLY   A 1 172 ? 10.779  9.587   16.343  1.00 50.27  ? 157 GLY   A H    1 
ATOM   2416 H HA2  . GLY   A 1 172 ? 10.037  11.600  16.861  1.00 51.42  ? 157 GLY   A HA2  1 
ATOM   2417 H HA3  . GLY   A 1 172 ? 8.803   11.376  15.900  1.00 51.42  ? 157 GLY   A HA3  1 
ATOM   2418 N N    . ILE   A 1 173 ? 7.903   11.544  18.331  1.00 48.30  ? 158 ILE   A N    1 
ATOM   2419 C CA   . ILE   A 1 173 ? 7.103   11.360  19.529  1.00 44.16  ? 158 ILE   A CA   1 
ATOM   2420 C C    . ILE   A 1 173 ? 5.897   10.459  19.314  1.00 38.45  ? 158 ILE   A C    1 
ATOM   2421 O O    . ILE   A 1 173 ? 5.238   10.083  20.289  1.00 33.79  ? 158 ILE   A O    1 
ATOM   2422 C CB   . ILE   A 1 173 ? 6.616   12.722  20.077  1.00 50.41  ? 158 ILE   A CB   1 
ATOM   2423 C CG1  . ILE   A 1 173 ? 5.846   13.481  18.998  1.00 42.49  ? 158 ILE   A CG1  1 
ATOM   2424 C CG2  . ILE   A 1 173 ? 7.778   13.545  20.587  1.00 52.86  ? 158 ILE   A CG2  1 
ATOM   2425 C CD1  . ILE   A 1 173 ? 4.369   13.143  18.960  1.00 42.93  ? 158 ILE   A CD1  1 
ATOM   2426 H H    . ILE   A 1 173 ? 7.923   12.357  18.052  1.00 57.96  ? 158 ILE   A H    1 
ATOM   2427 H HA   . ILE   A 1 173 ? 7.681   10.942  20.187  1.00 52.99  ? 158 ILE   A HA   1 
ATOM   2428 H HB   . ILE   A 1 173 ? 6.018   12.554  20.822  1.00 60.49  ? 158 ILE   A HB   1 
ATOM   2429 H HG12 . ILE   A 1 173 ? 5.929   14.432  19.166  1.00 50.99  ? 158 ILE   A HG12 1 
ATOM   2430 H HG13 . ILE   A 1 173 ? 6.224   13.262  18.132  1.00 50.99  ? 158 ILE   A HG13 1 
ATOM   2431 H HG21 . ILE   A 1 173 ? 7.441   14.380  20.945  1.00 63.43  ? 158 ILE   A HG21 1 
ATOM   2432 H HG22 . ILE   A 1 173 ? 8.236   13.047  21.283  1.00 63.43  ? 158 ILE   A HG22 1 
ATOM   2433 H HG23 . ILE   A 1 173 ? 8.387   13.721  19.852  1.00 63.43  ? 158 ILE   A HG23 1 
ATOM   2434 H HD11 . ILE   A 1 173 ? 3.894   13.855  18.503  1.00 51.51  ? 158 ILE   A HD11 1 
ATOM   2435 H HD12 . ILE   A 1 173 ? 4.249   12.306  18.483  1.00 51.51  ? 158 ILE   A HD12 1 
ATOM   2436 H HD13 . ILE   A 1 173 ? 4.041   13.056  19.868  1.00 51.51  ? 158 ILE   A HD13 1 
ATOM   2437 N N    . SER   A 1 174 ? 5.564   10.128  18.066  1.00 41.33  ? 159 SER   A N    1 
ATOM   2438 C CA   . SER   A 1 174 ? 4.425   9.244   17.839  1.00 43.14  ? 159 SER   A CA   1 
ATOM   2439 C C    . SER   A 1 174 ? 4.591   7.922   18.575  1.00 42.65  ? 159 SER   A C    1 
ATOM   2440 O O    . SER   A 1 174 ? 3.596   7.285   18.941  1.00 45.74  ? 159 SER   A O    1 
ATOM   2441 C CB   . SER   A 1 174 ? 4.234   8.985   16.349  1.00 53.89  ? 159 SER   A CB   1 
ATOM   2442 O OG   . SER   A 1 174 ? 3.234   7.999   16.145  1.00 47.24  ? 159 SER   A OG   1 
ATOM   2443 H H    . SER   A 1 174 ? 5.969   10.394  17.355  1.00 49.59  ? 159 SER   A H    1 
ATOM   2444 H HA   . SER   A 1 174 ? 3.627   9.686   18.170  1.00 51.76  ? 159 SER   A HA   1 
ATOM   2445 H HB2  . SER   A 1 174 ? 3.961   9.808   15.915  1.00 64.67  ? 159 SER   A HB2  1 
ATOM   2446 H HB3  . SER   A 1 174 ? 5.070   8.672   15.971  1.00 64.67  ? 159 SER   A HB3  1 
ATOM   2447 H HG   . SER   A 1 174 ? 3.116   7.875   15.323  1.00 56.69  ? 159 SER   A HG   1 
ATOM   2448 N N    . ALA   A 1 175 ? 5.832   7.496   18.809  1.00 37.18  ? 160 ALA   A N    1 
ATOM   2449 C CA   . ALA   A 1 175 ? 6.065   6.284   19.583  1.00 41.35  ? 160 ALA   A CA   1 
ATOM   2450 C C    . ALA   A 1 175 ? 5.785   6.481   21.064  1.00 31.79  ? 160 ALA   A C    1 
ATOM   2451 O O    . ALA   A 1 175 ? 5.674   5.489   21.791  1.00 39.56  ? 160 ALA   A O    1 
ATOM   2452 C CB   . ALA   A 1 175 ? 7.506   5.807   19.391  1.00 42.53  ? 160 ALA   A CB   1 
ATOM   2453 H H    . ALA   A 1 175 ? 6.546   7.888   18.533  1.00 44.62  ? 160 ALA   A H    1 
ATOM   2454 H HA   . ALA   A 1 175 ? 5.476   5.586   19.255  1.00 49.62  ? 160 ALA   A HA   1 
ATOM   2455 H HB1  . ALA   A 1 175 ? 7.644   5.000   19.911  1.00 51.04  ? 160 ALA   A HB1  1 
ATOM   2456 H HB2  . ALA   A 1 175 ? 7.655   5.624   18.450  1.00 51.04  ? 160 ALA   A HB2  1 
ATOM   2457 H HB3  . ALA   A 1 175 ? 8.111   6.502   19.692  1.00 51.04  ? 160 ALA   A HB3  1 
ATOM   2458 N N    . GLN   A 1 176 ? 5.673   7.724   21.524  1.00 31.88  ? 161 GLN   A N    1 
ATOM   2459 C CA   . GLN   A 1 176 ? 5.444   8.028   22.928  1.00 33.39  ? 161 GLN   A CA   1 
ATOM   2460 C C    . GLN   A 1 176 ? 3.991   8.335   23.251  1.00 31.87  ? 161 GLN   A C    1 
ATOM   2461 O O    . GLN   A 1 176 ? 3.672   8.559   24.418  1.00 33.37  ? 161 GLN   A O    1 
ATOM   2462 C CB   . GLN   A 1 176 ? 6.290   9.231   23.358  1.00 41.61  ? 161 GLN   A CB   1 
ATOM   2463 C CG   . GLN   A 1 176 ? 7.740   9.177   22.937  1.00 52.75  ? 161 GLN   A CG   1 
ATOM   2464 C CD   . GLN   A 1 176 ? 8.533   8.241   23.801  1.00 50.90  ? 161 GLN   A CD   1 
ATOM   2465 O OE1  . GLN   A 1 176 ? 9.042   8.629   24.851  1.00 59.91  ? 161 GLN   A OE1  1 
ATOM   2466 N NE2  . GLN   A 1 176 ? 8.627   6.988   23.376  1.00 63.89  ? 161 GLN   A NE2  1 
ATOM   2467 H H    . GLN   A 1 176 ? 5.729   8.424   21.028  1.00 38.25  ? 161 GLN   A H    1 
ATOM   2468 H HA   . GLN   A 1 176 ? 5.715   7.250   23.441  1.00 40.07  ? 161 GLN   A HA   1 
ATOM   2469 H HB2  . GLN   A 1 176 ? 5.904   10.032  22.969  1.00 49.93  ? 161 GLN   A HB2  1 
ATOM   2470 H HB3  . GLN   A 1 176 ? 6.270   9.290   24.326  1.00 49.93  ? 161 GLN   A HB3  1 
ATOM   2471 H HG2  . GLN   A 1 176 ? 7.796   8.867   22.020  1.00 63.30  ? 161 GLN   A HG2  1 
ATOM   2472 H HG3  . GLN   A 1 176 ? 8.129   10.063  23.012  1.00 63.30  ? 161 GLN   A HG3  1 
ATOM   2473 H HE21 . GLN   A 1 176 ? 8.246   6.753   22.642  1.00 76.67  ? 161 GLN   A HE21 1 
ATOM   2474 H HE22 . GLN   A 1 176 ? 9.071   6.411   23.835  1.00 76.67  ? 161 GLN   A HE22 1 
ATOM   2475 N N    . ILE   A 1 177 ? 3.113   8.390   22.254  1.00 31.85  ? 162 ILE   A N    1 
ATOM   2476 C CA   . ILE   A 1 177 ? 1.731   8.801   22.475  1.00 32.08  ? 162 ILE   A CA   1 
ATOM   2477 C C    . ILE   A 1 177 ? 0.869   8.271   21.338  1.00 32.05  ? 162 ILE   A C    1 
ATOM   2478 O O    . ILE   A 1 177 ? 1.386   7.821   20.313  1.00 40.28  ? 162 ILE   A O    1 
ATOM   2479 C CB   . ILE   A 1 177 ? 1.636   10.337  22.595  1.00 32.47  ? 162 ILE   A CB   1 
ATOM   2480 C CG1  . ILE   A 1 177 ? 0.335   10.758  23.283  1.00 34.03  ? 162 ILE   A CG1  1 
ATOM   2481 C CG2  . ILE   A 1 177 ? 1.741   10.990  21.221  1.00 38.76  ? 162 ILE   A CG2  1 
ATOM   2482 C CD1  . ILE   A 1 177 ? 0.357   12.210  23.787  1.00 36.32  ? 162 ILE   A CD1  1 
ATOM   2483 H H    . ILE   A 1 177 ? 3.294   8.192   21.437  1.00 38.22  ? 162 ILE   A H    1 
ATOM   2484 H HA   . ILE   A 1 177 ? 1.401   8.414   23.300  1.00 38.49  ? 162 ILE   A HA   1 
ATOM   2485 H HB   . ILE   A 1 177 ? 2.380   10.635  23.142  1.00 38.96  ? 162 ILE   A HB   1 
ATOM   2486 H HG12 . ILE   A 1 177 ? -0.396  10.672  22.651  1.00 40.84  ? 162 ILE   A HG12 1 
ATOM   2487 H HG13 . ILE   A 1 177 ? 0.182   10.179  24.047  1.00 40.84  ? 162 ILE   A HG13 1 
ATOM   2488 H HG21 . ILE   A 1 177 ? 1.956   11.930  21.334  1.00 46.52  ? 162 ILE   A HG21 1 
ATOM   2489 H HG22 . ILE   A 1 177 ? 2.440   10.549  20.714  1.00 46.52  ? 162 ILE   A HG22 1 
ATOM   2490 H HG23 . ILE   A 1 177 ? 0.891   10.899  20.763  1.00 46.52  ? 162 ILE   A HG23 1 
ATOM   2491 H HD11 . ILE   A 1 177 ? -0.509  12.426  24.167  1.00 43.59  ? 162 ILE   A HD11 1 
ATOM   2492 H HD12 . ILE   A 1 177 ? 1.047   12.300  24.463  1.00 43.59  ? 162 ILE   A HD12 1 
ATOM   2493 H HD13 . ILE   A 1 177 ? 0.548   12.800  23.040  1.00 43.59  ? 162 ILE   A HD13 1 
ATOM   2494 N N    . GLY   A 1 178 ? -0.443  8.304   21.514  1.00 32.22  ? 163 GLY   A N    1 
ATOM   2495 C CA   . GLY   A 1 178 ? -1.340  7.948   20.437  1.00 33.15  ? 163 GLY   A CA   1 
ATOM   2496 C C    . GLY   A 1 178 ? -1.488  6.447   20.238  1.00 39.81  ? 163 GLY   A C    1 
ATOM   2497 O O    . GLY   A 1 178 ? -1.201  5.625   21.118  1.00 31.82  ? 163 GLY   A O    1 
ATOM   2498 H H    . GLY   A 1 178 ? -0.834  8.528   22.246  1.00 38.66  ? 163 GLY   A H    1 
ATOM   2499 H HA2  . GLY   A 1 178 ? -2.218  8.315   20.623  1.00 39.78  ? 163 GLY   A HA2  1 
ATOM   2500 H HA3  . GLY   A 1 178 ? -1.007  8.330   19.610  1.00 39.78  ? 163 GLY   A HA3  1 
ATOM   2501 N N    . ALA   A 1 179 ? -1.953  6.092   19.037  1.00 38.22  ? 164 ALA   A N    1 
ATOM   2502 C CA   . ALA   A 1 179 ? -2.219  4.691   18.733  1.00 41.92  ? 164 ALA   A CA   1 
ATOM   2503 C C    . ALA   A 1 179 ? -0.936  3.873   18.653  1.00 33.85  ? 164 ALA   A C    1 
ATOM   2504 O O    . ALA   A 1 179 ? -0.954  2.672   18.933  1.00 33.88  ? 164 ALA   A O    1 
ATOM   2505 C CB   . ALA   A 1 179 ? -2.999  4.579   17.421  1.00 44.65  ? 164 ALA   A CB   1 
ATOM   2506 H H    . ALA   A 1 179 ? -2.119  6.637   18.393  1.00 45.87  ? 164 ALA   A H    1 
ATOM   2507 H HA   . ALA   A 1 179 ? -2.766  4.320   19.443  1.00 50.31  ? 164 ALA   A HA   1 
ATOM   2508 H HB1  . ALA   A 1 179 ? -3.168  3.643   17.233  1.00 53.58  ? 164 ALA   A HB1  1 
ATOM   2509 H HB2  . ALA   A 1 179 ? -3.839  5.055   17.512  1.00 53.58  ? 164 ALA   A HB2  1 
ATOM   2510 H HB3  . ALA   A 1 179 ? -2.473  4.970   16.707  1.00 53.58  ? 164 ALA   A HB3  1 
ATOM   2511 N N    . GLU   A 1 180 ? 0.183   4.491   18.269  1.00 31.77  ? 165 GLU   A N    1 
ATOM   2512 C CA   . GLU   A 1 180 ? 1.434   3.744   18.208  1.00 32.64  ? 165 GLU   A CA   1 
ATOM   2513 C C    . GLU   A 1 180 ? 1.877   3.312   19.603  1.00 32.52  ? 165 GLU   A C    1 
ATOM   2514 O O    . GLU   A 1 180 ? 2.228   2.146   19.816  1.00 32.40  ? 165 GLU   A O    1 
ATOM   2515 C CB   . GLU   A 1 180 ? 2.510   4.583   17.521  1.00 36.12  ? 165 GLU   A CB   1 
ATOM   2516 C CG   . GLU   A 1 180 ? 3.809   3.845   17.256  1.00 43.58  ? 165 GLU   A CG   1 
ATOM   2517 C CD   . GLU   A 1 180 ? 3.665   2.679   16.267  1.00 53.39  ? 165 GLU   A CD   1 
ATOM   2518 O OE1  . GLU   A 1 180 ? 2.541   2.418   15.774  1.00 43.26  ? 165 GLU   A OE1  1 
ATOM   2519 O OE2  . GLU   A 1 180 ? 4.691   2.020   15.978  1.00 47.43  ? 165 GLU   A OE2  1 
ATOM   2520 H H    . GLU   A 1 180 ? 0.240   5.319   18.045  1.00 38.12  ? 165 GLU   A H    1 
ATOM   2521 H HA   . GLU   A 1 180 ? 1.302   2.944   17.675  1.00 39.16  ? 165 GLU   A HA   1 
ATOM   2522 H HB2  . GLU   A 1 180 ? 2.166   4.887   16.667  1.00 43.34  ? 165 GLU   A HB2  1 
ATOM   2523 H HB3  . GLU   A 1 180 ? 2.715   5.344   18.086  1.00 43.34  ? 165 GLU   A HB3  1 
ATOM   2524 H HG2  . GLU   A 1 180 ? 4.453   4.468   16.887  1.00 52.29  ? 165 GLU   A HG2  1 
ATOM   2525 H HG3  . GLU   A 1 180 ? 4.140   3.483   18.093  1.00 52.29  ? 165 GLU   A HG3  1 
ATOM   2526 N N    . LEU   A 1 181 ? 1.846   4.236   20.570  1.00 32.81  ? 166 LEU   A N    1 
ATOM   2527 C CA   . LEU   A 1 181 ? 2.155   3.887   21.955  1.00 31.22  ? 166 LEU   A CA   1 
ATOM   2528 C C    . LEU   A 1 181 ? 1.267   2.753   22.447  1.00 31.13  ? 166 LEU   A C    1 
ATOM   2529 O O    . LEU   A 1 181 ? 1.745   1.826   23.114  1.00 31.02  ? 166 LEU   A O    1 
ATOM   2530 C CB   . LEU   A 1 181 ? 1.992   5.110   22.863  1.00 31.38  ? 166 LEU   A CB   1 
ATOM   2531 C CG   . LEU   A 1 181 ? 2.099   4.815   24.363  1.00 32.72  ? 166 LEU   A CG   1 
ATOM   2532 C CD1  . LEU   A 1 181 ? 3.517   4.464   24.749  1.00 31.35  ? 166 LEU   A CD1  1 
ATOM   2533 C CD2  . LEU   A 1 181 ? 1.582   5.990   25.193  1.00 31.68  ? 166 LEU   A CD2  1 
ATOM   2534 H H    . LEU   A 1 181 ? 1.651   5.065   20.449  1.00 39.37  ? 166 LEU   A H    1 
ATOM   2535 H HA   . LEU   A 1 181 ? 3.079   3.597   21.998  1.00 37.47  ? 166 LEU   A HA   1 
ATOM   2536 H HB2  . LEU   A 1 181 ? 2.685   5.751   22.641  1.00 37.65  ? 166 LEU   A HB2  1 
ATOM   2537 H HB3  . LEU   A 1 181 ? 1.117   5.497   22.703  1.00 37.65  ? 166 LEU   A HB3  1 
ATOM   2538 H HG   . LEU   A 1 181 ? 1.541   4.047   24.563  1.00 39.26  ? 166 LEU   A HG   1 
ATOM   2539 H HD11 . LEU   A 1 181 ? 3.551   4.290   25.703  1.00 37.62  ? 166 LEU   A HD11 1 
ATOM   2540 H HD12 . LEU   A 1 181 ? 3.791   3.673   24.259  1.00 37.62  ? 166 LEU   A HD12 1 
ATOM   2541 H HD13 . LEU   A 1 181 ? 4.098   5.208   24.527  1.00 37.62  ? 166 LEU   A HD13 1 
ATOM   2542 H HD21 . LEU   A 1 181 ? 1.675   5.776   26.135  1.00 38.01  ? 166 LEU   A HD21 1 
ATOM   2543 H HD22 . LEU   A 1 181 ? 2.103   6.780   24.980  1.00 38.01  ? 166 LEU   A HD22 1 
ATOM   2544 H HD23 . LEU   A 1 181 ? 0.648   6.141   24.979  1.00 38.01  ? 166 LEU   A HD23 1 
ATOM   2545 N N    . ALA   A 1 182 ? -0.031  2.818   22.152  1.00 31.22  ? 167 ALA   A N    1 
ATOM   2546 C CA   . ALA   A 1 182 ? -0.936  1.773   22.609  1.00 31.11  ? 167 ALA   A CA   1 
ATOM   2547 C C    . ALA   A 1 182 ? -0.561  0.429   21.999  1.00 32.27  ? 167 ALA   A C    1 
ATOM   2548 O O    . ALA   A 1 182 ? -0.605  -0.602  22.678  1.00 35.63  ? 167 ALA   A O    1 
ATOM   2549 C CB   . ALA   A 1 182 ? -2.378  2.150   22.270  1.00 31.37  ? 167 ALA   A CB   1 
ATOM   2550 H H    . ALA   A 1 182 ? -0.404  3.445   21.696  1.00 37.46  ? 167 ALA   A H    1 
ATOM   2551 H HA   . ALA   A 1 182 ? -0.873  1.690   23.574  1.00 37.33  ? 167 ALA   A HA   1 
ATOM   2552 H HB1  . ALA   A 1 182 ? -2.969  1.445   22.577  1.00 37.64  ? 167 ALA   A HB1  1 
ATOM   2553 H HB2  . ALA   A 1 182 ? -2.599  2.984   22.714  1.00 37.64  ? 167 ALA   A HB2  1 
ATOM   2554 H HB3  . ALA   A 1 182 ? -2.459  2.255   21.309  1.00 37.64  ? 167 ALA   A HB3  1 
ATOM   2555 N N    . ARG   A 1 183 ? -0.154  0.421   20.725  1.00 31.22  ? 168 ARG   A N    1 
ATOM   2556 C CA   . ARG   A 1 183 ? 0.238   -0.836  20.099  1.00 32.18  ? 168 ARG   A CA   1 
ATOM   2557 C C    . ARG   A 1 183 ? 1.521   -1.377  20.710  1.00 34.97  ? 168 ARG   A C    1 
ATOM   2558 O O    . ARG   A 1 183 ? 1.661   -2.592  20.894  1.00 32.76  ? 168 ARG   A O    1 
ATOM   2559 C CB   . ARG   A 1 183 ? 0.403   -0.644  18.596  1.00 37.27  ? 168 ARG   A CB   1 
ATOM   2560 C CG   . ARG   A 1 183 ? -0.898  -0.455  17.862  1.00 38.15  ? 168 ARG   A CG   1 
ATOM   2561 C CD   . ARG   A 1 183 ? -0.765  -1.034  16.474  1.00 49.79  ? 168 ARG   A CD   1 
ATOM   2562 N NE   . ARG   A 1 183 ? 0.385   -0.457  15.800  1.00 47.79  ? 168 ARG   A NE   1 
ATOM   2563 C CZ   . ARG   A 1 183 ? 1.106   -1.068  14.872  1.00 41.95  ? 168 ARG   A CZ   1 
ATOM   2564 N NH1  . ARG   A 1 183 ? 0.839   -2.307  14.493  1.00 43.22  ? 168 ARG   A NH1  1 
ATOM   2565 N NH2  . ARG   A 1 183 ? 2.123   -0.417  14.312  1.00 34.32  ? 168 ARG   A NH2  1 
ATOM   2566 H H    . ARG   A 1 183 ? -0.098  1.113   20.218  1.00 37.47  ? 168 ARG   A H    1 
ATOM   2567 H HA   . ARG   A 1 183 ? -0.465  -1.488  20.242  1.00 38.61  ? 168 ARG   A HA   1 
ATOM   2568 H HB2  . ARG   A 1 183 ? 0.948   0.144   18.441  1.00 44.73  ? 168 ARG   A HB2  1 
ATOM   2569 H HB3  . ARG   A 1 183 ? 0.840   -1.427  18.228  1.00 44.73  ? 168 ARG   A HB3  1 
ATOM   2570 H HG2  . ARG   A 1 183 ? -1.612  -0.917  18.330  1.00 45.78  ? 168 ARG   A HG2  1 
ATOM   2571 H HG3  . ARG   A 1 183 ? -1.105  0.490   17.792  1.00 45.78  ? 168 ARG   A HG3  1 
ATOM   2572 H HD2  . ARG   A 1 183 ? -0.642  -1.994  16.531  1.00 59.75  ? 168 ARG   A HD2  1 
ATOM   2573 H HD3  . ARG   A 1 183 ? -1.561  -0.831  15.958  1.00 59.75  ? 168 ARG   A HD3  1 
ATOM   2574 H HE   . ARG   A 1 183 ? 0.616   0.342   16.021  1.00 57.35  ? 168 ARG   A HE   1 
ATOM   2575 H HH11 . ARG   A 1 183 ? 0.185   -2.735  14.852  1.00 51.86  ? 168 ARG   A HH11 1 
ATOM   2576 H HH12 . ARG   A 1 183 ? 1.320   -2.685  13.889  1.00 51.86  ? 168 ARG   A HH12 1 
ATOM   2577 H HH21 . ARG   A 1 183 ? 2.304   0.388   14.555  1.00 41.18  ? 168 ARG   A HH21 1 
ATOM   2578 H HH22 . ARG   A 1 183 ? 2.600   -0.801  13.708  1.00 41.18  ? 168 ARG   A HH22 1 
ATOM   2579 N N    . ARG   A 1 184 ? 2.466   -0.494  21.043  1.00 31.02  ? 169 ARG   A N    1 
ATOM   2580 C CA   . ARG   A 1 184 ? 3.719   -0.950  21.634  1.00 30.97  ? 169 ARG   A CA   1 
ATOM   2581 C C    . ARG   A 1 184 ? 3.489   -1.549  23.018  1.00 38.42  ? 169 ARG   A C    1 
ATOM   2582 O O    . ARG   A 1 184 ? 4.043   -2.609  23.341  1.00 32.54  ? 169 ARG   A O    1 
ATOM   2583 C CB   . ARG   A 1 184 ? 4.721   0.206   21.700  1.00 39.04  ? 169 ARG   A CB   1 
ATOM   2584 C CG   . ARG   A 1 184 ? 4.932   0.896   20.363  1.00 41.64  ? 169 ARG   A CG   1 
ATOM   2585 C CD   . ARG   A 1 184 ? 6.282   1.580   20.226  1.00 37.62  ? 169 ARG   A CD   1 
ATOM   2586 N NE   . ARG   A 1 184 ? 6.483   1.995   18.841  1.00 50.14  ? 169 ARG   A NE   1 
ATOM   2587 C CZ   . ARG   A 1 184 ? 7.657   2.041   18.225  1.00 45.75  ? 169 ARG   A CZ   1 
ATOM   2588 N NH1  . ARG   A 1 184 ? 8.780   1.713   18.849  1.00 43.42  ? 169 ARG   A NH1  1 
ATOM   2589 N NH2  . ARG   A 1 184 ? 7.705   2.415   16.950  1.00 42.48  ? 169 ARG   A NH2  1 
ATOM   2590 H H    . ARG   A 1 184 ? 2.405   0.358   20.938  1.00 37.23  ? 169 ARG   A H    1 
ATOM   2591 H HA   . ARG   A 1 184 ? 4.100   -1.641  21.070  1.00 37.16  ? 169 ARG   A HA   1 
ATOM   2592 H HB2  . ARG   A 1 184 ? 4.394   0.869   22.329  1.00 46.85  ? 169 ARG   A HB2  1 
ATOM   2593 H HB3  . ARG   A 1 184 ? 5.578   -0.138  21.996  1.00 46.85  ? 169 ARG   A HB3  1 
ATOM   2594 H HG2  . ARG   A 1 184 ? 4.865   0.234   19.657  1.00 49.96  ? 169 ARG   A HG2  1 
ATOM   2595 H HG3  . ARG   A 1 184 ? 4.246   1.572   20.249  1.00 49.96  ? 169 ARG   A HG3  1 
ATOM   2596 H HD2  . ARG   A 1 184 ? 6.311   2.365   20.795  1.00 45.14  ? 169 ARG   A HD2  1 
ATOM   2597 H HD3  . ARG   A 1 184 ? 6.988   0.964   20.474  1.00 45.14  ? 169 ARG   A HD3  1 
ATOM   2598 H HE   . ARG   A 1 184 ? 5.789   2.227   18.391  1.00 60.17  ? 169 ARG   A HE   1 
ATOM   2599 H HH11 . ARG   A 1 184 ? 8.757   1.464   19.672  1.00 52.10  ? 169 ARG   A HH11 1 
ATOM   2600 H HH12 . ARG   A 1 184 ? 9.530   1.749   18.431  1.00 52.10  ? 169 ARG   A HH12 1 
ATOM   2601 H HH21 . ARG   A 1 184 ? 6.981   2.624   16.536  1.00 50.97  ? 169 ARG   A HH21 1 
ATOM   2602 H HH22 . ARG   A 1 184 ? 8.460   2.449   16.540  1.00 50.97  ? 169 ARG   A HH22 1 
ATOM   2603 N N    . LEU   A 1 185 ? 2.658   -0.901  23.841  1.00 36.11  ? 170 LEU   A N    1 
ATOM   2604 C CA   . LEU   A 1 185 ? 2.433   -1.388  25.200  1.00 34.38  ? 170 LEU   A CA   1 
ATOM   2605 C C    . LEU   A 1 185 ? 1.726   -2.736  25.193  1.00 37.86  ? 170 LEU   A C    1 
ATOM   2606 O O    . LEU   A 1 185 ? 2.031   -3.607  26.018  1.00 38.46  ? 170 LEU   A O    1 
ATOM   2607 C CB   . LEU   A 1 185 ? 1.626   -0.366  26.002  1.00 34.66  ? 170 LEU   A CB   1 
ATOM   2608 C CG   . LEU   A 1 185 ? 2.315   0.983   26.195  1.00 34.87  ? 170 LEU   A CG   1 
ATOM   2609 C CD1  . LEU   A 1 185 ? 1.332   1.963   26.771  1.00 38.81  ? 170 LEU   A CD1  1 
ATOM   2610 C CD2  . LEU   A 1 185 ? 3.551   0.847   27.086  1.00 36.90  ? 170 LEU   A CD2  1 
ATOM   2611 H H    . LEU   A 1 185 ? 2.221   -0.189  23.639  1.00 43.33  ? 170 LEU   A H    1 
ATOM   2612 H HA   . LEU   A 1 185 ? 3.293   -1.499  25.636  1.00 41.26  ? 170 LEU   A HA   1 
ATOM   2613 H HB2  . LEU   A 1 185 ? 0.790   -0.203  25.539  1.00 41.59  ? 170 LEU   A HB2  1 
ATOM   2614 H HB3  . LEU   A 1 185 ? 1.452   -0.734  26.882  1.00 41.59  ? 170 LEU   A HB3  1 
ATOM   2615 H HG   . LEU   A 1 185 ? 2.623   1.319   25.339  1.00 41.84  ? 170 LEU   A HG   1 
ATOM   2616 H HD11 . LEU   A 1 185 ? 1.794   2.791   26.974  1.00 46.58  ? 170 LEU   A HD11 1 
ATOM   2617 H HD12 . LEU   A 1 185 ? 0.631   2.126   26.122  1.00 46.58  ? 170 LEU   A HD12 1 
ATOM   2618 H HD13 . LEU   A 1 185 ? 0.952   1.590   27.582  1.00 46.58  ? 170 LEU   A HD13 1 
ATOM   2619 H HD21 . LEU   A 1 185 ? 3.912   1.730   27.262  1.00 44.28  ? 170 LEU   A HD21 1 
ATOM   2620 H HD22 . LEU   A 1 185 ? 3.294   0.423   27.920  1.00 44.28  ? 170 LEU   A HD22 1 
ATOM   2621 H HD23 . LEU   A 1 185 ? 4.212   0.305   26.629  1.00 44.28  ? 170 LEU   A HD23 1 
ATOM   2622 N N    . GLU   A 1 186 ? 0.776   -2.927  24.275  1.00 42.08  ? 171 GLU   A N    1 
ATOM   2623 C CA   . GLU   A 1 186 ? 0.167   -4.242  24.128  1.00 43.59  ? 171 GLU   A CA   1 
ATOM   2624 C C    . GLU   A 1 186 ? 1.223   -5.289  23.791  1.00 45.53  ? 171 GLU   A C    1 
ATOM   2625 O O    . GLU   A 1 186 ? 1.161   -6.424  24.274  1.00 45.84  ? 171 GLU   A O    1 
ATOM   2626 C CB   . GLU   A 1 186 ? -0.915  -4.208  23.049  1.00 45.93  ? 171 GLU   A CB   1 
ATOM   2627 C CG   . GLU   A 1 186 ? -1.681  -5.531  22.912  1.00 55.28  ? 171 GLU   A CG   1 
ATOM   2628 C CD   . GLU   A 1 186 ? -2.480  -5.636  21.621  1.00 64.62  ? 171 GLU   A CD   1 
ATOM   2629 O OE1  . GLU   A 1 186 ? -1.911  -5.377  20.537  1.00 56.89  ? 171 GLU   A OE1  1 
ATOM   2630 O OE2  . GLU   A 1 186 ? -3.680  -5.983  21.693  1.00 69.56  ? 171 GLU   A OE2  1 
ATOM   2631 H H    . GLU   A 1 186 ? 0.475   -2.324  23.740  1.00 50.49  ? 171 GLU   A H    1 
ATOM   2632 H HA   . GLU   A 1 186 ? -0.257  -4.488  24.965  1.00 52.31  ? 171 GLU   A HA   1 
ATOM   2633 H HB2  . GLU   A 1 186 ? -1.557  -3.515  23.271  1.00 55.12  ? 171 GLU   A HB2  1 
ATOM   2634 H HB3  . GLU   A 1 186 ? -0.500  -4.015  22.195  1.00 55.12  ? 171 GLU   A HB3  1 
ATOM   2635 H HG2  . GLU   A 1 186 ? -1.046  -6.264  22.928  1.00 66.33  ? 171 GLU   A HG2  1 
ATOM   2636 H HG3  . GLU   A 1 186 ? -2.301  -5.612  23.653  1.00 66.33  ? 171 GLU   A HG3  1 
ATOM   2637 N N    . PHE   A 1 187 ? 2.215   -4.917  22.979  1.00 35.92  ? 172 PHE   A N    1 
ATOM   2638 C CA   . PHE   A 1 187 ? 3.196   -5.895  22.528  1.00 41.15  ? 172 PHE   A CA   1 
ATOM   2639 C C    . PHE   A 1 187 ? 4.111   -6.343  23.660  1.00 46.64  ? 172 PHE   A C    1 
ATOM   2640 O O    . PHE   A 1 187 ? 4.471   -7.524  23.741  1.00 40.36  ? 172 PHE   A O    1 
ATOM   2641 C CB   . PHE   A 1 187 ? 4.046   -5.339  21.392  1.00 42.05  ? 172 PHE   A CB   1 
ATOM   2642 C CG   . PHE   A 1 187 ? 5.120   -6.287  20.941  1.00 36.67  ? 172 PHE   A CG   1 
ATOM   2643 C CD1  . PHE   A 1 187 ? 4.794   -7.412  20.207  1.00 40.22  ? 172 PHE   A CD1  1 
ATOM   2644 C CD2  . PHE   A 1 187 ? 6.444   -6.071  21.272  1.00 44.64  ? 172 PHE   A CD2  1 
ATOM   2645 C CE1  . PHE   A 1 187 ? 5.776   -8.299  19.793  1.00 48.21  ? 172 PHE   A CE1  1 
ATOM   2646 C CE2  . PHE   A 1 187 ? 7.432   -6.956  20.861  1.00 44.77  ? 172 PHE   A CE2  1 
ATOM   2647 C CZ   . PHE   A 1 187 ? 7.097   -8.067  20.121  1.00 44.34  ? 172 PHE   A CZ   1 
ATOM   2648 H H    . PHE   A 1 187 ? 2.339   -4.119  22.683  1.00 43.10  ? 172 PHE   A H    1 
ATOM   2649 H HA   . PHE   A 1 187 ? 2.702   -6.662  22.197  1.00 49.38  ? 172 PHE   A HA   1 
ATOM   2650 H HB2  . PHE   A 1 187 ? 3.473   -5.153  20.632  1.00 50.46  ? 172 PHE   A HB2  1 
ATOM   2651 H HB3  . PHE   A 1 187 ? 4.475   -4.522  21.691  1.00 50.46  ? 172 PHE   A HB3  1 
ATOM   2652 H HD1  . PHE   A 1 187 ? 3.906   -7.576  19.988  1.00 48.27  ? 172 PHE   A HD1  1 
ATOM   2653 H HD2  . PHE   A 1 187 ? 6.676   -5.324  21.775  1.00 53.57  ? 172 PHE   A HD2  1 
ATOM   2654 H HE1  . PHE   A 1 187 ? 5.545   -9.050  19.295  1.00 57.85  ? 172 PHE   A HE1  1 
ATOM   2655 H HE2  . PHE   A 1 187 ? 8.321   -6.799  21.087  1.00 53.73  ? 172 PHE   A HE2  1 
ATOM   2656 H HZ   . PHE   A 1 187 ? 7.758   -8.658  19.841  1.00 53.21  ? 172 PHE   A HZ   1 
ATOM   2657 N N    . ILE   A 1 188 ? 4.532   -5.411  24.522  1.00 34.79  ? 173 ILE   A N    1 
ATOM   2658 C CA   . ILE   A 1 188 ? 5.431   -5.777  25.613  1.00 35.88  ? 173 ILE   A CA   1 
ATOM   2659 C C    . ILE   A 1 188 ? 4.694   -6.377  26.796  1.00 36.90  ? 173 ILE   A C    1 
ATOM   2660 O O    . ILE   A 1 188 ? 5.339   -6.750  27.786  1.00 38.74  ? 173 ILE   A O    1 
ATOM   2661 C CB   . ILE   A 1 188 ? 6.266   -4.565  26.069  1.00 33.95  ? 173 ILE   A CB   1 
ATOM   2662 C CG1  . ILE   A 1 188 ? 5.394   -3.528  26.779  1.00 39.53  ? 173 ILE   A CG1  1 
ATOM   2663 C CG2  . ILE   A 1 188 ? 6.962   -3.922  24.870  1.00 42.14  ? 173 ILE   A CG2  1 
ATOM   2664 C CD1  . ILE   A 1 188 ? 6.172   -2.266  27.187  1.00 48.11  ? 173 ILE   A CD1  1 
ATOM   2665 H H    . ILE   A 1 188 ? 4.315   -4.580  24.495  1.00 41.75  ? 173 ILE   A H    1 
ATOM   2666 H HA   . ILE   A 1 188 ? 6.046   -6.452  25.285  1.00 43.06  ? 173 ILE   A HA   1 
ATOM   2667 H HB   . ILE   A 1 188 ? 6.932   -4.884  26.697  1.00 40.74  ? 173 ILE   A HB   1 
ATOM   2668 H HG12 . ILE   A 1 188 ? 4.677   -3.259  26.184  1.00 47.44  ? 173 ILE   A HG12 1 
ATOM   2669 H HG13 . ILE   A 1 188 ? 5.026   -3.926  27.584  1.00 47.44  ? 173 ILE   A HG13 1 
ATOM   2670 H HG21 . ILE   A 1 188 ? 7.741   -3.436  25.181  1.00 50.57  ? 173 ILE   A HG21 1 
ATOM   2671 H HG22 . ILE   A 1 188 ? 7.232   -4.619  24.251  1.00 50.57  ? 173 ILE   A HG22 1 
ATOM   2672 H HG23 . ILE   A 1 188 ? 6.344   -3.314  24.435  1.00 50.57  ? 173 ILE   A HG23 1 
ATOM   2673 H HD11 . ILE   A 1 188 ? 5.675   -1.798  27.875  1.00 57.73  ? 173 ILE   A HD11 1 
ATOM   2674 H HD12 . ILE   A 1 188 ? 7.042   -2.528  27.526  1.00 57.73  ? 173 ILE   A HD12 1 
ATOM   2675 H HD13 . ILE   A 1 188 ? 6.278   -1.696  26.409  1.00 57.73  ? 173 ILE   A HD13 1 
ATOM   2676 N N    . GLY   A 1 189 ? 3.369   -6.490  26.728  1.00 40.60  ? 174 GLY   A N    1 
ATOM   2677 C CA   . GLY   A 1 189 ? 2.594   -7.047  27.821  1.00 43.45  ? 174 GLY   A CA   1 
ATOM   2678 C C    . GLY   A 1 189 ? 2.201   -6.058  28.899  1.00 50.56  ? 174 GLY   A C    1 
ATOM   2679 O O    . GLY   A 1 189 ? 1.895   -6.478  30.025  1.00 44.15  ? 174 GLY   A O    1 
ATOM   2680 H H    . GLY   A 1 189 ? 2.897   -6.249  26.051  1.00 48.72  ? 174 GLY   A H    1 
ATOM   2681 H HA2  . GLY   A 1 189 ? 1.779   -7.428  27.459  1.00 52.14  ? 174 GLY   A HA2  1 
ATOM   2682 H HA3  . GLY   A 1 189 ? 3.112   -7.751  28.241  1.00 52.14  ? 174 GLY   A HA3  1 
ATOM   2683 N N    . THR   A 1 190 ? 2.174   -4.765  28.587  1.00 37.00  ? 175 THR   A N    1 
ATOM   2684 C CA   . THR   A 1 190 ? 2.028   -3.686  29.563  1.00 30.66  ? 175 THR   A CA   1 
ATOM   2685 C C    . THR   A 1 190 ? 3.252   -3.704  30.475  1.00 36.55  ? 175 THR   A C    1 
ATOM   2686 O O    . THR   A 1 190 ? 4.089   -4.612  30.380  1.00 32.08  ? 175 THR   A O    1 
ATOM   2687 C CB   . THR   A 1 190 ? 0.719   -3.788  30.353  1.00 40.24  ? 175 THR   A CB   1 
ATOM   2688 O OG1  . THR   A 1 190 ? 0.812   -4.765  31.399  1.00 45.23  ? 175 THR   A OG1  1 
ATOM   2689 C CG2  . THR   A 1 190 ? -0.440  -4.147  29.421  1.00 45.54  ? 175 THR   A CG2  1 
ATOM   2690 H H    . THR   A 1 190 ? 2.240   -4.472  27.782  1.00 44.40  ? 175 THR   A H    1 
ATOM   2691 H HA   . THR   A 1 190 ? 1.983   -2.831  29.107  1.00 36.79  ? 175 THR   A HA   1 
ATOM   2692 H HB   . THR   A 1 190 ? 0.542   -2.926  30.762  1.00 48.29  ? 175 THR   A HB   1 
ATOM   2693 H HG1  . THR   A 1 190 ? 0.890   -5.533  31.068  1.00 54.28  ? 175 THR   A HG1  1 
ATOM   2694 H HG21 . THR   A 1 190 ? -1.286  -3.998  29.871  1.00 54.64  ? 175 THR   A HG21 1 
ATOM   2695 H HG22 . THR   A 1 190 ? -0.407  -3.595  28.623  1.00 54.64  ? 175 THR   A HG22 1 
ATOM   2696 H HG23 . THR   A 1 190 ? -0.380  -5.079  29.161  1.00 54.64  ? 175 THR   A HG23 1 
ATOM   2697 N N    . PRO   A 1 191 ? 3.441   -2.681  31.305  1.00 33.41  ? 176 PRO   A N    1 
ATOM   2698 C CA   . PRO   A 1 191 ? 4.594   -2.659  32.222  1.00 33.53  ? 176 PRO   A CA   1 
ATOM   2699 C C    . PRO   A 1 191 ? 4.294   -3.054  33.661  1.00 32.78  ? 176 PRO   A C    1 
ATOM   2700 O O    . PRO   A 1 191 ? 5.229   -3.076  34.469  1.00 34.10  ? 176 PRO   A O    1 
ATOM   2701 C CB   . PRO   A 1 191 ? 5.010   -1.182  32.157  1.00 36.01  ? 176 PRO   A CB   1 
ATOM   2702 C CG   . PRO   A 1 191 ? 3.720   -0.455  31.996  1.00 35.35  ? 176 PRO   A CG   1 
ATOM   2703 C CD   . PRO   A 1 191 ? 2.813   -1.350  31.184  1.00 34.58  ? 176 PRO   A CD   1 
ATOM   2704 H HA   . PRO   A 1 191 ? 5.309   -3.219  31.882  1.00 40.23  ? 176 PRO   A HA   1 
ATOM   2705 H HB2  . PRO   A 1 191 ? 5.459   -0.924  32.977  1.00 43.21  ? 176 PRO   A HB2  1 
ATOM   2706 H HB3  . PRO   A 1 191 ? 5.595   -1.032  31.397  1.00 43.21  ? 176 PRO   A HB3  1 
ATOM   2707 H HG2  . PRO   A 1 191 ? 3.335   -0.284  32.870  1.00 42.42  ? 176 PRO   A HG2  1 
ATOM   2708 H HG3  . PRO   A 1 191 ? 3.876   0.382   31.532  1.00 42.42  ? 176 PRO   A HG3  1 
ATOM   2709 H HD2  . PRO   A 1 191 ? 1.916   -1.358  31.553  1.00 41.50  ? 176 PRO   A HD2  1 
ATOM   2710 H HD3  . PRO   A 1 191 ? 2.788   -1.065  30.257  1.00 41.50  ? 176 PRO   A HD3  1 
ATOM   2711 N N    . TYR   A 1 192 ? 3.038   -3.359  33.999  1.00 35.45  ? 177 TYR   A N    1 
ATOM   2712 C CA   . TYR   A 1 192 ? 2.657   -3.452  35.410  1.00 31.36  ? 177 TYR   A CA   1 
ATOM   2713 C C    . TYR   A 1 192 ? 3.333   -4.629  36.101  1.00 31.42  ? 177 TYR   A C    1 
ATOM   2714 O O    . TYR   A 1 192 ? 3.727   -4.516  37.266  1.00 31.76  ? 177 TYR   A O    1 
ATOM   2715 C CB   . TYR   A 1 192 ? 1.133   -3.524  35.531  1.00 30.46  ? 177 TYR   A CB   1 
ATOM   2716 C CG   . TYR   A 1 192 ? 0.484   -2.277  34.963  1.00 30.30  ? 177 TYR   A CG   1 
ATOM   2717 C CD1  . TYR   A 1 192 ? 0.568   -1.061  35.635  1.00 30.53  ? 177 TYR   A CD1  1 
ATOM   2718 C CD2  . TYR   A 1 192 ? -0.159  -2.300  33.735  1.00 30.86  ? 177 TYR   A CD2  1 
ATOM   2719 C CE1  . TYR   A 1 192 ? 0.008   0.091   35.110  1.00 31.46  ? 177 TYR   A CE1  1 
ATOM   2720 C CE2  . TYR   A 1 192 ? -0.722  -1.145  33.193  1.00 32.56  ? 177 TYR   A CE2  1 
ATOM   2721 C CZ   . TYR   A 1 192 ? -0.639  0.047   33.889  1.00 34.91  ? 177 TYR   A CZ   1 
ATOM   2722 O OH   . TYR   A 1 192 ? -1.198  1.194   33.360  1.00 35.22  ? 177 TYR   A OH   1 
ATOM   2723 H H    . TYR   A 1 192 ? 2.401   -3.514  33.443  1.00 42.54  ? 177 TYR   A H    1 
ATOM   2724 H HA   . TYR   A 1 192 ? 2.950   -2.650  35.870  1.00 37.63  ? 177 TYR   A HA   1 
ATOM   2725 H HB2  . TYR   A 1 192 ? 0.806   -4.293  35.038  1.00 36.55  ? 177 TYR   A HB2  1 
ATOM   2726 H HB3  . TYR   A 1 192 ? 0.887   -3.600  36.466  1.00 36.55  ? 177 TYR   A HB3  1 
ATOM   2727 H HD1  . TYR   A 1 192 ? 1.010   -1.021  36.452  1.00 36.64  ? 177 TYR   A HD1  1 
ATOM   2728 H HD2  . TYR   A 1 192 ? -0.215  -3.100  33.264  1.00 37.03  ? 177 TYR   A HD2  1 
ATOM   2729 H HE1  . TYR   A 1 192 ? 0.066   0.892   35.577  1.00 37.75  ? 177 TYR   A HE1  1 
ATOM   2730 H HE2  . TYR   A 1 192 ? -1.151  -1.176  32.368  1.00 39.07  ? 177 TYR   A HE2  1 
ATOM   2731 H HH   . TYR   A 1 192 ? -1.068  1.842   33.879  1.00 42.26  ? 177 TYR   A HH   1 
ATOM   2732 N N    . TRP   A 1 193 ? 3.508   -5.754  35.400  1.00 31.40  ? 178 TRP   A N    1 
ATOM   2733 C CA   . TRP   A 1 193 ? 4.198   -6.915  35.955  1.00 31.78  ? 178 TRP   A CA   1 
ATOM   2734 C C    . TRP   A 1 193 ? 5.682   -6.924  35.629  1.00 36.16  ? 178 TRP   A C    1 
ATOM   2735 O O    . TRP   A 1 193 ? 6.354   -7.934  35.855  1.00 32.90  ? 178 TRP   A O    1 
ATOM   2736 C CB   . TRP   A 1 193 ? 3.573   -8.209  35.432  1.00 31.46  ? 178 TRP   A CB   1 
ATOM   2737 C CG   . TRP   A 1 193 ? 2.145   -8.424  35.838  1.00 30.78  ? 178 TRP   A CG   1 
ATOM   2738 C CD1  . TRP   A 1 193 ? 1.687   -9.221  36.848  1.00 30.58  ? 178 TRP   A CD1  1 
ATOM   2739 C CD2  . TRP   A 1 193 ? 0.990   -7.839  35.233  1.00 31.79  ? 178 TRP   A CD2  1 
ATOM   2740 N NE1  . TRP   A 1 193 ? 0.315   -9.166  36.910  1.00 29.85  ? 178 TRP   A NE1  1 
ATOM   2741 C CE2  . TRP   A 1 193 ? -0.139  -8.326  35.928  1.00 34.81  ? 178 TRP   A CE2  1 
ATOM   2742 C CE3  . TRP   A 1 193 ? 0.798   -6.947  34.170  1.00 33.11  ? 178 TRP   A CE3  1 
ATOM   2743 C CZ2  . TRP   A 1 193 ? -1.441  -7.947  35.598  1.00 35.23  ? 178 TRP   A CZ2  1 
ATOM   2744 C CZ3  . TRP   A 1 193 ? -0.499  -6.571  33.845  1.00 36.19  ? 178 TRP   A CZ3  1 
ATOM   2745 C CH2  . TRP   A 1 193 ? -1.599  -7.070  34.557  1.00 30.28  ? 178 TRP   A CH2  1 
ATOM   2746 H H    . TRP   A 1 193 ? 3.231   -5.866  34.594  1.00 37.68  ? 178 TRP   A H    1 
ATOM   2747 H HA   . TRP   A 1 193 ? 4.091   -6.892  36.919  1.00 38.14  ? 178 TRP   A HA   1 
ATOM   2748 H HB2  . TRP   A 1 193 ? 3.603   -8.196  34.462  1.00 37.75  ? 178 TRP   A HB2  1 
ATOM   2749 H HB3  . TRP   A 1 193 ? 4.089   -8.958  35.769  1.00 37.75  ? 178 TRP   A HB3  1 
ATOM   2750 H HD1  . TRP   A 1 193 ? 2.226   -9.729  37.411  1.00 36.69  ? 178 TRP   A HD1  1 
ATOM   2751 H HE1  . TRP   A 1 193 ? -0.178  -9.590  37.474  1.00 35.82  ? 178 TRP   A HE1  1 
ATOM   2752 H HE3  . TRP   A 1 193 ? 1.523   -6.613  33.693  1.00 39.73  ? 178 TRP   A HE3  1 
ATOM   2753 H HZ2  . TRP   A 1 193 ? -2.173  -8.278  36.066  1.00 42.28  ? 178 TRP   A HZ2  1 
ATOM   2754 H HZ3  . TRP   A 1 193 ? -0.640  -5.979  33.142  1.00 43.42  ? 178 TRP   A HZ3  1 
ATOM   2755 H HH2  . TRP   A 1 193 ? -2.456  -6.799  34.317  1.00 36.33  ? 178 TRP   A HH2  1 
ATOM   2756 N N    . MET   A 1 194 ? 6.201   -5.827  35.093  1.00 32.95  ? 179 MET   A N    1 
ATOM   2757 C CA   . MET   A 1 194 ? 7.536   -5.786  34.524  1.00 36.27  ? 179 MET   A CA   1 
ATOM   2758 C C    . MET   A 1 194 ? 8.565   -5.471  35.598  1.00 33.88  ? 179 MET   A C    1 
ATOM   2759 O O    . MET   A 1 194 ? 8.357   -4.595  36.440  1.00 35.01  ? 179 MET   A O    1 
ATOM   2760 C CB   . MET   A 1 194 ? 7.566   -4.726  33.420  1.00 37.26  ? 179 MET   A CB   1 
ATOM   2761 C CG   . MET   A 1 194 ? 8.662   -4.857  32.433  1.00 35.84  ? 179 MET   A CG   1 
ATOM   2762 S SD   . MET   A 1 194 ? 8.514   -3.615  31.115  1.00 40.90  ? 179 MET   A SD   1 
ATOM   2763 C CE   . MET   A 1 194 ? 7.274   -4.362  30.063  1.00 39.25  ? 179 MET   A CE   1 
ATOM   2764 H H    . MET   A 1 194 ? 5.787   -5.075  35.048  1.00 39.54  ? 179 MET   A H    1 
ATOM   2765 H HA   . MET   A 1 194 ? 7.766   -6.646  34.139  1.00 43.53  ? 179 MET   A HA   1 
ATOM   2766 H HB2  . MET   A 1 194 ? 6.730   -4.774  32.930  1.00 44.71  ? 179 MET   A HB2  1 
ATOM   2767 H HB3  . MET   A 1 194 ? 7.657   -3.855  33.837  1.00 44.71  ? 179 MET   A HB3  1 
ATOM   2768 H HG2  . MET   A 1 194 ? 9.514   -4.730  32.880  1.00 43.01  ? 179 MET   A HG2  1 
ATOM   2769 H HG3  . MET   A 1 194 ? 8.627   -5.738  32.029  1.00 43.01  ? 179 MET   A HG3  1 
ATOM   2770 H HE1  . MET   A 1 194 ? 6.929   -3.689  29.456  1.00 47.09  ? 179 MET   A HE1  1 
ATOM   2771 H HE2  . MET   A 1 194 ? 7.681   -5.085  29.560  1.00 47.09  ? 179 MET   A HE2  1 
ATOM   2772 H HE3  . MET   A 1 194 ? 6.556   -4.707  30.617  1.00 47.09  ? 179 MET   A HE3  1 
ATOM   2773 N N    . ALA   A 1 195 ? 9.680   -6.195  35.572  1.00 34.46  ? 180 ALA   A N    1 
ATOM   2774 C CA   . ALA   A 1 195 ? 10.756  -5.919  36.507  1.00 35.31  ? 180 ALA   A CA   1 
ATOM   2775 C C    . ALA   A 1 195 ? 11.482  -4.635  36.108  1.00 37.74  ? 180 ALA   A C    1 
ATOM   2776 O O    . ALA   A 1 195 ? 11.467  -4.240  34.943  1.00 36.07  ? 180 ALA   A O    1 
ATOM   2777 C CB   . ALA   A 1 195 ? 11.741  -7.078  36.549  1.00 35.94  ? 180 ALA   A CB   1 
ATOM   2778 H H    . ALA   A 1 195 ? 9.833   -6.843  35.028  1.00 41.36  ? 180 ALA   A H    1 
ATOM   2779 H HA   . ALA   A 1 195 ? 10.388  -5.804  37.397  1.00 42.37  ? 180 ALA   A HA   1 
ATOM   2780 H HB1  . ALA   A 1 195 ? 12.432  -6.881  37.200  1.00 43.13  ? 180 ALA   A HB1  1 
ATOM   2781 H HB2  . ALA   A 1 195 ? 11.267  -7.885  36.803  1.00 43.13  ? 180 ALA   A HB2  1 
ATOM   2782 H HB3  . ALA   A 1 195 ? 12.136  -7.189  35.670  1.00 43.13  ? 180 ALA   A HB3  1 
ATOM   2783 N N    . PRO   A 1 196 ? 12.129  -3.964  37.069  1.00 36.21  ? 181 PRO   A N    1 
ATOM   2784 C CA   . PRO   A 1 196 ? 12.787  -2.687  36.729  1.00 36.43  ? 181 PRO   A CA   1 
ATOM   2785 C C    . PRO   A 1 196 ? 13.777  -2.808  35.587  1.00 38.53  ? 181 PRO   A C    1 
ATOM   2786 O O    . PRO   A 1 196 ? 13.733  -1.998  34.651  1.00 36.76  ? 181 PRO   A O    1 
ATOM   2787 C CB   . PRO   A 1 196 ? 13.462  -2.287  38.051  1.00 37.40  ? 181 PRO   A CB   1 
ATOM   2788 C CG   . PRO   A 1 196 ? 12.629  -2.926  39.102  1.00 42.23  ? 181 PRO   A CG   1 
ATOM   2789 C CD   . PRO   A 1 196 ? 12.174  -4.242  38.515  1.00 40.19  ? 181 PRO   A CD   1 
ATOM   2790 H HA   . PRO   A 1 196 ? 12.118  -2.024  36.498  1.00 43.71  ? 181 PRO   A HA   1 
ATOM   2791 H HB2  . PRO   A 1 196 ? 14.371  -2.624  38.074  1.00 44.88  ? 181 PRO   A HB2  1 
ATOM   2792 H HB3  . PRO   A 1 196 ? 13.463  -1.322  38.144  1.00 44.88  ? 181 PRO   A HB3  1 
ATOM   2793 H HG2  . PRO   A 1 196 ? 13.161  -3.070  39.900  1.00 50.67  ? 181 PRO   A HG2  1 
ATOM   2794 H HG3  . PRO   A 1 196 ? 11.869  -2.359  39.308  1.00 50.67  ? 181 PRO   A HG3  1 
ATOM   2795 H HD2  . PRO   A 1 196 ? 12.810  -4.947  38.711  1.00 48.23  ? 181 PRO   A HD2  1 
ATOM   2796 H HD3  . PRO   A 1 196 ? 11.296  -4.485  38.848  1.00 48.23  ? 181 PRO   A HD3  1 
ATOM   2797 N N    . GLU   A 1 197 ? 14.657  -3.812  35.613  1.00 41.87  ? 182 GLU   A N    1 
ATOM   2798 C CA   . GLU   A 1 197 ? 15.658  -3.922  34.555  1.00 36.96  ? 182 GLU   A CA   1 
ATOM   2799 C C    . GLU   A 1 197 ? 15.013  -4.114  33.190  1.00 37.38  ? 182 GLU   A C    1 
ATOM   2800 O O    . GLU   A 1 197 ? 15.549  -3.641  32.180  1.00 40.32  ? 182 GLU   A O    1 
ATOM   2801 C CB   . GLU   A 1 197 ? 16.635  -5.063  34.855  1.00 40.60  ? 182 GLU   A CB   1 
ATOM   2802 C CG   . GLU   A 1 197 ? 16.057  -6.477  34.825  1.00 44.87  ? 182 GLU   A CG   1 
ATOM   2803 C CD   . GLU   A 1 197 ? 15.432  -6.886  36.140  1.00 40.57  ? 182 GLU   A CD   1 
ATOM   2804 O OE1  . GLU   A 1 197 ? 14.983  -5.993  36.884  1.00 47.50  ? 182 GLU   A OE1  1 
ATOM   2805 O OE2  . GLU   A 1 197 ? 15.406  -8.100  36.437  1.00 38.14  ? 182 GLU   A OE2  1 
ATOM   2806 H H    . GLU   A 1 197 ? 14.694  -4.425  36.215  1.00 50.24  ? 182 GLU   A H    1 
ATOM   2807 H HA   . GLU   A 1 197 ? 16.171  -3.099  34.530  1.00 44.35  ? 182 GLU   A HA   1 
ATOM   2808 H HB2  . GLU   A 1 197 ? 17.346  -5.033  34.196  1.00 48.72  ? 182 GLU   A HB2  1 
ATOM   2809 H HB3  . GLU   A 1 197 ? 16.999  -4.923  35.743  1.00 48.72  ? 182 GLU   A HB3  1 
ATOM   2810 H HG2  . GLU   A 1 197 ? 15.370  -6.522  34.141  1.00 53.84  ? 182 GLU   A HG2  1 
ATOM   2811 H HG3  . GLU   A 1 197 ? 16.768  -7.104  34.624  1.00 53.84  ? 182 GLU   A HG3  1 
ATOM   2812 N N    . VAL   A 1 198 ? 13.869  -4.801  33.129  1.00 37.64  ? 183 VAL   A N    1 
ATOM   2813 C CA   . VAL   A 1 198 ? 13.158  -4.915  31.859  1.00 39.15  ? 183 VAL   A CA   1 
ATOM   2814 C C    . VAL   A 1 198 ? 12.609  -3.557  31.447  1.00 36.13  ? 183 VAL   A C    1 
ATOM   2815 O O    . VAL   A 1 198 ? 12.677  -3.169  30.275  1.00 38.22  ? 183 VAL   A O    1 
ATOM   2816 C CB   . VAL   A 1 198 ? 12.039  -5.969  31.962  1.00 40.67  ? 183 VAL   A CB   1 
ATOM   2817 C CG1  . VAL   A 1 198 ? 11.358  -6.164  30.613  1.00 41.86  ? 183 VAL   A CG1  1 
ATOM   2818 C CG2  . VAL   A 1 198 ? 12.595  -7.284  32.472  1.00 43.63  ? 183 VAL   A CG2  1 
ATOM   2819 H H    . VAL   A 1 198 ? 13.495  -5.199  33.793  1.00 45.17  ? 183 VAL   A H    1 
ATOM   2820 H HA   . VAL   A 1 198 ? 13.782  -5.212  31.179  1.00 46.98  ? 183 VAL   A HA   1 
ATOM   2821 H HB   . VAL   A 1 198 ? 11.372  -5.655  32.592  1.00 48.80  ? 183 VAL   A HB   1 
ATOM   2822 H HG11 . VAL   A 1 198 ? 10.746  -6.914  30.674  1.00 50.24  ? 183 VAL   A HG11 1 
ATOM   2823 H HG12 . VAL   A 1 198 ? 10.871  -5.357  30.385  1.00 50.24  ? 183 VAL   A HG12 1 
ATOM   2824 H HG13 . VAL   A 1 198 ? 12.034  -6.343  29.941  1.00 50.24  ? 183 VAL   A HG13 1 
ATOM   2825 H HG21 . VAL   A 1 198 ? 11.916  -7.970  32.380  1.00 52.36  ? 183 VAL   A HG21 1 
ATOM   2826 H HG22 . VAL   A 1 198 ? 13.377  -7.520  31.949  1.00 52.36  ? 183 VAL   A HG22 1 
ATOM   2827 H HG23 . VAL   A 1 198 ? 12.839  -7.182  33.405  1.00 52.36  ? 183 VAL   A HG23 1 
ATOM   2828 N N    . ALA   A 1 199 ? 12.065  -2.807  32.408  1.00 39.11  ? 184 ALA   A N    1 
ATOM   2829 C CA   . ALA   A 1 199 ? 11.570  -1.471  32.104  1.00 39.26  ? 184 ALA   A CA   1 
ATOM   2830 C C    . ALA   A 1 199 ? 12.671  -0.602  31.515  1.00 34.28  ? 184 ALA   A C    1 
ATOM   2831 O O    . ALA   A 1 199 ? 12.419  0.206   30.616  1.00 35.95  ? 184 ALA   A O    1 
ATOM   2832 C CB   . ALA   A 1 199 ? 10.994  -0.829  33.363  1.00 34.32  ? 184 ALA   A CB   1 
ATOM   2833 H H    . ALA   A 1 199 ? 11.974  -3.047  33.229  1.00 46.93  ? 184 ALA   A H    1 
ATOM   2834 H HA   . ALA   A 1 199 ? 10.857  -1.538  31.450  1.00 47.12  ? 184 ALA   A HA   1 
ATOM   2835 H HB1  . ALA   A 1 199 ? 10.669  0.058   33.145  1.00 41.18  ? 184 ALA   A HB1  1 
ATOM   2836 H HB2  . ALA   A 1 199 ? 10.264  -1.378  33.691  1.00 41.18  ? 184 ALA   A HB2  1 
ATOM   2837 H HB3  . ALA   A 1 199 ? 11.691  -0.771  34.035  1.00 41.18  ? 184 ALA   A HB3  1 
ATOM   2838 N N    . ALA   A 1 200 ? 13.902  -0.762  32.004  1.00 39.85  ? 185 ALA   A N    1 
ATOM   2839 C CA   . ALA   A 1 200 ? 15.014  0.013   31.470  1.00 39.28  ? 185 ALA   A CA   1 
ATOM   2840 C C    . ALA   A 1 200 ? 15.225  -0.294  29.994  1.00 40.79  ? 185 ALA   A C    1 
ATOM   2841 O O    . ALA   A 1 200 ? 15.402  0.620   29.178  1.00 40.54  ? 185 ALA   A O    1 
ATOM   2842 C CB   . ALA   A 1 200 ? 16.280  -0.275  32.276  1.00 37.30  ? 185 ALA   A CB   1 
ATOM   2843 H H    . ALA   A 1 200 ? 14.115  -1.306  32.636  1.00 47.81  ? 185 ALA   A H    1 
ATOM   2844 H HA   . ALA   A 1 200 ? 14.819  0.959   31.554  1.00 47.14  ? 185 ALA   A HA   1 
ATOM   2845 H HB1  . ALA   A 1 200 ? 17.013  0.243   31.909  1.00 44.76  ? 185 ALA   A HB1  1 
ATOM   2846 H HB2  . ALA   A 1 200 ? 16.129  -0.026  33.201  1.00 44.76  ? 185 ALA   A HB2  1 
ATOM   2847 H HB3  . ALA   A 1 200 ? 16.483  -1.222  32.218  1.00 44.76  ? 185 ALA   A HB3  1 
ATOM   2848 N N    . VAL   A 1 201 ? 15.178  -1.576  29.626  1.00 39.56  ? 186 VAL   A N    1 
ATOM   2849 C CA   . VAL   A 1 201 ? 15.366  -1.939  28.225  1.00 44.23  ? 186 VAL   A CA   1 
ATOM   2850 C C    . VAL   A 1 201 ? 14.203  -1.427  27.381  1.00 45.67  ? 186 VAL   A C    1 
ATOM   2851 O O    . VAL   A 1 201 ? 14.405  -0.898  26.281  1.00 43.31  ? 186 VAL   A O    1 
ATOM   2852 C CB   . VAL   A 1 201 ? 15.552  -3.460  28.092  1.00 47.56  ? 186 VAL   A CB   1 
ATOM   2853 C CG1  . VAL   A 1 201 ? 15.760  -3.846  26.636  1.00 47.90  ? 186 VAL   A CG1  1 
ATOM   2854 C CG2  . VAL   A 1 201 ? 16.733  -3.920  28.938  1.00 53.26  ? 186 VAL   A CG2  1 
ATOM   2855 H H    . VAL   A 1 201 ? 15.042  -2.239  30.157  1.00 47.48  ? 186 VAL   A H    1 
ATOM   2856 H HA   . VAL   A 1 201 ? 16.174  -1.513  27.898  1.00 53.08  ? 186 VAL   A HA   1 
ATOM   2857 H HB   . VAL   A 1 201 ? 14.751  -3.906  28.410  1.00 57.08  ? 186 VAL   A HB   1 
ATOM   2858 H HG11 . VAL   A 1 201 ? 16.237  -4.690  26.598  1.00 57.48  ? 186 VAL   A HG11 1 
ATOM   2859 H HG12 . VAL   A 1 201 ? 14.896  -3.935  26.206  1.00 57.48  ? 186 VAL   A HG12 1 
ATOM   2860 H HG13 . VAL   A 1 201 ? 16.279  -3.154  26.197  1.00 57.48  ? 186 VAL   A HG13 1 
ATOM   2861 H HG21 . VAL   A 1 201 ? 16.872  -4.869  28.797  1.00 63.92  ? 186 VAL   A HG21 1 
ATOM   2862 H HG22 . VAL   A 1 201 ? 17.524  -3.426  28.671  1.00 63.92  ? 186 VAL   A HG22 1 
ATOM   2863 H HG23 . VAL   A 1 201 ? 16.537  -3.749  29.873  1.00 63.92  ? 186 VAL   A HG23 1 
ATOM   2864 N N    . ALA   A 1 202 ? 12.973  -1.542  27.891  1.00 41.78  ? 187 ALA   A N    1 
ATOM   2865 C CA   . ALA   A 1 202 ? 11.819  -1.070  27.133  1.00 39.95  ? 187 ALA   A CA   1 
ATOM   2866 C C    . ALA   A 1 202 ? 11.910  0.416   26.811  1.00 43.30  ? 187 ALA   A C    1 
ATOM   2867 O O    . ALA   A 1 202 ? 11.265  0.874   25.863  1.00 41.55  ? 187 ALA   A O    1 
ATOM   2868 C CB   . ALA   A 1 202 ? 10.527  -1.337  27.899  1.00 40.79  ? 187 ALA   A CB   1 
ATOM   2869 H H    . ALA   A 1 202 ? 12.786  -1.884  28.657  1.00 50.14  ? 187 ALA   A H    1 
ATOM   2870 H HA   . ALA   A 1 202 ? 11.785  -1.566  26.301  1.00 47.94  ? 187 ALA   A HA   1 
ATOM   2871 H HB1  . ALA   A 1 202 ? 9.772   -1.121  27.329  1.00 48.95  ? 187 ALA   A HB1  1 
ATOM   2872 H HB2  . ALA   A 1 202 ? 10.496  -2.274  28.148  1.00 48.95  ? 187 ALA   A HB2  1 
ATOM   2873 H HB3  . ALA   A 1 202 ? 10.511  -0.783  28.694  1.00 48.95  ? 187 ALA   A HB3  1 
ATOM   2874 N N    . LEU   A 1 203 ? 12.672  1.182   27.584  1.00 40.96  ? 188 LEU   A N    1 
ATOM   2875 C CA   . LEU   A 1 203 ? 12.930  2.580   27.266  1.00 44.03  ? 188 LEU   A CA   1 
ATOM   2876 C C    . LEU   A 1 203 ? 14.230  2.759   26.482  1.00 46.15  ? 188 LEU   A C    1 
ATOM   2877 O O    . LEU   A 1 203 ? 14.713  3.887   26.355  1.00 44.00  ? 188 LEU   A O    1 
ATOM   2878 C CB   . LEU   A 1 203 ? 12.951  3.413   28.551  1.00 43.92  ? 188 LEU   A CB   1 
ATOM   2879 C CG   . LEU   A 1 203 ? 11.648  3.452   29.361  1.00 44.00  ? 188 LEU   A CG   1 
ATOM   2880 C CD1  . LEU   A 1 203 ? 11.838  4.242   30.653  1.00 39.76  ? 188 LEU   A CD1  1 
ATOM   2881 C CD2  . LEU   A 1 203 ? 10.495  4.044   28.558  1.00 41.13  ? 188 LEU   A CD2  1 
ATOM   2882 H H    . LEU   A 1 203 ? 13.055  0.911   28.305  1.00 49.16  ? 188 LEU   A H    1 
ATOM   2883 H HA   . LEU   A 1 203 ? 12.208  2.924   26.718  1.00 52.84  ? 188 LEU   A HA   1 
ATOM   2884 H HB2  . LEU   A 1 203 ? 13.638  3.051   29.132  1.00 52.70  ? 188 LEU   A HB2  1 
ATOM   2885 H HB3  . LEU   A 1 203 ? 13.167  4.328   28.312  1.00 52.70  ? 188 LEU   A HB3  1 
ATOM   2886 H HG   . LEU   A 1 203 ? 11.413  2.537   29.583  1.00 52.80  ? 188 LEU   A HG   1 
ATOM   2887 H HD11 . LEU   A 1 203 ? 11.001  4.251   31.144  1.00 47.71  ? 188 LEU   A HD11 1 
ATOM   2888 H HD12 . LEU   A 1 203 ? 12.529  3.817   31.185  1.00 47.71  ? 188 LEU   A HD12 1 
ATOM   2889 H HD13 . LEU   A 1 203 ? 12.102  5.149   30.433  1.00 47.71  ? 188 LEU   A HD13 1 
ATOM   2890 H HD21 . LEU   A 1 203 ? 9.724   4.142   29.137  1.00 49.35  ? 188 LEU   A HD21 1 
ATOM   2891 H HD22 . LEU   A 1 203 ? 10.762  4.911   28.214  1.00 49.35  ? 188 LEU   A HD22 1 
ATOM   2892 H HD23 . LEU   A 1 203 ? 10.283  3.448   27.823  1.00 49.35  ? 188 LEU   A HD23 1 
ATOM   2893 N N    . LYS   A 1 204 ? 14.809  1.667   25.976  1.00 55.75  ? 189 LYS   A N    1 
ATOM   2894 C CA   . LYS   A 1 204 ? 15.924  1.684   25.029  1.00 58.14  ? 189 LYS   A CA   1 
ATOM   2895 C C    . LYS   A 1 204 ? 17.251  2.020   25.704  1.00 59.82  ? 189 LYS   A C    1 
ATOM   2896 O O    . LYS   A 1 204 ? 18.061  2.788   25.167  1.00 62.70  ? 189 LYS   A O    1 
ATOM   2897 C CB   . LYS   A 1 204 ? 15.638  2.652   23.870  1.00 60.46  ? 189 LYS   A CB   1 
ATOM   2898 C CG   . LYS   A 1 204 ? 14.420  2.252   23.029  1.00 58.72  ? 189 LYS   A CG   1 
ATOM   2899 C CD   . LYS   A 1 204 ? 14.146  3.241   21.897  1.00 59.00  ? 189 LYS   A CD   1 
ATOM   2900 C CE   . LYS   A 1 204 ? 13.832  4.634   22.430  1.00 65.85  ? 189 LYS   A CE   1 
ATOM   2901 N NZ   . LYS   A 1 204 ? 13.673  5.637   21.338  1.00 76.84  ? 189 LYS   A NZ   1 
ATOM   2902 H H    . LYS   A 1 204 ? 14.563  0.868   26.175  1.00 66.90  ? 189 LYS   A H    1 
ATOM   2903 H HA   . LYS   A 1 204 ? 16.017  0.792   24.659  1.00 69.77  ? 189 LYS   A HA   1 
ATOM   2904 H HB2  . LYS   A 1 204 ? 15.471  3.536   24.234  1.00 72.55  ? 189 LYS   A HB2  1 
ATOM   2905 H HB3  . LYS   A 1 204 ? 16.410  2.675   23.284  1.00 72.55  ? 189 LYS   A HB3  1 
ATOM   2906 H HG2  . LYS   A 1 204 ? 14.578  1.380   22.636  1.00 70.46  ? 189 LYS   A HG2  1 
ATOM   2907 H HG3  . LYS   A 1 204 ? 13.636  2.222   23.600  1.00 70.46  ? 189 LYS   A HG3  1 
ATOM   2908 H HD2  . LYS   A 1 204 ? 14.929  3.302   21.327  1.00 70.80  ? 189 LYS   A HD2  1 
ATOM   2909 H HD3  . LYS   A 1 204 ? 13.384  2.934   21.381  1.00 70.80  ? 189 LYS   A HD3  1 
ATOM   2910 H HE2  . LYS   A 1 204 ? 13.004  4.603   22.933  1.00 79.02  ? 189 LYS   A HE2  1 
ATOM   2911 H HE3  . LYS   A 1 204 ? 14.559  4.925   23.003  1.00 79.02  ? 189 LYS   A HE3  1 
ATOM   2912 H HZ1  . LYS   A 1 204 ? 13.497  6.438   21.684  1.00 92.20  ? 189 LYS   A HZ1  1 
ATOM   2913 H HZ2  . LYS   A 1 204 ? 14.421  5.688   20.859  1.00 92.20  ? 189 LYS   A HZ2  1 
ATOM   2914 H HZ3  . LYS   A 1 204 ? 13.003  5.400   20.802  1.00 92.20  ? 189 LYS   A HZ3  1 
ATOM   2915 N N    . GLY   A 1 205 ? 17.494  1.427   26.869  1.00 46.08  ? 190 GLY   A N    1 
ATOM   2916 C CA   . GLY   A 1 205 ? 18.803  1.434   27.490  1.00 34.17  ? 190 GLY   A CA   1 
ATOM   2917 C C    . GLY   A 1 205 ? 19.590  0.184   27.141  1.00 50.63  ? 190 GLY   A C    1 
ATOM   2918 O O    . GLY   A 1 205 ? 19.218  -0.609  26.274  1.00 49.85  ? 190 GLY   A O    1 
ATOM   2919 H H    . GLY   A 1 205 ? 16.899  1.005   27.326  1.00 55.30  ? 190 GLY   A H    1 
ATOM   2920 H HA2  . GLY   A 1 205 ? 19.301  2.209   27.186  1.00 41.00  ? 190 GLY   A HA2  1 
ATOM   2921 H HA3  . GLY   A 1 205 ? 18.705  1.480   28.454  1.00 41.00  ? 190 GLY   A HA3  1 
ATOM   2922 N N    . GLY   A 1 206 ? 20.712  0.014   27.840  1.00 61.35  ? 191 GLY   A N    1 
ATOM   2923 C CA   . GLY   A 1 206 ? 21.535  -1.171  27.688  1.00 55.85  ? 191 GLY   A CA   1 
ATOM   2924 C C    . GLY   A 1 206 ? 22.634  -1.074  26.655  1.00 56.73  ? 191 GLY   A C    1 
ATOM   2925 O O    . GLY   A 1 206 ? 23.270  -2.093  26.353  1.00 49.58  ? 191 GLY   A O    1 
ATOM   2926 H H    . GLY   A 1 206 ? 21.016  0.578   28.413  1.00 73.62  ? 191 GLY   A H    1 
ATOM   2927 H HA2  . GLY   A 1 206 ? 21.952  -1.368  28.541  1.00 67.02  ? 191 GLY   A HA2  1 
ATOM   2928 H HA3  . GLY   A 1 206 ? 20.963  -1.913  27.437  1.00 67.02  ? 191 GLY   A HA3  1 
ATOM   2929 N N    . TYR   A 1 207 ? 22.878  0.113   26.107  1.00 54.42  ? 192 TYR   A N    1 
ATOM   2930 C CA   . TYR   A 1 207 ? 23.930  0.328   25.121  1.00 55.10  ? 192 TYR   A CA   1 
ATOM   2931 C C    . TYR   A 1 207 ? 24.167  1.829   25.024  1.00 48.05  ? 192 TYR   A C    1 
ATOM   2932 O O    . TYR   A 1 207 ? 23.378  2.630   25.533  1.00 47.77  ? 192 TYR   A O    1 
ATOM   2933 C CB   . TYR   A 1 207 ? 23.556  -0.274  23.766  1.00 48.22  ? 192 TYR   A CB   1 
ATOM   2934 C CG   . TYR   A 1 207 ? 22.251  0.239   23.205  1.00 51.25  ? 192 TYR   A CG   1 
ATOM   2935 C CD1  . TYR   A 1 207 ? 22.208  1.403   22.447  1.00 41.08  ? 192 TYR   A CD1  1 
ATOM   2936 C CD2  . TYR   A 1 207 ? 21.061  -0.441  23.430  1.00 46.46  ? 192 TYR   A CD2  1 
ATOM   2937 C CE1  . TYR   A 1 207 ? 21.010  1.873   21.925  1.00 47.71  ? 192 TYR   A CE1  1 
ATOM   2938 C CE2  . TYR   A 1 207 ? 19.864  0.023   22.913  1.00 46.87  ? 192 TYR   A CE2  1 
ATOM   2939 C CZ   . TYR   A 1 207 ? 19.848  1.178   22.162  1.00 37.58  ? 192 TYR   A CZ   1 
ATOM   2940 O OH   . TYR   A 1 207 ? 18.665  1.638   21.645  1.00 49.35  ? 192 TYR   A OH   1 
ATOM   2941 H H    . TYR   A 1 207 ? 22.437  0.827   26.295  1.00 65.30  ? 192 TYR   A H    1 
ATOM   2942 H HA   . TYR   A 1 207 ? 24.752  -0.096  25.411  1.00 66.12  ? 192 TYR   A HA   1 
ATOM   2943 H HB2  . TYR   A 1 207 ? 24.255  -0.062  23.128  1.00 57.86  ? 192 TYR   A HB2  1 
ATOM   2944 H HB3  . TYR   A 1 207 ? 23.477  -1.236  23.865  1.00 57.86  ? 192 TYR   A HB3  1 
ATOM   2945 H HD1  . TYR   A 1 207 ? 22.993  1.874   22.286  1.00 49.30  ? 192 TYR   A HD1  1 
ATOM   2946 H HD2  . TYR   A 1 207 ? 21.069  -1.222  23.936  1.00 55.76  ? 192 TYR   A HD2  1 
ATOM   2947 H HE1  . TYR   A 1 207 ? 20.994  2.653   21.419  1.00 57.25  ? 192 TYR   A HE1  1 
ATOM   2948 H HE2  . TYR   A 1 207 ? 19.074  -0.442  23.073  1.00 56.24  ? 192 TYR   A HE2  1 
ATOM   2949 H HH   . TYR   A 1 207 ? 18.038  1.120   21.856  1.00 59.22  ? 192 TYR   A HH   1 
ATOM   2950 N N    . ASN   A 1 208 ? 25.260  2.202   24.362  1.00 38.57  ? 193 ASN   A N    1 
ATOM   2951 C CA   . ASN   A 1 208 ? 25.768  3.563   24.411  1.00 41.95  ? 193 ASN   A CA   1 
ATOM   2952 C C    . ASN   A 1 208 ? 25.793  4.199   23.021  1.00 36.96  ? 193 ASN   A C    1 
ATOM   2953 O O    . ASN   A 1 208 ? 25.375  3.611   22.021  1.00 37.94  ? 193 ASN   A O    1 
ATOM   2954 C CB   . ASN   A 1 208 ? 27.166  3.594   25.040  1.00 45.59  ? 193 ASN   A CB   1 
ATOM   2955 C CG   . ASN   A 1 208 ? 28.236  2.991   24.136  1.00 49.82  ? 193 ASN   A CG   1 
ATOM   2956 O OD1  . ASN   A 1 208 ? 27.959  2.553   23.018  1.00 55.87  ? 193 ASN   A OD1  1 
ATOM   2957 N ND2  . ASN   A 1 208 ? 29.471  2.985   24.616  1.00 52.86  ? 193 ASN   A ND2  1 
ATOM   2958 H H    . ASN   A 1 208 ? 25.728  1.673   23.871  1.00 46.29  ? 193 ASN   A H    1 
ATOM   2959 H HA   . ASN   A 1 208 ? 25.159  4.087   24.955  1.00 50.33  ? 193 ASN   A HA   1 
ATOM   2960 H HB2  . ASN   A 1 208 ? 27.411  4.515   25.221  1.00 54.71  ? 193 ASN   A HB2  1 
ATOM   2961 H HB3  . ASN   A 1 208 ? 27.151  3.086   25.867  1.00 54.71  ? 193 ASN   A HB3  1 
ATOM   2962 H HD21 . ASN   A 1 208 ? 30.113  2.657   24.147  1.00 63.43  ? 193 ASN   A HD21 1 
ATOM   2963 H HD22 . ASN   A 1 208 ? 29.631  3.310   25.396  1.00 63.43  ? 193 ASN   A HD22 1 
ATOM   2964 N N    . GLU   A 1 209 ? 26.326  5.417   22.974  1.00 32.22  ? 194 GLU   A N    1 
ATOM   2965 C CA   . GLU   A 1 209 ? 26.204  6.252   21.787  1.00 31.24  ? 194 GLU   A CA   1 
ATOM   2966 C C    . GLU   A 1 209 ? 27.058  5.766   20.622  1.00 30.43  ? 194 GLU   A C    1 
ATOM   2967 O O    . GLU   A 1 209 ? 26.824  6.188   19.481  1.00 29.52  ? 194 GLU   A O    1 
ATOM   2968 C CB   . GLU   A 1 209 ? 26.564  7.700   22.142  1.00 31.74  ? 194 GLU   A CB   1 
ATOM   2969 C CG   . GLU   A 1 209 ? 28.043  7.964   22.353  1.00 33.88  ? 194 GLU   A CG   1 
ATOM   2970 C CD   . GLU   A 1 209 ? 28.501  7.728   23.765  1.00 42.87  ? 194 GLU   A CD   1 
ATOM   2971 O OE1  . GLU   A 1 209 ? 27.782  7.064   24.538  1.00 47.67  ? 194 GLU   A OE1  1 
ATOM   2972 O OE2  . GLU   A 1 209 ? 29.596  8.220   24.102  1.00 59.63  ? 194 GLU   A OE2  1 
ATOM   2973 H H    . GLU   A 1 209 ? 26.763  5.783   23.617  1.00 38.67  ? 194 GLU   A H    1 
ATOM   2974 H HA   . GLU   A 1 209 ? 25.281  6.229   21.487  1.00 37.48  ? 194 GLU   A HA   1 
ATOM   2975 H HB2  . GLU   A 1 209 ? 26.267  8.276   21.420  1.00 38.09  ? 194 GLU   A HB2  1 
ATOM   2976 H HB3  . GLU   A 1 209 ? 26.107  7.937   22.964  1.00 38.09  ? 194 GLU   A HB3  1 
ATOM   2977 H HG2  . GLU   A 1 209 ? 28.552  7.374   21.774  1.00 40.66  ? 194 GLU   A HG2  1 
ATOM   2978 H HG3  . GLU   A 1 209 ? 28.231  8.889   22.131  1.00 40.66  ? 194 GLU   A HG3  1 
ATOM   2979 N N    . LEU   A 1 210 ? 28.040  4.900   20.870  1.00 30.78  ? 195 LEU   A N    1 
ATOM   2980 C CA   . LEU   A 1 210 ? 28.871  4.411   19.777  1.00 31.69  ? 195 LEU   A CA   1 
ATOM   2981 C C    . LEU   A 1 210 ? 28.115  3.486   18.829  1.00 29.43  ? 195 LEU   A C    1 
ATOM   2982 O O    . LEU   A 1 210 ? 28.639  3.165   17.755  1.00 28.69  ? 195 LEU   A O    1 
ATOM   2983 C CB   . LEU   A 1 210 ? 30.111  3.720   20.347  1.00 32.88  ? 195 LEU   A CB   1 
ATOM   2984 C CG   . LEU   A 1 210 ? 31.103  4.695   20.995  1.00 31.13  ? 195 LEU   A CG   1 
ATOM   2985 C CD1  . LEU   A 1 210 ? 32.207  3.961   21.720  1.00 33.52  ? 195 LEU   A CD1  1 
ATOM   2986 C CD2  . LEU   A 1 210 ? 31.706  5.649   19.959  1.00 31.24  ? 195 LEU   A CD2  1 
ATOM   2987 H H    . LEU   A 1 210 ? 28.239  4.588   21.647  1.00 36.93  ? 195 LEU   A H    1 
ATOM   2988 H HA   . LEU   A 1 210 ? 29.179  5.162   19.245  1.00 38.03  ? 195 LEU   A HA   1 
ATOM   2989 H HB2  . LEU   A 1 210 ? 29.832  3.083   21.024  1.00 39.45  ? 195 LEU   A HB2  1 
ATOM   2990 H HB3  . LEU   A 1 210 ? 30.572  3.259   19.628  1.00 39.45  ? 195 LEU   A HB3  1 
ATOM   2991 H HG   . LEU   A 1 210 ? 30.611  5.222   21.644  1.00 37.35  ? 195 LEU   A HG   1 
ATOM   2992 H HD11 . LEU   A 1 210 ? 32.803  4.609   22.126  1.00 40.23  ? 195 LEU   A HD11 1 
ATOM   2993 H HD12 . LEU   A 1 210 ? 31.814  3.398   22.405  1.00 40.23  ? 195 LEU   A HD12 1 
ATOM   2994 H HD13 . LEU   A 1 210 ? 32.695  3.416   21.083  1.00 40.23  ? 195 LEU   A HD13 1 
ATOM   2995 H HD21 . LEU   A 1 210 ? 32.479  6.088   20.346  1.00 37.48  ? 195 LEU   A HD21 1 
ATOM   2996 H HD22 . LEU   A 1 210 ? 31.972  5.139   19.177  1.00 37.48  ? 195 LEU   A HD22 1 
ATOM   2997 H HD23 . LEU   A 1 210 ? 31.040  6.309   19.712  1.00 37.48  ? 195 LEU   A HD23 1 
ATOM   2998 N N    . CYS   A 1 211 ? 26.891  3.076   19.179  1.00 30.66  ? 196 CYS   A N    1 
ATOM   2999 C CA   . CYS   A 1 211 ? 26.067  2.331   18.231  1.00 29.83  ? 196 CYS   A CA   1 
ATOM   3000 C C    . CYS   A 1 211 ? 25.725  3.172   17.005  1.00 28.27  ? 196 CYS   A C    1 
ATOM   3001 O O    . CYS   A 1 211 ? 25.549  2.626   15.909  1.00 27.69  ? 196 CYS   A O    1 
ATOM   3002 C CB   . CYS   A 1 211 ? 24.787  1.846   18.917  1.00 33.81  ? 196 CYS   A CB   1 
ATOM   3003 S SG   . CYS   A 1 211 ? 23.539  3.136   19.186  1.00 39.75  ? 196 CYS   A SG   1 
ATOM   3004 H H    . CYS   A 1 211 ? 26.523  3.215   19.944  1.00 36.79  ? 196 CYS   A H    1 
ATOM   3005 H HA   . CYS   A 1 211 ? 26.562  1.552   17.933  1.00 35.80  ? 196 CYS   A HA   1 
ATOM   3006 H HB2  . CYS   A 1 211 ? 24.383  1.159   18.365  1.00 40.57  ? 196 CYS   A HB2  1 
ATOM   3007 H HB3  . CYS   A 1 211 ? 25.021  1.480   19.784  1.00 40.57  ? 196 CYS   A HB3  1 
ATOM   3008 H HG   . CYS   A 1 211 ? 22.578  2.645   19.711  1.00 47.70  ? 196 CYS   A HG   1 
ATOM   3009 N N    . ASP   A 1 212 ? 25.613  4.494   17.174  1.00 28.16  ? 197 ASP   A N    1 
ATOM   3010 C CA   . ASP   A 1 212 ? 25.342  5.379   16.045  1.00 27.30  ? 197 ASP   A CA   1 
ATOM   3011 C C    . ASP   A 1 212 ? 26.485  5.372   15.027  1.00 26.47  ? 197 ASP   A C    1 
ATOM   3012 O O    . ASP   A 1 212 ? 26.252  5.560   13.828  1.00 25.68  ? 197 ASP   A O    1 
ATOM   3013 C CB   . ASP   A 1 212 ? 25.114  6.820   16.534  1.00 27.46  ? 197 ASP   A CB   1 
ATOM   3014 C CG   . ASP   A 1 212 ? 23.807  7.001   17.329  1.00 28.10  ? 197 ASP   A CG   1 
ATOM   3015 O OD1  . ASP   A 1 212 ? 22.827  6.258   17.104  1.00 28.13  ? 197 ASP   A OD1  1 
ATOM   3016 O OD2  . ASP   A 1 212 ? 23.762  7.933   18.165  1.00 28.58  ? 197 ASP   A OD2  1 
ATOM   3017 H H    . ASP   A 1 212 ? 25.690  4.899   17.928  1.00 33.79  ? 197 ASP   A H    1 
ATOM   3018 H HA   . ASP   A 1 212 ? 24.534  5.066   15.609  1.00 32.76  ? 197 ASP   A HA   1 
ATOM   3019 H HB2  . ASP   A 1 212 ? 25.850  7.074   17.113  1.00 32.95  ? 197 ASP   A HB2  1 
ATOM   3020 H HB3  . ASP   A 1 212 ? 25.077  7.409   15.765  1.00 32.95  ? 197 ASP   A HB3  1 
ATOM   3021 N N    . ILE   A 1 213 ? 27.723  5.184   15.488  1.00 26.67  ? 198 ILE   A N    1 
ATOM   3022 C CA   . ILE   A 1 213 ? 28.863  5.151   14.574  1.00 25.86  ? 198 ILE   A CA   1 
ATOM   3023 C C    . ILE   A 1 213 ? 28.790  3.916   13.681  1.00 25.50  ? 198 ILE   A C    1 
ATOM   3024 O O    . ILE   A 1 213 ? 28.949  4.003   12.458  1.00 24.58  ? 198 ILE   A O    1 
ATOM   3025 C CB   . ILE   A 1 213 ? 30.181  5.208   15.367  1.00 26.30  ? 198 ILE   A CB   1 
ATOM   3026 C CG1  . ILE   A 1 213 ? 30.299  6.535   16.134  1.00 26.66  ? 198 ILE   A CG1  1 
ATOM   3027 C CG2  . ILE   A 1 213 ? 31.367  5.039   14.451  1.00 25.46  ? 198 ILE   A CG2  1 
ATOM   3028 C CD1  . ILE   A 1 213 ? 30.182  7.767   15.286  1.00 29.17  ? 198 ILE   A CD1  1 
ATOM   3029 H H    . ILE   A 1 213 ? 27.927  5.073   16.316  1.00 32.00  ? 198 ILE   A H    1 
ATOM   3030 H HA   . ILE   A 1 213 ? 28.826  5.932   14.000  1.00 31.04  ? 198 ILE   A HA   1 
ATOM   3031 H HB   . ILE   A 1 213 ? 30.170  4.477   16.004  1.00 31.56  ? 198 ILE   A HB   1 
ATOM   3032 H HG12 . ILE   A 1 213 ? 29.592  6.570   16.798  1.00 31.99  ? 198 ILE   A HG12 1 
ATOM   3033 H HG13 . ILE   A 1 213 ? 31.165  6.562   16.570  1.00 31.99  ? 198 ILE   A HG13 1 
ATOM   3034 H HG21 . ILE   A 1 213 ? 32.169  5.320   14.918  1.00 30.56  ? 198 ILE   A HG21 1 
ATOM   3035 H HG22 . ILE   A 1 213 ? 31.441  4.105   14.200  1.00 30.56  ? 198 ILE   A HG22 1 
ATOM   3036 H HG23 . ILE   A 1 213 ? 31.236  5.585   13.660  1.00 30.56  ? 198 ILE   A HG23 1 
ATOM   3037 H HD11 . ILE   A 1 213 ? 30.444  8.539   15.813  1.00 35.00  ? 198 ILE   A HD11 1 
ATOM   3038 H HD12 . ILE   A 1 213 ? 30.766  7.678   14.517  1.00 35.00  ? 198 ILE   A HD12 1 
ATOM   3039 H HD13 . ILE   A 1 213 ? 29.262  7.863   14.993  1.00 35.00  ? 198 ILE   A HD13 1 
ATOM   3040 N N    . TRP   A 1 214 ? 28.534  2.747   14.276  1.00 26.25  ? 199 TRP   A N    1 
ATOM   3041 C CA   . TRP   A 1 214 ? 28.320  1.544   13.476  1.00 26.06  ? 199 TRP   A CA   1 
ATOM   3042 C C    . TRP   A 1 214 ? 27.187  1.762   12.483  1.00 25.53  ? 199 TRP   A C    1 
ATOM   3043 O O    . TRP   A 1 214 ? 27.322  1.455   11.292  1.00 24.85  ? 199 TRP   A O    1 
ATOM   3044 C CB   . TRP   A 1 214 ? 28.022  0.345   14.388  1.00 27.07  ? 199 TRP   A CB   1 
ATOM   3045 C CG   . TRP   A 1 214 ? 27.659  -0.917  13.646  1.00 27.04  ? 199 TRP   A CG   1 
ATOM   3046 C CD1  . TRP   A 1 214 ? 26.480  -1.190  13.013  1.00 26.89  ? 199 TRP   A CD1  1 
ATOM   3047 C CD2  . TRP   A 1 214 ? 28.481  -2.079  13.476  1.00 27.26  ? 199 TRP   A CD2  1 
ATOM   3048 N NE1  . TRP   A 1 214 ? 26.523  -2.443  12.451  1.00 27.01  ? 199 TRP   A NE1  1 
ATOM   3049 C CE2  . TRP   A 1 214 ? 27.740  -3.008  12.724  1.00 27.23  ? 199 TRP   A CE2  1 
ATOM   3050 C CE3  . TRP   A 1 214 ? 29.764  -2.425  13.896  1.00 27.55  ? 199 TRP   A CE3  1 
ATOM   3051 C CZ2  . TRP   A 1 214 ? 28.244  -4.258  12.381  1.00 30.10  ? 199 TRP   A CZ2  1 
ATOM   3052 C CZ3  . TRP   A 1 214 ? 30.264  -3.653  13.549  1.00 27.78  ? 199 TRP   A CZ3  1 
ATOM   3053 C CH2  . TRP   A 1 214 ? 29.506  -4.560  12.804  1.00 28.36  ? 199 TRP   A CH2  1 
ATOM   3054 H H    . TRP   A 1 214 ? 28.481  2.627   15.126  1.00 31.50  ? 199 TRP   A H    1 
ATOM   3055 H HA   . TRP   A 1 214 ? 29.130  1.344   12.981  1.00 31.27  ? 199 TRP   A HA   1 
ATOM   3056 H HB2  . TRP   A 1 214 ? 28.809  0.157   14.922  1.00 32.48  ? 199 TRP   A HB2  1 
ATOM   3057 H HB3  . TRP   A 1 214 ? 27.276  0.572   14.965  1.00 32.48  ? 199 TRP   A HB3  1 
ATOM   3058 H HD1  . TRP   A 1 214 ? 25.753  -0.612  12.969  1.00 32.27  ? 199 TRP   A HD1  1 
ATOM   3059 H HE1  . TRP   A 1 214 ? 25.889  -2.812  12.002  1.00 32.42  ? 199 TRP   A HE1  1 
ATOM   3060 H HE3  . TRP   A 1 214 ? 30.272  -1.834  14.403  1.00 33.06  ? 199 TRP   A HE3  1 
ATOM   3061 H HZ2  . TRP   A 1 214 ? 27.742  -4.863  11.884  1.00 36.12  ? 199 TRP   A HZ2  1 
ATOM   3062 H HZ3  . TRP   A 1 214 ? 31.124  -3.887  13.813  1.00 33.34  ? 199 TRP   A HZ3  1 
ATOM   3063 H HH2  . TRP   A 1 214 ? 29.870  -5.389  12.592  1.00 34.03  ? 199 TRP   A HH2  1 
ATOM   3064 N N    . SER   A 1 215 ? 26.063  2.314   12.956  1.00 25.87  ? 200 SER   A N    1 
ATOM   3065 C CA   . SER   A 1 215 ? 24.926  2.529   12.069  1.00 25.52  ? 200 SER   A CA   1 
ATOM   3066 C C    . SER   A 1 215 ? 25.291  3.456   10.914  1.00 24.55  ? 200 SER   A C    1 
ATOM   3067 O O    . SER   A 1 215 ? 24.768  3.305   9.805   1.00 24.11  ? 200 SER   A O    1 
ATOM   3068 C CB   . SER   A 1 215 ? 23.744  3.099   12.852  1.00 26.06  ? 200 SER   A CB   1 
ATOM   3069 O OG   . SER   A 1 215 ? 23.271  2.194   13.834  1.00 26.88  ? 200 SER   A OG   1 
ATOM   3070 H H    . SER   A 1 215 ? 25.940  2.567   13.769  1.00 31.04  ? 200 SER   A H    1 
ATOM   3071 H HA   . SER   A 1 215 ? 24.654  1.675   11.699  1.00 30.62  ? 200 SER   A HA   1 
ATOM   3072 H HB2  . SER   A 1 215 ? 24.027  3.915   13.293  1.00 31.28  ? 200 SER   A HB2  1 
ATOM   3073 H HB3  . SER   A 1 215 ? 23.023  3.290   12.232  1.00 31.28  ? 200 SER   A HB3  1 
ATOM   3074 H HG   . SER   A 1 215 ? 23.034  1.474   13.471  1.00 32.25  ? 200 SER   A HG   1 
ATOM   3075 N N    . LEU   A 1 216 ? 26.180  4.420   11.146  1.00 24.22  ? 201 LEU   A N    1 
ATOM   3076 C CA   . LEU   A 1 216 ? 26.579  5.297   10.047  1.00 23.24  ? 201 LEU   A CA   1 
ATOM   3077 C C    . LEU   A 1 216 ? 27.372  4.526   8.999   1.00 22.53  ? 201 LEU   A C    1 
ATOM   3078 O O    . LEU   A 1 216 ? 27.180  4.726   7.799   1.00 22.71  ? 201 LEU   A O    1 
ATOM   3079 C CB   . LEU   A 1 216 ? 27.384  6.477   10.580  1.00 23.09  ? 201 LEU   A CB   1 
ATOM   3080 C CG   . LEU   A 1 216 ? 27.890  7.438   9.505   1.00 22.44  ? 201 LEU   A CG   1 
ATOM   3081 C CD1  . LEU   A 1 216 ? 26.740  7.990   8.677   1.00 22.89  ? 201 LEU   A CD1  1 
ATOM   3082 C CD2  . LEU   A 1 216 ? 28.662  8.554   10.144  1.00 29.24  ? 201 LEU   A CD2  1 
ATOM   3083 H H    . LEU   A 1 216 ? 26.555  4.582   11.902  1.00 29.07  ? 201 LEU   A H    1 
ATOM   3084 H HA   . LEU   A 1 216 ? 25.784  5.654   9.622   1.00 27.88  ? 201 LEU   A HA   1 
ATOM   3085 H HB2  . LEU   A 1 216 ? 26.821  6.985   11.185  1.00 27.71  ? 201 LEU   A HB2  1 
ATOM   3086 H HB3  . LEU   A 1 216 ? 28.157  6.134   11.054  1.00 27.71  ? 201 LEU   A HB3  1 
ATOM   3087 H HG   . LEU   A 1 216 ? 28.477  6.958   8.900   1.00 26.93  ? 201 LEU   A HG   1 
ATOM   3088 H HD11 . LEU   A 1 216 ? 27.074  8.697   8.103   1.00 27.46  ? 201 LEU   A HD11 1 
ATOM   3089 H HD12 . LEU   A 1 216 ? 26.367  7.275   8.138   1.00 27.46  ? 201 LEU   A HD12 1 
ATOM   3090 H HD13 . LEU   A 1 216 ? 26.062  8.343   9.274   1.00 27.46  ? 201 LEU   A HD13 1 
ATOM   3091 H HD21 . LEU   A 1 216 ? 28.987  9.151   9.452   1.00 35.08  ? 201 LEU   A HD21 1 
ATOM   3092 H HD22 . LEU   A 1 216 ? 28.077  9.036   10.749  1.00 35.08  ? 201 LEU   A HD22 1 
ATOM   3093 H HD23 . LEU   A 1 216 ? 29.410  8.179   10.636  1.00 35.08  ? 201 LEU   A HD23 1 
ATOM   3094 N N    . GLY   A 1 217 ? 28.244  3.622   9.441   1.00 25.18  ? 202 GLY   A N    1 
ATOM   3095 C CA   . GLY   A 1 217 ? 28.970  2.779   8.505   1.00 26.94  ? 202 GLY   A CA   1 
ATOM   3096 C C    . GLY   A 1 217 ? 28.050  1.960   7.622   1.00 22.25  ? 202 GLY   A C    1 
ATOM   3097 O O    . GLY   A 1 217 ? 28.262  1.857   6.415   1.00 22.68  ? 202 GLY   A O    1 
ATOM   3098 H H    . GLY   A 1 217 ? 28.430  3.481   10.268  1.00 30.21  ? 202 GLY   A H    1 
ATOM   3099 H HA2  . GLY   A 1 217 ? 29.523  3.335   7.935   1.00 32.33  ? 202 GLY   A HA2  1 
ATOM   3100 H HA3  . GLY   A 1 217 ? 29.539  2.169   9.000   1.00 32.33  ? 202 GLY   A HA3  1 
ATOM   3101 N N    . ILE   A 1 218 ? 27.014  1.370   8.212   1.00 24.10  ? 203 ILE   A N    1 
ATOM   3102 C CA   . ILE   A 1 218 ? 26.041  0.627   7.421   1.00 23.27  ? 203 ILE   A CA   1 
ATOM   3103 C C    . ILE   A 1 218 ? 25.321  1.561   6.458   1.00 22.71  ? 203 ILE   A C    1 
ATOM   3104 O O    . ILE   A 1 218 ? 24.992  1.179   5.327   1.00 22.43  ? 203 ILE   A O    1 
ATOM   3105 C CB   . ILE   A 1 218 ? 25.043  -0.098  8.343   1.00 24.74  ? 203 ILE   A CB   1 
ATOM   3106 C CG1  . ILE   A 1 218 ? 25.767  -1.034  9.312   1.00 24.94  ? 203 ILE   A CG1  1 
ATOM   3107 C CG2  . ILE   A 1 218 ? 24.010  -0.848  7.512   1.00 24.52  ? 203 ILE   A CG2  1 
ATOM   3108 C CD1  . ILE   A 1 218 ? 26.398  -2.213  8.680   1.00 27.16  ? 203 ILE   A CD1  1 
ATOM   3109 H H    . ILE   A 1 218 ? 26.854  1.385   9.057   1.00 28.92  ? 203 ILE   A H    1 
ATOM   3110 H HA   . ILE   A 1 218 ? 26.514  -0.041  6.901   1.00 27.92  ? 203 ILE   A HA   1 
ATOM   3111 H HB   . ILE   A 1 218 ? 24.582  0.567   8.877   1.00 29.69  ? 203 ILE   A HB   1 
ATOM   3112 H HG12 . ILE   A 1 218 ? 26.467  -0.533  9.759   1.00 29.93  ? 203 ILE   A HG12 1 
ATOM   3113 H HG13 . ILE   A 1 218 ? 25.125  -1.360  9.962   1.00 29.93  ? 203 ILE   A HG13 1 
ATOM   3114 H HG21 . ILE   A 1 218 ? 23.536  -1.470  8.085   1.00 29.43  ? 203 ILE   A HG21 1 
ATOM   3115 H HG22 . ILE   A 1 218 ? 23.388  -0.209  7.131   1.00 29.43  ? 203 ILE   A HG22 1 
ATOM   3116 H HG23 . ILE   A 1 218 ? 24.464  -1.330  6.804   1.00 29.43  ? 203 ILE   A HG23 1 
ATOM   3117 H HD11 . ILE   A 1 218 ? 26.887  -2.709  9.355   1.00 32.59  ? 203 ILE   A HD11 1 
ATOM   3118 H HD12 . ILE   A 1 218 ? 25.706  -2.773  8.295   1.00 32.59  ? 203 ILE   A HD12 1 
ATOM   3119 H HD13 . ILE   A 1 218 ? 27.005  -1.912  7.986   1.00 32.59  ? 203 ILE   A HD13 1 
ATOM   3120 N N    . THR   A 1 219 ? 25.032  2.787   6.900   1.00 22.65  ? 204 THR   A N    1 
ATOM   3121 C CA   . THR   A 1 219 ? 24.319  3.727   6.042   1.00 22.23  ? 204 THR   A CA   1 
ATOM   3122 C C    . THR   A 1 219 ? 25.166  4.114   4.836   1.00 21.16  ? 204 THR   A C    1 
ATOM   3123 O O    . THR   A 1 219 ? 24.642  4.294   3.733   1.00 20.82  ? 204 THR   A O    1 
ATOM   3124 C CB   . THR   A 1 219 ? 23.924  4.972   6.839   1.00 22.46  ? 204 THR   A CB   1 
ATOM   3125 O OG1  . THR   A 1 219 ? 23.080  4.594   7.936   1.00 24.78  ? 204 THR   A OG1  1 
ATOM   3126 C CG2  . THR   A 1 219 ? 23.175  5.951   5.956   1.00 22.13  ? 204 THR   A CG2  1 
ATOM   3127 H H    . THR   A 1 219 ? 25.235  3.091   7.678   1.00 27.18  ? 204 THR   A H    1 
ATOM   3128 H HA   . THR   A 1 219 ? 23.506  3.307   5.721   1.00 26.68  ? 204 THR   A HA   1 
ATOM   3129 H HB   . THR   A 1 219 ? 24.723  5.405   7.176   1.00 26.95  ? 204 THR   A HB   1 
ATOM   3130 H HG1  . THR   A 1 219 ? 23.491  4.068   8.447   1.00 29.73  ? 204 THR   A HG1  1 
ATOM   3131 H HG21 . THR   A 1 219 ? 22.763  6.641   6.500   1.00 26.55  ? 204 THR   A HG21 1 
ATOM   3132 H HG22 . THR   A 1 219 ? 23.786  6.368   5.329   1.00 26.55  ? 204 THR   A HG22 1 
ATOM   3133 H HG23 . THR   A 1 219 ? 22.482  5.488   5.460   1.00 26.55  ? 204 THR   A HG23 1 
ATOM   3134 N N    . ALA   A 1 220 ? 26.477  4.257   5.035   1.00 20.63  ? 205 ALA   A N    1 
ATOM   3135 C CA   . ALA   A 1 220 ? 27.373  4.557   3.923   1.00 23.01  ? 205 ALA   A CA   1 
ATOM   3136 C C    . ALA   A 1 220 ? 27.364  3.433   2.893   1.00 20.84  ? 205 ALA   A C    1 
ATOM   3137 O O    . ALA   A 1 220 ? 27.394  3.690   1.687   1.00 24.40  ? 205 ALA   A O    1 
ATOM   3138 C CB   . ALA   A 1 220 ? 28.787  4.786   4.452   1.00 21.45  ? 205 ALA   A CB   1 
ATOM   3139 H H    . ALA   A 1 220 ? 26.869  4.186   5.797   1.00 24.76  ? 205 ALA   A H    1 
ATOM   3140 H HA   . ALA   A 1 220 ? 27.076  5.369   3.484   1.00 27.61  ? 205 ALA   A HA   1 
ATOM   3141 H HB1  . ALA   A 1 220 ? 29.376  4.977   3.705   1.00 25.74  ? 205 ALA   A HB1  1 
ATOM   3142 H HB2  . ALA   A 1 220 ? 28.777  5.538   5.065   1.00 25.74  ? 205 ALA   A HB2  1 
ATOM   3143 H HB3  . ALA   A 1 220 ? 29.085  3.987   4.913   1.00 25.74  ? 205 ALA   A HB3  1 
ATOM   3144 N N    . ILE   A 1 221 ? 27.301  2.179   3.346   1.00 21.29  ? 206 ILE   A N    1 
ATOM   3145 C CA   . ILE   A 1 221 ? 27.147  1.077   2.401   1.00 20.08  ? 206 ILE   A CA   1 
ATOM   3146 C C    . ILE   A 1 221 ? 25.783  1.160   1.730   1.00 22.94  ? 206 ILE   A C    1 
ATOM   3147 O O    . ILE   A 1 221 ? 25.657  0.944   0.518   1.00 22.30  ? 206 ILE   A O    1 
ATOM   3148 C CB   . ILE   A 1 221 ? 27.361  -0.273  3.106   1.00 20.90  ? 206 ILE   A CB   1 
ATOM   3149 C CG1  . ILE   A 1 221 ? 28.797  -0.381  3.630   1.00 20.59  ? 206 ILE   A CG1  1 
ATOM   3150 C CG2  . ILE   A 1 221 ? 27.053  -1.431  2.153   1.00 21.14  ? 206 ILE   A CG2  1 
ATOM   3151 C CD1  . ILE   A 1 221 ? 29.083  -1.657  4.457   1.00 23.52  ? 206 ILE   A CD1  1 
ATOM   3152 H H    . ILE   A 1 221 ? 27.344  1.947   4.173   1.00 25.54  ? 206 ILE   A H    1 
ATOM   3153 H HA   . ILE   A 1 221 ? 27.827  1.155   1.714   1.00 24.09  ? 206 ILE   A HA   1 
ATOM   3154 H HB   . ILE   A 1 221 ? 26.753  -0.323  3.860   1.00 25.08  ? 206 ILE   A HB   1 
ATOM   3155 H HG12 . ILE   A 1 221 ? 29.404  -0.381  2.873   1.00 24.71  ? 206 ILE   A HG12 1 
ATOM   3156 H HG13 . ILE   A 1 221 ? 28.977  0.383   4.200   1.00 24.71  ? 206 ILE   A HG13 1 
ATOM   3157 H HG21 . ILE   A 1 221 ? 27.319  -2.264  2.572   1.00 25.37  ? 206 ILE   A HG21 1 
ATOM   3158 H HG22 . ILE   A 1 221 ? 26.102  -1.442  1.968   1.00 25.37  ? 206 ILE   A HG22 1 
ATOM   3159 H HG23 . ILE   A 1 221 ? 27.550  -1.302  1.330   1.00 25.37  ? 206 ILE   A HG23 1 
ATOM   3160 H HD11 . ILE   A 1 221 ? 29.916  -1.541  4.939   1.00 28.22  ? 206 ILE   A HD11 1 
ATOM   3161 H HD12 . ILE   A 1 221 ? 28.355  -1.798  5.082   1.00 28.22  ? 206 ILE   A HD12 1 
ATOM   3162 H HD13 . ILE   A 1 221 ? 29.153  -2.415  3.854   1.00 28.22  ? 206 ILE   A HD13 1 
ATOM   3163 N N    . GLU   A 1 222 ? 24.754  1.548   2.495   1.00 21.13  ? 207 GLU   A N    1 
ATOM   3164 C CA   . GLU   A 1 222 ? 23.404  1.671   1.954   1.00 21.56  ? 207 GLU   A CA   1 
ATOM   3165 C C    . GLU   A 1 222 ? 23.344  2.722   0.851   1.00 22.49  ? 207 GLU   A C    1 
ATOM   3166 O O    . GLU   A 1 222 ? 22.639  2.544   -0.153  1.00 20.92  ? 207 GLU   A O    1 
ATOM   3167 C CB   . GLU   A 1 222 ? 22.430  2.015   3.091   1.00 26.58  ? 207 GLU   A CB   1 
ATOM   3168 C CG   . GLU   A 1 222 ? 21.010  2.386   2.666   1.00 24.93  ? 207 GLU   A CG   1 
ATOM   3169 C CD   . GLU   A 1 222 ? 20.254  3.213   3.714   1.00 23.33  ? 207 GLU   A CD   1 
ATOM   3170 O OE1  . GLU   A 1 222 ? 20.784  3.442   4.818   1.00 23.38  ? 207 GLU   A OE1  1 
ATOM   3171 O OE2  . GLU   A 1 222 ? 19.118  3.629   3.413   1.00 23.82  ? 207 GLU   A OE2  1 
ATOM   3172 H H    . GLU   A 1 222 ? 24.816  1.746   3.330   1.00 25.35  ? 207 GLU   A H    1 
ATOM   3173 H HA   . GLU   A 1 222 ? 23.134  0.824   1.566   1.00 25.87  ? 207 GLU   A HA   1 
ATOM   3174 H HB2  . GLU   A 1 222 ? 22.362  1.245   3.676   1.00 31.89  ? 207 GLU   A HB2  1 
ATOM   3175 H HB3  . GLU   A 1 222 ? 22.790  2.772   3.580   1.00 31.89  ? 207 GLU   A HB3  1 
ATOM   3176 H HG2  . GLU   A 1 222 ? 21.054  2.909   1.851   1.00 29.92  ? 207 GLU   A HG2  1 
ATOM   3177 H HG3  . GLU   A 1 222 ? 20.507  1.571   2.512   1.00 29.92  ? 207 GLU   A HG3  1 
ATOM   3178 N N    . LEU   A 1 223 ? 24.051  3.838   1.030   1.00 21.67  ? 208 LEU   A N    1 
ATOM   3179 C CA   . LEU   A 1 223 ? 24.034  4.876   0.006   1.00 19.66  ? 208 LEU   A CA   1 
ATOM   3180 C C    . LEU   A 1 223 ? 24.832  4.464   -1.226  1.00 25.05  ? 208 LEU   A C    1 
ATOM   3181 O O    . LEU   A 1 223 ? 24.565  4.964   -2.325  1.00 24.35  ? 208 LEU   A O    1 
ATOM   3182 C CB   . LEU   A 1 223 ? 24.592  6.179   0.568   1.00 19.98  ? 208 LEU   A CB   1 
ATOM   3183 C CG   . LEU   A 1 223 ? 23.833  6.765   1.758   1.00 22.86  ? 208 LEU   A CG   1 
ATOM   3184 C CD1  . LEU   A 1 223 ? 24.463  8.057   2.201   1.00 21.04  ? 208 LEU   A CD1  1 
ATOM   3185 C CD2  . LEU   A 1 223 ? 22.368  6.975   1.394   1.00 23.12  ? 208 LEU   A CD2  1 
ATOM   3186 H H    . LEU   A 1 223 ? 24.536  4.012   1.718   1.00 26.01  ? 208 LEU   A H    1 
ATOM   3187 H HA   . LEU   A 1 223 ? 23.116  5.039   -0.262  1.00 23.60  ? 208 LEU   A HA   1 
ATOM   3188 H HB2  . LEU   A 1 223 ? 25.504  6.020   0.858   1.00 23.97  ? 208 LEU   A HB2  1 
ATOM   3189 H HB3  . LEU   A 1 223 ? 24.580  6.844   -0.138  1.00 23.97  ? 208 LEU   A HB3  1 
ATOM   3190 H HG   . LEU   A 1 223 ? 23.874  6.144   2.501   1.00 27.43  ? 208 LEU   A HG   1 
ATOM   3191 H HD11 . LEU   A 1 223 ? 23.968  8.406   2.959   1.00 25.25  ? 208 LEU   A HD11 1 
ATOM   3192 H HD12 . LEU   A 1 223 ? 25.383  7.888   2.456   1.00 25.25  ? 208 LEU   A HD12 1 
ATOM   3193 H HD13 . LEU   A 1 223 ? 24.433  8.691   1.467   1.00 25.25  ? 208 LEU   A HD13 1 
ATOM   3194 H HD21 . LEU   A 1 223 ? 21.948  7.520   2.078   1.00 27.75  ? 208 LEU   A HD21 1 
ATOM   3195 H HD22 . LEU   A 1 223 ? 22.317  7.424   0.536   1.00 27.75  ? 208 LEU   A HD22 1 
ATOM   3196 H HD23 . LEU   A 1 223 ? 21.928  6.112   1.343   1.00 27.75  ? 208 LEU   A HD23 1 
ATOM   3197 N N    . ALA   A 1 224 ? 25.786  3.559   -1.059  1.00 23.12  ? 209 ALA   A N    1 
ATOM   3198 C CA   . ALA   A 1 224 ? 26.620  3.086   -2.154  1.00 24.97  ? 209 ALA   A CA   1 
ATOM   3199 C C    . ALA   A 1 224 ? 25.986  1.942   -2.922  1.00 20.54  ? 209 ALA   A C    1 
ATOM   3200 O O    . ALA   A 1 224 ? 26.203  1.830   -4.133  1.00 32.56  ? 209 ALA   A O    1 
ATOM   3201 C CB   . ALA   A 1 224 ? 27.980  2.640   -1.610  1.00 23.57  ? 209 ALA   A CB   1 
ATOM   3202 H H    . ALA   A 1 224 ? 25.975  3.195   -0.303  1.00 27.75  ? 209 ALA   A H    1 
ATOM   3203 H HA   . ALA   A 1 224 ? 26.766  3.814   -2.777  1.00 29.97  ? 209 ALA   A HA   1 
ATOM   3204 H HB1  . ALA   A 1 224 ? 28.493  2.241   -2.330  1.00 28.29  ? 209 ALA   A HB1  1 
ATOM   3205 H HB2  . ALA   A 1 224 ? 28.449  3.414   -1.259  1.00 28.29  ? 209 ALA   A HB2  1 
ATOM   3206 H HB3  . ALA   A 1 224 ? 27.840  1.990   -0.903  1.00 28.29  ? 209 ALA   A HB3  1 
ATOM   3207 N N    . GLU   A 1 225 ? 25.194  1.102   -2.258  1.00 24.07  ? 210 GLU   A N    1 
ATOM   3208 C CA   . GLU   A 1 225 ? 24.719  -0.137  -2.856  1.00 21.04  ? 210 GLU   A CA   1 
ATOM   3209 C C    . GLU   A 1 225 ? 23.207  -0.278  -2.884  1.00 22.90  ? 210 GLU   A C    1 
ATOM   3210 O O    . GLU   A 1 225 ? 22.713  -1.274  -3.421  1.00 23.38  ? 210 GLU   A O    1 
ATOM   3211 C CB   . GLU   A 1 225 ? 25.355  -1.326  -2.119  1.00 23.30  ? 210 GLU   A CB   1 
ATOM   3212 C CG   . GLU   A 1 225 ? 26.898  -1.318  -2.206  1.00 28.16  ? 210 GLU   A CG   1 
ATOM   3213 C CD   . GLU   A 1 225 ? 27.567  -2.473  -1.474  1.00 29.15  ? 210 GLU   A CD   1 
ATOM   3214 O OE1  . GLU   A 1 225 ? 26.848  -3.337  -0.937  1.00 31.03  ? 210 GLU   A OE1  1 
ATOM   3215 O OE2  . GLU   A 1 225 ? 28.820  -2.514  -1.432  1.00 33.77  ? 210 GLU   A OE2  1 
ATOM   3216 H H    . GLU   A 1 225 ? 24.918  1.232   -1.454  1.00 28.89  ? 210 GLU   A H    1 
ATOM   3217 H HA   . GLU   A 1 225 ? 25.003  -0.166  -3.783  1.00 25.24  ? 210 GLU   A HA   1 
ATOM   3218 H HB2  . GLU   A 1 225 ? 25.106  -1.288  -1.182  1.00 27.96  ? 210 GLU   A HB2  1 
ATOM   3219 H HB3  . GLU   A 1 225 ? 25.034  -2.152  -2.514  1.00 27.96  ? 210 GLU   A HB3  1 
ATOM   3220 H HG2  . GLU   A 1 225 ? 27.157  -1.372  -3.140  1.00 33.79  ? 210 GLU   A HG2  1 
ATOM   3221 H HG3  . GLU   A 1 225 ? 27.227  -0.493  -1.818  1.00 33.79  ? 210 GLU   A HG3  1 
ATOM   3222 N N    . LEU   A 1 226 ? 22.454  0.690   -2.354  1.00 23.33  ? 211 LEU   A N    1 
ATOM   3223 C CA   . LEU   A 1 226 ? 20.987  0.745   -2.388  1.00 24.00  ? 211 LEU   A CA   1 
ATOM   3224 C C    . LEU   A 1 226 ? 20.334  -0.181  -1.370  1.00 27.51  ? 211 LEU   A C    1 
ATOM   3225 O O    . LEU   A 1 226 ? 19.105  -0.335  -1.390  1.00 24.90  ? 211 LEU   A O    1 
ATOM   3226 C CB   . LEU   A 1 226 ? 20.420  0.411   -3.772  1.00 25.24  ? 211 LEU   A CB   1 
ATOM   3227 C CG   . LEU   A 1 226 ? 20.970  1.246   -4.928  1.00 27.97  ? 211 LEU   A CG   1 
ATOM   3228 C CD1  . LEU   A 1 226 ? 20.337  0.844   -6.238  1.00 29.50  ? 211 LEU   A CD1  1 
ATOM   3229 C CD2  . LEU   A 1 226 ? 20.752  2.735   -4.651  1.00 32.80  ? 211 LEU   A CD2  1 
ATOM   3230 H H    . LEU   A 1 226 ? 22.793  1.366   -1.944  1.00 27.99  ? 211 LEU   A H    1 
ATOM   3231 H HA   . LEU   A 1 226 ? 20.734  1.654   -2.161  1.00 28.80  ? 211 LEU   A HA   1 
ATOM   3232 H HB2  . LEU   A 1 226 ? 20.618  -0.519  -3.966  1.00 30.29  ? 211 LEU   A HB2  1 
ATOM   3233 H HB3  . LEU   A 1 226 ? 19.460  0.547   -3.748  1.00 30.29  ? 211 LEU   A HB3  1 
ATOM   3234 H HG   . LEU   A 1 226 ? 21.923  1.086   -5.009  1.00 33.57  ? 211 LEU   A HG   1 
ATOM   3235 H HD11 . LEU   A 1 226 ? 20.711  1.386   -6.949  1.00 35.40  ? 211 LEU   A HD11 1 
ATOM   3236 H HD12 . LEU   A 1 226 ? 20.522  -0.094  -6.404  1.00 35.40  ? 211 LEU   A HD12 1 
ATOM   3237 H HD13 . LEU   A 1 226 ? 19.379  0.987   -6.182  1.00 35.40  ? 211 LEU   A HD13 1 
ATOM   3238 H HD21 . LEU   A 1 226 ? 20.970  3.241   -5.449  1.00 39.36  ? 211 LEU   A HD21 1 
ATOM   3239 H HD22 . LEU   A 1 226 ? 19.823  2.879   -4.411  1.00 39.36  ? 211 LEU   A HD22 1 
ATOM   3240 H HD23 . LEU   A 1 226 ? 21.328  3.008   -3.919  1.00 39.36  ? 211 LEU   A HD23 1 
ATOM   3241 N N    . GLN   A 1 227 ? 21.099  -0.809  -0.498  1.00 23.56  ? 212 GLN   A N    1 
ATOM   3242 C CA   . GLN   A 1 227 ? 20.511  -1.569  0.597   1.00 29.02  ? 212 GLN   A CA   1 
ATOM   3243 C C    . GLN   A 1 227 ? 21.621  -1.853  1.597   1.00 24.31  ? 212 GLN   A C    1 
ATOM   3244 O O    . GLN   A 1 227 ? 22.795  -1.885  1.217   1.00 25.33  ? 212 GLN   A O    1 
ATOM   3245 C CB   . GLN   A 1 227 ? 19.858  -2.861  0.096   1.00 33.81  ? 212 GLN   A CB   1 
ATOM   3246 C CG   . GLN   A 1 227 ? 20.819  -3.878  -0.477  1.00 34.55  ? 212 GLN   A CG   1 
ATOM   3247 C CD   . GLN   A 1 227 ? 20.143  -5.200  -0.789  1.00 49.75  ? 212 GLN   A CD   1 
ATOM   3248 O OE1  . GLN   A 1 227 ? 18.977  -5.234  -1.189  1.00 51.65  ? 212 GLN   A OE1  1 
ATOM   3249 N NE2  . GLN   A 1 227 ? 20.869  -6.301  -0.595  1.00 47.43  ? 212 GLN   A NE2  1 
ATOM   3250 H H    . GLN   A 1 227 ? 21.959  -0.812  -0.515  1.00 28.27  ? 212 GLN   A H    1 
ATOM   3251 H HA   . GLN   A 1 227 ? 19.804  -1.065  1.029   1.00 34.82  ? 212 GLN   A HA   1 
ATOM   3252 H HB2  . GLN   A 1 227 ? 19.397  -3.281  0.839   1.00 40.57  ? 212 GLN   A HB2  1 
ATOM   3253 H HB3  . GLN   A 1 227 ? 19.223  -2.634  -0.602  1.00 40.57  ? 212 GLN   A HB3  1 
ATOM   3254 H HG2  . GLN   A 1 227 ? 21.196  -3.530  -1.300  1.00 41.46  ? 212 GLN   A HG2  1 
ATOM   3255 H HG3  . GLN   A 1 227 ? 21.525  -4.045  0.167   1.00 41.46  ? 212 GLN   A HG3  1 
ATOM   3256 H HE21 . GLN   A 1 227 ? 21.677  -6.238  -0.306  1.00 56.91  ? 212 GLN   A HE21 1 
ATOM   3257 H HE22 . GLN   A 1 227 ? 20.530  -7.074  -0.757  1.00 56.91  ? 212 GLN   A HE22 1 
ATOM   3258 N N    . PRO   A 1 228 ? 21.306  -2.036  2.872   1.00 25.02  ? 213 PRO   A N    1 
ATOM   3259 C CA   . PRO   A 1 228 ? 22.337  -2.413  3.834   1.00 31.39  ? 213 PRO   A CA   1 
ATOM   3260 C C    . PRO   A 1 228 ? 22.824  -3.822  3.560   1.00 23.62  ? 213 PRO   A C    1 
ATOM   3261 O O    . PRO   A 1 228 ? 22.176  -4.575  2.818   1.00 24.39  ? 213 PRO   A O    1 
ATOM   3262 C CB   . PRO   A 1 228 ? 21.607  -2.329  5.181   1.00 28.23  ? 213 PRO   A CB   1 
ATOM   3263 C CG   . PRO   A 1 228 ? 20.206  -2.620  4.845   1.00 23.59  ? 213 PRO   A CG   1 
ATOM   3264 C CD   . PRO   A 1 228 ? 19.963  -2.050  3.474   1.00 25.79  ? 213 PRO   A CD   1 
ATOM   3265 H HA   . PRO   A 1 228 ? 23.081  -1.791  3.823   1.00 37.67  ? 213 PRO   A HA   1 
ATOM   3266 H HB2  . PRO   A 1 228 ? 21.964  -2.989  5.796   1.00 33.87  ? 213 PRO   A HB2  1 
ATOM   3267 H HB3  . PRO   A 1 228 ? 21.700  -1.440  5.557   1.00 33.87  ? 213 PRO   A HB3  1 
ATOM   3268 H HG2  . PRO   A 1 228 ? 20.066  -3.580  4.844   1.00 28.31  ? 213 PRO   A HG2  1 
ATOM   3269 H HG3  . PRO   A 1 228 ? 19.622  -2.201  5.496   1.00 28.31  ? 213 PRO   A HG3  1 
ATOM   3270 H HD2  . PRO   A 1 228 ? 19.363  -2.616  2.965   1.00 30.95  ? 213 PRO   A HD2  1 
ATOM   3271 H HD3  . PRO   A 1 228 ? 19.602  -1.151  3.533   1.00 30.95  ? 213 PRO   A HD3  1 
ATOM   3272 N N    . PRO   A 1 229 ? 23.957  -4.216  4.137   1.00 23.18  ? 214 PRO   A N    1 
ATOM   3273 C CA   . PRO   A 1 229 ? 24.411  -5.606  3.998   1.00 25.03  ? 214 PRO   A CA   1 
ATOM   3274 C C    . PRO   A 1 229 ? 23.391  -6.602  4.541   1.00 25.07  ? 214 PRO   A C    1 
ATOM   3275 O O    . PRO   A 1 229 ? 22.717  -6.345  5.543   1.00 25.11  ? 214 PRO   A O    1 
ATOM   3276 C CB   . PRO   A 1 229 ? 25.703  -5.635  4.822   1.00 26.67  ? 214 PRO   A CB   1 
ATOM   3277 C CG   . PRO   A 1 229 ? 26.161  -4.207  4.862   1.00 24.31  ? 214 PRO   A CG   1 
ATOM   3278 C CD   . PRO   A 1 229 ? 24.913  -3.391  4.890   1.00 22.41  ? 214 PRO   A CD   1 
ATOM   3279 H HA   . PRO   A 1 229 ? 24.596  -5.807  3.067   1.00 30.03  ? 214 PRO   A HA   1 
ATOM   3280 H HB2  . PRO   A 1 229 ? 25.519  -5.967  5.715   1.00 32.00  ? 214 PRO   A HB2  1 
ATOM   3281 H HB3  . PRO   A 1 229 ? 26.362  -6.200  4.388   1.00 32.00  ? 214 PRO   A HB3  1 
ATOM   3282 H HG2  . PRO   A 1 229 ? 26.691  -4.053  5.660   1.00 29.17  ? 214 PRO   A HG2  1 
ATOM   3283 H HG3  . PRO   A 1 229 ? 26.686  -4.007  4.071   1.00 29.17  ? 214 PRO   A HG3  1 
ATOM   3284 H HD2  . PRO   A 1 229 ? 24.610  -3.255  5.801   1.00 26.89  ? 214 PRO   A HD2  1 
ATOM   3285 H HD3  . PRO   A 1 229 ? 25.050  -2.536  4.453   1.00 26.89  ? 214 PRO   A HD3  1 
ATOM   3286 N N    . LEU   A 1 230 ? 23.287  -7.749  3.869   1.00 26.06  ? 215 LEU   A N    1 
ATOM   3287 C CA   . LEU   A 1 230 ? 22.465  -8.886  4.273   1.00 27.36  ? 215 LEU   A CA   1 
ATOM   3288 C C    . LEU   A 1 230 ? 20.977  -8.597  4.151   1.00 31.32  ? 215 LEU   A C    1 
ATOM   3289 O O    . LEU   A 1 230 ? 20.163  -9.357  4.682   1.00 28.87  ? 215 LEU   A O    1 
ATOM   3290 C CB   . LEU   A 1 230 ? 22.768  -9.328  5.711   1.00 27.75  ? 215 LEU   A CB   1 
ATOM   3291 C CG   . LEU   A 1 230 ? 24.215  -9.738  6.004   1.00 27.75  ? 215 LEU   A CG   1 
ATOM   3292 C CD1  . LEU   A 1 230 ? 24.397  -10.035 7.481   1.00 28.30  ? 215 LEU   A CD1  1 
ATOM   3293 C CD2  . LEU   A 1 230 ? 24.608  -10.939 5.173   1.00 32.36  ? 215 LEU   A CD2  1 
ATOM   3294 H H    . LEU   A 1 230 ? 23.710  -7.898  3.135   1.00 31.27  ? 215 LEU   A H    1 
ATOM   3295 H HA   . LEU   A 1 230 ? 22.674  -9.626  3.682   1.00 32.83  ? 215 LEU   A HA   1 
ATOM   3296 H HB2  . LEU   A 1 230 ? 22.554  -8.591  6.304   1.00 33.30  ? 215 LEU   A HB2  1 
ATOM   3297 H HB3  . LEU   A 1 230 ? 22.208  -10.093 5.916   1.00 33.30  ? 215 LEU   A HB3  1 
ATOM   3298 H HG   . LEU   A 1 230 ? 24.802  -9.002  5.768   1.00 33.30  ? 215 LEU   A HG   1 
ATOM   3299 H HD11 . LEU   A 1 230 ? 25.319  -10.294 7.640   1.00 33.96  ? 215 LEU   A HD11 1 
ATOM   3300 H HD12 . LEU   A 1 230 ? 24.185  -9.238  7.992   1.00 33.96  ? 215 LEU   A HD12 1 
ATOM   3301 H HD13 . LEU   A 1 230 ? 23.802  -10.758 7.734   1.00 33.96  ? 215 LEU   A HD13 1 
ATOM   3302 H HD21 . LEU   A 1 230 ? 25.506  -11.212 5.418   1.00 38.83  ? 215 LEU   A HD21 1 
ATOM   3303 H HD22 . LEU   A 1 230 ? 23.984  -11.661 5.347   1.00 38.83  ? 215 LEU   A HD22 1 
ATOM   3304 H HD23 . LEU   A 1 230 ? 24.580  -10.697 4.234   1.00 38.83  ? 215 LEU   A HD23 1 
ATOM   3305 N N    . PHE   A 1 231 ? 20.604  -7.510  3.467   1.00 27.01  ? 216 PHE   A N    1 
ATOM   3306 C CA   . PHE   A 1 231 ? 19.201  -7.128  3.365   1.00 29.77  ? 216 PHE   A CA   1 
ATOM   3307 C C    . PHE   A 1 231 ? 18.349  -8.202  2.702   1.00 29.02  ? 216 PHE   A C    1 
ATOM   3308 O O    . PHE   A 1 231 ? 17.127  -8.191  2.869   1.00 29.87  ? 216 PHE   A O    1 
ATOM   3309 C CB   . PHE   A 1 231 ? 19.073  -5.820  2.585   1.00 30.52  ? 216 PHE   A CB   1 
ATOM   3310 C CG   . PHE   A 1 231 ? 17.776  -5.094  2.816   1.00 34.61  ? 216 PHE   A CG   1 
ATOM   3311 C CD1  . PHE   A 1 231 ? 17.458  -4.592  4.067   1.00 34.16  ? 216 PHE   A CD1  1 
ATOM   3312 C CD2  . PHE   A 1 231 ? 16.891  -4.882  1.774   1.00 37.70  ? 216 PHE   A CD2  1 
ATOM   3313 C CE1  . PHE   A 1 231 ? 16.270  -3.907  4.282   1.00 31.62  ? 216 PHE   A CE1  1 
ATOM   3314 C CE2  . PHE   A 1 231 ? 15.700  -4.201  1.982   1.00 34.45  ? 216 PHE   A CE2  1 
ATOM   3315 C CZ   . PHE   A 1 231 ? 15.391  -3.711  3.240   1.00 30.14  ? 216 PHE   A CZ   1 
ATOM   3316 H H    . PHE   A 1 231 ? 21.144  -6.982  3.055   1.00 32.41  ? 216 PHE   A H    1 
ATOM   3317 H HA   . PHE   A 1 231 ? 18.856  -6.988  4.261   1.00 35.73  ? 216 PHE   A HA   1 
ATOM   3318 H HB2  . PHE   A 1 231 ? 19.794  -5.228  2.852   1.00 36.62  ? 216 PHE   A HB2  1 
ATOM   3319 H HB3  . PHE   A 1 231 ? 19.138  -6.015  1.637   1.00 36.62  ? 216 PHE   A HB3  1 
ATOM   3320 H HD1  . PHE   A 1 231 ? 18.049  -4.717  4.774   1.00 41.00  ? 216 PHE   A HD1  1 
ATOM   3321 H HD2  . PHE   A 1 231 ? 17.097  -5.199  0.924   1.00 45.23  ? 216 PHE   A HD2  1 
ATOM   3322 H HE1  . PHE   A 1 231 ? 16.067  -3.580  5.129   1.00 37.94  ? 216 PHE   A HE1  1 
ATOM   3323 H HE2  . PHE   A 1 231 ? 15.108  -4.074  1.276   1.00 41.34  ? 216 PHE   A HE2  1 
ATOM   3324 H HZ   . PHE   A 1 231 ? 14.595  -3.252  3.380   1.00 36.16  ? 216 PHE   A HZ   1 
ATOM   3325 N N    . ASP   A 1 232 ? 18.955  -9.114  1.944   1.00 30.69  ? 217 ASP   A N    1 
ATOM   3326 C CA   . ASP   A 1 232 ? 18.228  -10.222 1.341   1.00 31.18  ? 217 ASP   A CA   1 
ATOM   3327 C C    . ASP   A 1 232 ? 18.156  -11.440 2.252   1.00 33.65  ? 217 ASP   A C    1 
ATOM   3328 O O    . ASP   A 1 232 ? 17.673  -12.491 1.823   1.00 37.25  ? 217 ASP   A O    1 
ATOM   3329 C CB   . ASP   A 1 232 ? 18.884  -10.623 0.016   1.00 38.28  ? 217 ASP   A CB   1 
ATOM   3330 C CG   . ASP   A 1 232 ? 20.370  -10.846 0.159   1.00 38.93  ? 217 ASP   A CG   1 
ATOM   3331 O OD1  . ASP   A 1 232 ? 20.990  -10.117 0.962   1.00 34.26  ? 217 ASP   A OD1  1 
ATOM   3332 O OD2  . ASP   A 1 232 ? 20.914  -11.744 -0.516  1.00 34.73  ? 217 ASP   A OD2  1 
ATOM   3333 H H    . ASP   A 1 232 ? 19.796  -9.111  1.765   1.00 36.83  ? 217 ASP   A H    1 
ATOM   3334 H HA   . ASP   A 1 232 ? 17.323  -9.931  1.152   1.00 37.41  ? 217 ASP   A HA   1 
ATOM   3335 H HB2  . ASP   A 1 232 ? 18.483  -11.447 -0.301  1.00 45.94  ? 217 ASP   A HB2  1 
ATOM   3336 H HB3  . ASP   A 1 232 ? 18.745  -9.916  -0.634  1.00 45.94  ? 217 ASP   A HB3  1 
ATOM   3337 N N    . VAL   A 1 233 ? 18.653  -11.335 3.479   1.00 33.53  ? 218 VAL   A N    1 
ATOM   3338 C CA   . VAL   A 1 233 ? 18.668  -12.434 4.430   1.00 32.99  ? 218 VAL   A CA   1 
ATOM   3339 C C    . VAL   A 1 233 ? 17.587  -12.181 5.478   1.00 35.79  ? 218 VAL   A C    1 
ATOM   3340 O O    . VAL   A 1 233 ? 17.384  -11.044 5.911   1.00 32.44  ? 218 VAL   A O    1 
ATOM   3341 C CB   . VAL   A 1 233 ? 20.052  -12.577 5.094   1.00 32.36  ? 218 VAL   A CB   1 
ATOM   3342 C CG1  . VAL   A 1 233 ? 20.065  -13.763 6.049   1.00 33.89  ? 218 VAL   A CG1  1 
ATOM   3343 C CG2  . VAL   A 1 233 ? 21.135  -12.727 4.033   1.00 32.71  ? 218 VAL   A CG2  1 
ATOM   3344 H H    . VAL   A 1 233 ? 18.998  -10.612 3.791   1.00 40.23  ? 218 VAL   A H    1 
ATOM   3345 H HA   . VAL   A 1 233 ? 18.461  -13.262 3.970   1.00 39.58  ? 218 VAL   A HA   1 
ATOM   3346 H HB   . VAL   A 1 233 ? 20.240  -11.777 5.608   1.00 38.83  ? 218 VAL   A HB   1 
ATOM   3347 H HG11 . VAL   A 1 233 ? 20.979  -13.939 6.322   1.00 40.67  ? 218 VAL   A HG11 1 
ATOM   3348 H HG12 . VAL   A 1 233 ? 19.523  -13.550 6.825   1.00 40.67  ? 218 VAL   A HG12 1 
ATOM   3349 H HG13 . VAL   A 1 233 ? 19.700  -14.538 5.594   1.00 40.67  ? 218 VAL   A HG13 1 
ATOM   3350 H HG21 . VAL   A 1 233 ? 21.983  -12.905 4.469   1.00 39.25  ? 218 VAL   A HG21 1 
ATOM   3351 H HG22 . VAL   A 1 233 ? 20.904  -13.465 3.447   1.00 39.25  ? 218 VAL   A HG22 1 
ATOM   3352 H HG23 . VAL   A 1 233 ? 21.192  -11.904 3.522   1.00 39.25  ? 218 VAL   A HG23 1 
ATOM   3353 N N    . HIS   A 1 234 ? 16.916  -13.250 5.883   1.00 38.65  ? 219 HIS   A N    1 
ATOM   3354 C CA   . HIS   A 1 234 ? 15.808  -13.116 6.818   1.00 36.44  ? 219 HIS   A CA   1 
ATOM   3355 C C    . HIS   A 1 234 ? 16.266  -12.360 8.063   1.00 35.17  ? 219 HIS   A C    1 
ATOM   3356 O O    . HIS   A 1 234 ? 17.342  -12.644 8.604   1.00 34.85  ? 219 HIS   A O    1 
ATOM   3357 C CB   . HIS   A 1 234 ? 15.271  -14.495 7.207   1.00 39.47  ? 219 HIS   A CB   1 
ATOM   3358 C CG   . HIS   A 1 234 ? 13.985  -14.440 7.966   1.00 39.75  ? 219 HIS   A CG   1 
ATOM   3359 N ND1  . HIS   A 1 234 ? 13.934  -14.218 9.324   1.00 41.15  ? 219 HIS   A ND1  1 
ATOM   3360 C CD2  . HIS   A 1 234 ? 12.702  -14.566 7.555   1.00 43.82  ? 219 HIS   A CD2  1 
ATOM   3361 C CE1  . HIS   A 1 234 ? 12.673  -14.217 9.720   1.00 45.93  ? 219 HIS   A CE1  1 
ATOM   3362 N NE2  . HIS   A 1 234 ? 11.906  -14.425 8.666   1.00 50.37  ? 219 HIS   A NE2  1 
ATOM   3363 H H    . HIS   A 1 234 ? 17.079  -14.057 5.634   1.00 46.37  ? 219 HIS   A H    1 
ATOM   3364 H HA   . HIS   A 1 234 ? 15.090  -12.616 6.401   1.00 43.73  ? 219 HIS   A HA   1 
ATOM   3365 H HB2  . HIS   A 1 234 ? 15.118  -15.010 6.400   1.00 47.37  ? 219 HIS   A HB2  1 
ATOM   3366 H HB3  . HIS   A 1 234 ? 15.927  -14.940 7.766   1.00 47.37  ? 219 HIS   A HB3  1 
ATOM   3367 H HD2  . HIS   A 1 234 ? 12.413  -14.719 6.685   1.00 52.59  ? 219 HIS   A HD2  1 
ATOM   3368 H HE1  . HIS   A 1 234 ? 12.377  -14.092 10.593  1.00 55.12  ? 219 HIS   A HE1  1 
ATOM   3369 H HE2  . HIS   A 1 234 ? 11.047  -14.465 8.673   1.00 60.45  ? 219 HIS   A HE2  1 
ATOM   3370 N N    . PRO   A 1 235 ? 15.474  -11.407 8.552   1.00 34.81  ? 220 PRO   A N    1 
ATOM   3371 C CA   . PRO   A 1 235 ? 15.941  -10.593 9.687   1.00 33.82  ? 220 PRO   A CA   1 
ATOM   3372 C C    . PRO   A 1 235 ? 16.312  -11.412 10.906  1.00 34.92  ? 220 PRO   A C    1 
ATOM   3373 O O    . PRO   A 1 235 ? 17.282  -11.088 11.598  1.00 36.60  ? 220 PRO   A O    1 
ATOM   3374 C CB   . PRO   A 1 235 ? 14.750  -9.668  9.962   1.00 33.86  ? 220 PRO   A CB   1 
ATOM   3375 C CG   . PRO   A 1 235 ? 13.593  -10.299 9.318   1.00 38.15  ? 220 PRO   A CG   1 
ATOM   3376 C CD   . PRO   A 1 235 ? 14.116  -11.036 8.127   1.00 36.86  ? 220 PRO   A CD   1 
ATOM   3377 H HA   . PRO   A 1 235 ? 16.707  -10.063 9.416   1.00 40.59  ? 220 PRO   A HA   1 
ATOM   3378 H HB2  . PRO   A 1 235 ? 14.610  -9.590  10.919  1.00 40.64  ? 220 PRO   A HB2  1 
ATOM   3379 H HB3  . PRO   A 1 235 ? 14.921  -8.793  9.580   1.00 40.64  ? 220 PRO   A HB3  1 
ATOM   3380 H HG2  . PRO   A 1 235 ? 13.170  -10.912 9.939   1.00 45.78  ? 220 PRO   A HG2  1 
ATOM   3381 H HG3  . PRO   A 1 235 ? 12.961  -9.615  9.045   1.00 45.78  ? 220 PRO   A HG3  1 
ATOM   3382 H HD2  . PRO   A 1 235 ? 13.582  -11.824 7.943   1.00 44.23  ? 220 PRO   A HD2  1 
ATOM   3383 H HD3  . PRO   A 1 235 ? 14.141  -10.461 7.346   1.00 44.23  ? 220 PRO   A HD3  1 
ATOM   3384 N N    . LEU   A 1 236 ? 15.565  -12.473 11.195  1.00 36.93  ? 221 LEU   A N    1 
ATOM   3385 C CA   . LEU   A 1 236 ? 15.906  -13.309 12.338  1.00 40.35  ? 221 LEU   A CA   1 
ATOM   3386 C C    . LEU   A 1 236 ? 17.264  -13.969 12.127  1.00 40.92  ? 221 LEU   A C    1 
ATOM   3387 O O    . LEU   A 1 236 ? 18.122  -13.953 13.015  1.00 39.82  ? 221 LEU   A O    1 
ATOM   3388 C CB   . LEU   A 1 236 ? 14.804  -14.347 12.555  1.00 42.75  ? 221 LEU   A CB   1 
ATOM   3389 C CG   . LEU   A 1 236 ? 14.495  -14.781 13.984  1.00 45.71  ? 221 LEU   A CG   1 
ATOM   3390 C CD1  . LEU   A 1 236 ? 14.347  -13.589 14.926  1.00 49.46  ? 221 LEU   A CD1  1 
ATOM   3391 C CD2  . LEU   A 1 236 ? 13.228  -15.608 13.990  1.00 51.94  ? 221 LEU   A CD2  1 
ATOM   3392 H H    . LEU   A 1 236 ? 14.870  -12.725 10.754  1.00 44.31  ? 221 LEU   A H    1 
ATOM   3393 H HA   . LEU   A 1 236 ? 15.961  -12.766 13.140  1.00 48.42  ? 221 LEU   A HA   1 
ATOM   3394 H HB2  . LEU   A 1 236 ? 13.982  -13.984 12.191  1.00 51.30  ? 221 LEU   A HB2  1 
ATOM   3395 H HB3  . LEU   A 1 236 ? 15.056  -15.148 12.070  1.00 51.30  ? 221 LEU   A HB3  1 
ATOM   3396 H HG   . LEU   A 1 236 ? 15.237  -15.311 14.314  1.00 54.85  ? 221 LEU   A HG   1 
ATOM   3397 H HD11 . LEU   A 1 236 ? 13.859  -13.870 15.716  1.00 59.35  ? 221 LEU   A HD11 1 
ATOM   3398 H HD12 . LEU   A 1 236 ? 15.229  -13.272 15.177  1.00 59.35  ? 221 LEU   A HD12 1 
ATOM   3399 H HD13 . LEU   A 1 236 ? 13.860  -12.884 14.470  1.00 59.35  ? 221 LEU   A HD13 1 
ATOM   3400 H HD21 . LEU   A 1 236 ? 13.262  -16.233 14.731  1.00 62.33  ? 221 LEU   A HD21 1 
ATOM   3401 H HD22 . LEU   A 1 236 ? 12.465  -15.017 14.092  1.00 62.33  ? 221 LEU   A HD22 1 
ATOM   3402 H HD23 . LEU   A 1 236 ? 13.162  -16.091 13.152  1.00 62.33  ? 221 LEU   A HD23 1 
ATOM   3403 N N    . ARG   A 1 237 ? 17.492  -14.525 10.938  1.00 38.05  ? 222 ARG   A N    1 
ATOM   3404 C CA   . ARG   A 1 237 ? 18.783  -15.143 10.662  1.00 37.94  ? 222 ARG   A CA   1 
ATOM   3405 C C    . ARG   A 1 237 ? 19.918  -14.128 10.745  1.00 35.96  ? 222 ARG   A C    1 
ATOM   3406 O O    . ARG   A 1 237 ? 21.011  -14.450 11.229  1.00 36.10  ? 222 ARG   A O    1 
ATOM   3407 C CB   . ARG   A 1 237 ? 18.756  -15.810 9.292   1.00 44.37  ? 222 ARG   A CB   1 
ATOM   3408 C CG   . ARG   A 1 237 ? 20.051  -16.513 8.930   1.00 41.80  ? 222 ARG   A CG   1 
ATOM   3409 C CD   . ARG   A 1 237 ? 19.844  -17.494 7.790   1.00 43.27  ? 222 ARG   A CD   1 
ATOM   3410 N NE   . ARG   A 1 237 ? 19.086  -18.671 8.194   1.00 49.41  ? 222 ARG   A NE   1 
ATOM   3411 C CZ   . ARG   A 1 237 ? 17.832  -18.940 7.844   1.00 54.42  ? 222 ARG   A CZ   1 
ATOM   3412 N NH1  . ARG   A 1 237 ? 17.135  -18.130 7.064   1.00 49.78  ? 222 ARG   A NH1  1 
ATOM   3413 N NH2  . ARG   A 1 237 ? 17.264  -20.056 8.287   1.00 61.77  ? 222 ARG   A NH2  1 
ATOM   3414 H H    . ARG   A 1 237 ? 16.928  -14.557 10.289  1.00 45.67  ? 222 ARG   A H    1 
ATOM   3415 H HA   . ARG   A 1 237 ? 18.951  -15.827 11.329  1.00 45.52  ? 222 ARG   A HA   1 
ATOM   3416 H HB2  . ARG   A 1 237 ? 18.046  -16.472 9.281   1.00 53.25  ? 222 ARG   A HB2  1 
ATOM   3417 H HB3  . ARG   A 1 237 ? 18.588  -15.133 8.618   1.00 53.25  ? 222 ARG   A HB3  1 
ATOM   3418 H HG2  . ARG   A 1 237 ? 20.709  -15.856 8.653   1.00 50.16  ? 222 ARG   A HG2  1 
ATOM   3419 H HG3  . ARG   A 1 237 ? 20.378  -17.004 9.700   1.00 50.16  ? 222 ARG   A HG3  1 
ATOM   3420 H HD2  . ARG   A 1 237 ? 19.355  -17.052 7.077   1.00 51.92  ? 222 ARG   A HD2  1 
ATOM   3421 H HD3  . ARG   A 1 237 ? 20.708  -17.790 7.465   1.00 51.92  ? 222 ARG   A HD3  1 
ATOM   3422 H HE   . ARG   A 1 237 ? 19.483  -19.240 8.702   1.00 59.29  ? 222 ARG   A HE   1 
ATOM   3423 H HH11 . ARG   A 1 237 ? 17.491  -17.405 6.768   1.00 59.74  ? 222 ARG   A HH11 1 
ATOM   3424 H HH12 . ARG   A 1 237 ? 16.325  -18.328 6.853   1.00 59.74  ? 222 ARG   A HH12 1 
ATOM   3425 H HH21 . ARG   A 1 237 ? 17.707  -20.593 8.792   1.00 74.13  ? 222 ARG   A HH21 1 
ATOM   3426 H HH22 . ARG   A 1 237 ? 16.453  -20.242 8.068   1.00 74.13  ? 222 ARG   A HH22 1 
ATOM   3427 N N    . VAL   A 1 238 ? 19.685  -12.900 10.282  1.00 35.40  ? 223 VAL   A N    1 
ATOM   3428 C CA   . VAL   A 1 238 ? 20.713  -11.867 10.418  1.00 33.19  ? 223 VAL   A CA   1 
ATOM   3429 C C    . VAL   A 1 238 ? 21.046  -11.656 11.891  1.00 36.41  ? 223 VAL   A C    1 
ATOM   3430 O O    . VAL   A 1 238 ? 22.217  -11.622 12.284  1.00 32.59  ? 223 VAL   A O    1 
ATOM   3431 C CB   . VAL   A 1 238 ? 20.260  -10.559 9.747   1.00 31.03  ? 223 VAL   A CB   1 
ATOM   3432 C CG1  . VAL   A 1 238 ? 21.265  -9.468  10.021  1.00 29.86  ? 223 VAL   A CG1  1 
ATOM   3433 C CG2  . VAL   A 1 238 ? 20.084  -10.761 8.252   1.00 32.99  ? 223 VAL   A CG2  1 
ATOM   3434 H H    . VAL   A 1 238 ? 18.961  -12.644 9.896   1.00 42.48  ? 223 VAL   A H    1 
ATOM   3435 H HA   . VAL   A 1 238 ? 21.517  -12.166 9.965   1.00 39.83  ? 223 VAL   A HA   1 
ATOM   3436 H HB   . VAL   A 1 238 ? 19.403  -10.291 10.115  1.00 37.24  ? 223 VAL   A HB   1 
ATOM   3437 H HG11 . VAL   A 1 238 ? 21.120  -8.741  9.396   1.00 35.83  ? 223 VAL   A HG11 1 
ATOM   3438 H HG12 . VAL   A 1 238 ? 21.146  -9.150  10.930  1.00 35.83  ? 223 VAL   A HG12 1 
ATOM   3439 H HG13 . VAL   A 1 238 ? 22.159  -9.827  9.910   1.00 35.83  ? 223 VAL   A HG13 1 
ATOM   3440 H HG21 . VAL   A 1 238 ? 19.940  -9.899  7.831   1.00 39.59  ? 223 VAL   A HG21 1 
ATOM   3441 H HG22 . VAL   A 1 238 ? 20.885  -11.174 7.893   1.00 39.59  ? 223 VAL   A HG22 1 
ATOM   3442 H HG23 . VAL   A 1 238 ? 19.318  -11.336 8.098   1.00 39.59  ? 223 VAL   A HG23 1 
ATOM   3443 N N    . LEU   A 1 239 ? 20.010  -11.513 12.726  1.00 35.36  ? 224 LEU   A N    1 
ATOM   3444 C CA   . LEU   A 1 239 ? 20.206  -11.380 14.169  1.00 41.43  ? 224 LEU   A CA   1 
ATOM   3445 C C    . LEU   A 1 239 ? 21.041  -12.533 14.719  1.00 38.61  ? 224 LEU   A C    1 
ATOM   3446 O O    . LEU   A 1 239 ? 21.994  -12.319 15.476  1.00 37.05  ? 224 LEU   A O    1 
ATOM   3447 C CB   . LEU   A 1 239 ? 18.847  -11.322 14.881  1.00 42.85  ? 224 LEU   A CB   1 
ATOM   3448 C CG   . LEU   A 1 239 ? 18.152  -9.957  14.870  1.00 45.59  ? 224 LEU   A CG   1 
ATOM   3449 C CD1  . LEU   A 1 239 ? 16.722  -10.063 15.351  1.00 41.24  ? 224 LEU   A CD1  1 
ATOM   3450 C CD2  . LEU   A 1 239 ? 18.921  -8.951  15.728  1.00 39.93  ? 224 LEU   A CD2  1 
ATOM   3451 H H    . LEU   A 1 239 ? 19.186  -11.490 12.481  1.00 42.43  ? 224 LEU   A H    1 
ATOM   3452 H HA   . LEU   A 1 239 ? 20.679  -10.551 14.342  1.00 49.72  ? 224 LEU   A HA   1 
ATOM   3453 H HB2  . LEU   A 1 239 ? 18.251  -11.954 14.450  1.00 51.43  ? 224 LEU   A HB2  1 
ATOM   3454 H HB3  . LEU   A 1 239 ? 18.980  -11.570 15.809  1.00 51.43  ? 224 LEU   A HB3  1 
ATOM   3455 H HG   . LEU   A 1 239 ? 18.135  -9.634  13.955  1.00 54.71  ? 224 LEU   A HG   1 
ATOM   3456 H HD11 . LEU   A 1 239 ? 16.314  -9.183  15.326  1.00 49.49  ? 224 LEU   A HD11 1 
ATOM   3457 H HD12 . LEU   A 1 239 ? 16.237  -10.669 14.769  1.00 49.49  ? 224 LEU   A HD12 1 
ATOM   3458 H HD13 . LEU   A 1 239 ? 16.719  -10.403 16.259  1.00 49.49  ? 224 LEU   A HD13 1 
ATOM   3459 H HD21 . LEU   A 1 239 ? 18.392  -8.143  15.818  1.00 47.91  ? 224 LEU   A HD21 1 
ATOM   3460 H HD22 . LEU   A 1 239 ? 19.083  -9.339  16.602  1.00 47.91  ? 224 LEU   A HD22 1 
ATOM   3461 H HD23 . LEU   A 1 239 ? 19.765  -8.747  15.295  1.00 47.91  ? 224 LEU   A HD23 1 
ATOM   3462 N N    . PHE   A 1 240 ? 20.686  -13.767 14.351  1.00 37.21  ? 225 PHE   A N    1 
ATOM   3463 C CA   . PHE   A 1 240 ? 21.477  -14.917 14.772  1.00 38.79  ? 225 PHE   A CA   1 
ATOM   3464 C C    . PHE   A 1 240 ? 22.938  -14.751 14.358  1.00 42.55  ? 225 PHE   A C    1 
ATOM   3465 O O    . PHE   A 1 240 ? 23.848  -14.865 15.187  1.00 38.38  ? 225 PHE   A O    1 
ATOM   3466 C CB   . PHE   A 1 240 ? 20.896  -16.205 14.179  1.00 46.11  ? 225 PHE   A CB   1 
ATOM   3467 C CG   . PHE   A 1 240 ? 19.549  -16.607 14.749  1.00 42.14  ? 225 PHE   A CG   1 
ATOM   3468 C CD1  . PHE   A 1 240 ? 19.021  -15.983 15.868  1.00 50.79  ? 225 PHE   A CD1  1 
ATOM   3469 C CD2  . PHE   A 1 240 ? 18.818  -17.629 14.159  1.00 60.95  ? 225 PHE   A CD2  1 
ATOM   3470 C CE1  . PHE   A 1 240 ? 17.788  -16.365 16.384  1.00 57.01  ? 225 PHE   A CE1  1 
ATOM   3471 C CE2  . PHE   A 1 240 ? 17.584  -18.020 14.673  1.00 52.55  ? 225 PHE   A CE2  1 
ATOM   3472 C CZ   . PHE   A 1 240 ? 17.071  -17.387 15.784  1.00 46.78  ? 225 PHE   A CZ   1 
ATOM   3473 H H    . PHE   A 1 240 ? 20.002  -13.959 13.866  1.00 44.65  ? 225 PHE   A H    1 
ATOM   3474 H HA   . PHE   A 1 240 ? 21.436  -14.986 15.738  1.00 46.55  ? 225 PHE   A HA   1 
ATOM   3475 H HB2  . PHE   A 1 240 ? 20.786  -16.084 13.223  1.00 55.33  ? 225 PHE   A HB2  1 
ATOM   3476 H HB3  . PHE   A 1 240 ? 21.515  -16.932 14.352  1.00 55.33  ? 225 PHE   A HB3  1 
ATOM   3477 H HD1  . PHE   A 1 240 ? 19.498  -15.299 16.280  1.00 60.94  ? 225 PHE   A HD1  1 
ATOM   3478 H HD2  . PHE   A 1 240 ? 19.158  -18.060 13.408  1.00 73.14  ? 225 PHE   A HD2  1 
ATOM   3479 H HE1  . PHE   A 1 240 ? 17.444  -15.933 17.132  1.00 68.41  ? 225 PHE   A HE1  1 
ATOM   3480 H HE2  . PHE   A 1 240 ? 17.106  -18.707 14.267  1.00 63.06  ? 225 PHE   A HE2  1 
ATOM   3481 H HZ   . PHE   A 1 240 ? 16.247  -17.644 16.130  1.00 56.14  ? 225 PHE   A HZ   1 
ATOM   3482 N N    . LEU   A 1 241 ? 23.181  -14.463 13.077  1.00 40.77  ? 226 LEU   A N    1 
ATOM   3483 C CA   . LEU   A 1 241 ? 24.555  -14.349 12.597  1.00 35.63  ? 226 LEU   A CA   1 
ATOM   3484 C C    . LEU   A 1 241 ? 25.290  -13.194 13.266  1.00 46.89  ? 226 LEU   A C    1 
ATOM   3485 O O    . LEU   A 1 241 ? 26.468  -13.327 13.624  1.00 42.04  ? 226 LEU   A O    1 
ATOM   3486 C CB   . LEU   A 1 241 ? 24.561  -14.172 11.081  1.00 41.79  ? 226 LEU   A CB   1 
ATOM   3487 C CG   . LEU   A 1 241 ? 24.097  -15.380 10.258  1.00 49.00  ? 226 LEU   A CG   1 
ATOM   3488 C CD1  . LEU   A 1 241 ? 24.102  -15.027 8.783   1.00 44.30  ? 226 LEU   A CD1  1 
ATOM   3489 C CD2  . LEU   A 1 241 ? 24.970  -16.594 10.533  1.00 46.66  ? 226 LEU   A CD2  1 
ATOM   3490 H H    . LEU   A 1 241 ? 22.578  -14.331 12.478  1.00 48.93  ? 226 LEU   A H    1 
ATOM   3491 H HA   . LEU   A 1 241 ? 25.026  -15.169 12.815  1.00 42.75  ? 226 LEU   A HA   1 
ATOM   3492 H HB2  . LEU   A 1 241 ? 23.973  -13.433 10.861  1.00 50.15  ? 226 LEU   A HB2  1 
ATOM   3493 H HB3  . LEU   A 1 241 ? 25.468  -13.969 10.804  1.00 50.15  ? 226 LEU   A HB3  1 
ATOM   3494 H HG   . LEU   A 1 241 ? 23.192  -15.616 10.514  1.00 58.80  ? 226 LEU   A HG   1 
ATOM   3495 H HD11 . LEU   A 1 241 ? 23.808  -15.798 8.273   1.00 53.16  ? 226 LEU   A HD11 1 
ATOM   3496 H HD12 . LEU   A 1 241 ? 23.497  -14.283 8.635   1.00 53.16  ? 226 LEU   A HD12 1 
ATOM   3497 H HD13 . LEU   A 1 241 ? 25.002  -14.779 8.521   1.00 53.16  ? 226 LEU   A HD13 1 
ATOM   3498 H HD21 . LEU   A 1 241 ? 24.774  -17.279 9.875   1.00 56.00  ? 226 LEU   A HD21 1 
ATOM   3499 H HD22 . LEU   A 1 241 ? 25.902  -16.332 10.472  1.00 56.00  ? 226 LEU   A HD22 1 
ATOM   3500 H HD23 . LEU   A 1 241 ? 24.777  -16.926 11.424  1.00 56.00  ? 226 LEU   A HD23 1 
ATOM   3501 N N    . MET   A 1 242 ? 24.614  -12.052 13.443  1.00 39.09  ? 227 MET   A N    1 
ATOM   3502 C CA   . MET   A 1 242 ? 25.273  -10.863 13.973  1.00 41.07  ? 227 MET   A CA   1 
ATOM   3503 C C    . MET   A 1 242 ? 25.880  -11.090 15.349  1.00 44.35  ? 227 MET   A C    1 
ATOM   3504 O O    . MET   A 1 242 ? 26.876  -10.446 15.700  1.00 48.61  ? 227 MET   A O    1 
ATOM   3505 C CB   . MET   A 1 242 ? 24.284  -9.714  14.090  1.00 48.39  ? 227 MET   A CB   1 
ATOM   3506 C CG   . MET   A 1 242 ? 23.811  -9.137  12.801  1.00 55.95  ? 227 MET   A CG   1 
ATOM   3507 S SD   . MET   A 1 242 ? 22.837  -7.705  13.252  1.00 44.13  ? 227 MET   A SD   1 
ATOM   3508 C CE   . MET   A 1 242 ? 24.182  -6.576  13.617  1.00 32.10  ? 227 MET   A CE   1 
ATOM   3509 H H    . MET   A 1 242 ? 23.780  -11.943 13.263  1.00 46.90  ? 227 MET   A H    1 
ATOM   3510 H HA   . MET   A 1 242 ? 25.972  -10.631 13.342  1.00 49.28  ? 227 MET   A HA   1 
ATOM   3511 H HB2  . MET   A 1 242 ? 23.502  -10.033 14.567  1.00 58.07  ? 227 MET   A HB2  1 
ATOM   3512 H HB3  . MET   A 1 242 ? 24.707  -8.997  14.588  1.00 58.07  ? 227 MET   A HB3  1 
ATOM   3513 H HG2  . MET   A 1 242 ? 24.561  -8.867  12.249  1.00 67.14  ? 227 MET   A HG2  1 
ATOM   3514 H HG3  . MET   A 1 242 ? 23.259  -9.774  12.321  1.00 67.14  ? 227 MET   A HG3  1 
ATOM   3515 H HE1  . MET   A 1 242 ? 24.065  -6.226  14.515  1.00 38.52  ? 227 MET   A HE1  1 
ATOM   3516 H HE2  . MET   A 1 242 ? 25.023  -7.055  13.555  1.00 38.52  ? 227 MET   A HE2  1 
ATOM   3517 H HE3  . MET   A 1 242 ? 24.167  -5.849  12.975  1.00 38.52  ? 227 MET   A HE3  1 
ATOM   3518 N N    . THR   A 1 243 ? 25.274  -11.954 16.156  1.00 44.37  ? 228 THR   A N    1 
ATOM   3519 C CA   . THR   A 1 243 ? 25.673  -12.126 17.543  1.00 52.92  ? 228 THR   A CA   1 
ATOM   3520 C C    . THR   A 1 243 ? 26.534  -13.362 17.760  1.00 54.04  ? 228 THR   A C    1 
ATOM   3521 O O    . THR   A 1 243 ? 26.857  -13.681 18.908  1.00 66.08  ? 228 THR   A O    1 
ATOM   3522 C CB   . THR   A 1 243 ? 24.433  -12.173 18.439  1.00 48.03  ? 228 THR   A CB   1 
ATOM   3523 O OG1  . THR   A 1 243 ? 23.499  -13.127 17.921  1.00 58.38  ? 228 THR   A OG1  1 
ATOM   3524 C CG2  . THR   A 1 243 ? 23.769  -10.795 18.493  1.00 48.61  ? 228 THR   A CG2  1 
ATOM   3525 H H    . THR   A 1 243 ? 24.619  -12.458 15.917  1.00 53.24  ? 228 THR   A H    1 
ATOM   3526 H HA   . THR   A 1 243 ? 26.203  -11.359 17.811  1.00 63.50  ? 228 THR   A HA   1 
ATOM   3527 H HB   . THR   A 1 243 ? 24.690  -12.431 19.338  1.00 57.64  ? 228 THR   A HB   1 
ATOM   3528 H HG1  . THR   A 1 243 ? 23.204  -12.866 17.179  1.00 70.06  ? 228 THR   A HG1  1 
ATOM   3529 H HG21 . THR   A 1 243 ? 22.962  -10.836 19.030  1.00 58.33  ? 228 THR   A HG21 1 
ATOM   3530 H HG22 . THR   A 1 243 ? 24.377  -10.150 18.887  1.00 58.33  ? 228 THR   A HG22 1 
ATOM   3531 H HG23 . THR   A 1 243 ? 23.538  -10.503 17.597  1.00 58.33  ? 228 THR   A HG23 1 
ATOM   3532 N N    . LYS   A 1 244 ? 26.911  -14.064 16.694  1.00 56.14  ? 229 LYS   A N    1 
ATOM   3533 C CA   . LYS   A 1 244 ? 27.930  -15.099 16.815  1.00 53.52  ? 229 LYS   A CA   1 
ATOM   3534 C C    . LYS   A 1 244 ? 29.292  -14.444 17.021  1.00 56.21  ? 229 LYS   A C    1 
ATOM   3535 O O    . LYS   A 1 244 ? 29.578  -13.375 16.477  1.00 55.84  ? 229 LYS   A O    1 
ATOM   3536 C CB   . LYS   A 1 244 ? 27.957  -15.981 15.568  1.00 48.38  ? 229 LYS   A CB   1 
ATOM   3537 C CG   . LYS   A 1 244 ? 26.643  -16.675 15.262  1.00 55.15  ? 229 LYS   A CG   1 
ATOM   3538 C CD   . LYS   A 1 244 ? 26.488  -17.980 16.033  1.00 54.84  ? 229 LYS   A CD   1 
ATOM   3539 C CE   . LYS   A 1 244 ? 25.140  -18.628 15.746  1.00 72.26  ? 229 LYS   A CE   1 
ATOM   3540 N NZ   . LYS   A 1 244 ? 24.874  -18.760 14.282  1.00 70.70  ? 229 LYS   A NZ   1 
ATOM   3541 H H    . LYS   A 1 244 ? 26.595  -13.962 15.901  1.00 67.37  ? 229 LYS   A H    1 
ATOM   3542 H HA   . LYS   A 1 244 ? 27.734  -15.673 17.572  1.00 64.23  ? 229 LYS   A HA   1 
ATOM   3543 H HB2  . LYS   A 1 244 ? 28.181  -15.428 14.803  1.00 58.05  ? 229 LYS   A HB2  1 
ATOM   3544 H HB3  . LYS   A 1 244 ? 28.630  -16.668 15.690  1.00 58.05  ? 229 LYS   A HB3  1 
ATOM   3545 H HG2  . LYS   A 1 244 ? 25.909  -16.091 15.507  1.00 66.18  ? 229 LYS   A HG2  1 
ATOM   3546 H HG3  . LYS   A 1 244 ? 26.603  -16.878 14.314  1.00 66.18  ? 229 LYS   A HG3  1 
ATOM   3547 H HD2  . LYS   A 1 244 ? 27.188  -18.596 15.768  1.00 65.80  ? 229 LYS   A HD2  1 
ATOM   3548 H HD3  . LYS   A 1 244 ? 26.546  -17.801 16.985  1.00 65.80  ? 229 LYS   A HD3  1 
ATOM   3549 H HE2  . LYS   A 1 244 ? 25.124  -19.516 16.136  1.00 86.71  ? 229 LYS   A HE2  1 
ATOM   3550 H HE3  . LYS   A 1 244 ? 24.436  -18.083 16.132  1.00 86.71  ? 229 LYS   A HE3  1 
ATOM   3551 H HZ1  . LYS   A 1 244 ? 24.119  -19.211 14.149  1.00 84.84  ? 229 LYS   A HZ1  1 
ATOM   3552 H HZ2  . LYS   A 1 244 ? 24.798  -17.954 13.912  1.00 84.84  ? 229 LYS   A HZ2  1 
ATOM   3553 H HZ3  . LYS   A 1 244 ? 25.543  -19.196 13.889  1.00 84.84  ? 229 LYS   A HZ3  1 
ATOM   3554 N N    . SER   A 1 245 ? 30.143  -15.095 17.820  1.00 66.49  ? 230 SER   A N    1 
ATOM   3555 C CA   . SER   A 1 245 ? 31.450  -14.511 18.109  1.00 59.77  ? 230 SER   A CA   1 
ATOM   3556 C C    . SER   A 1 245 ? 32.321  -14.429 16.862  1.00 57.87  ? 230 SER   A C    1 
ATOM   3557 O O    . SER   A 1 245 ? 33.200  -13.564 16.780  1.00 66.82  ? 230 SER   A O    1 
ATOM   3558 C CB   . SER   A 1 245 ? 32.152  -15.320 19.192  1.00 66.87  ? 230 SER   A CB   1 
ATOM   3559 O OG   . SER   A 1 245 ? 32.364  -16.647 18.754  1.00 63.78  ? 230 SER   A OG   1 
ATOM   3560 H H    . SER   A 1 245 ? 29.990  -15.854 18.195  1.00 79.79  ? 230 SER   A H    1 
ATOM   3561 H HA   . SER   A 1 245 ? 31.320  -13.609 18.442  1.00 71.73  ? 230 SER   A HA   1 
ATOM   3562 H HB2  . SER   A 1 245 ? 33.009  -14.910 19.390  1.00 80.24  ? 230 SER   A HB2  1 
ATOM   3563 H HB3  . SER   A 1 245 ? 31.599  -15.333 19.989  1.00 80.24  ? 230 SER   A HB3  1 
ATOM   3564 H HG   . SER   A 1 245 ? 32.734  -17.095 19.361  1.00 76.54  ? 230 SER   A HG   1 
ATOM   3565 N N    . GLY   A 1 246 ? 32.093  -15.307 15.885  1.00 57.33  ? 231 GLY   A N    1 
ATOM   3566 C CA   . GLY   A 1 246 ? 32.824  -15.267 14.636  1.00 49.08  ? 231 GLY   A CA   1 
ATOM   3567 C C    . GLY   A 1 246 ? 32.346  -14.243 13.632  1.00 47.05  ? 231 GLY   A C    1 
ATOM   3568 O O    . GLY   A 1 246 ? 32.900  -14.165 12.532  1.00 37.05  ? 231 GLY   A O    1 
ATOM   3569 H H    . GLY   A 1 246 ? 31.512  -15.939 15.929  1.00 68.79  ? 231 GLY   A H    1 
ATOM   3570 H HA2  . GLY   A 1 246 ? 33.755  -15.075 14.830  1.00 58.89  ? 231 GLY   A HA2  1 
ATOM   3571 H HA3  . GLY   A 1 246 ? 32.762  -16.140 14.216  1.00 58.89  ? 231 GLY   A HA3  1 
ATOM   3572 N N    . TYR   A 1 247 ? 31.345  -13.436 13.979  1.00 41.97  ? 232 TYR   A N    1 
ATOM   3573 C CA   . TYR   A 1 247 ? 30.750  -12.538 13.000  1.00 43.35  ? 232 TYR   A CA   1 
ATOM   3574 C C    . TYR   A 1 247 ? 31.802  -11.628 12.379  1.00 36.02  ? 232 TYR   A C    1 
ATOM   3575 O O    . TYR   A 1 247 ? 32.607  -11.018 13.085  1.00 40.06  ? 232 TYR   A O    1 
ATOM   3576 C CB   . TYR   A 1 247 ? 29.655  -11.690 13.644  1.00 43.57  ? 232 TYR   A CB   1 
ATOM   3577 C CG   . TYR   A 1 247 ? 28.939  -10.791 12.661  1.00 38.84  ? 232 TYR   A CG   1 
ATOM   3578 C CD1  . TYR   A 1 247 ? 28.369  -11.310 11.504  1.00 40.90  ? 232 TYR   A CD1  1 
ATOM   3579 C CD2  . TYR   A 1 247 ? 28.827  -9.427  12.891  1.00 36.50  ? 232 TYR   A CD2  1 
ATOM   3580 C CE1  . TYR   A 1 247 ? 27.711  -10.497 10.606  1.00 42.30  ? 232 TYR   A CE1  1 
ATOM   3581 C CE2  . TYR   A 1 247 ? 28.165  -8.602  11.996  1.00 37.41  ? 232 TYR   A CE2  1 
ATOM   3582 C CZ   . TYR   A 1 247 ? 27.608  -9.145  10.857  1.00 39.94  ? 232 TYR   A CZ   1 
ATOM   3583 O OH   . TYR   A 1 247 ? 26.949  -8.334  9.961   1.00 35.42  ? 232 TYR   A OH   1 
ATOM   3584 H H    . TYR   A 1 247 ? 30.998  -13.392 14.765  1.00 50.36  ? 232 TYR   A H    1 
ATOM   3585 H HA   . TYR   A 1 247 ? 30.352  -13.075 12.297  1.00 52.02  ? 232 TYR   A HA   1 
ATOM   3586 H HB2  . TYR   A 1 247 ? 28.996  -12.279 14.043  1.00 52.29  ? 232 TYR   A HB2  1 
ATOM   3587 H HB3  . TYR   A 1 247 ? 30.054  -11.128 14.326  1.00 52.29  ? 232 TYR   A HB3  1 
ATOM   3588 H HD1  . TYR   A 1 247 ? 28.432  -12.222 11.333  1.00 49.09  ? 232 TYR   A HD1  1 
ATOM   3589 H HD2  . TYR   A 1 247 ? 29.202  -9.060  13.659  1.00 43.79  ? 232 TYR   A HD2  1 
ATOM   3590 H HE1  . TYR   A 1 247 ? 27.337  -10.859 9.834   1.00 50.76  ? 232 TYR   A HE1  1 
ATOM   3591 H HE2  . TYR   A 1 247 ? 28.097  -7.689  12.161  1.00 44.89  ? 232 TYR   A HE2  1 
ATOM   3592 H HH   . TYR   A 1 247 ? 26.655  -8.793  9.321   1.00 42.51  ? 232 TYR   A HH   1 
ATOM   3593 N N    . GLN   A 1 248 ? 31.787  -11.547 11.049  1.00 37.31  ? 233 GLN   A N    1 
ATOM   3594 C CA   . GLN   A 1 248 ? 32.678  -10.673 10.307  1.00 34.46  ? 233 GLN   A CA   1 
ATOM   3595 C C    . GLN   A 1 248 ? 31.935  -9.399  9.943   1.00 37.08  ? 233 GLN   A C    1 
ATOM   3596 O O    . GLN   A 1 248 ? 30.884  -9.485  9.288   1.00 32.62  ? 233 GLN   A O    1 
ATOM   3597 C CB   . GLN   A 1 248 ? 33.169  -11.371 9.045   1.00 36.65  ? 233 GLN   A CB   1 
ATOM   3598 C CG   . GLN   A 1 248 ? 34.056  -12.574 9.302   1.00 49.10  ? 233 GLN   A CG   1 
ATOM   3599 C CD   . GLN   A 1 248 ? 35.438  -12.181 9.782   1.00 60.64  ? 233 GLN   A CD   1 
ATOM   3600 O OE1  . GLN   A 1 248 ? 35.746  -12.278 10.971  1.00 67.86  ? 233 GLN   A OE1  1 
ATOM   3601 N NE2  . GLN   A 1 248 ? 36.282  -11.731 8.856   1.00 66.16  ? 233 GLN   A NE2  1 
ATOM   3602 H H    . GLN   A 1 248 ? 31.257  -12.000 10.547  1.00 44.78  ? 233 GLN   A H    1 
ATOM   3603 H HA   . GLN   A 1 248 ? 33.446  -10.443 10.854  1.00 41.35  ? 233 GLN   A HA   1 
ATOM   3604 H HB2  . GLN   A 1 248 ? 32.399  -11.676 8.541   1.00 43.98  ? 233 GLN   A HB2  1 
ATOM   3605 H HB3  . GLN   A 1 248 ? 33.680  -10.736 8.519   1.00 43.98  ? 233 GLN   A HB3  1 
ATOM   3606 H HG2  . GLN   A 1 248 ? 33.647  -13.130 9.984   1.00 58.92  ? 233 GLN   A HG2  1 
ATOM   3607 H HG3  . GLN   A 1 248 ? 34.155  -13.077 8.479   1.00 58.92  ? 233 GLN   A HG3  1 
ATOM   3608 H HE21 . GLN   A 1 248 ? 36.030  -11.676 8.035   1.00 79.39  ? 233 GLN   A HE21 1 
ATOM   3609 H HE22 . GLN   A 1 248 ? 37.078  -11.495 9.078   1.00 79.39  ? 233 GLN   A HE22 1 
ATOM   3610 N N    . PRO   A 1 249 ? 32.407  -8.217  10.330  1.00 34.83  ? 234 PRO   A N    1 
ATOM   3611 C CA   . PRO   A 1 249 ? 31.723  -6.993  9.926   1.00 32.93  ? 234 PRO   A CA   1 
ATOM   3612 C C    . PRO   A 1 249 ? 31.630  -6.905  8.410   1.00 29.68  ? 234 PRO   A C    1 
ATOM   3613 O O    . PRO   A 1 249 ? 32.546  -7.344  7.692   1.00 32.01  ? 234 PRO   A O    1 
ATOM   3614 C CB   . PRO   A 1 249 ? 32.608  -5.878  10.500  1.00 26.08  ? 234 PRO   A CB   1 
ATOM   3615 C CG   . PRO   A 1 249 ? 33.308  -6.503  11.633  1.00 37.40  ? 234 PRO   A CG   1 
ATOM   3616 C CD   . PRO   A 1 249 ? 33.552  -7.933  11.216  1.00 31.09  ? 234 PRO   A CD   1 
ATOM   3617 H HA   . PRO   A 1 249 ? 30.837  -6.947  10.318  1.00 39.52  ? 234 PRO   A HA   1 
ATOM   3618 H HB2  . PRO   A 1 249 ? 33.236  -5.574  9.826   1.00 31.30  ? 234 PRO   A HB2  1 
ATOM   3619 H HB3  . PRO   A 1 249 ? 32.056  -5.137  10.797  1.00 31.30  ? 234 PRO   A HB3  1 
ATOM   3620 H HG2  . PRO   A 1 249 ? 34.146  -6.044  11.795  1.00 44.88  ? 234 PRO   A HG2  1 
ATOM   3621 H HG3  . PRO   A 1 249 ? 32.750  -6.466  12.425  1.00 44.88  ? 234 PRO   A HG3  1 
ATOM   3622 H HD2  . PRO   A 1 249 ? 34.391  -8.016  10.736  1.00 37.30  ? 234 PRO   A HD2  1 
ATOM   3623 H HD3  . PRO   A 1 249 ? 33.550  -8.524  11.985  1.00 37.30  ? 234 PRO   A HD3  1 
ATOM   3624 N N    . PRO   A 1 250 ? 30.549  -6.339  7.893   1.00 27.90  ? 235 PRO   A N    1 
ATOM   3625 C CA   . PRO   A 1 250 ? 30.379  -6.266  6.439   1.00 29.18  ? 235 PRO   A CA   1 
ATOM   3626 C C    . PRO   A 1 250 ? 31.386  -5.330  5.785   1.00 33.34  ? 235 PRO   A C    1 
ATOM   3627 O O    . PRO   A 1 250 ? 32.113  -4.577  6.434   1.00 27.67  ? 235 PRO   A O    1 
ATOM   3628 C CB   . PRO   A 1 250 ? 28.947  -5.749  6.272   1.00 31.69  ? 235 PRO   A CB   1 
ATOM   3629 C CG   . PRO   A 1 250 ? 28.632  -5.063  7.540   1.00 34.46  ? 235 PRO   A CG   1 
ATOM   3630 C CD   . PRO   A 1 250 ? 29.387  -5.789  8.613   1.00 24.65  ? 235 PRO   A CD   1 
ATOM   3631 H HA   . PRO   A 1 250 ? 30.463  -7.150  6.048   1.00 35.01  ? 235 PRO   A HA   1 
ATOM   3632 H HB2  . PRO   A 1 250 ? 28.905  -5.132  5.525   1.00 38.03  ? 235 PRO   A HB2  1 
ATOM   3633 H HB3  . PRO   A 1 250 ? 28.343  -6.493  6.122   1.00 38.03  ? 235 PRO   A HB3  1 
ATOM   3634 H HG2  . PRO   A 1 250 ? 28.918  -4.138  7.489   1.00 41.35  ? 235 PRO   A HG2  1 
ATOM   3635 H HG3  . PRO   A 1 250 ? 27.677  -5.107  7.705   1.00 41.35  ? 235 PRO   A HG3  1 
ATOM   3636 H HD2  . PRO   A 1 250 ? 29.670  -5.178  9.311   1.00 29.58  ? 235 PRO   A HD2  1 
ATOM   3637 H HD3  . PRO   A 1 250 ? 28.848  -6.500  8.994   1.00 29.58  ? 235 PRO   A HD3  1 
ATOM   3638 N N    . ARG   A 1 251 ? 31.417  -5.406  4.454   1.00 29.88  ? 236 ARG   A N    1 
ATOM   3639 C CA   . ARG   A 1 251 ? 32.305  -4.609  3.622   1.00 31.20  ? 236 ARG   A CA   1 
ATOM   3640 C C    . ARG   A 1 251 ? 31.546  -4.166  2.379   1.00 32.15  ? 236 ARG   A C    1 
ATOM   3641 O O    . ARG   A 1 251 ? 30.492  -4.712  2.043   1.00 26.65  ? 236 ARG   A O    1 
ATOM   3642 C CB   . ARG   A 1 251 ? 33.553  -5.400  3.202   1.00 39.31  ? 236 ARG   A CB   1 
ATOM   3643 C CG   . ARG   A 1 251 ? 34.452  -5.844  4.350   1.00 47.70  ? 236 ARG   A CG   1 
ATOM   3644 C CD   . ARG   A 1 251 ? 35.214  -4.664  4.920   1.00 58.74  ? 236 ARG   A CD   1 
ATOM   3645 N NE   . ARG   A 1 251 ? 35.991  -5.021  6.103   1.00 54.73  ? 236 ARG   A NE   1 
ATOM   3646 C CZ   . ARG   A 1 251 ? 35.655  -4.715  7.351   1.00 51.98  ? 236 ARG   A CZ   1 
ATOM   3647 N NH1  . ARG   A 1 251 ? 34.533  -4.071  7.632   1.00 38.90  ? 236 ARG   A NH1  1 
ATOM   3648 N NH2  . ARG   A 1 251 ? 36.472  -5.059  8.342   1.00 49.72  ? 236 ARG   A NH2  1 
ATOM   3649 H H    . ARG   A 1 251 ? 30.914  -5.933  3.997   1.00 35.86  ? 236 ARG   A H    1 
ATOM   3650 H HA   . ARG   A 1 251 ? 32.589  -3.825  4.118   1.00 37.43  ? 236 ARG   A HA   1 
ATOM   3651 H HB2  . ARG   A 1 251 ? 33.266  -6.198  2.731   1.00 47.18  ? 236 ARG   A HB2  1 
ATOM   3652 H HB3  . ARG   A 1 251 ? 34.086  -4.842  2.614   1.00 47.18  ? 236 ARG   A HB3  1 
ATOM   3653 H HG2  . ARG   A 1 251 ? 33.910  -6.231  5.055   1.00 57.24  ? 236 ARG   A HG2  1 
ATOM   3654 H HG3  . ARG   A 1 251 ? 35.092  -6.498  4.027   1.00 57.24  ? 236 ARG   A HG3  1 
ATOM   3655 H HD2  . ARG   A 1 251 ? 35.827  -4.328  4.248   1.00 70.49  ? 236 ARG   A HD2  1 
ATOM   3656 H HD3  . ARG   A 1 251 ? 34.584  -3.971  5.172   1.00 70.49  ? 236 ARG   A HD3  1 
ATOM   3657 H HE   . ARG   A 1 251 ? 36.720  -5.462  5.983   1.00 65.68  ? 236 ARG   A HE   1 
ATOM   3658 H HH11 . ARG   A 1 251 ? 34.000  -3.839  6.999   1.00 46.68  ? 236 ARG   A HH11 1 
ATOM   3659 H HH12 . ARG   A 1 251 ? 34.337  -3.884  8.449   1.00 46.68  ? 236 ARG   A HH12 1 
ATOM   3660 H HH21 . ARG   A 1 251 ? 37.206  -5.473  8.170   1.00 59.66  ? 236 ARG   A HH21 1 
ATOM   3661 H HH22 . ARG   A 1 251 ? 36.267  -4.867  9.155   1.00 59.66  ? 236 ARG   A HH22 1 
ATOM   3662 N N    . LEU   A 1 252 ? 32.102  -3.162  1.697   1.00 29.79  ? 237 LEU   A N    1 
ATOM   3663 C CA   . LEU   A 1 252 ? 31.620  -2.796  0.371   1.00 26.03  ? 237 LEU   A CA   1 
ATOM   3664 C C    . LEU   A 1 252 ? 31.859  -3.941  -0.609  1.00 27.78  ? 237 LEU   A C    1 
ATOM   3665 O O    . LEU   A 1 252 ? 32.916  -4.575  -0.597  1.00 31.07  ? 237 LEU   A O    1 
ATOM   3666 C CB   . LEU   A 1 252 ? 32.331  -1.535  -0.118  1.00 23.42  ? 237 LEU   A CB   1 
ATOM   3667 C CG   . LEU   A 1 252 ? 32.074  -0.251  0.681   1.00 27.39  ? 237 LEU   A CG   1 
ATOM   3668 C CD1  . LEU   A 1 252 ? 33.138  0.812   0.410   1.00 23.58  ? 237 LEU   A CD1  1 
ATOM   3669 C CD2  . LEU   A 1 252 ? 30.706  0.292   0.355   1.00 24.26  ? 237 LEU   A CD2  1 
ATOM   3670 H H    . LEU   A 1 252 ? 32.755  -2.680  1.981   1.00 35.75  ? 237 LEU   A H    1 
ATOM   3671 H HA   . LEU   A 1 252 ? 30.668  -2.613  0.409   1.00 31.23  ? 237 LEU   A HA   1 
ATOM   3672 H HB2  . LEU   A 1 252 ? 33.286  -1.700  -0.093  1.00 28.11  ? 237 LEU   A HB2  1 
ATOM   3673 H HB3  . LEU   A 1 252 ? 32.047  -1.365  -1.030  1.00 28.11  ? 237 LEU   A HB3  1 
ATOM   3674 H HG   . LEU   A 1 252 ? 32.118  -0.466  1.625   1.00 32.87  ? 237 LEU   A HG   1 
ATOM   3675 H HD11 . LEU   A 1 252 ? 32.940  1.600   0.940   1.00 28.30  ? 237 LEU   A HD11 1 
ATOM   3676 H HD12 . LEU   A 1 252 ? 34.007  0.458   0.656   1.00 28.30  ? 237 LEU   A HD12 1 
ATOM   3677 H HD13 . LEU   A 1 252 ? 33.127  1.037   -0.533  1.00 28.30  ? 237 LEU   A HD13 1 
ATOM   3678 H HD21 . LEU   A 1 252 ? 30.557  1.101   0.868   1.00 29.11  ? 237 LEU   A HD21 1 
ATOM   3679 H HD22 . LEU   A 1 252 ? 30.662  0.489   -0.594  1.00 29.11  ? 237 LEU   A HD22 1 
ATOM   3680 H HD23 . LEU   A 1 252 ? 30.039  -0.374  0.586   1.00 29.11  ? 237 LEU   A HD23 1 
ATOM   3681 N N    . LYS   A 1 253 ? 30.870  -4.179  -1.479  1.00 26.41  ? 238 LYS   A N    1 
ATOM   3682 C CA   . LYS   A 1 253 ? 30.901  -5.302  -2.413  1.00 31.73  ? 238 LYS   A CA   1 
ATOM   3683 C C    . LYS   A 1 253 ? 31.966  -5.108  -3.490  1.00 37.76  ? 238 LYS   A C    1 
ATOM   3684 O O    . LYS   A 1 253 ? 32.833  -5.968  -3.678  1.00 38.51  ? 238 LYS   A O    1 
ATOM   3685 C CB   . LYS   A 1 253 ? 29.512  -5.467  -3.046  1.00 36.64  ? 238 LYS   A CB   1 
ATOM   3686 C CG   . LYS   A 1 253 ? 29.401  -6.491  -4.171  1.00 40.06  ? 238 LYS   A CG   1 
ATOM   3687 C CD   . LYS   A 1 253 ? 29.296  -7.915  -3.650  1.00 55.68  ? 238 LYS   A CD   1 
ATOM   3688 C CE   . LYS   A 1 253 ? 29.011  -8.913  -4.781  1.00 39.48  ? 238 LYS   A CE   1 
ATOM   3689 N NZ   . LYS   A 1 253 ? 27.602  -8.832  -5.266  1.00 46.94  ? 238 LYS   A NZ   1 
ATOM   3690 H H    . LYS   A 1 253 ? 30.161  -3.697  -1.546  1.00 31.69  ? 238 LYS   A H    1 
ATOM   3691 H HA   . LYS   A 1 253 ? 31.125  -6.111  -1.928  1.00 38.07  ? 238 LYS   A HA   1 
ATOM   3692 H HB2  . LYS   A 1 253 ? 28.894  -5.739  -2.349  1.00 43.97  ? 238 LYS   A HB2  1 
ATOM   3693 H HB3  . LYS   A 1 253 ? 29.243  -4.610  -3.412  1.00 43.97  ? 238 LYS   A HB3  1 
ATOM   3694 H HG2  . LYS   A 1 253 ? 28.606  -6.303  -4.694  1.00 48.07  ? 238 LYS   A HG2  1 
ATOM   3695 H HG3  . LYS   A 1 253 ? 30.190  -6.433  -4.733  1.00 48.07  ? 238 LYS   A HG3  1 
ATOM   3696 H HD2  . LYS   A 1 253 ? 30.134  -8.165  -3.229  1.00 66.82  ? 238 LYS   A HD2  1 
ATOM   3697 H HD3  . LYS   A 1 253 ? 28.572  -7.969  -3.007  1.00 66.82  ? 238 LYS   A HD3  1 
ATOM   3698 H HE2  . LYS   A 1 253 ? 29.599  -8.723  -5.529  1.00 47.37  ? 238 LYS   A HE2  1 
ATOM   3699 H HE3  . LYS   A 1 253 ? 29.168  -9.814  -4.457  1.00 47.37  ? 238 LYS   A HE3  1 
ATOM   3700 H HZ1  . LYS   A 1 253 ? 27.337  -9.626  -5.567  1.00 56.33  ? 238 LYS   A HZ1  1 
ATOM   3701 H HZ2  . LYS   A 1 253 ? 27.066  -8.581  -4.601  1.00 56.33  ? 238 LYS   A HZ2  1 
ATOM   3702 H HZ3  . LYS   A 1 253 ? 27.541  -8.238  -5.926  1.00 56.33  ? 238 LYS   A HZ3  1 
ATOM   3703 N N    . GLU   A 1 254 ? 31.906  -3.995  -4.220  1.00 38.88  ? 239 GLU   A N    1 
ATOM   3704 C CA   . GLU   A 1 254 ? 32.796  -3.742  -5.354  1.00 41.76  ? 239 GLU   A CA   1 
ATOM   3705 C C    . GLU   A 1 254 ? 34.047  -3.018  -4.868  1.00 37.33  ? 239 GLU   A C    1 
ATOM   3706 O O    . GLU   A 1 254 ? 33.974  -1.858  -4.455  1.00 46.87  ? 239 GLU   A O    1 
ATOM   3707 C CB   . GLU   A 1 254 ? 32.089  -2.911  -6.421  1.00 39.11  ? 239 GLU   A CB   1 
ATOM   3708 C CG   . GLU   A 1 254 ? 30.798  -3.516  -6.920  1.00 53.91  ? 239 GLU   A CG   1 
ATOM   3709 C CD   . GLU   A 1 254 ? 30.199  -2.736  -8.071  1.00 63.01  ? 239 GLU   A CD   1 
ATOM   3710 O OE1  . GLU   A 1 254 ? 30.961  -2.340  -8.978  1.00 63.22  ? 239 GLU   A OE1  1 
ATOM   3711 O OE2  . GLU   A 1 254 ? 28.968  -2.518  -8.066  1.00 61.43  ? 239 GLU   A OE2  1 
ATOM   3712 H H    . GLU   A 1 254 ? 31.346  -3.359  -4.077  1.00 46.65  ? 239 GLU   A H    1 
ATOM   3713 H HA   . GLU   A 1 254 ? 33.059  -4.595  -5.734  1.00 50.12  ? 239 GLU   A HA   1 
ATOM   3714 H HB2  . GLU   A 1 254 ? 31.882  -2.040  -6.049  1.00 46.93  ? 239 GLU   A HB2  1 
ATOM   3715 H HB3  . GLU   A 1 254 ? 32.683  -2.814  -7.182  1.00 46.93  ? 239 GLU   A HB3  1 
ATOM   3716 H HG2  . GLU   A 1 254 ? 30.969  -4.420  -7.227  1.00 64.69  ? 239 GLU   A HG2  1 
ATOM   3717 H HG3  . GLU   A 1 254 ? 30.153  -3.528  -6.196  1.00 64.69  ? 239 GLU   A HG3  1 
ATOM   3718 N N    . LYS   A 1 255 ? 35.200  -3.682  -4.954  1.00 37.77  ? 240 LYS   A N    1 
ATOM   3719 C CA   . LYS   A 1 255 ? 36.412  -3.132  -4.358  1.00 32.67  ? 240 LYS   A CA   1 
ATOM   3720 C C    . LYS   A 1 255 ? 36.941  -1.944  -5.156  1.00 36.08  ? 240 LYS   A C    1 
ATOM   3721 O O    . LYS   A 1 255 ? 37.211  -0.876  -4.595  1.00 36.68  ? 240 LYS   A O    1 
ATOM   3722 C CB   . LYS   A 1 255 ? 37.476  -4.223  -4.250  1.00 36.19  ? 240 LYS   A CB   1 
ATOM   3723 C CG   . LYS   A 1 255 ? 36.992  -5.495  -3.580  1.00 44.57  ? 240 LYS   A CG   1 
ATOM   3724 C CD   . LYS   A 1 255 ? 36.333  -5.219  -2.248  1.00 33.10  ? 240 LYS   A CD   1 
ATOM   3725 C CE   . LYS   A 1 255 ? 36.010  -6.524  -1.511  1.00 46.89  ? 240 LYS   A CE   1 
ATOM   3726 N NZ   . LYS   A 1 255 ? 35.199  -6.293  -0.272  1.00 40.25  ? 240 LYS   A NZ   1 
ATOM   3727 H H    . LYS   A 1 255 ? 35.304  -4.441  -5.346  1.00 45.33  ? 240 LYS   A H    1 
ATOM   3728 H HA   . LYS   A 1 255 ? 36.203  -2.817  -3.464  1.00 39.20  ? 240 LYS   A HA   1 
ATOM   3729 H HB2  . LYS   A 1 255 ? 37.774  -4.455  -5.143  1.00 43.42  ? 240 LYS   A HB2  1 
ATOM   3730 H HB3  . LYS   A 1 255 ? 38.220  -3.881  -3.730  1.00 43.42  ? 240 LYS   A HB3  1 
ATOM   3731 H HG2  . LYS   A 1 255 ? 36.343  -5.931  -4.154  1.00 53.49  ? 240 LYS   A HG2  1 
ATOM   3732 H HG3  . LYS   A 1 255 ? 37.748  -6.083  -3.427  1.00 53.49  ? 240 LYS   A HG3  1 
ATOM   3733 H HD2  . LYS   A 1 255 ? 36.931  -4.694  -1.694  1.00 39.72  ? 240 LYS   A HD2  1 
ATOM   3734 H HD3  . LYS   A 1 255 ? 35.504  -4.735  -2.392  1.00 39.72  ? 240 LYS   A HD3  1 
ATOM   3735 H HE2  . LYS   A 1 255 ? 35.503  -7.104  -2.100  1.00 56.27  ? 240 LYS   A HE2  1 
ATOM   3736 H HE3  . LYS   A 1 255 ? 36.839  -6.956  -1.252  1.00 56.27  ? 240 LYS   A HE3  1 
ATOM   3737 H HZ1  . LYS   A 1 255 ? 35.024  -7.069  0.127   1.00 48.30  ? 240 LYS   A HZ1  1 
ATOM   3738 H HZ2  . LYS   A 1 255 ? 35.648  -5.772  0.293   1.00 48.30  ? 240 LYS   A HZ2  1 
ATOM   3739 H HZ3  . LYS   A 1 255 ? 34.430  -5.896  -0.481  1.00 48.30  ? 240 LYS   A HZ3  1 
ATOM   3740 N N    . GLY   A 1 256 ? 37.092  -2.110  -6.471  1.00 31.72  ? 241 GLY   A N    1 
ATOM   3741 C CA   . GLY   A 1 256 ? 37.748  -1.102  -7.285  1.00 32.11  ? 241 GLY   A CA   1 
ATOM   3742 C C    . GLY   A 1 256 ? 36.936  0.158   -7.482  1.00 37.23  ? 241 GLY   A C    1 
ATOM   3743 O O    . GLY   A 1 256 ? 37.489  1.181   -7.900  1.00 33.45  ? 241 GLY   A O    1 
ATOM   3744 H H    . GLY   A 1 256 ? 36.823  -2.798  -6.910  1.00 38.07  ? 241 GLY   A H    1 
ATOM   3745 H HA2  . GLY   A 1 256 ? 38.586  -0.855  -6.864  1.00 38.53  ? 241 GLY   A HA2  1 
ATOM   3746 H HA3  . GLY   A 1 256 ? 37.932  -1.478  -8.160  1.00 38.53  ? 241 GLY   A HA3  1 
ATOM   3747 N N    . LYS   A 1 257 ? 35.635  0.108   -7.200  1.00 37.95  ? 242 LYS   A N    1 
ATOM   3748 C CA   . LYS   A 1 257 ? 34.794  1.283   -7.379  1.00 38.75  ? 242 LYS   A CA   1 
ATOM   3749 C C    . LYS   A 1 257 ? 35.055  2.346   -6.320  1.00 31.78  ? 242 LYS   A C    1 
ATOM   3750 O O    . LYS   A 1 257 ? 34.724  3.513   -6.541  1.00 32.08  ? 242 LYS   A O    1 
ATOM   3751 C CB   . LYS   A 1 257 ? 33.317  0.882   -7.355  1.00 35.84  ? 242 LYS   A CB   1 
ATOM   3752 C CG   . LYS   A 1 257 ? 32.360  2.046   -7.528  1.00 41.00  ? 242 LYS   A CG   1 
ATOM   3753 C CD   . LYS   A 1 257 ? 30.943  1.583   -7.834  1.00 41.62  ? 242 LYS   A CD   1 
ATOM   3754 C CE   . LYS   A 1 257 ? 29.990  2.773   -8.012  1.00 39.02  ? 242 LYS   A CE   1 
ATOM   3755 N NZ   . LYS   A 1 257 ? 28.624  2.334   -8.433  1.00 48.28  ? 242 LYS   A NZ   1 
ATOM   3756 H H    . LYS   A 1 257 ? 35.222  -0.587  -6.908  1.00 45.54  ? 242 LYS   A H    1 
ATOM   3757 H HA   . LYS   A 1 257 ? 34.986  1.672   -8.247  1.00 46.50  ? 242 LYS   A HA   1 
ATOM   3758 H HB2  . LYS   A 1 257 ? 33.153  0.255   -8.076  1.00 43.01  ? 242 LYS   A HB2  1 
ATOM   3759 H HB3  . LYS   A 1 257 ? 33.122  0.464   -6.501  1.00 43.01  ? 242 LYS   A HB3  1 
ATOM   3760 H HG2  . LYS   A 1 257 ? 32.338  2.566   -6.709  1.00 49.20  ? 242 LYS   A HG2  1 
ATOM   3761 H HG3  . LYS   A 1 257 ? 32.662  2.600   -8.265  1.00 49.20  ? 242 LYS   A HG3  1 
ATOM   3762 H HD2  . LYS   A 1 257 ? 30.944  1.066   -8.655  1.00 49.94  ? 242 LYS   A HD2  1 
ATOM   3763 H HD3  . LYS   A 1 257 ? 30.618  1.038   -7.100  1.00 49.94  ? 242 LYS   A HD3  1 
ATOM   3764 H HE2  . LYS   A 1 257 ? 29.911  3.248   -7.170  1.00 46.82  ? 242 LYS   A HE2  1 
ATOM   3765 H HE3  . LYS   A 1 257 ? 30.342  3.365   -8.695  1.00 46.82  ? 242 LYS   A HE3  1 
ATOM   3766 H HZ1  . LYS   A 1 257 ? 28.091  3.041   -8.523  1.00 57.93  ? 242 LYS   A HZ1  1 
ATOM   3767 H HZ2  . LYS   A 1 257 ? 28.668  1.904   -9.210  1.00 57.93  ? 242 LYS   A HZ2  1 
ATOM   3768 H HZ3  . LYS   A 1 257 ? 28.278  1.789   -7.820  1.00 57.93  ? 242 LYS   A HZ3  1 
ATOM   3769 N N    . TRP   A 1 258 ? 35.656  1.981   -5.193  1.00 26.36  ? 243 TRP   A N    1 
ATOM   3770 C CA   . TRP   A 1 258 ? 35.787  2.891   -4.066  1.00 27.77  ? 243 TRP   A CA   1 
ATOM   3771 C C    . TRP   A 1 258 ? 37.243  3.016   -3.657  1.00 31.59  ? 243 TRP   A C    1 
ATOM   3772 O O    . TRP   A 1 258 ? 38.036  2.081   -3.800  1.00 29.14  ? 243 TRP   A O    1 
ATOM   3773 C CB   . TRP   A 1 258 ? 34.939  2.417   -2.884  1.00 25.61  ? 243 TRP   A CB   1 
ATOM   3774 C CG   . TRP   A 1 258 ? 33.559  1.984   -3.289  1.00 25.49  ? 243 TRP   A CG   1 
ATOM   3775 C CD1  . TRP   A 1 258 ? 33.094  0.701   -3.356  1.00 27.13  ? 243 TRP   A CD1  1 
ATOM   3776 C CD2  . TRP   A 1 258 ? 32.476  2.825   -3.706  1.00 23.03  ? 243 TRP   A CD2  1 
ATOM   3777 N NE1  . TRP   A 1 258 ? 31.785  0.695   -3.771  1.00 29.38  ? 243 TRP   A NE1  1 
ATOM   3778 C CE2  . TRP   A 1 258 ? 31.383  1.982   -3.996  1.00 23.01  ? 243 TRP   A CE2  1 
ATOM   3779 C CE3  . TRP   A 1 258 ? 32.317  4.212   -3.851  1.00 31.41  ? 243 TRP   A CE3  1 
ATOM   3780 C CZ2  . TRP   A 1 258 ? 30.150  2.474   -4.428  1.00 24.00  ? 243 TRP   A CZ2  1 
ATOM   3781 C CZ3  . TRP   A 1 258 ? 31.088  4.702   -4.278  1.00 24.80  ? 243 TRP   A CZ3  1 
ATOM   3782 C CH2  . TRP   A 1 258 ? 30.019  3.832   -4.560  1.00 27.99  ? 243 TRP   A CH2  1 
ATOM   3783 H H    . TRP   A 1 258 ? 35.999  1.204   -5.057  1.00 31.64  ? 243 TRP   A H    1 
ATOM   3784 H HA   . TRP   A 1 258 ? 35.487  3.776   -4.325  1.00 33.32  ? 243 TRP   A HA   1 
ATOM   3785 H HB2  . TRP   A 1 258 ? 35.379  1.661   -2.464  1.00 30.73  ? 243 TRP   A HB2  1 
ATOM   3786 H HB3  . TRP   A 1 258 ? 34.851  3.144   -2.248  1.00 30.73  ? 243 TRP   A HB3  1 
ATOM   3787 H HD1  . TRP   A 1 258 ? 33.592  -0.058  -3.151  1.00 32.56  ? 243 TRP   A HD1  1 
ATOM   3788 H HE1  . TRP   A 1 258 ? 31.296  -0.005  -3.872  1.00 35.25  ? 243 TRP   A HE1  1 
ATOM   3789 H HE3  . TRP   A 1 258 ? 33.020  4.792   -3.665  1.00 37.69  ? 243 TRP   A HE3  1 
ATOM   3790 H HZ2  . TRP   A 1 258 ? 29.442  1.902   -4.619  1.00 28.80  ? 243 TRP   A HZ2  1 
ATOM   3791 H HZ3  . TRP   A 1 258 ? 30.971  5.619   -4.379  1.00 29.76  ? 243 TRP   A HZ3  1 
ATOM   3792 H HH2  . TRP   A 1 258 ? 29.207  4.186   -4.841  1.00 33.59  ? 243 TRP   A HH2  1 
ATOM   3793 N N    . SER   A 1 259 ? 37.580  4.194   -3.139  1.00 27.38  ? 244 SER   A N    1 
ATOM   3794 C CA   . SER   A 1 259 ? 38.949  4.507   -2.772  1.00 25.62  ? 244 SER   A CA   1 
ATOM   3795 C C    . SER   A 1 259 ? 39.321  3.834   -1.457  1.00 25.35  ? 244 SER   A C    1 
ATOM   3796 O O    . SER   A 1 259 ? 38.463  3.461   -0.647  1.00 30.21  ? 244 SER   A O    1 
ATOM   3797 C CB   . SER   A 1 259 ? 39.144  6.018   -2.636  1.00 25.75  ? 244 SER   A CB   1 
ATOM   3798 O OG   . SER   A 1 259 ? 38.609  6.477   -1.402  1.00 24.81  ? 244 SER   A OG   1 
ATOM   3799 H H    . SER   A 1 259 ? 37.026  4.834   -2.990  1.00 32.85  ? 244 SER   A H    1 
ATOM   3800 H HA   . SER   A 1 259 ? 39.541  4.180   -3.467  1.00 30.75  ? 244 SER   A HA   1 
ATOM   3801 H HB2  . SER   A 1 259 ? 40.092  6.220   -2.666  1.00 30.90  ? 244 SER   A HB2  1 
ATOM   3802 H HB3  . SER   A 1 259 ? 38.686  6.463   -3.366  1.00 30.90  ? 244 SER   A HB3  1 
ATOM   3803 H HG   . SER   A 1 259 ? 37.788  6.302   -1.361  1.00 29.77  ? 244 SER   A HG   1 
ATOM   3804 N N    . ALA   A 1 260 ? 40.633  3.709   -1.239  1.00 26.47  ? 245 ALA   A N    1 
ATOM   3805 C CA   . ALA   A 1 260 ? 41.129  3.172   0.024   1.00 26.42  ? 245 ALA   A CA   1 
ATOM   3806 C C    . ALA   A 1 260 ? 40.552  3.926   1.215   1.00 29.54  ? 245 ALA   A C    1 
ATOM   3807 O O    . ALA   A 1 260 ? 40.209  3.322   2.239   1.00 28.76  ? 245 ALA   A O    1 
ATOM   3808 C CB   . ALA   A 1 260 ? 42.658  3.232   0.054   1.00 27.86  ? 245 ALA   A CB   1 
ATOM   3809 H H    . ALA   A 1 260 ? 41.248  3.925   -1.801  1.00 31.76  ? 245 ALA   A H    1 
ATOM   3810 H HA   . ALA   A 1 260 ? 40.857  2.244   0.093   1.00 31.70  ? 245 ALA   A HA   1 
ATOM   3811 H HB1  . ALA   A 1 260 ? 42.972  2.870   0.897   1.00 33.43  ? 245 ALA   A HB1  1 
ATOM   3812 H HB2  . ALA   A 1 260 ? 43.009  2.708   -0.683  1.00 33.43  ? 245 ALA   A HB2  1 
ATOM   3813 H HB3  . ALA   A 1 260 ? 42.939  4.157   -0.033  1.00 33.43  ? 245 ALA   A HB3  1 
ATOM   3814 N N    . ALA   A 1 261 ? 40.441  5.253   1.108   1.00 27.44  ? 246 ALA   A N    1 
ATOM   3815 C CA   . ALA   A 1 261 ? 39.905  6.030   2.223   1.00 24.66  ? 246 ALA   A CA   1 
ATOM   3816 C C    . ALA   A 1 261 ? 38.491  5.589   2.567   1.00 23.47  ? 246 ALA   A C    1 
ATOM   3817 O O    . ALA   A 1 261 ? 38.147  5.443   3.744   1.00 26.01  ? 246 ALA   A O    1 
ATOM   3818 C CB   . ALA   A 1 261 ? 39.946  7.525   1.896   1.00 30.33  ? 246 ALA   A CB   1 
ATOM   3819 H H    . ALA   A 1 261 ? 40.664  5.714   0.418   1.00 32.92  ? 246 ALA   A H    1 
ATOM   3820 H HA   . ALA   A 1 261 ? 40.463  5.885   3.003   1.00 29.59  ? 246 ALA   A HA   1 
ATOM   3821 H HB1  . ALA   A 1 261 ? 39.585  8.022   2.646   1.00 36.40  ? 246 ALA   A HB1  1 
ATOM   3822 H HB2  . ALA   A 1 261 ? 40.865  7.788   1.736   1.00 36.40  ? 246 ALA   A HB2  1 
ATOM   3823 H HB3  . ALA   A 1 261 ? 39.411  7.689   1.103   1.00 36.40  ? 246 ALA   A HB3  1 
ATOM   3824 N N    . PHE   A 1 262 ? 37.655  5.369   1.555   1.00 23.10  ? 247 PHE   A N    1 
ATOM   3825 C CA   . PHE   A 1 262 ? 36.284  4.925   1.803   1.00 22.19  ? 247 PHE   A CA   1 
ATOM   3826 C C    . PHE   A 1 262 ? 36.273  3.532   2.428   1.00 22.22  ? 247 PHE   A C    1 
ATOM   3827 O O    . PHE   A 1 262 ? 35.572  3.292   3.414   1.00 22.18  ? 247 PHE   A O    1 
ATOM   3828 C CB   . PHE   A 1 262 ? 35.505  4.968   0.489   1.00 22.12  ? 247 PHE   A CB   1 
ATOM   3829 C CG   . PHE   A 1 262 ? 34.018  4.754   0.628   1.00 21.39  ? 247 PHE   A CG   1 
ATOM   3830 C CD1  . PHE   A 1 262 ? 33.394  4.751   1.863   1.00 29.76  ? 247 PHE   A CD1  1 
ATOM   3831 C CD2  . PHE   A 1 262 ? 33.240  4.559   -0.506  1.00 24.95  ? 247 PHE   A CD2  1 
ATOM   3832 C CE1  . PHE   A 1 262 ? 32.024  4.561   1.966   1.00 24.12  ? 247 PHE   A CE1  1 
ATOM   3833 C CE2  . PHE   A 1 262 ? 31.875  4.365   -0.411  1.00 27.48  ? 247 PHE   A CE2  1 
ATOM   3834 C CZ   . PHE   A 1 262 ? 31.264  4.368   0.833   1.00 23.77  ? 247 PHE   A CZ   1 
ATOM   3835 H H    . PHE   A 1 262 ? 37.853  5.468   0.724   1.00 27.72  ? 247 PHE   A H    1 
ATOM   3836 H HA   . PHE   A 1 262 ? 35.845  5.522   2.429   1.00 26.63  ? 247 PHE   A HA   1 
ATOM   3837 H HB2  . PHE   A 1 262 ? 35.637  5.838   0.081   1.00 26.55  ? 247 PHE   A HB2  1 
ATOM   3838 H HB3  . PHE   A 1 262 ? 35.846  4.272   -0.094  1.00 26.55  ? 247 PHE   A HB3  1 
ATOM   3839 H HD1  . PHE   A 1 262 ? 33.900  4.877   2.634   1.00 35.71  ? 247 PHE   A HD1  1 
ATOM   3840 H HD2  . PHE   A 1 262 ? 33.645  4.559   -1.343  1.00 29.93  ? 247 PHE   A HD2  1 
ATOM   3841 H HE1  . PHE   A 1 262 ? 31.617  4.564   2.802   1.00 28.95  ? 247 PHE   A HE1  1 
ATOM   3842 H HE2  . PHE   A 1 262 ? 31.368  4.233   -1.179  1.00 32.97  ? 247 PHE   A HE2  1 
ATOM   3843 H HZ   . PHE   A 1 262 ? 30.346  4.240   0.902   1.00 28.53  ? 247 PHE   A HZ   1 
ATOM   3844 N N    . HIS   A 1 263 ? 37.064  2.602   1.880   1.00 24.16  ? 248 HIS   A N    1 
ATOM   3845 C CA   . HIS   A 1 263 ? 37.155  1.271   2.470   1.00 23.90  ? 248 HIS   A CA   1 
ATOM   3846 C C    . HIS   A 1 263 ? 37.582  1.351   3.929   1.00 28.46  ? 248 HIS   A C    1 
ATOM   3847 O O    . HIS   A 1 263 ? 37.040  0.641   4.786   1.00 23.24  ? 248 HIS   A O    1 
ATOM   3848 C CB   . HIS   A 1 263 ? 38.139  0.404   1.687   1.00 25.36  ? 248 HIS   A CB   1 
ATOM   3849 C CG   . HIS   A 1 263 ? 37.607  -0.085  0.377   1.00 26.08  ? 248 HIS   A CG   1 
ATOM   3850 N ND1  . HIS   A 1 263 ? 36.506  -0.906  0.281   1.00 26.90  ? 248 HIS   A ND1  1 
ATOM   3851 C CD2  . HIS   A 1 263 ? 38.036  0.117   -0.892  1.00 24.88  ? 248 HIS   A CD2  1 
ATOM   3852 C CE1  . HIS   A 1 263 ? 36.271  -1.181  -0.988  1.00 31.25  ? 248 HIS   A CE1  1 
ATOM   3853 N NE2  . HIS   A 1 263 ? 37.185  -0.573  -1.722  1.00 24.82  ? 248 HIS   A NE2  1 
ATOM   3854 H H    . HIS   A 1 263 ? 37.548  2.718   1.179   1.00 28.99  ? 248 HIS   A H    1 
ATOM   3855 H HA   . HIS   A 1 263 ? 36.281  0.854   2.422   1.00 28.67  ? 248 HIS   A HA   1 
ATOM   3856 H HB2  . HIS   A 1 263 ? 38.937  0.925   1.506   1.00 30.43  ? 248 HIS   A HB2  1 
ATOM   3857 H HB3  . HIS   A 1 263 ? 38.364  -0.372  2.223   1.00 30.43  ? 248 HIS   A HB3  1 
ATOM   3858 H HD1  . HIS   A 1 263 ? 36.042  -1.194  0.946   1.00 32.27  ? 248 HIS   A HD1  1 
ATOM   3859 H HD2  . HIS   A 1 263 ? 38.768  0.628   -1.153  1.00 29.86  ? 248 HIS   A HD2  1 
ATOM   3860 H HE1  . HIS   A 1 263 ? 35.580  -1.713  -1.311  1.00 37.50  ? 248 HIS   A HE1  1 
ATOM   3861 H HE2  . HIS   A 1 263 ? 37.240  -0.604  -2.580  1.00 29.79  ? 248 HIS   A HE2  1 
ATOM   3862 N N    . ASN   A 1 264 ? 38.546  2.220   4.233   1.00 24.59  ? 249 ASN   A N    1 
ATOM   3863 C CA   . ASN   A 1 264 ? 39.040  2.319   5.601   1.00 30.15  ? 249 ASN   A CA   1 
ATOM   3864 C C    . ASN   A 1 264 ? 37.997  2.948   6.519   1.00 27.20  ? 249 ASN   A C    1 
ATOM   3865 O O    . ASN   A 1 264 ? 37.884  2.571   7.691   1.00 25.49  ? 249 ASN   A O    1 
ATOM   3866 C CB   . ASN   A 1 264 ? 40.336  3.123   5.636   1.00 28.66  ? 249 ASN   A CB   1 
ATOM   3867 C CG   . ASN   A 1 264 ? 40.917  3.207   7.024   1.00 31.88  ? 249 ASN   A CG   1 
ATOM   3868 O OD1  . ASN   A 1 264 ? 40.672  4.165   7.751   1.00 31.20  ? 249 ASN   A OD1  1 
ATOM   3869 N ND2  . ASN   A 1 264 ? 41.667  2.184   7.415   1.00 37.00  ? 249 ASN   A ND2  1 
ATOM   3870 H H    . ASN   A 1 264 ? 38.924  2.753   3.674   1.00 29.51  ? 249 ASN   A H    1 
ATOM   3871 H HA   . ASN   A 1 264 ? 39.233  1.427   5.927   1.00 36.18  ? 249 ASN   A HA   1 
ATOM   3872 H HB2  . ASN   A 1 264 ? 40.991  2.697   5.060   1.00 34.39  ? 249 ASN   A HB2  1 
ATOM   3873 H HB3  . ASN   A 1 264 ? 40.160  4.026   5.327   1.00 34.39  ? 249 ASN   A HB3  1 
ATOM   3874 H HD21 . ASN   A 1 264 ? 42.021  2.186   8.199   1.00 44.40  ? 249 ASN   A HD21 1 
ATOM   3875 H HD22 . ASN   A 1 264 ? 41.799  1.520   6.885   1.00 44.40  ? 249 ASN   A HD22 1 
ATOM   3876 N N    . PHE   A 1 265 ? 37.229  3.906   6.000   1.00 22.52  ? 250 PHE   A N    1 
ATOM   3877 C CA   . PHE   A 1 265 ? 36.116  4.467   6.763   1.00 28.10  ? 250 PHE   A CA   1 
ATOM   3878 C C    . PHE   A 1 265 ? 35.125  3.379   7.152   1.00 29.97  ? 250 PHE   A C    1 
ATOM   3879 O O    . PHE   A 1 265 ? 34.655  3.331   8.294   1.00 27.31  ? 250 PHE   A O    1 
ATOM   3880 C CB   . PHE   A 1 265 ? 35.436  5.560   5.934   1.00 23.43  ? 250 PHE   A CB   1 
ATOM   3881 C CG   . PHE   A 1 265 ? 34.294  6.268   6.629   1.00 23.00  ? 250 PHE   A CG   1 
ATOM   3882 C CD1  . PHE   A 1 265 ? 33.000  5.796   6.511   1.00 25.67  ? 250 PHE   A CD1  1 
ATOM   3883 C CD2  . PHE   A 1 265 ? 34.507  7.448   7.333   1.00 25.59  ? 250 PHE   A CD2  1 
ATOM   3884 C CE1  . PHE   A 1 265 ? 31.938  6.450   7.117   1.00 23.16  ? 250 PHE   A CE1  1 
ATOM   3885 C CE2  . PHE   A 1 265 ? 33.448  8.118   7.941   1.00 23.47  ? 250 PHE   A CE2  1 
ATOM   3886 C CZ   . PHE   A 1 265 ? 32.157  7.614   7.834   1.00 19.48  ? 250 PHE   A CZ   1 
ATOM   3887 H H    . PHE   A 1 265 ? 37.329  4.246   5.216   1.00 27.03  ? 250 PHE   A H    1 
ATOM   3888 H HA   . PHE   A 1 265 ? 36.447  4.871   7.580   1.00 33.72  ? 250 PHE   A HA   1 
ATOM   3889 H HB2  . PHE   A 1 265 ? 36.099  6.231   5.706   1.00 28.12  ? 250 PHE   A HB2  1 
ATOM   3890 H HB3  . PHE   A 1 265 ? 35.080  5.157   5.126   1.00 28.12  ? 250 PHE   A HB3  1 
ATOM   3891 H HD1  . PHE   A 1 265 ? 32.839  5.025   6.016   1.00 30.81  ? 250 PHE   A HD1  1 
ATOM   3892 H HD2  . PHE   A 1 265 ? 35.367  7.795   7.398   1.00 30.71  ? 250 PHE   A HD2  1 
ATOM   3893 H HE1  . PHE   A 1 265 ? 31.077  6.106   7.041   1.00 27.80  ? 250 PHE   A HE1  1 
ATOM   3894 H HE2  . PHE   A 1 265 ? 33.605  8.901   8.418   1.00 28.16  ? 250 PHE   A HE2  1 
ATOM   3895 H HZ   . PHE   A 1 265 ? 31.447  8.054   8.241   1.00 23.38  ? 250 PHE   A HZ   1 
ATOM   3896 N N    . ILE   A 1 266 ? 34.805  2.486   6.219   1.00 25.10  ? 251 ILE   A N    1 
ATOM   3897 C CA   . ILE   A 1 266 ? 33.913  1.378   6.538   1.00 21.80  ? 251 ILE   A CA   1 
ATOM   3898 C C    . ILE   A 1 266 ? 34.563  0.462   7.567   1.00 30.44  ? 251 ILE   A C    1 
ATOM   3899 O O    . ILE   A 1 266 ? 33.908  -0.012  8.504   1.00 28.13  ? 251 ILE   A O    1 
ATOM   3900 C CB   . ILE   A 1 266 ? 33.541  0.617   5.254   1.00 25.77  ? 251 ILE   A CB   1 
ATOM   3901 C CG1  . ILE   A 1 266 ? 32.655  1.481   4.353   1.00 25.18  ? 251 ILE   A CG1  1 
ATOM   3902 C CG2  . ILE   A 1 266 ? 32.872  -0.717  5.592   1.00 27.25  ? 251 ILE   A CG2  1 
ATOM   3903 C CD1  . ILE   A 1 266 ? 31.427  2.058   5.040   1.00 24.24  ? 251 ILE   A CD1  1 
ATOM   3904 H H    . ILE   A 1 266 ? 35.087  2.499   5.407   1.00 30.13  ? 251 ILE   A H    1 
ATOM   3905 H HA   . ILE   A 1 266 ? 33.096  1.730   6.925   1.00 26.16  ? 251 ILE   A HA   1 
ATOM   3906 H HB   . ILE   A 1 266 ? 34.355  0.422   4.765   1.00 30.92  ? 251 ILE   A HB   1 
ATOM   3907 H HG12 . ILE   A 1 266 ? 33.183  2.225   4.024   1.00 30.21  ? 251 ILE   A HG12 1 
ATOM   3908 H HG13 . ILE   A 1 266 ? 32.347  0.939   3.610   1.00 30.21  ? 251 ILE   A HG13 1 
ATOM   3909 H HG21 . ILE   A 1 266 ? 32.421  -1.053  4.802   1.00 32.70  ? 251 ILE   A HG21 1 
ATOM   3910 H HG22 . ILE   A 1 266 ? 33.552  -1.347  5.878   1.00 32.70  ? 251 ILE   A HG22 1 
ATOM   3911 H HG23 . ILE   A 1 266 ? 32.230  -0.577  6.305   1.00 32.70  ? 251 ILE   A HG23 1 
ATOM   3912 H HD11 . ILE   A 1 266 ? 30.781  2.320   4.366   1.00 29.09  ? 251 ILE   A HD11 1 
ATOM   3913 H HD12 . ILE   A 1 266 ? 31.043  1.382   5.620   1.00 29.09  ? 251 ILE   A HD12 1 
ATOM   3914 H HD13 . ILE   A 1 266 ? 31.691  2.831   5.564   1.00 29.09  ? 251 ILE   A HD13 1 
ATOM   3915 N N    . LYS   A 1 267 ? 35.868  0.221   7.423   1.00 28.78  ? 252 LYS   A N    1 
ATOM   3916 C CA   . LYS   A 1 267 ? 36.564  -0.689  8.322   1.00 23.98  ? 252 LYS   A CA   1 
ATOM   3917 C C    . LYS   A 1 267 ? 36.482  -0.221  9.768   1.00 27.50  ? 252 LYS   A C    1 
ATOM   3918 O O    . LYS   A 1 267 ? 36.223  -1.017  10.676  1.00 29.42  ? 252 LYS   A O    1 
ATOM   3919 C CB   . LYS   A 1 267 ? 38.025  -0.826  7.900   1.00 24.95  ? 252 LYS   A CB   1 
ATOM   3920 C CG   . LYS   A 1 267 ? 38.823  -1.768  8.791   1.00 38.39  ? 252 LYS   A CG   1 
ATOM   3921 C CD   . LYS   A 1 267 ? 40.255  -1.961  8.302   1.00 35.70  ? 252 LYS   A CD   1 
ATOM   3922 C CE   . LYS   A 1 267 ? 41.009  -2.927  9.203   1.00 38.47  ? 252 LYS   A CE   1 
ATOM   3923 N NZ   . LYS   A 1 267 ? 42.418  -3.123  8.782   1.00 53.14  ? 252 LYS   A NZ   1 
ATOM   3924 H H    . LYS   A 1 267 ? 36.367  0.570   6.817   1.00 34.53  ? 252 LYS   A H    1 
ATOM   3925 H HA   . LYS   A 1 267 ? 36.140  -1.559  8.261   1.00 28.77  ? 252 LYS   A HA   1 
ATOM   3926 H HB2  . LYS   A 1 267 ? 38.059  -1.171  6.994   1.00 29.94  ? 252 LYS   A HB2  1 
ATOM   3927 H HB3  . LYS   A 1 267 ? 38.446  0.048   7.937   1.00 29.94  ? 252 LYS   A HB3  1 
ATOM   3928 H HG2  . LYS   A 1 267 ? 38.858  -1.403  9.689   1.00 46.07  ? 252 LYS   A HG2  1 
ATOM   3929 H HG3  . LYS   A 1 267 ? 38.390  -2.636  8.803   1.00 46.07  ? 252 LYS   A HG3  1 
ATOM   3930 H HD2  . LYS   A 1 267 ? 40.244  -2.323  7.403   1.00 42.84  ? 252 LYS   A HD2  1 
ATOM   3931 H HD3  . LYS   A 1 267 ? 40.717  -1.108  8.311   1.00 42.84  ? 252 LYS   A HD3  1 
ATOM   3932 H HE2  . LYS   A 1 267 ? 41.012  -2.579  10.108  1.00 46.16  ? 252 LYS   A HE2  1 
ATOM   3933 H HE3  . LYS   A 1 267 ? 40.567  -3.791  9.181   1.00 46.16  ? 252 LYS   A HE3  1 
ATOM   3934 H HZ1  . LYS   A 1 267 ? 42.824  -3.691  9.334   1.00 63.77  ? 252 LYS   A HZ1  1 
ATOM   3935 H HZ2  . LYS   A 1 267 ? 42.446  -3.452  7.956   1.00 63.77  ? 252 LYS   A HZ2  1 
ATOM   3936 H HZ3  . LYS   A 1 267 ? 42.851  -2.346  8.798   1.00 63.77  ? 252 LYS   A HZ3  1 
ATOM   3937 N N    . VAL   A 1 268 ? 36.713  1.069   10.009  1.00 29.44  ? 253 VAL   A N    1 
ATOM   3938 C CA   . VAL   A 1 268 ? 36.868  1.525   11.386  1.00 26.05  ? 253 VAL   A CA   1 
ATOM   3939 C C    . VAL   A 1 268 ? 35.532  1.849   12.048  1.00 23.47  ? 253 VAL   A C    1 
ATOM   3940 O O    . VAL   A 1 268 ? 35.395  1.650   13.255  1.00 26.81  ? 253 VAL   A O    1 
ATOM   3941 C CB   . VAL   A 1 268 ? 37.832  2.724   11.462  1.00 30.45  ? 253 VAL   A CB   1 
ATOM   3942 C CG1  . VAL   A 1 268 ? 39.213  2.295   10.994  1.00 28.51  ? 253 VAL   A CG1  1 
ATOM   3943 C CG2  . VAL   A 1 268 ? 37.303  3.927   10.653  1.00 29.08  ? 253 VAL   A CG2  1 
ATOM   3944 H H    . VAL   A 1 268 ? 36.782  1.682   9.410   1.00 35.33  ? 253 VAL   A H    1 
ATOM   3945 H HA   . VAL   A 1 268 ? 37.265  0.799   11.892  1.00 31.26  ? 253 VAL   A HA   1 
ATOM   3946 H HB   . VAL   A 1 268 ? 37.898  3.023   12.382  1.00 36.54  ? 253 VAL   A HB   1 
ATOM   3947 H HG11 . VAL   A 1 268 ? 39.825  3.042   11.088  1.00 34.22  ? 253 VAL   A HG11 1 
ATOM   3948 H HG12 . VAL   A 1 268 ? 39.514  1.550   11.538  1.00 34.22  ? 253 VAL   A HG12 1 
ATOM   3949 H HG13 . VAL   A 1 268 ? 39.161  2.025   10.063  1.00 34.22  ? 253 VAL   A HG13 1 
ATOM   3950 H HG21 . VAL   A 1 268 ? 37.948  4.650   10.704  1.00 34.89  ? 253 VAL   A HG21 1 
ATOM   3951 H HG22 . VAL   A 1 268 ? 37.182  3.657   9.729   1.00 34.89  ? 253 VAL   A HG22 1 
ATOM   3952 H HG23 . VAL   A 1 268 ? 36.456  4.212   11.028  1.00 34.89  ? 253 VAL   A HG23 1 
ATOM   3953 N N    . THR   A 1 269 ? 34.534  2.341   11.302  1.00 22.40  ? 254 THR   A N    1 
ATOM   3954 C CA   . THR   A 1 269 ? 33.228  2.530   11.922  1.00 23.22  ? 254 THR   A CA   1 
ATOM   3955 C C    . THR   A 1 269 ? 32.613  1.188   12.300  1.00 29.26  ? 254 THR   A C    1 
ATOM   3956 O O    . THR   A 1 269 ? 32.008  1.056   13.370  1.00 27.17  ? 254 THR   A O    1 
ATOM   3957 C CB   . THR   A 1 269 ? 32.276  3.309   11.010  1.00 24.82  ? 254 THR   A CB   1 
ATOM   3958 O OG1  . THR   A 1 269 ? 32.139  2.642   9.756   1.00 23.40  ? 254 THR   A OG1  1 
ATOM   3959 C CG2  . THR   A 1 269 ? 32.769  4.753   10.791  1.00 21.94  ? 254 THR   A CG2  1 
ATOM   3960 H H    . THR   A 1 269 ? 34.590  2.563   10.473  1.00 26.88  ? 254 THR   A H    1 
ATOM   3961 H HA   . THR   A 1 269 ? 33.351  3.062   12.723  1.00 27.86  ? 254 THR   A HA   1 
ATOM   3962 H HB   . THR   A 1 269 ? 31.405  3.358   11.434  1.00 29.79  ? 254 THR   A HB   1 
ATOM   3963 H HG1  . THR   A 1 269 ? 32.888  2.582   9.379   1.00 28.08  ? 254 THR   A HG1  1 
ATOM   3964 H HG21 . THR   A 1 269 ? 32.153  5.230   10.213  1.00 26.33  ? 254 THR   A HG21 1 
ATOM   3965 H HG22 . THR   A 1 269 ? 32.826  5.216   11.641  1.00 26.33  ? 254 THR   A HG22 1 
ATOM   3966 H HG23 . THR   A 1 269 ? 33.646  4.745   10.377  1.00 26.33  ? 254 THR   A HG23 1 
ATOM   3967 N N    . LEU   A 1 270 ? 32.779  0.180   11.447  1.00 22.55  ? 255 LEU   A N    1 
ATOM   3968 C CA   . LEU   A 1 270 ? 32.208  -1.143  11.697  1.00 23.14  ? 255 LEU   A CA   1 
ATOM   3969 C C    . LEU   A 1 270 ? 33.136  -1.999  12.551  1.00 24.44  ? 255 LEU   A C    1 
ATOM   3970 O O    . LEU   A 1 270 ? 33.423  -3.152  12.249  1.00 28.72  ? 255 LEU   A O    1 
ATOM   3971 C CB   . LEU   A 1 270 ? 31.884  -1.814  10.372  1.00 28.52  ? 255 LEU   A CB   1 
ATOM   3972 C CG   . LEU   A 1 270 ? 30.874  -1.051  9.506   1.00 26.89  ? 255 LEU   A CG   1 
ATOM   3973 C CD1  . LEU   A 1 270 ? 30.511  -1.889  8.279   1.00 29.19  ? 255 LEU   A CD1  1 
ATOM   3974 C CD2  . LEU   A 1 270 ? 29.639  -0.684  10.281  1.00 21.63  ? 255 LEU   A CD2  1 
ATOM   3975 H H    . LEU   A 1 270 ? 33.222  0.237   10.711  1.00 27.06  ? 255 LEU   A H    1 
ATOM   3976 H HA   . LEU   A 1 270 ? 31.377  -1.042  12.187  1.00 27.77  ? 255 LEU   A HA   1 
ATOM   3977 H HB2  . LEU   A 1 270 ? 32.704  -1.901  9.862   1.00 34.23  ? 255 LEU   A HB2  1 
ATOM   3978 H HB3  . LEU   A 1 270 ? 31.511  -2.691  10.554  1.00 34.23  ? 255 LEU   A HB3  1 
ATOM   3979 H HG   . LEU   A 1 270 ? 31.280  -0.220  9.213   1.00 32.27  ? 255 LEU   A HG   1 
ATOM   3980 H HD11 . LEU   A 1 270 ? 29.845  -1.414  7.758   1.00 35.02  ? 255 LEU   A HD11 1 
ATOM   3981 H HD12 . LEU   A 1 270 ? 31.309  -2.032  7.746   1.00 35.02  ? 255 LEU   A HD12 1 
ATOM   3982 H HD13 . LEU   A 1 270 ? 30.153  -2.742  8.574   1.00 35.02  ? 255 LEU   A HD13 1 
ATOM   3983 H HD21 . LEU   A 1 270 ? 28.946  -0.410  9.659   1.00 25.96  ? 255 LEU   A HD21 1 
ATOM   3984 H HD22 . LEU   A 1 270 ? 29.343  -1.456  10.787  1.00 25.96  ? 255 LEU   A HD22 1 
ATOM   3985 H HD23 . LEU   A 1 270 ? 29.850  0.046   10.884  1.00 25.96  ? 255 LEU   A HD23 1 
ATOM   3986 N N    . THR   A 1 271 ? 33.602  -1.420  13.649  1.00 28.15  ? 256 THR   A N    1 
ATOM   3987 C CA   . THR   A 1 271 ? 34.334  -2.167  14.659  1.00 32.36  ? 256 THR   A CA   1 
ATOM   3988 C C    . THR   A 1 271 ? 33.346  -2.839  15.597  1.00 32.00  ? 256 THR   A C    1 
ATOM   3989 O O    . THR   A 1 271 ? 32.424  -2.193  16.100  1.00 31.29  ? 256 THR   A O    1 
ATOM   3990 C CB   . THR   A 1 271 ? 35.255  -1.241  15.447  1.00 33.65  ? 256 THR   A CB   1 
ATOM   3991 O OG1  . THR   A 1 271 ? 36.149  -0.587  14.545  1.00 26.49  ? 256 THR   A OG1  1 
ATOM   3992 C CG2  . THR   A 1 271 ? 36.039  -2.021  16.481  1.00 30.72  ? 256 THR   A CG2  1 
ATOM   3993 H H    . THR   A 1 271 ? 33.505  -0.586  13.834  1.00 33.78  ? 256 THR   A H    1 
ATOM   3994 H HA   . THR   A 1 271 ? 34.882  -2.844  14.232  1.00 38.83  ? 256 THR   A HA   1 
ATOM   3995 H HB   . THR   A 1 271 ? 34.729  -0.575  15.917  1.00 40.37  ? 256 THR   A HB   1 
ATOM   3996 H HG1  . THR   A 1 271 ? 35.714  -0.125  13.994  1.00 31.79  ? 256 THR   A HG1  1 
ATOM   3997 H HG21 . THR   A 1 271 ? 36.738  -1.464  16.857  1.00 36.87  ? 256 THR   A HG21 1 
ATOM   3998 H HG22 . THR   A 1 271 ? 35.450  -2.312  17.195  1.00 36.87  ? 256 THR   A HG22 1 
ATOM   3999 H HG23 . THR   A 1 271 ? 36.445  -2.801  16.071  1.00 36.87  ? 256 THR   A HG23 1 
ATOM   4000 N N    . LYS   A 1 272 ? 33.559  -4.135  15.847  1.00 31.09  ? 257 LYS   A N    1 
ATOM   4001 C CA   . LYS   A 1 272 ? 32.582  -4.938  16.574  1.00 31.07  ? 257 LYS   A CA   1 
ATOM   4002 C C    . LYS   A 1 272 ? 32.490  -4.531  18.036  1.00 29.84  ? 257 LYS   A C    1 
ATOM   4003 O O    . LYS   A 1 272 ? 31.393  -4.318  18.562  1.00 37.50  ? 257 LYS   A O    1 
ATOM   4004 C CB   . LYS   A 1 272 ? 32.948  -6.420  16.473  1.00 32.00  ? 257 LYS   A CB   1 
ATOM   4005 C CG   . LYS   A 1 272 ? 32.030  -7.237  15.592  1.00 38.57  ? 257 LYS   A CG   1 
ATOM   4006 C CD   . LYS   A 1 272 ? 32.295  -8.743  15.741  1.00 42.73  ? 257 LYS   A CD   1 
ATOM   4007 C CE   . LYS   A 1 272 ? 33.726  -9.106  15.378  1.00 45.14  ? 257 LYS   A CE   1 
ATOM   4008 N NZ   . LYS   A 1 272 ? 33.951  -10.583 15.402  1.00 60.22  ? 257 LYS   A NZ   1 
ATOM   4009 H H    . LYS   A 1 272 ? 34.261  -4.570  15.606  1.00 37.31  ? 257 LYS   A H    1 
ATOM   4010 H HA   . LYS   A 1 272 ? 31.714  -4.796  16.165  1.00 37.28  ? 257 LYS   A HA   1 
ATOM   4011 H HB2  . LYS   A 1 272 ? 33.844  -6.493  16.108  1.00 38.40  ? 257 LYS   A HB2  1 
ATOM   4012 H HB3  . LYS   A 1 272 ? 32.920  -6.806  17.362  1.00 38.40  ? 257 LYS   A HB3  1 
ATOM   4013 H HG2  . LYS   A 1 272 ? 31.108  -7.064  15.841  1.00 46.28  ? 257 LYS   A HG2  1 
ATOM   4014 H HG3  . LYS   A 1 272 ? 32.174  -6.993  14.664  1.00 46.28  ? 257 LYS   A HG3  1 
ATOM   4015 H HD2  . LYS   A 1 272 ? 32.140  -9.006  16.662  1.00 51.27  ? 257 LYS   A HD2  1 
ATOM   4016 H HD3  . LYS   A 1 272 ? 31.700  -9.233  15.152  1.00 51.27  ? 257 LYS   A HD3  1 
ATOM   4017 H HE2  . LYS   A 1 272 ? 33.919  -8.785  14.483  1.00 54.17  ? 257 LYS   A HE2  1 
ATOM   4018 H HE3  . LYS   A 1 272 ? 34.331  -8.697  16.016  1.00 54.17  ? 257 LYS   A HE3  1 
ATOM   4019 H HZ1  . LYS   A 1 272 ? 34.795  -10.765 15.186  1.00 72.26  ? 257 LYS   A HZ1  1 
ATOM   4020 H HZ2  . LYS   A 1 272 ? 33.786  -10.903 16.216  1.00 72.26  ? 257 LYS   A HZ2  1 
ATOM   4021 H HZ3  . LYS   A 1 272 ? 33.411  -10.983 14.819  1.00 72.26  ? 257 LYS   A HZ3  1 
ATOM   4022 N N    . SER   A 1 273 ? 33.618  -4.486  18.722  1.00 31.84  ? 258 SER   A N    1 
ATOM   4023 C CA   . SER   A 1 273 ? 33.614  -4.133  20.136  1.00 36.04  ? 258 SER   A CA   1 
ATOM   4024 C C    . SER   A 1 273 ? 33.345  -2.642  20.302  1.00 32.14  ? 258 SER   A C    1 
ATOM   4025 O O    . SER   A 1 273 ? 34.034  -1.824  19.684  1.00 34.32  ? 258 SER   A O    1 
ATOM   4026 C CB   . SER   A 1 273 ? 34.952  -4.491  20.771  1.00 39.46  ? 258 SER   A CB   1 
ATOM   4027 O OG   . SER   A 1 273 ? 35.035  -3.948  22.078  1.00 63.58  ? 258 SER   A OG   1 
ATOM   4028 H H    . SER   A 1 273 ? 34.397  -4.654  18.398  1.00 38.20  ? 258 SER   A H    1 
ATOM   4029 H HA   . SER   A 1 273 ? 32.913  -4.627  20.588  1.00 43.25  ? 258 SER   A HA   1 
ATOM   4030 H HB2  . SER   A 1 273 ? 35.032  -5.457  20.823  1.00 47.36  ? 258 SER   A HB2  1 
ATOM   4031 H HB3  . SER   A 1 273 ? 35.670  -4.127  20.230  1.00 47.36  ? 258 SER   A HB3  1 
ATOM   4032 H HG   . SER   A 1 273 ? 35.776  -4.140  22.423  1.00 76.29  ? 258 SER   A HG   1 
ATOM   4033 N N    . PRO   A 1 274 ? 32.364  -2.244  21.120  1.00 41.03  ? 259 PRO   A N    1 
ATOM   4034 C CA   . PRO   A 1 274 ? 32.134  -0.804  21.317  1.00 31.88  ? 259 PRO   A CA   1 
ATOM   4035 C C    . PRO   A 1 274 ? 33.295  -0.105  22.000  1.00 41.16  ? 259 PRO   A C    1 
ATOM   4036 O O    . PRO   A 1 274 ? 33.468  1.106   21.820  1.00 39.28  ? 259 PRO   A O    1 
ATOM   4037 C CB   . PRO   A 1 274 ? 30.865  -0.757  22.182  1.00 37.41  ? 259 PRO   A CB   1 
ATOM   4038 C CG   . PRO   A 1 274 ? 30.309  -2.137  22.165  1.00 40.26  ? 259 PRO   A CG   1 
ATOM   4039 C CD   . PRO   A 1 274 ? 31.459  -3.056  21.948  1.00 41.80  ? 259 PRO   A CD   1 
ATOM   4040 H HA   . PRO   A 1 274 ? 31.951  -0.380  20.464  1.00 38.26  ? 259 PRO   A HA   1 
ATOM   4041 H HB2  . PRO   A 1 274 ? 31.096  -0.490  23.086  1.00 44.89  ? 259 PRO   A HB2  1 
ATOM   4042 H HB3  . PRO   A 1 274 ? 30.233  -0.127  21.801  1.00 44.89  ? 259 PRO   A HB3  1 
ATOM   4043 H HG2  . PRO   A 1 274 ? 29.879  -2.323  23.014  1.00 48.31  ? 259 PRO   A HG2  1 
ATOM   4044 H HG3  . PRO   A 1 274 ? 29.667  -2.218  21.442  1.00 48.31  ? 259 PRO   A HG3  1 
ATOM   4045 H HD2  . PRO   A 1 274 ? 31.877  -3.295  22.790  1.00 50.16  ? 259 PRO   A HD2  1 
ATOM   4046 H HD3  . PRO   A 1 274 ? 31.180  -3.857  21.477  1.00 50.16  ? 259 PRO   A HD3  1 
ATOM   4047 N N    . LYS   A 1 275 ? 34.096  -0.830  22.786  1.00 39.31  ? 260 LYS   A N    1 
ATOM   4048 C CA   . LYS   A 1 275 ? 35.226  -0.219  23.475  1.00 50.92  ? 260 LYS   A CA   1 
ATOM   4049 C C    . LYS   A 1 275 ? 36.331  0.217   22.521  1.00 48.72  ? 260 LYS   A C    1 
ATOM   4050 O O    . LYS   A 1 275 ? 37.161  1.052   22.894  1.00 54.33  ? 260 LYS   A O    1 
ATOM   4051 C CB   . LYS   A 1 275 ? 35.802  -1.193  24.502  1.00 50.88  ? 260 LYS   A CB   1 
ATOM   4052 C CG   . LYS   A 1 275 ? 36.028  -0.582  25.880  1.00 65.36  ? 260 LYS   A CG   1 
ATOM   4053 C CD   . LYS   A 1 275 ? 36.122  -1.654  26.962  1.00 68.69  ? 260 LYS   A CD   1 
ATOM   4054 C CE   . LYS   A 1 275 ? 36.276  -1.030  28.341  1.00 71.02  ? 260 LYS   A CE   1 
ATOM   4055 N NZ   . LYS   A 1 275 ? 36.307  -2.046  29.422  1.00 73.22  ? 260 LYS   A NZ   1 
ATOM   4056 H H    . LYS   A 1 275 ? 34.004  -1.673  22.933  1.00 47.17  ? 260 LYS   A H    1 
ATOM   4057 H HA   . LYS   A 1 275 ? 34.905  0.569   23.941  1.00 61.11  ? 260 LYS   A HA   1 
ATOM   4058 H HB2  . LYS   A 1 275 ? 35.185  -1.934  24.606  1.00 61.05  ? 260 LYS   A HB2  1 
ATOM   4059 H HB3  . LYS   A 1 275 ? 36.657  -1.515  24.178  1.00 61.05  ? 260 LYS   A HB3  1 
ATOM   4060 H HG2  . LYS   A 1 275 ? 36.858  -0.080  25.877  1.00 78.43  ? 260 LYS   A HG2  1 
ATOM   4061 H HG3  . LYS   A 1 275 ? 35.287  0.005   26.097  1.00 78.43  ? 260 LYS   A HG3  1 
ATOM   4062 H HD2  . LYS   A 1 275 ? 35.313  -2.190  26.956  1.00 82.43  ? 260 LYS   A HD2  1 
ATOM   4063 H HD3  . LYS   A 1 275 ? 36.894  -2.217  26.792  1.00 82.43  ? 260 LYS   A HD3  1 
ATOM   4064 H HE2  . LYS   A 1 275 ? 37.107  -0.530  28.372  1.00 85.22  ? 260 LYS   A HE2  1 
ATOM   4065 H HE3  . LYS   A 1 275 ? 35.526  -0.437  28.506  1.00 85.22  ? 260 LYS   A HE3  1 
ATOM   4066 H HZ1  . LYS   A 1 275 ? 36.396  -1.646  30.213  1.00 87.86  ? 260 LYS   A HZ1  1 
ATOM   4067 H HZ2  . LYS   A 1 275 ? 35.552  -2.517  29.420  1.00 87.86  ? 260 LYS   A HZ2  1 
ATOM   4068 H HZ3  . LYS   A 1 275 ? 36.993  -2.600  29.300  1.00 87.86  ? 260 LYS   A HZ3  1 
ATOM   4069 N N    . LYS   A 1 276 ? 36.369  -0.332  21.312  1.00 43.49  ? 261 LYS   A N    1 
ATOM   4070 C CA   . LYS   A 1 276 ? 37.375  0.023   20.326  1.00 37.95  ? 261 LYS   A CA   1 
ATOM   4071 C C    . LYS   A 1 276 ? 36.811  0.854   19.186  1.00 39.51  ? 261 LYS   A C    1 
ATOM   4072 O O    . LYS   A 1 276 ? 37.567  1.243   18.291  1.00 47.00  ? 261 LYS   A O    1 
ATOM   4073 C CB   . LYS   A 1 276 ? 38.022  -1.245  19.759  1.00 41.23  ? 261 LYS   A CB   1 
ATOM   4074 C CG   . LYS   A 1 276 ? 38.925  -1.990  20.736  1.00 45.21  ? 261 LYS   A CG   1 
ATOM   4075 C CD   . LYS   A 1 276 ? 40.354  -1.465  20.684  1.00 52.14  ? 261 LYS   A CD   1 
ATOM   4076 C CE   . LYS   A 1 276 ? 41.257  -2.207  21.654  1.00 57.45  ? 261 LYS   A CE   1 
ATOM   4077 N NZ   . LYS   A 1 276 ? 42.608  -1.585  21.746  1.00 65.14  ? 261 LYS   A NZ   1 
ATOM   4078 H H    . LYS   A 1 276 ? 35.810  -0.925  21.037  1.00 52.19  ? 261 LYS   A H    1 
ATOM   4079 H HA   . LYS   A 1 276 ? 38.067  0.544   20.763  1.00 45.55  ? 261 LYS   A HA   1 
ATOM   4080 H HB2  . LYS   A 1 276 ? 37.318  -1.856  19.488  1.00 49.48  ? 261 LYS   A HB2  1 
ATOM   4081 H HB3  . LYS   A 1 276 ? 38.562  -0.999  18.991  1.00 49.48  ? 261 LYS   A HB3  1 
ATOM   4082 H HG2  . LYS   A 1 276 ? 38.589  -1.871  21.638  1.00 54.25  ? 261 LYS   A HG2  1 
ATOM   4083 H HG3  . LYS   A 1 276 ? 38.937  -2.933  20.508  1.00 54.25  ? 261 LYS   A HG3  1 
ATOM   4084 H HD2  . LYS   A 1 276 ? 40.706  -1.583  19.788  1.00 62.57  ? 261 LYS   A HD2  1 
ATOM   4085 H HD3  . LYS   A 1 276 ? 40.359  -0.524  20.921  1.00 62.57  ? 261 LYS   A HD3  1 
ATOM   4086 H HE2  . LYS   A 1 276 ? 40.857  -2.194  22.537  1.00 68.94  ? 261 LYS   A HE2  1 
ATOM   4087 H HE3  . LYS   A 1 276 ? 41.366  -3.122  21.352  1.00 68.94  ? 261 LYS   A HE3  1 
ATOM   4088 H HZ1  . LYS   A 1 276 ? 43.114  -2.040  22.319  1.00 78.17  ? 261 LYS   A HZ1  1 
ATOM   4089 H HZ2  . LYS   A 1 276 ? 43.000  -1.589  20.947  1.00 78.17  ? 261 LYS   A HZ2  1 
ATOM   4090 H HZ3  . LYS   A 1 276 ? 42.536  -0.744  22.029  1.00 78.17  ? 261 LYS   A HZ3  1 
ATOM   4091 N N    . ARG   A 1 277 ? 35.512  1.124   19.183  1.00 31.35  ? 262 ARG   A N    1 
ATOM   4092 C CA   . ARG   A 1 277 ? 34.904  1.827   18.057  1.00 28.12  ? 262 ARG   A CA   1 
ATOM   4093 C C    . ARG   A 1 277 ? 35.158  3.327   18.182  1.00 29.78  ? 262 ARG   A C    1 
ATOM   4094 O O    . ARG   A 1 277 ? 34.974  3.894   19.263  1.00 27.48  ? 262 ARG   A O    1 
ATOM   4095 C CB   . ARG   A 1 277 ? 33.405  1.538   18.001  1.00 26.01  ? 262 ARG   A CB   1 
ATOM   4096 C CG   . ARG   A 1 277 ? 32.727  1.965   16.705  1.00 25.60  ? 262 ARG   A CG   1 
ATOM   4097 C CD   . ARG   A 1 277 ? 31.252  1.550   16.692  1.00 24.08  ? 262 ARG   A CD   1 
ATOM   4098 N NE   . ARG   A 1 277 ? 31.097  0.113   16.906  1.00 25.52  ? 262 ARG   A NE   1 
ATOM   4099 C CZ   . ARG   A 1 277 ? 30.120  -0.451  17.606  1.00 29.16  ? 262 ARG   A CZ   1 
ATOM   4100 N NH1  . ARG   A 1 277 ? 29.154  0.267   18.155  1.00 25.25  ? 262 ARG   A NH1  1 
ATOM   4101 N NH2  . ARG   A 1 277 ? 30.116  -1.772  17.764  1.00 30.80  ? 262 ARG   A NH2  1 
ATOM   4102 H H    . ARG   A 1 277 ? 34.965  0.915   19.812  1.00 37.62  ? 262 ARG   A H    1 
ATOM   4103 H HA   . ARG   A 1 277 ? 35.300  1.524   17.225  1.00 33.75  ? 262 ARG   A HA   1 
ATOM   4104 H HB2  . ARG   A 1 277 ? 33.271  0.583   18.102  1.00 31.21  ? 262 ARG   A HB2  1 
ATOM   4105 H HB3  . ARG   A 1 277 ? 32.972  2.013   18.728  1.00 31.21  ? 262 ARG   A HB3  1 
ATOM   4106 H HG2  . ARG   A 1 277 ? 32.775  2.930   16.618  1.00 30.73  ? 262 ARG   A HG2  1 
ATOM   4107 H HG3  . ARG   A 1 277 ? 33.171  1.542   15.953  1.00 30.73  ? 262 ARG   A HG3  1 
ATOM   4108 H HD2  . ARG   A 1 277 ? 30.782  2.016   17.400  1.00 28.90  ? 262 ARG   A HD2  1 
ATOM   4109 H HD3  . ARG   A 1 277 ? 30.863  1.774   15.832  1.00 28.90  ? 262 ARG   A HD3  1 
ATOM   4110 H HE   . ARG   A 1 277 ? 31.683  -0.407  16.551  1.00 30.63  ? 262 ARG   A HE   1 
ATOM   4111 H HH11 . ARG   A 1 277 ? 29.149  1.122   18.063  1.00 30.29  ? 262 ARG   A HH11 1 
ATOM   4112 H HH12 . ARG   A 1 277 ? 28.532  -0.121  18.604  1.00 30.29  ? 262 ARG   A HH12 1 
ATOM   4113 H HH21 . ARG   A 1 277 ? 30.741  -2.249  17.415  1.00 36.96  ? 262 ARG   A HH21 1 
ATOM   4114 H HH22 . ARG   A 1 277 ? 29.488  -2.149  18.215  1.00 36.96  ? 262 ARG   A HH22 1 
ATOM   4115 N N    . PRO   A 1 278 ? 35.579  4.001   17.113  1.00 28.47  ? 263 PRO   A N    1 
ATOM   4116 C CA   . PRO   A 1 278 ? 35.891  5.432   17.226  1.00 28.74  ? 263 PRO   A CA   1 
ATOM   4117 C C    . PRO   A 1 278 ? 34.648  6.280   17.438  1.00 28.37  ? 263 PRO   A C    1 
ATOM   4118 O O    . PRO   A 1 278 ? 33.551  5.951   16.986  1.00 29.90  ? 263 PRO   A O    1 
ATOM   4119 C CB   . PRO   A 1 278 ? 36.564  5.754   15.886  1.00 27.74  ? 263 PRO   A CB   1 
ATOM   4120 C CG   . PRO   A 1 278 ? 36.052  4.723   14.948  1.00 32.11  ? 263 PRO   A CG   1 
ATOM   4121 C CD   . PRO   A 1 278 ? 35.882  3.478   15.768  1.00 35.14  ? 263 PRO   A CD   1 
ATOM   4122 H HA   . PRO   A 1 278 ? 36.511  5.587   17.956  1.00 34.48  ? 263 PRO   A HA   1 
ATOM   4123 H HB2  . PRO   A 1 278 ? 36.312  6.645   15.595  1.00 33.29  ? 263 PRO   A HB2  1 
ATOM   4124 H HB3  . PRO   A 1 278 ? 37.528  5.695   15.976  1.00 33.29  ? 263 PRO   A HB3  1 
ATOM   4125 H HG2  . PRO   A 1 278 ? 35.203  5.010   14.577  1.00 38.53  ? 263 PRO   A HG2  1 
ATOM   4126 H HG3  . PRO   A 1 278 ? 36.695  4.581   14.235  1.00 38.53  ? 263 PRO   A HG3  1 
ATOM   4127 H HD2  . PRO   A 1 278 ? 35.147  2.941   15.432  1.00 42.17  ? 263 PRO   A HD2  1 
ATOM   4128 H HD3  . PRO   A 1 278 ? 36.699  2.955   15.776  1.00 42.17  ? 263 PRO   A HD3  1 
ATOM   4129 N N    . SER   A 1 279 ? 34.834  7.393   18.146  1.00 27.29  ? 264 SER   A N    1 
ATOM   4130 C CA   . SER   A 1 279 ? 33.748  8.310   18.454  1.00 26.78  ? 264 SER   A CA   1 
ATOM   4131 C C    . SER   A 1 279 ? 33.386  9.156   17.231  1.00 26.80  ? 264 SER   A C    1 
ATOM   4132 O O    . SER   A 1 279 ? 34.020  9.083   16.177  1.00 22.79  ? 264 SER   A O    1 
ATOM   4133 C CB   . SER   A 1 279 ? 34.134  9.204   19.630  1.00 29.89  ? 264 SER   A CB   1 
ATOM   4134 O OG   . SER   A 1 279 ? 35.254  10.008  19.312  1.00 30.80  ? 264 SER   A OG   1 
ATOM   4135 H H    . SER   A 1 279 ? 35.594  7.640   18.463  1.00 32.75  ? 264 SER   A H    1 
ATOM   4136 H HA   . SER   A 1 279 ? 32.969  7.786   18.699  1.00 32.13  ? 264 SER   A HA   1 
ATOM   4137 H HB2  . SER   A 1 279 ? 33.385  9.780   19.847  1.00 35.87  ? 264 SER   A HB2  1 
ATOM   4138 H HB3  . SER   A 1 279 ? 34.355  8.645   20.391  1.00 35.87  ? 264 SER   A HB3  1 
ATOM   4139 H HG   . SER   A 1 279 ? 35.914  9.521   19.128  1.00 36.97  ? 264 SER   A HG   1 
ATOM   4140 N N    . ALA   A 1 280 ? 32.340  9.971   17.368  1.00 23.32  ? 265 ALA   A N    1 
ATOM   4141 C CA   . ALA   A 1 280 ? 31.960  10.843  16.265  1.00 25.18  ? 265 ALA   A CA   1 
ATOM   4142 C C    . ALA   A 1 280 ? 33.034  11.897  16.023  1.00 28.50  ? 265 ALA   A C    1 
ATOM   4143 O O    . ALA   A 1 280 ? 33.412  12.156  14.876  1.00 25.35  ? 265 ALA   A O    1 
ATOM   4144 C CB   . ALA   A 1 280 ? 30.606  11.493  16.541  1.00 24.05  ? 265 ALA   A CB   1 
ATOM   4145 H H    . ALA   A 1 280 ? 31.848  10.035  18.071  1.00 27.98  ? 265 ALA   A H    1 
ATOM   4146 H HA   . ALA   A 1 280 ? 31.864  10.313  15.458  1.00 30.21  ? 265 ALA   A HA   1 
ATOM   4147 H HB1  . ALA   A 1 280 ? 30.377  12.073  15.798  1.00 28.85  ? 265 ALA   A HB1  1 
ATOM   4148 H HB2  . ALA   A 1 280 ? 29.936  10.798  16.636  1.00 28.85  ? 265 ALA   A HB2  1 
ATOM   4149 H HB3  . ALA   A 1 280 ? 30.665  12.010  17.359  1.00 28.85  ? 265 ALA   A HB3  1 
ATOM   4150 N N    . THR   A 1 281 ? 33.555  12.492  17.097  1.00 30.64  ? 266 THR   A N    1 
ATOM   4151 C CA   . THR   A 1 281 ? 34.618  13.473  16.950  1.00 28.26  ? 266 THR   A CA   1 
ATOM   4152 C C    . THR   A 1 281 ? 35.839  12.862  16.272  1.00 28.09  ? 266 THR   A C    1 
ATOM   4153 O O    . THR   A 1 281 ? 36.414  13.457  15.356  1.00 27.69  ? 266 THR   A O    1 
ATOM   4154 C CB   . THR   A 1 281 ? 34.996  14.052  18.314  1.00 26.90  ? 266 THR   A CB   1 
ATOM   4155 O OG1  . THR   A 1 281 ? 33.883  14.774  18.849  1.00 30.14  ? 266 THR   A OG1  1 
ATOM   4156 C CG2  . THR   A 1 281 ? 36.183  14.991  18.180  1.00 28.52  ? 266 THR   A CG2  1 
ATOM   4157 H H    . THR   A 1 281 ? 33.312  12.345  17.908  1.00 36.77  ? 266 THR   A H    1 
ATOM   4158 H HA   . THR   A 1 281 ? 34.294  14.199  16.395  1.00 33.92  ? 266 THR   A HA   1 
ATOM   4159 H HB   . THR   A 1 281 ? 35.238  13.332  18.917  1.00 32.29  ? 266 THR   A HB   1 
ATOM   4160 H HG1  . THR   A 1 281 ? 33.226  14.260  18.946  1.00 36.17  ? 266 THR   A HG1  1 
ATOM   4161 H HG21 . THR   A 1 281 ? 36.258  15.545  18.973  1.00 34.22  ? 266 THR   A HG21 1 
ATOM   4162 H HG22 . THR   A 1 281 ? 37.001  14.479  18.076  1.00 34.22  ? 266 THR   A HG22 1 
ATOM   4163 H HG23 . THR   A 1 281 ? 36.068  15.563  17.405  1.00 34.22  ? 266 THR   A HG23 1 
ATOM   4164 N N    . LYS   A 1 282 ? 36.262  11.677  16.713  1.00 30.30  ? 267 LYS   A N    1 
ATOM   4165 C CA   . LYS   A 1 282 ? 37.421  11.057  16.076  1.00 26.42  ? 267 LYS   A CA   1 
ATOM   4166 C C    . LYS   A 1 282 ? 37.159  10.802  14.596  1.00 25.98  ? 267 LYS   A C    1 
ATOM   4167 O O    . LYS   A 1 282 ? 38.043  11.005  13.757  1.00 28.71  ? 267 LYS   A O    1 
ATOM   4168 C CB   . LYS   A 1 282 ? 37.804  9.756   16.779  1.00 28.22  ? 267 LYS   A CB   1 
ATOM   4169 C CG   . LYS   A 1 282 ? 38.954  9.030   16.085  1.00 29.40  ? 267 LYS   A CG   1 
ATOM   4170 C CD   . LYS   A 1 282 ? 39.547  7.927   16.928  1.00 37.21  ? 267 LYS   A CD   1 
ATOM   4171 C CE   . LYS   A 1 282 ? 40.654  7.206   16.157  1.00 35.38  ? 267 LYS   A CE   1 
ATOM   4172 N NZ   . LYS   A 1 282 ? 41.289  6.118   16.939  1.00 48.80  ? 267 LYS   A NZ   1 
ATOM   4173 H H    . LYS   A 1 282 ? 35.908  11.227  17.355  1.00 36.36  ? 267 LYS   A H    1 
ATOM   4174 H HA   . LYS   A 1 282 ? 38.173  11.664  16.159  1.00 31.70  ? 267 LYS   A HA   1 
ATOM   4175 H HB2  . LYS   A 1 282 ? 38.079  9.957   17.687  1.00 33.86  ? 267 LYS   A HB2  1 
ATOM   4176 H HB3  . LYS   A 1 282 ? 37.036  9.163   16.788  1.00 33.86  ? 267 LYS   A HB3  1 
ATOM   4177 H HG2  . LYS   A 1 282 ? 38.627  8.634   15.262  1.00 35.28  ? 267 LYS   A HG2  1 
ATOM   4178 H HG3  . LYS   A 1 282 ? 39.658  9.668   15.889  1.00 35.28  ? 267 LYS   A HG3  1 
ATOM   4179 H HD2  . LYS   A 1 282 ? 39.927  8.304   17.737  1.00 44.65  ? 267 LYS   A HD2  1 
ATOM   4180 H HD3  . LYS   A 1 282 ? 38.857  7.284   17.154  1.00 44.65  ? 267 LYS   A HD3  1 
ATOM   4181 H HE2  . LYS   A 1 282 ? 40.277  6.816   15.354  1.00 42.45  ? 267 LYS   A HE2  1 
ATOM   4182 H HE3  . LYS   A 1 282 ? 41.344  7.847   15.923  1.00 42.45  ? 267 LYS   A HE3  1 
ATOM   4183 H HZ1  . LYS   A 1 282 ? 41.929  5.731   16.457  1.00 58.56  ? 267 LYS   A HZ1  1 
ATOM   4184 H HZ2  . LYS   A 1 282 ? 41.647  6.448   17.684  1.00 58.56  ? 267 LYS   A HZ2  1 
ATOM   4185 H HZ3  . LYS   A 1 282 ? 40.681  5.506   17.157  1.00 58.56  ? 267 LYS   A HZ3  1 
ATOM   4186 N N    . MET   A 1 283 ? 35.945  10.360  14.257  1.00 26.52  ? 268 MET   A N    1 
ATOM   4187 C CA   . MET   A 1 283 ? 35.613  10.086  12.862  1.00 24.71  ? 268 MET   A CA   1 
ATOM   4188 C C    . MET   A 1 283 ? 35.613  11.357  12.015  1.00 26.82  ? 268 MET   A C    1 
ATOM   4189 O O    . MET   A 1 283 ? 35.899  11.299  10.814  1.00 22.95  ? 268 MET   A O    1 
ATOM   4190 C CB   . MET   A 1 283 ? 34.248  9.395   12.785  1.00 21.39  ? 268 MET   A CB   1 
ATOM   4191 C CG   . MET   A 1 283 ? 34.260  7.919   13.238  1.00 25.79  ? 268 MET   A CG   1 
ATOM   4192 S SD   . MET   A 1 283 ? 35.509  6.899   12.403  1.00 28.36  ? 268 MET   A SD   1 
ATOM   4193 C CE   . MET   A 1 283 ? 35.184  7.298   10.700  1.00 24.64  ? 268 MET   A CE   1 
ATOM   4194 H H    . MET   A 1 283 ? 35.304  10.213  14.811  1.00 31.83  ? 268 MET   A H    1 
ATOM   4195 H HA   . MET   A 1 283 ? 36.278  9.480   12.500  1.00 29.66  ? 268 MET   A HA   1 
ATOM   4196 H HB2  . MET   A 1 283 ? 33.626  9.873   13.355  1.00 25.67  ? 268 MET   A HB2  1 
ATOM   4197 H HB3  . MET   A 1 283 ? 33.941  9.419   11.865  1.00 25.67  ? 268 MET   A HB3  1 
ATOM   4198 H HG2  . MET   A 1 283 ? 34.443  7.887   14.190  1.00 30.95  ? 268 MET   A HG2  1 
ATOM   4199 H HG3  . MET   A 1 283 ? 33.391  7.530   13.054  1.00 30.95  ? 268 MET   A HG3  1 
ATOM   4200 H HE1  . MET   A 1 283 ? 35.729  6.731   10.133  1.00 29.57  ? 268 MET   A HE1  1 
ATOM   4201 H HE2  . MET   A 1 283 ? 34.244  7.145   10.514  1.00 29.57  ? 268 MET   A HE2  1 
ATOM   4202 H HE3  . MET   A 1 283 ? 35.404  8.230   10.546  1.00 29.57  ? 268 MET   A HE3  1 
ATOM   4203 N N    . LEU   A 1 284 ? 35.294  12.507  12.612  1.00 28.83  ? 269 LEU   A N    1 
ATOM   4204 C CA   . LEU   A 1 284 ? 35.315  13.761  11.865  1.00 22.28  ? 269 LEU   A CA   1 
ATOM   4205 C C    . LEU   A 1 284 ? 36.722  14.142  11.429  1.00 25.47  ? 269 LEU   A C    1 
ATOM   4206 O O    . LEU   A 1 284 ? 36.873  14.987  10.538  1.00 29.02  ? 269 LEU   A O    1 
ATOM   4207 C CB   . LEU   A 1 284 ? 34.693  14.882  12.706  1.00 30.44  ? 269 LEU   A CB   1 
ATOM   4208 C CG   . LEU   A 1 284 ? 33.159  14.899  12.695  1.00 27.78  ? 269 LEU   A CG   1 
ATOM   4209 C CD1  . LEU   A 1 284 ? 32.610  15.893  13.700  1.00 29.41  ? 269 LEU   A CD1  1 
ATOM   4210 C CD2  . LEU   A 1 284 ? 32.639  15.215  11.301  1.00 26.82  ? 269 LEU   A CD2  1 
ATOM   4211 H H    . LEU   A 1 284 ? 35.065  12.586  13.437  1.00 34.59  ? 269 LEU   A H    1 
ATOM   4212 H HA   . LEU   A 1 284 ? 34.776  13.662  11.065  1.00 26.73  ? 269 LEU   A HA   1 
ATOM   4213 H HB2  . LEU   A 1 284 ? 34.980  14.775  13.626  1.00 36.53  ? 269 LEU   A HB2  1 
ATOM   4214 H HB3  . LEU   A 1 284 ? 35.000  15.735  12.360  1.00 36.53  ? 269 LEU   A HB3  1 
ATOM   4215 H HG   . LEU   A 1 284 ? 32.843  14.018  12.950  1.00 33.34  ? 269 LEU   A HG   1 
ATOM   4216 H HD11 . LEU   A 1 284 ? 31.640  15.872  13.668  1.00 35.29  ? 269 LEU   A HD11 1 
ATOM   4217 H HD12 . LEU   A 1 284 ? 32.916  15.648  14.587  1.00 35.29  ? 269 LEU   A HD12 1 
ATOM   4218 H HD13 . LEU   A 1 284 ? 32.929  16.781  13.474  1.00 35.29  ? 269 LEU   A HD13 1 
ATOM   4219 H HD21 . LEU   A 1 284 ? 31.702  15.460  11.362  1.00 32.19  ? 269 LEU   A HD21 1 
ATOM   4220 H HD22 . LEU   A 1 284 ? 33.150  15.953  10.934  1.00 32.19  ? 269 LEU   A HD22 1 
ATOM   4221 H HD23 . LEU   A 1 284 ? 32.741  14.430  10.740  1.00 32.19  ? 269 LEU   A HD23 1 
ATOM   4222 N N    . SER   A 1 285 ? 37.744  13.541  12.024  1.00 24.93  ? 270 SER   A N    1 
ATOM   4223 C CA   . SER   A 1 285 ? 39.120  13.713  11.585  1.00 30.35  ? 270 SER   A CA   1 
ATOM   4224 C C    . SER   A 1 285 ? 39.534  12.710  10.516  1.00 36.10  ? 270 SER   A C    1 
ATOM   4225 O O    . SER   A 1 285 ? 40.700  12.710  10.110  1.00 30.24  ? 270 SER   A O    1 
ATOM   4226 C CB   . SER   A 1 285 ? 40.073  13.584  12.777  1.00 28.22  ? 270 SER   A CB   1 
ATOM   4227 O OG   . SER   A 1 285 ? 39.798  14.568  13.756  1.00 47.46  ? 270 SER   A OG   1 
ATOM   4228 H H    . SER   A 1 285 ? 37.663  13.015  12.700  1.00 29.91  ? 270 SER   A H    1 
ATOM   4229 H HA   . SER   A 1 285 ? 39.210  14.605  11.215  1.00 36.42  ? 270 SER   A HA   1 
ATOM   4230 H HB2  . SER   A 1 285 ? 39.964  12.706  13.173  1.00 33.87  ? 270 SER   A HB2  1 
ATOM   4231 H HB3  . SER   A 1 285 ? 40.985  13.697  12.465  1.00 33.87  ? 270 SER   A HB3  1 
ATOM   4232 H HG   . SER   A 1 285 ? 40.307  14.465  14.416  1.00 56.95  ? 270 SER   A HG   1 
ATOM   4233 N N    . HIS   A 1 286 ? 38.629  11.848  10.062  1.00 32.79  ? 271 HIS   A N    1 
ATOM   4234 C CA   . HIS   A 1 286 ? 39.009  10.831  9.094   1.00 26.11  ? 271 HIS   A CA   1 
ATOM   4235 C C    . HIS   A 1 286 ? 39.202  11.435  7.708   1.00 30.38  ? 271 HIS   A C    1 
ATOM   4236 O O    . HIS   A 1 286 ? 38.477  12.345  7.302   1.00 26.36  ? 271 HIS   A O    1 
ATOM   4237 C CB   . HIS   A 1 286 ? 37.956  9.731   9.028   1.00 23.01  ? 271 HIS   A CB   1 
ATOM   4238 C CG   . HIS   A 1 286 ? 38.402  8.522   8.267   1.00 23.21  ? 271 HIS   A CG   1 
ATOM   4239 N ND1  . HIS   A 1 286 ? 38.210  8.387   6.910   1.00 22.95  ? 271 HIS   A ND1  1 
ATOM   4240 C CD2  . HIS   A 1 286 ? 39.033  7.394   8.672   1.00 25.65  ? 271 HIS   A CD2  1 
ATOM   4241 C CE1  . HIS   A 1 286 ? 38.705  7.230   6.508   1.00 24.52  ? 271 HIS   A CE1  1 
ATOM   4242 N NE2  . HIS   A 1 286 ? 39.207  6.604   7.560   1.00 26.42  ? 271 HIS   A NE2  1 
ATOM   4243 H H    . HIS   A 1 286 ? 37.801  11.833  10.295  1.00 39.34  ? 271 HIS   A H    1 
ATOM   4244 H HA   . HIS   A 1 286 ? 39.850  10.437  9.375   1.00 31.33  ? 271 HIS   A HA   1 
ATOM   4245 H HB2  . HIS   A 1 286 ? 37.741  9.451   9.931   1.00 27.62  ? 271 HIS   A HB2  1 
ATOM   4246 H HB3  . HIS   A 1 286 ? 37.164  10.082  8.592   1.00 27.62  ? 271 HIS   A HB3  1 
ATOM   4247 H HD2  . HIS   A 1 286 ? 39.299  7.191   9.540   1.00 30.78  ? 271 HIS   A HD2  1 
ATOM   4248 H HE1  . HIS   A 1 286 ? 38.702  6.911   5.635   1.00 29.42  ? 271 HIS   A HE1  1 
ATOM   4249 H HE2  . HIS   A 1 286 ? 39.580  5.829   7.549   1.00 31.70  ? 271 HIS   A HE2  1 
ATOM   4250 N N    . GLN   A 1 287 ? 40.182  10.902  6.976   1.00 25.82  ? 272 GLN   A N    1 
ATOM   4251 C CA   . GLN   A 1 287 ? 40.497  11.410  5.648   1.00 25.36  ? 272 GLN   A CA   1 
ATOM   4252 C C    . GLN   A 1 287 ? 39.240  11.581  4.801   1.00 31.99  ? 272 GLN   A C    1 
ATOM   4253 O O    . GLN   A 1 287 ? 39.047  12.615  4.155   1.00 28.38  ? 272 GLN   A O    1 
ATOM   4254 C CB   . GLN   A 1 287 ? 41.489  10.466  4.965   1.00 29.95  ? 272 GLN   A CB   1 
ATOM   4255 C CG   . GLN   A 1 287 ? 42.144  11.051  3.753   1.00 34.82  ? 272 GLN   A CG   1 
ATOM   4256 C CD   . GLN   A 1 287 ? 43.079  10.087  3.048   1.00 41.36  ? 272 GLN   A CD   1 
ATOM   4257 O OE1  . GLN   A 1 287 ? 43.233  8.937   3.452   1.00 32.52  ? 272 GLN   A OE1  1 
ATOM   4258 N NE2  . GLN   A 1 287 ? 43.723  10.567  1.992   1.00 46.04  ? 272 GLN   A NE2  1 
ATOM   4259 H H    . GLN   A 1 287 ? 40.677  10.246  7.227   1.00 30.99  ? 272 GLN   A H    1 
ATOM   4260 H HA   . GLN   A 1 287 ? 40.911  12.283  5.734   1.00 30.43  ? 272 GLN   A HA   1 
ATOM   4261 H HB2  . GLN   A 1 287 ? 42.188  10.238  5.598   1.00 35.94  ? 272 GLN   A HB2  1 
ATOM   4262 H HB3  . GLN   A 1 287 ? 41.017  9.664   4.689   1.00 35.94  ? 272 GLN   A HB3  1 
ATOM   4263 H HG2  . GLN   A 1 287 ? 41.456  11.313  3.122   1.00 41.79  ? 272 GLN   A HG2  1 
ATOM   4264 H HG3  . GLN   A 1 287 ? 42.662  11.826  4.021   1.00 41.79  ? 272 GLN   A HG3  1 
ATOM   4265 H HE21 . GLN   A 1 287 ? 43.597  11.382  1.745   1.00 55.25  ? 272 GLN   A HE21 1 
ATOM   4266 H HE22 . GLN   A 1 287 ? 44.266  10.064  1.554   1.00 55.25  ? 272 GLN   A HE22 1 
ATOM   4267 N N    . LEU   A 1 288 ? 38.351  10.582  4.818   1.00 24.07  ? 273 LEU   A N    1 
ATOM   4268 C CA   . LEU   A 1 288 ? 37.208  10.592  3.907   1.00 25.58  ? 273 LEU   A CA   1 
ATOM   4269 C C    . LEU   A 1 288 ? 36.335  11.830  4.077   1.00 29.65  ? 273 LEU   A C    1 
ATOM   4270 O O    . LEU   A 1 288 ? 35.863  12.397  3.085   1.00 27.47  ? 273 LEU   A O    1 
ATOM   4271 C CB   . LEU   A 1 288 ? 36.352  9.349   4.116   1.00 22.43  ? 273 LEU   A CB   1 
ATOM   4272 C CG   . LEU   A 1 288 ? 35.263  9.166   3.056   1.00 25.84  ? 273 LEU   A CG   1 
ATOM   4273 C CD1  . LEU   A 1 288 ? 35.865  8.648   1.745   1.00 25.63  ? 273 LEU   A CD1  1 
ATOM   4274 C CD2  . LEU   A 1 288 ? 34.181  8.229   3.561   1.00 29.84  ? 273 LEU   A CD2  1 
ATOM   4275 H H    . LEU   A 1 288 ? 38.388  9.899   5.338   1.00 28.89  ? 273 LEU   A H    1 
ATOM   4276 H HA   . LEU   A 1 288 ? 37.563  10.592  3.005   1.00 30.70  ? 273 LEU   A HA   1 
ATOM   4277 H HB2  . LEU   A 1 288 ? 36.926  8.567   4.089   1.00 26.91  ? 273 LEU   A HB2  1 
ATOM   4278 H HB3  . LEU   A 1 288 ? 35.917  9.412   4.980   1.00 26.91  ? 273 LEU   A HB3  1 
ATOM   4279 H HG   . LEU   A 1 288 ? 34.852  10.025  2.873   1.00 31.01  ? 273 LEU   A HG   1 
ATOM   4280 H HD11 . LEU   A 1 288 ? 35.151  8.501   1.105   1.00 30.76  ? 273 LEU   A HD11 1 
ATOM   4281 H HD12 . LEU   A 1 288 ? 36.487  9.308   1.400   1.00 30.76  ? 273 LEU   A HD12 1 
ATOM   4282 H HD13 . LEU   A 1 288 ? 36.331  7.814   1.918   1.00 30.76  ? 273 LEU   A HD13 1 
ATOM   4283 H HD21 . LEU   A 1 288 ? 33.505  8.127   2.873   1.00 35.81  ? 273 LEU   A HD21 1 
ATOM   4284 H HD22 . LEU   A 1 288 ? 34.579  7.368   3.764   1.00 35.81  ? 273 LEU   A HD22 1 
ATOM   4285 H HD23 . LEU   A 1 288 ? 33.785  8.607   4.361   1.00 35.81  ? 273 LEU   A HD23 1 
ATOM   4286 N N    . VAL   A 1 289 ? 36.052  12.223  5.326   1.00 22.79  ? 274 VAL   A N    1 
ATOM   4287 C CA   . VAL   A 1 289 ? 35.181  13.356  5.610   1.00 25.38  ? 274 VAL   A CA   1 
ATOM   4288 C C    . VAL   A 1 289 ? 35.952  14.650  5.841   1.00 28.25  ? 274 VAL   A C    1 
ATOM   4289 O O    . VAL   A 1 289 ? 35.327  15.700  6.034   1.00 27.97  ? 274 VAL   A O    1 
ATOM   4290 C CB   . VAL   A 1 289 ? 34.276  13.078  6.830   1.00 24.81  ? 274 VAL   A CB   1 
ATOM   4291 C CG1  . VAL   A 1 289 ? 33.407  11.852  6.581   1.00 26.66  ? 274 VAL   A CG1  1 
ATOM   4292 C CG2  . VAL   A 1 289 ? 35.106  12.890  8.103   1.00 25.04  ? 274 VAL   A CG2  1 
ATOM   4293 H H    . VAL   A 1 289 ? 36.359  11.839  6.032   1.00 27.35  ? 274 VAL   A H    1 
ATOM   4294 H HA   . VAL   A 1 289 ? 34.618  13.484  4.830   1.00 30.46  ? 274 VAL   A HA   1 
ATOM   4295 H HB   . VAL   A 1 289 ? 33.698  13.845  6.962   1.00 29.77  ? 274 VAL   A HB   1 
ATOM   4296 H HG11 . VAL   A 1 289 ? 32.811  11.728  7.336   1.00 31.99  ? 274 VAL   A HG11 1 
ATOM   4297 H HG12 . VAL   A 1 289 ? 32.891  11.990  5.771   1.00 31.99  ? 274 VAL   A HG12 1 
ATOM   4298 H HG13 . VAL   A 1 289 ? 33.979  11.075  6.480   1.00 31.99  ? 274 VAL   A HG13 1 
ATOM   4299 H HG21 . VAL   A 1 289 ? 34.519  12.616  8.825   1.00 30.04  ? 274 VAL   A HG21 1 
ATOM   4300 H HG22 . VAL   A 1 289 ? 35.776  12.207  7.945   1.00 30.04  ? 274 VAL   A HG22 1 
ATOM   4301 H HG23 . VAL   A 1 289 ? 35.536  13.730  8.326   1.00 30.04  ? 274 VAL   A HG23 1 
ATOM   4302 N N    . SER   A 1 290 ? 37.286  14.604  5.857   1.00 28.55  ? 275 SER   A N    1 
ATOM   4303 C CA   . SER   A 1 290 ? 38.110  15.786  6.068   1.00 25.98  ? 275 SER   A CA   1 
ATOM   4304 C C    . SER   A 1 290 ? 38.622  16.380  4.768   1.00 31.98  ? 275 SER   A C    1 
ATOM   4305 O O    . SER   A 1 290 ? 39.185  17.480  4.782   1.00 29.46  ? 275 SER   A O    1 
ATOM   4306 C CB   . SER   A 1 290 ? 39.308  15.448  6.963   1.00 26.29  ? 275 SER   A CB   1 
ATOM   4307 O OG   . SER   A 1 290 ? 38.874  15.208  8.284   1.00 44.66  ? 275 SER   A OG   1 
ATOM   4308 H H    . SER   A 1 290 ? 37.743  13.884  5.744   1.00 34.25  ? 275 SER   A H    1 
ATOM   4309 H HA   . SER   A 1 290 ? 37.578  16.457  6.524   1.00 31.18  ? 275 SER   A HA   1 
ATOM   4310 H HB2  . SER   A 1 290 ? 39.746  14.652  6.622   1.00 31.55  ? 275 SER   A HB2  1 
ATOM   4311 H HB3  . SER   A 1 290 ? 39.928  16.194  6.961   1.00 31.55  ? 275 SER   A HB3  1 
ATOM   4312 H HG   . SER   A 1 290 ? 38.336  14.563  8.297   1.00 53.59  ? 275 SER   A HG   1 
ATOM   4313 N N    . GLN   A 1 291 ? 38.437  15.686  3.652   1.00 32.26  ? 276 GLN   A N    1 
ATOM   4314 C CA   . GLN   A 1 291 ? 39.011  16.125  2.395   1.00 39.64  ? 276 GLN   A CA   1 
ATOM   4315 C C    . GLN   A 1 291 ? 38.317  17.396  1.899   1.00 31.78  ? 276 GLN   A C    1 
ATOM   4316 O O    . GLN   A 1 291 ? 37.174  17.680  2.256   1.00 31.93  ? 276 GLN   A O    1 
ATOM   4317 C CB   . GLN   A 1 291 ? 38.905  15.012  1.354   1.00 29.12  ? 276 GLN   A CB   1 
ATOM   4318 C CG   . GLN   A 1 291 ? 37.517  14.462  1.179   1.00 36.39  ? 276 GLN   A CG   1 
ATOM   4319 C CD   . GLN   A 1 291 ? 37.450  13.367  0.141   1.00 31.04  ? 276 GLN   A CD   1 
ATOM   4320 O OE1  . GLN   A 1 291 ? 38.149  13.418  -0.863  1.00 37.24  ? 276 GLN   A OE1  1 
ATOM   4321 N NE2  . GLN   A 1 291 ? 36.596  12.367  0.378   1.00 25.26  ? 276 GLN   A NE2  1 
ATOM   4322 H H    . GLN   A 1 291 ? 37.983  14.958  3.599   1.00 38.72  ? 276 GLN   A H    1 
ATOM   4323 H HA   . GLN   A 1 291 ? 39.950  16.333  2.519   1.00 47.56  ? 276 GLN   A HA   1 
ATOM   4324 H HB2  . GLN   A 1 291 ? 39.194  15.361  0.497   1.00 34.94  ? 276 GLN   A HB2  1 
ATOM   4325 H HB3  . GLN   A 1 291 ? 39.480  14.279  1.624   1.00 34.94  ? 276 GLN   A HB3  1 
ATOM   4326 H HG2  . GLN   A 1 291 ? 37.214  14.094  2.024   1.00 43.67  ? 276 GLN   A HG2  1 
ATOM   4327 H HG3  . GLN   A 1 291 ? 36.926  15.178  0.898   1.00 43.67  ? 276 GLN   A HG3  1 
ATOM   4328 H HE21 . GLN   A 1 291 ? 36.119  12.369  1.093   1.00 30.31  ? 276 GLN   A HE21 1 
ATOM   4329 H HE22 . GLN   A 1 291 ? 36.524  11.721  -0.186  1.00 30.31  ? 276 GLN   A HE22 1 
ATOM   4330 N N    . PRO   A 1 292 ? 39.017  18.189  1.082   1.00 35.89  ? 277 PRO   A N    1 
ATOM   4331 C CA   . PRO   A 1 292 ? 38.410  19.407  0.542   1.00 34.11  ? 277 PRO   A CA   1 
ATOM   4332 C C    . PRO   A 1 292 ? 37.340  19.083  -0.488  1.00 28.65  ? 277 PRO   A C    1 
ATOM   4333 O O    . PRO   A 1 292 ? 37.243  17.962  -1.000  1.00 36.72  ? 277 PRO   A O    1 
ATOM   4334 C CB   . PRO   A 1 292 ? 39.599  20.136  -0.103  1.00 37.60  ? 277 PRO   A CB   1 
ATOM   4335 C CG   . PRO   A 1 292 ? 40.537  19.038  -0.478  1.00 38.25  ? 277 PRO   A CG   1 
ATOM   4336 C CD   . PRO   A 1 292 ? 40.397  18.001  0.602   1.00 39.02  ? 277 PRO   A CD   1 
ATOM   4337 H HA   . PRO   A 1 292 ? 38.032  19.954  1.248   1.00 40.93  ? 277 PRO   A HA   1 
ATOM   4338 H HB2  . PRO   A 1 292 ? 39.305  20.629  -0.885  1.00 45.12  ? 277 PRO   A HB2  1 
ATOM   4339 H HB3  . PRO   A 1 292 ? 40.006  20.742  0.537   1.00 45.12  ? 277 PRO   A HB3  1 
ATOM   4340 H HG2  . PRO   A 1 292 ? 40.286  18.673  -1.341  1.00 45.91  ? 277 PRO   A HG2  1 
ATOM   4341 H HG3  . PRO   A 1 292 ? 41.444  19.379  -0.514  1.00 45.91  ? 277 PRO   A HG3  1 
ATOM   4342 H HD2  . PRO   A 1 292 ? 40.518  17.109  0.241   1.00 46.83  ? 277 PRO   A HD2  1 
ATOM   4343 H HD3  . PRO   A 1 292 ? 41.035  18.159  1.316   1.00 46.83  ? 277 PRO   A HD3  1 
ATOM   4344 N N    . GLY   A 1 293 ? 36.519  20.078  -0.778  1.00 29.92  ? 278 GLY   A N    1 
ATOM   4345 C CA   . GLY   A 1 293 ? 35.528  19.943  -1.820  1.00 28.97  ? 278 GLY   A CA   1 
ATOM   4346 C C    . GLY   A 1 293 ? 34.244  19.277  -1.405  1.00 30.15  ? 278 GLY   A C    1 
ATOM   4347 O O    . GLY   A 1 293 ? 33.424  18.960  -2.272  1.00 38.00  ? 278 GLY   A O    1 
ATOM   4348 H H    . GLY   A 1 293 ? 36.519  20.842  -0.383  1.00 35.91  ? 278 GLY   A H    1 
ATOM   4349 H HA2  . GLY   A 1 293 ? 35.306  20.827  -2.152  1.00 34.76  ? 278 GLY   A HA2  1 
ATOM   4350 H HA3  . GLY   A 1 293 ? 35.909  19.420  -2.543  1.00 34.76  ? 278 GLY   A HA3  1 
ATOM   4351 N N    . LEU   A 1 294 ? 34.031  19.051  -0.111  1.00 30.06  ? 279 LEU   A N    1 
ATOM   4352 C CA   . LEU   A 1 294 ? 32.766  18.509  0.370   1.00 26.34  ? 279 LEU   A CA   1 
ATOM   4353 C C    . LEU   A 1 294 ? 31.862  19.689  0.703   1.00 29.78  ? 279 LEU   A C    1 
ATOM   4354 O O    . LEU   A 1 294 ? 32.141  20.447  1.637   1.00 27.56  ? 279 LEU   A O    1 
ATOM   4355 C CB   . LEU   A 1 294 ? 32.976  17.603  1.577   1.00 28.03  ? 279 LEU   A CB   1 
ATOM   4356 C CG   . LEU   A 1 294 ? 33.952  16.434  1.374   1.00 27.41  ? 279 LEU   A CG   1 
ATOM   4357 C CD1  . LEU   A 1 294 ? 33.930  15.514  2.570   1.00 27.54  ? 279 LEU   A CD1  1 
ATOM   4358 C CD2  . LEU   A 1 294 ? 33.631  15.665  0.114   1.00 24.43  ? 279 LEU   A CD2  1 
ATOM   4359 H H    . LEU   A 1 294 ? 34.607  19.204  0.508   1.00 36.07  ? 279 LEU   A H    1 
ATOM   4360 H HA   . LEU   A 1 294 ? 32.349  17.972  -0.322  1.00 31.60  ? 279 LEU   A HA   1 
ATOM   4361 H HB2  . LEU   A 1 294 ? 33.321  18.143  2.305   1.00 33.63  ? 279 LEU   A HB2  1 
ATOM   4362 H HB3  . LEU   A 1 294 ? 32.118  17.223  1.823   1.00 33.63  ? 279 LEU   A HB3  1 
ATOM   4363 H HG   . LEU   A 1 294 ? 34.847  16.794  1.280   1.00 32.89  ? 279 LEU   A HG   1 
ATOM   4364 H HD11 . LEU   A 1 294 ? 34.555  14.787  2.421   1.00 33.05  ? 279 LEU   A HD11 1 
ATOM   4365 H HD12 . LEU   A 1 294 ? 34.188  16.016  3.359   1.00 33.05  ? 279 LEU   A HD12 1 
ATOM   4366 H HD13 . LEU   A 1 294 ? 33.033  15.161  2.681   1.00 33.05  ? 279 LEU   A HD13 1 
ATOM   4367 H HD21 . LEU   A 1 294 ? 34.160  14.852  0.096   1.00 29.32  ? 279 LEU   A HD21 1 
ATOM   4368 H HD22 . LEU   A 1 294 ? 32.687  15.446  0.109   1.00 29.32  ? 279 LEU   A HD22 1 
ATOM   4369 H HD23 . LEU   A 1 294 ? 33.847  16.216  -0.655  1.00 29.32  ? 279 LEU   A HD23 1 
ATOM   4370 N N    . ASN   A 1 295 ? 30.795  19.857  -0.074  1.00 26.05  ? 280 ASN   A N    1 
ATOM   4371 C CA   . ASN   A 1 295 ? 29.831  20.922  0.165   1.00 31.04  ? 280 ASN   A CA   1 
ATOM   4372 C C    . ASN   A 1 295 ? 28.512  20.530  -0.479  1.00 27.47  ? 280 ASN   A C    1 
ATOM   4373 O O    . ASN   A 1 295 ? 28.432  19.576  -1.256  1.00 25.96  ? 280 ASN   A O    1 
ATOM   4374 C CB   . ASN   A 1 295 ? 30.322  22.260  -0.388  1.00 27.82  ? 280 ASN   A CB   1 
ATOM   4375 C CG   . ASN   A 1 295 ? 30.559  22.212  -1.873  1.00 33.73  ? 280 ASN   A CG   1 
ATOM   4376 O OD1  . ASN   A 1 295 ? 29.631  22.013  -2.659  1.00 30.95  ? 280 ASN   A OD1  1 
ATOM   4377 N ND2  . ASN   A 1 295 ? 31.802  22.408  -2.274  1.00 36.16  ? 280 ASN   A ND2  1 
ATOM   4378 H H    . ASN   A 1 295 ? 30.607  19.362  -0.751  1.00 31.25  ? 280 ASN   A H    1 
ATOM   4379 H HA   . ASN   A 1 295 ? 29.696  21.015  1.121   1.00 37.25  ? 280 ASN   A HA   1 
ATOM   4380 H HB2  . ASN   A 1 295 ? 29.655  22.941  -0.210  1.00 33.39  ? 280 ASN   A HB2  1 
ATOM   4381 H HB3  . ASN   A 1 295 ? 31.158  22.494  0.044   1.00 33.39  ? 280 ASN   A HB3  1 
ATOM   4382 H HD21 . ASN   A 1 295 ? 31.991  22.391  -3.113  1.00 43.40  ? 280 ASN   A HD21 1 
ATOM   4383 H HD22 . ASN   A 1 295 ? 32.423  22.553  -1.696  1.00 43.40  ? 280 ASN   A HD22 1 
ATOM   4384 N N    . ARG   A 1 296 ? 27.478  21.308  -0.162  1.00 27.45  ? 281 ARG   A N    1 
ATOM   4385 C CA   . ARG   A 1 296 ? 26.129  21.004  -0.619  1.00 26.25  ? 281 ARG   A CA   1 
ATOM   4386 C C    . ARG   A 1 296 ? 26.013  20.973  -2.136  1.00 26.78  ? 281 ARG   A C    1 
ATOM   4387 O O    . ARG   A 1 296 ? 25.041  20.410  -2.654  1.00 29.14  ? 281 ARG   A O    1 
ATOM   4388 C CB   . ARG   A 1 296 ? 25.155  22.033  -0.042  1.00 26.14  ? 281 ARG   A CB   1 
ATOM   4389 C CG   . ARG   A 1 296 ? 25.436  23.462  -0.519  1.00 26.80  ? 281 ARG   A CG   1 
ATOM   4390 C CD   . ARG   A 1 296 ? 24.667  24.472  0.301   1.00 29.96  ? 281 ARG   A CD   1 
ATOM   4391 N NE   . ARG   A 1 296 ? 24.866  25.825  -0.215  1.00 23.58  ? 281 ARG   A NE   1 
ATOM   4392 C CZ   . ARG   A 1 296 ? 24.018  26.459  -1.016  1.00 25.08  ? 281 ARG   A CZ   1 
ATOM   4393 N NH1  . ARG   A 1 296 ? 22.863  25.921  -1.368  1.00 29.05  ? 281 ARG   A NH1  1 
ATOM   4394 N NH2  . ARG   A 1 296 ? 24.335  27.668  -1.469  1.00 28.43  ? 281 ARG   A NH2  1 
ATOM   4395 H H    . ARG   A 1 296 ? 27.533  22.019  0.318   1.00 32.94  ? 281 ARG   A H    1 
ATOM   4396 H HA   . ARG   A 1 296 ? 25.880  20.125  -0.294  1.00 31.50  ? 281 ARG   A HA   1 
ATOM   4397 H HB2  . ARG   A 1 296 ? 24.254  21.800  -0.313  1.00 31.37  ? 281 ARG   A HB2  1 
ATOM   4398 H HB3  . ARG   A 1 296 ? 25.224  22.023  0.926   1.00 31.37  ? 281 ARG   A HB3  1 
ATOM   4399 H HG2  . ARG   A 1 296 ? 26.383  23.652  -0.429  1.00 32.16  ? 281 ARG   A HG2  1 
ATOM   4400 H HG3  . ARG   A 1 296 ? 25.166  23.551  -1.446  1.00 32.16  ? 281 ARG   A HG3  1 
ATOM   4401 H HD2  . ARG   A 1 296 ? 23.720  24.265  0.263   1.00 35.95  ? 281 ARG   A HD2  1 
ATOM   4402 H HD3  . ARG   A 1 296 ? 24.977  24.445  1.219   1.00 35.95  ? 281 ARG   A HD3  1 
ATOM   4403 H HE   . ARG   A 1 296 ? 25.582  26.239  0.016   1.00 28.29  ? 281 ARG   A HE   1 
ATOM   4404 H HH11 . ARG   A 1 296 ? 22.645  25.142  -1.076  1.00 34.87  ? 281 ARG   A HH11 1 
ATOM   4405 H HH12 . ARG   A 1 296 ? 22.329  26.350  -1.888  1.00 34.87  ? 281 ARG   A HH12 1 
ATOM   4406 H HH21 . ARG   A 1 296 ? 25.081  28.031  -1.243  1.00 34.12  ? 281 ARG   A HH21 1 
ATOM   4407 H HH22 . ARG   A 1 296 ? 23.793  28.088  -1.989  1.00 34.12  ? 281 ARG   A HH22 1 
ATOM   4408 N N    . GLY   A 1 297 ? 26.953  21.579  -2.859  1.00 24.42  ? 282 GLY   A N    1 
ATOM   4409 C CA   . GLY   A 1 297 ? 26.947  21.455  -4.310  1.00 28.45  ? 282 GLY   A CA   1 
ATOM   4410 C C    . GLY   A 1 297 ? 26.868  20.011  -4.782  1.00 29.84  ? 282 GLY   A C    1 
ATOM   4411 O O    . GLY   A 1 297 ? 26.207  19.705  -5.776  1.00 28.20  ? 282 GLY   A O    1 
ATOM   4412 H H    . GLY   A 1 297 ? 27.591  22.059  -2.539  1.00 29.31  ? 282 GLY   A H    1 
ATOM   4413 H HA2  . GLY   A 1 297 ? 26.183  21.934  -4.668  1.00 34.14  ? 282 GLY   A HA2  1 
ATOM   4414 H HA3  . GLY   A 1 297 ? 27.760  21.847  -4.667  1.00 34.14  ? 282 GLY   A HA3  1 
ATOM   4415 N N    . LEU   A 1 298 ? 27.528  19.101  -4.069  1.00 28.41  ? 283 LEU   A N    1 
ATOM   4416 C CA   . LEU   A 1 298 ? 27.482  17.696  -4.466  1.00 29.31  ? 283 LEU   A CA   1 
ATOM   4417 C C    . LEU   A 1 298 ? 26.055  17.161  -4.430  1.00 31.30  ? 283 LEU   A C    1 
ATOM   4418 O O    . LEU   A 1 298 ? 25.669  16.341  -5.275  1.00 31.21  ? 283 LEU   A O    1 
ATOM   4419 C CB   . LEU   A 1 298 ? 28.385  16.871  -3.556  1.00 28.60  ? 283 LEU   A CB   1 
ATOM   4420 C CG   . LEU   A 1 298 ? 29.859  17.257  -3.599  1.00 25.97  ? 283 LEU   A CG   1 
ATOM   4421 C CD1  . LEU   A 1 298 ? 30.598  16.642  -2.440  1.00 31.80  ? 283 LEU   A CD1  1 
ATOM   4422 C CD2  . LEU   A 1 298 ? 30.489  16.830  -4.911  1.00 39.14  ? 283 LEU   A CD2  1 
ATOM   4423 H H    . LEU   A 1 298 ? 27.998  19.266  -3.368  1.00 34.09  ? 283 LEU   A H    1 
ATOM   4424 H HA   . LEU   A 1 298 ? 27.812  17.614  -5.375  1.00 35.18  ? 283 LEU   A HA   1 
ATOM   4425 H HB2  . LEU   A 1 298 ? 28.081  16.979  -2.641  1.00 34.32  ? 283 LEU   A HB2  1 
ATOM   4426 H HB3  . LEU   A 1 298 ? 28.319  15.940  -3.820  1.00 34.32  ? 283 LEU   A HB3  1 
ATOM   4427 H HG   . LEU   A 1 298 ? 29.931  18.222  -3.531  1.00 31.16  ? 283 LEU   A HG   1 
ATOM   4428 H HD11 . LEU   A 1 298 ? 31.533  16.897  -2.491  1.00 38.16  ? 283 LEU   A HD11 1 
ATOM   4429 H HD12 . LEU   A 1 298 ? 30.212  16.966  -1.612  1.00 38.16  ? 283 LEU   A HD12 1 
ATOM   4430 H HD13 . LEU   A 1 298 ? 30.515  15.677  -2.489  1.00 38.16  ? 283 LEU   A HD13 1 
ATOM   4431 H HD21 . LEU   A 1 298 ? 31.434  17.047  -4.893  1.00 46.96  ? 283 LEU   A HD21 1 
ATOM   4432 H HD22 . LEU   A 1 298 ? 30.372  15.873  -5.021  1.00 46.96  ? 283 LEU   A HD22 1 
ATOM   4433 H HD23 . LEU   A 1 298 ? 30.055  17.302  -5.639  1.00 46.96  ? 283 LEU   A HD23 1 
ATOM   4434 N N    . ILE   A 1 299 ? 25.259  17.621  -3.462  1.00 24.57  ? 284 ILE   A N    1 
ATOM   4435 C CA   . ILE   A 1 299 ? 23.883  17.161  -3.340  1.00 24.86  ? 284 ILE   A CA   1 
ATOM   4436 C C    . ILE   A 1 299 ? 22.964  17.927  -4.286  1.00 26.22  ? 284 ILE   A C    1 
ATOM   4437 O O    . ILE   A 1 299 ? 21.979  17.368  -4.777  1.00 28.76  ? 284 ILE   A O    1 
ATOM   4438 C CB   . ILE   A 1 299 ? 23.410  17.274  -1.879  1.00 29.14  ? 284 ILE   A CB   1 
ATOM   4439 C CG1  . ILE   A 1 299 ? 24.275  16.412  -0.951  1.00 25.21  ? 284 ILE   A CG1  1 
ATOM   4440 C CG2  . ILE   A 1 299 ? 21.953  16.855  -1.743  1.00 23.81  ? 284 ILE   A CG2  1 
ATOM   4441 C CD1  . ILE   A 1 299 ? 24.443  14.972  -1.414  1.00 27.12  ? 284 ILE   A CD1  1 
ATOM   4442 H H    . ILE   A 1 299 ? 25.492  18.197  -2.868  1.00 29.49  ? 284 ILE   A H    1 
ATOM   4443 H HA   . ILE   A 1 299 ? 23.849  16.225  -3.593  1.00 29.83  ? 284 ILE   A HA   1 
ATOM   4444 H HB   . ILE   A 1 299 ? 23.500  18.205  -1.621  1.00 34.97  ? 284 ILE   A HB   1 
ATOM   4445 H HG12 . ILE   A 1 299 ? 25.158  16.808  -0.894  1.00 30.25  ? 284 ILE   A HG12 1 
ATOM   4446 H HG13 . ILE   A 1 299 ? 23.863  16.392  -0.073  1.00 30.25  ? 284 ILE   A HG13 1 
ATOM   4447 H HG21 . ILE   A 1 299 ? 21.747  16.728  -0.803  1.00 28.57  ? 284 ILE   A HG21 1 
ATOM   4448 H HG22 . ILE   A 1 299 ? 21.388  17.550  -2.114  1.00 28.57  ? 284 ILE   A HG22 1 
ATOM   4449 H HG23 . ILE   A 1 299 ? 21.817  16.025  -2.226  1.00 28.57  ? 284 ILE   A HG23 1 
ATOM   4450 H HD11 . ILE   A 1 299 ? 24.807  14.446  -0.685  1.00 32.54  ? 284 ILE   A HD11 1 
ATOM   4451 H HD12 . ILE   A 1 299 ? 23.577  14.621  -1.675  1.00 32.54  ? 284 ILE   A HD12 1 
ATOM   4452 H HD13 . ILE   A 1 299 ? 25.049  14.952  -2.171  1.00 32.54  ? 284 ILE   A HD13 1 
ATOM   4453 N N    . LEU   A 1 300 ? 23.244  19.203  -4.553  1.00 27.39  ? 285 LEU   A N    1 
ATOM   4454 C CA   . LEU   A 1 300 ? 22.512  19.902  -5.604  1.00 27.81  ? 285 LEU   A CA   1 
ATOM   4455 C C    . LEU   A 1 300 ? 22.583  19.136  -6.922  1.00 29.67  ? 285 LEU   A C    1 
ATOM   4456 O O    . LEU   A 1 300 ? 21.589  19.041  -7.647  1.00 30.97  ? 285 LEU   A O    1 
ATOM   4457 C CB   . LEU   A 1 300 ? 23.054  21.323  -5.769  1.00 28.28  ? 285 LEU   A CB   1 
ATOM   4458 C CG   . LEU   A 1 300 ? 22.804  22.269  -4.591  1.00 26.36  ? 285 LEU   A CG   1 
ATOM   4459 C CD1  . LEU   A 1 300 ? 23.337  23.649  -4.931  1.00 31.18  ? 285 LEU   A CD1  1 
ATOM   4460 C CD2  . LEU   A 1 300 ? 21.335  22.337  -4.227  1.00 28.06  ? 285 LEU   A CD2  1 
ATOM   4461 H H    . LEU   A 1 300 ? 23.839  19.675  -4.149  1.00 32.87  ? 285 LEU   A H    1 
ATOM   4462 H HA   . LEU   A 1 300 ? 21.579  19.972  -5.347  1.00 33.38  ? 285 LEU   A HA   1 
ATOM   4463 H HB2  . LEU   A 1 300 ? 24.014  21.269  -5.897  1.00 33.94  ? 285 LEU   A HB2  1 
ATOM   4464 H HB3  . LEU   A 1 300 ? 22.637  21.718  -6.551  1.00 33.94  ? 285 LEU   A HB3  1 
ATOM   4465 H HG   . LEU   A 1 300 ? 23.270  21.931  -3.810  1.00 31.64  ? 285 LEU   A HG   1 
ATOM   4466 H HD11 . LEU   A 1 300 ? 23.175  24.243  -4.182  1.00 37.41  ? 285 LEU   A HD11 1 
ATOM   4467 H HD12 . LEU   A 1 300 ? 24.289  23.586  -5.104  1.00 37.41  ? 285 LEU   A HD12 1 
ATOM   4468 H HD13 . LEU   A 1 300 ? 22.878  23.979  -5.720  1.00 37.41  ? 285 LEU   A HD13 1 
ATOM   4469 H HD21 . LEU   A 1 300 ? 21.192  23.086  -3.627  1.00 33.67  ? 285 LEU   A HD21 1 
ATOM   4470 H HD22 . LEU   A 1 300 ? 20.814  22.457  -5.036  1.00 33.67  ? 285 LEU   A HD22 1 
ATOM   4471 H HD23 . LEU   A 1 300 ? 21.080  21.510  -3.788  1.00 33.67  ? 285 LEU   A HD23 1 
ATOM   4472 N N    . ASP   A 1 301 ? 23.751  18.573  -7.245  1.00 30.63  ? 286 ASP   A N    1 
ATOM   4473 C CA   . ASP   A 1 301 ? 23.858  17.728  -8.438  1.00 31.59  ? 286 ASP   A CA   1 
ATOM   4474 C C    . ASP   A 1 301 ? 22.910  16.536  -8.358  1.00 36.29  ? 286 ASP   A C    1 
ATOM   4475 O O    . ASP   A 1 301 ? 22.246  16.189  -9.342  1.00 33.58  ? 286 ASP   A O    1 
ATOM   4476 C CB   . ASP   A 1 301 ? 25.295  17.239  -8.619  1.00 33.41  ? 286 ASP   A CB   1 
ATOM   4477 C CG   . ASP   A 1 301 ? 26.154  18.210  -9.421  1.00 54.01  ? 286 ASP   A CG   1 
ATOM   4478 O OD1  . ASP   A 1 301 ? 25.603  18.947  -10.269 1.00 66.68  ? 286 ASP   A OD1  1 
ATOM   4479 O OD2  . ASP   A 1 301 ? 27.386  18.234  -9.208  1.00 52.02  ? 286 ASP   A OD2  1 
ATOM   4480 H H    . ASP   A 1 301 ? 24.482  18.661  -6.801  1.00 36.76  ? 286 ASP   A H    1 
ATOM   4481 H HA   . ASP   A 1 301 ? 23.619  18.262  -9.212  1.00 37.91  ? 286 ASP   A HA   1 
ATOM   4482 H HB2  . ASP   A 1 301 ? 25.703  17.128  -7.746  1.00 40.09  ? 286 ASP   A HB2  1 
ATOM   4483 H HB3  . ASP   A 1 301 ? 25.283  16.390  -9.090  1.00 40.09  ? 286 ASP   A HB3  1 
ATOM   4484 N N    . LEU   A 1 302 ? 22.843  15.894  -7.190  1.00 38.00  ? 287 LEU   A N    1 
ATOM   4485 C CA   . LEU   A 1 302 ? 21.948  14.755  -7.009  1.00 30.71  ? 287 LEU   A CA   1 
ATOM   4486 C C    . LEU   A 1 302 ? 20.494  15.173  -7.170  1.00 31.29  ? 287 LEU   A C    1 
ATOM   4487 O O    . LEU   A 1 302 ? 19.694  14.452  -7.780  1.00 32.53  ? 287 LEU   A O    1 
ATOM   4488 C CB   . LEU   A 1 302 ? 22.189  14.147  -5.628  1.00 33.55  ? 287 LEU   A CB   1 
ATOM   4489 C CG   . LEU   A 1 302 ? 21.490  12.837  -5.258  1.00 28.89  ? 287 LEU   A CG   1 
ATOM   4490 C CD1  . LEU   A 1 302 ? 21.930  11.690  -6.154  1.00 30.22  ? 287 LEU   A CD1  1 
ATOM   4491 C CD2  . LEU   A 1 302 ? 21.786  12.521  -3.812  1.00 26.97  ? 287 LEU   A CD2  1 
ATOM   4492 H H    . LEU   A 1 302 ? 23.301  16.098  -6.492  1.00 45.60  ? 287 LEU   A H    1 
ATOM   4493 H HA   . LEU   A 1 302 ? 22.136  14.080  -7.680  1.00 36.85  ? 287 LEU   A HA   1 
ATOM   4494 H HB2  . LEU   A 1 302 ? 23.142  13.981  -5.547  1.00 40.26  ? 287 LEU   A HB2  1 
ATOM   4495 H HB3  . LEU   A 1 302 ? 21.909  14.802  -4.970  1.00 40.26  ? 287 LEU   A HB3  1 
ATOM   4496 H HG   . LEU   A 1 302 ? 20.534  12.937  -5.384  1.00 34.67  ? 287 LEU   A HG   1 
ATOM   4497 H HD11 . LEU   A 1 302 ? 21.568  10.860  -5.805  1.00 36.26  ? 287 LEU   A HD11 1 
ATOM   4498 H HD12 . LEU   A 1 302 ? 21.595  11.844  -7.052  1.00 36.26  ? 287 LEU   A HD12 1 
ATOM   4499 H HD13 . LEU   A 1 302 ? 22.899  11.650  -6.164  1.00 36.26  ? 287 LEU   A HD13 1 
ATOM   4500 H HD21 . LEU   A 1 302 ? 21.352  11.686  -3.576  1.00 32.37  ? 287 LEU   A HD21 1 
ATOM   4501 H HD22 . LEU   A 1 302 ? 22.745  12.439  -3.697  1.00 32.37  ? 287 LEU   A HD22 1 
ATOM   4502 H HD23 . LEU   A 1 302 ? 21.446  13.239  -3.256  1.00 32.37  ? 287 LEU   A HD23 1 
ATOM   4503 N N    . LEU   A 1 303 ? 20.137  16.348  -6.635  1.00 30.46  ? 288 LEU   A N    1 
ATOM   4504 C CA   . LEU   A 1 303 ? 18.755  16.812  -6.693  1.00 30.90  ? 288 LEU   A CA   1 
ATOM   4505 C C    . LEU   A 1 303 ? 18.350  17.201  -8.111  1.00 32.92  ? 288 LEU   A C    1 
ATOM   4506 O O    . LEU   A 1 303 ? 17.188  17.026  -8.489  1.00 33.87  ? 288 LEU   A O    1 
ATOM   4507 C CB   . LEU   A 1 303 ? 18.556  17.988  -5.730  1.00 29.98  ? 288 LEU   A CB   1 
ATOM   4508 C CG   . LEU   A 1 303 ? 18.785  17.685  -4.243  1.00 29.61  ? 288 LEU   A CG   1 
ATOM   4509 C CD1  . LEU   A 1 303 ? 18.312  18.853  -3.388  1.00 26.34  ? 288 LEU   A CD1  1 
ATOM   4510 C CD2  . LEU   A 1 303 ? 18.084  16.414  -3.820  1.00 28.54  ? 288 LEU   A CD2  1 
ATOM   4511 H H    . LEU   A 1 303 ? 20.675  16.888  -6.237  1.00 36.55  ? 288 LEU   A H    1 
ATOM   4512 H HA   . LEU   A 1 303 ? 18.170  16.092  -6.407  1.00 37.08  ? 288 LEU   A HA   1 
ATOM   4513 H HB2  . LEU   A 1 303 ? 19.175  18.691  -5.979  1.00 35.97  ? 288 LEU   A HB2  1 
ATOM   4514 H HB3  . LEU   A 1 303 ? 17.643  18.302  -5.822  1.00 35.97  ? 288 LEU   A HB3  1 
ATOM   4515 H HG   . LEU   A 1 303 ? 19.736  17.556  -4.102  1.00 35.53  ? 288 LEU   A HG   1 
ATOM   4516 H HD11 . LEU   A 1 303 ? 18.478  18.648  -2.454  1.00 31.61  ? 288 LEU   A HD11 1 
ATOM   4517 H HD12 . LEU   A 1 303 ? 18.802  19.650  -3.643  1.00 31.61  ? 288 LEU   A HD12 1 
ATOM   4518 H HD13 . LEU   A 1 303 ? 17.363  18.987  -3.533  1.00 31.61  ? 288 LEU   A HD13 1 
ATOM   4519 H HD21 . LEU   A 1 303 ? 18.083  16.362  -2.851  1.00 34.25  ? 288 LEU   A HD21 1 
ATOM   4520 H HD22 . LEU   A 1 303 ? 17.173  16.431  -4.151  1.00 34.25  ? 288 LEU   A HD22 1 
ATOM   4521 H HD23 . LEU   A 1 303 ? 18.557  15.654  -4.192  1.00 34.25  ? 288 LEU   A HD23 1 
ATOM   4522 N N    . ASP   A 1 304 ? 19.280  17.723  -8.907  1.00 33.64  ? 289 ASP   A N    1 
ATOM   4523 C CA   . ASP   A 1 304 ? 18.989  17.920  -10.322 1.00 36.36  ? 289 ASP   A CA   1 
ATOM   4524 C C    . ASP   A 1 304 ? 18.696  16.588  -11.007 1.00 37.95  ? 289 ASP   A C    1 
ATOM   4525 O O    . ASP   A 1 304 ? 17.714  16.454  -11.747 1.00 38.44  ? 289 ASP   A O    1 
ATOM   4526 C CB   . ASP   A 1 304 ? 20.158  18.625  -11.000 1.00 36.19  ? 289 ASP   A CB   1 
ATOM   4527 C CG   . ASP   A 1 304 ? 20.037  18.615  -12.504 1.00 47.70  ? 289 ASP   A CG   1 
ATOM   4528 O OD1  . ASP   A 1 304 ? 19.025  19.143  -13.010 1.00 48.42  ? 289 ASP   A OD1  1 
ATOM   4529 O OD2  . ASP   A 1 304 ? 20.942  18.073  -13.177 1.00 51.96  ? 289 ASP   A OD2  1 
ATOM   4530 H H    . ASP   A 1 304 ? 20.067  17.964  -8.659  1.00 40.36  ? 289 ASP   A H    1 
ATOM   4531 H HA   . ASP   A 1 304 ? 18.206  18.485  -10.407 1.00 43.63  ? 289 ASP   A HA   1 
ATOM   4532 H HB2  . ASP   A 1 304 ? 20.187  19.548  -10.705 1.00 43.43  ? 289 ASP   A HB2  1 
ATOM   4533 H HB3  . ASP   A 1 304 ? 20.983  18.174  -10.760 1.00 43.43  ? 289 ASP   A HB3  1 
ATOM   4534 N N    . LYS   A 1 305 ? 19.543  15.585  -10.767 1.00 36.57  ? 290 LYS   A N    1 
ATOM   4535 C CA   . LYS   A 1 305 ? 19.283  14.250  -11.302 1.00 37.69  ? 290 LYS   A CA   1 
ATOM   4536 C C    . LYS   A 1 305 ? 17.915  13.746  -10.857 1.00 40.17  ? 290 LYS   A C    1 
ATOM   4537 O O    . LYS   A 1 305 ? 17.156  13.192  -11.661 1.00 39.17  ? 290 LYS   A O    1 
ATOM   4538 C CB   . LYS   A 1 305 ? 20.392  13.298  -10.858 1.00 36.89  ? 290 LYS   A CB   1 
ATOM   4539 C CG   . LYS   A 1 305 ? 20.374  11.934  -11.542 1.00 43.20  ? 290 LYS   A CG   1 
ATOM   4540 C CD   . LYS   A 1 305 ? 21.506  11.056  -11.030 1.00 38.93  ? 290 LYS   A CD   1 
ATOM   4541 C CE   . LYS   A 1 305 ? 21.402  9.629   -11.546 1.00 45.04  ? 290 LYS   A CE   1 
ATOM   4542 N NZ   . LYS   A 1 305 ? 22.319  8.724   -10.793 1.00 43.51  ? 290 LYS   A NZ   1 
ATOM   4543 H H    . LYS   A 1 305 ? 20.265  15.651  -10.304 1.00 43.88  ? 290 LYS   A H    1 
ATOM   4544 H HA   . LYS   A 1 305 ? 19.287  14.281  -12.272 1.00 45.23  ? 290 LYS   A HA   1 
ATOM   4545 H HB2  . LYS   A 1 305 ? 21.248  13.710  -11.052 1.00 44.27  ? 290 LYS   A HB2  1 
ATOM   4546 H HB3  . LYS   A 1 305 ? 20.305  13.147  -9.904  1.00 44.27  ? 290 LYS   A HB3  1 
ATOM   4547 H HG2  . LYS   A 1 305 ? 19.532  11.490  -11.355 1.00 51.84  ? 290 LYS   A HG2  1 
ATOM   4548 H HG3  . LYS   A 1 305 ? 20.483  12.050  -12.498 1.00 51.84  ? 290 LYS   A HG3  1 
ATOM   4549 H HD2  . LYS   A 1 305 ? 22.353  11.423  -11.326 1.00 46.72  ? 290 LYS   A HD2  1 
ATOM   4550 H HD3  . LYS   A 1 305 ? 21.476  11.029  -10.061 1.00 46.72  ? 290 LYS   A HD3  1 
ATOM   4551 H HE2  . LYS   A 1 305 ? 20.493  9.309   -11.433 1.00 54.05  ? 290 LYS   A HE2  1 
ATOM   4552 H HE3  . LYS   A 1 305 ? 21.649  9.605   -12.484 1.00 54.05  ? 290 LYS   A HE3  1 
ATOM   4553 H HZ1  . LYS   A 1 305 ? 23.160  8.999   -10.883 1.00 52.21  ? 290 LYS   A HZ1  1 
ATOM   4554 H HZ2  . LYS   A 1 305 ? 22.105  8.725   -9.929  1.00 52.21  ? 290 LYS   A HZ2  1 
ATOM   4555 H HZ3  . LYS   A 1 305 ? 22.252  7.894   -11.106 1.00 52.21  ? 290 LYS   A HZ3  1 
ATOM   4556 N N    . LEU   A 1 306 ? 17.569  13.967  -9.588  1.00 38.13  ? 291 LEU   A N    1 
ATOM   4557 C CA   . LEU   A 1 306 ? 16.293  13.490  -9.066  1.00 35.68  ? 291 LEU   A CA   1 
ATOM   4558 C C    . LEU   A 1 306 ? 15.118  14.125  -9.799  1.00 42.00  ? 291 LEU   A C    1 
ATOM   4559 O O    . LEU   A 1 306 ? 14.117  13.456  -10.082 1.00 43.02  ? 291 LEU   A O    1 
ATOM   4560 C CB   . LEU   A 1 306 ? 16.210  13.793  -7.572  1.00 35.43  ? 291 LEU   A CB   1 
ATOM   4561 C CG   . LEU   A 1 306 ? 14.890  13.495  -6.863  1.00 41.30  ? 291 LEU   A CG   1 
ATOM   4562 C CD1  . LEU   A 1 306 ? 14.697  11.990  -6.726  1.00 33.34  ? 291 LEU   A CD1  1 
ATOM   4563 C CD2  . LEU   A 1 306 ? 14.852  14.186  -5.507  1.00 34.63  ? 291 LEU   A CD2  1 
ATOM   4564 H H    . LEU   A 1 306 ? 18.052  14.387  -9.013  1.00 45.75  ? 291 LEU   A H    1 
ATOM   4565 H HA   . LEU   A 1 306 ? 16.239  12.530  -9.195  1.00 42.81  ? 291 LEU   A HA   1 
ATOM   4566 H HB2  . LEU   A 1 306 ? 16.893  13.268  -7.125  1.00 42.52  ? 291 LEU   A HB2  1 
ATOM   4567 H HB3  . LEU   A 1 306 ? 16.387  14.739  -7.451  1.00 42.52  ? 291 LEU   A HB3  1 
ATOM   4568 H HG   . LEU   A 1 306 ? 14.151  13.841  -7.388  1.00 49.56  ? 291 LEU   A HG   1 
ATOM   4569 H HD11 . LEU   A 1 306 ? 13.848  11.819  -6.289  1.00 40.01  ? 291 LEU   A HD11 1 
ATOM   4570 H HD12 . LEU   A 1 306 ? 14.701  11.589  -7.609  1.00 40.01  ? 291 LEU   A HD12 1 
ATOM   4571 H HD13 . LEU   A 1 306 ? 15.422  11.626  -6.194  1.00 40.01  ? 291 LEU   A HD13 1 
ATOM   4572 H HD21 . LEU   A 1 306 ? 14.010  13.979  -5.071  1.00 41.56  ? 291 LEU   A HD21 1 
ATOM   4573 H HD22 . LEU   A 1 306 ? 15.591  13.865  -4.968  1.00 41.56  ? 291 LEU   A HD22 1 
ATOM   4574 H HD23 . LEU   A 1 306 ? 14.929  15.144  -5.638  1.00 41.56  ? 291 LEU   A HD23 1 
ATOM   4575 N N    . LYS   A 1 307 ? 15.218  15.415  -10.113 1.00 41.71  ? 292 LYS   A N    1 
ATOM   4576 C CA   . LYS   A 1 307 ? 14.080  16.151  -10.649 1.00 45.68  ? 292 LYS   A CA   1 
ATOM   4577 C C    . LYS   A 1 307 ? 13.998  16.115  -12.168 1.00 44.21  ? 292 LYS   A C    1 
ATOM   4578 O O    . LYS   A 1 307 ? 12.893  16.204  -12.718 1.00 52.86  ? 292 LYS   A O    1 
ATOM   4579 C CB   . LYS   A 1 307 ? 14.126  17.613  -10.180 1.00 49.30  ? 292 LYS   A CB   1 
ATOM   4580 C CG   . LYS   A 1 307 ? 13.759  17.809  -8.701  1.00 60.88  ? 292 LYS   A CG   1 
ATOM   4581 C CD   . LYS   A 1 307 ? 12.376  17.222  -8.375  1.00 64.78  ? 292 LYS   A CD   1 
ATOM   4582 C CE   . LYS   A 1 307 ? 11.831  17.702  -7.028  1.00 69.59  ? 292 LYS   A CE   1 
ATOM   4583 N NZ   . LYS   A 1 307 ? 12.074  16.723  -5.927  1.00 67.56  ? 292 LYS   A NZ   1 
ATOM   4584 H H    . LYS   A 1 307 ? 15.933  15.884  -10.025 1.00 50.05  ? 292 LYS   A H    1 
ATOM   4585 H HA   . LYS   A 1 307 ? 13.269  15.747  -10.304 1.00 54.81  ? 292 LYS   A HA   1 
ATOM   4586 H HB2  . LYS   A 1 307 ? 15.026  17.952  -10.308 1.00 59.16  ? 292 LYS   A HB2  1 
ATOM   4587 H HB3  . LYS   A 1 307 ? 13.499  18.130  -10.710 1.00 59.16  ? 292 LYS   A HB3  1 
ATOM   4588 H HG2  . LYS   A 1 307 ? 14.417  17.363  -8.146  1.00 73.05  ? 292 LYS   A HG2  1 
ATOM   4589 H HG3  . LYS   A 1 307 ? 13.742  18.757  -8.498  1.00 73.05  ? 292 LYS   A HG3  1 
ATOM   4590 H HD2  . LYS   A 1 307 ? 11.749  17.490  -9.064  1.00 77.73  ? 292 LYS   A HD2  1 
ATOM   4591 H HD3  . LYS   A 1 307 ? 12.443  16.255  -8.343  1.00 77.73  ? 292 LYS   A HD3  1 
ATOM   4592 H HE2  . LYS   A 1 307 ? 12.266  18.536  -6.790  1.00 83.51  ? 292 LYS   A HE2  1 
ATOM   4593 H HE3  . LYS   A 1 307 ? 10.874  17.837  -7.104  1.00 83.51  ? 292 LYS   A HE3  1 
ATOM   4594 H HZ1  . LYS   A 1 307 ? 11.737  17.033  -5.164  1.00 81.07  ? 292 LYS   A HZ1  1 
ATOM   4595 H HZ2  . LYS   A 1 307 ? 11.686  15.946  -6.119  1.00 81.07  ? 292 LYS   A HZ2  1 
ATOM   4596 H HZ3  . LYS   A 1 307 ? 12.949  16.591  -5.824  1.00 81.07  ? 292 LYS   A HZ3  1 
ATOM   4597 N N    . ASN   A 1 308 ? 15.122  15.967  -12.864 1.00 49.23  ? 293 ASN   A N    1 
ATOM   4598 C CA   . ASN   A 1 308 ? 15.147  16.142  -14.307 1.00 48.88  ? 293 ASN   A CA   1 
ATOM   4599 C C    . ASN   A 1 308 ? 15.689  14.952  -15.080 1.00 47.27  ? 293 ASN   A C    1 
ATOM   4600 O O    . ASN   A 1 308 ? 15.686  14.990  -16.316 1.00 60.70  ? 293 ASN   A O    1 
ATOM   4601 C CB   . ASN   A 1 308 ? 15.972  17.391  -14.662 1.00 47.70  ? 293 ASN   A CB   1 
ATOM   4602 C CG   . ASN   A 1 308 ? 15.342  18.679  -14.146 1.00 58.35  ? 293 ASN   A CG   1 
ATOM   4603 O OD1  . ASN   A 1 308 ? 15.530  19.064  -12.990 1.00 50.13  ? 293 ASN   A OD1  1 
ATOM   4604 N ND2  . ASN   A 1 308 ? 14.594  19.354  -15.010 1.00 69.80  ? 293 ASN   A ND2  1 
ATOM   4605 H H    . ASN   A 1 308 ? 15.884  15.764  -12.519 1.00 59.07  ? 293 ASN   A H    1 
ATOM   4606 H HA   . ASN   A 1 308 ? 14.232  16.273  -14.604 1.00 58.65  ? 293 ASN   A HA   1 
ATOM   4607 H HB2  . ASN   A 1 308 ? 16.855  17.309  -14.268 1.00 57.24  ? 293 ASN   A HB2  1 
ATOM   4608 H HB3  . ASN   A 1 308 ? 16.044  17.458  -15.627 1.00 57.24  ? 293 ASN   A HB3  1 
ATOM   4609 H HD21 . ASN   A 1 308 ? 14.215  20.088  -14.769 1.00 83.77  ? 293 ASN   A HD21 1 
ATOM   4610 H HD22 . ASN   A 1 308 ? 14.487  19.058  -15.810 1.00 83.77  ? 293 ASN   A HD22 1 
ATOM   4611 N N    . GLY   A 1 309 ? 16.143  13.899  -14.412 1.00 47.08  ? 294 GLY   A N    1 
ATOM   4612 C CA   . GLY   A 1 309 ? 16.731  12.767  -15.095 1.00 47.95  ? 294 GLY   A CA   1 
ATOM   4613 C C    . GLY   A 1 309 ? 18.239  12.884  -15.231 1.00 54.09  ? 294 GLY   A C    1 
ATOM   4614 O O    . GLY   A 1 309 ? 18.839  13.947  -15.057 1.00 63.16  ? 294 GLY   A O    1 
ATOM   4615 H H    . GLY   A 1 309 ? 16.120  13.820  -13.556 1.00 56.49  ? 294 GLY   A H    1 
ATOM   4616 H HA2  . GLY   A 1 309 ? 16.531  11.956  -14.602 1.00 57.54  ? 294 GLY   A HA2  1 
ATOM   4617 H HA3  . GLY   A 1 309 ? 16.349  12.697  -15.985 1.00 57.54  ? 294 GLY   A HA3  1 
ATOM   4618 N N    . ASN   A 1 310 ? 18.861  11.751  -15.562 1.00 79.50  ? 295 ASN   A N    1 
ATOM   4619 C CA   . ASN   A 1 310 ? 20.319  11.672  -15.545 1.00 86.62  ? 295 ASN   A CA   1 
ATOM   4620 C C    . ASN   A 1 310 ? 20.936  12.657  -16.530 1.00 86.75  ? 295 ASN   A C    1 
ATOM   4621 O O    . ASN   A 1 310 ? 21.721  13.532  -16.147 1.00 89.62  ? 295 ASN   A O    1 
ATOM   4622 C CB   . ASN   A 1 310 ? 20.770  10.244  -15.858 1.00 90.86  ? 295 ASN   A CB   1 
ATOM   4623 C CG   . ASN   A 1 310 ? 22.148  9.933   -15.300 1.00 92.91  ? 295 ASN   A CG   1 
ATOM   4624 O OD1  . ASN   A 1 310 ? 22.877  10.834  -14.880 1.00 89.15  ? 295 ASN   A OD1  1 
ATOM   4625 N ND2  . ASN   A 1 310 ? 22.512  8.652   -15.294 1.00 91.74  ? 295 ASN   A ND2  1 
ATOM   4626 H H    . ASN   A 1 310 ? 18.467  11.024  -15.798 1.00 95.40  ? 295 ASN   A H    1 
ATOM   4627 H HA   . ASN   A 1 310 ? 20.629  11.900  -14.655 1.00 103.95 ? 295 ASN   A HA   1 
ATOM   4628 H HB2  . ASN   A 1 310 ? 20.139  9.619   -15.467 1.00 109.03 ? 295 ASN   A HB2  1 
ATOM   4629 H HB3  . ASN   A 1 310 ? 20.802  10.125  -16.820 1.00 109.03 ? 295 ASN   A HB3  1 
ATOM   4630 H HD21 . ASN   A 1 310 ? 23.283  8.425   -14.988 1.00 110.09 ? 295 ASN   A HD21 1 
ATOM   4631 H HD22 . ASN   A 1 310 ? 21.976  8.051   -15.596 1.00 110.09 ? 295 ASN   A HD22 1 
ATOM   4632 N N    . SER   A 1 311 ? 20.588  12.530  -17.807 1.00 77.96  ? 296 SER   A N    1 
ATOM   4633 C CA   . SER   A 1 311 ? 21.156  13.377  -18.851 1.00 86.70  ? 296 SER   A CA   1 
ATOM   4634 C C    . SER   A 1 311 ? 20.997  14.857  -18.510 1.00 81.14  ? 296 SER   A C    1 
ATOM   4635 O O    . SER   A 1 311 ? 19.892  15.326  -18.235 1.00 74.94  ? 296 SER   A O    1 
ATOM   4636 C CB   . SER   A 1 311 ? 20.497  13.072  -20.199 1.00 78.98  ? 296 SER   A CB   1 
ATOM   4637 O OG   . SER   A 1 311 ? 20.457  11.674  -20.440 1.00 77.38  ? 296 SER   A OG   1 
ATOM   4638 H H    . SER   A 1 311 ? 20.018  11.955  -18.098 1.00 93.55  ? 296 SER   A H    1 
ATOM   4639 H HA   . SER   A 1 311 ? 22.105  13.191  -18.927 1.00 104.04 ? 296 SER   A HA   1 
ATOM   4640 H HB2  . SER   A 1 311 ? 19.591  13.416  -20.192 1.00 94.78  ? 296 SER   A HB2  1 
ATOM   4641 H HB3  . SER   A 1 311 ? 21.009  13.498  -20.904 1.00 94.78  ? 296 SER   A HB3  1 
ATOM   4642 H HG   . SER   A 1 311 ? 20.084  11.520  -21.176 1.00 92.85  ? 296 SER   A HG   1 
ATOM   4643 N N    . ILE   B 1 23  ? 6.813   -32.470 13.320  1.00 76.23  ? 8   ILE   B N    1 
ATOM   4644 C CA   . ILE   B 1 23  ? 5.735   -31.661 12.766  1.00 78.74  ? 8   ILE   B CA   1 
ATOM   4645 C C    . ILE   B 1 23  ? 4.940   -32.486 11.757  1.00 76.38  ? 8   ILE   B C    1 
ATOM   4646 O O    . ILE   B 1 23  ? 5.473   -33.407 11.143  1.00 86.97  ? 8   ILE   B O    1 
ATOM   4647 C CB   . ILE   B 1 23  ? 6.276   -30.374 12.110  1.00 80.24  ? 8   ILE   B CB   1 
ATOM   4648 C CG1  . ILE   B 1 23  ? 7.309   -29.703 13.022  1.00 81.08  ? 8   ILE   B CG1  1 
ATOM   4649 C CG2  . ILE   B 1 23  ? 5.132   -29.406 11.798  1.00 69.72  ? 8   ILE   B CG2  1 
ATOM   4650 C CD1  . ILE   B 1 23  ? 7.792   -28.346 12.519  1.00 79.29  ? 8   ILE   B CD1  1 
ATOM   4651 H HA   . ILE   B 1 23  ? 5.143   -31.394 13.486  1.00 94.49  ? 8   ILE   B HA   1 
ATOM   4652 H HB   . ILE   B 1 23  ? 6.711   -30.618 11.278  1.00 96.29  ? 8   ILE   B HB   1 
ATOM   4653 H HG12 . ILE   B 1 23  ? 6.910   -29.569 13.896  1.00 97.30  ? 8   ILE   B HG12 1 
ATOM   4654 H HG13 . ILE   B 1 23  ? 8.082   -30.283 13.096  1.00 97.30  ? 8   ILE   B HG13 1 
ATOM   4655 H HG21 . ILE   B 1 23  ? 5.486   -28.643 11.315  1.00 83.66  ? 8   ILE   B HG21 1 
ATOM   4656 H HG22 . ILE   B 1 23  ? 4.471   -29.864 11.254  1.00 83.66  ? 8   ILE   B HG22 1 
ATOM   4657 H HG23 . ILE   B 1 23  ? 4.729   -29.114 12.630  1.00 83.66  ? 8   ILE   B HG23 1 
ATOM   4658 H HD11 . ILE   B 1 23  ? 8.592   -28.095 13.008  1.00 95.14  ? 8   ILE   B HD11 1 
ATOM   4659 H HD12 . ILE   B 1 23  ? 7.990   -28.412 11.572  1.00 95.14  ? 8   ILE   B HD12 1 
ATOM   4660 H HD13 . ILE   B 1 23  ? 7.095   -27.688 12.666  1.00 95.14  ? 8   ILE   B HD13 1 
ATOM   4661 N N    . PHE   B 1 24  ? 3.660   -32.156 11.603  1.00 87.30  ? 9   PHE   B N    1 
ATOM   4662 C CA   . PHE   B 1 24  ? 2.789   -32.772 10.614  1.00 84.95  ? 9   PHE   B CA   1 
ATOM   4663 C C    . PHE   B 1 24  ? 2.461   -31.756 9.527   1.00 84.55  ? 9   PHE   B C    1 
ATOM   4664 O O    . PHE   B 1 24  ? 2.161   -30.594 9.821   1.00 83.82  ? 9   PHE   B O    1 
ATOM   4665 C CB   . PHE   B 1 24  ? 1.489   -33.279 11.247  1.00 87.83  ? 9   PHE   B CB   1 
ATOM   4666 C CG   . PHE   B 1 24  ? 1.650   -34.525 12.084  1.00 95.59  ? 9   PHE   B CG   1 
ATOM   4667 C CD1  . PHE   B 1 24  ? 2.901   -35.077 12.323  1.00 96.29  ? 9   PHE   B CD1  1 
ATOM   4668 C CD2  . PHE   B 1 24  ? 0.535   -35.151 12.624  1.00 90.90  ? 9   PHE   B CD2  1 
ATOM   4669 C CE1  . PHE   B 1 24  ? 3.033   -36.222 13.090  1.00 96.56  ? 9   PHE   B CE1  1 
ATOM   4670 C CE2  . PHE   B 1 24  ? 0.662   -36.295 13.388  1.00 89.97  ? 9   PHE   B CE2  1 
ATOM   4671 C CZ   . PHE   B 1 24  ? 1.911   -36.830 13.622  1.00 97.33  ? 9   PHE   B CZ   1 
ATOM   4672 H H    . PHE   B 1 24  ? 3.264   -31.559 12.078  1.00 104.76 ? 9   PHE   B H    1 
ATOM   4673 H HA   . PHE   B 1 24  ? 3.244   -33.529 10.214  1.00 101.94 ? 9   PHE   B HA   1 
ATOM   4674 H HB2  . PHE   B 1 24  ? 1.131   -32.584 11.821  1.00 105.40 ? 9   PHE   B HB2  1 
ATOM   4675 H HB3  . PHE   B 1 24  ? 0.857   -33.481 10.538  1.00 105.40 ? 9   PHE   B HB3  1 
ATOM   4676 H HD1  . PHE   B 1 24  ? 3.658   -34.673 11.965  1.00 115.55 ? 9   PHE   B HD1  1 
ATOM   4677 H HD2  . PHE   B 1 24  ? -0.310  -34.795 12.468  1.00 109.08 ? 9   PHE   B HD2  1 
ATOM   4678 H HE1  . PHE   B 1 24  ? 3.876   -36.582 13.247  1.00 115.87 ? 9   PHE   B HE1  1 
ATOM   4679 H HE2  . PHE   B 1 24  ? -0.094  -36.703 13.745  1.00 107.97 ? 9   PHE   B HE2  1 
ATOM   4680 H HZ   . PHE   B 1 24  ? 1.998   -37.600 14.138  1.00 116.79 ? 9   PHE   B HZ   1 
ATOM   4681 N N    . ASN   B 1 25  ? 2.515   -32.196 8.273   1.00 78.64  ? 10  ASN   B N    1 
ATOM   4682 C CA   . ASN   B 1 25  ? 2.186   -31.352 7.127   1.00 79.59  ? 10  ASN   B CA   1 
ATOM   4683 C C    . ASN   B 1 25  ? 0.785   -31.637 6.602   1.00 83.13  ? 10  ASN   B C    1 
ATOM   4684 O O    . ASN   B 1 25  ? 0.544   -31.621 5.390   1.00 83.76  ? 10  ASN   B O    1 
ATOM   4685 C CB   . ASN   B 1 25  ? 3.228   -31.533 6.029   1.00 81.17  ? 10  ASN   B CB   1 
ATOM   4686 C CG   . ASN   B 1 25  ? 4.501   -30.756 6.309   1.00 87.85  ? 10  ASN   B CG   1 
ATOM   4687 O OD1  . ASN   B 1 25  ? 5.244   -31.073 7.238   1.00 87.35  ? 10  ASN   B OD1  1 
ATOM   4688 N ND2  . ASN   B 1 25  ? 4.755   -29.728 5.506   1.00 83.13  ? 10  ASN   B ND2  1 
ATOM   4689 H H    . ASN   B 1 25  ? 2.745   -32.996 8.057   1.00 94.37  ? 10  ASN   B H    1 
ATOM   4690 H HA   . ASN   B 1 25  ? 2.208   -30.423 7.404   1.00 95.50  ? 10  ASN   B HA   1 
ATOM   4691 H HB2  . ASN   B 1 25  ? 3.457   -32.473 5.960   1.00 97.41  ? 10  ASN   B HB2  1 
ATOM   4692 H HB3  . ASN   B 1 25  ? 2.861   -31.218 5.188   1.00 97.41  ? 10  ASN   B HB3  1 
ATOM   4693 H HD21 . ASN   B 1 25  ? 5.465   -29.257 5.623   1.00 99.75  ? 10  ASN   B HD21 1 
ATOM   4694 H HD22 . ASN   B 1 25  ? 4.211   -29.535 4.869   1.00 99.75  ? 10  ASN   B HD22 1 
ATOM   4695 N N    . ARG   B 1 26  ? -0.156  -31.894 7.504   1.00 82.77  ? 11  ARG   B N    1 
ATOM   4696 C CA   . ARG   B 1 26  ? -1.545  -32.150 7.165   1.00 87.23  ? 11  ARG   B CA   1 
ATOM   4697 C C    . ARG   B 1 26  ? -2.422  -31.000 7.642   1.00 83.34  ? 11  ARG   B C    1 
ATOM   4698 O O    . ARG   B 1 26  ? -1.966  -30.073 8.315   1.00 82.91  ? 11  ARG   B O    1 
ATOM   4699 C CB   . ARG   B 1 26  ? -2.035  -33.455 7.803   1.00 85.45  ? 11  ARG   B CB   1 
ATOM   4700 C CG   . ARG   B 1 26  ? -1.156  -34.663 7.551   1.00 92.65  ? 11  ARG   B CG   1 
ATOM   4701 C CD   . ARG   B 1 26  ? -1.637  -35.839 8.382   1.00 95.42  ? 11  ARG   B CD   1 
ATOM   4702 N NE   . ARG   B 1 26  ? -3.071  -36.057 8.222   1.00 96.74  ? 11  ARG   B NE   1 
ATOM   4703 C CZ   . ARG   B 1 26  ? -3.617  -36.946 7.402   1.00 94.99  ? 11  ARG   B CZ   1 
ATOM   4704 N NH1  . ARG   B 1 26  ? -2.876  -37.750 6.658   1.00 97.14  ? 11  ARG   B NH1  1 
ATOM   4705 N NH2  . ARG   B 1 26  ? -4.942  -37.033 7.332   1.00 97.88  ? 11  ARG   B NH2  1 
ATOM   4706 H H    . ARG   B 1 26  ? -0.005  -31.926 8.350   1.00 99.32  ? 11  ARG   B H    1 
ATOM   4707 H HA   . ARG   B 1 26  ? -1.619  -32.227 6.201   1.00 104.68 ? 11  ARG   B HA   1 
ATOM   4708 H HB2  . ARG   B 1 26  ? -2.085  -33.327 8.763   1.00 102.54 ? 11  ARG   B HB2  1 
ATOM   4709 H HB3  . ARG   B 1 26  ? -2.915  -33.658 7.449   1.00 102.54 ? 11  ARG   B HB3  1 
ATOM   4710 H HG2  . ARG   B 1 26  ? -1.197  -34.907 6.613   1.00 111.18 ? 11  ARG   B HG2  1 
ATOM   4711 H HG3  . ARG   B 1 26  ? -0.241  -34.459 7.801   1.00 111.18 ? 11  ARG   B HG3  1 
ATOM   4712 H HD2  . ARG   B 1 26  ? -1.173  -36.642 8.099   1.00 114.51 ? 11  ARG   B HD2  1 
ATOM   4713 H HD3  . ARG   B 1 26  ? -1.458  -35.664 9.319   1.00 114.51 ? 11  ARG   B HD3  1 
ATOM   4714 H HE   . ARG   B 1 26  ? -3.601  -35.573 8.695   1.00 116.09 ? 11  ARG   B HE   1 
ATOM   4715 H HH11 . ARG   B 1 26  ? -2.019  -37.705 6.698   1.00 116.57 ? 11  ARG   B HH11 1 
ATOM   4716 H HH12 . ARG   B 1 26  ? -3.253  -38.319 6.133   1.00 116.57 ? 11  ARG   B HH12 1 
ATOM   4717 H HH21 . ARG   B 1 26  ? -5.433  -36.518 7.814   1.00 117.46 ? 11  ARG   B HH21 1 
ATOM   4718 H HH22 . ARG   B 1 26  ? -5.308  -37.605 6.804   1.00 117.46 ? 11  ARG   B HH22 1 
ATOM   4719 N N    . ASP   B 1 27  ? -3.698  -31.075 7.290   1.00 80.23  ? 12  ASP   B N    1 
ATOM   4720 C CA   . ASP   B 1 27  ? -4.692  -30.223 7.926   1.00 73.52  ? 12  ASP   B CA   1 
ATOM   4721 C C    . ASP   B 1 27  ? -5.019  -30.820 9.288   1.00 68.78  ? 12  ASP   B C    1 
ATOM   4722 O O    . ASP   B 1 27  ? -5.406  -31.991 9.360   1.00 64.70  ? 12  ASP   B O    1 
ATOM   4723 C CB   . ASP   B 1 27  ? -5.952  -30.113 7.074   1.00 74.49  ? 12  ASP   B CB   1 
ATOM   4724 C CG   . ASP   B 1 27  ? -6.868  -28.983 7.528   1.00 68.20  ? 12  ASP   B CG   1 
ATOM   4725 O OD1  . ASP   B 1 27  ? -7.066  -28.824 8.749   1.00 64.98  ? 12  ASP   B OD1  1 
ATOM   4726 O OD2  . ASP   B 1 27  ? -7.386  -28.246 6.662   1.00 73.51  ? 12  ASP   B OD2  1 
ATOM   4727 H H    . ASP   B 1 27  ? -4.012  -31.607 6.691   1.00 96.28  ? 12  ASP   B H    1 
ATOM   4728 H HA   . ASP   B 1 27  ? -4.348  -29.323 8.036   1.00 88.22  ? 12  ASP   B HA   1 
ATOM   4729 H HB2  . ASP   B 1 27  ? -5.698  -29.942 6.154   1.00 89.39  ? 12  ASP   B HB2  1 
ATOM   4730 H HB3  . ASP   B 1 27  ? -6.448  -30.944 7.133   1.00 89.39  ? 12  ASP   B HB3  1 
ATOM   4731 N N    . PRO   B 1 28  ? -4.855  -30.078 10.384  1.00 74.45  ? 13  PRO   B N    1 
ATOM   4732 C CA   . PRO   B 1 28  ? -5.142  -30.668 11.700  1.00 63.14  ? 13  PRO   B CA   1 
ATOM   4733 C C    . PRO   B 1 28  ? -6.571  -31.149 11.843  1.00 67.38  ? 13  PRO   B C    1 
ATOM   4734 O O    . PRO   B 1 28  ? -6.827  -32.066 12.633  1.00 60.82  ? 13  PRO   B O    1 
ATOM   4735 C CB   . PRO   B 1 28  ? -4.836  -29.520 12.671  1.00 60.92  ? 13  PRO   B CB   1 
ATOM   4736 C CG   . PRO   B 1 28  ? -4.958  -28.291 11.850  1.00 59.65  ? 13  PRO   B CG   1 
ATOM   4737 C CD   . PRO   B 1 28  ? -4.477  -28.658 10.492  1.00 60.08  ? 13  PRO   B CD   1 
ATOM   4738 H HA   . PRO   B 1 28  ? -4.536  -31.406 11.871  1.00 75.77  ? 13  PRO   B HA   1 
ATOM   4739 H HB2  . PRO   B 1 28  ? -5.479  -29.520 13.397  1.00 73.10  ? 13  PRO   B HB2  1 
ATOM   4740 H HB3  . PRO   B 1 28  ? -3.938  -29.615 13.024  1.00 73.10  ? 13  PRO   B HB3  1 
ATOM   4741 H HG2  . PRO   B 1 28  ? -5.886  -28.008 11.821  1.00 71.58  ? 13  PRO   B HG2  1 
ATOM   4742 H HG3  . PRO   B 1 28  ? -4.409  -27.588 12.231  1.00 71.58  ? 13  PRO   B HG3  1 
ATOM   4743 H HD2  . PRO   B 1 28  ? -4.920  -28.128 9.811   1.00 72.10  ? 13  PRO   B HD2  1 
ATOM   4744 H HD3  . PRO   B 1 28  ? -3.515  -28.549 10.423  1.00 72.10  ? 13  PRO   B HD3  1 
ATOM   4745 N N    . ARG   B 1 29  ? -7.514  -30.555 11.107  1.00 67.90  ? 14  ARG   B N    1 
ATOM   4746 C CA   . ARG   B 1 29  ? -8.906  -30.983 11.193  1.00 69.07  ? 14  ARG   B CA   1 
ATOM   4747 C C    . ARG   B 1 29  ? -9.103  -32.406 10.692  1.00 68.07  ? 14  ARG   B C    1 
ATOM   4748 O O    . ARG   B 1 29  ? -10.158 -32.997 10.957  1.00 65.38  ? 14  ARG   B O    1 
ATOM   4749 C CB   . ARG   B 1 29  ? -9.797  -30.008 10.422  1.00 62.41  ? 14  ARG   B CB   1 
ATOM   4750 C CG   . ARG   B 1 29  ? -9.990  -28.695 11.157  1.00 60.54  ? 14  ARG   B CG   1 
ATOM   4751 C CD   . ARG   B 1 29  ? -10.879 -27.717 10.415  1.00 61.09  ? 14  ARG   B CD   1 
ATOM   4752 N NE   . ARG   B 1 29  ? -10.266 -27.242 9.181   1.00 69.54  ? 14  ARG   B NE   1 
ATOM   4753 C CZ   . ARG   B 1 29  ? -10.521 -26.068 8.615   1.00 77.20  ? 14  ARG   B CZ   1 
ATOM   4754 N NH1  . ARG   B 1 29  ? -11.337 -25.189 9.178   1.00 71.90  ? 14  ARG   B NH1  1 
ATOM   4755 N NH2  . ARG   B 1 29  ? -9.936  -25.764 7.459   1.00 71.89  ? 14  ARG   B NH2  1 
ATOM   4756 H H    . ARG   B 1 29  ? -7.372  -29.909 10.557  1.00 81.48  ? 14  ARG   B H    1 
ATOM   4757 H HA   . ARG   B 1 29  ? -9.191  -30.962 12.120  1.00 82.89  ? 14  ARG   B HA   1 
ATOM   4758 H HB2  . ARG   B 1 29  ? -9.388  -29.816 9.563   1.00 74.89  ? 14  ARG   B HB2  1 
ATOM   4759 H HB3  . ARG   B 1 29  ? -10.669 -30.412 10.291  1.00 74.89  ? 14  ARG   B HB3  1 
ATOM   4760 H HG2  . ARG   B 1 29  ? -10.399 -28.874 12.019  1.00 72.65  ? 14  ARG   B HG2  1 
ATOM   4761 H HG3  . ARG   B 1 29  ? -9.125  -28.274 11.282  1.00 72.65  ? 14  ARG   B HG3  1 
ATOM   4762 H HD2  . ARG   B 1 29  ? -11.714 -28.156 10.189  1.00 73.31  ? 14  ARG   B HD2  1 
ATOM   4763 H HD3  . ARG   B 1 29  ? -11.050 -26.949 10.982  1.00 73.31  ? 14  ARG   B HD3  1 
ATOM   4764 H HE   . ARG   B 1 29  ? -9.700  -27.759 8.791   1.00 83.44  ? 14  ARG   B HE   1 
ATOM   4765 H HH11 . ARG   B 1 29  ? -11.716 -25.373 9.927   1.00 86.28  ? 14  ARG   B HH11 1 
ATOM   4766 H HH12 . ARG   B 1 29  ? -11.488 -24.435 8.794   1.00 86.28  ? 14  ARG   B HH12 1 
ATOM   4767 H HH21 . ARG   B 1 29  ? -9.400  -26.326 7.088   1.00 86.27  ? 14  ARG   B HH21 1 
ATOM   4768 H HH22 . ARG   B 1 29  ? -10.093 -25.007 7.083   1.00 86.27  ? 14  ARG   B HH22 1 
ATOM   4769 N N    . ASP   B 1 30  ? -8.120  -32.972 9.990   1.00 67.31  ? 15  ASP   B N    1 
ATOM   4770 C CA   . ASP   B 1 30  ? -8.159  -34.399 9.700   1.00 71.93  ? 15  ASP   B CA   1 
ATOM   4771 C C    . ASP   B 1 30  ? -8.136  -35.221 10.982  1.00 69.44  ? 15  ASP   B C    1 
ATOM   4772 O O    . ASP   B 1 30  ? -8.721  -36.306 11.033  1.00 76.87  ? 15  ASP   B O    1 
ATOM   4773 C CB   . ASP   B 1 30  ? -6.979  -34.792 8.809   1.00 72.19  ? 15  ASP   B CB   1 
ATOM   4774 C CG   . ASP   B 1 30  ? -6.934  -34.005 7.508   1.00 74.87  ? 15  ASP   B CG   1 
ATOM   4775 O OD1  . ASP   B 1 30  ? -7.912  -33.289 7.208   1.00 77.56  ? 15  ASP   B OD1  1 
ATOM   4776 O OD2  . ASP   B 1 30  ? -5.915  -34.098 6.788   1.00 70.67  ? 15  ASP   B OD2  1 
ATOM   4777 H H    . ASP   B 1 30  ? -7.434  -32.558 9.677   1.00 80.77  ? 15  ASP   B H    1 
ATOM   4778 H HA   . ASP   B 1 30  ? -8.978  -34.597 9.219   1.00 86.32  ? 15  ASP   B HA   1 
ATOM   4779 H HB2  . ASP   B 1 30  ? -6.152  -34.626 9.288   1.00 86.63  ? 15  ASP   B HB2  1 
ATOM   4780 H HB3  . ASP   B 1 30  ? -7.050  -35.734 8.587   1.00 86.63  ? 15  ASP   B HB3  1 
ATOM   4781 N N    . HIS   B 1 31  ? -7.475  -34.715 12.030  1.00 64.47  ? 16  HIS   B N    1 
ATOM   4782 C CA   . HIS   B 1 31  ? -7.282  -35.463 13.263  1.00 63.84  ? 16  HIS   B CA   1 
ATOM   4783 C C    . HIS   B 1 31  ? -8.125  -34.967 14.428  1.00 63.16  ? 16  HIS   B C    1 
ATOM   4784 O O    . HIS   B 1 31  ? -8.252  -35.688 15.422  1.00 61.89  ? 16  HIS   B O    1 
ATOM   4785 C CB   . HIS   B 1 31  ? -5.804  -35.423 13.687  1.00 63.09  ? 16  HIS   B CB   1 
ATOM   4786 C CG   . HIS   B 1 31  ? -4.869  -36.074 12.712  1.00 66.13  ? 16  HIS   B CG   1 
ATOM   4787 N ND1  . HIS   B 1 31  ? -4.073  -37.148 13.048  1.00 75.11  ? 16  HIS   B ND1  1 
ATOM   4788 C CD2  . HIS   B 1 31  ? -4.594  -35.794 11.416  1.00 72.77  ? 16  HIS   B CD2  1 
ATOM   4789 C CE1  . HIS   B 1 31  ? -3.353  -37.505 12.000  1.00 67.70  ? 16  HIS   B CE1  1 
ATOM   4790 N NE2  . HIS   B 1 31  ? -3.649  -36.699 10.997  1.00 73.07  ? 16  HIS   B NE2  1 
ATOM   4791 H H    . HIS   B 1 31  ? -7.127  -33.929 12.045  1.00 77.37  ? 16  HIS   B H    1 
ATOM   4792 H HA   . HIS   B 1 31  ? -7.525  -36.387 13.094  1.00 76.61  ? 16  HIS   B HA   1 
ATOM   4793 H HB2  . HIS   B 1 31  ? -5.534  -34.497 13.782  1.00 75.71  ? 16  HIS   B HB2  1 
ATOM   4794 H HB3  . HIS   B 1 31  ? -5.713  -35.884 14.536  1.00 75.71  ? 16  HIS   B HB3  1 
ATOM   4795 H HD1  . HIS   B 1 31  ? -4.050  -37.527 13.819  1.00 90.14  ? 16  HIS   B HD1  1 
ATOM   4796 H HD2  . HIS   B 1 31  ? -4.974  -35.116 10.905  1.00 87.32  ? 16  HIS   B HD2  1 
ATOM   4797 H HE1  . HIS   B 1 31  ? -2.741  -38.205 11.973  1.00 81.24  ? 16  HIS   B HE1  1 
ATOM   4798 N N    . TYR   B 1 32  ? -8.698  -33.769 14.342  1.00 61.08  ? 17  TYR   B N    1 
ATOM   4799 C CA   . TYR   B 1 32  ? -9.470  -33.213 15.440  1.00 59.57  ? 17  TYR   B CA   1 
ATOM   4800 C C    . TYR   B 1 32  ? -10.737 -32.562 14.910  1.00 60.04  ? 17  TYR   B C    1 
ATOM   4801 O O    . TYR   B 1 32  ? -10.781 -32.079 13.777  1.00 65.53  ? 17  TYR   B O    1 
ATOM   4802 C CB   . TYR   B 1 32  ? -8.666  -32.171 16.232  1.00 57.44  ? 17  TYR   B CB   1 
ATOM   4803 C CG   . TYR   B 1 32  ? -7.380  -32.697 16.822  1.00 57.80  ? 17  TYR   B CG   1 
ATOM   4804 C CD1  . TYR   B 1 32  ? -6.192  -32.654 16.102  1.00 57.47  ? 17  TYR   B CD1  1 
ATOM   4805 C CD2  . TYR   B 1 32  ? -7.349  -33.227 18.103  1.00 56.20  ? 17  TYR   B CD2  1 
ATOM   4806 C CE1  . TYR   B 1 32  ? -5.013  -33.130 16.642  1.00 57.27  ? 17  TYR   B CE1  1 
ATOM   4807 C CE2  . TYR   B 1 32  ? -6.175  -33.704 18.647  1.00 55.94  ? 17  TYR   B CE2  1 
ATOM   4808 C CZ   . TYR   B 1 32  ? -5.012  -33.653 17.914  1.00 56.50  ? 17  TYR   B CZ   1 
ATOM   4809 O OH   . TYR   B 1 32  ? -3.841  -34.128 18.450  1.00 56.45  ? 17  TYR   B OH   1 
ATOM   4810 H H    . TYR   B 1 32  ? -8.650  -33.258 13.651  1.00 73.30  ? 17  TYR   B H    1 
ATOM   4811 H HA   . TYR   B 1 32  ? -9.724  -33.935 16.036  1.00 71.49  ? 17  TYR   B HA   1 
ATOM   4812 H HB2  . TYR   B 1 32  ? -8.439  -31.439 15.638  1.00 68.93  ? 17  TYR   B HB2  1 
ATOM   4813 H HB3  . TYR   B 1 32  ? -9.214  -31.848 16.963  1.00 68.93  ? 17  TYR   B HB3  1 
ATOM   4814 H HD1  . TYR   B 1 32  ? -6.192  -32.299 15.243  1.00 68.96  ? 17  TYR   B HD1  1 
ATOM   4815 H HD2  . TYR   B 1 32  ? -8.132  -33.262 18.602  1.00 67.45  ? 17  TYR   B HD2  1 
ATOM   4816 H HE1  . TYR   B 1 32  ? -4.225  -33.096 16.148  1.00 68.72  ? 17  TYR   B HE1  1 
ATOM   4817 H HE2  . TYR   B 1 32  ? -6.170  -34.059 19.507  1.00 67.12  ? 17  TYR   B HE2  1 
ATOM   4818 H HH   . TYR   B 1 32  ? -3.975  -34.408 19.231  1.00 67.74  ? 17  TYR   B HH   1 
ATOM   4819 N N    . ASP   B 1 33  ? -11.768 -32.559 15.749  1.00 67.71  ? 18  ASP   B N    1 
ATOM   4820 C CA   . ASP   B 1 33  ? -12.988 -31.804 15.507  1.00 61.51  ? 18  ASP   B CA   1 
ATOM   4821 C C    . ASP   B 1 33  ? -12.901 -30.496 16.278  1.00 58.21  ? 18  ASP   B C    1 
ATOM   4822 O O    . ASP   B 1 33  ? -12.661 -30.506 17.490  1.00 56.61  ? 18  ASP   B O    1 
ATOM   4823 C CB   . ASP   B 1 33  ? -14.230 -32.579 15.952  1.00 65.11  ? 18  ASP   B CB   1 
ATOM   4824 C CG   . ASP   B 1 33  ? -14.463 -33.841 15.137  1.00 76.36  ? 18  ASP   B CG   1 
ATOM   4825 O OD1  . ASP   B 1 33  ? -14.153 -33.841 13.926  1.00 76.01  ? 18  ASP   B OD1  1 
ATOM   4826 O OD2  . ASP   B 1 33  ? -14.961 -34.833 15.713  1.00 80.86  ? 18  ASP   B OD2  1 
ATOM   4827 H H    . ASP   B 1 33  ? -11.783 -33.001 16.487  1.00 81.25  ? 18  ASP   B H    1 
ATOM   4828 H HA   . ASP   B 1 33  ? -13.075 -31.624 14.558  1.00 73.81  ? 18  ASP   B HA   1 
ATOM   4829 H HB2  . ASP   B 1 33  ? -14.124 -32.838 16.881  1.00 78.13  ? 18  ASP   B HB2  1 
ATOM   4830 H HB3  . ASP   B 1 33  ? -15.009 -32.011 15.852  1.00 78.13  ? 18  ASP   B HB3  1 
ATOM   4831 N N    . LEU   B 1 34  ? -13.081 -29.380 15.580  1.00 57.90  ? 19  LEU   B N    1 
ATOM   4832 C CA   . LEU   B 1 34  ? -13.168 -28.094 16.257  1.00 59.35  ? 19  LEU   B CA   1 
ATOM   4833 C C    . LEU   B 1 34  ? -14.503 -27.999 16.986  1.00 56.53  ? 19  LEU   B C    1 
ATOM   4834 O O    . LEU   B 1 34  ? -15.566 -28.214 16.393  1.00 58.11  ? 19  LEU   B O    1 
ATOM   4835 C CB   . LEU   B 1 34  ? -13.019 -26.941 15.266  1.00 56.49  ? 19  LEU   B CB   1 
ATOM   4836 C CG   . LEU   B 1 34  ? -11.648 -26.748 14.612  1.00 60.07  ? 19  LEU   B CG   1 
ATOM   4837 C CD1  . LEU   B 1 34  ? -11.611 -25.463 13.771  1.00 57.21  ? 19  LEU   B CD1  1 
ATOM   4838 C CD2  . LEU   B 1 34  ? -10.535 -26.730 15.651  1.00 57.60  ? 19  LEU   B CD2  1 
ATOM   4839 H H    . LEU   B 1 34  ? -13.156 -29.341 14.724  1.00 69.48  ? 19  LEU   B H    1 
ATOM   4840 H HA   . LEU   B 1 34  ? -12.446 -28.016 16.900  1.00 71.22  ? 19  LEU   B HA   1 
ATOM   4841 H HB2  . LEU   B 1 34  ? -13.656 -27.082 14.548  1.00 67.79  ? 19  LEU   B HB2  1 
ATOM   4842 H HB3  . LEU   B 1 34  ? -13.225 -26.117 15.735  1.00 67.79  ? 19  LEU   B HB3  1 
ATOM   4843 H HG   . LEU   B 1 34  ? -11.493 -27.501 14.020  1.00 72.09  ? 19  LEU   B HG   1 
ATOM   4844 H HD11 . LEU   B 1 34  ? -10.734 -25.375 13.367  1.00 68.65  ? 19  LEU   B HD11 1 
ATOM   4845 H HD12 . LEU   B 1 34  ? -12.289 -25.518 13.080  1.00 68.65  ? 19  LEU   B HD12 1 
ATOM   4846 H HD13 . LEU   B 1 34  ? -11.788 -24.703 14.348  1.00 68.65  ? 19  LEU   B HD13 1 
ATOM   4847 H HD21 . LEU   B 1 34  ? -9.715  -26.427 15.230  1.00 69.12  ? 19  LEU   B HD21 1 
ATOM   4848 H HD22 . LEU   B 1 34  ? -10.782 -26.125 16.367  1.00 69.12  ? 19  LEU   B HD22 1 
ATOM   4849 H HD23 . LEU   B 1 34  ? -10.415 -27.626 16.001  1.00 69.12  ? 19  LEU   B HD23 1 
ATOM   4850 N N    . LEU   B 1 35  ? -14.443 -27.692 18.281  1.00 56.77  ? 20  LEU   B N    1 
ATOM   4851 C CA   . LEU   B 1 35  ? -15.637 -27.530 19.102  1.00 59.67  ? 20  LEU   B CA   1 
ATOM   4852 C C    . LEU   B 1 35  ? -16.055 -26.066 19.200  1.00 59.24  ? 20  LEU   B C    1 
ATOM   4853 O O    . LEU   B 1 35  ? -17.177 -25.715 18.824  1.00 64.70  ? 20  LEU   B O    1 
ATOM   4854 C CB   . LEU   B 1 35  ? -15.398 -28.118 20.499  1.00 54.15  ? 20  LEU   B CB   1 
ATOM   4855 C CG   . LEU   B 1 35  ? -14.962 -29.583 20.534  1.00 55.38  ? 20  LEU   B CG   1 
ATOM   4856 C CD1  . LEU   B 1 35  ? -14.956 -30.097 21.964  1.00 65.60  ? 20  LEU   B CD1  1 
ATOM   4857 C CD2  . LEU   B 1 35  ? -15.845 -30.453 19.657  1.00 56.92  ? 20  LEU   B CD2  1 
ATOM   4858 H H    . LEU   B 1 35  ? -13.709 -27.570 18.712  1.00 68.12  ? 20  LEU   B H    1 
ATOM   4859 H HA   . LEU   B 1 35  ? -16.367 -28.023 18.694  1.00 71.60  ? 20  LEU   B HA   1 
ATOM   4860 H HB2  . LEU   B 1 35  ? -14.703 -27.599 20.932  1.00 64.98  ? 20  LEU   B HB2  1 
ATOM   4861 H HB3  . LEU   B 1 35  ? -16.225 -28.050 21.002  1.00 64.98  ? 20  LEU   B HB3  1 
ATOM   4862 H HG   . LEU   B 1 35  ? -14.061 -29.642 20.180  1.00 66.46  ? 20  LEU   B HG   1 
ATOM   4863 H HD11 . LEU   B 1 35  ? -14.866 -31.063 21.952  1.00 78.72  ? 20  LEU   B HD11 1 
ATOM   4864 H HD12 . LEU   B 1 35  ? -14.209 -29.701 22.439  1.00 78.72  ? 20  LEU   B HD12 1 
ATOM   4865 H HD13 . LEU   B 1 35  ? -15.790 -29.848 22.392  1.00 78.72  ? 20  LEU   B HD13 1 
ATOM   4866 H HD21 . LEU   B 1 35  ? -15.634 -31.386 19.822  1.00 68.30  ? 20  LEU   B HD21 1 
ATOM   4867 H HD22 . LEU   B 1 35  ? -16.775 -30.281 19.874  1.00 68.30  ? 20  LEU   B HD22 1 
ATOM   4868 H HD23 . LEU   B 1 35  ? -15.678 -30.236 18.726  1.00 68.30  ? 20  LEU   B HD23 1 
ATOM   4869 N N    . GLN   B 1 36  ? -15.172 -25.201 19.695  1.00 58.35  ? 21  GLN   B N    1 
ATOM   4870 C CA   . GLN   B 1 36  ? -15.502 -23.787 19.800  1.00 65.32  ? 21  GLN   B CA   1 
ATOM   4871 C C    . GLN   B 1 36  ? -14.231 -22.961 19.921  1.00 64.46  ? 21  GLN   B C    1 
ATOM   4872 O O    . GLN   B 1 36  ? -13.167 -23.462 20.294  1.00 55.57  ? 21  GLN   B O    1 
ATOM   4873 C CB   . GLN   B 1 36  ? -16.422 -23.507 20.994  1.00 65.26  ? 21  GLN   B CB   1 
ATOM   4874 C CG   . GLN   B 1 36  ? -15.876 -23.980 22.326  1.00 72.47  ? 21  GLN   B CG   1 
ATOM   4875 C CD   . GLN   B 1 36  ? -16.814 -23.662 23.486  1.00 74.70  ? 21  GLN   B CD   1 
ATOM   4876 O OE1  . GLN   B 1 36  ? -17.222 -22.514 23.672  1.00 74.54  ? 21  GLN   B OE1  1 
ATOM   4877 N NE2  . GLN   B 1 36  ? -17.168 -24.683 24.263  1.00 71.45  ? 21  GLN   B NE2  1 
ATOM   4878 H H    . GLN   B 1 36  ? -14.385 -25.408 19.973  1.00 70.02  ? 21  GLN   B H    1 
ATOM   4879 H HA   . GLN   B 1 36  ? -15.953 -23.523 18.983  1.00 78.39  ? 21  GLN   B HA   1 
ATOM   4880 H HB2  . GLN   B 1 36  ? -16.564 -22.550 21.058  1.00 78.31  ? 21  GLN   B HB2  1 
ATOM   4881 H HB3  . GLN   B 1 36  ? -17.268 -23.959 20.846  1.00 78.31  ? 21  GLN   B HB3  1 
ATOM   4882 H HG2  . GLN   B 1 36  ? -15.751 -24.941 22.294  1.00 86.97  ? 21  GLN   B HG2  1 
ATOM   4883 H HG3  . GLN   B 1 36  ? -15.028 -23.540 22.495  1.00 86.97  ? 21  GLN   B HG3  1 
ATOM   4884 H HE21 . GLN   B 1 36  ? -16.869 -25.473 24.098  1.00 85.74  ? 21  GLN   B HE21 1 
ATOM   4885 H HE22 . GLN   B 1 36  ? -17.695 -24.554 24.930  1.00 85.74  ? 21  GLN   B HE22 1 
ATOM   4886 N N    . ARG   B 1 37  ? -14.374 -21.680 19.603  1.00 69.70  ? 22  ARG   B N    1 
ATOM   4887 C CA   . ARG   B 1 37  ? -13.294 -20.707 19.712  1.00 67.20  ? 22  ARG   B CA   1 
ATOM   4888 C C    . ARG   B 1 37  ? -13.234 -20.200 21.148  1.00 61.40  ? 22  ARG   B C    1 
ATOM   4889 O O    . ARG   B 1 37  ? -14.220 -19.662 21.660  1.00 67.16  ? 22  ARG   B O    1 
ATOM   4890 C CB   . ARG   B 1 37  ? -13.550 -19.572 18.721  1.00 71.98  ? 22  ARG   B CB   1 
ATOM   4891 C CG   . ARG   B 1 37  ? -12.443 -18.541 18.545  1.00 72.44  ? 22  ARG   B CG   1 
ATOM   4892 C CD   . ARG   B 1 37  ? -12.847 -17.559 17.443  1.00 69.28  ? 22  ARG   B CD   1 
ATOM   4893 N NE   . ARG   B 1 37  ? -11.906 -16.461 17.250  1.00 80.58  ? 22  ARG   B NE   1 
ATOM   4894 C CZ   . ARG   B 1 37  ? -11.900 -15.340 17.961  1.00 84.18  ? 22  ARG   B CZ   1 
ATOM   4895 N NH1  . ARG   B 1 37  ? -12.724 -15.161 18.982  1.00 80.34  ? 22  ARG   B NH1  1 
ATOM   4896 N NH2  . ARG   B 1 37  ? -11.045 -14.374 17.639  1.00 78.14  ? 22  ARG   B NH2  1 
ATOM   4897 H H    . ARG   B 1 37  ? -15.108 -21.339 19.312  1.00 83.64  ? 22  ARG   B H    1 
ATOM   4898 H HA   . ARG   B 1 37  ? -12.436 -21.107 19.503  1.00 80.64  ? 22  ARG   B HA   1 
ATOM   4899 H HB2  . ARG   B 1 37  ? -13.709 -19.966 17.849  1.00 86.37  ? 22  ARG   B HB2  1 
ATOM   4900 H HB3  . ARG   B 1 37  ? -14.339 -19.090 19.016  1.00 86.37  ? 22  ARG   B HB3  1 
ATOM   4901 H HG2  . ARG   B 1 37  ? -12.312 -18.050 19.372  1.00 86.92  ? 22  ARG   B HG2  1 
ATOM   4902 H HG3  . ARG   B 1 37  ? -11.618 -18.982 18.287  1.00 86.92  ? 22  ARG   B HG3  1 
ATOM   4903 H HD2  . ARG   B 1 37  ? -12.912 -18.041 16.604  1.00 83.13  ? 22  ARG   B HD2  1 
ATOM   4904 H HD3  . ARG   B 1 37  ? -13.707 -17.172 17.671  1.00 83.13  ? 22  ARG   B HD3  1 
ATOM   4905 H HE   . ARG   B 1 37  ? -11.314 -16.546 16.633  1.00 96.69  ? 22  ARG   B HE   1 
ATOM   4906 H HH11 . ARG   B 1 37  ? -13.281 -15.779 19.199  1.00 96.41  ? 22  ARG   B HH11 1 
ATOM   4907 H HH12 . ARG   B 1 37  ? -12.702 -14.426 19.429  1.00 96.41  ? 22  ARG   B HH12 1 
ATOM   4908 H HH21 . ARG   B 1 37  ? -10.506 -14.480 16.977  1.00 93.77  ? 22  ARG   B HH21 1 
ATOM   4909 H HH22 . ARG   B 1 37  ? -11.031 -13.643 18.092  1.00 93.77  ? 22  ARG   B HH22 1 
ATOM   4910 N N    . LEU   B 1 38  ? -12.087 -20.388 21.808  1.00 55.86  ? 23  LEU   B N    1 
ATOM   4911 C CA   . LEU   B 1 38  ? -11.931 -19.999 23.203  1.00 49.02  ? 23  LEU   B CA   1 
ATOM   4912 C C    . LEU   B 1 38  ? -11.308 -18.623 23.378  1.00 59.61  ? 23  LEU   B C    1 
ATOM   4913 O O    . LEU   B 1 38  ? -11.483 -18.007 24.434  1.00 58.61  ? 23  LEU   B O    1 
ATOM   4914 C CB   . LEU   B 1 38  ? -11.062 -21.016 23.951  1.00 50.92  ? 23  LEU   B CB   1 
ATOM   4915 C CG   . LEU   B 1 38  ? -11.521 -22.472 23.920  1.00 56.11  ? 23  LEU   B CG   1 
ATOM   4916 C CD1  . LEU   B 1 38  ? -10.607 -23.338 24.774  1.00 51.44  ? 23  LEU   B CD1  1 
ATOM   4917 C CD2  . LEU   B 1 38  ? -12.963 -22.588 24.385  1.00 62.06  ? 23  LEU   B CD2  1 
ATOM   4918 H H    . LEU   B 1 38  ? -11.383 -20.742 21.463  1.00 67.03  ? 23  LEU   B H    1 
ATOM   4919 H HA   . LEU   B 1 38  ? -12.810 -19.991 23.614  1.00 58.82  ? 23  LEU   B HA   1 
ATOM   4920 H HB2  . LEU   B 1 38  ? -10.173 -20.990 23.565  1.00 61.10  ? 23  LEU   B HB2  1 
ATOM   4921 H HB3  . LEU   B 1 38  ? -11.026 -20.750 24.883  1.00 61.10  ? 23  LEU   B HB3  1 
ATOM   4922 H HG   . LEU   B 1 38  ? -11.475 -22.799 23.007  1.00 67.33  ? 23  LEU   B HG   1 
ATOM   4923 H HD11 . LEU   B 1 38  ? -11.068 -23.569 25.595  1.00 61.73  ? 23  LEU   B HD11 1 
ATOM   4924 H HD12 . LEU   B 1 38  ? -10.385 -24.144 24.282  1.00 61.73  ? 23  LEU   B HD12 1 
ATOM   4925 H HD13 . LEU   B 1 38  ? -9.800  -22.841 24.977  1.00 61.73  ? 23  LEU   B HD13 1 
ATOM   4926 H HD21 . LEU   B 1 38  ? -13.175 -23.525 24.524  1.00 74.47  ? 23  LEU   B HD21 1 
ATOM   4927 H HD22 . LEU   B 1 38  ? -13.067 -22.098 25.215  1.00 74.47  ? 23  LEU   B HD22 1 
ATOM   4928 H HD23 . LEU   B 1 38  ? -13.545 -22.215 23.705  1.00 74.47  ? 23  LEU   B HD23 1 
ATOM   4929 N N    . GLY   B 1 39  ? -10.580 -18.139 22.380  1.00 58.26  ? 24  GLY   B N    1 
ATOM   4930 C CA   . GLY   B 1 39  ? -9.905  -16.867 22.494  1.00 58.32  ? 24  GLY   B CA   1 
ATOM   4931 C C    . GLY   B 1 39  ? -9.047  -16.587 21.282  1.00 57.00  ? 24  GLY   B C    1 
ATOM   4932 O O    . GLY   B 1 39  ? -8.291  -17.452 20.833  1.00 59.41  ? 24  GLY   B O    1 
ATOM   4933 H H    . GLY   B 1 39  ? -10.464 -18.534 21.625  1.00 69.91  ? 24  GLY   B H    1 
ATOM   4934 H HA2  . GLY   B 1 39  ? -10.561 -16.158 22.579  1.00 69.98  ? 24  GLY   B HA2  1 
ATOM   4935 H HA3  . GLY   B 1 39  ? -9.338  -16.869 23.281  1.00 69.98  ? 24  GLY   B HA3  1 
ATOM   4936 N N    . GLY   B 1 40  ? -9.167  -15.385 20.734  1.00 71.96  ? 25  GLY   B N    1 
ATOM   4937 C CA   . GLY   B 1 40  ? -8.359  -14.993 19.602  1.00 72.01  ? 25  GLY   B CA   1 
ATOM   4938 C C    . GLY   B 1 40  ? -7.617  -13.709 19.878  1.00 70.24  ? 25  GLY   B C    1 
ATOM   4939 O O    . GLY   B 1 40  ? -7.572  -13.245 21.021  1.00 77.68  ? 25  GLY   B O    1 
ATOM   4940 H H    . GLY   B 1 40  ? -9.714  -14.778 21.004  1.00 86.35  ? 25  GLY   B H    1 
ATOM   4941 H HA2  . GLY   B 1 40  ? -7.713  -15.690 19.407  1.00 86.41  ? 25  GLY   B HA2  1 
ATOM   4942 H HA3  . GLY   B 1 40  ? -8.927  -14.863 18.826  1.00 86.41  ? 25  GLY   B HA3  1 
ATOM   4943 N N    . GLY   B 1 41  ? -7.029  -13.132 18.846  1.00 70.90  ? 26  GLY   B N    1 
ATOM   4944 C CA   . GLY   B 1 41  ? -6.344  -11.868 18.995  1.00 74.04  ? 26  GLY   B CA   1 
ATOM   4945 C C    . GLY   B 1 41  ? -5.284  -11.705 17.930  1.00 71.62  ? 26  GLY   B C    1 
ATOM   4946 O O    . GLY   B 1 41  ? -5.126  -12.537 17.035  1.00 69.02  ? 26  GLY   B O    1 
ATOM   4947 H H    . GLY   B 1 41  ? -7.013  -13.454 18.049  1.00 85.08  ? 26  GLY   B H    1 
ATOM   4948 H HA2  . GLY   B 1 41  ? -6.979  -11.139 18.917  1.00 88.84  ? 26  GLY   B HA2  1 
ATOM   4949 H HA3  . GLY   B 1 41  ? -5.919  -11.826 19.866  1.00 88.84  ? 26  GLY   B HA3  1 
ATOM   4950 N N    . THR   B 1 42  ? -4.554  -10.599 18.056  1.00 81.88  ? 27  THR   B N    1 
ATOM   4951 C CA   . THR   B 1 42  ? -3.517  -10.283 17.082  1.00 78.91  ? 27  THR   B CA   1 
ATOM   4952 C C    . THR   B 1 42  ? -2.499  -11.413 16.972  1.00 73.00  ? 27  THR   B C    1 
ATOM   4953 O O    . THR   B 1 42  ? -2.013  -11.716 15.876  1.00 77.32  ? 27  THR   B O    1 
ATOM   4954 C CB   . THR   B 1 42  ? -2.832  -8.968  17.467  1.00 76.68  ? 27  THR   B CB   1 
ATOM   4955 O OG1  . THR   B 1 42  ? -3.809  -7.919  17.544  1.00 80.71  ? 27  THR   B OG1  1 
ATOM   4956 C CG2  . THR   B 1 42  ? -1.766  -8.587  16.450  1.00 77.06  ? 27  THR   B CG2  1 
ATOM   4957 H H    . THR   B 1 42  ? -4.638  -10.022 18.688  1.00 98.26  ? 27  THR   B H    1 
ATOM   4958 H HA   . THR   B 1 42  ? -3.925  -10.168 16.209  1.00 94.69  ? 27  THR   B HA   1 
ATOM   4959 H HB   . THR   B 1 42  ? -2.401  -9.077  18.329  1.00 92.02  ? 27  THR   B HB   1 
ATOM   4960 H HG1  . THR   B 1 42  ? -3.441  -7.201  17.775  1.00 96.85  ? 27  THR   B HG1  1 
ATOM   4961 H HG21 . THR   B 1 42  ? -1.456  -7.683  16.617  1.00 92.47  ? 27  THR   B HG21 1 
ATOM   4962 H HG22 . THR   B 1 42  ? -1.013  -9.195  16.515  1.00 92.47  ? 27  THR   B HG22 1 
ATOM   4963 H HG23 . THR   B 1 42  ? -2.132  -8.634  15.553  1.00 92.47  ? 27  THR   B HG23 1 
ATOM   4964 N N    . TYR   B 1 43  ? -2.187  -12.071 18.090  1.00 65.28  ? 28  TYR   B N    1 
ATOM   4965 C CA   . TYR   B 1 43  ? -1.045  -12.974 18.162  1.00 65.75  ? 28  TYR   B CA   1 
ATOM   4966 C C    . TYR   B 1 43  ? -1.430  -14.447 18.241  1.00 60.51  ? 28  TYR   B C    1 
ATOM   4967 O O    . TYR   B 1 43  ? -0.565  -15.288 18.509  1.00 61.07  ? 28  TYR   B O    1 
ATOM   4968 C CB   . TYR   B 1 43  ? -0.172  -12.594 19.358  1.00 57.54  ? 28  TYR   B CB   1 
ATOM   4969 C CG   . TYR   B 1 43  ? 0.288   -11.159 19.319  1.00 59.95  ? 28  TYR   B CG   1 
ATOM   4970 C CD1  . TYR   B 1 43  ? 1.393   -10.786 18.566  1.00 58.52  ? 28  TYR   B CD1  1 
ATOM   4971 C CD2  . TYR   B 1 43  ? -0.384  -10.174 20.029  1.00 62.40  ? 28  TYR   B CD2  1 
ATOM   4972 C CE1  . TYR   B 1 43  ? 1.821   -9.471  18.524  1.00 54.07  ? 28  TYR   B CE1  1 
ATOM   4973 C CE2  . TYR   B 1 43  ? 0.037   -8.854  19.994  1.00 61.49  ? 28  TYR   B CE2  1 
ATOM   4974 C CZ   . TYR   B 1 43  ? 1.140   -8.509  19.237  1.00 61.51  ? 28  TYR   B CZ   1 
ATOM   4975 O OH   . TYR   B 1 43  ? 1.569   -7.201  19.196  1.00 52.55  ? 28  TYR   B OH   1 
ATOM   4976 H H    . TYR   B 1 43  ? -2.628  -12.007 18.826  1.00 78.33  ? 28  TYR   B H    1 
ATOM   4977 H HA   . TYR   B 1 43  ? -0.527  -12.869 17.349  1.00 78.90  ? 28  TYR   B HA   1 
ATOM   4978 H HB2  . TYR   B 1 43  ? -0.681  -12.723 20.174  1.00 69.05  ? 28  TYR   B HB2  1 
ATOM   4979 H HB3  . TYR   B 1 43  ? 0.616   -13.161 19.366  1.00 69.05  ? 28  TYR   B HB3  1 
ATOM   4980 H HD1  . TYR   B 1 43  ? 1.854   -11.432 18.081  1.00 70.22  ? 28  TYR   B HD1  1 
ATOM   4981 H HD2  . TYR   B 1 43  ? -1.129  -10.403 20.537  1.00 74.88  ? 28  TYR   B HD2  1 
ATOM   4982 H HE1  . TYR   B 1 43  ? 2.565   -9.238  18.016  1.00 64.88  ? 28  TYR   B HE1  1 
ATOM   4983 H HE2  . TYR   B 1 43  ? -0.421  -8.204  20.477  1.00 73.79  ? 28  TYR   B HE2  1 
ATOM   4984 H HH   . TYR   B 1 43  ? 1.060   -6.717  19.658  1.00 63.06  ? 28  TYR   B HH   1 
ATOM   4985 N N    . GLY   B 1 44  ? -2.684  -14.786 17.999  1.00 55.60  ? 29  GLY   B N    1 
ATOM   4986 C CA   . GLY   B 1 44  ? -3.066  -16.182 17.949  1.00 61.85  ? 29  GLY   B CA   1 
ATOM   4987 C C    . GLY   B 1 44  ? -4.534  -16.373 18.229  1.00 57.94  ? 29  GLY   B C    1 
ATOM   4988 O O    . GLY   B 1 44  ? -5.220  -15.497 18.760  1.00 63.46  ? 29  GLY   B O    1 
ATOM   4989 H H    . GLY   B 1 44  ? -3.326  -14.231 17.863  1.00 66.72  ? 29  GLY   B H    1 
ATOM   4990 H HA2  . GLY   B 1 44  ? -2.872  -16.538 17.068  1.00 74.22  ? 29  GLY   B HA2  1 
ATOM   4991 H HA3  . GLY   B 1 44  ? -2.559  -16.680 18.609  1.00 74.22  ? 29  GLY   B HA3  1 
ATOM   4992 N N    . GLU   B 1 45  ? -5.021  -17.552 17.847  1.00 48.24  ? 30  GLU   B N    1 
ATOM   4993 C CA   . GLU   B 1 45  ? -6.385  -17.987 18.107  1.00 48.44  ? 30  GLU   B CA   1 
ATOM   4994 C C    . GLU   B 1 45  ? -6.339  -19.373 18.725  1.00 47.52  ? 30  GLU   B C    1 
ATOM   4995 O O    . GLU   B 1 45  ? -5.569  -20.228 18.282  1.00 48.19  ? 30  GLU   B O    1 
ATOM   4996 C CB   . GLU   B 1 45  ? -7.228  -18.020 16.829  1.00 54.72  ? 30  GLU   B CB   1 
ATOM   4997 C CG   . GLU   B 1 45  ? -7.542  -16.649 16.259  1.00 62.28  ? 30  GLU   B CG   1 
ATOM   4998 C CD   . GLU   B 1 45  ? -8.192  -16.728 14.894  1.00 61.98  ? 30  GLU   B CD   1 
ATOM   4999 O OE1  . GLU   B 1 45  ? -9.242  -17.395 14.775  1.00 62.13  ? 30  GLU   B OE1  1 
ATOM   5000 O OE2  . GLU   B 1 45  ? -7.645  -16.132 13.940  1.00 65.11  ? 30  GLU   B OE2  1 
ATOM   5001 H H    . GLU   B 1 45  ? -4.560  -18.138 17.418  1.00 57.89  ? 30  GLU   B H    1 
ATOM   5002 H HA   . GLU   B 1 45  ? -6.812  -17.373 18.725  1.00 58.13  ? 30  GLU   B HA   1 
ATOM   5003 H HB2  . GLU   B 1 45  ? -6.744  -18.517 16.151  1.00 65.67  ? 30  GLU   B HB2  1 
ATOM   5004 H HB3  . GLU   B 1 45  ? -8.071  -18.458 17.024  1.00 65.67  ? 30  GLU   B HB3  1 
ATOM   5005 H HG2  . GLU   B 1 45  ? -8.151  -16.189 16.857  1.00 74.73  ? 30  GLU   B HG2  1 
ATOM   5006 H HG3  . GLU   B 1 45  ? -6.718  -16.145 16.172  1.00 74.73  ? 30  GLU   B HG3  1 
ATOM   5007 N N    . VAL   B 1 46  ? -7.167  -19.589 19.744  1.00 46.90  ? 31  VAL   B N    1 
ATOM   5008 C CA   . VAL   B 1 46  ? -7.177  -20.822 20.521  1.00 48.90  ? 31  VAL   B CA   1 
ATOM   5009 C C    . VAL   B 1 46  ? -8.550  -21.464 20.397  1.00 47.18  ? 31  VAL   B C    1 
ATOM   5010 O O    . VAL   B 1 46  ? -9.571  -20.787 20.549  1.00 48.88  ? 31  VAL   B O    1 
ATOM   5011 C CB   . VAL   B 1 46  ? -6.838  -20.559 21.999  1.00 45.24  ? 31  VAL   B CB   1 
ATOM   5012 C CG1  . VAL   B 1 46  ? -6.790  -21.862 22.777  1.00 44.95  ? 31  VAL   B CG1  1 
ATOM   5013 C CG2  . VAL   B 1 46  ? -5.528  -19.814 22.113  1.00 44.78  ? 31  VAL   B CG2  1 
ATOM   5014 H H    . VAL   B 1 46  ? -7.750  -19.016 20.011  1.00 56.29  ? 31  VAL   B H    1 
ATOM   5015 H HA   . VAL   B 1 46  ? -6.520  -21.434 20.153  1.00 58.68  ? 31  VAL   B HA   1 
ATOM   5016 H HB   . VAL   B 1 46  ? -7.534  -20.007 22.389  1.00 54.29  ? 31  VAL   B HB   1 
ATOM   5017 H HG11 . VAL   B 1 46  ? -6.430  -21.688 23.661  1.00 53.94  ? 31  VAL   B HG11 1 
ATOM   5018 H HG12 . VAL   B 1 46  ? -7.688  -22.220 22.849  1.00 53.94  ? 31  VAL   B HG12 1 
ATOM   5019 H HG13 . VAL   B 1 46  ? -6.220  -22.489 22.306  1.00 53.94  ? 31  VAL   B HG13 1 
ATOM   5020 H HG21 . VAL   B 1 46  ? -5.287  -19.739 23.049  1.00 53.74  ? 31  VAL   B HG21 1 
ATOM   5021 H HG22 . VAL   B 1 46  ? -4.843  -20.305 21.633  1.00 53.74  ? 31  VAL   B HG22 1 
ATOM   5022 H HG23 . VAL   B 1 46  ? -5.633  -18.930 21.727  1.00 53.74  ? 31  VAL   B HG23 1 
ATOM   5023 N N    . PHE   B 1 47  ? -8.571  -22.769 20.142  1.00 47.78  ? 32  PHE   B N    1 
ATOM   5024 C CA   . PHE   B 1 47  ? -9.802  -23.512 19.940  1.00 48.70  ? 32  PHE   B CA   1 
ATOM   5025 C C    . PHE   B 1 47  ? -9.868  -24.692 20.899  1.00 48.42  ? 32  PHE   B C    1 
ATOM   5026 O O    . PHE   B 1 47  ? -8.853  -25.335 21.182  1.00 48.07  ? 32  PHE   B O    1 
ATOM   5027 C CB   . PHE   B 1 47  ? -9.913  -24.037 18.500  1.00 50.19  ? 32  PHE   B CB   1 
ATOM   5028 C CG   . PHE   B 1 47  ? -9.923  -22.960 17.458  1.00 50.71  ? 32  PHE   B CG   1 
ATOM   5029 C CD1  . PHE   B 1 47  ? -11.113 -22.386 17.053  1.00 51.47  ? 32  PHE   B CD1  1 
ATOM   5030 C CD2  . PHE   B 1 47  ? -8.744  -22.525 16.880  1.00 50.84  ? 32  PHE   B CD2  1 
ATOM   5031 C CE1  . PHE   B 1 47  ? -11.127 -21.393 16.090  1.00 52.06  ? 32  PHE   B CE1  1 
ATOM   5032 C CE2  . PHE   B 1 47  ? -8.750  -21.530 15.917  1.00 52.38  ? 32  PHE   B CE2  1 
ATOM   5033 C CZ   . PHE   B 1 47  ? -9.946  -20.965 15.521  1.00 51.89  ? 32  PHE   B CZ   1 
ATOM   5034 H H    . PHE   B 1 47  ? -7.864  -23.255 20.080  1.00 57.34  ? 32  PHE   B H    1 
ATOM   5035 H HA   . PHE   B 1 47  ? -10.552 -22.924 20.122  1.00 58.44  ? 32  PHE   B HA   1 
ATOM   5036 H HB2  . PHE   B 1 47  ? -9.154  -24.614 18.321  1.00 60.23  ? 32  PHE   B HB2  1 
ATOM   5037 H HB3  . PHE   B 1 47  ? -10.738 -24.539 18.415  1.00 60.23  ? 32  PHE   B HB3  1 
ATOM   5038 H HD1  . PHE   B 1 47  ? -11.913 -22.670 17.432  1.00 61.76  ? 32  PHE   B HD1  1 
ATOM   5039 H HD2  . PHE   B 1 47  ? -7.936  -22.905 17.142  1.00 61.01  ? 32  PHE   B HD2  1 
ATOM   5040 H HE1  . PHE   B 1 47  ? -11.934 -21.014 15.826  1.00 62.47  ? 32  PHE   B HE1  1 
ATOM   5041 H HE2  . PHE   B 1 47  ? -7.951  -21.243 15.537  1.00 62.85  ? 32  PHE   B HE2  1 
ATOM   5042 H HZ   . PHE   B 1 47  ? -9.956  -20.298 14.872  1.00 62.27  ? 32  PHE   B HZ   1 
ATOM   5043 N N    . LYS   B 1 48  ? -11.070 -24.967 21.391  1.00 48.74  ? 33  LYS   B N    1 
ATOM   5044 C CA   . LYS   B 1 48  ? -11.354 -26.220 22.072  1.00 48.96  ? 33  LYS   B CA   1 
ATOM   5045 C C    . LYS   B 1 48  ? -11.685 -27.268 21.019  1.00 52.72  ? 33  LYS   B C    1 
ATOM   5046 O O    . LYS   B 1 48  ? -12.516 -27.027 20.138  1.00 51.67  ? 33  LYS   B O    1 
ATOM   5047 C CB   . LYS   B 1 48  ? -12.515 -26.039 23.047  1.00 53.42  ? 33  LYS   B CB   1 
ATOM   5048 C CG   . LYS   B 1 48  ? -12.884 -27.273 23.860  1.00 49.36  ? 33  LYS   B CG   1 
ATOM   5049 C CD   . LYS   B 1 48  ? -14.061 -26.975 24.781  1.00 50.16  ? 33  LYS   B CD   1 
ATOM   5050 C CE   . LYS   B 1 48  ? -14.465 -28.183 25.608  1.00 60.37  ? 33  LYS   B CE   1 
ATOM   5051 N NZ   . LYS   B 1 48  ? -15.641 -27.889 26.485  1.00 62.15  ? 33  LYS   B NZ   1 
ATOM   5052 H H    . LYS   B 1 48  ? -11.745 -24.438 21.342  1.00 58.49  ? 33  LYS   B H    1 
ATOM   5053 H HA   . LYS   B 1 48  ? -10.588 -26.517 22.588  1.00 58.75  ? 33  LYS   B HA   1 
ATOM   5054 H HB2  . LYS   B 1 48  ? -12.279 -25.339 23.675  1.00 64.11  ? 33  LYS   B HB2  1 
ATOM   5055 H HB3  . LYS   B 1 48  ? -13.301 -25.780 22.541  1.00 64.11  ? 33  LYS   B HB3  1 
ATOM   5056 H HG2  . LYS   B 1 48  ? -13.135 -27.994 23.261  1.00 59.23  ? 33  LYS   B HG2  1 
ATOM   5057 H HG3  . LYS   B 1 48  ? -12.127 -27.543 24.403  1.00 59.23  ? 33  LYS   B HG3  1 
ATOM   5058 H HD2  . LYS   B 1 48  ? -13.816 -26.261 25.390  1.00 60.20  ? 33  LYS   B HD2  1 
ATOM   5059 H HD3  . LYS   B 1 48  ? -14.824 -26.707 24.246  1.00 60.20  ? 33  LYS   B HD3  1 
ATOM   5060 H HE2  . LYS   B 1 48  ? -14.704 -28.912 25.014  1.00 72.45  ? 33  LYS   B HE2  1 
ATOM   5061 H HE3  . LYS   B 1 48  ? -13.722 -28.446 26.174  1.00 72.45  ? 33  LYS   B HE3  1 
ATOM   5062 H HZ1  . LYS   B 1 48  ? -15.858 -28.613 26.956  1.00 74.58  ? 33  LYS   B HZ1  1 
ATOM   5063 H HZ2  . LYS   B 1 48  ? -15.443 -27.228 27.047  1.00 74.58  ? 33  LYS   B HZ2  1 
ATOM   5064 H HZ3  . LYS   B 1 48  ? -16.338 -27.647 25.989  1.00 74.58  ? 33  LYS   B HZ3  1 
ATOM   5065 N N    . ALA   B 1 49  ? -11.016 -28.418 21.090  1.00 50.86  ? 34  ALA   B N    1 
ATOM   5066 C CA   . ALA   B 1 49  ? -11.175 -29.460 20.089  1.00 52.94  ? 34  ALA   B CA   1 
ATOM   5067 C C    . ALA   B 1 49  ? -11.192 -30.824 20.762  1.00 53.00  ? 34  ALA   B C    1 
ATOM   5068 O O    . ALA   B 1 49  ? -10.787 -30.975 21.917  1.00 53.05  ? 34  ALA   B O    1 
ATOM   5069 C CB   . ALA   B 1 49  ? -10.053 -29.404 19.043  1.00 55.83  ? 34  ALA   B CB   1 
ATOM   5070 H H    . ALA   B 1 49  ? -10.460 -28.615 21.715  1.00 61.03  ? 34  ALA   B H    1 
ATOM   5071 H HA   . ALA   B 1 49  ? -12.026 -29.342 19.639  1.00 63.52  ? 34  ALA   B HA   1 
ATOM   5072 H HB1  . ALA   B 1 49  ? -10.178 -30.125 18.406  1.00 67.00  ? 34  ALA   B HB1  1 
ATOM   5073 H HB2  . ALA   B 1 49  ? -10.089 -28.549 18.586  1.00 67.00  ? 34  ALA   B HB2  1 
ATOM   5074 H HB3  . ALA   B 1 49  ? -9.198  -29.504 19.491  1.00 67.00  ? 34  ALA   B HB3  1 
ATOM   5075 N N    . ARG   B 1 50  ? -11.671 -31.821 20.020  1.00 55.26  ? 35  ARG   B N    1 
ATOM   5076 C CA   . ARG   B 1 50  ? -11.722 -33.199 20.483  1.00 59.08  ? 35  ARG   B CA   1 
ATOM   5077 C C    . ARG   B 1 50  ? -10.991 -34.108 19.506  1.00 57.13  ? 35  ARG   B C    1 
ATOM   5078 O O    . ARG   B 1 50  ? -11.170 -34.001 18.288  1.00 58.20  ? 35  ARG   B O    1 
ATOM   5079 C CB   . ARG   B 1 50  ? -13.161 -33.688 20.645  1.00 67.04  ? 35  ARG   B CB   1 
ATOM   5080 C CG   . ARG   B 1 50  ? -13.248 -35.165 21.036  1.00 70.47  ? 35  ARG   B CG   1 
ATOM   5081 C CD   . ARG   B 1 50  ? -14.663 -35.600 21.397  1.00 76.92  ? 35  ARG   B CD   1 
ATOM   5082 N NE   . ARG   B 1 50  ? -15.250 -34.763 22.438  1.00 72.30  ? 35  ARG   B NE   1 
ATOM   5083 C CZ   . ARG   B 1 50  ? -16.205 -33.860 22.240  1.00 75.26  ? 35  ARG   B CZ   1 
ATOM   5084 N NH1  . ARG   B 1 50  ? -16.730 -33.654 21.040  1.00 74.92  ? 35  ARG   B NH1  1 
ATOM   5085 N NH2  . ARG   B 1 50  ? -16.646 -33.149 23.274  1.00 66.43  ? 35  ARG   B NH2  1 
ATOM   5086 H H    . ARG   B 1 50  ? -11.980 -31.718 19.224  1.00 66.31  ? 35  ARG   B H    1 
ATOM   5087 H HA   . ARG   B 1 50  ? -11.280 -33.252 21.346  1.00 70.90  ? 35  ARG   B HA   1 
ATOM   5088 H HB2  . ARG   B 1 50  ? -13.594 -33.168 21.340  1.00 80.45  ? 35  ARG   B HB2  1 
ATOM   5089 H HB3  . ARG   B 1 50  ? -13.629 -33.573 19.803  1.00 80.45  ? 35  ARG   B HB3  1 
ATOM   5090 H HG2  . ARG   B 1 50  ? -12.950 -35.708 20.289  1.00 84.56  ? 35  ARG   B HG2  1 
ATOM   5091 H HG3  . ARG   B 1 50  ? -12.681 -35.322 21.807  1.00 84.56  ? 35  ARG   B HG3  1 
ATOM   5092 H HD2  . ARG   B 1 50  ? -15.225 -35.539 20.609  1.00 92.30  ? 35  ARG   B HD2  1 
ATOM   5093 H HD3  . ARG   B 1 50  ? -14.642 -36.514 21.720  1.00 92.30  ? 35  ARG   B HD3  1 
ATOM   5094 H HE   . ARG   B 1 50  ? -14.957 -34.863 23.241  1.00 86.76  ? 35  ARG   B HE   1 
ATOM   5095 H HH11 . ARG   B 1 50  ? -16.454 -34.110 20.365  1.00 89.91  ? 35  ARG   B HH11 1 
ATOM   5096 H HH12 . ARG   B 1 50  ? -17.346 -33.063 20.936  1.00 89.91  ? 35  ARG   B HH12 1 
ATOM   5097 H HH21 . ARG   B 1 50  ? -16.314 -33.278 24.057  1.00 79.71  ? 35  ARG   B HH21 1 
ATOM   5098 H HH22 . ARG   B 1 50  ? -17.263 -32.561 23.160  1.00 79.71  ? 35  ARG   B HH22 1 
ATOM   5099 N N    . ASP   B 1 51  ? -10.175 -35.007 20.050  1.00 62.48  ? 36  ASP   B N    1 
ATOM   5100 C CA   . ASP   B 1 51  ? -9.470  -35.984 19.230  1.00 68.28  ? 36  ASP   B CA   1 
ATOM   5101 C C    . ASP   B 1 51  ? -10.456 -36.994 18.653  1.00 70.86  ? 36  ASP   B C    1 
ATOM   5102 O O    . ASP   B 1 51  ? -11.354 -37.479 19.346  1.00 71.62  ? 36  ASP   B O    1 
ATOM   5103 C CB   . ASP   B 1 51  ? -8.404  -36.692 20.070  1.00 64.22  ? 36  ASP   B CB   1 
ATOM   5104 C CG   . ASP   B 1 51  ? -7.351  -37.394 19.224  1.00 73.97  ? 36  ASP   B CG   1 
ATOM   5105 O OD1  . ASP   B 1 51  ? -7.718  -38.174 18.320  1.00 75.38  ? 36  ASP   B OD1  1 
ATOM   5106 O OD2  . ASP   B 1 51  ? -6.147  -37.166 19.473  1.00 78.91  ? 36  ASP   B OD2  1 
ATOM   5107 H H    . ASP   B 1 51  ? -10.013 -35.071 20.892  1.00 74.97  ? 36  ASP   B H    1 
ATOM   5108 H HA   . ASP   B 1 51  ? -9.025  -35.541 18.490  1.00 81.93  ? 36  ASP   B HA   1 
ATOM   5109 H HB2  . ASP   B 1 51  ? -7.953  -36.036 20.625  1.00 77.06  ? 36  ASP   B HB2  1 
ATOM   5110 H HB3  . ASP   B 1 51  ? -8.834  -37.359 20.627  1.00 77.06  ? 36  ASP   B HB3  1 
ATOM   5111 N N    . LYS   B 1 52  ? -10.286 -37.311 17.368  1.00 73.34  ? 37  LYS   B N    1 
ATOM   5112 C CA   . LYS   B 1 52  ? -11.225 -38.206 16.697  1.00 81.44  ? 37  LYS   B CA   1 
ATOM   5113 C C    . LYS   B 1 52  ? -11.066 -39.643 17.178  1.00 79.72  ? 37  LYS   B C    1 
ATOM   5114 O O    . LYS   B 1 52  ? -12.042 -40.285 17.583  1.00 81.57  ? 37  LYS   B O    1 
ATOM   5115 C CB   . LYS   B 1 52  ? -11.033 -38.130 15.182  1.00 76.01  ? 37  LYS   B CB   1 
ATOM   5116 C CG   . LYS   B 1 52  ? -11.403 -36.792 14.570  1.00 74.22  ? 37  LYS   B CG   1 
ATOM   5117 C CD   . LYS   B 1 52  ? -11.267 -36.836 13.053  1.00 81.93  ? 37  LYS   B CD   1 
ATOM   5118 C CE   . LYS   B 1 52  ? -11.585 -35.494 12.415  1.00 70.73  ? 37  LYS   B CE   1 
ATOM   5119 N NZ   . LYS   B 1 52  ? -11.499 -35.562 10.929  1.00 78.19  ? 37  LYS   B NZ   1 
ATOM   5120 H H    . LYS   B 1 52  ? -9.644  -37.026 16.871  1.00 88.01  ? 37  LYS   B H    1 
ATOM   5121 H HA   . LYS   B 1 52  ? -12.127 -37.915 16.906  1.00 97.73  ? 37  LYS   B HA   1 
ATOM   5122 H HB2  . LYS   B 1 52  ? -10.099 -38.297 14.980  1.00 91.21  ? 37  LYS   B HB2  1 
ATOM   5123 H HB3  . LYS   B 1 52  ? -11.589 -38.807 14.766  1.00 91.21  ? 37  LYS   B HB3  1 
ATOM   5124 H HG2  . LYS   B 1 52  ? -12.323 -36.577 14.790  1.00 89.07  ? 37  LYS   B HG2  1 
ATOM   5125 H HG3  . LYS   B 1 52  ? -10.811 -36.104 14.912  1.00 89.07  ? 37  LYS   B HG3  1 
ATOM   5126 H HD2  . LYS   B 1 52  ? -10.356 -37.073 12.820  1.00 98.31  ? 37  LYS   B HD2  1 
ATOM   5127 H HD3  . LYS   B 1 52  ? -11.883 -37.494 12.696  1.00 98.31  ? 37  LYS   B HD3  1 
ATOM   5128 H HE2  . LYS   B 1 52  ? -12.486 -35.229 12.656  1.00 84.88  ? 37  LYS   B HE2  1 
ATOM   5129 H HE3  . LYS   B 1 52  ? -10.949 -34.831 12.727  1.00 84.88  ? 37  LYS   B HE3  1 
ATOM   5130 H HZ1  . LYS   B 1 52  ? -11.674 -34.764 10.577  1.00 93.82  ? 37  LYS   B HZ1  1 
ATOM   5131 H HZ2  . LYS   B 1 52  ? -10.681 -35.814 10.683  1.00 93.82  ? 37  LYS   B HZ2  1 
ATOM   5132 H HZ3  . LYS   B 1 52  ? -12.088 -36.151 10.617  1.00 93.82  ? 37  LYS   B HZ3  1 
ATOM   5133 N N    . VAL   B 1 53  ? -9.838  -40.167 17.140  1.00 81.79  ? 38  VAL   B N    1 
ATOM   5134 C CA   . VAL   B 1 53  ? -9.626  -41.571 17.475  1.00 86.38  ? 38  VAL   B CA   1 
ATOM   5135 C C    . VAL   B 1 53  ? -9.779  -41.815 18.972  1.00 86.01  ? 38  VAL   B C    1 
ATOM   5136 O O    . VAL   B 1 53  ? -10.249 -42.883 19.384  1.00 89.59  ? 38  VAL   B O    1 
ATOM   5137 C CB   . VAL   B 1 53  ? -8.246  -42.039 16.968  1.00 88.04  ? 38  VAL   B CB   1 
ATOM   5138 C CG1  . VAL   B 1 53  ? -7.124  -41.211 17.594  1.00 88.25  ? 38  VAL   B CG1  1 
ATOM   5139 C CG2  . VAL   B 1 53  ? -8.043  -43.522 17.255  1.00 89.24  ? 38  VAL   B CG2  1 
ATOM   5140 H H    . VAL   B 1 53  ? -9.124  -39.736 16.927  1.00 98.15  ? 38  VAL   B H    1 
ATOM   5141 H HA   . VAL   B 1 53  ? -10.309 -42.091 17.024  1.00 103.65 ? 38  VAL   B HA   1 
ATOM   5142 H HB   . VAL   B 1 53  ? -8.211  -41.908 16.008  1.00 105.64 ? 38  VAL   B HB   1 
ATOM   5143 H HG11 . VAL   B 1 53  ? -6.269  -41.574 17.314  1.00 105.90 ? 38  VAL   B HG11 1 
ATOM   5144 H HG12 . VAL   B 1 53  ? -7.206  -40.291 17.295  1.00 105.90 ? 38  VAL   B HG12 1 
ATOM   5145 H HG13 . VAL   B 1 53  ? -7.202  -41.253 18.560  1.00 105.90 ? 38  VAL   B HG13 1 
ATOM   5146 H HG21 . VAL   B 1 53  ? -7.257  -43.831 16.779  1.00 107.09 ? 38  VAL   B HG21 1 
ATOM   5147 H HG22 . VAL   B 1 53  ? -7.921  -43.645 18.210  1.00 107.09 ? 38  VAL   B HG22 1 
ATOM   5148 H HG23 . VAL   B 1 53  ? -8.825  -44.011 16.956  1.00 107.09 ? 38  VAL   B HG23 1 
ATOM   5149 N N    . SER   B 1 54  ? -9.397  -40.846 19.812  1.00 82.83  ? 39  SER   B N    1 
ATOM   5150 C CA   . SER   B 1 54  ? -9.381  -41.046 21.255  1.00 81.12  ? 39  SER   B CA   1 
ATOM   5151 C C    . SER   B 1 54  ? -10.487 -40.315 22.003  1.00 77.55  ? 39  SER   B C    1 
ATOM   5152 O O    . SER   B 1 54  ? -10.790 -40.694 23.138  1.00 83.19  ? 39  SER   B O    1 
ATOM   5153 C CB   . SER   B 1 54  ? -8.027  -40.610 21.837  1.00 75.90  ? 39  SER   B CB   1 
ATOM   5154 O OG   . SER   B 1 54  ? -7.885  -39.203 21.794  1.00 76.84  ? 39  SER   B OG   1 
ATOM   5155 H H    . SER   B 1 54  ? -9.144  -40.062 19.564  1.00 99.40  ? 39  SER   B H    1 
ATOM   5156 H HA   . SER   B 1 54  ? -9.494  -41.994 21.428  1.00 97.34  ? 39  SER   B HA   1 
ATOM   5157 H HB2  . SER   B 1 54  ? -7.970  -40.904 22.759  1.00 91.08  ? 39  SER   B HB2  1 
ATOM   5158 H HB3  . SER   B 1 54  ? -7.315  -41.014 21.316  1.00 91.08  ? 39  SER   B HB3  1 
ATOM   5159 H HG   . SER   B 1 54  ? -7.147  -38.978 22.126  1.00 92.21  ? 39  SER   B HG   1 
ATOM   5160 N N    . GLY   B 1 55  ? -11.089 -39.286 21.411  1.00 74.90  ? 40  GLY   B N    1 
ATOM   5161 C CA   . GLY   B 1 55  ? -12.144 -38.542 22.066  1.00 68.19  ? 40  GLY   B CA   1 
ATOM   5162 C C    . GLY   B 1 55  ? -11.682 -37.530 23.093  1.00 71.52  ? 40  GLY   B C    1 
ATOM   5163 O O    . GLY   B 1 55  ? -12.529 -36.896 23.738  1.00 65.95  ? 40  GLY   B O    1 
ATOM   5164 H H    . GLY   B 1 55  ? -10.898 -39.002 20.622  1.00 89.88  ? 40  GLY   B H    1 
ATOM   5165 H HA2  . GLY   B 1 55  ? -12.650 -38.064 21.390  1.00 81.83  ? 40  GLY   B HA2  1 
ATOM   5166 H HA3  . GLY   B 1 55  ? -12.731 -39.169 22.515  1.00 81.83  ? 40  GLY   B HA3  1 
ATOM   5167 N N    . ASP   B 1 56  ? -10.376 -37.350 23.266  1.00 60.22  ? 41  ASP   B N    1 
ATOM   5168 C CA   . ASP   B 1 56  ? -9.868  -36.453 24.295  1.00 66.39  ? 41  ASP   B CA   1 
ATOM   5169 C C    . ASP   B 1 56  ? -10.018 -34.994 23.876  1.00 60.43  ? 41  ASP   B C    1 
ATOM   5170 O O    . ASP   B 1 56  ? -9.846  -34.647 22.704  1.00 63.61  ? 41  ASP   B O    1 
ATOM   5171 C CB   . ASP   B 1 56  ? -8.398  -36.757 24.582  1.00 67.97  ? 41  ASP   B CB   1 
ATOM   5172 C CG   . ASP   B 1 56  ? -8.191  -38.139 25.175  1.00 72.88  ? 41  ASP   B CG   1 
ATOM   5173 O OD1  . ASP   B 1 56  ? -9.050  -38.587 25.966  1.00 73.59  ? 41  ASP   B OD1  1 
ATOM   5174 O OD2  . ASP   B 1 56  ? -7.166  -38.776 24.849  1.00 71.14  ? 41  ASP   B OD2  1 
ATOM   5175 H H    . ASP   B 1 56  ? -9.765  -37.736 22.801  1.00 72.26  ? 41  ASP   B H    1 
ATOM   5176 H HA   . ASP   B 1 56  ? -10.380 -36.584 25.108  1.00 79.66  ? 41  ASP   B HA   1 
ATOM   5177 H HB2  . ASP   B 1 56  ? -7.897  -36.708 23.753  1.00 81.56  ? 41  ASP   B HB2  1 
ATOM   5178 H HB3  . ASP   B 1 56  ? -8.058  -36.105 25.215  1.00 81.56  ? 41  ASP   B HB3  1 
ATOM   5179 N N    . LEU   B 1 57  ? -10.342 -34.141 24.846  1.00 53.87  ? 42  LEU   B N    1 
ATOM   5180 C CA   . LEU   B 1 57  ? -10.384 -32.704 24.613  1.00 56.29  ? 42  LEU   B CA   1 
ATOM   5181 C C    . LEU   B 1 57  ? -8.972  -32.132 24.588  1.00 54.86  ? 42  LEU   B C    1 
ATOM   5182 O O    . LEU   B 1 57  ? -8.105  -32.549 25.362  1.00 52.88  ? 42  LEU   B O    1 
ATOM   5183 C CB   . LEU   B 1 57  ? -11.199 -31.998 25.696  1.00 50.37  ? 42  LEU   B CB   1 
ATOM   5184 C CG   . LEU   B 1 57  ? -12.692 -32.315 25.793  1.00 57.61  ? 42  LEU   B CG   1 
ATOM   5185 C CD1  . LEU   B 1 57  ? -13.334 -31.428 26.852  1.00 58.70  ? 42  LEU   B CD1  1 
ATOM   5186 C CD2  . LEU   B 1 57  ? -13.396 -32.152 24.454  1.00 53.91  ? 42  LEU   B CD2  1 
ATOM   5187 H H    . LEU   B 1 57  ? -10.543 -34.372 25.649  1.00 64.64  ? 42  LEU   B H    1 
ATOM   5188 H HA   . LEU   B 1 57  ? -10.809 -32.536 23.757  1.00 67.55  ? 42  LEU   B HA   1 
ATOM   5189 H HB2  . LEU   B 1 57  ? -10.810 -32.227 26.554  1.00 60.45  ? 42  LEU   B HB2  1 
ATOM   5190 H HB3  . LEU   B 1 57  ? -11.127 -31.043 25.543  1.00 60.45  ? 42  LEU   B HB3  1 
ATOM   5191 H HG   . LEU   B 1 57  ? -12.797 -33.244 26.051  1.00 69.13  ? 42  LEU   B HG   1 
ATOM   5192 H HD11 . LEU   B 1 57  ? -14.298 -31.532 26.809  1.00 70.44  ? 42  LEU   B HD11 1 
ATOM   5193 H HD12 . LEU   B 1 57  ? -13.011 -31.696 27.726  1.00 70.44  ? 42  LEU   B HD12 1 
ATOM   5194 H HD13 . LEU   B 1 57  ? -13.093 -30.505 26.679  1.00 70.44  ? 42  LEU   B HD13 1 
ATOM   5195 H HD21 . LEU   B 1 57  ? -14.352 -32.254 24.586  1.00 64.69  ? 42  LEU   B HD21 1 
ATOM   5196 H HD22 . LEU   B 1 57  ? -13.203 -31.270 24.101  1.00 64.69  ? 42  LEU   B HD22 1 
ATOM   5197 H HD23 . LEU   B 1 57  ? -13.072 -32.832 23.842  1.00 64.69  ? 42  LEU   B HD23 1 
ATOM   5198 N N    . VAL   B 1 58  ? -8.749  -31.162 23.701  1.00 52.30  ? 43  VAL   B N    1 
ATOM   5199 C CA   . VAL   B 1 58  ? -7.451  -30.522 23.539  1.00 49.01  ? 43  VAL   B CA   1 
ATOM   5200 C C    . VAL   B 1 58  ? -7.659  -29.036 23.272  1.00 48.18  ? 43  VAL   B C    1 
ATOM   5201 O O    . VAL   B 1 58  ? -8.769  -28.575 23.003  1.00 48.43  ? 43  VAL   B O    1 
ATOM   5202 C CB   . VAL   B 1 58  ? -6.625  -31.147 22.392  1.00 51.46  ? 43  VAL   B CB   1 
ATOM   5203 C CG1  . VAL   B 1 58  ? -6.191  -32.558 22.746  1.00 52.78  ? 43  VAL   B CG1  1 
ATOM   5204 C CG2  . VAL   B 1 58  ? -7.422  -31.127 21.096  1.00 51.51  ? 43  VAL   B CG2  1 
ATOM   5205 H H    . VAL   B 1 58  ? -9.352  -30.853 23.171  1.00 62.76  ? 43  VAL   B H    1 
ATOM   5206 H HA   . VAL   B 1 58  ? -6.957  -30.617 24.368  1.00 58.81  ? 43  VAL   B HA   1 
ATOM   5207 H HB   . VAL   B 1 58  ? -5.822  -30.619 22.259  1.00 61.76  ? 43  VAL   B HB   1 
ATOM   5208 H HG11 . VAL   B 1 58  ? -5.656  -32.915 22.020  1.00 63.33  ? 43  VAL   B HG11 1 
ATOM   5209 H HG12 . VAL   B 1 58  ? -5.667  -32.532 23.562  1.00 63.33  ? 43  VAL   B HG12 1 
ATOM   5210 H HG13 . VAL   B 1 58  ? -6.980  -33.107 22.877  1.00 63.33  ? 43  VAL   B HG13 1 
ATOM   5211 H HG21 . VAL   B 1 58  ? -6.914  -31.582 20.406  1.00 61.82  ? 43  VAL   B HG21 1 
ATOM   5212 H HG22 . VAL   B 1 58  ? -8.267  -31.582 21.238  1.00 61.82  ? 43  VAL   B HG22 1 
ATOM   5213 H HG23 . VAL   B 1 58  ? -7.581  -30.206 20.837  1.00 61.82  ? 43  VAL   B HG23 1 
ATOM   5214 N N    . ALA   B 1 59  ? -6.563  -28.289 23.349  1.00 47.37  ? 44  ALA   B N    1 
ATOM   5215 C CA   . ALA   B 1 59  ? -6.526  -26.892 22.945  1.00 50.70  ? 44  ALA   B CA   1 
ATOM   5216 C C    . ALA   B 1 59  ? -5.640  -26.765 21.714  1.00 47.59  ? 44  ALA   B C    1 
ATOM   5217 O O    . ALA   B 1 59  ? -4.522  -27.289 21.694  1.00 47.82  ? 44  ALA   B O    1 
ATOM   5218 C CB   . ALA   B 1 59  ? -6.002  -26.000 24.070  1.00 45.42  ? 44  ALA   B CB   1 
ATOM   5219 H H    . ALA   B 1 59  ? -5.808  -28.580 23.640  1.00 56.85  ? 44  ALA   B H    1 
ATOM   5220 H HA   . ALA   B 1 59  ? -7.421  -26.590 22.723  1.00 60.85  ? 44  ALA   B HA   1 
ATOM   5221 H HB1  . ALA   B 1 59  ? -5.991  -25.080 23.765  1.00 54.51  ? 44  ALA   B HB1  1 
ATOM   5222 H HB2  . ALA   B 1 59  ? -6.585  -26.087 24.840  1.00 54.51  ? 44  ALA   B HB2  1 
ATOM   5223 H HB3  . ALA   B 1 59  ? -5.103  -26.282 24.303  1.00 54.51  ? 44  ALA   B HB3  1 
ATOM   5224 N N    . LEU   B 1 60  ? -6.145  -26.087 20.690  1.00 48.14  ? 45  LEU   B N    1 
ATOM   5225 C CA   . LEU   B 1 60  ? -5.392  -25.832 19.470  1.00 48.94  ? 45  LEU   B CA   1 
ATOM   5226 C C    . LEU   B 1 60  ? -5.148  -24.335 19.356  1.00 48.28  ? 45  LEU   B C    1 
ATOM   5227 O O    . LEU   B 1 60  ? -6.101  -23.550 19.345  1.00 48.08  ? 45  LEU   B O    1 
ATOM   5228 C CB   . LEU   B 1 60  ? -6.139  -26.351 18.242  1.00 50.44  ? 45  LEU   B CB   1 
ATOM   5229 C CG   . LEU   B 1 60  ? -6.123  -27.864 18.010  1.00 53.86  ? 45  LEU   B CG   1 
ATOM   5230 C CD1  . LEU   B 1 60  ? -7.022  -28.234 16.842  1.00 54.55  ? 45  LEU   B CD1  1 
ATOM   5231 C CD2  . LEU   B 1 60  ? -4.710  -28.364 17.757  1.00 52.54  ? 45  LEU   B CD2  1 
ATOM   5232 H H    . LEU   B 1 60  ? -6.939  -25.757 20.680  1.00 57.76  ? 45  LEU   B H    1 
ATOM   5233 H HA   . LEU   B 1 60  ? -4.536  -26.286 19.515  1.00 58.73  ? 45  LEU   B HA   1 
ATOM   5234 H HB2  . LEU   B 1 60  ? -7.069  -26.087 18.323  1.00 60.52  ? 45  LEU   B HB2  1 
ATOM   5235 H HB3  . LEU   B 1 60  ? -5.745  -25.940 17.456  1.00 60.52  ? 45  LEU   B HB3  1 
ATOM   5236 H HG   . LEU   B 1 60  ? -6.458  -28.299 18.809  1.00 64.64  ? 45  LEU   B HG   1 
ATOM   5237 H HD11 . LEU   B 1 60  ? -6.993  -29.195 16.713  1.00 65.47  ? 45  LEU   B HD11 1 
ATOM   5238 H HD12 . LEU   B 1 60  ? -7.929  -27.954 17.041  1.00 65.47  ? 45  LEU   B HD12 1 
ATOM   5239 H HD13 . LEU   B 1 60  ? -6.704  -27.784 16.044  1.00 65.47  ? 45  LEU   B HD13 1 
ATOM   5240 H HD21 . LEU   B 1 60  ? -4.745  -29.303 17.520  1.00 63.05  ? 45  LEU   B HD21 1 
ATOM   5241 H HD22 . LEU   B 1 60  ? -4.320  -27.853 17.030  1.00 63.05  ? 45  LEU   B HD22 1 
ATOM   5242 H HD23 . LEU   B 1 60  ? -4.184  -28.246 18.563  1.00 63.05  ? 45  LEU   B HD23 1 
ATOM   5243 N N    . LYS   B 1 61  ? -3.876  -23.945 19.290  1.00 48.10  ? 46  LYS   B N    1 
ATOM   5244 C CA   . LYS   B 1 61  ? -3.495  -22.558 19.061  1.00 47.77  ? 46  LYS   B CA   1 
ATOM   5245 C C    . LYS   B 1 61  ? -3.044  -22.400 17.613  1.00 49.97  ? 46  LYS   B C    1 
ATOM   5246 O O    . LYS   B 1 61  ? -2.044  -22.998 17.202  1.00 49.70  ? 46  LYS   B O    1 
ATOM   5247 C CB   . LYS   B 1 61  ? -2.380  -22.112 20.007  1.00 46.89  ? 46  LYS   B CB   1 
ATOM   5248 C CG   . LYS   B 1 61  ? -2.058  -20.626 19.874  1.00 49.47  ? 46  LYS   B CG   1 
ATOM   5249 C CD   . LYS   B 1 61  ? -0.840  -20.210 20.674  1.00 52.12  ? 46  LYS   B CD   1 
ATOM   5250 C CE   . LYS   B 1 61  ? -0.694  -18.690 20.679  1.00 51.92  ? 46  LYS   B CE   1 
ATOM   5251 N NZ   . LYS   B 1 61  ? 0.522   -18.238 21.407  1.00 55.25  ? 46  LYS   B NZ   1 
ATOM   5252 H H    . LYS   B 1 61  ? -3.206  -24.477 19.377  1.00 57.72  ? 46  LYS   B H    1 
ATOM   5253 H HA   . LYS   B 1 61  ? -4.268  -21.994 19.218  1.00 57.32  ? 46  LYS   B HA   1 
ATOM   5254 H HB2  . LYS   B 1 61  ? -2.656  -22.280 20.921  1.00 56.26  ? 46  LYS   B HB2  1 
ATOM   5255 H HB3  . LYS   B 1 61  ? -1.575  -22.614 19.805  1.00 56.26  ? 46  LYS   B HB3  1 
ATOM   5256 H HG2  . LYS   B 1 61  ? -1.886  -20.422 18.941  1.00 59.36  ? 46  LYS   B HG2  1 
ATOM   5257 H HG3  . LYS   B 1 61  ? -2.815  -20.109 20.192  1.00 59.36  ? 46  LYS   B HG3  1 
ATOM   5258 H HD2  . LYS   B 1 61  ? -0.934  -20.513 21.591  1.00 62.55  ? 46  LYS   B HD2  1 
ATOM   5259 H HD3  . LYS   B 1 61  ? -0.043  -20.595 20.277  1.00 62.55  ? 46  LYS   B HD3  1 
ATOM   5260 H HE2  . LYS   B 1 61  ? -0.631  -18.375 19.764  1.00 62.30  ? 46  LYS   B HE2  1 
ATOM   5261 H HE3  . LYS   B 1 61  ? -1.468  -18.298 21.113  1.00 62.30  ? 46  LYS   B HE3  1 
ATOM   5262 H HZ1  . LYS   B 1 61  ? 0.594   -17.353 21.360  1.00 66.30  ? 46  LYS   B HZ1  1 
ATOM   5263 H HZ2  . LYS   B 1 61  ? 0.472   -18.479 22.263  1.00 66.30  ? 46  LYS   B HZ2  1 
ATOM   5264 H HZ3  . LYS   B 1 61  ? 1.248   -18.606 21.046  1.00 66.30  ? 46  LYS   B HZ3  1 
ATOM   5265 N N    . MET   B 1 62  ? -3.770  -21.587 16.853  1.00 50.19  ? 47  MET   B N    1 
ATOM   5266 C CA   . MET   B 1 62  ? -3.436  -21.307 15.467  1.00 50.64  ? 47  MET   B CA   1 
ATOM   5267 C C    . MET   B 1 62  ? -2.653  -20.004 15.391  1.00 50.41  ? 47  MET   B C    1 
ATOM   5268 O O    . MET   B 1 62  ? -3.094  -18.977 15.916  1.00 49.68  ? 47  MET   B O    1 
ATOM   5269 C CB   . MET   B 1 62  ? -4.692  -21.208 14.602  1.00 51.48  ? 47  MET   B CB   1 
ATOM   5270 C CG   . MET   B 1 62  ? -4.382  -21.050 13.117  1.00 55.60  ? 47  MET   B CG   1 
ATOM   5271 S SD   . MET   B 1 62  ? -5.195  -19.640 12.344  1.00 66.88  ? 47  MET   B SD   1 
ATOM   5272 C CE   . MET   B 1 62  ? -4.314  -18.268 13.082  1.00 59.03  ? 47  MET   B CE   1 
ATOM   5273 H H    . MET   B 1 62  ? -4.476  -21.179 17.126  1.00 60.23  ? 47  MET   B H    1 
ATOM   5274 H HA   . MET   B 1 62  ? -2.893  -22.034 15.122  1.00 60.77  ? 47  MET   B HA   1 
ATOM   5275 H HB2  . MET   B 1 62  ? -5.215  -22.017 14.714  1.00 61.78  ? 47  MET   B HB2  1 
ATOM   5276 H HB3  . MET   B 1 62  ? -5.208  -20.437 14.883  1.00 61.78  ? 47  MET   B HB3  1 
ATOM   5277 H HG2  . MET   B 1 62  ? -3.425  -20.934 13.009  1.00 66.72  ? 47  MET   B HG2  1 
ATOM   5278 H HG3  . MET   B 1 62  ? -4.674  -21.850 12.651  1.00 66.72  ? 47  MET   B HG3  1 
ATOM   5279 H HE1  . MET   B 1 62  ? -4.664  -17.438 12.724  1.00 70.83  ? 47  MET   B HE1  1 
ATOM   5280 H HE2  . MET   B 1 62  ? -4.440  -18.293 14.044  1.00 70.83  ? 47  MET   B HE2  1 
ATOM   5281 H HE3  . MET   B 1 62  ? -3.371  -18.349 12.871  1.00 70.83  ? 47  MET   B HE3  1 
ATOM   5282 N N    . VAL   B 1 63  ? -1.494  -20.053 14.742  1.00 51.19  ? 48  VAL   B N    1 
ATOM   5283 C CA   . VAL   B 1 63  ? -0.687  -18.873 14.464  1.00 51.37  ? 48  VAL   B CA   1 
ATOM   5284 C C    . VAL   B 1 63  ? -0.545  -18.762 12.956  1.00 52.90  ? 48  VAL   B C    1 
ATOM   5285 O O    . VAL   B 1 63  ? -0.178  -19.738 12.291  1.00 53.90  ? 48  VAL   B O    1 
ATOM   5286 C CB   . VAL   B 1 63  ? 0.695   -18.949 15.137  1.00 51.11  ? 48  VAL   B CB   1 
ATOM   5287 C CG1  . VAL   B 1 63  ? 1.417   -17.629 14.997  1.00 51.73  ? 48  VAL   B CG1  1 
ATOM   5288 C CG2  . VAL   B 1 63  ? 0.556   -19.325 16.600  1.00 55.30  ? 48  VAL   B CG2  1 
ATOM   5289 H H    . VAL   B 1 63  ? -1.145  -20.780 14.444  1.00 61.43  ? 48  VAL   B H    1 
ATOM   5290 H HA   . VAL   B 1 63  ? -1.139  -18.083 14.800  1.00 61.64  ? 48  VAL   B HA   1 
ATOM   5291 H HB   . VAL   B 1 63  ? 1.220   -19.636 14.698  1.00 61.33  ? 48  VAL   B HB   1 
ATOM   5292 H HG11 . VAL   B 1 63  ? 2.251   -17.672 15.492  1.00 62.07  ? 48  VAL   B HG11 1 
ATOM   5293 H HG12 . VAL   B 1 63  ? 1.598   -17.466 14.058  1.00 62.07  ? 48  VAL   B HG12 1 
ATOM   5294 H HG13 . VAL   B 1 63  ? 0.856   -16.923 15.353  1.00 62.07  ? 48  VAL   B HG13 1 
ATOM   5295 H HG21 . VAL   B 1 63  ? 1.423   -19.254 17.028  1.00 66.35  ? 48  VAL   B HG21 1 
ATOM   5296 H HG22 . VAL   B 1 63  ? -0.072  -18.718 17.024  1.00 66.35  ? 48  VAL   B HG22 1 
ATOM   5297 H HG23 . VAL   B 1 63  ? 0.229   -20.236 16.663  1.00 66.35  ? 48  VAL   B HG23 1 
ATOM   5298 N N    . LYS   B 1 64  ? -0.846  -17.587 12.416  1.00 57.77  ? 49  LYS   B N    1 
ATOM   5299 C CA   . LYS   B 1 64  ? -0.687  -17.358 10.987  1.00 57.76  ? 49  LYS   B CA   1 
ATOM   5300 C C    . LYS   B 1 64  ? 0.774   -17.095 10.652  1.00 57.09  ? 49  LYS   B C    1 
ATOM   5301 O O    . LYS   B 1 64  ? 1.466   -16.352 11.352  1.00 54.89  ? 49  LYS   B O    1 
ATOM   5302 C CB   . LYS   B 1 64  ? -1.550  -16.183 10.533  1.00 55.42  ? 49  LYS   B CB   1 
ATOM   5303 C CG   . LYS   B 1 64  ? -2.970  -16.584 10.171  1.00 62.35  ? 49  LYS   B CG   1 
ATOM   5304 C CD   . LYS   B 1 64  ? -3.851  -15.375 9.927   1.00 69.17  ? 49  LYS   B CD   1 
ATOM   5305 C CE   . LYS   B 1 64  ? -5.242  -15.794 9.483   1.00 70.55  ? 49  LYS   B CE   1 
ATOM   5306 N NZ   . LYS   B 1 64  ? -6.139  -14.621 9.297   1.00 71.32  ? 49  LYS   B NZ   1 
ATOM   5307 H H    . LYS   B 1 64  ? -1.143  -16.910 12.854  1.00 69.32  ? 49  LYS   B H    1 
ATOM   5308 H HA   . LYS   B 1 64  ? -0.975  -18.145 10.500  1.00 69.31  ? 49  LYS   B HA   1 
ATOM   5309 H HB2  . LYS   B 1 64  ? -1.598  -15.533 11.252  1.00 66.50  ? 49  LYS   B HB2  1 
ATOM   5310 H HB3  . LYS   B 1 64  ? -1.145  -15.781 9.749   1.00 66.50  ? 49  LYS   B HB3  1 
ATOM   5311 H HG2  . LYS   B 1 64  ? -2.956  -17.117 9.361   1.00 74.82  ? 49  LYS   B HG2  1 
ATOM   5312 H HG3  . LYS   B 1 64  ? -3.354  -17.097 10.899  1.00 74.82  ? 49  LYS   B HG3  1 
ATOM   5313 H HD2  . LYS   B 1 64  ? -3.933  -14.864 10.747  1.00 83.00  ? 49  LYS   B HD2  1 
ATOM   5314 H HD3  . LYS   B 1 64  ? -3.460  -14.825 9.230   1.00 83.00  ? 49  LYS   B HD3  1 
ATOM   5315 H HE2  . LYS   B 1 64  ? -5.180  -16.266 8.637   1.00 84.66  ? 49  LYS   B HE2  1 
ATOM   5316 H HE3  . LYS   B 1 64  ? -5.633  -16.372 10.157  1.00 84.66  ? 49  LYS   B HE3  1 
ATOM   5317 H HZ1  . LYS   B 1 64  ? -6.946  -14.893 9.036   1.00 85.59  ? 49  LYS   B HZ1  1 
ATOM   5318 H HZ2  . LYS   B 1 64  ? -6.218  -14.174 10.062  1.00 85.59  ? 49  LYS   B HZ2  1 
ATOM   5319 H HZ3  . LYS   B 1 64  ? -5.804  -14.077 8.677   1.00 85.59  ? 49  LYS   B HZ3  1 
ATOM   5320 N N    . MET   B 1 65  ? 1.243   -17.718 9.575   1.00 57.73  ? 50  MET   B N    1 
ATOM   5321 C CA   . MET   B 1 65  ? 2.621   -17.588 9.136   1.00 59.32  ? 50  MET   B CA   1 
ATOM   5322 C C    . MET   B 1 65  ? 2.706   -16.798 7.839   1.00 60.54  ? 50  MET   B C    1 
ATOM   5323 O O    . MET   B 1 65  ? 1.724   -16.630 7.111   1.00 66.96  ? 50  MET   B O    1 
ATOM   5324 C CB   . MET   B 1 65  ? 3.270   -18.961 8.930   1.00 61.44  ? 50  MET   B CB   1 
ATOM   5325 C CG   . MET   B 1 65  ? 3.615   -19.675 10.218  1.00 62.32  ? 50  MET   B CG   1 
ATOM   5326 S SD   . MET   B 1 65  ? 4.749   -21.046 9.957   1.00 73.95  ? 50  MET   B SD   1 
ATOM   5327 C CE   . MET   B 1 65  ? 6.230   -20.173 9.448   1.00 60.44  ? 50  MET   B CE   1 
ATOM   5328 H H    . MET   B 1 65  ? 0.768   -18.232 9.075   1.00 69.27  ? 50  MET   B H    1 
ATOM   5329 H HA   . MET   B 1 65  ? 3.112   -17.116 9.827   1.00 71.18  ? 50  MET   B HA   1 
ATOM   5330 H HB2  . MET   B 1 65  ? 2.655   -19.524 8.435   1.00 73.73  ? 50  MET   B HB2  1 
ATOM   5331 H HB3  . MET   B 1 65  ? 4.091   -18.844 8.428   1.00 73.73  ? 50  MET   B HB3  1 
ATOM   5332 H HG2  . MET   B 1 65  ? 4.035   -19.048 10.827  1.00 74.78  ? 50  MET   B HG2  1 
ATOM   5333 H HG3  . MET   B 1 65  ? 2.802   -20.027 10.613  1.00 74.78  ? 50  MET   B HG3  1 
ATOM   5334 H HE1  . MET   B 1 65  ? 6.973   -20.796 9.431   1.00 72.53  ? 50  MET   B HE1  1 
ATOM   5335 H HE2  . MET   B 1 65  ? 6.089   -19.802 8.563   1.00 72.53  ? 50  MET   B HE2  1 
ATOM   5336 H HE3  . MET   B 1 65  ? 6.410   -19.461 10.081  1.00 72.53  ? 50  MET   B HE3  1 
ATOM   5337 N N    . GLU   B 1 66  ? 3.906   -16.320 7.561   1.00 61.63  ? 51  GLU   B N    1 
ATOM   5338 C CA   . GLU   B 1 66  ? 4.241   -15.636 6.330   1.00 65.98  ? 51  GLU   B CA   1 
ATOM   5339 C C    . GLU   B 1 66  ? 5.095   -16.536 5.448   1.00 63.63  ? 51  GLU   B C    1 
ATOM   5340 O O    . GLU   B 1 66  ? 5.739   -17.469 5.938   1.00 63.62  ? 51  GLU   B O    1 
ATOM   5341 C CB   . GLU   B 1 66  ? 5.021   -14.346 6.623   1.00 71.13  ? 51  GLU   B CB   1 
ATOM   5342 C CG   . GLU   B 1 66  ? 4.404   -13.434 7.680   1.00 72.09  ? 51  GLU   B CG   1 
ATOM   5343 C CD   . GLU   B 1 66  ? 3.339   -12.508 7.123   1.00 70.97  ? 51  GLU   B CD   1 
ATOM   5344 O OE1  . GLU   B 1 66  ? 3.312   -12.294 5.891   1.00 70.40  ? 51  GLU   B OE1  1 
ATOM   5345 O OE2  . GLU   B 1 66  ? 2.532   -11.989 7.923   1.00 72.80  ? 51  GLU   B OE2  1 
ATOM   5346 H H    . GLU   B 1 66  ? 4.574   -16.384 8.098   1.00 73.96  ? 51  GLU   B H    1 
ATOM   5347 H HA   . GLU   B 1 66  ? 3.428   -15.400 5.855   1.00 79.17  ? 51  GLU   B HA   1 
ATOM   5348 H HB2  . GLU   B 1 66  ? 5.908   -14.589 6.933   1.00 85.35  ? 51  GLU   B HB2  1 
ATOM   5349 H HB3  . GLU   B 1 66  ? 5.086   -13.834 5.802   1.00 85.35  ? 51  GLU   B HB3  1 
ATOM   5350 H HG2  . GLU   B 1 66  ? 3.993   -13.982 8.367   1.00 86.50  ? 51  GLU   B HG2  1 
ATOM   5351 H HG3  . GLU   B 1 66  ? 5.103   -12.884 8.069   1.00 86.50  ? 51  GLU   B HG3  1 
ATOM   5352 N N    . PRO   B 1 67  ? 5.120   -16.298 4.136   1.00 69.08  ? 52  PRO   B N    1 
ATOM   5353 C CA   . PRO   B 1 67  ? 6.291   -16.745 3.365   1.00 67.21  ? 52  PRO   B CA   1 
ATOM   5354 C C    . PRO   B 1 67  ? 7.564   -16.098 3.882   1.00 67.43  ? 52  PRO   B C    1 
ATOM   5355 O O    . PRO   B 1 67  ? 8.615   -16.748 3.961   1.00 68.36  ? 52  PRO   B O    1 
ATOM   5356 C CB   . PRO   B 1 67  ? 5.951   -16.315 1.933   1.00 68.82  ? 52  PRO   B CB   1 
ATOM   5357 C CG   . PRO   B 1 67  ? 4.462   -16.252 1.902   1.00 67.85  ? 52  PRO   B CG   1 
ATOM   5358 C CD   . PRO   B 1 67  ? 4.051   -15.777 3.264   1.00 66.25  ? 52  PRO   B CD   1 
ATOM   5359 H HA   . PRO   B 1 67  ? 6.377   -17.711 3.377   1.00 80.65  ? 52  PRO   B HA   1 
ATOM   5360 H HB2  . PRO   B 1 67  ? 6.340   -15.447 1.745   1.00 82.58  ? 52  PRO   B HB2  1 
ATOM   5361 H HB3  . PRO   B 1 67  ? 6.285   -16.972 1.302   1.00 82.58  ? 52  PRO   B HB3  1 
ATOM   5362 H HG2  . PRO   B 1 67  ? 4.174   -15.628 1.218   1.00 81.42  ? 52  PRO   B HG2  1 
ATOM   5363 H HG3  . PRO   B 1 67  ? 4.100   -17.134 1.721   1.00 81.42  ? 52  PRO   B HG3  1 
ATOM   5364 H HD2  . PRO   B 1 67  ? 4.018   -14.809 3.298   1.00 79.50  ? 52  PRO   B HD2  1 
ATOM   5365 H HD3  . PRO   B 1 67  ? 3.190   -16.147 3.515   1.00 79.50  ? 52  PRO   B HD3  1 
ATOM   5366 N N    . ASP   B 1 68  ? 7.472   -14.825 4.284   1.00 76.43  ? 53  ASP   B N    1 
ATOM   5367 C CA   . ASP   B 1 68  ? 8.572   -14.096 4.907   1.00 74.70  ? 53  ASP   B CA   1 
ATOM   5368 C C    . ASP   B 1 68  ? 8.960   -14.678 6.258   1.00 75.79  ? 53  ASP   B C    1 
ATOM   5369 O O    . ASP   B 1 68  ? 9.859   -14.145 6.923   1.00 73.77  ? 53  ASP   B O    1 
ATOM   5370 C CB   . ASP   B 1 68  ? 8.199   -12.618 5.077   1.00 82.86  ? 53  ASP   B CB   1 
ATOM   5371 C CG   . ASP   B 1 68  ? 8.607   -11.762 3.890   1.00 85.18  ? 53  ASP   B CG   1 
ATOM   5372 O OD1  . ASP   B 1 68  ? 9.627   -12.073 3.238   1.00 81.76  ? 53  ASP   B OD1  1 
ATOM   5373 O OD2  . ASP   B 1 68  ? 7.903   -10.769 3.615   1.00 91.45  ? 53  ASP   B OD2  1 
ATOM   5374 H H    . ASP   B 1 68  ? 6.760   -14.350 4.202   1.00 91.71  ? 53  ASP   B H    1 
ATOM   5375 H HA   . ASP   B 1 68  ? 9.344   -14.142 4.321   1.00 89.65  ? 53  ASP   B HA   1 
ATOM   5376 H HB2  . ASP   B 1 68  ? 7.238   -12.546 5.182   1.00 99.44  ? 53  ASP   B HB2  1 
ATOM   5377 H HB3  . ASP   B 1 68  ? 8.646   -12.270 5.864   1.00 99.44  ? 53  ASP   B HB3  1 
ATOM   5378 N N    . ASP   B 1 69  ? 8.292   -15.739 6.697   1.00 73.53  ? 54  ASP   B N    1 
ATOM   5379 C CA   . ASP   B 1 69  ? 8.684   -16.424 7.914   1.00 67.84  ? 54  ASP   B CA   1 
ATOM   5380 C C    . ASP   B 1 69  ? 9.745   -17.476 7.604   1.00 64.99  ? 54  ASP   B C    1 
ATOM   5381 O O    . ASP   B 1 69  ? 10.031  -17.789 6.447   1.00 66.77  ? 54  ASP   B O    1 
ATOM   5382 C CB   . ASP   B 1 69  ? 7.476   -17.061 8.599   1.00 65.07  ? 54  ASP   B CB   1 
ATOM   5383 C CG   . ASP   B 1 69  ? 6.769   -16.104 9.533   1.00 59.91  ? 54  ASP   B CG   1 
ATOM   5384 O OD1  . ASP   B 1 69  ? 7.465   -15.359 10.253  1.00 59.62  ? 54  ASP   B OD1  1 
ATOM   5385 O OD2  . ASP   B 1 69  ? 5.522   -16.093 9.540   1.00 59.00  ? 54  ASP   B OD2  1 
ATOM   5386 H H    . ASP   B 1 69  ? 7.608   -16.080 6.303   1.00 88.24  ? 54  ASP   B H    1 
ATOM   5387 H HA   . ASP   B 1 69  ? 9.059   -15.778 8.534   1.00 81.41  ? 54  ASP   B HA   1 
ATOM   5388 H HB2  . ASP   B 1 69  ? 6.842   -17.346 7.923   1.00 78.08  ? 54  ASP   B HB2  1 
ATOM   5389 H HB3  . ASP   B 1 69  ? 7.773   -17.825 9.119   1.00 78.08  ? 54  ASP   B HB3  1 
ATOM   5390 N N    . ASP   B 1 70  ? 10.333  -18.017 8.668   1.00 64.44  ? 55  ASP   B N    1 
ATOM   5391 C CA   . ASP   B 1 70  ? 11.501  -18.890 8.579   1.00 66.03  ? 55  ASP   B CA   1 
ATOM   5392 C C    . ASP   B 1 70  ? 11.191  -20.185 9.322   1.00 65.21  ? 55  ASP   B C    1 
ATOM   5393 O O    . ASP   B 1 70  ? 11.205  -20.213 10.555  1.00 63.81  ? 55  ASP   B O    1 
ATOM   5394 C CB   . ASP   B 1 70  ? 12.729  -18.209 9.166   1.00 66.61  ? 55  ASP   B CB   1 
ATOM   5395 C CG   . ASP   B 1 70  ? 14.010  -18.924 8.815   1.00 68.84  ? 55  ASP   B CG   1 
ATOM   5396 O OD1  . ASP   B 1 70  ? 14.536  -18.679 7.709   1.00 70.81  ? 55  ASP   B OD1  1 
ATOM   5397 O OD2  . ASP   B 1 70  ? 14.483  -19.734 9.639   1.00 70.67  ? 55  ASP   B OD2  1 
ATOM   5398 H H    . ASP   B 1 70  ? 10.066  -17.889 9.476   1.00 77.32  ? 55  ASP   B H    1 
ATOM   5399 H HA   . ASP   B 1 70  ? 11.669  -19.105 7.648   1.00 79.24  ? 55  ASP   B HA   1 
ATOM   5400 H HB2  . ASP   B 1 70  ? 12.785  -17.304 8.820   1.00 79.94  ? 55  ASP   B HB2  1 
ATOM   5401 H HB3  . ASP   B 1 70  ? 12.649  -18.190 10.133  1.00 79.94  ? 55  ASP   B HB3  1 
ATOM   5402 N N    . VAL   B 1 71  ? 10.933  -21.257 8.571   1.00 66.24  ? 56  VAL   B N    1 
ATOM   5403 C CA   . VAL   B 1 71  ? 10.544  -22.512 9.202   1.00 69.28  ? 56  VAL   B CA   1 
ATOM   5404 C C    . VAL   B 1 71  ? 11.731  -23.231 9.826   1.00 67.45  ? 56  VAL   B C    1 
ATOM   5405 O O    . VAL   B 1 71  ? 11.535  -24.113 10.669  1.00 66.29  ? 56  VAL   B O    1 
ATOM   5406 C CB   . VAL   B 1 71  ? 9.832   -23.432 8.194   1.00 66.98  ? 56  VAL   B CB   1 
ATOM   5407 C CG1  . VAL   B 1 71  ? 10.820  -24.038 7.217   1.00 69.23  ? 56  VAL   B CG1  1 
ATOM   5408 C CG2  . VAL   B 1 71  ? 9.058   -24.519 8.931   1.00 71.80  ? 56  VAL   B CG2  1 
ATOM   5409 H H    . VAL   B 1 71  ? 10.977  -21.281 7.712   1.00 79.48  ? 56  VAL   B H    1 
ATOM   5410 H HA   . VAL   B 1 71  ? 9.918   -22.307 9.914   1.00 83.14  ? 56  VAL   B HA   1 
ATOM   5411 H HB   . VAL   B 1 71  ? 9.202   -22.904 7.680   1.00 80.37  ? 56  VAL   B HB   1 
ATOM   5412 H HG11 . VAL   B 1 71  ? 10.335  -24.378 6.449   1.00 83.07  ? 56  VAL   B HG11 1 
ATOM   5413 H HG12 . VAL   B 1 71  ? 11.447  -23.353 6.936   1.00 83.07  ? 56  VAL   B HG12 1 
ATOM   5414 H HG13 . VAL   B 1 71  ? 11.295  -24.761 7.655   1.00 83.07  ? 56  VAL   B HG13 1 
ATOM   5415 H HG21 . VAL   B 1 71  ? 8.557   -25.042 8.286   1.00 86.16  ? 56  VAL   B HG21 1 
ATOM   5416 H HG22 . VAL   B 1 71  ? 9.685   -25.089 9.403   1.00 86.16  ? 56  VAL   B HG22 1 
ATOM   5417 H HG23 . VAL   B 1 71  ? 8.451   -24.101 9.562   1.00 86.16  ? 56  VAL   B HG23 1 
ATOM   5418 N N    . SER   B 1 72  ? 12.960  -22.877 9.450   1.00 68.32  ? 57  SER   B N    1 
ATOM   5419 C CA   . SER   B 1 72  ? 14.121  -23.510 10.065  1.00 69.43  ? 57  SER   B CA   1 
ATOM   5420 C C    . SER   B 1 72  ? 14.160  -23.236 11.563  1.00 71.67  ? 57  SER   B C    1 
ATOM   5421 O O    . SER   B 1 72  ? 14.316  -24.159 12.371  1.00 69.32  ? 57  SER   B O    1 
ATOM   5422 C CB   . SER   B 1 72  ? 15.403  -23.023 9.389   1.00 73.53  ? 57  SER   B CB   1 
ATOM   5423 O OG   . SER   B 1 72  ? 15.566  -23.628 8.117   1.00 73.91  ? 57  SER   B OG   1 
ATOM   5424 H H    . SER   B 1 72  ? 13.144  -22.284 8.854   1.00 81.99  ? 57  SER   B H    1 
ATOM   5425 H HA   . SER   B 1 72  ? 14.062  -24.470 9.935   1.00 83.32  ? 57  SER   B HA   1 
ATOM   5426 H HB2  . SER   B 1 72  ? 15.354  -22.061 9.277   1.00 88.24  ? 57  SER   B HB2  1 
ATOM   5427 H HB3  . SER   B 1 72  ? 16.161  -23.255 9.948   1.00 88.24  ? 57  SER   B HB3  1 
ATOM   5428 H HG   . SER   B 1 72  ? 16.285  -23.371 7.767   1.00 88.69  ? 57  SER   B HG   1 
ATOM   5429 N N    . THR   B 1 73  ? 14.000  -21.969 11.955  1.00 87.71  ? 58  THR   B N    1 
ATOM   5430 C CA   . THR   B 1 73  ? 14.102  -21.612 13.367  1.00 87.44  ? 58  THR   B CA   1 
ATOM   5431 C C    . THR   B 1 73  ? 13.042  -22.327 14.198  1.00 79.74  ? 58  THR   B C    1 
ATOM   5432 O O    . THR   B 1 73  ? 13.354  -22.953 15.217  1.00 80.05  ? 58  THR   B O    1 
ATOM   5433 C CB   . THR   B 1 73  ? 13.982  -20.095 13.539  1.00 83.72  ? 58  THR   B CB   1 
ATOM   5434 O OG1  . THR   B 1 73  ? 12.701  -19.653 13.071  1.00 87.07  ? 58  THR   B OG1  1 
ATOM   5435 C CG2  . THR   B 1 73  ? 15.078  -19.378 12.765  1.00 79.37  ? 58  THR   B CG2  1 
ATOM   5436 H H    . THR   B 1 73  ? 13.834  -21.309 11.429  1.00 105.26 ? 58  THR   B H    1 
ATOM   5437 H HA   . THR   B 1 73  ? 14.975  -21.885 13.689  1.00 104.93 ? 58  THR   B HA   1 
ATOM   5438 H HB   . THR   B 1 73  ? 14.075  -19.872 14.479  1.00 100.47 ? 58  THR   B HB   1 
ATOM   5439 H HG1  . THR   B 1 73  ? 12.613  -19.840 12.257  1.00 104.48 ? 58  THR   B HG1  1 
ATOM   5440 H HG21 . THR   B 1 73  ? 15.281  -18.528 13.188  1.00 95.25  ? 58  THR   B HG21 1 
ATOM   5441 H HG22 . THR   B 1 73  ? 15.882  -19.921 12.748  1.00 95.25  ? 58  THR   B HG22 1 
ATOM   5442 H HG23 . THR   B 1 73  ? 14.789  -19.215 11.854  1.00 95.25  ? 58  THR   B HG23 1 
ATOM   5443 N N    . LEU   B 1 74  ? 11.777  -22.239 13.782  1.00 76.96  ? 59  LEU   B N    1 
ATOM   5444 C CA   . LEU   B 1 74  ? 10.712  -22.880 14.547  1.00 88.25  ? 59  LEU   B CA   1 
ATOM   5445 C C    . LEU   B 1 74  ? 10.850  -24.398 14.542  1.00 85.26  ? 59  LEU   B C    1 
ATOM   5446 O O    . LEU   B 1 74  ? 10.422  -25.061 15.494  1.00 76.39  ? 59  LEU   B O    1 
ATOM   5447 C CB   . LEU   B 1 74  ? 9.345   -22.467 13.999  1.00 89.36  ? 59  LEU   B CB   1 
ATOM   5448 C CG   . LEU   B 1 74  ? 8.952   -22.984 12.612  1.00 90.71  ? 59  LEU   B CG   1 
ATOM   5449 C CD1  . LEU   B 1 74  ? 8.154   -24.281 12.706  1.00 87.90  ? 59  LEU   B CD1  1 
ATOM   5450 C CD2  . LEU   B 1 74  ? 8.163   -21.924 11.864  1.00 87.74  ? 59  LEU   B CD2  1 
ATOM   5451 H H    . LEU   B 1 74  ? 11.515  -21.824 13.075  1.00 92.35  ? 59  LEU   B H    1 
ATOM   5452 H HA   . LEU   B 1 74  ? 10.767  -22.578 15.467  1.00 105.90 ? 59  LEU   B HA   1 
ATOM   5453 H HB2  . LEU   B 1 74  ? 8.669   -22.785 14.618  1.00 107.23 ? 59  LEU   B HB2  1 
ATOM   5454 H HB3  . LEU   B 1 74  ? 9.324   -21.499 13.953  1.00 107.23 ? 59  LEU   B HB3  1 
ATOM   5455 H HG   . LEU   B 1 74  ? 9.761   -23.180 12.113  1.00 108.85 ? 59  LEU   B HG   1 
ATOM   5456 H HD11 . LEU   B 1 74  ? 7.851   -24.531 11.819  1.00 105.48 ? 59  LEU   B HD11 1 
ATOM   5457 H HD12 . LEU   B 1 74  ? 8.723   -24.977 13.069  1.00 105.48 ? 59  LEU   B HD12 1 
ATOM   5458 H HD13 . LEU   B 1 74  ? 7.391   -24.141 13.289  1.00 105.48 ? 59  LEU   B HD13 1 
ATOM   5459 H HD21 . LEU   B 1 74  ? 7.888   -22.283 11.005  1.00 105.29 ? 59  LEU   B HD21 1 
ATOM   5460 H HD22 . LEU   B 1 74  ? 7.383   -21.683 12.387  1.00 105.29 ? 59  LEU   B HD22 1 
ATOM   5461 H HD23 . LEU   B 1 74  ? 8.727   -21.146 11.731  1.00 105.29 ? 59  LEU   B HD23 1 
ATOM   5462 N N    . GLN   B 1 75  ? 11.436  -24.966 13.485  1.00 74.05  ? 60  GLN   B N    1 
ATOM   5463 C CA   . GLN   B 1 75  ? 11.663  -26.406 13.458  1.00 70.45  ? 60  GLN   B CA   1 
ATOM   5464 C C    . GLN   B 1 75  ? 12.531  -26.839 14.632  1.00 73.84  ? 60  GLN   B C    1 
ATOM   5465 O O    . GLN   B 1 75  ? 12.273  -27.873 15.260  1.00 69.19  ? 60  GLN   B O    1 
ATOM   5466 C CB   . GLN   B 1 75  ? 12.312  -26.804 12.132  1.00 67.10  ? 60  GLN   B CB   1 
ATOM   5467 C CG   . GLN   B 1 75  ? 11.845  -28.138 11.583  1.00 69.12  ? 60  GLN   B CG   1 
ATOM   5468 C CD   . GLN   B 1 75  ? 11.959  -28.213 10.071  1.00 77.99  ? 60  GLN   B CD   1 
ATOM   5469 O OE1  . GLN   B 1 75  ? 13.009  -27.916 9.496   1.00 71.71  ? 60  GLN   B OE1  1 
ATOM   5470 N NE2  . GLN   B 1 75  ? 10.870  -28.602 9.417   1.00 79.04  ? 60  GLN   B NE2  1 
ATOM   5471 H H    . GLN   B 1 75  ? 11.705  -24.545 12.784  1.00 88.86  ? 60  GLN   B H    1 
ATOM   5472 H HA   . GLN   B 1 75  ? 10.812  -26.866 13.524  1.00 84.54  ? 60  GLN   B HA   1 
ATOM   5473 H HB2  . GLN   B 1 75  ? 12.105  -26.125 11.470  1.00 80.52  ? 60  GLN   B HB2  1 
ATOM   5474 H HB3  . GLN   B 1 75  ? 13.272  -26.859 12.261  1.00 80.52  ? 60  GLN   B HB3  1 
ATOM   5475 H HG2  . GLN   B 1 75  ? 12.390  -28.845 11.962  1.00 82.94  ? 60  GLN   B HG2  1 
ATOM   5476 H HG3  . GLN   B 1 75  ? 10.915  -28.271 11.822  1.00 82.94  ? 60  GLN   B HG3  1 
ATOM   5477 H HE21 . GLN   B 1 75  ? 10.153  -28.795 9.851   1.00 94.85  ? 60  GLN   B HE21 1 
ATOM   5478 H HE22 . GLN   B 1 75  ? 10.882  -28.662 8.559   1.00 94.85  ? 60  GLN   B HE22 1 
ATOM   5479 N N    . LYS   B 1 76  ? 13.559  -26.049 14.952  1.00 87.19  ? 61  LYS   B N    1 
ATOM   5480 C CA   . LYS   B 1 76  ? 14.440  -26.393 16.063  1.00 89.93  ? 61  LYS   B CA   1 
ATOM   5481 C C    . LYS   B 1 76  ? 13.722  -26.232 17.398  1.00 87.11  ? 61  LYS   B C    1 
ATOM   5482 O O    . LYS   B 1 76  ? 13.824  -27.097 18.276  1.00 86.56  ? 61  LYS   B O    1 
ATOM   5483 C CB   . LYS   B 1 76  ? 15.698  -25.521 16.029  1.00 87.58  ? 61  LYS   B CB   1 
ATOM   5484 C CG   . LYS   B 1 76  ? 16.345  -25.367 14.654  1.00 90.86  ? 61  LYS   B CG   1 
ATOM   5485 C CD   . LYS   B 1 76  ? 17.059  -26.623 14.199  1.00 91.34  ? 61  LYS   B CD   1 
ATOM   5486 C CE   . LYS   B 1 76  ? 18.353  -26.832 14.967  1.00 96.69  ? 61  LYS   B CE   1 
ATOM   5487 N NZ   . LYS   B 1 76  ? 19.161  -27.957 14.409  1.00 104.63 ? 61  LYS   B NZ   1 
ATOM   5488 H H    . LYS   B 1 76  ? 13.765  -25.320 14.546  1.00 104.62 ? 61  LYS   B H    1 
ATOM   5489 H HA   . LYS   B 1 76  ? 14.713  -27.319 15.970  1.00 107.91 ? 61  LYS   B HA   1 
ATOM   5490 H HB2  . LYS   B 1 76  ? 15.464  -24.633 16.341  1.00 105.10 ? 61  LYS   B HB2  1 
ATOM   5491 H HB3  . LYS   B 1 76  ? 16.360  -25.916 16.618  1.00 105.10 ? 61  LYS   B HB3  1 
ATOM   5492 H HG2  . LYS   B 1 76  ? 15.657  -25.160 14.002  1.00 109.03 ? 61  LYS   B HG2  1 
ATOM   5493 H HG3  . LYS   B 1 76  ? 16.995  -24.648 14.689  1.00 109.03 ? 61  LYS   B HG3  1 
ATOM   5494 H HD2  . LYS   B 1 76  ? 16.487  -27.391 14.349  1.00 109.60 ? 61  LYS   B HD2  1 
ATOM   5495 H HD3  . LYS   B 1 76  ? 17.273  -26.548 13.256  1.00 109.60 ? 61  LYS   B HD3  1 
ATOM   5496 H HE2  . LYS   B 1 76  ? 18.887  -26.024 14.920  1.00 116.02 ? 61  LYS   B HE2  1 
ATOM   5497 H HE3  . LYS   B 1 76  ? 18.146  -27.039 15.892  1.00 116.02 ? 61  LYS   B HE3  1 
ATOM   5498 H HZ1  . LYS   B 1 76  ? 19.909  -28.057 14.880  1.00 125.55 ? 61  LYS   B HZ1  1 
ATOM   5499 H HZ2  . LYS   B 1 76  ? 18.694  -28.713 14.444  1.00 125.55 ? 61  LYS   B HZ2  1 
ATOM   5500 H HZ3  . LYS   B 1 76  ? 19.373  -27.787 13.561  1.00 125.55 ? 61  LYS   B HZ3  1 
ATOM   5501 N N    . GLU   B 1 77  ? 12.989  -25.131 17.569  1.00 87.78  ? 62  GLU   B N    1 
ATOM   5502 C CA   . GLU   B 1 77  ? 12.254  -24.923 18.812  1.00 88.05  ? 62  GLU   B CA   1 
ATOM   5503 C C    . GLU   B 1 77  ? 11.205  -26.006 19.022  1.00 85.92  ? 62  GLU   B C    1 
ATOM   5504 O O    . GLU   B 1 77  ? 10.886  -26.349 20.167  1.00 80.67  ? 62  GLU   B O    1 
ATOM   5505 C CB   . GLU   B 1 77  ? 11.605  -23.538 18.803  1.00 85.91  ? 62  GLU   B CB   1 
ATOM   5506 C CG   . GLU   B 1 77  ? 12.587  -22.385 18.591  1.00 93.90  ? 62  GLU   B CG   1 
ATOM   5507 C CD   . GLU   B 1 77  ? 13.004  -21.705 19.892  1.00 93.61  ? 62  GLU   B CD   1 
ATOM   5508 O OE1  . GLU   B 1 77  ? 12.160  -21.012 20.502  1.00 83.73  ? 62  GLU   B OE1  1 
ATOM   5509 O OE2  . GLU   B 1 77  ? 14.174  -21.865 20.305  1.00 91.87  ? 62  GLU   B OE2  1 
ATOM   5510 H H    . GLU   B 1 77  ? 12.904  -24.500 16.991  1.00 105.34 ? 62  GLU   B H    1 
ATOM   5511 H HA   . GLU   B 1 77  ? 12.872  -24.958 19.559  1.00 105.66 ? 62  GLU   B HA   1 
ATOM   5512 H HB2  . GLU   B 1 77  ? 10.954  -23.506 18.085  1.00 103.09 ? 62  GLU   B HB2  1 
ATOM   5513 H HB3  . GLU   B 1 77  ? 11.165  -23.397 19.656  1.00 103.09 ? 62  GLU   B HB3  1 
ATOM   5514 H HG2  . GLU   B 1 77  ? 13.388  -22.729 18.164  1.00 112.68 ? 62  GLU   B HG2  1 
ATOM   5515 H HG3  . GLU   B 1 77  ? 12.170  -21.717 18.025  1.00 112.68 ? 62  GLU   B HG3  1 
ATOM   5516 N N    . ILE   B 1 78  ? 10.665  -26.560 17.932  1.00 80.77  ? 63  ILE   B N    1 
ATOM   5517 C CA   . ILE   B 1 78  ? 9.692   -27.643 18.045  1.00 75.00  ? 63  ILE   B CA   1 
ATOM   5518 C C    . ILE   B 1 78  ? 10.301  -28.829 18.777  1.00 78.46  ? 63  ILE   B C    1 
ATOM   5519 O O    . ILE   B 1 78  ? 9.671   -29.426 19.659  1.00 76.11  ? 63  ILE   B O    1 
ATOM   5520 C CB   . ILE   B 1 78  ? 9.185   -28.049 16.648  1.00 74.31  ? 63  ILE   B CB   1 
ATOM   5521 C CG1  . ILE   B 1 78  ? 8.167   -27.034 16.127  1.00 70.86  ? 63  ILE   B CG1  1 
ATOM   5522 C CG2  . ILE   B 1 78  ? 8.575   -29.448 16.682  1.00 70.17  ? 63  ILE   B CG2  1 
ATOM   5523 C CD1  . ILE   B 1 78  ? 6.775   -27.216 16.696  1.00 70.89  ? 63  ILE   B CD1  1 
ATOM   5524 H H    . ILE   B 1 78  ? 10.844  -26.327 17.124  1.00 96.93  ? 63  ILE   B H    1 
ATOM   5525 H HA   . ILE   B 1 78  ? 8.937   -27.324 18.563  1.00 90.00  ? 63  ILE   B HA   1 
ATOM   5526 H HB   . ILE   B 1 78  ? 9.945   -28.059 16.045  1.00 89.17  ? 63  ILE   B HB   1 
ATOM   5527 H HG12 . ILE   B 1 78  ? 8.468   -26.142 16.361  1.00 85.03  ? 63  ILE   B HG12 1 
ATOM   5528 H HG13 . ILE   B 1 78  ? 8.106   -27.121 15.163  1.00 85.03  ? 63  ILE   B HG13 1 
ATOM   5529 H HG21 . ILE   B 1 78  ? 8.024   -29.571 15.893  1.00 84.20  ? 63  ILE   B HG21 1 
ATOM   5530 H HG22 . ILE   B 1 78  ? 9.290   -30.104 16.691  1.00 84.20  ? 63  ILE   B HG22 1 
ATOM   5531 H HG23 . ILE   B 1 78  ? 8.034   -29.537 17.481  1.00 84.20  ? 63  ILE   B HG23 1 
ATOM   5532 H HD11 . ILE   B 1 78  ? 6.259   -26.411 16.532  1.00 85.07  ? 63  ILE   B HD11 1 
ATOM   5533 H HD12 . ILE   B 1 78  ? 6.353   -27.974 16.262  1.00 85.07  ? 63  ILE   B HD12 1 
ATOM   5534 H HD13 . ILE   B 1 78  ? 6.842   -27.376 17.650  1.00 85.07  ? 63  ILE   B HD13 1 
ATOM   5535 N N    . LEU   B 1 79  ? 11.535  -29.193 18.420  1.00 93.34  ? 64  LEU   B N    1 
ATOM   5536 C CA   . LEU   B 1 79  ? 12.136  -30.403 18.970  1.00 92.84  ? 64  LEU   B CA   1 
ATOM   5537 C C    . LEU   B 1 79  ? 12.257  -30.336 20.487  1.00 89.60  ? 64  LEU   B C    1 
ATOM   5538 O O    . LEU   B 1 79  ? 12.130  -31.362 21.164  1.00 88.04  ? 64  LEU   B O    1 
ATOM   5539 C CB   . LEU   B 1 79  ? 13.505  -30.643 18.331  1.00 87.20  ? 64  LEU   B CB   1 
ATOM   5540 C CG   . LEU   B 1 79  ? 13.504  -31.536 17.084  1.00 102.08 ? 64  LEU   B CG   1 
ATOM   5541 C CD1  . LEU   B 1 79  ? 12.871  -30.823 15.892  1.00 94.21  ? 64  LEU   B CD1  1 
ATOM   5542 C CD2  . LEU   B 1 79  ? 14.920  -32.016 16.749  1.00 96.93  ? 64  LEU   B CD2  1 
ATOM   5543 H H    . LEU   B 1 79  ? 12.036  -28.763 17.869  1.00 112.01 ? 64  LEU   B H    1 
ATOM   5544 H HA   . LEU   B 1 79  ? 11.567  -31.158 18.755  1.00 111.41 ? 64  LEU   B HA   1 
ATOM   5545 H HB2  . LEU   B 1 79  ? 13.875  -29.785 18.073  1.00 104.64 ? 64  LEU   B HB2  1 
ATOM   5546 H HB3  . LEU   B 1 79  ? 14.077  -31.067 18.990  1.00 104.64 ? 64  LEU   B HB3  1 
ATOM   5547 H HG   . LEU   B 1 79  ? 12.965  -32.320 17.272  1.00 122.50 ? 64  LEU   B HG   1 
ATOM   5548 H HD11 . LEU   B 1 79  ? 12.852  -31.429 15.135  1.00 113.06 ? 64  LEU   B HD11 1 
ATOM   5549 H HD12 . LEU   B 1 79  ? 11.967  -30.559 16.126  1.00 113.06 ? 64  LEU   B HD12 1 
ATOM   5550 H HD13 . LEU   B 1 79  ? 13.399  -30.039 15.676  1.00 113.06 ? 64  LEU   B HD13 1 
ATOM   5551 H HD21 . LEU   B 1 79  ? 14.885  -32.576 15.958  1.00 116.32 ? 64  LEU   B HD21 1 
ATOM   5552 H HD22 . LEU   B 1 79  ? 15.484  -31.244 16.583  1.00 116.32 ? 64  LEU   B HD22 1 
ATOM   5553 H HD23 . LEU   B 1 79  ? 15.267  -32.523 17.499  1.00 116.32 ? 64  LEU   B HD23 1 
ATOM   5554 N N    . ILE   B 1 80  ? 12.487  -29.146 21.044  1.00 85.70  ? 65  ILE   B N    1 
ATOM   5555 C CA   . ILE   B 1 80  ? 12.655  -29.034 22.491  1.00 85.05  ? 65  ILE   B CA   1 
ATOM   5556 C C    . ILE   B 1 80  ? 11.376  -29.456 23.203  1.00 86.54  ? 65  ILE   B C    1 
ATOM   5557 O O    . ILE   B 1 80  ? 11.391  -30.324 24.085  1.00 83.31  ? 65  ILE   B O    1 
ATOM   5558 C CB   . ILE   B 1 80  ? 13.076  -27.603 22.876  1.00 88.27  ? 65  ILE   B CB   1 
ATOM   5559 C CG1  . ILE   B 1 80  ? 14.349  -27.209 22.117  1.00 81.32  ? 65  ILE   B CG1  1 
ATOM   5560 C CG2  . ILE   B 1 80  ? 13.279  -27.501 24.389  1.00 87.49  ? 65  ILE   B CG2  1 
ATOM   5561 C CD1  . ILE   B 1 80  ? 14.926  -25.863 22.519  1.00 86.64  ? 65  ILE   B CD1  1 
ATOM   5562 H H    . ILE   B 1 80  ? 12.549  -28.403 20.615  1.00 102.84 ? 65  ILE   B H    1 
ATOM   5563 H HA   . ILE   B 1 80  ? 13.364  -29.635 22.767  1.00 102.06 ? 65  ILE   B HA   1 
ATOM   5564 H HB   . ILE   B 1 80  ? 12.370  -26.987 22.625  1.00 105.93 ? 65  ILE   B HB   1 
ATOM   5565 H HG12 . ILE   B 1 80  ? 15.029  -27.880 22.283  1.00 97.59  ? 65  ILE   B HG12 1 
ATOM   5566 H HG13 . ILE   B 1 80  ? 14.145  -27.170 21.170  1.00 97.59  ? 65  ILE   B HG13 1 
ATOM   5567 H HG21 . ILE   B 1 80  ? 13.556  -26.598 24.611  1.00 104.99 ? 65  ILE   B HG21 1 
ATOM   5568 H HG22 . ILE   B 1 80  ? 12.443  -27.710 24.835  1.00 104.99 ? 65  ILE   B HG22 1 
ATOM   5569 H HG23 . ILE   B 1 80  ? 13.964  -28.133 24.659  1.00 104.99 ? 65  ILE   B HG23 1 
ATOM   5570 H HD11 . ILE   B 1 80  ? 15.571  -25.583 21.850  1.00 103.96 ? 65  ILE   B HD11 1 
ATOM   5571 H HD12 . ILE   B 1 80  ? 14.206  -25.215 22.575  1.00 103.96 ? 65  ILE   B HD12 1 
ATOM   5572 H HD13 . ILE   B 1 80  ? 15.361  -25.950 23.381  1.00 103.96 ? 65  ILE   B HD13 1 
ATOM   5573 N N    . LEU   B 1 81  ? 10.245  -28.856 22.817  1.00 79.27  ? 66  LEU   B N    1 
ATOM   5574 C CA   . LEU   B 1 81  ? 8.972   -29.202 23.442  1.00 75.71  ? 66  LEU   B CA   1 
ATOM   5575 C C    . LEU   B 1 81  ? 8.636   -30.668 23.215  1.00 76.68  ? 66  LEU   B C    1 
ATOM   5576 O O    . LEU   B 1 81  ? 8.086   -31.337 24.097  1.00 77.20  ? 66  LEU   B O    1 
ATOM   5577 C CB   . LEU   B 1 81  ? 7.856   -28.316 22.887  1.00 78.08  ? 66  LEU   B CB   1 
ATOM   5578 C CG   . LEU   B 1 81  ? 8.207   -26.869 22.530  1.00 68.57  ? 66  LEU   B CG   1 
ATOM   5579 C CD1  . LEU   B 1 81  ? 6.997   -26.182 21.930  1.00 69.77  ? 66  LEU   B CD1  1 
ATOM   5580 C CD2  . LEU   B 1 81  ? 8.720   -26.108 23.745  1.00 72.24  ? 66  LEU   B CD2  1 
ATOM   5581 H H    . LEU   B 1 81  ? 10.190  -28.255 22.205  1.00 95.12  ? 66  LEU   B H    1 
ATOM   5582 H HA   . LEU   B 1 81  ? 9.040   -29.043 24.396  1.00 90.85  ? 66  LEU   B HA   1 
ATOM   5583 H HB2  . LEU   B 1 81  ? 7.525   -28.732 22.076  1.00 93.69  ? 66  LEU   B HB2  1 
ATOM   5584 H HB3  . LEU   B 1 81  ? 7.151   -28.278 23.552  1.00 93.69  ? 66  LEU   B HB3  1 
ATOM   5585 H HG   . LEU   B 1 81  ? 8.920   -26.868 21.873  1.00 82.29  ? 66  LEU   B HG   1 
ATOM   5586 H HD11 . LEU   B 1 81  ? 7.234   -25.269 21.700  1.00 83.73  ? 66  LEU   B HD11 1 
ATOM   5587 H HD12 . LEU   B 1 81  ? 6.724   -26.663 21.133  1.00 83.73  ? 66  LEU   B HD12 1 
ATOM   5588 H HD13 . LEU   B 1 81  ? 6.278   -26.183 22.580  1.00 83.73  ? 66  LEU   B HD13 1 
ATOM   5589 H HD21 . LEU   B 1 81  ? 8.914   -25.193 23.486  1.00 86.69  ? 66  LEU   B HD21 1 
ATOM   5590 H HD22 . LEU   B 1 81  ? 8.039   -26.119 24.435  1.00 86.69  ? 66  LEU   B HD22 1 
ATOM   5591 H HD23 . LEU   B 1 81  ? 9.527   -26.538 24.069  1.00 86.69  ? 66  LEU   B HD23 1 
ATOM   5592 N N    . LYS   B 1 82  ? 8.961   -31.183 22.029  1.00 83.74  ? 67  LYS   B N    1 
ATOM   5593 C CA   . LYS   B 1 82  ? 8.709   -32.582 21.716  1.00 84.16  ? 67  LYS   B CA   1 
ATOM   5594 C C    . LYS   B 1 82  ? 9.469   -33.522 22.639  1.00 93.85  ? 67  LYS   B C    1 
ATOM   5595 O O    . LYS   B 1 82  ? 9.095   -34.694 22.755  1.00 94.93  ? 67  LYS   B O    1 
ATOM   5596 C CB   . LYS   B 1 82  ? 9.098   -32.846 20.262  1.00 85.20  ? 67  LYS   B CB   1 
ATOM   5597 C CG   . LYS   B 1 82  ? 8.596   -34.151 19.680  1.00 80.33  ? 67  LYS   B CG   1 
ATOM   5598 C CD   . LYS   B 1 82  ? 8.982   -34.240 18.209  1.00 89.41  ? 67  LYS   B CD   1 
ATOM   5599 C CE   . LYS   B 1 82  ? 8.537   -35.547 17.569  1.00 94.09  ? 67  LYS   B CE   1 
ATOM   5600 N NZ   . LYS   B 1 82  ? 9.042   -35.670 16.169  1.00 97.35  ? 67  LYS   B NZ   1 
ATOM   5601 H H    . LYS   B 1 82  ? 9.328   -30.740 21.390  1.00 100.48 ? 67  LYS   B H    1 
ATOM   5602 H HA   . LYS   B 1 82  ? 7.764   -32.771 21.823  1.00 100.99 ? 67  LYS   B HA   1 
ATOM   5603 H HB2  . LYS   B 1 82  ? 8.738   -32.129 19.715  1.00 102.24 ? 67  LYS   B HB2  1 
ATOM   5604 H HB3  . LYS   B 1 82  ? 10.066  -32.855 20.201  1.00 102.24 ? 67  LYS   B HB3  1 
ATOM   5605 H HG2  . LYS   B 1 82  ? 8.998   -34.897 20.154  1.00 96.40  ? 67  LYS   B HG2  1 
ATOM   5606 H HG3  . LYS   B 1 82  ? 7.630   -34.194 19.753  1.00 96.40  ? 67  LYS   B HG3  1 
ATOM   5607 H HD2  . LYS   B 1 82  ? 8.562   -33.511 17.726  1.00 107.30 ? 67  LYS   B HD2  1 
ATOM   5608 H HD3  . LYS   B 1 82  ? 9.946   -34.179 18.129  1.00 107.30 ? 67  LYS   B HD3  1 
ATOM   5609 H HE2  . LYS   B 1 82  ? 8.884   -36.291 18.085  1.00 112.91 ? 67  LYS   B HE2  1 
ATOM   5610 H HE3  . LYS   B 1 82  ? 7.568   -35.581 17.548  1.00 112.91 ? 67  LYS   B HE3  1 
ATOM   5611 H HZ1  . LYS   B 1 82  ? 8.771   -36.440 15.815  1.00 116.83 ? 67  LYS   B HZ1  1 
ATOM   5612 H HZ2  . LYS   B 1 82  ? 8.731   -34.999 15.674  1.00 116.83 ? 67  LYS   B HZ2  1 
ATOM   5613 H HZ3  . LYS   B 1 82  ? 9.931   -35.646 16.163  1.00 116.83 ? 67  LYS   B HZ3  1 
ATOM   5614 N N    . THR   B 1 83  ? 10.519  -33.036 23.300  1.00 106.28 ? 68  THR   B N    1 
ATOM   5615 C CA   . THR   B 1 83  ? 11.420  -33.868 24.091  1.00 103.34 ? 68  THR   B CA   1 
ATOM   5616 C C    . THR   B 1 83  ? 11.244  -33.713 25.593  1.00 99.65  ? 68  THR   B C    1 
ATOM   5617 O O    . THR   B 1 83  ? 11.361  -34.699 26.324  1.00 99.57  ? 68  THR   B O    1 
ATOM   5618 C CB   . THR   B 1 83  ? 12.880  -33.543 23.733  1.00 109.51 ? 68  THR   B CB   1 
ATOM   5619 O OG1  . THR   B 1 83  ? 13.130  -33.874 22.360  1.00 107.84 ? 68  THR   B OG1  1 
ATOM   5620 C CG2  . THR   B 1 83  ? 13.851  -34.316 24.625  1.00 107.03 ? 68  THR   B CG2  1 
ATOM   5621 H H    . THR   B 1 83  ? 10.735  -32.204 23.304  1.00 127.54 ? 68  THR   B H    1 
ATOM   5622 H HA   . THR   B 1 83  ? 11.246  -34.796 23.870  1.00 124.01 ? 68  THR   B HA   1 
ATOM   5623 H HB   . THR   B 1 83  ? 13.035  -32.596 23.871  1.00 131.42 ? 68  THR   B HB   1 
ATOM   5624 H HG1  . THR   B 1 83  ? 12.647  -33.403 21.859  1.00 129.41 ? 68  THR   B HG1  1 
ATOM   5625 H HG21 . THR   B 1 83  ? 14.736  -34.319 24.228  1.00 128.43 ? 68  THR   B HG21 1 
ATOM   5626 H HG22 . THR   B 1 83  ? 13.900  -33.900 25.500  1.00 128.43 ? 68  THR   B HG22 1 
ATOM   5627 H HG23 . THR   B 1 83  ? 13.549  -35.232 24.728  1.00 128.43 ? 68  THR   B HG23 1 
ATOM   5628 N N    . CYS   B 1 84  ? 10.954  -32.507 26.072  1.00 96.85  ? 69  CYS   B N    1 
ATOM   5629 C CA   . CYS   B 1 84  ? 11.118  -32.153 27.477  1.00 90.07  ? 69  CYS   B CA   1 
ATOM   5630 C C    . CYS   B 1 84  ? 9.772   -31.805 28.096  1.00 89.46  ? 69  CYS   B C    1 
ATOM   5631 O O    . CYS   B 1 84  ? 8.996   -31.038 27.515  1.00 86.65  ? 69  CYS   B O    1 
ATOM   5632 C CB   . CYS   B 1 84  ? 12.100  -30.985 27.597  1.00 88.48  ? 69  CYS   B CB   1 
ATOM   5633 S SG   . CYS   B 1 84  ? 13.655  -31.267 26.692  1.00 94.93  ? 69  CYS   B SG   1 
ATOM   5634 H H    . CYS   B 1 84  ? 10.654  -31.861 25.590  1.00 116.22 ? 69  CYS   B H    1 
ATOM   5635 H HA   . CYS   B 1 84  ? 11.460  -32.911 27.977  1.00 108.09 ? 69  CYS   B HA   1 
ATOM   5636 H HB2  . CYS   B 1 84  ? 11.684  -30.187 27.236  1.00 106.17 ? 69  CYS   B HB2  1 
ATOM   5637 H HB3  . CYS   B 1 84  ? 12.318  -30.852 28.533  1.00 106.17 ? 69  CYS   B HB3  1 
ATOM   5638 H HG   . CYS   B 1 84  ? 14.360  -30.304 26.819  1.00 113.92 ? 69  CYS   B HG   1 
ATOM   5639 N N    . ARG   B 1 85  ? 9.506   -32.366 29.282  1.00 79.81  ? 70  ARG   B N    1 
ATOM   5640 C CA   . ARG   B 1 85  ? 8.220   -32.255 29.954  1.00 71.07  ? 70  ARG   B CA   1 
ATOM   5641 C C    . ARG   B 1 85  ? 8.392   -31.706 31.368  1.00 61.17  ? 70  ARG   B C    1 
ATOM   5642 O O    . ARG   B 1 85  ? 9.494   -31.671 31.921  1.00 63.27  ? 70  ARG   B O    1 
ATOM   5643 C CB   . ARG   B 1 85  ? 7.510   -33.618 30.038  1.00 65.38  ? 70  ARG   B CB   1 
ATOM   5644 C CG   . ARG   B 1 85  ? 7.353   -34.348 28.724  1.00 75.32  ? 70  ARG   B CG   1 
ATOM   5645 C CD   . ARG   B 1 85  ? 8.575   -35.186 28.387  1.00 75.28  ? 70  ARG   B CD   1 
ATOM   5646 N NE   . ARG   B 1 85  ? 8.265   -36.214 27.400  1.00 81.56  ? 70  ARG   B NE   1 
ATOM   5647 C CZ   . ARG   B 1 85  ? 8.085   -35.985 26.106  1.00 83.89  ? 70  ARG   B CZ   1 
ATOM   5648 N NH1  . ARG   B 1 85  ? 8.165   -34.763 25.602  1.00 83.38  ? 70  ARG   B NH1  1 
ATOM   5649 N NH2  . ARG   B 1 85  ? 7.814   -37.006 25.298  1.00 88.56  ? 70  ARG   B NH2  1 
ATOM   5650 H H    . ARG   B 1 85  ? 10.078  -32.830 29.726  1.00 95.77  ? 70  ARG   B H    1 
ATOM   5651 H HA   . ARG   B 1 85  ? 7.676   -31.632 29.447  1.00 85.29  ? 70  ARG   B HA   1 
ATOM   5652 H HB2  . ARG   B 1 85  ? 8.022   -34.192 30.629  1.00 78.46  ? 70  ARG   B HB2  1 
ATOM   5653 H HB3  . ARG   B 1 85  ? 6.621   -33.477 30.400  1.00 78.46  ? 70  ARG   B HB3  1 
ATOM   5654 H HG2  . ARG   B 1 85  ? 6.586   -34.939 28.777  1.00 90.38  ? 70  ARG   B HG2  1 
ATOM   5655 H HG3  . ARG   B 1 85  ? 7.225   -33.701 28.013  1.00 90.38  ? 70  ARG   B HG3  1 
ATOM   5656 H HD2  . ARG   B 1 85  ? 9.267   -34.613 28.023  1.00 90.34  ? 70  ARG   B HD2  1 
ATOM   5657 H HD3  . ARG   B 1 85  ? 8.896   -35.623 29.192  1.00 90.34  ? 70  ARG   B HD3  1 
ATOM   5658 H HE   . ARG   B 1 85  ? 8.194   -37.026 27.676  1.00 97.87  ? 70  ARG   B HE   1 
ATOM   5659 H HH11 . ARG   B 1 85  ? 8.337   -34.095 26.116  1.00 100.06 ? 70  ARG   B HH11 1 
ATOM   5660 H HH12 . ARG   B 1 85  ? 8.045   -34.636 24.759  1.00 100.06 ? 70  ARG   B HH12 1 
ATOM   5661 H HH21 . ARG   B 1 85  ? 7.757   -37.803 25.616  1.00 106.27 ? 70  ARG   B HH21 1 
ATOM   5662 H HH22 . ARG   B 1 85  ? 7.695   -36.870 24.457  1.00 106.27 ? 70  ARG   B HH22 1 
ATOM   5663 N N    . HIS   B 1 86  ? 7.268   -31.283 31.948  1.00 53.29  ? 71  HIS   B N    1 
ATOM   5664 C CA   . HIS   B 1 86  ? 7.142   -30.973 33.367  1.00 50.76  ? 71  HIS   B CA   1 
ATOM   5665 C C    . HIS   B 1 86  ? 5.659   -30.843 33.683  1.00 45.77  ? 71  HIS   B C    1 
ATOM   5666 O O    . HIS   B 1 86  ? 4.898   -30.306 32.875  1.00 45.26  ? 71  HIS   B O    1 
ATOM   5667 C CB   . HIS   B 1 86  ? 7.881   -29.684 33.747  1.00 46.95  ? 71  HIS   B CB   1 
ATOM   5668 C CG   . HIS   B 1 86  ? 7.956   -29.440 35.224  1.00 45.90  ? 71  HIS   B CG   1 
ATOM   5669 N ND1  . HIS   B 1 86  ? 6.946   -28.824 35.928  1.00 45.29  ? 71  HIS   B ND1  1 
ATOM   5670 C CD2  . HIS   B 1 86  ? 8.924   -29.722 36.127  1.00 46.58  ? 71  HIS   B CD2  1 
ATOM   5671 C CE1  . HIS   B 1 86  ? 7.286   -28.736 37.202  1.00 44.14  ? 71  HIS   B CE1  1 
ATOM   5672 N NE2  . HIS   B 1 86  ? 8.482   -29.276 37.350  1.00 45.43  ? 71  HIS   B NE2  1 
ATOM   5673 H H    . HIS   B 1 86  ? 6.532   -31.162 31.520  1.00 63.94  ? 71  HIS   B H    1 
ATOM   5674 H HA   . HIS   B 1 86  ? 7.525   -31.691 33.894  1.00 60.91  ? 71  HIS   B HA   1 
ATOM   5675 H HB2  . HIS   B 1 86  ? 8.789   -29.734 33.409  1.00 56.34  ? 71  HIS   B HB2  1 
ATOM   5676 H HB3  . HIS   B 1 86  ? 7.419   -28.931 33.346  1.00 56.34  ? 71  HIS   B HB3  1 
ATOM   5677 H HD2  . HIS   B 1 86  ? 9.737   -30.138 35.953  1.00 55.90  ? 71  HIS   B HD2  1 
ATOM   5678 H HE1  . HIS   B 1 86  ? 6.771   -28.359 37.879  1.00 52.96  ? 71  HIS   B HE1  1 
ATOM   5679 H HE2  . HIS   B 1 86  ? 8.914   -29.339 38.090  1.00 54.52  ? 71  HIS   B HE2  1 
ATOM   5680 N N    . ALA   B 1 87  ? 5.258   -31.331 34.857  1.00 45.32  ? 72  ALA   B N    1 
ATOM   5681 C CA   . ALA   B 1 87  ? 3.838   -31.371 35.189  1.00 44.32  ? 72  ALA   B CA   1 
ATOM   5682 C C    . ALA   B 1 87  ? 3.201   -29.984 35.137  1.00 43.01  ? 72  ALA   B C    1 
ATOM   5683 O O    . ALA   B 1 87  ? 2.075   -29.830 34.649  1.00 42.59  ? 72  ALA   B O    1 
ATOM   5684 C CB   . ALA   B 1 87  ? 3.644   -31.989 36.573  1.00 46.04  ? 72  ALA   B CB   1 
ATOM   5685 H H    . ALA   B 1 87  ? 5.780   -31.638 35.468  1.00 54.38  ? 72  ALA   B H    1 
ATOM   5686 H HA   . ALA   B 1 87  ? 3.388   -31.928 34.535  1.00 53.18  ? 72  ALA   B HA   1 
ATOM   5687 H HB1  . ALA   B 1 87  ? 2.696   -32.009 36.779  1.00 55.25  ? 72  ALA   B HB1  1 
ATOM   5688 H HB2  . ALA   B 1 87  ? 4.000   -32.891 36.568  1.00 55.25  ? 72  ALA   B HB2  1 
ATOM   5689 H HB3  . ALA   B 1 87  ? 4.114   -31.451 37.228  1.00 55.25  ? 72  ALA   B HB3  1 
ATOM   5690 N N    . ASN   B 1 88  ? 3.898   -28.967 35.636  1.00 42.54  ? 73  ASN   B N    1 
ATOM   5691 C CA   . ASN   B 1 88  ? 3.364   -27.611 35.689  1.00 41.47  ? 73  ASN   B CA   1 
ATOM   5692 C C    . ASN   B 1 88  ? 3.503   -26.853 34.370  1.00 41.68  ? 73  ASN   B C    1 
ATOM   5693 O O    . ASN   B 1 88  ? 3.265   -25.640 34.346  1.00 41.06  ? 73  ASN   B O    1 
ATOM   5694 C CB   . ASN   B 1 88  ? 4.058   -26.818 36.802  1.00 44.14  ? 73  ASN   B CB   1 
ATOM   5695 C CG   . ASN   B 1 88  ? 3.759   -27.365 38.184  1.00 40.70  ? 73  ASN   B CG   1 
ATOM   5696 O OD1  . ASN   B 1 88  ? 4.644   -27.880 38.862  1.00 41.27  ? 73  ASN   B OD1  1 
ATOM   5697 N ND2  . ASN   B 1 88  ? 2.509   -27.241 38.612  1.00 39.90  ? 73  ASN   B ND2  1 
ATOM   5698 H H    . ASN   B 1 88  ? 4.694   -29.038 35.955  1.00 51.04  ? 73  ASN   B H    1 
ATOM   5699 H HA   . ASN   B 1 88  ? 2.419   -27.670 35.896  1.00 49.76  ? 73  ASN   B HA   1 
ATOM   5700 H HB2  . ASN   B 1 88  ? 5.017   -26.855 36.665  1.00 52.96  ? 73  ASN   B HB2  1 
ATOM   5701 H HB3  . ASN   B 1 88  ? 3.753   -25.897 36.771  1.00 52.96  ? 73  ASN   B HB3  1 
ATOM   5702 H HD21 . ASN   B 1 88  ? 2.290   -27.536 39.390  1.00 47.88  ? 73  ASN   B HD21 1 
ATOM   5703 H HD22 . ASN   B 1 88  ? 1.918   -26.866 38.112  1.00 47.88  ? 73  ASN   B HD22 1 
ATOM   5704 N N    . ILE   B 1 89  ? 3.886   -27.519 33.285  1.00 45.02  ? 74  ILE   B N    1 
ATOM   5705 C CA   . ILE   B 1 89  ? 3.944   -26.917 31.959  1.00 43.06  ? 74  ILE   B CA   1 
ATOM   5706 C C    . ILE   B 1 89  ? 2.866   -27.562 31.104  1.00 43.28  ? 74  ILE   B C    1 
ATOM   5707 O O    . ILE   B 1 89  ? 2.730   -28.792 31.091  1.00 43.95  ? 74  ILE   B O    1 
ATOM   5708 C CB   . ILE   B 1 89  ? 5.328   -27.090 31.313  1.00 47.03  ? 74  ILE   B CB   1 
ATOM   5709 C CG1  . ILE   B 1 89  ? 6.420   -26.462 32.187  1.00 45.14  ? 74  ILE   B CG1  1 
ATOM   5710 C CG2  . ILE   B 1 89  ? 5.336   -26.477 29.916  1.00 44.77  ? 74  ILE   B CG2  1 
ATOM   5711 C CD1  . ILE   B 1 89  ? 6.332   -24.954 32.311  1.00 44.25  ? 74  ILE   B CD1  1 
ATOM   5712 H H    . ILE   B 1 89  ? 4.123   -28.346 33.294  1.00 54.02  ? 74  ILE   B H    1 
ATOM   5713 H HA   . ILE   B 1 89  ? 3.761   -25.967 32.032  1.00 51.67  ? 74  ILE   B HA   1 
ATOM   5714 H HB   . ILE   B 1 89  ? 5.513   -28.039 31.237  1.00 56.44  ? 74  ILE   B HB   1 
ATOM   5715 H HG12 . ILE   B 1 89  ? 6.353   -26.834 33.080  1.00 54.17  ? 74  ILE   B HG12 1 
ATOM   5716 H HG13 . ILE   B 1 89  ? 7.285   -26.675 31.803  1.00 54.17  ? 74  ILE   B HG13 1 
ATOM   5717 H HG21 . ILE   B 1 89  ? 6.254   -26.399 29.611  1.00 53.73  ? 74  ILE   B HG21 1 
ATOM   5718 H HG22 . ILE   B 1 89  ? 4.836   -27.051 29.316  1.00 53.73  ? 74  ILE   B HG22 1 
ATOM   5719 H HG23 . ILE   B 1 89  ? 4.925   -25.599 29.955  1.00 53.73  ? 74  ILE   B HG23 1 
ATOM   5720 H HD11 . ILE   B 1 89  ? 7.038   -24.644 32.901  1.00 53.10  ? 74  ILE   B HD11 1 
ATOM   5721 H HD12 . ILE   B 1 89  ? 6.438   -24.558 31.432  1.00 53.10  ? 74  ILE   B HD12 1 
ATOM   5722 H HD13 . ILE   B 1 89  ? 5.467   -24.717 32.679  1.00 53.10  ? 74  ILE   B HD13 1 
ATOM   5723 N N    . VAL   B 1 90  ? 2.102   -26.733 30.391  1.00 42.87  ? 75  VAL   B N    1 
ATOM   5724 C CA   . VAL   B 1 90  ? 1.056   -27.247 29.516  1.00 44.68  ? 75  VAL   B CA   1 
ATOM   5725 C C    . VAL   B 1 90  ? 1.658   -28.270 28.569  1.00 44.61  ? 75  VAL   B C    1 
ATOM   5726 O O    . VAL   B 1 90  ? 2.678   -28.012 27.922  1.00 48.37  ? 75  VAL   B O    1 
ATOM   5727 C CB   . VAL   B 1 90  ? 0.384   -26.096 28.746  1.00 43.22  ? 75  VAL   B CB   1 
ATOM   5728 C CG1  . VAL   B 1 90  ? -0.696  -26.634 27.821  1.00 46.60  ? 75  VAL   B CG1  1 
ATOM   5729 C CG2  . VAL   B 1 90  ? -0.218  -25.082 29.711  1.00 49.38  ? 75  VAL   B CG2  1 
ATOM   5730 H H    . VAL   B 1 90  ? 2.170   -25.876 30.398  1.00 51.44  ? 75  VAL   B H    1 
ATOM   5731 H HA   . VAL   B 1 90  ? 0.379   -27.684 30.057  1.00 53.62  ? 75  VAL   B HA   1 
ATOM   5732 H HB   . VAL   B 1 90  ? 1.058   -25.649 28.211  1.00 51.87  ? 75  VAL   B HB   1 
ATOM   5733 H HG11 . VAL   B 1 90  ? -1.071  -25.898 27.312  1.00 55.92  ? 75  VAL   B HG11 1 
ATOM   5734 H HG12 . VAL   B 1 90  ? -0.302  -27.285 27.221  1.00 55.92  ? 75  VAL   B HG12 1 
ATOM   5735 H HG13 . VAL   B 1 90  ? -1.389  -27.053 28.355  1.00 55.92  ? 75  VAL   B HG13 1 
ATOM   5736 H HG21 . VAL   B 1 90  ? -0.579  -24.339 29.203  1.00 59.25  ? 75  VAL   B HG21 1 
ATOM   5737 H HG22 . VAL   B 1 90  ? -0.924  -25.510 30.219  1.00 59.25  ? 75  VAL   B HG22 1 
ATOM   5738 H HG23 . VAL   B 1 90  ? 0.477   -24.766 30.311  1.00 59.25  ? 75  VAL   B HG23 1 
ATOM   5739 N N    . ALA   B 1 91  ? 1.020   -29.433 28.475  1.00 45.18  ? 76  ALA   B N    1 
ATOM   5740 C CA   . ALA   B 1 91  ? 1.588   -30.536 27.711  1.00 46.70  ? 76  ALA   B CA   1 
ATOM   5741 C C    . ALA   B 1 91  ? 1.529   -30.259 26.215  1.00 47.50  ? 76  ALA   B C    1 
ATOM   5742 O O    . ALA   B 1 91  ? 0.538   -29.735 25.699  1.00 47.11  ? 76  ALA   B O    1 
ATOM   5743 C CB   . ALA   B 1 91  ? 0.846   -31.837 28.021  1.00 47.26  ? 76  ALA   B CB   1 
ATOM   5744 H H    . ALA   B 1 91  ? 0.262   -29.607 28.842  1.00 54.22  ? 76  ALA   B H    1 
ATOM   5745 H HA   . ALA   B 1 91  ? 2.519   -30.641 27.963  1.00 56.05  ? 76  ALA   B HA   1 
ATOM   5746 H HB1  . ALA   B 1 91  ? 1.350   -32.582 27.657  1.00 56.71  ? 76  ALA   B HB1  1 
ATOM   5747 H HB2  . ALA   B 1 91  ? 0.764   -31.932 28.983  1.00 56.71  ? 76  ALA   B HB2  1 
ATOM   5748 H HB3  . ALA   B 1 91  ? -0.034  -31.803 27.616  1.00 56.71  ? 76  ALA   B HB3  1 
ATOM   5749 N N    . TYR   B 1 92  ? 2.603   -30.623 25.520  1.00 54.09  ? 77  TYR   B N    1 
ATOM   5750 C CA   . TYR   B 1 92  ? 2.677   -30.523 24.068  1.00 50.41  ? 77  TYR   B CA   1 
ATOM   5751 C C    . TYR   B 1 92  ? 2.269   -31.854 23.446  1.00 53.95  ? 77  TYR   B C    1 
ATOM   5752 O O    . TYR   B 1 92  ? 2.795   -32.906 23.819  1.00 55.86  ? 77  TYR   B O    1 
ATOM   5753 C CB   . TYR   B 1 92  ? 4.093   -30.145 23.637  1.00 51.86  ? 77  TYR   B CB   1 
ATOM   5754 C CG   . TYR   B 1 92  ? 4.318   -30.191 22.146  1.00 59.34  ? 77  TYR   B CG   1 
ATOM   5755 C CD1  . TYR   B 1 92  ? 3.947   -29.126 21.335  1.00 64.48  ? 77  TYR   B CD1  1 
ATOM   5756 C CD2  . TYR   B 1 92  ? 4.910   -31.293 21.549  1.00 59.19  ? 77  TYR   B CD2  1 
ATOM   5757 C CE1  . TYR   B 1 92  ? 4.154   -29.162 19.968  1.00 60.59  ? 77  TYR   B CE1  1 
ATOM   5758 C CE2  . TYR   B 1 92  ? 5.122   -31.338 20.184  1.00 63.65  ? 77  TYR   B CE2  1 
ATOM   5759 C CZ   . TYR   B 1 92  ? 4.743   -30.270 19.398  1.00 61.22  ? 77  TYR   B CZ   1 
ATOM   5760 O OH   . TYR   B 1 92  ? 4.951   -30.308 18.037  1.00 61.99  ? 77  TYR   B OH   1 
ATOM   5761 H H    . TYR   B 1 92  ? 3.319   -30.938 25.877  1.00 64.91  ? 77  TYR   B H    1 
ATOM   5762 H HA   . TYR   B 1 92  ? 2.067   -29.838 23.751  1.00 60.49  ? 77  TYR   B HA   1 
ATOM   5763 H HB2  . TYR   B 1 92  ? 4.277   -29.240 23.934  1.00 62.23  ? 77  TYR   B HB2  1 
ATOM   5764 H HB3  . TYR   B 1 92  ? 4.718   -30.762 24.048  1.00 62.23  ? 77  TYR   B HB3  1 
ATOM   5765 H HD1  . TYR   B 1 92  ? 3.552   -28.377 21.717  1.00 77.37  ? 77  TYR   B HD1  1 
ATOM   5766 H HD2  . TYR   B 1 92  ? 5.170   -32.014 22.076  1.00 71.03  ? 77  TYR   B HD2  1 
ATOM   5767 H HE1  . TYR   B 1 92  ? 3.898   -28.443 19.437  1.00 72.70  ? 77  TYR   B HE1  1 
ATOM   5768 H HE2  . TYR   B 1 92  ? 5.519   -32.085 19.797  1.00 76.39  ? 77  TYR   B HE2  1 
ATOM   5769 H HH   . TYR   B 1 92  ? 5.326   -31.029 17.824  1.00 74.39  ? 77  TYR   B HH   1 
ATOM   5770 N N    . HIS   B 1 93  ? 1.330   -31.804 22.497  1.00 51.60  ? 78  HIS   B N    1 
ATOM   5771 C CA   . HIS   B 1 93  ? 0.804   -33.008 21.869  1.00 53.06  ? 78  HIS   B CA   1 
ATOM   5772 C C    . HIS   B 1 93  ? 1.135   -33.131 20.389  1.00 54.65  ? 78  HIS   B C    1 
ATOM   5773 O O    . HIS   B 1 93  ? 1.131   -34.249 19.867  1.00 56.29  ? 78  HIS   B O    1 
ATOM   5774 C CB   . HIS   B 1 93  ? -0.723  -33.070 22.028  1.00 52.50  ? 78  HIS   B CB   1 
ATOM   5775 C CG   . HIS   B 1 93  ? -1.178  -33.237 23.444  1.00 51.83  ? 78  HIS   B CG   1 
ATOM   5776 N ND1  . HIS   B 1 93  ? -0.405  -33.850 24.407  1.00 58.52  ? 78  HIS   B ND1  1 
ATOM   5777 C CD2  . HIS   B 1 93  ? -2.325  -32.866 24.062  1.00 53.78  ? 78  HIS   B CD2  1 
ATOM   5778 C CE1  . HIS   B 1 93  ? -1.057  -33.853 25.556  1.00 58.71  ? 78  HIS   B CE1  1 
ATOM   5779 N NE2  . HIS   B 1 93  ? -2.223  -33.260 25.374  1.00 62.51  ? 78  HIS   B NE2  1 
ATOM   5780 H H    . HIS   B 1 93  ? 0.982   -31.076 22.200  1.00 61.92  ? 78  HIS   B H    1 
ATOM   5781 H HA   . HIS   B 1 93  ? 1.186   -33.776 22.322  1.00 63.67  ? 78  HIS   B HA   1 
ATOM   5782 H HB2  . HIS   B 1 93  ? -1.106  -32.245 21.690  1.00 63.00  ? 78  HIS   B HB2  1 
ATOM   5783 H HB3  . HIS   B 1 93  ? -1.059  -33.824 21.519  1.00 63.00  ? 78  HIS   B HB3  1 
ATOM   5784 H HD2  . HIS   B 1 93  ? -3.045  -32.428 23.671  1.00 64.53  ? 78  HIS   B HD2  1 
ATOM   5785 H HE1  . HIS   B 1 93  ? -0.748  -34.211 26.356  1.00 70.45  ? 78  HIS   B HE1  1 
ATOM   5786 H HE2  . HIS   B 1 93  ? -2.822  -33.139 25.979  1.00 75.01  ? 78  HIS   B HE2  1 
ATOM   5787 N N    . GLY   B 1 94  ? 1.407   -32.030 19.705  1.00 58.73  ? 79  GLY   B N    1 
ATOM   5788 C CA   . GLY   B 1 94  ? 1.692   -32.084 18.286  1.00 58.09  ? 79  GLY   B CA   1 
ATOM   5789 C C    . GLY   B 1 94  ? 1.508   -30.732 17.642  1.00 55.20  ? 79  GLY   B C    1 
ATOM   5790 O O    . GLY   B 1 94  ? 0.954   -29.803 18.228  1.00 53.62  ? 79  GLY   B O    1 
ATOM   5791 H H    . GLY   B 1 94  ? 1.432   -31.239 20.042  1.00 70.47  ? 79  GLY   B H    1 
ATOM   5792 H HA2  . GLY   B 1 94  ? 2.609   -32.371 18.148  1.00 69.71  ? 79  GLY   B HA2  1 
ATOM   5793 H HA3  . GLY   B 1 94  ? 1.095   -32.717 17.857  1.00 69.71  ? 79  GLY   B HA3  1 
ATOM   5794 N N    . SER   B 1 95  ? 1.987   -30.639 16.405  1.00 56.58  ? 80  SER   B N    1 
ATOM   5795 C CA   . SER   B 1 95  ? 1.938   -29.398 15.645  1.00 56.94  ? 80  SER   B CA   1 
ATOM   5796 C C    . SER   B 1 95  ? 1.638   -29.706 14.187  1.00 57.98  ? 80  SER   B C    1 
ATOM   5797 O O    . SER   B 1 95  ? 1.964   -30.783 13.681  1.00 60.28  ? 80  SER   B O    1 
ATOM   5798 C CB   . SER   B 1 95  ? 3.254   -28.613 15.767  1.00 57.49  ? 80  SER   B CB   1 
ATOM   5799 O OG   . SER   B 1 95  ? 4.379   -29.458 15.607  1.00 60.38  ? 80  SER   B OG   1 
ATOM   5800 H H    . SER   B 1 95  ? 2.349   -31.292 15.978  1.00 67.90  ? 80  SER   B H    1 
ATOM   5801 H HA   . SER   B 1 95  ? 1.221   -28.838 15.981  1.00 68.33  ? 80  SER   B HA   1 
ATOM   5802 H HB2  . SER   B 1 95  ? 3.276   -27.929 15.080  1.00 68.99  ? 80  SER   B HB2  1 
ATOM   5803 H HB3  . SER   B 1 95  ? 3.294   -28.203 16.645  1.00 68.99  ? 80  SER   B HB3  1 
ATOM   5804 H HG   . SER   B 1 95  ? 4.396   -30.034 16.218  1.00 72.45  ? 80  SER   B HG   1 
ATOM   5805 N N    . TYR   B 1 96  ? 1.002   -28.747 13.517  1.00 57.67  ? 81  TYR   B N    1 
ATOM   5806 C CA   . TYR   B 1 96  ? 0.577   -28.912 12.133  1.00 59.46  ? 81  TYR   B CA   1 
ATOM   5807 C C    . TYR   B 1 96  ? 0.857   -27.634 11.358  1.00 60.23  ? 81  TYR   B C    1 
ATOM   5808 O O    . TYR   B 1 96  ? 0.469   -26.544 11.794  1.00 57.80  ? 81  TYR   B O    1 
ATOM   5809 C CB   . TYR   B 1 96  ? -0.919  -29.249 12.049  1.00 59.14  ? 81  TYR   B CB   1 
ATOM   5810 C CG   . TYR   B 1 96  ? -1.317  -30.511 12.776  1.00 59.30  ? 81  TYR   B CG   1 
ATOM   5811 C CD1  . TYR   B 1 96  ? -1.450  -30.524 14.155  1.00 57.74  ? 81  TYR   B CD1  1 
ATOM   5812 C CD2  . TYR   B 1 96  ? -1.575  -31.685 12.082  1.00 63.24  ? 81  TYR   B CD2  1 
ATOM   5813 C CE1  . TYR   B 1 96  ? -1.816  -31.666 14.825  1.00 57.98  ? 81  TYR   B CE1  1 
ATOM   5814 C CE2  . TYR   B 1 96  ? -1.946  -32.836 12.747  1.00 61.47  ? 81  TYR   B CE2  1 
ATOM   5815 C CZ   . TYR   B 1 96  ? -2.063  -32.820 14.120  1.00 63.47  ? 81  TYR   B CZ   1 
ATOM   5816 O OH   . TYR   B 1 96  ? -2.431  -33.955 14.806  1.00 65.73  ? 81  TYR   B OH   1 
ATOM   5817 H H    . TYR   B 1 96  ? 0.803   -27.980 13.850  1.00 69.21  ? 81  TYR   B H    1 
ATOM   5818 H HA   . TYR   B 1 96  ? 1.085   -29.632 11.729  1.00 71.36  ? 81  TYR   B HA   1 
ATOM   5819 H HB2  . TYR   B 1 96  ? -1.423  -28.516 12.437  1.00 70.97  ? 81  TYR   B HB2  1 
ATOM   5820 H HB3  . TYR   B 1 96  ? -1.159  -29.360 11.116  1.00 70.97  ? 81  TYR   B HB3  1 
ATOM   5821 H HD1  . TYR   B 1 96  ? -1.288  -29.745 14.636  1.00 69.28  ? 81  TYR   B HD1  1 
ATOM   5822 H HD2  . TYR   B 1 96  ? -1.498  -31.696 11.156  1.00 75.88  ? 81  TYR   B HD2  1 
ATOM   5823 H HE1  . TYR   B 1 96  ? -1.896  -31.658 15.751  1.00 69.58  ? 81  TYR   B HE1  1 
ATOM   5824 H HE2  . TYR   B 1 96  ? -2.114  -33.617 12.271  1.00 73.76  ? 81  TYR   B HE2  1 
ATOM   5825 H HH   . TYR   B 1 96  ? -2.545  -34.591 14.269  1.00 78.87  ? 81  TYR   B HH   1 
ATOM   5826 N N    . LEU   B 1 97  ? 1.525   -27.771 10.213  1.00 60.95  ? 82  LEU   B N    1 
ATOM   5827 C CA   . LEU   B 1 97  ? 1.754   -26.670 9.285   1.00 61.36  ? 82  LEU   B CA   1 
ATOM   5828 C C    . LEU   B 1 97  ? 0.899   -26.902 8.046   1.00 64.11  ? 82  LEU   B C    1 
ATOM   5829 O O    . LEU   B 1 97  ? 1.038   -27.932 7.378   1.00 65.35  ? 82  LEU   B O    1 
ATOM   5830 C CB   . LEU   B 1 97  ? 3.231   -26.557 8.907   1.00 62.48  ? 82  LEU   B CB   1 
ATOM   5831 C CG   . LEU   B 1 97  ? 3.571   -25.453 7.898   1.00 63.79  ? 82  LEU   B CG   1 
ATOM   5832 C CD1  . LEU   B 1 97  ? 3.190   -24.081 8.436   1.00 63.53  ? 82  LEU   B CD1  1 
ATOM   5833 C CD2  . LEU   B 1 97  ? 5.045   -25.492 7.534   1.00 66.01  ? 82  LEU   B CD2  1 
ATOM   5834 H H    . LEU   B 1 97  ? 1.864   -28.515 9.947   1.00 73.14  ? 82  LEU   B H    1 
ATOM   5835 H HA   . LEU   B 1 97  ? 1.488   -25.834 9.700   1.00 73.63  ? 82  LEU   B HA   1 
ATOM   5836 H HB2  . LEU   B 1 97  ? 3.739   -26.379 9.714   1.00 74.97  ? 82  LEU   B HB2  1 
ATOM   5837 H HB3  . LEU   B 1 97  ? 3.510   -27.401 8.519   1.00 74.97  ? 82  LEU   B HB3  1 
ATOM   5838 H HG   . LEU   B 1 97  ? 3.056   -25.608 7.091   1.00 76.55  ? 82  LEU   B HG   1 
ATOM   5839 H HD11 . LEU   B 1 97  ? 3.515   -23.401 7.824   1.00 76.24  ? 82  LEU   B HD11 1 
ATOM   5840 H HD12 . LEU   B 1 97  ? 2.225   -24.027 8.509   1.00 76.24  ? 82  LEU   B HD12 1 
ATOM   5841 H HD13 . LEU   B 1 97  ? 3.595   -23.961 9.309   1.00 76.24  ? 82  LEU   B HD13 1 
ATOM   5842 H HD21 . LEU   B 1 97  ? 5.231   -24.786 6.896   1.00 79.21  ? 82  LEU   B HD21 1 
ATOM   5843 H HD22 . LEU   B 1 97  ? 5.572   -25.359 8.338   1.00 79.21  ? 82  LEU   B HD22 1 
ATOM   5844 H HD23 . LEU   B 1 97  ? 5.251   -26.355 7.143   1.00 79.21  ? 82  LEU   B HD23 1 
ATOM   5845 N N    . TRP   B 1 98  ? 0.024   -25.946 7.740   1.00 62.14  ? 83  TRP   B N    1 
ATOM   5846 C CA   . TRP   B 1 98  ? -0.932  -26.118 6.654   1.00 63.38  ? 83  TRP   B CA   1 
ATOM   5847 C C    . TRP   B 1 98  ? -1.517  -24.763 6.292   1.00 64.88  ? 83  TRP   B C    1 
ATOM   5848 O O    . TRP   B 1 98  ? -1.950  -24.019 7.178   1.00 61.56  ? 83  TRP   B O    1 
ATOM   5849 C CB   . TRP   B 1 98  ? -2.039  -27.093 7.070   1.00 67.63  ? 83  TRP   B CB   1 
ATOM   5850 C CG   . TRP   B 1 98  ? -2.881  -27.585 5.938   1.00 69.75  ? 83  TRP   B CG   1 
ATOM   5851 C CD1  . TRP   B 1 98  ? -4.211  -27.356 5.745   1.00 69.01  ? 83  TRP   B CD1  1 
ATOM   5852 C CD2  . TRP   B 1 98  ? -2.449  -28.397 4.838   1.00 76.29  ? 83  TRP   B CD2  1 
ATOM   5853 N NE1  . TRP   B 1 98  ? -4.636  -27.973 4.594   1.00 76.53  ? 83  TRP   B NE1  1 
ATOM   5854 C CE2  . TRP   B 1 98  ? -3.573  -28.619 4.018   1.00 78.28  ? 83  TRP   B CE2  1 
ATOM   5855 C CE3  . TRP   B 1 98  ? -1.220  -28.957 4.468   1.00 75.31  ? 83  TRP   B CE3  1 
ATOM   5856 C CZ2  . TRP   B 1 98  ? -3.507  -29.377 2.848   1.00 82.38  ? 83  TRP   B CZ2  1 
ATOM   5857 C CZ3  . TRP   B 1 98  ? -1.156  -29.709 3.307   1.00 81.38  ? 83  TRP   B CZ3  1 
ATOM   5858 C CH2  . TRP   B 1 98  ? -2.293  -29.911 2.510   1.00 82.74  ? 83  TRP   B CH2  1 
ATOM   5859 H H    . TRP   B 1 98  ? -0.034  -25.190 8.146   1.00 74.56  ? 83  TRP   B H    1 
ATOM   5860 H HA   . TRP   B 1 98  ? -0.485  -26.468 5.869   1.00 76.06  ? 83  TRP   B HA   1 
ATOM   5861 H HB2  . TRP   B 1 98  ? -1.630  -27.866 7.489   1.00 81.16  ? 83  TRP   B HB2  1 
ATOM   5862 H HB3  . TRP   B 1 98  ? -2.626  -26.646 7.700   1.00 81.16  ? 83  TRP   B HB3  1 
ATOM   5863 H HD1  . TRP   B 1 98  ? -4.752  -26.854 6.311   1.00 82.81  ? 83  TRP   B HD1  1 
ATOM   5864 H HE1  . TRP   B 1 98  ? -5.439  -27.957 4.286   1.00 91.84  ? 83  TRP   B HE1  1 
ATOM   5865 H HE3  . TRP   B 1 98  ? -0.462  -28.826 4.991   1.00 90.38  ? 83  TRP   B HE3  1 
ATOM   5866 H HZ2  . TRP   B 1 98  ? -4.259  -29.514 2.319   1.00 98.86  ? 83  TRP   B HZ2  1 
ATOM   5867 H HZ3  . TRP   B 1 98  ? -0.345  -30.086 3.051   1.00 97.66  ? 83  TRP   B HZ3  1 
ATOM   5868 H HH2  . TRP   B 1 98  ? -2.220  -30.420 1.735   1.00 99.29  ? 83  TRP   B HH2  1 
ATOM   5869 N N    . LEU   B 1 99  ? -1.533  -24.444 4.995   1.00 68.37  ? 84  LEU   B N    1 
ATOM   5870 C CA   . LEU   B 1 99  ? -2.119  -23.192 4.514   1.00 68.55  ? 84  LEU   B CA   1 
ATOM   5871 C C    . LEU   B 1 99  ? -1.470  -21.988 5.194   1.00 70.62  ? 84  LEU   B C    1 
ATOM   5872 O O    . LEU   B 1 99  ? -2.137  -21.007 5.532   1.00 68.49  ? 84  LEU   B O    1 
ATOM   5873 C CB   . LEU   B 1 99  ? -3.636  -23.181 4.727   1.00 72.67  ? 84  LEU   B CB   1 
ATOM   5874 C CG   . LEU   B 1 99  ? -4.520  -23.769 3.622   1.00 81.07  ? 84  LEU   B CG   1 
ATOM   5875 C CD1  . LEU   B 1 99  ? -3.995  -25.103 3.128   1.00 75.51  ? 84  LEU   B CD1  1 
ATOM   5876 C CD2  . LEU   B 1 99  ? -5.958  -23.906 4.120   1.00 75.44  ? 84  LEU   B CD2  1 
ATOM   5877 H H    . LEU   B 1 99  ? -1.209  -24.940 4.372   1.00 82.05  ? 84  LEU   B H    1 
ATOM   5878 H HA   . LEU   B 1 99  ? -1.948  -23.118 3.562   1.00 82.26  ? 84  LEU   B HA   1 
ATOM   5879 H HB2  . LEU   B 1 99  ? -3.824  -23.687 5.533   1.00 87.20  ? 84  LEU   B HB2  1 
ATOM   5880 H HB3  . LEU   B 1 99  ? -3.911  -22.258 4.842   1.00 87.20  ? 84  LEU   B HB3  1 
ATOM   5881 H HG   . LEU   B 1 99  ? -4.507  -23.164 2.864   1.00 97.29  ? 84  LEU   B HG   1 
ATOM   5882 H HD11 . LEU   B 1 99  ? -4.739  -25.635 2.804   1.00 90.61  ? 84  LEU   B HD11 1 
ATOM   5883 H HD12 . LEU   B 1 99  ? -3.363  -24.947 2.409   1.00 90.61  ? 84  LEU   B HD12 1 
ATOM   5884 H HD13 . LEU   B 1 99  ? -3.555  -25.560 3.861   1.00 90.61  ? 84  LEU   B HD13 1 
ATOM   5885 H HD21 . LEU   B 1 99  ? -6.511  -24.244 3.399   1.00 90.53  ? 84  LEU   B HD21 1 
ATOM   5886 H HD22 . LEU   B 1 99  ? -5.975  -24.525 4.867   1.00 90.53  ? 84  LEU   B HD22 1 
ATOM   5887 H HD23 . LEU   B 1 99  ? -6.278  -23.036 4.404   1.00 90.53  ? 84  LEU   B HD23 1 
ATOM   5888 N N    . GLN   B 1 100 ? -0.155  -22.064 5.403   1.00 72.84  ? 85  GLN   B N    1 
ATOM   5889 C CA   . GLN   B 1 100 ? 0.595   -21.015 6.095   1.00 67.40  ? 85  GLN   B CA   1 
ATOM   5890 C C    . GLN   B 1 100 ? 0.032   -20.741 7.488   1.00 67.65  ? 85  GLN   B C    1 
ATOM   5891 O O    . GLN   B 1 100 ? 0.138   -19.627 8.008   1.00 66.76  ? 85  GLN   B O    1 
ATOM   5892 C CB   . GLN   B 1 100 ? 0.632   -19.725 5.268   1.00 75.37  ? 85  GLN   B CB   1 
ATOM   5893 C CG   . GLN   B 1 100 ? 1.592   -19.778 4.090   1.00 69.27  ? 85  GLN   B CG   1 
ATOM   5894 C CD   . GLN   B 1 100 ? 1.306   -18.708 3.051   1.00 78.13  ? 85  GLN   B CD   1 
ATOM   5895 O OE1  . GLN   B 1 100 ? 0.350   -17.946 3.178   1.00 75.58  ? 85  GLN   B OE1  1 
ATOM   5896 N NE2  . GLN   B 1 100 ? 2.132   -18.654 2.012   1.00 73.34  ? 85  GLN   B NE2  1 
ATOM   5897 H H    . GLN   B 1 100 ? 0.334   -22.724 5.148   1.00 87.41  ? 85  GLN   B H    1 
ATOM   5898 H HA   . GLN   B 1 100 ? 1.508   -21.322 6.210   1.00 80.88  ? 85  GLN   B HA   1 
ATOM   5899 H HB2  . GLN   B 1 100 ? -0.257  -19.553 4.918   1.00 90.44  ? 85  GLN   B HB2  1 
ATOM   5900 H HB3  . GLN   B 1 100 ? 0.908   -18.994 5.843   1.00 90.44  ? 85  GLN   B HB3  1 
ATOM   5901 H HG2  . GLN   B 1 100 ? 2.497   -19.647 4.413   1.00 83.12  ? 85  GLN   B HG2  1 
ATOM   5902 H HG3  . GLN   B 1 100 ? 1.516   -20.643 3.658   1.00 83.12  ? 85  GLN   B HG3  1 
ATOM   5903 H HE21 . GLN   B 1 100 ? 2.787   -19.208 1.954   1.00 88.01  ? 85  GLN   B HE21 1 
ATOM   5904 H HE22 . GLN   B 1 100 ? 2.010   -18.065 1.397   1.00 88.01  ? 85  GLN   B HE22 1 
ATOM   5905 N N    . LYS   B 1 101 ? -0.564  -21.753 8.110   1.00 60.35  ? 86  LYS   B N    1 
ATOM   5906 C CA   . LYS   B 1 101 ? -1.063  -21.653 9.475   1.00 57.40  ? 86  LYS   B CA   1 
ATOM   5907 C C    . LYS   B 1 101 ? -0.385  -22.718 10.324  1.00 56.46  ? 86  LYS   B C    1 
ATOM   5908 O O    . LYS   B 1 101 ? -0.362  -23.896 9.951   1.00 57.14  ? 86  LYS   B O    1 
ATOM   5909 C CB   . LYS   B 1 101 ? -2.586  -21.816 9.531   1.00 59.70  ? 86  LYS   B CB   1 
ATOM   5910 C CG   . LYS   B 1 101 ? -3.366  -20.581 9.108   1.00 60.57  ? 86  LYS   B CG   1 
ATOM   5911 C CD   . LYS   B 1 101 ? -4.871  -20.818 9.179   1.00 63.27  ? 86  LYS   B CD   1 
ATOM   5912 C CE   . LYS   B 1 101 ? -5.451  -21.227 7.830   1.00 75.53  ? 86  LYS   B CE   1 
ATOM   5913 N NZ   . LYS   B 1 101 ? -5.360  -20.132 6.819   1.00 86.71  ? 86  LYS   B NZ   1 
ATOM   5914 H H    . LYS   B 1 101 ? -0.692  -22.525 7.753   1.00 72.42  ? 86  LYS   B H    1 
ATOM   5915 H HA   . LYS   B 1 101 ? -0.846  -20.780 9.837   1.00 68.88  ? 86  LYS   B HA   1 
ATOM   5916 H HB2  . LYS   B 1 101 ? -2.841  -22.541 8.940   1.00 71.64  ? 86  LYS   B HB2  1 
ATOM   5917 H HB3  . LYS   B 1 101 ? -2.841  -22.026 10.443  1.00 71.64  ? 86  LYS   B HB3  1 
ATOM   5918 H HG2  . LYS   B 1 101 ? -3.145  -19.843 9.699   1.00 72.68  ? 86  LYS   B HG2  1 
ATOM   5919 H HG3  . LYS   B 1 101 ? -3.136  -20.353 8.193   1.00 72.68  ? 86  LYS   B HG3  1 
ATOM   5920 H HD2  . LYS   B 1 101 ? -5.052  -21.529 9.814   1.00 75.93  ? 86  LYS   B HD2  1 
ATOM   5921 H HD3  . LYS   B 1 101 ? -5.310  -20.001 9.462   1.00 75.93  ? 86  LYS   B HD3  1 
ATOM   5922 H HE2  . LYS   B 1 101 ? -4.960  -21.992 7.492   1.00 90.64  ? 86  LYS   B HE2  1 
ATOM   5923 H HE3  . LYS   B 1 101 ? -6.386  -21.457 7.943   1.00 90.64  ? 86  LYS   B HE3  1 
ATOM   5924 H HZ1  . LYS   B 1 101 ? -5.764  -20.380 6.066   1.00 104.05 ? 86  LYS   B HZ1  1 
ATOM   5925 H HZ2  . LYS   B 1 101 ? -5.754  -19.397 7.130   1.00 104.05 ? 86  LYS   B HZ2  1 
ATOM   5926 H HZ3  . LYS   B 1 101 ? -4.507  -19.950 6.643   1.00 104.05 ? 86  LYS   B HZ3  1 
ATOM   5927 N N    . LEU   B 1 102 ? 0.178   -22.299 11.450  1.00 53.21  ? 87  LEU   B N    1 
ATOM   5928 C CA   . LEU   B 1 102 ? 0.807   -23.209 12.394  1.00 52.22  ? 87  LEU   B CA   1 
ATOM   5929 C C    . LEU   B 1 102 ? -0.170  -23.474 13.528  1.00 50.00  ? 87  LEU   B C    1 
ATOM   5930 O O    . LEU   B 1 102 ? -0.649  -22.535 14.172  1.00 51.82  ? 87  LEU   B O    1 
ATOM   5931 C CB   . LEU   B 1 102 ? 2.113   -22.638 12.939  1.00 54.33  ? 87  LEU   B CB   1 
ATOM   5932 C CG   . LEU   B 1 102 ? 2.879   -23.598 13.853  1.00 53.87  ? 87  LEU   B CG   1 
ATOM   5933 C CD1  . LEU   B 1 102 ? 3.418   -24.781 13.056  1.00 56.16  ? 87  LEU   B CD1  1 
ATOM   5934 C CD2  . LEU   B 1 102 ? 4.003   -22.883 14.585  1.00 51.75  ? 87  LEU   B CD2  1 
ATOM   5935 H H    . LEU   B 1 102 ? 0.208   -21.475 11.693  1.00 63.85  ? 87  LEU   B H    1 
ATOM   5936 H HA   . LEU   B 1 102 ? 1.013   -24.045 11.946  1.00 62.67  ? 87  LEU   B HA   1 
ATOM   5937 H HB2  . LEU   B 1 102 ? 2.691   -22.417 12.192  1.00 65.19  ? 87  LEU   B HB2  1 
ATOM   5938 H HB3  . LEU   B 1 102 ? 1.912   -21.839 13.451  1.00 65.19  ? 87  LEU   B HB3  1 
ATOM   5939 H HG   . LEU   B 1 102 ? 2.268   -23.940 14.524  1.00 64.65  ? 87  LEU   B HG   1 
ATOM   5940 H HD11 . LEU   B 1 102 ? 4.014   -25.297 13.621  1.00 67.39  ? 87  LEU   B HD11 1 
ATOM   5941 H HD12 . LEU   B 1 102 ? 2.674   -25.333 12.769  1.00 67.39  ? 87  LEU   B HD12 1 
ATOM   5942 H HD13 . LEU   B 1 102 ? 3.900   -24.447 12.283  1.00 67.39  ? 87  LEU   B HD13 1 
ATOM   5943 H HD21 . LEU   B 1 102 ? 4.465   -23.520 15.153  1.00 62.10  ? 87  LEU   B HD21 1 
ATOM   5944 H HD22 . LEU   B 1 102 ? 4.619   -22.513 13.934  1.00 62.10  ? 87  LEU   B HD22 1 
ATOM   5945 H HD23 . LEU   B 1 102 ? 3.625   -22.171 15.125  1.00 62.10  ? 87  LEU   B HD23 1 
ATOM   5946 N N    . TRP   B 1 103 ? -0.466  -24.747 13.759  1.00 51.86  ? 88  TRP   B N    1 
ATOM   5947 C CA   . TRP   B 1 103 ? -1.308  -25.182 14.860  1.00 48.73  ? 88  TRP   B CA   1 
ATOM   5948 C C    . TRP   B 1 103 ? -0.439  -25.904 15.876  1.00 49.22  ? 88  TRP   B C    1 
ATOM   5949 O O    . TRP   B 1 103 ? 0.361   -26.770 15.505  1.00 52.01  ? 88  TRP   B O    1 
ATOM   5950 C CB   . TRP   B 1 103 ? -2.415  -26.116 14.375  1.00 51.91  ? 88  TRP   B CB   1 
ATOM   5951 C CG   . TRP   B 1 103 ? -3.316  -25.517 13.357  1.00 51.59  ? 88  TRP   B CG   1 
ATOM   5952 C CD1  . TRP   B 1 103 ? -3.035  -25.301 12.042  1.00 54.28  ? 88  TRP   B CD1  1 
ATOM   5953 C CD2  . TRP   B 1 103 ? -4.660  -25.076 13.559  1.00 51.07  ? 88  TRP   B CD2  1 
ATOM   5954 N NE1  . TRP   B 1 103 ? -4.121  -24.745 11.413  1.00 58.67  ? 88  TRP   B NE1  1 
ATOM   5955 C CE2  . TRP   B 1 103 ? -5.133  -24.597 12.324  1.00 53.05  ? 88  TRP   B CE2  1 
ATOM   5956 C CE3  . TRP   B 1 103 ? -5.509  -25.036 14.667  1.00 55.05  ? 88  TRP   B CE3  1 
ATOM   5957 C CZ2  . TRP   B 1 103 ? -6.414  -24.080 12.164  1.00 59.58  ? 88  TRP   B CZ2  1 
ATOM   5958 C CZ3  . TRP   B 1 103 ? -6.782  -24.523 14.507  1.00 61.08  ? 88  TRP   B CZ3  1 
ATOM   5959 C CH2  . TRP   B 1 103 ? -7.222  -24.053 13.264  1.00 51.69  ? 88  TRP   B CH2  1 
ATOM   5960 H H    . TRP   B 1 103 ? -0.180  -25.396 13.274  1.00 62.23  ? 88  TRP   B H    1 
ATOM   5961 H HA   . TRP   B 1 103 ? -1.723  -24.412 15.279  1.00 58.48  ? 88  TRP   B HA   1 
ATOM   5962 H HB2  . TRP   B 1 103 ? -2.007  -26.902 13.980  1.00 62.29  ? 88  TRP   B HB2  1 
ATOM   5963 H HB3  . TRP   B 1 103 ? -2.961  -26.372 15.135  1.00 62.29  ? 88  TRP   B HB3  1 
ATOM   5964 H HD1  . TRP   B 1 103 ? -2.226  -25.501 11.630  1.00 65.13  ? 88  TRP   B HD1  1 
ATOM   5965 H HE1  . TRP   B 1 103 ? -4.159  -24.525 10.583  1.00 70.41  ? 88  TRP   B HE1  1 
ATOM   5966 H HE3  . TRP   B 1 103 ? -5.224  -25.347 15.496  1.00 66.06  ? 88  TRP   B HE3  1 
ATOM   5967 H HZ2  . TRP   B 1 103 ? -6.708  -23.764 11.340  1.00 71.49  ? 88  TRP   B HZ2  1 
ATOM   5968 H HZ3  . TRP   B 1 103 ? -7.357  -24.491 15.237  1.00 73.30  ? 88  TRP   B HZ3  1 
ATOM   5969 H HH2  . TRP   B 1 103 ? -8.085  -23.714 13.186  1.00 62.03  ? 88  TRP   B HH2  1 
ATOM   5970 N N    . ILE   B 1 104 ? -0.589  -25.540 17.145  1.00 45.36  ? 89  ILE   B N    1 
ATOM   5971 C CA   . ILE   B 1 104 ? 0.054   -26.231 18.255  1.00 49.31  ? 89  ILE   B CA   1 
ATOM   5972 C C    . ILE   B 1 104 ? -1.046  -26.864 19.095  1.00 47.02  ? 89  ILE   B C    1 
ATOM   5973 O O    . ILE   B 1 104 ? -1.941  -26.164 19.588  1.00 42.28  ? 89  ILE   B O    1 
ATOM   5974 C CB   . ILE   B 1 104 ? 0.920   -25.286 19.102  1.00 47.92  ? 89  ILE   B CB   1 
ATOM   5975 C CG1  . ILE   B 1 104 ? 2.019   -24.649 18.247  1.00 43.58  ? 89  ILE   B CG1  1 
ATOM   5976 C CG2  . ILE   B 1 104 ? 1.542   -26.046 20.266  1.00 41.74  ? 89  ILE   B CG2  1 
ATOM   5977 C CD1  . ILE   B 1 104 ? 1.857   -23.160 18.059  1.00 44.64  ? 89  ILE   B CD1  1 
ATOM   5978 H H    . ILE   B 1 104 ? -1.073  -24.874 17.395  1.00 54.43  ? 89  ILE   B H    1 
ATOM   5979 H HA   . ILE   B 1 104 ? 0.629   -26.931 17.908  1.00 59.18  ? 89  ILE   B HA   1 
ATOM   5980 H HB   . ILE   B 1 104 ? 0.350   -24.583 19.449  1.00 57.50  ? 89  ILE   B HB   1 
ATOM   5981 H HG12 . ILE   B 1 104 ? 2.875   -24.802 18.676  1.00 52.29  ? 89  ILE   B HG12 1 
ATOM   5982 H HG13 . ILE   B 1 104 ? 2.009   -25.061 17.369  1.00 52.29  ? 89  ILE   B HG13 1 
ATOM   5983 H HG21 . ILE   B 1 104 ? 2.194   -25.476 20.703  1.00 50.09  ? 89  ILE   B HG21 1 
ATOM   5984 H HG22 . ILE   B 1 104 ? 0.844   -26.290 20.893  1.00 50.09  ? 89  ILE   B HG22 1 
ATOM   5985 H HG23 . ILE   B 1 104 ? 1.976   -26.844 19.926  1.00 50.09  ? 89  ILE   B HG23 1 
ATOM   5986 H HD11 . ILE   B 1 104 ? 2.584   -22.830 17.508  1.00 53.57  ? 89  ILE   B HD11 1 
ATOM   5987 H HD12 . ILE   B 1 104 ? 1.008   -22.987 17.624  1.00 53.57  ? 89  ILE   B HD12 1 
ATOM   5988 H HD13 . ILE   B 1 104 ? 1.878   -22.728 18.927  1.00 53.57  ? 89  ILE   B HD13 1 
ATOM   5989 N N    . CYS   B 1 105 ? -0.982  -28.182 19.251  1.00 49.22  ? 90  CYS   B N    1 
ATOM   5990 C CA   . CYS   B 1 105 ? -1.945  -28.922 20.051  1.00 43.92  ? 90  CYS   B CA   1 
ATOM   5991 C C    . CYS   B 1 105 ? -1.400  -29.076 21.464  1.00 51.13  ? 90  CYS   B C    1 
ATOM   5992 O O    . CYS   B 1 105 ? -0.266  -29.530 21.651  1.00 50.25  ? 90  CYS   B O    1 
ATOM   5993 C CB   . CYS   B 1 105 ? -2.218  -30.290 19.428  1.00 49.29  ? 90  CYS   B CB   1 
ATOM   5994 S SG   . CYS   B 1 105 ? -3.477  -31.258 20.279  1.00 56.23  ? 90  CYS   B SG   1 
ATOM   5995 H H    . CYS   B 1 105 ? -0.377  -28.678 18.895  1.00 59.07  ? 90  CYS   B H    1 
ATOM   5996 H HA   . CYS   B 1 105 ? -2.787  -28.441 20.094  1.00 52.70  ? 90  CYS   B HA   1 
ATOM   5997 H HB2  . CYS   B 1 105 ? -2.516  -30.160 18.514  1.00 59.15  ? 90  CYS   B HB2  1 
ATOM   5998 H HB3  . CYS   B 1 105 ? -1.396  -30.804 19.438  1.00 59.15  ? 90  CYS   B HB3  1 
ATOM   5999 H HG   . CYS   B 1 105 ? -3.442  -32.387 19.873  1.00 67.48  ? 90  CYS   B HG   1 
ATOM   6000 N N    . MET   B 1 106 ? -2.213  -28.702 22.453  1.00 40.86  ? 91  MET   B N    1 
ATOM   6001 C CA   . MET   B 1 106 ? -1.765  -28.624 23.830  1.00 39.04  ? 91  MET   B CA   1 
ATOM   6002 C C    . MET   B 1 106 ? -2.796  -29.240 24.761  1.00 40.07  ? 91  MET   B C    1 
ATOM   6003 O O    . MET   B 1 106 ? -3.951  -29.472 24.393  1.00 39.41  ? 91  MET   B O    1 
ATOM   6004 C CB   . MET   B 1 106 ? -1.527  -27.175 24.268  1.00 44.06  ? 91  MET   B CB   1 
ATOM   6005 C CG   . MET   B 1 106 ? -0.619  -26.375 23.371  1.00 51.86  ? 91  MET   B CG   1 
ATOM   6006 S SD   . MET   B 1 106 ? -0.745  -24.636 23.803  1.00 42.99  ? 91  MET   B SD   1 
ATOM   6007 C CE   . MET   B 1 106 ? -2.359  -24.239 23.130  1.00 39.63  ? 91  MET   B CE   1 
ATOM   6008 H H    . MET   B 1 106 ? -3.038  -28.487 22.343  1.00 49.03  ? 91  MET   B H    1 
ATOM   6009 H HA   . MET   B 1 106 ? -0.937  -29.126 23.887  1.00 46.85  ? 91  MET   B HA   1 
ATOM   6010 H HB2  . MET   B 1 106 ? -2.383  -26.719 24.295  1.00 52.88  ? 91  MET   B HB2  1 
ATOM   6011 H HB3  . MET   B 1 106 ? -1.128  -27.184 25.152  1.00 52.88  ? 91  MET   B HB3  1 
ATOM   6012 H HG2  . MET   B 1 106 ? 0.300   -26.664 23.491  1.00 62.24  ? 91  MET   B HG2  1 
ATOM   6013 H HG3  . MET   B 1 106 ? -0.885  -26.490 22.446  1.00 62.24  ? 91  MET   B HG3  1 
ATOM   6014 H HE1  . MET   B 1 106 ? -2.487  -23.278 23.163  1.00 47.55  ? 91  MET   B HE1  1 
ATOM   6015 H HE2  . MET   B 1 106 ? -2.403  -24.547 22.212  1.00 47.55  ? 91  MET   B HE2  1 
ATOM   6016 H HE3  . MET   B 1 106 ? -3.040  -24.681 23.661  1.00 47.55  ? 91  MET   B HE3  1 
ATOM   6017 N N    . GLU   B 1 107 ? -2.339  -29.486 25.989  1.00 43.57  ? 92  GLU   B N    1 
ATOM   6018 C CA   . GLU   B 1 107 ? -3.203  -29.875 27.095  1.00 44.76  ? 92  GLU   B CA   1 
ATOM   6019 C C    . GLU   B 1 107 ? -4.311  -28.854 27.298  1.00 44.81  ? 92  GLU   B C    1 
ATOM   6020 O O    . GLU   B 1 107 ? -4.060  -27.646 27.329  1.00 41.63  ? 92  GLU   B O    1 
ATOM   6021 C CB   . GLU   B 1 107 ? -2.351  -29.998 28.362  1.00 45.97  ? 92  GLU   B CB   1 
ATOM   6022 C CG   . GLU   B 1 107 ? -3.094  -30.141 29.668  1.00 42.49  ? 92  GLU   B CG   1 
ATOM   6023 C CD   . GLU   B 1 107 ? -2.137  -30.169 30.861  1.00 53.55  ? 92  GLU   B CD   1 
ATOM   6024 O OE1  . GLU   B 1 107 ? -0.909  -30.045 30.643  1.00 39.19  ? 92  GLU   B OE1  1 
ATOM   6025 O OE2  . GLU   B 1 107 ? -2.605  -30.302 32.013  1.00 53.47  ? 92  GLU   B OE2  1 
ATOM   6026 H H    . GLU   B 1 107 ? -1.510  -29.433 26.211  1.00 52.28  ? 92  GLU   B H    1 
ATOM   6027 H HA   . GLU   B 1 107 ? -3.623  -30.729 26.906  1.00 53.71  ? 92  GLU   B HA   1 
ATOM   6028 H HB2  . GLU   B 1 107 ? -1.788  -30.782 28.269  1.00 55.16  ? 92  GLU   B HB2  1 
ATOM   6029 H HB3  . GLU   B 1 107 ? -1.803  -29.201 28.433  1.00 55.16  ? 92  GLU   B HB3  1 
ATOM   6030 H HG2  . GLU   B 1 107 ? -3.696  -29.388 29.779  1.00 50.99  ? 92  GLU   B HG2  1 
ATOM   6031 H HG3  . GLU   B 1 107 ? -3.597  -30.970 29.662  1.00 50.99  ? 92  GLU   B HG3  1 
ATOM   6032 N N    . PHE   B 1 108 ? -5.538  -29.345 27.455  1.00 36.90  ? 93  PHE   B N    1 
ATOM   6033 C CA   . PHE   B 1 108 ? -6.690  -28.478 27.650  1.00 36.46  ? 93  PHE   B CA   1 
ATOM   6034 C C    . PHE   B 1 108 ? -6.917  -28.228 29.135  1.00 43.91  ? 93  PHE   B C    1 
ATOM   6035 O O    . PHE   B 1 108 ? -6.966  -29.170 29.936  1.00 38.18  ? 93  PHE   B O    1 
ATOM   6036 C CB   . PHE   B 1 108 ? -7.945  -29.083 27.020  1.00 38.04  ? 93  PHE   B CB   1 
ATOM   6037 C CG   . PHE   B 1 108 ? -9.197  -28.274 27.266  1.00 43.23  ? 93  PHE   B CG   1 
ATOM   6038 C CD1  . PHE   B 1 108 ? -9.399  -27.062 26.620  1.00 42.61  ? 93  PHE   B CD1  1 
ATOM   6039 C CD2  . PHE   B 1 108 ? -10.171 -28.727 28.144  1.00 41.72  ? 93  PHE   B CD2  1 
ATOM   6040 C CE1  . PHE   B 1 108 ? -10.552 -26.316 26.852  1.00 47.28  ? 93  PHE   B CE1  1 
ATOM   6041 C CE2  . PHE   B 1 108 ? -11.319 -27.994 28.374  1.00 39.39  ? 93  PHE   B CE2  1 
ATOM   6042 C CZ   . PHE   B 1 108 ? -11.513 -26.787 27.731  1.00 46.11  ? 93  PHE   B CZ   1 
ATOM   6043 H H    . PHE   B 1 108 ? -5.728  -30.183 27.452  1.00 44.28  ? 93  PHE   B H    1 
ATOM   6044 H HA   . PHE   B 1 108 ? -6.517  -27.625 27.221  1.00 43.75  ? 93  PHE   B HA   1 
ATOM   6045 H HB2  . PHE   B 1 108 ? -7.814  -29.143 26.060  1.00 45.65  ? 93  PHE   B HB2  1 
ATOM   6046 H HB3  . PHE   B 1 108 ? -8.086  -29.967 27.392  1.00 45.65  ? 93  PHE   B HB3  1 
ATOM   6047 H HD1  . PHE   B 1 108 ? -8.757  -26.745 26.027  1.00 51.13  ? 93  PHE   B HD1  1 
ATOM   6048 H HD2  . PHE   B 1 108 ? -10.048 -29.536 28.586  1.00 50.06  ? 93  PHE   B HD2  1 
ATOM   6049 H HE1  . PHE   B 1 108 ? -10.677 -25.503 26.417  1.00 56.74  ? 93  PHE   B HE1  1 
ATOM   6050 H HE2  . PHE   B 1 108 ? -11.964 -28.315 28.962  1.00 47.27  ? 93  PHE   B HE2  1 
ATOM   6051 H HZ   . PHE   B 1 108 ? -12.285 -26.293 27.889  1.00 55.34  ? 93  PHE   B HZ   1 
ATOM   6052 N N    . CYS   B 1 109 ? -7.063  -26.956 29.492  1.00 38.93  ? 94  CYS   B N    1 
ATOM   6053 C CA   . CYS   B 1 109 ? -7.273  -26.519 30.870  1.00 43.47  ? 94  CYS   B CA   1 
ATOM   6054 C C    . CYS   B 1 109 ? -8.672  -25.920 30.956  1.00 38.21  ? 94  CYS   B C    1 
ATOM   6055 O O    . CYS   B 1 109 ? -8.918  -24.818 30.454  1.00 37.57  ? 94  CYS   B O    1 
ATOM   6056 C CB   . CYS   B 1 109 ? -6.195  -25.522 31.279  1.00 35.75  ? 94  CYS   B CB   1 
ATOM   6057 S SG   . CYS   B 1 109 ? -4.526  -26.246 31.288  1.00 43.65  ? 94  CYS   B SG   1 
ATOM   6058 H H    . CYS   B 1 109 ? -7.044  -26.303 28.933  1.00 46.72  ? 94  CYS   B H    1 
ATOM   6059 H HA   . CYS   B 1 109 ? -7.230  -27.273 31.479  1.00 52.16  ? 94  CYS   B HA   1 
ATOM   6060 H HB2  . CYS   B 1 109 ? -6.196  -24.782 30.653  1.00 42.90  ? 94  CYS   B HB2  1 
ATOM   6061 H HB3  . CYS   B 1 109 ? -6.386  -25.200 32.174  1.00 42.90  ? 94  CYS   B HB3  1 
ATOM   6062 H HG   . CYS   B 1 109 ? -3.736  -25.403 31.611  1.00 52.38  ? 94  CYS   B HG   1 
ATOM   6063 N N    . GLY   B 1 110 ? -9.587  -26.654 31.587  1.00 34.48  ? 95  GLY   B N    1 
ATOM   6064 C CA   . GLY   B 1 110 ? -11.001 -26.349 31.472  1.00 41.55  ? 95  GLY   B CA   1 
ATOM   6065 C C    . GLY   B 1 110 ? -11.449 -25.103 32.208  1.00 39.70  ? 95  GLY   B C    1 
ATOM   6066 O O    . GLY   B 1 110 ? -12.489 -24.536 31.859  1.00 46.91  ? 95  GLY   B O    1 
ATOM   6067 H H    . GLY   B 1 110 ? -9.411  -27.332 32.085  1.00 41.38  ? 95  GLY   B H    1 
ATOM   6068 H HA2  . GLY   B 1 110 ? -11.219 -26.232 30.534  1.00 49.86  ? 95  GLY   B HA2  1 
ATOM   6069 H HA3  . GLY   B 1 110 ? -11.510 -27.097 31.824  1.00 49.86  ? 95  GLY   B HA3  1 
ATOM   6070 N N    . ALA   B 1 111 ? -10.707 -24.666 33.217  1.00 35.06  ? 96  ALA   B N    1 
ATOM   6071 C CA   . ALA   B 1 111 ? -11.114 -23.504 33.991  1.00 39.87  ? 96  ALA   B CA   1 
ATOM   6072 C C    . ALA   B 1 111 ? -10.554 -22.193 33.450  1.00 38.97  ? 96  ALA   B C    1 
ATOM   6073 O O    . ALA   B 1 111 ? -10.878 -21.133 33.993  1.00 33.81  ? 96  ALA   B O    1 
ATOM   6074 C CB   . ALA   B 1 111 ? -10.700 -23.667 35.456  1.00 38.50  ? 96  ALA   B CB   1 
ATOM   6075 H H    . ALA   B 1 111 ? -9.967  -25.025 33.471  1.00 42.07  ? 96  ALA   B H    1 
ATOM   6076 H HA   . ALA   B 1 111 ? -12.082 -23.446 33.960  1.00 47.85  ? 96  ALA   B HA   1 
ATOM   6077 H HB1  . ALA   B 1 111 ? -10.985 -22.885 35.954  1.00 46.20  ? 96  ALA   B HB1  1 
ATOM   6078 H HB2  . ALA   B 1 111 ? -11.123 -24.462 35.817  1.00 46.20  ? 96  ALA   B HB2  1 
ATOM   6079 H HB3  . ALA   B 1 111 ? -9.735  -23.756 35.503  1.00 46.20  ? 96  ALA   B HB3  1 
ATOM   6080 N N    . GLY   B 1 112 ? -9.743  -22.228 32.393  1.00 38.39  ? 97  GLY   B N    1 
ATOM   6081 C CA   . GLY   B 1 112 ? -9.180  -21.004 31.852  1.00 34.60  ? 97  GLY   B CA   1 
ATOM   6082 C C    . GLY   B 1 112 ? -8.003  -20.480 32.652  1.00 33.40  ? 97  GLY   B C    1 
ATOM   6083 O O    . GLY   B 1 112 ? -7.181  -21.260 33.142  1.00 33.37  ? 97  GLY   B O    1 
ATOM   6084 H H    . GLY   B 1 112 ? -9.509  -22.944 31.978  1.00 46.07  ? 97  GLY   B H    1 
ATOM   6085 H HA2  . GLY   B 1 112 ? -8.880  -21.167 30.944  1.00 41.52  ? 97  GLY   B HA2  1 
ATOM   6086 H HA3  . GLY   B 1 112 ? -9.866  -20.318 31.839  1.00 41.52  ? 97  GLY   B HA3  1 
ATOM   6087 N N    . SER   B 1 113 ? -7.907  -19.161 32.779  1.00 35.59  ? 98  SER   B N    1 
ATOM   6088 C CA   . SER   B 1 113 ? -6.849  -18.509 33.535  1.00 29.73  ? 98  SER   B CA   1 
ATOM   6089 C C    . SER   B 1 113 ? -7.362  -18.079 34.907  1.00 30.36  ? 98  SER   B C    1 
ATOM   6090 O O    . SER   B 1 113 ? -8.566  -18.025 35.161  1.00 30.06  ? 98  SER   B O    1 
ATOM   6091 C CB   . SER   B 1 113 ? -6.313  -17.290 32.777  1.00 38.06  ? 98  SER   B CB   1 
ATOM   6092 O OG   . SER   B 1 113 ? -7.289  -16.263 32.718  1.00 31.62  ? 98  SER   B OG   1 
ATOM   6093 H H    . SER   B 1 113 ? -8.461  -18.607 32.425  1.00 42.71  ? 98  SER   B H    1 
ATOM   6094 H HA   . SER   B 1 113 ? -6.117  -19.132 33.662  1.00 35.68  ? 98  SER   B HA   1 
ATOM   6095 H HB2  . SER   B 1 113 ? -5.528  -16.953 33.236  1.00 45.67  ? 98  SER   B HB2  1 
ATOM   6096 H HB3  . SER   B 1 113 ? -6.080  -17.556 31.874  1.00 45.67  ? 98  SER   B HB3  1 
ATOM   6097 H HG   . SER   B 1 113 ? -6.984  -15.599 32.304  1.00 37.95  ? 98  SER   B HG   1 
ATOM   6098 N N    . LEU   B 1 114 ? -6.418  -17.783 35.800  1.00 28.51  ? 99  LEU   B N    1 
ATOM   6099 C CA   . LEU   B 1 114 ? -6.787  -17.253 37.107  1.00 28.69  ? 99  LEU   B CA   1 
ATOM   6100 C C    . LEU   B 1 114 ? -7.484  -15.906 36.985  1.00 29.56  ? 99  LEU   B C    1 
ATOM   6101 O O    . LEU   B 1 114 ? -8.328  -15.565 37.819  1.00 34.61  ? 99  LEU   B O    1 
ATOM   6102 C CB   . LEU   B 1 114 ? -5.550  -17.126 37.988  1.00 27.96  ? 99  LEU   B CB   1 
ATOM   6103 C CG   . LEU   B 1 114 ? -5.135  -18.415 38.690  1.00 28.94  ? 99  LEU   B CG   1 
ATOM   6104 C CD1  . LEU   B 1 114 ? -3.778  -18.246 39.363  1.00 35.76  ? 99  LEU   B CD1  1 
ATOM   6105 C CD2  . LEU   B 1 114 ? -6.191  -18.801 39.709  1.00 28.56  ? 99  LEU   B CD2  1 
ATOM   6106 H H    . LEU   B 1 114 ? -5.572  -17.878 35.676  1.00 34.21  ? 99  LEU   B H    1 
ATOM   6107 H HA   . LEU   B 1 114 ? -7.400  -17.873 37.534  1.00 34.43  ? 99  LEU   B HA   1 
ATOM   6108 H HB2  . LEU   B 1 114 ? -4.806  -16.841 37.434  1.00 33.56  ? 99  LEU   B HB2  1 
ATOM   6109 H HB3  . LEU   B 1 114 ? -5.727  -16.462 38.673  1.00 33.56  ? 99  LEU   B HB3  1 
ATOM   6110 H HG   . LEU   B 1 114 ? -5.054  -19.128 38.038  1.00 34.73  ? 99  LEU   B HG   1 
ATOM   6111 H HD11 . LEU   B 1 114 ? -3.529  -19.083 39.786  1.00 42.92  ? 99  LEU   B HD11 1 
ATOM   6112 H HD12 . LEU   B 1 114 ? -3.120  -18.006 38.692  1.00 42.92  ? 99  LEU   B HD12 1 
ATOM   6113 H HD13 . LEU   B 1 114 ? -3.841  -17.545 40.030  1.00 42.92  ? 99  LEU   B HD13 1 
ATOM   6114 H HD21 . LEU   B 1 114 ? -5.812  -19.448 40.326  1.00 34.27  ? 99  LEU   B HD21 1 
ATOM   6115 H HD22 . LEU   B 1 114 ? -6.470  -18.008 40.191  1.00 34.27  ? 99  LEU   B HD22 1 
ATOM   6116 H HD23 . LEU   B 1 114 ? -6.949  -19.191 39.246  1.00 34.27  ? 99  LEU   B HD23 1 
ATOM   6117 N N    . GLN   B 1 115 ? -7.142  -15.124 35.958  1.00 29.18  ? 100 GLN   B N    1 
ATOM   6118 C CA   . GLN   B 1 115 ? -7.852  -13.873 35.729  1.00 31.15  ? 100 GLN   B CA   1 
ATOM   6119 C C    . GLN   B 1 115 ? -9.313  -14.130 35.369  1.00 34.74  ? 100 GLN   B C    1 
ATOM   6120 O O    . GLN   B 1 115 ? -10.207 -13.425 35.850  1.00 32.94  ? 100 GLN   B O    1 
ATOM   6121 C CB   . GLN   B 1 115 ? -7.158  -13.069 34.632  1.00 31.52  ? 100 GLN   B CB   1 
ATOM   6122 C CG   . GLN   B 1 115 ? -7.748  -11.685 34.418  1.00 37.78  ? 100 GLN   B CG   1 
ATOM   6123 C CD   . GLN   B 1 115 ? -7.074  -10.956 33.278  1.00 32.65  ? 100 GLN   B CD   1 
ATOM   6124 O OE1  . GLN   B 1 115 ? -5.955  -10.469 33.415  1.00 44.09  ? 100 GLN   B OE1  1 
ATOM   6125 N NE2  . GLN   B 1 115 ? -7.741  -10.902 32.137  1.00 41.85  ? 100 GLN   B NE2  1 
ATOM   6126 H H    . GLN   B 1 115 ? -6.516  -15.294 35.394  1.00 35.02  ? 100 GLN   B H    1 
ATOM   6127 H HA   . GLN   B 1 115 ? -7.831  -13.346 36.543  1.00 37.38  ? 100 GLN   B HA   1 
ATOM   6128 H HB2  . GLN   B 1 115 ? -6.225  -12.959 34.870  1.00 37.83  ? 100 GLN   B HB2  1 
ATOM   6129 H HB3  . GLN   B 1 115 ? -7.233  -13.555 33.796  1.00 37.83  ? 100 GLN   B HB3  1 
ATOM   6130 H HG2  . GLN   B 1 115 ? -8.692  -11.768 34.210  1.00 45.33  ? 100 GLN   B HG2  1 
ATOM   6131 H HG3  . GLN   B 1 115 ? -7.632  -11.159 35.225  1.00 45.33  ? 100 GLN   B HG3  1 
ATOM   6132 H HE21 . GLN   B 1 115 ? -8.516  -11.270 32.074  1.00 50.22  ? 100 GLN   B HE21 1 
ATOM   6133 H HE22 . GLN   B 1 115 ? -7.400  -10.499 31.458  1.00 50.22  ? 100 GLN   B HE22 1 
ATOM   6134 N N    . ASP   B 1 116 ? -9.578  -15.132 34.526  1.00 31.24  ? 101 ASP   B N    1 
ATOM   6135 C CA   . ASP   B 1 116 ? -10.963 -15.492 34.248  1.00 32.80  ? 101 ASP   B CA   1 
ATOM   6136 C C    . ASP   B 1 116 ? -11.694 -15.896 35.519  1.00 33.05  ? 101 ASP   B C    1 
ATOM   6137 O O    . ASP   B 1 116 ? -12.907 -15.698 35.633  1.00 40.38  ? 101 ASP   B O    1 
ATOM   6138 C CB   . ASP   B 1 116 ? -11.034 -16.645 33.251  1.00 38.55  ? 101 ASP   B CB   1 
ATOM   6139 C CG   . ASP   B 1 116 ? -10.412 -16.309 31.930  1.00 37.00  ? 101 ASP   B CG   1 
ATOM   6140 O OD1  . ASP   B 1 116 ? -10.380 -15.117 31.566  1.00 41.05  ? 101 ASP   B OD1  1 
ATOM   6141 O OD2  . ASP   B 1 116 ? -9.961  -17.253 31.253  1.00 38.66  ? 101 ASP   B OD2  1 
ATOM   6142 H H    . ASP   B 1 116 ? -8.988  -15.604 34.115  1.00 37.49  ? 101 ASP   B H    1 
ATOM   6143 H HA   . ASP   B 1 116 ? -11.399 -14.720 33.856  1.00 39.36  ? 101 ASP   B HA   1 
ATOM   6144 H HB2  . ASP   B 1 116 ? -10.564 -17.410 33.617  1.00 46.26  ? 101 ASP   B HB2  1 
ATOM   6145 H HB3  . ASP   B 1 116 ? -11.965 -16.870 33.095  1.00 46.26  ? 101 ASP   B HB3  1 
ATOM   6146 N N    . ILE   B 1 117 ? -10.980 -16.476 36.479  1.00 39.77  ? 102 ILE   B N    1 
ATOM   6147 C CA   . ILE   B 1 117 ? -11.636 -16.993 37.671  1.00 39.91  ? 102 ILE   B CA   1 
ATOM   6148 C C    . ILE   B 1 117 ? -11.864 -15.880 38.681  1.00 37.54  ? 102 ILE   B C    1 
ATOM   6149 O O    . ILE   B 1 117 ? -12.987 -15.686 39.166  1.00 38.72  ? 102 ILE   B O    1 
ATOM   6150 C CB   . ILE   B 1 117 ? -10.815 -18.148 38.275  1.00 35.63  ? 102 ILE   B CB   1 
ATOM   6151 C CG1  . ILE   B 1 117 ? -10.761 -19.318 37.293  1.00 37.94  ? 102 ILE   B CG1  1 
ATOM   6152 C CG2  . ILE   B 1 117 ? -11.405 -18.575 39.617  1.00 32.85  ? 102 ILE   B CG2  1 
ATOM   6153 C CD1  . ILE   B 1 117 ? -9.761  -20.380 37.658  1.00 38.51  ? 102 ILE   B CD1  1 
ATOM   6154 H H    . ILE   B 1 117 ? -10.126 -16.580 36.464  1.00 47.73  ? 102 ILE   B H    1 
ATOM   6155 H HA   . ILE   B 1 117 ? -12.503 -17.346 37.417  1.00 47.89  ? 102 ILE   B HA   1 
ATOM   6156 H HB   . ILE   B 1 117 ? -9.907  -17.843 38.432  1.00 42.76  ? 102 ILE   B HB   1 
ATOM   6157 H HG12 . ILE   B 1 117 ? -11.636 -19.736 37.259  1.00 45.53  ? 102 ILE   B HG12 1 
ATOM   6158 H HG13 . ILE   B 1 117 ? -10.522 -18.978 36.416  1.00 45.53  ? 102 ILE   B HG13 1 
ATOM   6159 H HG21 . ILE   B 1 117 ? -11.028 -19.432 39.869  1.00 39.42  ? 102 ILE   B HG21 1 
ATOM   6160 H HG22 . ILE   B 1 117 ? -11.186 -17.907 40.285  1.00 39.42  ? 102 ILE   B HG22 1 
ATOM   6161 H HG23 . ILE   B 1 117 ? -12.368 -18.650 39.528  1.00 39.42  ? 102 ILE   B HG23 1 
ATOM   6162 H HD11 . ILE   B 1 117 ? -9.675  -21.001 36.918  1.00 46.21  ? 102 ILE   B HD11 1 
ATOM   6163 H HD12 . ILE   B 1 117 ? -8.905  -19.960 37.838  1.00 46.21  ? 102 ILE   B HD12 1 
ATOM   6164 H HD13 . ILE   B 1 117 ? -10.072 -20.849 38.448  1.00 46.21  ? 102 ILE   B HD13 1 
ATOM   6165 N N    . TYR   B 1 118 ? -10.815 -15.121 39.014  1.00 34.20  ? 103 TYR   B N    1 
ATOM   6166 C CA   . TYR   B 1 118 ? -10.971 -14.146 40.089  1.00 38.97  ? 103 TYR   B CA   1 
ATOM   6167 C C    . TYR   B 1 118 ? -11.844 -12.967 39.677  1.00 44.20  ? 103 TYR   B C    1 
ATOM   6168 O O    . TYR   B 1 118 ? -12.418 -12.307 40.549  1.00 43.40  ? 103 TYR   B O    1 
ATOM   6169 C CB   . TYR   B 1 118 ? -9.604  -13.670 40.615  1.00 38.10  ? 103 TYR   B CB   1 
ATOM   6170 C CG   . TYR   B 1 118 ? -8.755  -12.764 39.737  1.00 36.97  ? 103 TYR   B CG   1 
ATOM   6171 C CD1  . TYR   B 1 118 ? -9.232  -11.547 39.274  1.00 36.00  ? 103 TYR   B CD1  1 
ATOM   6172 C CD2  . TYR   B 1 118 ? -7.446  -13.105 39.429  1.00 32.02  ? 103 TYR   B CD2  1 
ATOM   6173 C CE1  . TYR   B 1 118 ? -8.445  -10.718 38.497  1.00 39.20  ? 103 TYR   B CE1  1 
ATOM   6174 C CE2  . TYR   B 1 118 ? -6.653  -12.279 38.658  1.00 29.77  ? 103 TYR   B CE2  1 
ATOM   6175 C CZ   . TYR   B 1 118 ? -7.157  -11.088 38.196  1.00 30.58  ? 103 TYR   B CZ   1 
ATOM   6176 O OH   . TYR   B 1 118 ? -6.375  -10.256 37.425  1.00 32.43  ? 103 TYR   B OH   1 
ATOM   6177 H H    . TYR   B 1 118 ? -10.038 -15.152 38.647  1.00 41.05  ? 103 TYR   B H    1 
ATOM   6178 H HA   . TYR   B 1 118 ? -11.409 -14.583 40.836  1.00 46.76  ? 103 TYR   B HA   1 
ATOM   6179 H HB2  . TYR   B 1 118 ? -9.761  -13.184 41.440  1.00 45.72  ? 103 TYR   B HB2  1 
ATOM   6180 H HB3  . TYR   B 1 118 ? -9.068  -14.460 40.793  1.00 45.72  ? 103 TYR   B HB3  1 
ATOM   6181 H HD1  . TYR   B 1 118 ? -10.098 -11.284 39.491  1.00 43.20  ? 103 TYR   B HD1  1 
ATOM   6182 H HD2  . TYR   B 1 118 ? -7.096  -13.906 39.748  1.00 38.43  ? 103 TYR   B HD2  1 
ATOM   6183 H HE1  . TYR   B 1 118 ? -8.786  -9.913  38.180  1.00 47.04  ? 103 TYR   B HE1  1 
ATOM   6184 H HE2  . TYR   B 1 118 ? -5.780  -12.528 38.452  1.00 35.72  ? 103 TYR   B HE2  1 
ATOM   6185 H HH   . TYR   B 1 118 ? -5.616  -10.599 37.313  1.00 38.91  ? 103 TYR   B HH   1 
ATOM   6186 N N    . GLN   B 1 119 ? -11.980 -12.693 38.378  1.00 37.19  ? 104 GLN   B N    1 
ATOM   6187 C CA   . GLN   B 1 119 ? -12.926 -11.662 37.962  1.00 44.87  ? 104 GLN   B CA   1 
ATOM   6188 C C    . GLN   B 1 119 ? -14.357 -12.024 38.336  1.00 50.62  ? 104 GLN   B C    1 
ATOM   6189 O O    . GLN   B 1 119 ? -15.222 -11.144 38.356  1.00 48.00  ? 104 GLN   B O    1 
ATOM   6190 C CB   . GLN   B 1 119 ? -12.826 -11.421 36.458  1.00 45.53  ? 104 GLN   B CB   1 
ATOM   6191 C CG   . GLN   B 1 119 ? -11.635 -10.571 36.055  1.00 43.10  ? 104 GLN   B CG   1 
ATOM   6192 C CD   . GLN   B 1 119 ? -11.509 -10.430 34.553  1.00 42.93  ? 104 GLN   B CD   1 
ATOM   6193 O OE1  . GLN   B 1 119 ? -12.138 -11.169 33.794  1.00 49.70  ? 104 GLN   B OE1  1 
ATOM   6194 N NE2  . GLN   B 1 119 ? -10.699 -9.480  34.115  1.00 37.08  ? 104 GLN   B NE2  1 
ATOM   6195 H H    . GLN   B 1 119 ? -11.550 -13.077 37.740  1.00 44.63  ? 104 GLN   B H    1 
ATOM   6196 H HA   . GLN   B 1 119 ? -12.695 -10.832 38.407  1.00 53.84  ? 104 GLN   B HA   1 
ATOM   6197 H HB2  . GLN   B 1 119 ? -12.745 -12.277 36.009  1.00 54.64  ? 104 GLN   B HB2  1 
ATOM   6198 H HB3  . GLN   B 1 119 ? -13.629 -10.965 36.161  1.00 54.64  ? 104 GLN   B HB3  1 
ATOM   6199 H HG2  . GLN   B 1 119 ? -11.735 -9.684  36.434  1.00 51.72  ? 104 GLN   B HG2  1 
ATOM   6200 H HG3  . GLN   B 1 119 ? -10.823 -10.985 36.387  1.00 51.72  ? 104 GLN   B HG3  1 
ATOM   6201 H HE21 . GLN   B 1 119 ? -10.277 -8.982  34.675  1.00 44.50  ? 104 GLN   B HE21 1 
ATOM   6202 H HE22 . GLN   B 1 119 ? -10.594 -9.360  33.270  1.00 44.50  ? 104 GLN   B HE22 1 
ATOM   6203 N N    . VAL   B 1 120 ? -14.622 -13.291 38.634  1.00 50.73  ? 105 VAL   B N    1 
ATOM   6204 C CA   . VAL   B 1 120 ? -15.936 -13.735 39.090  1.00 52.47  ? 105 VAL   B CA   1 
ATOM   6205 C C    . VAL   B 1 120 ? -15.939 -14.011 40.588  1.00 46.92  ? 105 VAL   B C    1 
ATOM   6206 O O    . VAL   B 1 120 ? -16.853 -13.605 41.304  1.00 42.86  ? 105 VAL   B O    1 
ATOM   6207 C CB   . VAL   B 1 120 ? -16.381 -14.985 38.298  1.00 51.03  ? 105 VAL   B CB   1 
ATOM   6208 C CG1  . VAL   B 1 120 ? -17.797 -15.376 38.688  1.00 55.52  ? 105 VAL   B CG1  1 
ATOM   6209 C CG2  . VAL   B 1 120 ? -16.273 -14.747 36.794  1.00 47.62  ? 105 VAL   B CG2  1 
ATOM   6210 H H    . VAL   B 1 120 ? -14.045 -13.926 38.579  1.00 60.88  ? 105 VAL   B H    1 
ATOM   6211 H HA   . VAL   B 1 120 ? -16.574 -13.025 38.917  1.00 62.96  ? 105 VAL   B HA   1 
ATOM   6212 H HB   . VAL   B 1 120 ? -15.791 -15.723 38.518  1.00 61.23  ? 105 VAL   B HB   1 
ATOM   6213 H HG11 . VAL   B 1 120 ? -18.112 -16.065 38.083  1.00 66.62  ? 105 VAL   B HG11 1 
ATOM   6214 H HG12 . VAL   B 1 120 ? -17.792 -15.711 39.599  1.00 66.62  ? 105 VAL   B HG12 1 
ATOM   6215 H HG13 . VAL   B 1 120 ? -18.368 -14.594 38.627  1.00 66.62  ? 105 VAL   B HG13 1 
ATOM   6216 H HG21 . VAL   B 1 120 ? -16.666 -15.500 36.325  1.00 57.14  ? 105 VAL   B HG21 1 
ATOM   6217 H HG22 . VAL   B 1 120 ? -16.748 -13.933 36.568  1.00 57.14  ? 105 VAL   B HG22 1 
ATOM   6218 H HG23 . VAL   B 1 120 ? -15.337 -14.661 36.554  1.00 57.14  ? 105 VAL   B HG23 1 
ATOM   6219 N N    . THR   B 1 121 ? -14.918 -14.706 41.079  1.00 43.58  ? 106 THR   B N    1 
ATOM   6220 C CA   . THR   B 1 121 ? -14.909 -15.152 42.464  1.00 42.13  ? 106 THR   B CA   1 
ATOM   6221 C C    . THR   B 1 121 ? -14.498 -14.063 43.439  1.00 46.42  ? 106 THR   B C    1 
ATOM   6222 O O    . THR   B 1 121 ? -14.822 -14.163 44.625  1.00 42.42  ? 106 THR   B O    1 
ATOM   6223 C CB   . THR   B 1 121 ? -13.955 -16.334 42.626  1.00 45.28  ? 106 THR   B CB   1 
ATOM   6224 O OG1  . THR   B 1 121 ? -12.622 -15.914 42.304  1.00 42.92  ? 106 THR   B OG1  1 
ATOM   6225 C CG2  . THR   B 1 121 ? -14.355 -17.478 41.710  1.00 44.32  ? 106 THR   B CG2  1 
ATOM   6226 H H    . THR   B 1 121 ? -14.219 -14.932 40.630  1.00 52.29  ? 106 THR   B H    1 
ATOM   6227 H HA   . THR   B 1 121 ? -15.808 -15.439 42.691  1.00 50.55  ? 106 THR   B HA   1 
ATOM   6228 H HB   . THR   B 1 121 ? -13.986 -16.654 43.541  1.00 54.34  ? 106 THR   B HB   1 
ATOM   6229 H HG1  . THR   B 1 121 ? -12.095 -16.567 42.350  1.00 51.50  ? 106 THR   B HG1  1 
ATOM   6230 H HG21 . THR   B 1 121 ? -13.793 -18.250 41.879  1.00 53.19  ? 106 THR   B HG21 1 
ATOM   6231 H HG22 . THR   B 1 121 ? -15.281 -17.721 41.869  1.00 53.19  ? 106 THR   B HG22 1 
ATOM   6232 H HG23 . THR   B 1 121 ? -14.255 -17.211 40.783  1.00 53.19  ? 106 THR   B HG23 1 
ATOM   6233 N N    . GLY   B 1 122 ? -13.803 -13.029 42.972  1.00 42.88  ? 107 GLY   B N    1 
ATOM   6234 C CA   . GLY   B 1 122 ? -13.143 -12.110 43.876  1.00 38.33  ? 107 GLY   B CA   1 
ATOM   6235 C C    . GLY   B 1 122 ? -11.748 -12.594 44.222  1.00 40.71  ? 107 GLY   B C    1 
ATOM   6236 O O    . GLY   B 1 122 ? -11.260 -13.614 43.728  1.00 35.30  ? 107 GLY   B O    1 
ATOM   6237 H H    . GLY   B 1 122 ? -13.702 -12.844 42.139  1.00 51.45  ? 107 GLY   B H    1 
ATOM   6238 H HA2  . GLY   B 1 122 ? -13.076 -11.237 43.460  1.00 45.99  ? 107 GLY   B HA2  1 
ATOM   6239 H HA3  . GLY   B 1 122 ? -13.658 -12.032 44.694  1.00 45.99  ? 107 GLY   B HA3  1 
ATOM   6240 N N    . SER   B 1 123 ? -11.098 -11.847 45.112  1.00 40.08  ? 108 SER   B N    1 
ATOM   6241 C CA   . SER   B 1 123 ? -9.691  -12.087 45.407  1.00 37.87  ? 108 SER   B CA   1 
ATOM   6242 C C    . SER   B 1 123 ? -9.477  -13.462 46.039  1.00 39.13  ? 108 SER   B C    1 
ATOM   6243 O O    . SER   B 1 123 ? -10.365 -14.021 46.686  1.00 38.10  ? 108 SER   B O    1 
ATOM   6244 C CB   . SER   B 1 123 ? -9.154  -10.997 46.336  1.00 36.08  ? 108 SER   B CB   1 
ATOM   6245 O OG   . SER   B 1 123 ? -9.718  -11.089 47.633  1.00 37.56  ? 108 SER   B OG   1 
ATOM   6246 H H    . SER   B 1 123 ? -11.448 -11.199 45.556  1.00 48.10  ? 108 SER   B H    1 
ATOM   6247 H HA   . SER   B 1 123 ? -9.188  -12.065 44.577  1.00 45.44  ? 108 SER   B HA   1 
ATOM   6248 H HB2  . SER   B 1 123 ? -8.192  -11.092 46.406  1.00 43.30  ? 108 SER   B HB2  1 
ATOM   6249 H HB3  . SER   B 1 123 ? -9.375  -10.130 45.960  1.00 43.30  ? 108 SER   B HB3  1 
ATOM   6250 H HG   . SER   B 1 123 ? -9.403  -10.486 48.126  1.00 45.07  ? 108 SER   B HG   1 
ATOM   6251 N N    . LEU   B 1 124 ? -8.272  -14.000 45.856  1.00 34.70  ? 109 LEU   B N    1 
ATOM   6252 C CA   . LEU   B 1 124 ? -7.929  -15.305 46.398  1.00 35.61  ? 109 LEU   B CA   1 
ATOM   6253 C C    . LEU   B 1 124 ? -7.481  -15.206 47.851  1.00 33.89  ? 109 LEU   B C    1 
ATOM   6254 O O    . LEU   B 1 124 ? -6.993  -14.171 48.301  1.00 34.15  ? 109 LEU   B O    1 
ATOM   6255 C CB   . LEU   B 1 124 ? -6.813  -15.951 45.575  1.00 36.14  ? 109 LEU   B CB   1 
ATOM   6256 C CG   . LEU   B 1 124 ? -7.237  -16.707 44.315  1.00 31.83  ? 109 LEU   B CG   1 
ATOM   6257 C CD1  . LEU   B 1 124 ? -7.906  -15.764 43.298  1.00 31.44  ? 109 LEU   B CD1  1 
ATOM   6258 C CD2  . LEU   B 1 124 ? -6.043  -17.416 43.711  1.00 33.35  ? 109 LEU   B CD2  1 
ATOM   6259 H H    . LEU   B 1 124 ? -7.634  -13.624 45.419  1.00 41.64  ? 109 LEU   B H    1 
ATOM   6260 H HA   . LEU   B 1 124 ? -8.717  -15.870 46.361  1.00 42.74  ? 109 LEU   B HA   1 
ATOM   6261 H HB2  . LEU   B 1 124 ? -6.204  -15.250 45.295  1.00 43.37  ? 109 LEU   B HB2  1 
ATOM   6262 H HB3  . LEU   B 1 124 ? -6.350  -16.585 46.145  1.00 43.37  ? 109 LEU   B HB3  1 
ATOM   6263 H HG   . LEU   B 1 124 ? -7.897  -17.377 44.551  1.00 38.20  ? 109 LEU   B HG   1 
ATOM   6264 H HD11 . LEU   B 1 124 ? -8.121  -16.266 42.496  1.00 37.72  ? 109 LEU   B HD11 1 
ATOM   6265 H HD12 . LEU   B 1 124 ? -8.717  -15.402 43.688  1.00 37.72  ? 109 LEU   B HD12 1 
ATOM   6266 H HD13 . LEU   B 1 124 ? -7.292  -15.044 43.083  1.00 37.72  ? 109 LEU   B HD13 1 
ATOM   6267 H HD21 . LEU   B 1 124 ? -6.327  -17.892 42.916  1.00 40.03  ? 109 LEU   B HD21 1 
ATOM   6268 H HD22 . LEU   B 1 124 ? -5.369  -16.758 43.480  1.00 40.03  ? 109 LEU   B HD22 1 
ATOM   6269 H HD23 . LEU   B 1 124 ? -5.685  -18.041 44.361  1.00 40.03  ? 109 LEU   B HD23 1 
ATOM   6270 N N    . SER   B 1 125 ? -7.644  -16.314 48.580  1.00 36.60  ? 110 SER   B N    1 
ATOM   6271 C CA   . SER   B 1 125 ? -7.120  -16.418 49.933  1.00 35.09  ? 110 SER   B CA   1 
ATOM   6272 C C    . SER   B 1 125 ? -5.609  -16.614 49.907  1.00 34.39  ? 110 SER   B C    1 
ATOM   6273 O O    . SER   B 1 125 ? -5.028  -17.053 48.908  1.00 37.26  ? 110 SER   B O    1 
ATOM   6274 C CB   . SER   B 1 125 ? -7.744  -17.604 50.657  1.00 36.11  ? 110 SER   B CB   1 
ATOM   6275 O OG   . SER   B 1 125 ? -7.156  -18.802 50.166  1.00 35.04  ? 110 SER   B OG   1 
ATOM   6276 H H    . SER   B 1 125 ? -8.056  -17.018 48.309  1.00 43.92  ? 110 SER   B H    1 
ATOM   6277 H HA   . SER   B 1 125 ? -7.331  -15.603 50.414  1.00 42.11  ? 110 SER   B HA   1 
ATOM   6278 H HB2  . SER   B 1 125 ? -7.575  -17.527 51.609  1.00 43.33  ? 110 SER   B HB2  1 
ATOM   6279 H HB3  . SER   B 1 125 ? -8.699  -17.619 50.489  1.00 43.33  ? 110 SER   B HB3  1 
ATOM   6280 H HG   . SER   B 1 125 ? -7.480  -19.466 50.566  1.00 42.05  ? 110 SER   B HG   1 
ATOM   6281 N N    . GLU   B 1 126 ? -4.969  -16.338 51.045  1.00 34.59  ? 111 GLU   B N    1 
ATOM   6282 C CA   . GLU   B 1 126 ? -3.520  -16.472 51.103  1.00 33.74  ? 111 GLU   B CA   1 
ATOM   6283 C C    . GLU   B 1 126 ? -3.084  -17.905 50.819  1.00 39.82  ? 111 GLU   B C    1 
ATOM   6284 O O    . GLU   B 1 126 ? -2.077  -18.129 50.137  1.00 32.00  ? 111 GLU   B O    1 
ATOM   6285 C CB   . GLU   B 1 126 ? -2.991  -16.015 52.456  1.00 34.94  ? 111 GLU   B CB   1 
ATOM   6286 C CG   . GLU   B 1 126 ? -1.477  -16.114 52.576  1.00 37.33  ? 111 GLU   B CG   1 
ATOM   6287 C CD   . GLU   B 1 126 ? -0.943  -15.476 53.849  1.00 48.54  ? 111 GLU   B CD   1 
ATOM   6288 O OE1  . GLU   B 1 126 ? -1.542  -14.482 54.328  1.00 46.93  ? 111 GLU   B OE1  1 
ATOM   6289 O OE2  . GLU   B 1 126 ? 0.076   -15.973 54.372  1.00 38.44  ? 111 GLU   B OE2  1 
ATOM   6290 H H    . GLU   B 1 126 ? -5.343  -16.079 51.775  1.00 41.50  ? 111 GLU   B H    1 
ATOM   6291 H HA   . GLU   B 1 126 ? -3.134  -15.896 50.425  1.00 40.49  ? 111 GLU   B HA   1 
ATOM   6292 H HB2  . GLU   B 1 126 ? -3.242  -15.089 52.594  1.00 41.93  ? 111 GLU   B HB2  1 
ATOM   6293 H HB3  . GLU   B 1 126 ? -3.382  -16.571 53.149  1.00 41.93  ? 111 GLU   B HB3  1 
ATOM   6294 H HG2  . GLU   B 1 126 ? -1.220  -17.049 52.579  1.00 44.80  ? 111 GLU   B HG2  1 
ATOM   6295 H HG3  . GLU   B 1 126 ? -1.070  -15.661 51.821  1.00 44.80  ? 111 GLU   B HG3  1 
ATOM   6296 N N    . LEU   B 1 127 ? -3.825  -18.892 51.328  1.00 37.84  ? 112 LEU   B N    1 
ATOM   6297 C CA   . LEU   B 1 127 ? -3.439  -20.278 51.089  1.00 33.54  ? 112 LEU   B CA   1 
ATOM   6298 C C    . LEU   B 1 127 ? -3.510  -20.608 49.602  1.00 32.28  ? 112 LEU   B C    1 
ATOM   6299 O O    . LEU   B 1 127 ? -2.585  -21.201 49.046  1.00 31.51  ? 112 LEU   B O    1 
ATOM   6300 C CB   . LEU   B 1 127 ? -4.321  -21.232 51.894  1.00 34.91  ? 112 LEU   B CB   1 
ATOM   6301 C CG   . LEU   B 1 127 ? -3.933  -21.522 53.345  1.00 40.39  ? 112 LEU   B CG   1 
ATOM   6302 C CD1  . LEU   B 1 127 ? -4.685  -22.766 53.820  1.00 53.39  ? 112 LEU   B CD1  1 
ATOM   6303 C CD2  . LEU   B 1 127 ? -2.435  -21.711 53.543  1.00 40.76  ? 112 LEU   B CD2  1 
ATOM   6304 H H    . LEU   B 1 127 ? -4.535  -18.787 51.801  1.00 45.40  ? 112 LEU   B H    1 
ATOM   6305 H HA   . LEU   B 1 127 ? -2.526  -20.402 51.392  1.00 40.25  ? 112 LEU   B HA   1 
ATOM   6306 H HB2  . LEU   B 1 127 ? -5.216  -20.857 51.915  1.00 41.89  ? 112 LEU   B HB2  1 
ATOM   6307 H HB3  . LEU   B 1 127 ? -4.329  -22.085 51.432  1.00 41.89  ? 112 LEU   B HB3  1 
ATOM   6308 H HG   . LEU   B 1 127 ? -4.177  -20.751 53.881  1.00 48.47  ? 112 LEU   B HG   1 
ATOM   6309 H HD11 . LEU   B 1 127 ? -4.460  -22.936 54.748  1.00 64.07  ? 112 LEU   B HD11 1 
ATOM   6310 H HD12 . LEU   B 1 127 ? -5.639  -22.611 53.734  1.00 64.07  ? 112 LEU   B HD12 1 
ATOM   6311 H HD13 . LEU   B 1 127 ? -4.423  -23.522 53.272  1.00 64.07  ? 112 LEU   B HD13 1 
ATOM   6312 H HD21 . LEU   B 1 127 ? -2.280  -22.125 54.406  1.00 48.91  ? 112 LEU   B HD21 1 
ATOM   6313 H HD22 . LEU   B 1 127 ? -2.092  -22.282 52.836  1.00 48.91  ? 112 LEU   B HD22 1 
ATOM   6314 H HD23 . LEU   B 1 127 ? -2.000  -20.845 53.508  1.00 48.91  ? 112 LEU   B HD23 1 
ATOM   6315 N N    . GLN   B 1 128 ? -4.604  -20.218 48.944  1.00 32.27  ? 113 GLN   B N    1 
ATOM   6316 C CA   . GLN   B 1 128 ? -4.729  -20.442 47.512  1.00 31.28  ? 113 GLN   B CA   1 
ATOM   6317 C C    . GLN   B 1 128 ? -3.598  -19.767 46.740  1.00 32.29  ? 113 GLN   B C    1 
ATOM   6318 O O    . GLN   B 1 128 ? -3.052  -20.345 45.791  1.00 29.70  ? 113 GLN   B O    1 
ATOM   6319 C CB   . GLN   B 1 128 ? -6.090  -19.941 47.029  1.00 31.73  ? 113 GLN   B CB   1 
ATOM   6320 C CG   . GLN   B 1 128 ? -7.280  -20.753 47.552  1.00 34.33  ? 113 GLN   B CG   1 
ATOM   6321 C CD   . GLN   B 1 128 ? -8.602  -20.036 47.373  1.00 33.97  ? 113 GLN   B CD   1 
ATOM   6322 O OE1  . GLN   B 1 128 ? -8.647  -18.810 47.272  1.00 39.09  ? 113 GLN   B OE1  1 
ATOM   6323 N NE2  . GLN   B 1 128 ? -9.687  -20.796 47.335  1.00 34.92  ? 113 GLN   B NE2  1 
ATOM   6324 H H    . GLN   B 1 128 ? -5.279  -19.825 49.303  1.00 38.72  ? 113 GLN   B H    1 
ATOM   6325 H HA   . GLN   B 1 128 ? -4.676  -21.395 47.336  1.00 37.53  ? 113 GLN   B HA   1 
ATOM   6326 H HB2  . GLN   B 1 128 ? -6.206  -19.025 47.324  1.00 38.08  ? 113 GLN   B HB2  1 
ATOM   6327 H HB3  . GLN   B 1 128 ? -6.109  -19.982 46.060  1.00 38.08  ? 113 GLN   B HB3  1 
ATOM   6328 H HG2  . GLN   B 1 128 ? -7.326  -21.593 47.070  1.00 41.20  ? 113 GLN   B HG2  1 
ATOM   6329 H HG3  . GLN   B 1 128 ? -7.156  -20.920 48.500  1.00 41.20  ? 113 GLN   B HG3  1 
ATOM   6330 H HE21 . GLN   B 1 128 ? -9.617  -21.649 47.411  1.00 41.90  ? 113 GLN   B HE21 1 
ATOM   6331 H HE22 . GLN   B 1 128 ? -10.461 -20.435 47.235  1.00 41.90  ? 113 GLN   B HE22 1 
ATOM   6332 N N    . ILE   B 1 129 ? -3.241  -18.542 47.123  1.00 30.13  ? 114 ILE   B N    1 
ATOM   6333 C CA   . ILE   B 1 129 ? -2.130  -17.860 46.471  1.00 29.62  ? 114 ILE   B CA   1 
ATOM   6334 C C    . ILE   B 1 129 ? -0.820  -18.583 46.759  1.00 30.89  ? 114 ILE   B C    1 
ATOM   6335 O O    . ILE   B 1 129 ? 0.036   -18.718 45.875  1.00 32.51  ? 114 ILE   B O    1 
ATOM   6336 C CB   . ILE   B 1 129 ? -2.080  -16.385 46.920  1.00 29.62  ? 114 ILE   B CB   1 
ATOM   6337 C CG1  . ILE   B 1 129 ? -3.373  -15.665 46.504  1.00 32.80  ? 114 ILE   B CG1  1 
ATOM   6338 C CG2  . ILE   B 1 129 ? -0.836  -15.703 46.360  1.00 28.91  ? 114 ILE   B CG2  1 
ATOM   6339 C CD1  . ILE   B 1 129 ? -3.457  -14.192 46.948  1.00 34.12  ? 114 ILE   B CD1  1 
ATOM   6340 H H    . ILE   B 1 129 ? -3.621  -18.092 47.749  1.00 36.15  ? 114 ILE   B H    1 
ATOM   6341 H HA   . ILE   B 1 129 ? -2.274  -17.878 45.512  1.00 35.54  ? 114 ILE   B HA   1 
ATOM   6342 H HB   . ILE   B 1 129 ? -2.019  -16.346 47.887  1.00 35.54  ? 114 ILE   B HB   1 
ATOM   6343 H HG12 . ILE   B 1 129 ? -3.438  -15.684 45.536  1.00 39.36  ? 114 ILE   B HG12 1 
ATOM   6344 H HG13 . ILE   B 1 129 ? -4.126  -16.133 46.896  1.00 39.36  ? 114 ILE   B HG13 1 
ATOM   6345 H HG21 . ILE   B 1 129 ? -0.896  -14.749 46.528  1.00 34.70  ? 114 ILE   B HG21 1 
ATOM   6346 H HG22 . ILE   B 1 129 ? -0.051  -16.067 46.799  1.00 34.70  ? 114 ILE   B HG22 1 
ATOM   6347 H HG23 . ILE   B 1 129 ? -0.788  -15.868 45.405  1.00 34.70  ? 114 ILE   B HG23 1 
ATOM   6348 H HD11 . ILE   B 1 129 ? -4.367  -13.878 46.831  1.00 40.95  ? 114 ILE   B HD11 1 
ATOM   6349 H HD12 . ILE   B 1 129 ? -3.202  -14.129 47.882  1.00 40.95  ? 114 ILE   B HD12 1 
ATOM   6350 H HD13 . ILE   B 1 129 ? -2.852  -13.663 46.404  1.00 40.95  ? 114 ILE   B HD13 1 
ATOM   6351 N N    . SER   B 1 130 ? -0.634  -19.044 47.997  1.00 29.82  ? 115 SER   B N    1 
ATOM   6352 C CA   . SER   B 1 130 ? 0.563   -19.807 48.331  1.00 31.06  ? 115 SER   B CA   1 
ATOM   6353 C C    . SER   B 1 130 ? 0.706   -21.027 47.426  1.00 30.21  ? 115 SER   B C    1 
ATOM   6354 O O    . SER   B 1 130 ? 1.802   -21.321 46.932  1.00 31.54  ? 115 SER   B O    1 
ATOM   6355 C CB   . SER   B 1 130 ? 0.520   -20.239 49.800  1.00 34.59  ? 115 SER   B CB   1 
ATOM   6356 O OG   . SER   B 1 130 ? 0.529   -19.125 50.670  1.00 36.13  ? 115 SER   B OG   1 
ATOM   6357 H H    . SER   B 1 130 ? -1.179  -18.929 48.653  1.00 35.78  ? 115 SER   B H    1 
ATOM   6358 H HA   . SER   B 1 130 ? 1.339   -19.240 48.204  1.00 37.27  ? 115 SER   B HA   1 
ATOM   6359 H HB2  . SER   B 1 130 ? -0.292  -20.748 49.953  1.00 41.51  ? 115 SER   B HB2  1 
ATOM   6360 H HB3  . SER   B 1 130 ? 1.297   -20.789 49.988  1.00 41.51  ? 115 SER   B HB3  1 
ATOM   6361 H HG   . SER   B 1 130 ? -0.149  -18.649 50.534  1.00 43.36  ? 115 SER   B HG   1 
ATOM   6362 N N    . TYR   B 1 131 ? -0.395  -21.745 47.192  1.00 31.34  ? 116 TYR   B N    1 
ATOM   6363 C CA   . TYR   B 1 131 ? -0.338  -22.922 46.330  1.00 32.58  ? 116 TYR   B CA   1 
ATOM   6364 C C    . TYR   B 1 131 ? -0.054  -22.525 44.890  1.00 28.57  ? 116 TYR   B C    1 
ATOM   6365 O O    . TYR   B 1 131 ? 0.747   -23.170 44.206  1.00 28.49  ? 116 TYR   B O    1 
ATOM   6366 C CB   . TYR   B 1 131 ? -1.647  -23.700 46.439  1.00 30.11  ? 116 TYR   B CB   1 
ATOM   6367 C CG   . TYR   B 1 131 ? -1.838  -24.772 45.403  1.00 30.06  ? 116 TYR   B CG   1 
ATOM   6368 C CD1  . TYR   B 1 131 ? -1.141  -25.970 45.471  1.00 34.83  ? 116 TYR   B CD1  1 
ATOM   6369 C CD2  . TYR   B 1 131 ? -2.733  -24.598 44.365  1.00 30.99  ? 116 TYR   B CD2  1 
ATOM   6370 C CE1  . TYR   B 1 131 ? -1.327  -26.958 44.530  1.00 33.20  ? 116 TYR   B CE1  1 
ATOM   6371 C CE2  . TYR   B 1 131 ? -2.923  -25.586 43.416  1.00 35.02  ? 116 TYR   B CE2  1 
ATOM   6372 C CZ   . TYR   B 1 131 ? -2.219  -26.760 43.508  1.00 31.32  ? 116 TYR   B CZ   1 
ATOM   6373 O OH   . TYR   B 1 131 ? -2.394  -27.736 42.562  1.00 37.22  ? 116 TYR   B OH   1 
ATOM   6374 H H    . TYR   B 1 131 ? -1.173  -21.574 47.516  1.00 37.60  ? 116 TYR   B H    1 
ATOM   6375 H HA   . TYR   B 1 131 ? 0.379   -23.506 46.624  1.00 39.10  ? 116 TYR   B HA   1 
ATOM   6376 H HB2  . TYR   B 1 131 ? -1.677  -24.128 47.309  1.00 36.14  ? 116 TYR   B HB2  1 
ATOM   6377 H HB3  . TYR   B 1 131 ? -2.383  -23.075 46.351  1.00 36.14  ? 116 TYR   B HB3  1 
ATOM   6378 H HD1  . TYR   B 1 131 ? -0.537  -26.108 46.164  1.00 41.80  ? 116 TYR   B HD1  1 
ATOM   6379 H HD2  . TYR   B 1 131 ? -3.216  -23.806 44.303  1.00 37.18  ? 116 TYR   B HD2  1 
ATOM   6380 H HE1  . TYR   B 1 131 ? -0.851  -27.755 44.588  1.00 39.84  ? 116 TYR   B HE1  1 
ATOM   6381 H HE2  . TYR   B 1 131 ? -3.524  -25.455 42.719  1.00 42.03  ? 116 TYR   B HE2  1 
ATOM   6382 H HH   . TYR   B 1 131 ? -2.955  -27.484 41.990  1.00 44.66  ? 116 TYR   B HH   1 
ATOM   6383 N N    . VAL   B 1 132 ? -0.678  -21.448 44.417  1.00 29.86  ? 117 VAL   B N    1 
ATOM   6384 C CA   . VAL   B 1 132 ? -0.415  -21.012 43.051  1.00 29.84  ? 117 VAL   B CA   1 
ATOM   6385 C C    . VAL   B 1 132 ? 1.052   -20.636 42.890  1.00 29.90  ? 117 VAL   B C    1 
ATOM   6386 O O    . VAL   B 1 132 ? 1.701   -21.012 41.905  1.00 28.22  ? 117 VAL   B O    1 
ATOM   6387 C CB   . VAL   B 1 132 ? -1.353  -19.853 42.677  1.00 32.47  ? 117 VAL   B CB   1 
ATOM   6388 C CG1  . VAL   B 1 132 ? -0.907  -19.210 41.368  1.00 28.71  ? 117 VAL   B CG1  1 
ATOM   6389 C CG2  . VAL   B 1 132 ? -2.787  -20.352 42.578  1.00 27.80  ? 117 VAL   B CG2  1 
ATOM   6390 H H    . VAL   B 1 132 ? -1.241  -20.967 44.854  1.00 35.83  ? 117 VAL   B H    1 
ATOM   6391 H HA   . VAL   B 1 132 ? -0.599  -21.747 42.445  1.00 35.81  ? 117 VAL   B HA   1 
ATOM   6392 H HB   . VAL   B 1 132 ? -1.317  -19.174 43.369  1.00 38.97  ? 117 VAL   B HB   1 
ATOM   6393 H HG11 . VAL   B 1 132 ? -1.623  -18.649 41.031  1.00 34.45  ? 117 VAL   B HG11 1 
ATOM   6394 H HG12 . VAL   B 1 132 ? -0.116  -18.673 41.533  1.00 34.45  ? 117 VAL   B HG12 1 
ATOM   6395 H HG13 . VAL   B 1 132 ? -0.704  -19.908 40.726  1.00 34.45  ? 117 VAL   B HG13 1 
ATOM   6396 H HG21 . VAL   B 1 132 ? -3.376  -19.595 42.431  1.00 33.36  ? 117 VAL   B HG21 1 
ATOM   6397 H HG22 . VAL   B 1 132 ? -2.855  -20.972 41.835  1.00 33.36  ? 117 VAL   B HG22 1 
ATOM   6398 H HG23 . VAL   B 1 132 ? -3.024  -20.800 43.405  1.00 33.36  ? 117 VAL   B HG23 1 
ATOM   6399 N N    . CYS   B 1 133 ? 1.605   -19.901 43.855  1.00 29.05  ? 118 CYS   B N    1 
ATOM   6400 C CA   . CYS   B 1 133 ? 2.998   -19.481 43.735  1.00 31.55  ? 118 CYS   B CA   1 
ATOM   6401 C C    . CYS   B 1 133 ? 3.952   -20.669 43.772  1.00 32.55  ? 118 CYS   B C    1 
ATOM   6402 O O    . CYS   B 1 133 ? 4.959   -20.675 43.059  1.00 27.58  ? 118 CYS   B O    1 
ATOM   6403 C CB   . CYS   B 1 133 ? 3.343   -18.489 44.839  1.00 36.02  ? 118 CYS   B CB   1 
ATOM   6404 S SG   . CYS   B 1 133 ? 2.587   -16.883 44.583  1.00 35.44  ? 118 CYS   B SG   1 
ATOM   6405 H H    . CYS   B 1 133 ? 1.206   -19.639 44.570  1.00 34.86  ? 118 CYS   B H    1 
ATOM   6406 H HA   . CYS   B 1 133 ? 3.110   -19.037 42.880  1.00 37.86  ? 118 CYS   B HA   1 
ATOM   6407 H HB2  . CYS   B 1 133 ? 3.028   -18.838 45.688  1.00 43.22  ? 118 CYS   B HB2  1 
ATOM   6408 H HB3  . CYS   B 1 133 ? 4.305   -18.369 44.867  1.00 43.22  ? 118 CYS   B HB3  1 
ATOM   6409 H HG   . CYS   B 1 133 ? 2.918   -16.148 45.472  1.00 42.53  ? 118 CYS   B HG   1 
ATOM   6410 N N    . ARG   B 1 134 ? 3.666   -21.676 44.606  1.00 30.87  ? 119 ARG   B N    1 
ATOM   6411 C CA   . ARG   B 1 134 ? 4.517   -22.861 44.644  1.00 28.77  ? 119 ARG   B CA   1 
ATOM   6412 C C    . ARG   B 1 134 ? 4.554   -23.545 43.281  1.00 29.94  ? 119 ARG   B C    1 
ATOM   6413 O O    . ARG   B 1 134 ? 5.629   -23.823 42.740  1.00 31.28  ? 119 ARG   B O    1 
ATOM   6414 C CB   . ARG   B 1 134 ? 4.025   -23.838 45.717  1.00 31.70  ? 119 ARG   B CB   1 
ATOM   6415 C CG   . ARG   B 1 134 ? 4.952   -25.025 45.923  1.00 31.47  ? 119 ARG   B CG   1 
ATOM   6416 C CD   . ARG   B 1 134 ? 4.353   -26.092 46.845  1.00 34.80  ? 119 ARG   B CD   1 
ATOM   6417 N NE   . ARG   B 1 134 ? 3.289   -26.848 46.197  1.00 37.24  ? 119 ARG   B NE   1 
ATOM   6418 C CZ   . ARG   B 1 134 ? 2.543   -27.758 46.803  1.00 34.96  ? 119 ARG   B CZ   1 
ATOM   6419 N NH1  . ARG   B 1 134 ? 2.727   -28.067 48.076  1.00 39.35  ? 119 ARG   B NH1  1 
ATOM   6420 N NH2  . ARG   B 1 134 ? 1.577   -28.365 46.121  1.00 41.92  ? 119 ARG   B NH2  1 
ATOM   6421 H H    . ARG   B 1 134 ? 2.998   -21.694 45.148  1.00 37.04  ? 119 ARG   B H    1 
ATOM   6422 H HA   . ARG   B 1 134 ? 5.418   -22.588 44.879  1.00 34.53  ? 119 ARG   B HA   1 
ATOM   6423 H HB2  . ARG   B 1 134 ? 3.954   -23.366 46.561  1.00 38.05  ? 119 ARG   B HB2  1 
ATOM   6424 H HB3  . ARG   B 1 134 ? 3.157   -24.181 45.454  1.00 38.05  ? 119 ARG   B HB3  1 
ATOM   6425 H HG2  . ARG   B 1 134 ? 5.132   -25.438 45.064  1.00 37.77  ? 119 ARG   B HG2  1 
ATOM   6426 H HG3  . ARG   B 1 134 ? 5.780   -24.714 46.322  1.00 37.77  ? 119 ARG   B HG3  1 
ATOM   6427 H HD2  . ARG   B 1 134 ? 5.050   -26.714 47.105  1.00 41.76  ? 119 ARG   B HD2  1 
ATOM   6428 H HD3  . ARG   B 1 134 ? 3.983   -25.662 47.631  1.00 41.76  ? 119 ARG   B HD3  1 
ATOM   6429 H HE   . ARG   B 1 134 ? 3.136   -26.692 45.365  1.00 44.68  ? 119 ARG   B HE   1 
ATOM   6430 H HH11 . ARG   B 1 134 ? 3.343   -27.673 48.529  1.00 47.22  ? 119 ARG   B HH11 1 
ATOM   6431 H HH12 . ARG   B 1 134 ? 2.231   -28.662 48.450  1.00 47.22  ? 119 ARG   B HH12 1 
ATOM   6432 H HH21 . ARG   B 1 134 ? 1.443   -28.165 45.295  1.00 50.30  ? 119 ARG   B HH21 1 
ATOM   6433 H HH22 . ARG   B 1 134 ? 1.087   -28.958 46.505  1.00 50.30  ? 119 ARG   B HH22 1 
ATOM   6434 N N    . GLU   B 1 135 ? 3.377   -23.807 42.709  1.00 29.49  ? 120 GLU   B N    1 
ATOM   6435 C CA   . GLU   B 1 135 ? 3.301   -24.499 41.431  1.00 32.27  ? 120 GLU   B CA   1 
ATOM   6436 C C    . GLU   B 1 135 ? 3.932   -23.674 40.315  1.00 27.98  ? 120 GLU   B C    1 
ATOM   6437 O O    . GLU   B 1 135 ? 4.607   -24.218 39.435  1.00 28.40  ? 120 GLU   B O    1 
ATOM   6438 C CB   . GLU   B 1 135 ? 1.837   -24.822 41.115  1.00 32.30  ? 120 GLU   B CB   1 
ATOM   6439 C CG   . GLU   B 1 135 ? 1.152   -25.697 42.169  1.00 32.07  ? 120 GLU   B CG   1 
ATOM   6440 C CD   . GLU   B 1 135 ? 1.826   -27.047 42.316  1.00 36.00  ? 120 GLU   B CD   1 
ATOM   6441 O OE1  . GLU   B 1 135 ? 1.766   -27.847 41.357  1.00 31.59  ? 120 GLU   B OE1  1 
ATOM   6442 O OE2  . GLU   B 1 135 ? 2.440   -27.299 43.378  1.00 34.98  ? 120 GLU   B OE2  1 
ATOM   6443 H H    . GLU   B 1 135 ? 2.613   -23.594 43.042  1.00 35.39  ? 120 GLU   B H    1 
ATOM   6444 H HA   . GLU   B 1 135 ? 3.791   -25.334 41.487  1.00 38.72  ? 120 GLU   B HA   1 
ATOM   6445 H HB2  . GLU   B 1 135 ? 1.341   -23.990 41.054  1.00 38.76  ? 120 GLU   B HB2  1 
ATOM   6446 H HB3  . GLU   B 1 135 ? 1.798   -25.294 40.269  1.00 38.76  ? 120 GLU   B HB3  1 
ATOM   6447 H HG2  . GLU   B 1 135 ? 1.185   -25.247 43.027  1.00 38.49  ? 120 GLU   B HG2  1 
ATOM   6448 H HG3  . GLU   B 1 135 ? 0.230   -25.846 41.908  1.00 38.49  ? 120 GLU   B HG3  1 
ATOM   6449 N N    . VAL   B 1 136 ? 3.721   -22.357 40.326  1.00 29.15  ? 121 VAL   B N    1 
ATOM   6450 C CA   . VAL   B 1 136 ? 4.331   -21.518 39.301  1.00 30.56  ? 121 VAL   B CA   1 
ATOM   6451 C C    . VAL   B 1 136 ? 5.847   -21.544 39.434  1.00 31.10  ? 121 VAL   B C    1 
ATOM   6452 O O    . VAL   B 1 136 ? 6.571   -21.591 38.435  1.00 27.99  ? 121 VAL   B O    1 
ATOM   6453 C CB   . VAL   B 1 136 ? 3.784   -20.079 39.377  1.00 26.55  ? 121 VAL   B CB   1 
ATOM   6454 C CG1  . VAL   B 1 136 ? 4.642   -19.125 38.515  1.00 26.50  ? 121 VAL   B CG1  1 
ATOM   6455 C CG2  . VAL   B 1 136 ? 2.339   -20.051 38.918  1.00 30.39  ? 121 VAL   B CG2  1 
ATOM   6456 H H    . VAL   B 1 136 ? 3.241   -21.937 40.902  1.00 34.97  ? 121 VAL   B H    1 
ATOM   6457 H HA   . VAL   B 1 136 ? 4.094   -21.877 38.432  1.00 36.67  ? 121 VAL   B HA   1 
ATOM   6458 H HB   . VAL   B 1 136 ? 3.825   -19.771 40.296  1.00 31.86  ? 121 VAL   B HB   1 
ATOM   6459 H HG11 . VAL   B 1 136 ? 4.144   -18.308 38.356  1.00 31.80  ? 121 VAL   B HG11 1 
ATOM   6460 H HG12 . VAL   B 1 136 ? 5.464   -18.924 38.990  1.00 31.80  ? 121 VAL   B HG12 1 
ATOM   6461 H HG13 . VAL   B 1 136 ? 4.845   -19.558 37.671  1.00 31.80  ? 121 VAL   B HG13 1 
ATOM   6462 H HG21 . VAL   B 1 136 ? 1.987   -19.155 39.039  1.00 36.47  ? 121 VAL   B HG21 1 
ATOM   6463 H HG22 . VAL   B 1 136 ? 2.300   -20.298 37.981  1.00 36.47  ? 121 VAL   B HG22 1 
ATOM   6464 H HG23 . VAL   B 1 136 ? 1.827   -20.681 39.449  1.00 36.47  ? 121 VAL   B HG23 1 
ATOM   6465 N N    . LEU   B 1 137 ? 6.351   -21.517 40.669  1.00 32.18  ? 122 LEU   B N    1 
ATOM   6466 C CA   . LEU   B 1 137 ? 7.794   -21.571 40.870  1.00 30.54  ? 122 LEU   B CA   1 
ATOM   6467 C C    . LEU   B 1 137 ? 8.372   -22.892 40.377  1.00 29.58  ? 122 LEU   B C    1 
ATOM   6468 O O    . LEU   B 1 137 ? 9.476   -22.922 39.821  1.00 35.71  ? 122 LEU   B O    1 
ATOM   6469 C CB   . LEU   B 1 137 ? 8.123   -21.363 42.344  1.00 31.85  ? 122 LEU   B CB   1 
ATOM   6470 C CG   . LEU   B 1 137 ? 8.045   -19.915 42.834  1.00 32.32  ? 122 LEU   B CG   1 
ATOM   6471 C CD1  . LEU   B 1 137 ? 8.051   -19.890 44.358  1.00 29.92  ? 122 LEU   B CD1  1 
ATOM   6472 C CD2  . LEU   B 1 137 ? 9.199   -19.105 42.271  1.00 29.70  ? 122 LEU   B CD2  1 
ATOM   6473 H H    . LEU   B 1 137 ? 5.887   -21.468 41.392  1.00 38.62  ? 122 LEU   B H    1 
ATOM   6474 H HA   . LEU   B 1 137 ? 8.206   -20.855 40.362  1.00 36.65  ? 122 LEU   B HA   1 
ATOM   6475 H HB2  . LEU   B 1 137 ? 7.497   -21.883 42.872  1.00 38.22  ? 122 LEU   B HB2  1 
ATOM   6476 H HB3  . LEU   B 1 137 ? 9.028   -21.674 42.501  1.00 38.22  ? 122 LEU   B HB3  1 
ATOM   6477 H HG   . LEU   B 1 137 ? 7.221   -19.506 42.526  1.00 38.78  ? 122 LEU   B HG   1 
ATOM   6478 H HD11 . LEU   B 1 137 ? 8.017   -18.968 44.659  1.00 35.90  ? 122 LEU   B HD11 1 
ATOM   6479 H HD12 . LEU   B 1 137 ? 7.276   -20.374 44.685  1.00 35.90  ? 122 LEU   B HD12 1 
ATOM   6480 H HD13 . LEU   B 1 137 ? 8.863   -20.312 44.678  1.00 35.90  ? 122 LEU   B HD13 1 
ATOM   6481 H HD21 . LEU   B 1 137 ? 9.195   -18.225 42.679  1.00 35.64  ? 122 LEU   B HD21 1 
ATOM   6482 H HD22 . LEU   B 1 137 ? 10.032  -19.559 42.472  1.00 35.64  ? 122 LEU   B HD22 1 
ATOM   6483 H HD23 . LEU   B 1 137 ? 9.089   -19.025 41.310  1.00 35.64  ? 122 LEU   B HD23 1 
ATOM   6484 N N    . GLN   B 1 138 ? 7.654   -24.000 40.583  1.00 29.67  ? 123 GLN   B N    1 
ATOM   6485 C CA   . GLN   B 1 138 ? 8.125   -25.290 40.086  1.00 31.18  ? 123 GLN   B CA   1 
ATOM   6486 C C    . GLN   B 1 138 ? 8.246   -25.260 38.566  1.00 31.39  ? 123 GLN   B C    1 
ATOM   6487 O O    . GLN   B 1 138 ? 9.269   -25.664 38.003  1.00 33.45  ? 123 GLN   B O    1 
ATOM   6488 C CB   . GLN   B 1 138 ? 7.184   -26.407 40.553  1.00 31.09  ? 123 GLN   B CB   1 
ATOM   6489 C CG   . GLN   B 1 138 ? 7.230   -26.640 42.068  1.00 31.39  ? 123 GLN   B CG   1 
ATOM   6490 C CD   . GLN   B 1 138 ? 6.079   -27.476 42.607  1.00 33.01  ? 123 GLN   B CD   1 
ATOM   6491 O OE1  . GLN   B 1 138 ? 5.192   -27.909 41.868  1.00 35.07  ? 123 GLN   B OE1  1 
ATOM   6492 N NE2  . GLN   B 1 138 ? 6.083   -27.693 43.915  1.00 38.03  ? 123 GLN   B NE2  1 
ATOM   6493 H H    . GLN   B 1 138 ? 6.903   -24.029 41.002  1.00 35.60  ? 123 GLN   B H    1 
ATOM   6494 H HA   . GLN   B 1 138 ? 9.003   -25.480 40.453  1.00 37.42  ? 123 GLN   B HA   1 
ATOM   6495 H HB2  . GLN   B 1 138 ? 6.274   -26.171 40.314  1.00 37.30  ? 123 GLN   B HB2  1 
ATOM   6496 H HB3  . GLN   B 1 138 ? 7.438   -27.235 40.116  1.00 37.30  ? 123 GLN   B HB3  1 
ATOM   6497 H HG2  . GLN   B 1 138 ? 8.055   -27.100 42.287  1.00 37.67  ? 123 GLN   B HG2  1 
ATOM   6498 H HG3  . GLN   B 1 138 ? 7.201   -25.779 42.515  1.00 37.67  ? 123 GLN   B HG3  1 
ATOM   6499 H HE21 . GLN   B 1 138 ? 6.712   -27.367 44.402  1.00 45.63  ? 123 GLN   B HE21 1 
ATOM   6500 H HE22 . GLN   B 1 138 ? 5.457   -28.159 44.275  1.00 45.63  ? 123 GLN   B HE22 1 
ATOM   6501 N N    . GLY   B 1 139 ? 7.225   -24.745 37.886  1.00 29.88  ? 124 GLY   B N    1 
ATOM   6502 C CA   . GLY   B 1 139 ? 7.318   -24.599 36.445  1.00 30.10  ? 124 GLY   B CA   1 
ATOM   6503 C C    . GLY   B 1 139 ? 8.426   -23.651 36.027  1.00 36.37  ? 124 GLY   B C    1 
ATOM   6504 O O    . GLY   B 1 139 ? 9.135   -23.901 35.048  1.00 39.76  ? 124 GLY   B O    1 
ATOM   6505 H H    . GLY   B 1 139 ? 6.483   -24.478 38.231  1.00 35.86  ? 124 GLY   B H    1 
ATOM   6506 H HA2  . GLY   B 1 139 ? 7.491   -25.466 36.046  1.00 36.12  ? 124 GLY   B HA2  1 
ATOM   6507 H HA3  . GLY   B 1 139 ? 6.478   -24.255 36.103  1.00 36.12  ? 124 GLY   B HA3  1 
ATOM   6508 N N    . LEU   B 1 140 ? 8.601   -22.554 36.768  1.00 31.13  ? 125 LEU   B N    1 
ATOM   6509 C CA   . LEU   B 1 140 ? 9.664   -21.611 36.431  1.00 36.13  ? 125 LEU   B CA   1 
ATOM   6510 C C    . LEU   B 1 140 ? 11.033  -22.250 36.617  1.00 31.58  ? 125 LEU   B C    1 
ATOM   6511 O O    . LEU   B 1 140 ? 11.891  -22.171 35.733  1.00 38.53  ? 125 LEU   B O    1 
ATOM   6512 C CB   . LEU   B 1 140 ? 9.546   -20.344 37.275  1.00 29.99  ? 125 LEU   B CB   1 
ATOM   6513 C CG   . LEU   B 1 140 ? 8.436   -19.355 36.899  1.00 29.42  ? 125 LEU   B CG   1 
ATOM   6514 C CD1  . LEU   B 1 140 ? 8.487   -18.133 37.801  1.00 29.97  ? 125 LEU   B CD1  1 
ATOM   6515 C CD2  . LEU   B 1 140 ? 8.531   -18.936 35.455  1.00 35.94  ? 125 LEU   B CD2  1 
ATOM   6516 H H    . LEU   B 1 140 ? 8.130   -22.340 37.455  1.00 37.35  ? 125 LEU   B H    1 
ATOM   6517 H HA   . LEU   B 1 140 ? 9.565   -21.356 35.500  1.00 43.35  ? 125 LEU   B HA   1 
ATOM   6518 H HB2  . LEU   B 1 140 ? 9.387   -20.611 38.194  1.00 35.99  ? 125 LEU   B HB2  1 
ATOM   6519 H HB3  . LEU   B 1 140 ? 10.387  -19.864 37.210  1.00 35.99  ? 125 LEU   B HB3  1 
ATOM   6520 H HG   . LEU   B 1 140 ? 7.582   -19.799 37.019  1.00 35.31  ? 125 LEU   B HG   1 
ATOM   6521 H HD11 . LEU   B 1 140 ? 7.768   -17.529 37.557  1.00 35.96  ? 125 LEU   B HD11 1 
ATOM   6522 H HD12 . LEU   B 1 140 ? 8.382   -18.417 38.723  1.00 35.96  ? 125 LEU   B HD12 1 
ATOM   6523 H HD13 . LEU   B 1 140 ? 9.343   -17.691 37.687  1.00 35.96  ? 125 LEU   B HD13 1 
ATOM   6524 H HD21 . LEU   B 1 140 ? 7.961   -18.165 35.311  1.00 43.13  ? 125 LEU   B HD21 1 
ATOM   6525 H HD22 . LEU   B 1 140 ? 9.452   -18.708 35.252  1.00 43.13  ? 125 LEU   B HD22 1 
ATOM   6526 H HD23 . LEU   B 1 140 ? 8.241   -19.671 34.893  1.00 43.13  ? 125 LEU   B HD23 1 
ATOM   6527 N N    . ALA   B 1 141 ? 11.261  -22.882 37.768  1.00 32.21  ? 126 ALA   B N    1 
ATOM   6528 C CA   . ALA   B 1 141 ? 12.534  -23.548 38.001  1.00 36.38  ? 126 ALA   B CA   1 
ATOM   6529 C C    . ALA   B 1 141 ? 12.879  -24.473 36.843  1.00 39.38  ? 126 ALA   B C    1 
ATOM   6530 O O    . ALA   B 1 141 ? 14.037  -24.544 36.415  1.00 38.01  ? 126 ALA   B O    1 
ATOM   6531 C CB   . ALA   B 1 141 ? 12.484  -24.327 39.313  1.00 33.44  ? 126 ALA   B CB   1 
ATOM   6532 H H    . ALA   B 1 141 ? 10.702  -22.938 38.419  1.00 38.65  ? 126 ALA   B H    1 
ATOM   6533 H HA   . ALA   B 1 141 ? 13.234  -22.881 38.078  1.00 43.66  ? 126 ALA   B HA   1 
ATOM   6534 H HB1  . ALA   B 1 141 ? 13.340  -24.762 39.456  1.00 40.13  ? 126 ALA   B HB1  1 
ATOM   6535 H HB2  . ALA   B 1 141 ? 12.301  -23.711 40.040  1.00 40.13  ? 126 ALA   B HB2  1 
ATOM   6536 H HB3  . ALA   B 1 141 ? 11.781  -24.993 39.259  1.00 40.13  ? 126 ALA   B HB3  1 
ATOM   6537 N N    . TYR   B 1 142 ? 11.876  -25.170 36.307  1.00 36.98  ? 127 TYR   B N    1 
ATOM   6538 C CA   . TYR   B 1 142 ? 12.106  -26.070 35.184  1.00 43.51  ? 127 TYR   B CA   1 
ATOM   6539 C C    . TYR   B 1 142 ? 12.448  -25.288 33.920  1.00 44.75  ? 127 TYR   B C    1 
ATOM   6540 O O    . TYR   B 1 142 ? 13.439  -25.585 33.242  1.00 38.73  ? 127 TYR   B O    1 
ATOM   6541 C CB   . TYR   B 1 142 ? 10.875  -26.950 34.959  1.00 38.54  ? 127 TYR   B CB   1 
ATOM   6542 C CG   . TYR   B 1 142 ? 10.913  -27.696 33.647  1.00 49.38  ? 127 TYR   B CG   1 
ATOM   6543 C CD1  . TYR   B 1 142 ? 11.632  -28.877 33.518  1.00 47.42  ? 127 TYR   B CD1  1 
ATOM   6544 C CD2  . TYR   B 1 142 ? 10.244  -27.211 32.531  1.00 52.14  ? 127 TYR   B CD2  1 
ATOM   6545 C CE1  . TYR   B 1 142 ? 11.680  -29.561 32.313  1.00 52.75  ? 127 TYR   B CE1  1 
ATOM   6546 C CE2  . TYR   B 1 142 ? 10.287  -27.890 31.317  1.00 55.50  ? 127 TYR   B CE2  1 
ATOM   6547 C CZ   . TYR   B 1 142 ? 11.006  -29.063 31.218  1.00 54.89  ? 127 TYR   B CZ   1 
ATOM   6548 O OH   . TYR   B 1 142 ? 11.049  -29.737 30.018  1.00 58.45  ? 127 TYR   B OH   1 
ATOM   6549 H H    . TYR   B 1 142 ? 11.059  -25.138 36.574  1.00 44.38  ? 127 TYR   B H    1 
ATOM   6550 H HA   . TYR   B 1 142 ? 12.855  -26.650 35.392  1.00 52.22  ? 127 TYR   B HA   1 
ATOM   6551 H HB2  . TYR   B 1 142 ? 10.821  -27.603 35.674  1.00 46.25  ? 127 TYR   B HB2  1 
ATOM   6552 H HB3  . TYR   B 1 142 ? 10.083  -26.389 34.962  1.00 46.25  ? 127 TYR   B HB3  1 
ATOM   6553 H HD1  . TYR   B 1 142 ? 12.091  -29.215 34.254  1.00 56.90  ? 127 TYR   B HD1  1 
ATOM   6554 H HD2  . TYR   B 1 142 ? 9.760   -26.420 32.595  1.00 62.57  ? 127 TYR   B HD2  1 
ATOM   6555 H HE1  . TYR   B 1 142 ? 12.165  -30.352 32.244  1.00 63.30  ? 127 TYR   B HE1  1 
ATOM   6556 H HE2  . TYR   B 1 142 ? 9.835   -27.555 30.577  1.00 66.60  ? 127 TYR   B HE2  1 
ATOM   6557 H HH   . TYR   B 1 142 ? 10.587  -29.332 29.445  1.00 70.14  ? 127 TYR   B HH   1 
ATOM   6558 N N    . LEU   B 1 143 ? 11.644  -24.273 33.594  1.00 47.99  ? 128 LEU   B N    1 
ATOM   6559 C CA   . LEU   B 1 143 ? 11.899  -23.487 32.393  1.00 37.56  ? 128 LEU   B CA   1 
ATOM   6560 C C    . LEU   B 1 143 ? 13.285  -22.861 32.426  1.00 41.27  ? 128 LEU   B C    1 
ATOM   6561 O O    . LEU   B 1 143 ? 14.008  -22.877 31.420  1.00 43.06  ? 128 LEU   B O    1 
ATOM   6562 C CB   . LEU   B 1 143 ? 10.832  -22.406 32.241  1.00 34.36  ? 128 LEU   B CB   1 
ATOM   6563 C CG   . LEU   B 1 143 ? 9.465   -22.896 31.772  1.00 36.29  ? 128 LEU   B CG   1 
ATOM   6564 C CD1  . LEU   B 1 143 ? 8.459   -21.786 31.943  1.00 32.89  ? 128 LEU   B CD1  1 
ATOM   6565 C CD2  . LEU   B 1 143 ? 9.507   -23.376 30.319  1.00 36.28  ? 128 LEU   B CD2  1 
ATOM   6566 H H    . LEU   B 1 143 ? 10.955  -24.025 34.046  1.00 57.59  ? 128 LEU   B H    1 
ATOM   6567 H HA   . LEU   B 1 143 ? 11.851  -24.073 31.622  1.00 45.08  ? 128 LEU   B HA   1 
ATOM   6568 H HB2  . LEU   B 1 143 ? 10.707  -21.978 33.103  1.00 41.23  ? 128 LEU   B HB2  1 
ATOM   6569 H HB3  . LEU   B 1 143 ? 11.146  -21.757 31.592  1.00 41.23  ? 128 LEU   B HB3  1 
ATOM   6570 H HG   . LEU   B 1 143 ? 9.194   -23.659 32.307  1.00 43.55  ? 128 LEU   B HG   1 
ATOM   6571 H HD11 . LEU   B 1 143 ? 7.595   -22.091 31.625  1.00 39.47  ? 128 LEU   B HD11 1 
ATOM   6572 H HD12 . LEU   B 1 143 ? 8.403   -21.552 32.883  1.00 39.47  ? 128 LEU   B HD12 1 
ATOM   6573 H HD13 . LEU   B 1 143 ? 8.748   -21.016 31.428  1.00 39.47  ? 128 LEU   B HD13 1 
ATOM   6574 H HD21 . LEU   B 1 143 ? 8.605   -23.584 30.029  1.00 43.53  ? 128 LEU   B HD21 1 
ATOM   6575 H HD22 . LEU   B 1 143 ? 9.878   -22.672 29.765  1.00 43.53  ? 128 LEU   B HD22 1 
ATOM   6576 H HD23 . LEU   B 1 143 ? 10.064  -24.168 30.264  1.00 43.53  ? 128 LEU   B HD23 1 
ATOM   6577 N N    . HIS   B 1 144 ? 13.668  -22.293 33.569  1.00 34.80  ? 129 HIS   B N    1 
ATOM   6578 C CA   . HIS   B 1 144 ? 14.983  -21.674 33.684  1.00 37.64  ? 129 HIS   B CA   1 
ATOM   6579 C C    . HIS   B 1 144 ? 16.097  -22.702 33.532  1.00 39.33  ? 129 HIS   B C    1 
ATOM   6580 O O    . HIS   B 1 144 ? 17.148  -22.408 32.952  1.00 39.99  ? 129 HIS   B O    1 
ATOM   6581 C CB   . HIS   B 1 144 ? 15.088  -20.945 35.023  1.00 37.23  ? 129 HIS   B CB   1 
ATOM   6582 C CG   . HIS   B 1 144 ? 14.092  -19.840 35.177  1.00 35.05  ? 129 HIS   B CG   1 
ATOM   6583 N ND1  . HIS   B 1 144 ? 13.913  -19.154 36.358  1.00 40.44  ? 129 HIS   B ND1  1 
ATOM   6584 C CD2  . HIS   B 1 144 ? 13.217  -19.303 34.295  1.00 33.45  ? 129 HIS   B CD2  1 
ATOM   6585 C CE1  . HIS   B 1 144 ? 12.972  -18.240 36.196  1.00 35.34  ? 129 HIS   B CE1  1 
ATOM   6586 N NE2  . HIS   B 1 144 ? 12.535  -18.308 34.952  1.00 36.58  ? 129 HIS   B NE2  1 
ATOM   6587 H H    . HIS   B 1 144 ? 13.190  -22.254 34.283  1.00 41.76  ? 129 HIS   B H    1 
ATOM   6588 H HA   . HIS   B 1 144 ? 15.093  -21.021 32.975  1.00 45.17  ? 129 HIS   B HA   1 
ATOM   6589 H HB2  . HIS   B 1 144 ? 14.939  -21.582 35.740  1.00 44.67  ? 129 HIS   B HB2  1 
ATOM   6590 H HB3  . HIS   B 1 144 ? 15.975  -20.560 35.102  1.00 44.67  ? 129 HIS   B HB3  1 
ATOM   6591 H HD1  . HIS   B 1 144 ? 14.345  -19.298 37.088  1.00 48.53  ? 129 HIS   B HD1  1 
ATOM   6592 H HD2  . HIS   B 1 144 ? 13.100  -19.560 33.408  1.00 40.13  ? 129 HIS   B HD2  1 
ATOM   6593 H HE1  . HIS   B 1 144 ? 12.670  -17.649 36.848  1.00 42.41  ? 129 HIS   B HE1  1 
ATOM   6594 H HE2  . HIS   B 1 144 ? 11.923  -17.811 34.609  1.00 43.89  ? 129 HIS   B HE2  1 
ATOM   6595 N N    . SER   B 1 145 ? 15.887  -23.918 34.043  1.00 38.13  ? 130 SER   B N    1 
ATOM   6596 C CA   . SER   B 1 145 ? 16.889  -24.962 33.862  1.00 40.74  ? 130 SER   B CA   1 
ATOM   6597 C C    . SER   B 1 145 ? 17.083  -25.291 32.388  1.00 44.69  ? 130 SER   B C    1 
ATOM   6598 O O    . SER   B 1 145 ? 18.195  -25.627 31.970  1.00 48.65  ? 130 SER   B O    1 
ATOM   6599 C CB   . SER   B 1 145 ? 16.490  -26.216 34.637  1.00 40.40  ? 130 SER   B CB   1 
ATOM   6600 O OG   . SER   B 1 145 ? 15.371  -26.842 34.039  1.00 46.04  ? 130 SER   B OG   1 
ATOM   6601 H H    . SER   B 1 145 ? 15.189  -24.156 34.486  1.00 45.75  ? 130 SER   B H    1 
ATOM   6602 H HA   . SER   B 1 145 ? 17.735  -24.650 34.219  1.00 48.89  ? 130 SER   B HA   1 
ATOM   6603 H HB2  . SER   B 1 145 ? 17.236  -26.836 34.638  1.00 48.48  ? 130 SER   B HB2  1 
ATOM   6604 H HB3  . SER   B 1 145 ? 16.264  -25.967 35.546  1.00 48.48  ? 130 SER   B HB3  1 
ATOM   6605 H HG   . SER   B 1 145 ? 14.706  -26.329 34.066  1.00 55.24  ? 130 SER   B HG   1 
ATOM   6606 N N    . GLN   B 1 146 ? 16.021  -25.201 31.587  1.00 46.82  ? 131 GLN   B N    1 
ATOM   6607 C CA   . GLN   B 1 146 ? 16.125  -25.341 30.140  1.00 45.41  ? 131 GLN   B CA   1 
ATOM   6608 C C    . GLN   B 1 146 ? 16.640  -24.070 29.465  1.00 42.99  ? 131 GLN   B C    1 
ATOM   6609 O O    . GLN   B 1 146 ? 16.595  -23.976 28.234  1.00 47.19  ? 131 GLN   B O    1 
ATOM   6610 C CB   . GLN   B 1 146 ? 14.764  -25.715 29.540  1.00 49.43  ? 131 GLN   B CB   1 
ATOM   6611 C CG   . GLN   B 1 146 ? 14.079  -26.907 30.193  1.00 54.34  ? 131 GLN   B CG   1 
ATOM   6612 C CD   . GLN   B 1 146 ? 14.829  -28.194 29.995  1.00 63.48  ? 131 GLN   B CD   1 
ATOM   6613 O OE1  . GLN   B 1 146 ? 15.299  -28.803 30.957  1.00 64.95  ? 131 GLN   B OE1  1 
ATOM   6614 N NE2  . GLN   B 1 146 ? 14.941  -28.629 28.743  1.00 66.53  ? 131 GLN   B NE2  1 
ATOM   6615 H H    . GLN   B 1 146 ? 15.220  -25.058 31.865  1.00 56.18  ? 131 GLN   B H    1 
ATOM   6616 H HA   . GLN   B 1 146 ? 16.744  -26.063 29.948  1.00 54.49  ? 131 GLN   B HA   1 
ATOM   6617 H HB2  . GLN   B 1 146 ? 14.170  -24.953 29.628  1.00 59.32  ? 131 GLN   B HB2  1 
ATOM   6618 H HB3  . GLN   B 1 146 ? 14.890  -25.930 28.602  1.00 59.32  ? 131 GLN   B HB3  1 
ATOM   6619 H HG2  . GLN   B 1 146 ? 14.009  -26.746 31.147  1.00 65.21  ? 131 GLN   B HG2  1 
ATOM   6620 H HG3  . GLN   B 1 146 ? 13.196  -27.013 29.808  1.00 65.21  ? 131 GLN   B HG3  1 
ATOM   6621 H HE21 . GLN   B 1 146 ? 14.594  -28.179 28.099  1.00 79.83  ? 131 GLN   B HE21 1 
ATOM   6622 H HE22 . GLN   B 1 146 ? 15.362  -29.361 28.579  1.00 79.83  ? 131 GLN   B HE22 1 
ATOM   6623 N N    . LYS   B 1 147 ? 17.122  -23.097 30.241  1.00 46.43  ? 132 LYS   B N    1 
ATOM   6624 C CA   . LYS   B 1 147 ? 17.598  -21.820 29.706  1.00 47.29  ? 132 LYS   B CA   1 
ATOM   6625 C C    . LYS   B 1 147 ? 16.486  -21.090 28.952  1.00 44.61  ? 132 LYS   B C    1 
ATOM   6626 O O    . LYS   B 1 147 ? 16.706  -20.501 27.891  1.00 42.78  ? 132 LYS   B O    1 
ATOM   6627 C CB   . LYS   B 1 147 ? 18.826  -22.022 28.814  1.00 55.17  ? 132 LYS   B CB   1 
ATOM   6628 C CG   . LYS   B 1 147 ? 20.058  -22.547 29.558  1.00 56.64  ? 132 LYS   B CG   1 
ATOM   6629 C CD   . LYS   B 1 147 ? 20.568  -21.542 30.594  1.00 64.85  ? 132 LYS   B CD   1 
ATOM   6630 C CE   . LYS   B 1 147 ? 21.707  -22.114 31.431  1.00 68.67  ? 132 LYS   B CE   1 
ATOM   6631 N NZ   . LYS   B 1 147 ? 21.251  -23.242 32.301  1.00 67.76  ? 132 LYS   B NZ   1 
ATOM   6632 H H    . LYS   B 1 147 ? 17.184  -23.153 31.097  1.00 55.72  ? 132 LYS   B H    1 
ATOM   6633 H HA   . LYS   B 1 147 ? 17.861  -21.253 30.448  1.00 56.75  ? 132 LYS   B HA   1 
ATOM   6634 H HB2  . LYS   B 1 147 ? 18.605  -22.664 28.122  1.00 66.20  ? 132 LYS   B HB2  1 
ATOM   6635 H HB3  . LYS   B 1 147 ? 19.063  -21.171 28.415  1.00 66.20  ? 132 LYS   B HB3  1 
ATOM   6636 H HG2  . LYS   B 1 147 ? 19.828  -23.368 30.019  1.00 67.97  ? 132 LYS   B HG2  1 
ATOM   6637 H HG3  . LYS   B 1 147 ? 20.770  -22.713 28.920  1.00 67.97  ? 132 LYS   B HG3  1 
ATOM   6638 H HD2  . LYS   B 1 147 ? 20.895  -20.751 30.137  1.00 77.82  ? 132 LYS   B HD2  1 
ATOM   6639 H HD3  . LYS   B 1 147 ? 19.842  -21.304 31.192  1.00 77.82  ? 132 LYS   B HD3  1 
ATOM   6640 H HE2  . LYS   B 1 147 ? 22.400  -22.447 30.841  1.00 82.40  ? 132 LYS   B HE2  1 
ATOM   6641 H HE3  . LYS   B 1 147 ? 22.064  -21.416 32.002  1.00 82.40  ? 132 LYS   B HE3  1 
ATOM   6642 H HZ1  . LYS   B 1 147 ? 21.931  -23.542 32.792  1.00 81.31  ? 132 LYS   B HZ1  1 
ATOM   6643 H HZ2  . LYS   B 1 147 ? 20.603  -22.965 32.844  1.00 81.31  ? 132 LYS   B HZ2  1 
ATOM   6644 H HZ3  . LYS   B 1 147 ? 20.942  -23.909 31.799  1.00 81.31  ? 132 LYS   B HZ3  1 
ATOM   6645 N N    . LYS   B 1 148 ? 15.283  -21.120 29.514  1.00 42.87  ? 133 LYS   B N    1 
ATOM   6646 C CA   . LYS   B 1 148 ? 14.133  -20.430 28.956  1.00 48.08  ? 133 LYS   B CA   1 
ATOM   6647 C C    . LYS   B 1 148 ? 13.626  -19.386 29.938  1.00 39.89  ? 133 LYS   B C    1 
ATOM   6648 O O    . LYS   B 1 148 ? 13.824  -19.491 31.151  1.00 49.01  ? 133 LYS   B O    1 
ATOM   6649 C CB   . LYS   B 1 148 ? 12.996  -21.402 28.621  1.00 44.95  ? 133 LYS   B CB   1 
ATOM   6650 C CG   . LYS   B 1 148 ? 12.985  -21.842 27.179  1.00 51.04  ? 133 LYS   B CG   1 
ATOM   6651 C CD   . LYS   B 1 148 ? 11.995  -22.964 26.940  1.00 47.30  ? 133 LYS   B CD   1 
ATOM   6652 C CE   . LYS   B 1 148 ? 12.622  -24.058 26.082  1.00 59.64  ? 133 LYS   B CE   1 
ATOM   6653 N NZ   . LYS   B 1 148 ? 11.631  -25.087 25.656  1.00 59.78  ? 133 LYS   B NZ   1 
ATOM   6654 H H    . LYS   B 1 148 ? 15.106  -21.547 30.240  1.00 51.44  ? 133 LYS   B H    1 
ATOM   6655 H HA   . LYS   B 1 148 ? 14.403  -19.984 28.139  1.00 57.70  ? 133 LYS   B HA   1 
ATOM   6656 H HB2  . LYS   B 1 148 ? 13.089  -22.194 29.173  1.00 53.94  ? 133 LYS   B HB2  1 
ATOM   6657 H HB3  . LYS   B 1 148 ? 12.148  -20.967 28.806  1.00 53.94  ? 133 LYS   B HB3  1 
ATOM   6658 H HG2  . LYS   B 1 148 ? 12.735  -21.092 26.618  1.00 61.25  ? 133 LYS   B HG2  1 
ATOM   6659 H HG3  . LYS   B 1 148 ? 13.868  -22.160 26.935  1.00 61.25  ? 133 LYS   B HG3  1 
ATOM   6660 H HD2  . LYS   B 1 148 ? 11.731  -23.351 27.790  1.00 56.76  ? 133 LYS   B HD2  1 
ATOM   6661 H HD3  . LYS   B 1 148 ? 11.216  -22.617 26.477  1.00 56.76  ? 133 LYS   B HD3  1 
ATOM   6662 H HE2  . LYS   B 1 148 ? 13.002  -23.657 25.284  1.00 71.56  ? 133 LYS   B HE2  1 
ATOM   6663 H HE3  . LYS   B 1 148 ? 13.317  -24.502 26.593  1.00 71.56  ? 133 LYS   B HE3  1 
ATOM   6664 H HZ1  . LYS   B 1 148 ? 11.597  -25.744 26.256  1.00 71.74  ? 133 LYS   B HZ1  1 
ATOM   6665 H HZ2  . LYS   B 1 148 ? 10.823  -24.720 25.583  1.00 71.74  ? 133 LYS   B HZ2  1 
ATOM   6666 H HZ3  . LYS   B 1 148 ? 11.865  -25.428 24.868  1.00 71.74  ? 133 LYS   B HZ3  1 
ATOM   6667 N N    . ILE   B 1 149 ? 12.954  -18.378 29.395  1.00 43.14  ? 134 ILE   B N    1 
ATOM   6668 C CA   . ILE   B 1 149 ? 12.352  -17.311 30.179  1.00 41.35  ? 134 ILE   B CA   1 
ATOM   6669 C C    . ILE   B 1 149 ? 10.894  -17.206 29.760  1.00 41.15  ? 134 ILE   B C    1 
ATOM   6670 O O    . ILE   B 1 149 ? 10.591  -17.147 28.564  1.00 41.99  ? 134 ILE   B O    1 
ATOM   6671 C CB   . ILE   B 1 149 ? 13.079  -15.969 29.976  1.00 40.59  ? 134 ILE   B CB   1 
ATOM   6672 C CG1  . ILE   B 1 149 ? 14.573  -16.132 30.252  1.00 48.00  ? 134 ILE   B CG1  1 
ATOM   6673 C CG2  . ILE   B 1 149 ? 12.490  -14.889 30.889  1.00 45.29  ? 134 ILE   B CG2  1 
ATOM   6674 C CD1  . ILE   B 1 149 ? 15.359  -14.826 30.203  1.00 41.32  ? 134 ILE   B CD1  1 
ATOM   6675 H H    . ILE   B 1 149 ? 12.830  -18.289 28.549  1.00 51.77  ? 134 ILE   B H    1 
ATOM   6676 H HA   . ILE   B 1 149 ? 12.392  -17.530 31.123  1.00 49.62  ? 134 ILE   B HA   1 
ATOM   6677 H HB   . ILE   B 1 149 ? 12.955  -15.694 29.054  1.00 48.70  ? 134 ILE   B HB   1 
ATOM   6678 H HG12 . ILE   B 1 149 ? 14.687  -16.512 31.138  1.00 57.60  ? 134 ILE   B HG12 1 
ATOM   6679 H HG13 . ILE   B 1 149 ? 14.949  -16.728 29.586  1.00 57.60  ? 134 ILE   B HG13 1 
ATOM   6680 H HG21 . ILE   B 1 149 ? 12.851  -14.027 30.632  1.00 54.35  ? 134 ILE   B HG21 1 
ATOM   6681 H HG22 . ILE   B 1 149 ? 11.525  -14.886 30.793  1.00 54.35  ? 134 ILE   B HG22 1 
ATOM   6682 H HG23 . ILE   B 1 149 ? 12.730  -15.088 31.808  1.00 54.35  ? 134 ILE   B HG23 1 
ATOM   6683 H HD11 . ILE   B 1 149 ? 16.308  -15.028 30.192  1.00 49.59  ? 134 ILE   B HD11 1 
ATOM   6684 H HD12 . ILE   B 1 149 ? 15.115  -14.341 29.399  1.00 49.59  ? 134 ILE   B HD12 1 
ATOM   6685 H HD13 . ILE   B 1 149 ? 15.143  -14.298 30.987  1.00 49.59  ? 134 ILE   B HD13 1 
ATOM   6686 N N    . HIS   B 1 150 ? 9.991   -17.191 30.740  1.00 34.60  ? 135 HIS   B N    1 
ATOM   6687 C CA   . HIS   B 1 150 ? 8.572   -17.108 30.417  1.00 40.33  ? 135 HIS   B CA   1 
ATOM   6688 C C    . HIS   B 1 150 ? 8.218   -15.725 29.876  1.00 30.30  ? 135 HIS   B C    1 
ATOM   6689 O O    . HIS   B 1 150 ? 7.518   -15.604 28.868  1.00 33.38  ? 135 HIS   B O    1 
ATOM   6690 C CB   . HIS   B 1 150 ? 7.730   -17.443 31.647  1.00 35.66  ? 135 HIS   B CB   1 
ATOM   6691 C CG   . HIS   B 1 150 ? 6.261   -17.535 31.373  1.00 34.56  ? 135 HIS   B CG   1 
ATOM   6692 N ND1  . HIS   B 1 150 ? 5.469   -16.427 31.165  1.00 32.83  ? 135 HIS   B ND1  1 
ATOM   6693 C CD2  . HIS   B 1 150 ? 5.438   -18.607 31.281  1.00 33.63  ? 135 HIS   B CD2  1 
ATOM   6694 C CE1  . HIS   B 1 150 ? 4.224   -16.811 30.950  1.00 32.70  ? 135 HIS   B CE1  1 
ATOM   6695 N NE2  . HIS   B 1 150 ? 4.178   -18.130 31.013  1.00 37.77  ? 135 HIS   B NE2  1 
ATOM   6696 H H    . HIS   B 1 150 ? 10.171  -17.226 31.580  1.00 41.52  ? 135 HIS   B H    1 
ATOM   6697 H HA   . HIS   B 1 150 ? 8.366   -17.764 29.731  1.00 48.40  ? 135 HIS   B HA   1 
ATOM   6698 H HB2  . HIS   B 1 150 ? 8.019   -18.299 31.999  1.00 42.80  ? 135 HIS   B HB2  1 
ATOM   6699 H HB3  . HIS   B 1 150 ? 7.862   -16.749 32.313  1.00 42.80  ? 135 HIS   B HB3  1 
ATOM   6700 H HD2  . HIS   B 1 150 ? 5.680   -19.500 31.381  1.00 40.35  ? 135 HIS   B HD2  1 
ATOM   6701 H HE1  . HIS   B 1 150 ? 3.502   -16.249 30.783  1.00 39.24  ? 135 HIS   B HE1  1 
ATOM   6702 H HE2  . HIS   B 1 150 ? 3.473   -18.611 30.905  1.00 45.33  ? 135 HIS   B HE2  1 
ATOM   6703 N N    . ARG   B 1 151 ? 8.673   -14.676 30.559  1.00 36.54  ? 136 ARG   B N    1 
ATOM   6704 C CA   . ARG   B 1 151 ? 8.610   -13.277 30.168  1.00 36.68  ? 136 ARG   B CA   1 
ATOM   6705 C C    . ARG   B 1 151 ? 7.227   -12.658 30.377  1.00 36.24  ? 136 ARG   B C    1 
ATOM   6706 O O    . ARG   B 1 151 ? 7.099   -11.433 30.261  1.00 39.80  ? 136 ARG   B O    1 
ATOM   6707 C CB   . ARG   B 1 151 ? 9.028   -13.044 28.700  1.00 35.45  ? 136 ARG   B CB   1 
ATOM   6708 C CG   . ARG   B 1 151 ? 10.431  -13.482 28.397  1.00 41.65  ? 136 ARG   B CG   1 
ATOM   6709 C CD   . ARG   B 1 151 ? 10.737  -13.369 26.900  1.00 49.28  ? 136 ARG   B CD   1 
ATOM   6710 N NE   . ARG   B 1 151 ? 11.637  -14.427 26.450  1.00 52.34  ? 136 ARG   B NE   1 
ATOM   6711 C CZ   . ARG   B 1 151 ? 12.957  -14.315 26.371  1.00 50.08  ? 136 ARG   B CZ   1 
ATOM   6712 N NH1  . ARG   B 1 151 ? 13.575  -13.184 26.668  1.00 59.34  ? 136 ARG   B NH1  1 
ATOM   6713 N NH2  . ARG   B 1 151 ? 13.673  -15.365 25.983  1.00 58.53  ? 136 ARG   B NH2  1 
ATOM   6714 H H    . ARG   B 1 151 ? 9.057   -14.767 31.322  1.00 43.85  ? 136 ARG   B H    1 
ATOM   6715 H HA   . ARG   B 1 151 ? 9.228   -12.792 30.738  1.00 44.02  ? 136 ARG   B HA   1 
ATOM   6716 H HB2  . ARG   B 1 151 ? 8.430   -13.543 28.122  1.00 42.55  ? 136 ARG   B HB2  1 
ATOM   6717 H HB3  . ARG   B 1 151 ? 8.965   -12.096 28.504  1.00 42.55  ? 136 ARG   B HB3  1 
ATOM   6718 H HG2  . ARG   B 1 151 ? 11.056  -12.920 28.880  1.00 49.98  ? 136 ARG   B HG2  1 
ATOM   6719 H HG3  . ARG   B 1 151 ? 10.544  -14.408 28.662  1.00 49.98  ? 136 ARG   B HG3  1 
ATOM   6720 H HD2  . ARG   B 1 151 ? 9.910   -13.439 26.398  1.00 59.13  ? 136 ARG   B HD2  1 
ATOM   6721 H HD3  . ARG   B 1 151 ? 11.161  -12.514 26.724  1.00 59.13  ? 136 ARG   B HD3  1 
ATOM   6722 H HE   . ARG   B 1 151 ? 11.286  -15.178 26.219  1.00 62.81  ? 136 ARG   B HE   1 
ATOM   6723 H HH11 . ARG   B 1 151 ? 13.121  -12.498 26.919  1.00 71.21  ? 136 ARG   B HH11 1 
ATOM   6724 H HH12 . ARG   B 1 151 ? 14.432  -13.134 26.609  1.00 71.21  ? 136 ARG   B HH12 1 
ATOM   6725 H HH21 . ARG   B 1 151 ? 13.280  -16.105 25.788  1.00 70.23  ? 136 ARG   B HH21 1 
ATOM   6726 H HH22 . ARG   B 1 151 ? 14.529  -15.305 25.928  1.00 70.23  ? 136 ARG   B HH22 1 
ATOM   6727 N N    . ASP   B 1 152 ? 6.190   -13.431 30.675  1.00 31.42  ? 137 ASP   B N    1 
ATOM   6728 C CA   . ASP   B 1 152 ? 4.839   -12.883 30.747  1.00 29.62  ? 137 ASP   B CA   1 
ATOM   6729 C C    . ASP   B 1 152 ? 4.046   -13.527 31.880  1.00 27.62  ? 137 ASP   B C    1 
ATOM   6730 O O    . ASP   B 1 152 ? 2.899   -13.932 31.709  1.00 27.47  ? 137 ASP   B O    1 
ATOM   6731 C CB   . ASP   B 1 152 ? 4.118   -13.064 29.413  1.00 29.72  ? 137 ASP   B CB   1 
ATOM   6732 C CG   . ASP   B 1 152 ? 3.048   -12.015 29.173  1.00 38.78  ? 137 ASP   B CG   1 
ATOM   6733 O OD1  . ASP   B 1 152 ? 2.974   -11.040 29.952  1.00 42.74  ? 137 ASP   B OD1  1 
ATOM   6734 O OD2  . ASP   B 1 152 ? 2.278   -12.165 28.202  1.00 38.52  ? 137 ASP   B OD2  1 
ATOM   6735 H H    . ASP   B 1 152 ? 6.243   -14.274 30.840  1.00 37.71  ? 137 ASP   B H    1 
ATOM   6736 H HA   . ASP   B 1 152 ? 4.912   -11.936 30.948  1.00 35.54  ? 137 ASP   B HA   1 
ATOM   6737 H HB2  . ASP   B 1 152 ? 4.765   -13.001 28.693  1.00 35.66  ? 137 ASP   B HB2  1 
ATOM   6738 H HB3  . ASP   B 1 152 ? 3.691   -13.935 29.400  1.00 35.66  ? 137 ASP   B HB3  1 
ATOM   6739 N N    . ILE   B 1 153 ? 4.645   -13.607 33.060  1.00 27.27  ? 138 ILE   B N    1 
ATOM   6740 C CA   . ILE   B 1 153 ? 3.957   -14.187 34.214  1.00 26.74  ? 138 ILE   B CA   1 
ATOM   6741 C C    . ILE   B 1 153 ? 2.946   -13.184 34.756  1.00 36.51  ? 138 ILE   B C    1 
ATOM   6742 O O    . ILE   B 1 153 ? 3.289   -12.032 35.063  1.00 28.55  ? 138 ILE   B O    1 
ATOM   6743 C CB   . ILE   B 1 153 ? 4.970   -14.598 35.298  1.00 27.28  ? 138 ILE   B CB   1 
ATOM   6744 C CG1  . ILE   B 1 153 ? 5.858   -15.742 34.795  1.00 26.98  ? 138 ILE   B CG1  1 
ATOM   6745 C CG2  . ILE   B 1 153 ? 4.245   -15.004 36.569  1.00 29.00  ? 138 ILE   B CG2  1 
ATOM   6746 C CD1  . ILE   B 1 153 ? 5.117   -17.072 34.635  1.00 34.85  ? 138 ILE   B CD1  1 
ATOM   6747 H H    . ILE   B 1 153 ? 5.445   -13.336 33.221  1.00 32.73  ? 138 ILE   B H    1 
ATOM   6748 H HA   . ILE   B 1 153 ? 3.473   -14.978 33.929  1.00 32.08  ? 138 ILE   B HA   1 
ATOM   6749 H HB   . ILE   B 1 153 ? 5.537   -13.835 35.495  1.00 32.73  ? 138 ILE   B HB   1 
ATOM   6750 H HG12 . ILE   B 1 153 ? 6.220   -15.499 33.929  1.00 32.38  ? 138 ILE   B HG12 1 
ATOM   6751 H HG13 . ILE   B 1 153 ? 6.579   -15.880 35.430  1.00 32.38  ? 138 ILE   B HG13 1 
ATOM   6752 H HG21 . ILE   B 1 153 ? 4.850   -15.515 37.129  1.00 34.80  ? 138 ILE   B HG21 1 
ATOM   6753 H HG22 . ILE   B 1 153 ? 3.956   -14.205 37.037  1.00 34.80  ? 138 ILE   B HG22 1 
ATOM   6754 H HG23 . ILE   B 1 153 ? 3.475   -15.547 36.334  1.00 34.80  ? 138 ILE   B HG23 1 
ATOM   6755 H HD11 . ILE   B 1 153 ? 5.732   -17.736 34.286  1.00 41.81  ? 138 ILE   B HD11 1 
ATOM   6756 H HD12 . ILE   B 1 153 ? 4.783   -17.353 35.501  1.00 41.81  ? 138 ILE   B HD12 1 
ATOM   6757 H HD13 . ILE   B 1 153 ? 4.379   -16.949 34.019  1.00 41.81  ? 138 ILE   B HD13 1 
ATOM   6758 N N    . LYS   B 1 154 ? 1.692   -13.622 34.874  1.00 33.05  ? 139 LYS   B N    1 
ATOM   6759 C CA   . LYS   B 1 154 ? 0.573   -12.819 35.347  1.00 28.44  ? 139 LYS   B CA   1 
ATOM   6760 C C    . LYS   B 1 154 ? -0.655  -13.720 35.394  1.00 26.57  ? 139 LYS   B C    1 
ATOM   6761 O O    . LYS   B 1 154 ? -0.665  -14.809 34.810  1.00 28.98  ? 139 LYS   B O    1 
ATOM   6762 C CB   . LYS   B 1 154 ? 0.311   -11.609 34.445  1.00 28.53  ? 139 LYS   B CB   1 
ATOM   6763 C CG   . LYS   B 1 154 ? -0.330  -11.978 33.116  1.00 39.11  ? 139 LYS   B CG   1 
ATOM   6764 C CD   . LYS   B 1 154 ? 0.185   -11.131 31.978  1.00 35.25  ? 139 LYS   B CD   1 
ATOM   6765 C CE   . LYS   B 1 154 ? -0.151  -9.691  32.154  1.00 38.69  ? 139 LYS   B CE   1 
ATOM   6766 N NZ   . LYS   B 1 154 ? 0.195   -8.908  30.919  1.00 48.46  ? 139 LYS   B NZ   1 
ATOM   6767 H H    . LYS   B 1 154 ? 1.455   -14.424 34.675  1.00 39.66  ? 139 LYS   B H    1 
ATOM   6768 H HA   . LYS   B 1 154 ? 0.757   -12.493 36.241  1.00 34.13  ? 139 LYS   B HA   1 
ATOM   6769 H HB2  . LYS   B 1 154 ? -0.287  -10.999 34.905  1.00 34.23  ? 139 LYS   B HB2  1 
ATOM   6770 H HB3  . LYS   B 1 154 ? 1.155   -11.169 34.257  1.00 34.23  ? 139 LYS   B HB3  1 
ATOM   6771 H HG2  . LYS   B 1 154 ? -0.132  -12.906 32.914  1.00 46.93  ? 139 LYS   B HG2  1 
ATOM   6772 H HG3  . LYS   B 1 154 ? -1.289  -11.849 33.178  1.00 46.93  ? 139 LYS   B HG3  1 
ATOM   6773 H HD2  . LYS   B 1 154 ? 1.150   -11.213 31.930  1.00 42.30  ? 139 LYS   B HD2  1 
ATOM   6774 H HD3  . LYS   B 1 154 ? -0.215  -11.435 31.148  1.00 42.30  ? 139 LYS   B HD3  1 
ATOM   6775 H HE2  . LYS   B 1 154 ? -1.102  -9.598  32.322  1.00 46.43  ? 139 LYS   B HE2  1 
ATOM   6776 H HE3  . LYS   B 1 154 ? 0.354   -9.330  32.899  1.00 46.43  ? 139 LYS   B HE3  1 
ATOM   6777 H HZ1  . LYS   B 1 154 ? -0.011  -8.050  31.035  1.00 58.15  ? 139 LYS   B HZ1  1 
ATOM   6778 H HZ2  . LYS   B 1 154 ? 1.066   -8.975  30.749  1.00 58.15  ? 139 LYS   B HZ2  1 
ATOM   6779 H HZ3  . LYS   B 1 154 ? -0.261  -9.222  30.222  1.00 58.15  ? 139 LYS   B HZ3  1 
ATOM   6780 N N    . GLY   B 1 155 ? -1.690  -13.249 36.092  1.00 28.77  ? 140 GLY   B N    1 
ATOM   6781 C CA   . GLY   B 1 155 ? -2.885  -14.060 36.282  1.00 31.24  ? 140 GLY   B CA   1 
ATOM   6782 C C    . GLY   B 1 155 ? -3.496  -14.563 34.991  1.00 34.40  ? 140 GLY   B C    1 
ATOM   6783 O O    . GLY   B 1 155 ? -4.027  -15.675 34.938  1.00 27.44  ? 140 GLY   B O    1 
ATOM   6784 H H    . GLY   B 1 155 ? -1.724  -12.473 36.461  1.00 34.52  ? 140 GLY   B H    1 
ATOM   6785 H HA2  . GLY   B 1 155 ? -2.659  -14.831 36.826  1.00 37.49  ? 140 GLY   B HA2  1 
ATOM   6786 H HA3  . GLY   B 1 155 ? -3.554  -13.532 36.745  1.00 37.49  ? 140 GLY   B HA3  1 
ATOM   6787 N N    . ALA   B 1 156 ? -3.420  -13.758 33.929  1.00 31.52  ? 141 ALA   B N    1 
ATOM   6788 C CA   . ALA   B 1 156 ? -4.008  -14.109 32.641  1.00 28.27  ? 141 ALA   B CA   1 
ATOM   6789 C C    . ALA   B 1 156 ? -3.282  -15.269 31.967  1.00 29.93  ? 141 ALA   B C    1 
ATOM   6790 O O    . ALA   B 1 156 ? -3.860  -15.920 31.092  1.00 29.04  ? 141 ALA   B O    1 
ATOM   6791 C CB   . ALA   B 1 156 ? -4.006  -12.874 31.721  1.00 28.77  ? 141 ALA   B CB   1 
ATOM   6792 H H    . ALA   B 1 156 ? -3.029  -12.992 33.930  1.00 37.82  ? 141 ALA   B H    1 
ATOM   6793 H HA   . ALA   B 1 156 ? -4.928  -14.383 32.776  1.00 33.93  ? 141 ALA   B HA   1 
ATOM   6794 H HB1  . ALA   B 1 156 ? -4.396  -13.115 30.866  1.00 34.52  ? 141 ALA   B HB1  1 
ATOM   6795 H HB2  . ALA   B 1 156 ? -4.528  -12.170 32.136  1.00 34.52  ? 141 ALA   B HB2  1 
ATOM   6796 H HB3  . ALA   B 1 156 ? -3.091  -12.576 31.594  1.00 34.52  ? 141 ALA   B HB3  1 
ATOM   6797 N N    . ASN   B 1 157 ? -2.043  -15.554 32.362  1.00 29.18  ? 142 ASN   B N    1 
ATOM   6798 C CA   . ASN   B 1 157 ? -1.254  -16.609 31.743  1.00 27.95  ? 142 ASN   B CA   1 
ATOM   6799 C C    . ASN   B 1 157 ? -0.982  -17.771 32.692  1.00 33.46  ? 142 ASN   B C    1 
ATOM   6800 O O    . ASN   B 1 157 ? -0.159  -18.634 32.379  1.00 33.51  ? 142 ASN   B O    1 
ATOM   6801 C CB   . ASN   B 1 157 ? 0.057   -16.029 31.211  1.00 27.54  ? 142 ASN   B CB   1 
ATOM   6802 C CG   . ASN   B 1 157 ? -0.175  -14.949 30.172  1.00 33.87  ? 142 ASN   B CG   1 
ATOM   6803 O OD1  . ASN   B 1 157 ? -1.135  -15.015 29.404  1.00 33.76  ? 142 ASN   B OD1  1 
ATOM   6804 N ND2  . ASN   B 1 157 ? 0.688   -13.940 30.156  1.00 28.15  ? 142 ASN   B ND2  1 
ATOM   6805 H H    . ASN   B 1 157 ? -1.635  -15.142 32.997  1.00 35.01  ? 142 ASN   B H    1 
ATOM   6806 H HA   . ASN   B 1 157 ? -1.747  -16.967 30.989  1.00 33.54  ? 142 ASN   B HA   1 
ATOM   6807 H HB2  . ASN   B 1 157 ? 0.554   -15.638 31.947  1.00 33.05  ? 142 ASN   B HB2  1 
ATOM   6808 H HB3  . ASN   B 1 157 ? 0.575   -16.738 30.800  1.00 33.05  ? 142 ASN   B HB3  1 
ATOM   6809 H HD21 . ASN   B 1 157 ? 0.597   -13.305 29.584  1.00 33.78  ? 142 ASN   B HD21 1 
ATOM   6810 H HD22 . ASN   B 1 157 ? 1.339   -13.923 30.718  1.00 33.78  ? 142 ASN   B HD22 1 
ATOM   6811 N N    . ILE   B 1 158 ? -1.650  -17.816 33.833  1.00 28.39  ? 143 ILE   B N    1 
ATOM   6812 C CA   . ILE   B 1 158 ? -1.595  -18.965 34.727  1.00 31.67  ? 143 ILE   B CA   1 
ATOM   6813 C C    . ILE   B 1 158 ? -2.896  -19.729 34.532  1.00 30.00  ? 143 ILE   B C    1 
ATOM   6814 O O    . ILE   B 1 158 ? -3.973  -19.235 34.881  1.00 29.21  ? 143 ILE   B O    1 
ATOM   6815 C CB   . ILE   B 1 158 ? -1.398  -18.540 36.185  1.00 30.26  ? 143 ILE   B CB   1 
ATOM   6816 C CG1  . ILE   B 1 158 ? -0.102  -17.749 36.330  1.00 28.76  ? 143 ILE   B CG1  1 
ATOM   6817 C CG2  . ILE   B 1 158 ? -1.358  -19.758 37.074  1.00 31.54  ? 143 ILE   B CG2  1 
ATOM   6818 C CD1  . ILE   B 1 158 ? 0.095   -17.164 37.702  1.00 32.79  ? 143 ILE   B CD1  1 
ATOM   6819 H H    . ILE   B 1 158 ? -2.154  -17.180 34.119  1.00 34.07  ? 143 ILE   B H    1 
ATOM   6820 H HA   . ILE   B 1 158 ? -0.852  -19.540 34.485  1.00 38.00  ? 143 ILE   B HA   1 
ATOM   6821 H HB   . ILE   B 1 158 ? -2.142  -17.976 36.447  1.00 36.32  ? 143 ILE   B HB   1 
ATOM   6822 H HG12 . ILE   B 1 158 ? 0.646   -18.339 36.149  1.00 34.52  ? 143 ILE   B HG12 1 
ATOM   6823 H HG13 . ILE   B 1 158 ? -0.109  -17.017 35.693  1.00 34.52  ? 143 ILE   B HG13 1 
ATOM   6824 H HG21 . ILE   B 1 158 ? -1.230  -19.474 37.992  1.00 37.85  ? 143 ILE   B HG21 1 
ATOM   6825 H HG22 . ILE   B 1 158 ? -2.197  -20.238 36.989  1.00 37.85  ? 143 ILE   B HG22 1 
ATOM   6826 H HG23 . ILE   B 1 158 ? -0.622  -20.326 36.798  1.00 37.85  ? 143 ILE   B HG23 1 
ATOM   6827 H HD11 . ILE   B 1 158 ? 0.851   -16.556 37.681  1.00 39.35  ? 143 ILE   B HD11 1 
ATOM   6828 H HD12 . ILE   B 1 158 ? -0.708  -16.684 37.959  1.00 39.35  ? 143 ILE   B HD12 1 
ATOM   6829 H HD13 . ILE   B 1 158 ? 0.266   -17.883 38.330  1.00 39.35  ? 143 ILE   B HD13 1 
ATOM   6830 N N    . LEU   B 1 159 ? -2.802  -20.921 33.954  1.00 30.73  ? 144 LEU   B N    1 
ATOM   6831 C CA   . LEU   B 1 159 ? -3.966  -21.697 33.563  1.00 30.98  ? 144 LEU   B CA   1 
ATOM   6832 C C    . LEU   B 1 159 ? -4.306  -22.723 34.638  1.00 33.67  ? 144 LEU   B C    1 
ATOM   6833 O O    . LEU   B 1 159 ? -3.427  -23.222 35.347  1.00 28.37  ? 144 LEU   B O    1 
ATOM   6834 C CB   . LEU   B 1 159 ? -3.713  -22.394 32.223  1.00 31.30  ? 144 LEU   B CB   1 
ATOM   6835 C CG   . LEU   B 1 159 ? -3.137  -21.502 31.123  1.00 33.54  ? 144 LEU   B CG   1 
ATOM   6836 C CD1  . LEU   B 1 159 ? -3.104  -22.223 29.782  1.00 38.83  ? 144 LEU   B CD1  1 
ATOM   6837 C CD2  . LEU   B 1 159 ? -3.932  -20.208 31.028  1.00 37.17  ? 144 LEU   B CD2  1 
ATOM   6838 H H    . LEU   B 1 159 ? -2.056  -21.309 33.776  1.00 36.87  ? 144 LEU   B H    1 
ATOM   6839 H HA   . LEU   B 1 159 ? -4.733  -21.112 33.460  1.00 37.18  ? 144 LEU   B HA   1 
ATOM   6840 H HB2  . LEU   B 1 159 ? -3.085  -23.118 32.369  1.00 37.56  ? 144 LEU   B HB2  1 
ATOM   6841 H HB3  . LEU   B 1 159 ? -4.556  -22.747 31.899  1.00 37.56  ? 144 LEU   B HB3  1 
ATOM   6842 H HG   . LEU   B 1 159 ? -2.219  -21.282 31.348  1.00 40.25  ? 144 LEU   B HG   1 
ATOM   6843 H HD11 . LEU   B 1 159 ? -2.725  -21.630 29.114  1.00 46.60  ? 144 LEU   B HD11 1 
ATOM   6844 H HD12 . LEU   B 1 159 ? -2.558  -23.020 29.864  1.00 46.60  ? 144 LEU   B HD12 1 
ATOM   6845 H HD13 . LEU   B 1 159 ? -4.010  -22.466 29.532  1.00 46.60  ? 144 LEU   B HD13 1 
ATOM   6846 H HD21 . LEU   B 1 159 ? -3.769  -19.799 30.164  1.00 44.61  ? 144 LEU   B HD21 1 
ATOM   6847 H HD22 . LEU   B 1 159 ? -4.876  -20.410 31.126  1.00 44.61  ? 144 LEU   B HD22 1 
ATOM   6848 H HD23 . LEU   B 1 159 ? -3.647  -19.610 31.737  1.00 44.61  ? 144 LEU   B HD23 1 
ATOM   6849 N N    . ILE   B 1 160 ? -5.601  -23.040 34.735  1.00 29.28  ? 145 ILE   B N    1 
ATOM   6850 C CA   . ILE   B 1 160 ? -6.152  -23.931 35.751  1.00 29.73  ? 145 ILE   B CA   1 
ATOM   6851 C C    . ILE   B 1 160 ? -7.013  -24.969 35.045  1.00 34.88  ? 145 ILE   B C    1 
ATOM   6852 O O    . ILE   B 1 160 ? -7.869  -24.612 34.228  1.00 36.80  ? 145 ILE   B O    1 
ATOM   6853 C CB   . ILE   B 1 160 ? -7.005  -23.169 36.789  1.00 33.52  ? 145 ILE   B CB   1 
ATOM   6854 C CG1  . ILE   B 1 160 ? -6.253  -21.968 37.377  1.00 28.94  ? 145 ILE   B CG1  1 
ATOM   6855 C CG2  . ILE   B 1 160 ? -7.459  -24.115 37.906  1.00 36.28  ? 145 ILE   B CG2  1 
ATOM   6856 C CD1  . ILE   B 1 160 ? -5.117  -22.323 38.322  1.00 32.51  ? 145 ILE   B CD1  1 
ATOM   6857 H H    . ILE   B 1 160 ? -6.202  -22.738 34.198  1.00 35.13  ? 145 ILE   B H    1 
ATOM   6858 H HA   . ILE   B 1 160 ? -5.424  -24.374 36.214  1.00 35.67  ? 145 ILE   B HA   1 
ATOM   6859 H HB   . ILE   B 1 160 ? -7.785  -22.827 36.325  1.00 40.23  ? 145 ILE   B HB   1 
ATOM   6860 H HG12 . ILE   B 1 160 ? -5.875  -21.455 36.647  1.00 34.73  ? 145 ILE   B HG12 1 
ATOM   6861 H HG13 . ILE   B 1 160 ? -6.885  -21.423 37.873  1.00 34.73  ? 145 ILE   B HG13 1 
ATOM   6862 H HG21 . ILE   B 1 160 ? -7.854  -23.592 38.622  1.00 43.53  ? 145 ILE   B HG21 1 
ATOM   6863 H HG22 . ILE   B 1 160 ? -8.114  -24.735 37.549  1.00 43.53  ? 145 ILE   B HG22 1 
ATOM   6864 H HG23 . ILE   B 1 160 ? -6.689  -24.602 38.239  1.00 43.53  ? 145 ILE   B HG23 1 
ATOM   6865 H HD11 . ILE   B 1 160 ? -4.616  -21.519 38.529  1.00 39.01  ? 145 ILE   B HD11 1 
ATOM   6866 H HD12 . ILE   B 1 160 ? -5.489  -22.700 39.135  1.00 39.01  ? 145 ILE   B HD12 1 
ATOM   6867 H HD13 . ILE   B 1 160 ? -4.539  -22.971 37.890  1.00 39.01  ? 145 ILE   B HD13 1 
ATOM   6868 N N    . ASN   B 1 161 ? -6.799  -26.244 35.357  1.00 34.51  ? 146 ASN   B N    1 
ATOM   6869 C CA   . ASN   B 1 161 ? -7.635  -27.304 34.810  1.00 32.54  ? 146 ASN   B CA   1 
ATOM   6870 C C    . ASN   B 1 161 ? -8.703  -27.704 35.824  1.00 37.89  ? 146 ASN   B C    1 
ATOM   6871 O O    . ASN   B 1 161 ? -8.699  -27.270 36.977  1.00 39.50  ? 146 ASN   B O    1 
ATOM   6872 C CB   . ASN   B 1 161 ? -6.795  -28.512 34.385  1.00 33.03  ? 146 ASN   B CB   1 
ATOM   6873 C CG   . ASN   B 1 161 ? -6.202  -29.278 35.552  1.00 33.05  ? 146 ASN   B CG   1 
ATOM   6874 O OD1  . ASN   B 1 161 ? -6.601  -29.114 36.709  1.00 37.64  ? 146 ASN   B OD1  1 
ATOM   6875 N ND2  . ASN   B 1 161 ? -5.255  -30.149 35.243  1.00 38.46  ? 146 ASN   B ND2  1 
ATOM   6876 H H    . ASN   B 1 161 ? -6.176  -26.518 35.882  1.00 41.42  ? 146 ASN   B H    1 
ATOM   6877 H HA   . ASN   B 1 161 ? -8.081  -26.976 34.014  1.00 39.05  ? 146 ASN   B HA   1 
ATOM   6878 H HB2  . ASN   B 1 161 ? -7.357  -29.124 33.884  1.00 39.64  ? 146 ASN   B HB2  1 
ATOM   6879 H HB3  . ASN   B 1 161 ? -6.062  -28.204 33.829  1.00 39.64  ? 146 ASN   B HB3  1 
ATOM   6880 H HD21 . ASN   B 1 161 ? -4.880  -30.614 35.862  1.00 46.15  ? 146 ASN   B HD21 1 
ATOM   6881 H HD22 . ASN   B 1 161 ? -5.014  -30.250 34.424  1.00 46.15  ? 146 ASN   B HD22 1 
ATOM   6882 N N    . ASP   B 1 162 ? -9.642  -28.533 35.371  1.00 35.78  ? 147 ASP   B N    1 
ATOM   6883 C CA   . ASP   B 1 162 ? -10.769 -28.889 36.223  1.00 40.20  ? 147 ASP   B CA   1 
ATOM   6884 C C    . ASP   B 1 162 ? -10.346 -29.692 37.446  1.00 41.76  ? 147 ASP   B C    1 
ATOM   6885 O O    . ASP   B 1 162 ? -11.125 -29.799 38.399  1.00 44.35  ? 147 ASP   B O    1 
ATOM   6886 C CB   . ASP   B 1 162 ? -11.807 -29.663 35.417  1.00 44.72  ? 147 ASP   B CB   1 
ATOM   6887 C CG   . ASP   B 1 162 ? -12.438 -28.815 34.338  1.00 50.15  ? 147 ASP   B CG   1 
ATOM   6888 O OD1  . ASP   B 1 162 ? -12.501 -27.583 34.527  1.00 53.39  ? 147 ASP   B OD1  1 
ATOM   6889 O OD2  . ASP   B 1 162 ? -12.859 -29.371 33.301  1.00 72.80  ? 147 ASP   B OD2  1 
ATOM   6890 H H    . ASP   B 1 162 ? -9.649  -28.895 34.591  1.00 42.93  ? 147 ASP   B H    1 
ATOM   6891 H HA   . ASP   B 1 162 ? -11.186 -28.074 36.542  1.00 48.24  ? 147 ASP   B HA   1 
ATOM   6892 H HB2  . ASP   B 1 162 ? -11.378 -30.423 34.993  1.00 53.67  ? 147 ASP   B HB2  1 
ATOM   6893 H HB3  . ASP   B 1 162 ? -12.509 -29.967 36.013  1.00 53.67  ? 147 ASP   B HB3  1 
ATOM   6894 N N    . ALA   B 1 163 ? -9.137  -30.243 37.450  1.00 38.50  ? 148 ALA   B N    1 
ATOM   6895 C CA   . ALA   B 1 163 ? -8.612  -30.905 38.633  1.00 35.69  ? 148 ALA   B CA   1 
ATOM   6896 C C    . ALA   B 1 163 ? -8.030  -29.930 39.643  1.00 37.51  ? 148 ALA   B C    1 
ATOM   6897 O O    . ALA   B 1 163 ? -7.538  -30.370 40.687  1.00 34.51  ? 148 ALA   B O    1 
ATOM   6898 C CB   . ALA   B 1 163 ? -7.535  -31.917 38.240  1.00 35.70  ? 148 ALA   B CB   1 
ATOM   6899 H H    . ALA   B 1 163 ? -8.602  -30.245 36.777  1.00 46.20  ? 148 ALA   B H    1 
ATOM   6900 H HA   . ALA   B 1 163 ? -9.338  -31.389 39.058  1.00 42.83  ? 148 ALA   B HA   1 
ATOM   6901 H HB1  . ALA   B 1 163 ? -7.196  -32.345 39.042  1.00 42.84  ? 148 ALA   B HB1  1 
ATOM   6902 H HB2  . ALA   B 1 163 ? -7.926  -32.581 37.651  1.00 42.84  ? 148 ALA   B HB2  1 
ATOM   6903 H HB3  . ALA   B 1 163 ? -6.816  -31.452 37.785  1.00 42.84  ? 148 ALA   B HB3  1 
ATOM   6904 N N    . GLY   B 1 164 ? -8.060  -28.626 39.357  1.00 33.37  ? 149 GLY   B N    1 
ATOM   6905 C CA   . GLY   B 1 164 ? -7.470  -27.645 40.238  1.00 32.45  ? 149 GLY   B CA   1 
ATOM   6906 C C    . GLY   B 1 164 ? -5.964  -27.526 40.169  1.00 34.38  ? 149 GLY   B C    1 
ATOM   6907 O O    . GLY   B 1 164 ? -5.371  -26.910 41.062  1.00 30.99  ? 149 GLY   B O    1 
ATOM   6908 H H    . GLY   B 1 164 ? -8.421  -28.292 38.651  1.00 40.04  ? 149 GLY   B H    1 
ATOM   6909 H HA2  . GLY   B 1 164 ? -7.842  -26.775 40.023  1.00 38.94  ? 149 GLY   B HA2  1 
ATOM   6910 H HA3  . GLY   B 1 164 ? -7.704  -27.871 41.151  1.00 38.94  ? 149 GLY   B HA3  1 
ATOM   6911 N N    . GLU   B 1 165 ? -5.326  -28.084 39.142  1.00 31.49  ? 150 GLU   B N    1 
ATOM   6912 C CA   . GLU   B 1 165 ? -3.879  -28.017 38.990  1.00 32.26  ? 150 GLU   B CA   1 
ATOM   6913 C C    . GLU   B 1 165 ? -3.475  -26.746 38.241  1.00 29.91  ? 150 GLU   B C    1 
ATOM   6914 O O    . GLU   B 1 165 ? -4.284  -26.128 37.546  1.00 30.38  ? 150 GLU   B O    1 
ATOM   6915 C CB   . GLU   B 1 165 ? -3.367  -29.258 38.251  1.00 36.09  ? 150 GLU   B CB   1 
ATOM   6916 C CG   . GLU   B 1 165 ? -3.594  -30.567 39.017  1.00 38.43  ? 150 GLU   B CG   1 
ATOM   6917 C CD   . GLU   B 1 165 ? -3.322  -31.809 38.177  1.00 44.78  ? 150 GLU   B CD   1 
ATOM   6918 O OE1  . GLU   B 1 165 ? -3.925  -31.947 37.091  1.00 42.11  ? 150 GLU   B OE1  1 
ATOM   6919 O OE2  . GLU   B 1 165 ? -2.503  -32.650 38.606  1.00 55.02  ? 150 GLU   B OE2  1 
ATOM   6920 H H    . GLU   B 1 165 ? -5.719  -28.515 38.509  1.00 37.79  ? 150 GLU   B H    1 
ATOM   6921 H HA   . GLU   B 1 165 ? -3.459  -27.992 39.864  1.00 38.71  ? 150 GLU   B HA   1 
ATOM   6922 H HB2  . GLU   B 1 165 ? -3.829  -29.327 37.401  1.00 43.31  ? 150 GLU   B HB2  1 
ATOM   6923 H HB3  . GLU   B 1 165 ? -2.413  -29.162 38.104  1.00 43.31  ? 150 GLU   B HB3  1 
ATOM   6924 H HG2  . GLU   B 1 165 ? -3.000  -30.590 39.784  1.00 46.11  ? 150 GLU   B HG2  1 
ATOM   6925 H HG3  . GLU   B 1 165 ? -4.518  -30.603 39.312  1.00 46.11  ? 150 GLU   B HG3  1 
ATOM   6926 N N    . VAL   B 1 166 ? -2.208  -26.361 38.396  1.00 39.33  ? 151 VAL   B N    1 
ATOM   6927 C CA   . VAL   B 1 166 ? -1.679  -25.101 37.886  1.00 39.54  ? 151 VAL   B CA   1 
ATOM   6928 C C    . VAL   B 1 166 ? -0.716  -25.380 36.734  1.00 40.04  ? 151 VAL   B C    1 
ATOM   6929 O O    . VAL   B 1 166 ? 0.160   -26.245 36.848  1.00 40.35  ? 151 VAL   B O    1 
ATOM   6930 C CB   . VAL   B 1 166 ? -0.975  -24.299 38.995  1.00 39.54  ? 151 VAL   B CB   1 
ATOM   6931 C CG1  . VAL   B 1 166 ? -0.534  -22.945 38.478  1.00 39.71  ? 151 VAL   B CG1  1 
ATOM   6932 C CG2  . VAL   B 1 166 ? -1.890  -24.133 40.202  1.00 41.58  ? 151 VAL   B CG2  1 
ATOM   6933 H H    . VAL   B 1 166 ? -1.617  -26.832 38.809  1.00 47.20  ? 151 VAL   B H    1 
ATOM   6934 H HA   . VAL   B 1 166 ? -2.417  -24.578 37.535  1.00 47.45  ? 151 VAL   B HA   1 
ATOM   6935 H HB   . VAL   B 1 166 ? -0.187  -24.789 39.276  1.00 47.45  ? 151 VAL   B HB   1 
ATOM   6936 H HG11 . VAL   B 1 166 ? -0.214  -22.412 39.223  1.00 47.65  ? 151 VAL   B HG11 1 
ATOM   6937 H HG12 . VAL   B 1 166 ? 0.178   -23.070 37.831  1.00 47.65  ? 151 VAL   B HG12 1 
ATOM   6938 H HG13 . VAL   B 1 166 ? -1.289  -22.505 38.058  1.00 47.65  ? 151 VAL   B HG13 1 
ATOM   6939 H HG21 . VAL   B 1 166 ? -1.462  -23.544 40.844  1.00 49.89  ? 151 VAL   B HG21 1 
ATOM   6940 H HG22 . VAL   B 1 166 ? -2.731  -23.748 39.910  1.00 49.89  ? 151 VAL   B HG22 1 
ATOM   6941 H HG23 . VAL   B 1 166 ? -2.044  -25.002 40.603  1.00 49.89  ? 151 VAL   B HG23 1 
ATOM   6942 N N    . ARG   B 1 167 ? -0.852  -24.622 35.647  1.00 40.13  ? 152 ARG   B N    1 
ATOM   6943 C CA   . ARG   B 1 167 ? -0.052  -24.837 34.448  1.00 40.55  ? 152 ARG   B CA   1 
ATOM   6944 C C    . ARG   B 1 167 ? 0.449   -23.515 33.883  1.00 40.59  ? 152 ARG   B C    1 
ATOM   6945 O O    . ARG   B 1 167 ? -0.257  -22.506 33.926  1.00 40.32  ? 152 ARG   B O    1 
ATOM   6946 C CB   . ARG   B 1 167 ? -0.865  -25.560 33.364  1.00 40.65  ? 152 ARG   B CB   1 
ATOM   6947 C CG   . ARG   B 1 167 ? -1.422  -26.914 33.775  1.00 40.62  ? 152 ARG   B CG   1 
ATOM   6948 C CD   . ARG   B 1 167 ? -0.359  -27.995 33.720  1.00 41.76  ? 152 ARG   B CD   1 
ATOM   6949 N NE   . ARG   B 1 167 ? -0.922  -29.315 33.988  1.00 41.03  ? 152 ARG   B NE   1 
ATOM   6950 C CZ   . ARG   B 1 167 ? -0.971  -29.883 35.186  1.00 41.42  ? 152 ARG   B CZ   1 
ATOM   6951 N NH1  . ARG   B 1 167 ? -0.493  -29.277 36.261  1.00 40.59  ? 152 ARG   B NH1  1 
ATOM   6952 N NH2  . ARG   B 1 167 ? -1.510  -31.092 35.308  1.00 43.93  ? 152 ARG   B NH2  1 
ATOM   6953 H H    . ARG   B 1 167 ? -1.409  -23.970 35.581  1.00 48.16  ? 152 ARG   B H    1 
ATOM   6954 H HA   . ARG   B 1 167 ? 0.722   -25.369 34.689  1.00 48.66  ? 152 ARG   B HA   1 
ATOM   6955 H HB2  . ARG   B 1 167 ? -1.616  -24.998 33.118  1.00 48.78  ? 152 ARG   B HB2  1 
ATOM   6956 H HB3  . ARG   B 1 167 ? -0.291  -25.703 32.595  1.00 48.78  ? 152 ARG   B HB3  1 
ATOM   6957 H HG2  . ARG   B 1 167 ? -1.756  -26.861 34.684  1.00 48.74  ? 152 ARG   B HG2  1 
ATOM   6958 H HG3  . ARG   B 1 167 ? -2.140  -27.162 33.171  1.00 48.74  ? 152 ARG   B HG3  1 
ATOM   6959 H HD2  . ARG   B 1 167 ? 0.041   -28.007 32.836  1.00 50.12  ? 152 ARG   B HD2  1 
ATOM   6960 H HD3  . ARG   B 1 167 ? 0.320   -27.811 34.388  1.00 50.12  ? 152 ARG   B HD3  1 
ATOM   6961 H HE   . ARG   B 1 167 ? -1.245  -29.754 33.323  1.00 49.24  ? 152 ARG   B HE   1 
ATOM   6962 H HH11 . ARG   B 1 167 ? -0.141  -28.495 36.193  1.00 48.70  ? 152 ARG   B HH11 1 
ATOM   6963 H HH12 . ARG   B 1 167 ? -0.536  -29.664 37.028  1.00 48.70  ? 152 ARG   B HH12 1 
ATOM   6964 H HH21 . ARG   B 1 167 ? -1.821  -31.496 34.615  1.00 52.72  ? 152 ARG   B HH21 1 
ATOM   6965 H HH22 . ARG   B 1 167 ? -1.547  -31.470 36.079  1.00 52.72  ? 152 ARG   B HH22 1 
ATOM   6966 N N    . LEU   B 1 168 ? 1.671   -23.530 33.350  1.00 40.91  ? 153 LEU   B N    1 
ATOM   6967 C CA   . LEU   B 1 168 ? 2.215   -22.434 32.563  1.00 40.93  ? 153 LEU   B CA   1 
ATOM   6968 C C    . LEU   B 1 168 ? 2.323   -22.864 31.105  1.00 43.74  ? 153 LEU   B C    1 
ATOM   6969 O O    . LEU   B 1 168 ? 2.638   -24.022 30.814  1.00 44.78  ? 153 LEU   B O    1 
ATOM   6970 C CB   . LEU   B 1 168 ? 3.601   -22.013 33.053  1.00 41.10  ? 153 LEU   B CB   1 
ATOM   6971 C CG   . LEU   B 1 168 ? 3.752   -21.487 34.475  1.00 43.80  ? 153 LEU   B CG   1 
ATOM   6972 C CD1  . LEU   B 1 168 ? 5.219   -21.199 34.760  1.00 41.29  ? 153 LEU   B CD1  1 
ATOM   6973 C CD2  . LEU   B 1 168 ? 2.903   -20.246 34.679  1.00 40.64  ? 153 LEU   B CD2  1 
ATOM   6974 H H    . LEU   B 1 168 ? 2.219   -24.188 33.437  1.00 49.10  ? 153 LEU   B H    1 
ATOM   6975 H HA   . LEU   B 1 168 ? 1.621   -21.671 32.636  1.00 49.12  ? 153 LEU   B HA   1 
ATOM   6976 H HB2  . LEU   B 1 168 ? 4.181   -22.788 32.984  1.00 49.32  ? 153 LEU   B HB2  1 
ATOM   6977 H HB3  . LEU   B 1 168 ? 3.916   -21.309 32.465  1.00 49.32  ? 153 LEU   B HB3  1 
ATOM   6978 H HG   . LEU   B 1 168 ? 3.443   -22.156 35.106  1.00 52.56  ? 153 LEU   B HG   1 
ATOM   6979 H HD11 . LEU   B 1 168 ? 5.305   -20.865 35.667  1.00 49.55  ? 153 LEU   B HD11 1 
ATOM   6980 H HD12 . LEU   B 1 168 ? 5.727   -22.019 34.660  1.00 49.55  ? 153 LEU   B HD12 1 
ATOM   6981 H HD13 . LEU   B 1 168 ? 5.538   -20.533 34.131  1.00 49.55  ? 153 LEU   B HD13 1 
ATOM   6982 H HD21 . LEU   B 1 168 ? 3.058   -19.901 35.572  1.00 48.77  ? 153 LEU   B HD21 1 
ATOM   6983 H HD22 . LEU   B 1 168 ? 3.154   -19.581 34.019  1.00 48.77  ? 153 LEU   B HD22 1 
ATOM   6984 H HD23 . LEU   B 1 168 ? 1.969   -20.482 34.572  1.00 48.77  ? 153 LEU   B HD23 1 
ATOM   6985 N N    . ALA   B 1 169 ? 2.086   -21.926 30.195  1.00 41.64  ? 154 ALA   B N    1 
ATOM   6986 C CA   . ALA   B 1 169 ? 2.205   -22.174 28.764  1.00 51.68  ? 154 ALA   B CA   1 
ATOM   6987 C C    . ALA   B 1 169 ? 3.578   -21.729 28.278  1.00 52.66  ? 154 ALA   B C    1 
ATOM   6988 O O    . ALA   B 1 169 ? 4.009   -20.609 28.567  1.00 55.85  ? 154 ALA   B O    1 
ATOM   6989 C CB   . ALA   B 1 169 ? 1.111   -21.437 27.992  1.00 60.45  ? 154 ALA   B CB   1 
ATOM   6990 H H    . ALA   B 1 169 ? 1.849   -21.122 30.386  1.00 49.96  ? 154 ALA   B H    1 
ATOM   6991 H HA   . ALA   B 1 169 ? 2.114   -23.125 28.595  1.00 62.02  ? 154 ALA   B HA   1 
ATOM   6992 H HB1  . ALA   B 1 169 ? 1.214   -21.621 27.045  1.00 72.55  ? 154 ALA   B HB1  1 
ATOM   6993 H HB2  . ALA   B 1 169 ? 0.244   -21.749 28.296  1.00 72.55  ? 154 ALA   B HB2  1 
ATOM   6994 H HB3  . ALA   B 1 169 ? 1.195   -20.485 28.155  1.00 72.55  ? 154 ALA   B HB3  1 
ATOM   6995 N N    . ASP   B 1 170 ? 4.262   -22.609 27.548  1.00 57.49  ? 155 ASP   B N    1 
ATOM   6996 C CA   . ASP   B 1 170 ? 5.536   -22.282 26.910  1.00 60.80  ? 155 ASP   B CA   1 
ATOM   6997 C C    . ASP   B 1 170 ? 5.247   -21.799 25.489  1.00 55.68  ? 155 ASP   B C    1 
ATOM   6998 O O    . ASP   B 1 170 ? 4.886   -22.596 24.617  1.00 58.72  ? 155 ASP   B O    1 
ATOM   6999 C CB   . ASP   B 1 170 ? 6.466   -23.496 26.914  1.00 57.88  ? 155 ASP   B CB   1 
ATOM   7000 C CG   . ASP   B 1 170 ? 7.829   -23.200 26.295  1.00 60.38  ? 155 ASP   B CG   1 
ATOM   7001 O OD1  . ASP   B 1 170 ? 8.716   -22.685 27.007  1.00 67.18  ? 155 ASP   B OD1  1 
ATOM   7002 O OD2  . ASP   B 1 170 ? 8.013   -23.486 25.094  1.00 66.37  ? 155 ASP   B OD2  1 
ATOM   7003 H H    . ASP   B 1 170 ? 4.004   -23.417 27.406  1.00 68.99  ? 155 ASP   B H    1 
ATOM   7004 H HA   . ASP   B 1 170 ? 5.976   -21.567 27.396  1.00 72.96  ? 155 ASP   B HA   1 
ATOM   7005 H HB2  . ASP   B 1 170 ? 6.608   -23.782 27.829  1.00 69.45  ? 155 ASP   B HB2  1 
ATOM   7006 H HB3  . ASP   B 1 170 ? 6.053   -24.210 26.403  1.00 69.45  ? 155 ASP   B HB3  1 
ATOM   7007 N N    . PHE   B 1 171 ? 5.409   -20.497 25.255  1.00 53.10  ? 156 PHE   B N    1 
ATOM   7008 C CA   . PHE   B 1 171 ? 5.052   -19.880 23.983  1.00 60.97  ? 156 PHE   B CA   1 
ATOM   7009 C C    . PHE   B 1 171 ? 6.268   -19.479 23.152  1.00 59.10  ? 156 PHE   B C    1 
ATOM   7010 O O    . PHE   B 1 171 ? 6.112   -18.762 22.158  1.00 64.40  ? 156 PHE   B O    1 
ATOM   7011 C CB   . PHE   B 1 171 ? 4.173   -18.643 24.217  1.00 54.21  ? 156 PHE   B CB   1 
ATOM   7012 C CG   . PHE   B 1 171 ? 2.708   -18.953 24.453  1.00 66.39  ? 156 PHE   B CG   1 
ATOM   7013 C CD1  . PHE   B 1 171 ? 2.115   -20.092 23.923  1.00 64.20  ? 156 PHE   B CD1  1 
ATOM   7014 C CD2  . PHE   B 1 171 ? 1.922   -18.087 25.197  1.00 63.75  ? 156 PHE   B CD2  1 
ATOM   7015 C CE1  . PHE   B 1 171 ? 0.773   -20.358 24.142  1.00 63.52  ? 156 PHE   B CE1  1 
ATOM   7016 C CE2  . PHE   B 1 171 ? 0.584   -18.350 25.414  1.00 56.59  ? 156 PHE   B CE2  1 
ATOM   7017 C CZ   . PHE   B 1 171 ? 0.011   -19.485 24.886  1.00 61.48  ? 156 PHE   B CZ   1 
ATOM   7018 H H    . PHE   B 1 171 ? 5.729   -19.943 25.829  1.00 63.72  ? 156 PHE   B H    1 
ATOM   7019 H HA   . PHE   B 1 171 ? 4.543   -20.530 23.474  1.00 73.17  ? 156 PHE   B HA   1 
ATOM   7020 H HB2  . PHE   B 1 171 ? 4.502   -18.172 24.998  1.00 65.06  ? 156 PHE   B HB2  1 
ATOM   7021 H HB3  . PHE   B 1 171 ? 4.229   -18.071 23.436  1.00 65.06  ? 156 PHE   B HB3  1 
ATOM   7022 H HD1  . PHE   B 1 171 ? 2.624   -20.682 23.416  1.00 77.04  ? 156 PHE   B HD1  1 
ATOM   7023 H HD2  . PHE   B 1 171 ? 2.302   -17.317 25.556  1.00 76.50  ? 156 PHE   B HD2  1 
ATOM   7024 H HE1  . PHE   B 1 171 ? 0.387   -21.126 23.786  1.00 76.22  ? 156 PHE   B HE1  1 
ATOM   7025 H HE2  . PHE   B 1 171 ? 0.070   -17.761 25.918  1.00 67.90  ? 156 PHE   B HE2  1 
ATOM   7026 H HZ   . PHE   B 1 171 ? -0.890  -19.662 25.032  1.00 73.77  ? 156 PHE   B HZ   1 
ATOM   7027 N N    . GLY   B 1 172 ? 7.466   -19.929 23.521  1.00 48.70  ? 157 GLY   B N    1 
ATOM   7028 C CA   . GLY   B 1 172 ? 8.664   -19.445 22.855  1.00 46.88  ? 157 GLY   B CA   1 
ATOM   7029 C C    . GLY   B 1 172 ? 8.607   -19.538 21.344  1.00 54.45  ? 157 GLY   B C    1 
ATOM   7030 O O    . GLY   B 1 172 ? 9.194   -18.707 20.643  1.00 50.67  ? 157 GLY   B O    1 
ATOM   7031 H H    . GLY   B 1 172 ? 7.607   -20.506 24.143  1.00 58.44  ? 157 GLY   B H    1 
ATOM   7032 H HA2  . GLY   B 1 172 ? 8.802   -18.515 23.093  1.00 56.26  ? 157 GLY   B HA2  1 
ATOM   7033 H HA3  . GLY   B 1 172 ? 9.425   -19.965 23.159  1.00 56.26  ? 157 GLY   B HA3  1 
ATOM   7034 N N    . ILE   B 1 173 ? 7.901   -20.541 20.816  1.00 52.25  ? 158 ILE   B N    1 
ATOM   7035 C CA   . ILE   B 1 173 ? 7.836   -20.721 19.369  1.00 57.69  ? 158 ILE   B CA   1 
ATOM   7036 C C    . ILE   B 1 173 ? 7.089   -19.562 18.721  1.00 59.28  ? 158 ILE   B C    1 
ATOM   7037 O O    . ILE   B 1 173 ? 7.560   -18.963 17.748  1.00 57.43  ? 158 ILE   B O    1 
ATOM   7038 C CB   . ILE   B 1 173 ? 7.184   -22.074 19.025  1.00 64.77  ? 158 ILE   B CB   1 
ATOM   7039 C CG1  . ILE   B 1 173 ? 8.078   -23.215 19.522  1.00 72.81  ? 158 ILE   B CG1  1 
ATOM   7040 C CG2  . ILE   B 1 173 ? 6.921   -22.180 17.516  1.00 68.82  ? 158 ILE   B CG2  1 
ATOM   7041 C CD1  . ILE   B 1 173 ? 7.794   -24.567 18.893  1.00 74.42  ? 158 ILE   B CD1  1 
ATOM   7042 H H    . ILE   B 1 173 ? 7.457   -21.122 21.269  1.00 62.70  ? 158 ILE   B H    1 
ATOM   7043 H HA   . ILE   B 1 173 ? 8.740   -20.725 19.020  1.00 69.23  ? 158 ILE   B HA   1 
ATOM   7044 H HB   . ILE   B 1 173 ? 6.327   -22.138 19.475  1.00 77.72  ? 158 ILE   B HB   1 
ATOM   7045 H HG12 . ILE   B 1 173 ? 9.001   -22.990 19.325  1.00 87.37  ? 158 ILE   B HG12 1 
ATOM   7046 H HG13 . ILE   B 1 173 ? 7.955   -23.307 20.480  1.00 87.37  ? 158 ILE   B HG13 1 
ATOM   7047 H HG21 . ILE   B 1 173 ? 6.493   -23.030 17.329  1.00 82.58  ? 158 ILE   B HG21 1 
ATOM   7048 H HG22 . ILE   B 1 173 ? 6.341   -21.451 17.244  1.00 82.58  ? 158 ILE   B HG22 1 
ATOM   7049 H HG23 . ILE   B 1 173 ? 7.766   -22.124 17.043  1.00 82.58  ? 158 ILE   B HG23 1 
ATOM   7050 H HD11 . ILE   B 1 173 ? 8.239   -25.256 19.411  1.00 89.30  ? 158 ILE   B HD11 1 
ATOM   7051 H HD12 . ILE   B 1 173 ? 6.836   -24.721 18.894  1.00 89.30  ? 158 ILE   B HD12 1 
ATOM   7052 H HD13 . ILE   B 1 173 ? 8.129   -24.569 17.983  1.00 89.30  ? 158 ILE   B HD13 1 
ATOM   7053 N N    . SER   B 1 174 ? 5.916   -19.227 19.256  1.00 59.39  ? 159 SER   B N    1 
ATOM   7054 C CA   . SER   B 1 174 ? 5.069   -18.228 18.616  1.00 60.64  ? 159 SER   B CA   1 
ATOM   7055 C C    . SER   B 1 174 ? 5.779   -16.884 18.478  1.00 57.33  ? 159 SER   B C    1 
ATOM   7056 O O    . SER   B 1 174 ? 5.464   -16.106 17.569  1.00 49.12  ? 159 SER   B O    1 
ATOM   7057 C CB   . SER   B 1 174 ? 3.771   -18.076 19.412  1.00 58.46  ? 159 SER   B CB   1 
ATOM   7058 O OG   . SER   B 1 174 ? 2.889   -17.169 18.776  1.00 73.54  ? 159 SER   B OG   1 
ATOM   7059 H H    . SER   B 1 174 ? 5.591   -19.560 19.980  1.00 71.27  ? 159 SER   B H    1 
ATOM   7060 H HA   . SER   B 1 174 ? 4.846   -18.528 17.721  1.00 72.76  ? 159 SER   B HA   1 
ATOM   7061 H HB2  . SER   B 1 174 ? 3.338   -18.942 19.478  1.00 70.15  ? 159 SER   B HB2  1 
ATOM   7062 H HB3  . SER   B 1 174 ? 3.981   -17.741 20.298  1.00 70.15  ? 159 SER   B HB3  1 
ATOM   7063 H HG   . SER   B 1 174 ? 3.224   -16.399 18.770  1.00 88.25  ? 159 SER   B HG   1 
ATOM   7064 N N    . ALA   B 1 175 ? 6.746   -16.599 19.346  1.00 47.60  ? 160 ALA   B N    1 
ATOM   7065 C CA   . ALA   B 1 175 ? 7.345   -15.272 19.375  1.00 48.38  ? 160 ALA   B CA   1 
ATOM   7066 C C    . ALA   B 1 175 ? 8.323   -15.021 18.234  1.00 46.93  ? 160 ALA   B C    1 
ATOM   7067 O O    . ALA   B 1 175 ? 8.765   -13.880 18.064  1.00 39.08  ? 160 ALA   B O    1 
ATOM   7068 C CB   . ALA   B 1 175 ? 8.053   -15.046 20.714  1.00 47.04  ? 160 ALA   B CB   1 
ATOM   7069 H H    . ALA   B 1 175 ? 7.068   -17.152 19.921  1.00 57.12  ? 160 ALA   B H    1 
ATOM   7070 H HA   . ALA   B 1 175 ? 6.634   -14.616 19.294  1.00 58.06  ? 160 ALA   B HA   1 
ATOM   7071 H HB1  . ALA   B 1 175 ? 8.446   -14.159 20.718  1.00 56.45  ? 160 ALA   B HB1  1 
ATOM   7072 H HB2  . ALA   B 1 175 ? 7.404   -15.123 21.431  1.00 56.45  ? 160 ALA   B HB2  1 
ATOM   7073 H HB3  . ALA   B 1 175 ? 8.746   -15.716 20.822  1.00 56.45  ? 160 ALA   B HB3  1 
ATOM   7074 N N    . GLN   B 1 176 ? 8.665   -16.035 17.436  1.00 39.32  ? 161 GLN   B N    1 
ATOM   7075 C CA   . GLN   B 1 176 ? 9.626   -15.847 16.355  1.00 41.14  ? 161 GLN   B CA   1 
ATOM   7076 C C    . GLN   B 1 176 ? 9.021   -16.094 14.979  1.00 39.13  ? 161 GLN   B C    1 
ATOM   7077 O O    . GLN   B 1 176 ? 9.759   -16.241 14.001  1.00 39.27  ? 161 GLN   B O    1 
ATOM   7078 C CB   . GLN   B 1 176 ? 10.851  -16.735 16.581  1.00 48.92  ? 161 GLN   B CB   1 
ATOM   7079 C CG   . GLN   B 1 176 ? 11.683  -16.299 17.789  1.00 51.04  ? 161 GLN   B CG   1 
ATOM   7080 C CD   . GLN   B 1 176 ? 13.002  -17.043 17.902  1.00 61.71  ? 161 GLN   B CD   1 
ATOM   7081 O OE1  . GLN   B 1 176 ? 13.111  -18.205 17.508  1.00 70.94  ? 161 GLN   B OE1  1 
ATOM   7082 N NE2  . GLN   B 1 176 ? 14.013  -16.372 18.444  1.00 58.05  ? 161 GLN   B NE2  1 
ATOM   7083 H H    . GLN   B 1 176 ? 8.355   -16.834 17.503  1.00 47.18  ? 161 GLN   B H    1 
ATOM   7084 H HA   . GLN   B 1 176 ? 9.919   -14.923 16.364  1.00 49.37  ? 161 GLN   B HA   1 
ATOM   7085 H HB2  . GLN   B 1 176 ? 10.557  -17.647 16.732  1.00 58.70  ? 161 GLN   B HB2  1 
ATOM   7086 H HB3  . GLN   B 1 176 ? 11.419  -16.696 15.795  1.00 58.70  ? 161 GLN   B HB3  1 
ATOM   7087 H HG2  . GLN   B 1 176 ? 11.880  -15.352 17.711  1.00 61.25  ? 161 GLN   B HG2  1 
ATOM   7088 H HG3  . GLN   B 1 176 ? 11.176  -16.466 18.599  1.00 61.25  ? 161 GLN   B HG3  1 
ATOM   7089 H HE21 . GLN   B 1 176 ? 13.899  -15.562 18.708  1.00 69.66  ? 161 GLN   B HE21 1 
ATOM   7090 H HE22 . GLN   B 1 176 ? 14.781  -16.749 18.531  1.00 69.66  ? 161 GLN   B HE22 1 
ATOM   7091 N N    . ILE   B 1 177 ? 7.696   -16.099 14.870  1.00 39.36  ? 162 ILE   B N    1 
ATOM   7092 C CA   . ILE   B 1 177 ? 7.012   -16.246 13.592  1.00 43.33  ? 162 ILE   B CA   1 
ATOM   7093 C C    . ILE   B 1 177 ? 5.762   -15.377 13.613  1.00 39.41  ? 162 ILE   B C    1 
ATOM   7094 O O    . ILE   B 1 177 ? 5.346   -14.871 14.654  1.00 39.28  ? 162 ILE   B O    1 
ATOM   7095 C CB   . ILE   B 1 177 ? 6.629   -17.714 13.287  1.00 42.38  ? 162 ILE   B CB   1 
ATOM   7096 C CG1  . ILE   B 1 177 ? 5.609   -18.218 14.308  1.00 40.79  ? 162 ILE   B CG1  1 
ATOM   7097 C CG2  . ILE   B 1 177 ? 7.864   -18.599 13.283  1.00 44.43  ? 162 ILE   B CG2  1 
ATOM   7098 C CD1  . ILE   B 1 177 ? 5.119   -19.631 14.054  1.00 48.10  ? 162 ILE   B CD1  1 
ATOM   7099 H H    . ILE   B 1 177 ? 7.161   -16.017 15.538  1.00 47.24  ? 162 ILE   B H    1 
ATOM   7100 H HA   . ILE   B 1 177 ? 7.599   -15.934 12.885  1.00 51.99  ? 162 ILE   B HA   1 
ATOM   7101 H HB   . ILE   B 1 177 ? 6.226   -17.747 12.405  1.00 50.86  ? 162 ILE   B HB   1 
ATOM   7102 H HG12 . ILE   B 1 177 ? 6.018   -18.203 15.187  1.00 48.94  ? 162 ILE   B HG12 1 
ATOM   7103 H HG13 . ILE   B 1 177 ? 4.837   -17.632 14.290  1.00 48.94  ? 162 ILE   B HG13 1 
ATOM   7104 H HG21 . ILE   B 1 177 ? 7.622   -19.478 12.951  1.00 53.31  ? 162 ILE   B HG21 1 
ATOM   7105 H HG22 . ILE   B 1 177 ? 8.536   -18.202 12.707  1.00 53.31  ? 162 ILE   B HG22 1 
ATOM   7106 H HG23 . ILE   B 1 177 ? 8.205   -18.670 14.189  1.00 53.31  ? 162 ILE   B HG23 1 
ATOM   7107 H HD11 . ILE   B 1 177 ? 4.393   -19.828 14.667  1.00 57.72  ? 162 ILE   B HD11 1 
ATOM   7108 H HD12 . ILE   B 1 177 ? 4.805   -19.696 13.138  1.00 57.72  ? 162 ILE   B HD12 1 
ATOM   7109 H HD13 . ILE   B 1 177 ? 5.851   -20.250 14.198  1.00 57.72  ? 162 ILE   B HD13 1 
ATOM   7110 N N    . GLY   B 1 178 ? 5.160   -15.220 12.439  1.00 40.15  ? 163 GLY   B N    1 
ATOM   7111 C CA   . GLY   B 1 178 ? 3.860   -14.603 12.337  1.00 40.68  ? 163 GLY   B CA   1 
ATOM   7112 C C    . GLY   B 1 178 ? 3.853   -13.168 12.834  1.00 40.18  ? 163 GLY   B C    1 
ATOM   7113 O O    . GLY   B 1 178 ? 4.835   -12.428 12.731  1.00 38.28  ? 163 GLY   B O    1 
ATOM   7114 H H    . GLY   B 1 178 ? 5.492   -15.467 11.685  1.00 48.18  ? 163 GLY   B H    1 
ATOM   7115 H HA2  . GLY   B 1 178 ? 3.576   -14.605 11.410  1.00 48.81  ? 163 GLY   B HA2  1 
ATOM   7116 H HA3  . GLY   B 1 178 ? 3.222   -15.110 12.863  1.00 48.81  ? 163 GLY   B HA3  1 
ATOM   7117 N N    . ALA   B 1 179 ? 2.711   -12.776 13.404  1.00 39.09  ? 164 ALA   B N    1 
ATOM   7118 C CA   . ALA   B 1 179 ? 2.518   -11.388 13.807  1.00 40.01  ? 164 ALA   B CA   1 
ATOM   7119 C C    . ALA   B 1 179 ? 3.495   -10.981 14.904  1.00 41.53  ? 164 ALA   B C    1 
ATOM   7120 O O    . ALA   B 1 179 ? 4.023   -9.862  14.890  1.00 37.57  ? 164 ALA   B O    1 
ATOM   7121 C CB   . ALA   B 1 179 ? 1.077   -11.184 14.268  1.00 46.44  ? 164 ALA   B CB   1 
ATOM   7122 H H    . ALA   B 1 179 ? 2.041   -13.290 13.566  1.00 46.91  ? 164 ALA   B H    1 
ATOM   7123 H HA   . ALA   B 1 179 ? 2.681   -10.813 13.043  1.00 48.01  ? 164 ALA   B HA   1 
ATOM   7124 H HB1  . ALA   B 1 179 ? 0.958   -10.259 14.533  1.00 55.72  ? 164 ALA   B HB1  1 
ATOM   7125 H HB2  . ALA   B 1 179 ? 0.479   -11.398 13.535  1.00 55.72  ? 164 ALA   B HB2  1 
ATOM   7126 H HB3  . ALA   B 1 179 ? 0.901   -11.769 15.021  1.00 55.72  ? 164 ALA   B HB3  1 
ATOM   7127 N N    . GLU   B 1 180 ? 3.757   -11.875 15.857  1.00 40.13  ? 165 GLU   B N    1 
ATOM   7128 C CA   . GLU   B 1 180 ? 4.648   -11.538 16.962  1.00 43.18  ? 165 GLU   B CA   1 
ATOM   7129 C C    . GLU   B 1 180 ? 6.021   -11.112 16.449  1.00 42.50  ? 165 GLU   B C    1 
ATOM   7130 O O    . GLU   B 1 180 ? 6.576   -10.097 16.886  1.00 37.17  ? 165 GLU   B O    1 
ATOM   7131 C CB   . GLU   B 1 180 ? 4.755   -12.724 17.919  1.00 42.53  ? 165 GLU   B CB   1 
ATOM   7132 C CG   . GLU   B 1 180 ? 4.876   -12.331 19.382  1.00 46.52  ? 165 GLU   B CG   1 
ATOM   7133 C CD   . GLU   B 1 180 ? 4.500   -13.457 20.329  1.00 53.43  ? 165 GLU   B CD   1 
ATOM   7134 O OE1  . GLU   B 1 180 ? 3.616   -14.266 19.975  1.00 51.00  ? 165 GLU   B OE1  1 
ATOM   7135 O OE2  . GLU   B 1 180 ? 5.095   -13.535 21.425  1.00 59.77  ? 165 GLU   B OE2  1 
ATOM   7136 H H    . GLU   B 1 180 ? 3.436   -12.672 15.885  1.00 48.15  ? 165 GLU   B H    1 
ATOM   7137 H HA   . GLU   B 1 180 ? 4.276   -10.790 17.456  1.00 51.82  ? 165 GLU   B HA   1 
ATOM   7138 H HB2  . GLU   B 1 180 ? 3.959   -13.271 17.825  1.00 51.04  ? 165 GLU   B HB2  1 
ATOM   7139 H HB3  . GLU   B 1 180 ? 5.542   -13.241 17.686  1.00 51.04  ? 165 GLU   B HB3  1 
ATOM   7140 H HG2  . GLU   B 1 180 ? 5.795   -12.079 19.567  1.00 55.83  ? 165 GLU   B HG2  1 
ATOM   7141 H HG3  . GLU   B 1 180 ? 4.285   -11.582 19.558  1.00 55.83  ? 165 GLU   B HG3  1 
ATOM   7142 N N    . LEU   B 1 181 ? 6.578   -11.871 15.498  1.00 37.73  ? 166 LEU   B N    1 
ATOM   7143 C CA   . LEU   B 1 181 ? 7.851   -11.484 14.903  1.00 37.19  ? 166 LEU   B CA   1 
ATOM   7144 C C    . LEU   B 1 181 ? 7.740   -10.146 14.181  1.00 36.53  ? 166 LEU   B C    1 
ATOM   7145 O O    . LEU   B 1 181 ? 8.616   -9.285  14.321  1.00 35.93  ? 166 LEU   B O    1 
ATOM   7146 C CB   . LEU   B 1 181 ? 8.338   -12.569 13.940  1.00 39.21  ? 166 LEU   B CB   1 
ATOM   7147 C CG   . LEU   B 1 181 ? 9.639   -12.234 13.202  1.00 37.01  ? 166 LEU   B CG   1 
ATOM   7148 C CD1  . LEU   B 1 181 ? 10.744  -11.933 14.189  1.00 36.97  ? 166 LEU   B CD1  1 
ATOM   7149 C CD2  . LEU   B 1 181 ? 10.046  -13.378 12.266  1.00 38.95  ? 166 LEU   B CD2  1 
ATOM   7150 H H    . LEU   B 1 181 ? 6.242   -12.600 15.189  1.00 45.28  ? 166 LEU   B H    1 
ATOM   7151 H HA   . LEU   B 1 181 ? 8.507   -11.393 15.612  1.00 44.63  ? 166 LEU   B HA   1 
ATOM   7152 H HB2  . LEU   B 1 181 ? 8.490   -13.383 14.445  1.00 47.06  ? 166 LEU   B HB2  1 
ATOM   7153 H HB3  . LEU   B 1 181 ? 7.652   -12.717 13.270  1.00 47.06  ? 166 LEU   B HB3  1 
ATOM   7154 H HG   . LEU   B 1 181 ? 9.495   -11.444 12.658  1.00 44.42  ? 166 LEU   B HG   1 
ATOM   7155 H HD11 . LEU   B 1 181 ? 11.588  -11.885 13.713  1.00 44.37  ? 166 LEU   B HD11 1 
ATOM   7156 H HD12 . LEU   B 1 181 ? 10.559  -11.084 14.620  1.00 44.37  ? 166 LEU   B HD12 1 
ATOM   7157 H HD13 . LEU   B 1 181 ? 10.777  -12.640 14.851  1.00 44.37  ? 166 LEU   B HD13 1 
ATOM   7158 H HD21 . LEU   B 1 181 ? 10.828  -13.108 11.759  1.00 46.74  ? 166 LEU   B HD21 1 
ATOM   7159 H HD22 . LEU   B 1 181 ? 10.251  -14.163 12.797  1.00 46.74  ? 166 LEU   B HD22 1 
ATOM   7160 H HD23 . LEU   B 1 181 ? 9.311   -13.570 11.663  1.00 46.74  ? 166 LEU   B HD23 1 
ATOM   7161 N N    . ALA   B 1 182 ? 6.671   -9.952  13.404  1.00 36.66  ? 167 ALA   B N    1 
ATOM   7162 C CA   . ALA   B 1 182 ? 6.522   -8.710  12.651  1.00 38.32  ? 167 ALA   B CA   1 
ATOM   7163 C C    . ALA   B 1 182 ? 6.498   -7.502  13.582  1.00 35.69  ? 167 ALA   B C    1 
ATOM   7164 O O    . ALA   B 1 182 ? 7.215   -6.521  13.361  1.00 35.00  ? 167 ALA   B O    1 
ATOM   7165 C CB   . ALA   B 1 182 ? 5.252   -8.756  11.802  1.00 38.37  ? 167 ALA   B CB   1 
ATOM   7166 H H    . ALA   B 1 182 ? 6.030   -10.516 13.298  1.00 44.00  ? 167 ALA   B H    1 
ATOM   7167 H HA   . ALA   B 1 182 ? 7.280   -8.618  12.054  1.00 45.98  ? 167 ALA   B HA   1 
ATOM   7168 H HB1  . ALA   B 1 182 ? 5.169   -7.923  11.312  1.00 46.05  ? 167 ALA   B HB1  1 
ATOM   7169 H HB2  . ALA   B 1 182 ? 5.312   -9.500  11.183  1.00 46.05  ? 167 ALA   B HB2  1 
ATOM   7170 H HB3  . ALA   B 1 182 ? 4.486   -8.873  12.386  1.00 46.05  ? 167 ALA   B HB3  1 
ATOM   7171 N N    . ARG   B 1 183 ? 5.673   -7.558  14.634  1.00 36.14  ? 168 ARG   B N    1 
ATOM   7172 C CA   . ARG   B 1 183 ? 5.606   -6.441  15.568  1.00 35.89  ? 168 ARG   B CA   1 
ATOM   7173 C C    . ARG   B 1 183 ? 6.956   -6.208  16.235  1.00 35.80  ? 168 ARG   B C    1 
ATOM   7174 O O    . ARG   B 1 183 ? 7.367   -5.060  16.442  1.00 35.01  ? 168 ARG   B O    1 
ATOM   7175 C CB   . ARG   B 1 183 ? 4.526   -6.685  16.626  1.00 37.34  ? 168 ARG   B CB   1 
ATOM   7176 C CG   . ARG   B 1 183 ? 3.130   -7.002  16.085  1.00 41.50  ? 168 ARG   B CG   1 
ATOM   7177 C CD   . ARG   B 1 183 ? 2.471   -5.821  15.419  1.00 36.73  ? 168 ARG   B CD   1 
ATOM   7178 N NE   . ARG   B 1 183 ? 3.104   -5.490  14.152  1.00 46.36  ? 168 ARG   B NE   1 
ATOM   7179 C CZ   . ARG   B 1 183 ? 2.912   -6.150  13.020  1.00 43.45  ? 168 ARG   B CZ   1 
ATOM   7180 N NH1  . ARG   B 1 183 ? 2.118   -7.208  12.963  1.00 48.15  ? 168 ARG   B NH1  1 
ATOM   7181 N NH2  . ARG   B 1 183 ? 3.537   -5.743  11.919  1.00 41.35  ? 168 ARG   B NH2  1 
ATOM   7182 H H    . ARG   B 1 183 ? 5.156   -8.219  14.823  1.00 43.37  ? 168 ARG   B H    1 
ATOM   7183 H HA   . ARG   B 1 183 ? 5.361   -5.642  15.075  1.00 43.07  ? 168 ARG   B HA   1 
ATOM   7184 H HB2  . ARG   B 1 183 ? 4.801   -7.438  17.173  1.00 44.80  ? 168 ARG   B HB2  1 
ATOM   7185 H HB3  . ARG   B 1 183 ? 4.449   -5.888  17.173  1.00 44.80  ? 168 ARG   B HB3  1 
ATOM   7186 H HG2  . ARG   B 1 183 ? 3.200   -7.714  15.429  1.00 49.80  ? 168 ARG   B HG2  1 
ATOM   7187 H HG3  . ARG   B 1 183 ? 2.564   -7.284  16.820  1.00 49.80  ? 168 ARG   B HG3  1 
ATOM   7188 H HD2  . ARG   B 1 183 ? 1.539   -6.030  15.246  1.00 44.07  ? 168 ARG   B HD2  1 
ATOM   7189 H HD3  . ARG   B 1 183 ? 2.535   -5.048  16.001  1.00 44.07  ? 168 ARG   B HD3  1 
ATOM   7190 H HE   . ARG   B 1 183 ? 3.641   -4.818  14.138  1.00 55.63  ? 168 ARG   B HE   1 
ATOM   7191 H HH11 . ARG   B 1 183 ? 1.713   -7.480  13.672  1.00 57.78  ? 168 ARG   B HH11 1 
ATOM   7192 H HH12 . ARG   B 1 183 ? 2.006   -7.623  12.218  1.00 57.78  ? 168 ARG   B HH12 1 
ATOM   7193 H HH21 . ARG   B 1 183 ? 4.057   -5.060  11.948  1.00 49.62  ? 168 ARG   B HH21 1 
ATOM   7194 H HH22 . ARG   B 1 183 ? 3.420   -6.164  11.178  1.00 49.62  ? 168 ARG   B HH22 1 
ATOM   7195 N N    . ARG   B 1 184 ? 7.658   -7.289  16.584  1.00 35.78  ? 169 ARG   B N    1 
ATOM   7196 C CA   . ARG   B 1 184 ? 8.987   -7.141  17.168  1.00 35.50  ? 169 ARG   B CA   1 
ATOM   7197 C C    . ARG   B 1 184 ? 9.905   -6.370  16.228  1.00 35.40  ? 169 ARG   B C    1 
ATOM   7198 O O    . ARG   B 1 184 ? 10.564  -5.408  16.637  1.00 36.42  ? 169 ARG   B O    1 
ATOM   7199 C CB   . ARG   B 1 184 ? 9.572   -8.515  17.498  1.00 38.67  ? 169 ARG   B CB   1 
ATOM   7200 C CG   . ARG   B 1 184 ? 10.994  -8.465  18.018  1.00 40.00  ? 169 ARG   B CG   1 
ATOM   7201 C CD   . ARG   B 1 184 ? 11.208  -9.434  19.171  1.00 56.85  ? 169 ARG   B CD   1 
ATOM   7202 N NE   . ARG   B 1 184 ? 11.100  -10.831 18.768  1.00 57.97  ? 169 ARG   B NE   1 
ATOM   7203 C CZ   . ARG   B 1 184 ? 12.133  -11.626 18.513  1.00 66.19  ? 169 ARG   B CZ   1 
ATOM   7204 N NH1  . ARG   B 1 184 ? 13.381  -11.188 18.586  1.00 60.20  ? 169 ARG   B NH1  1 
ATOM   7205 N NH2  . ARG   B 1 184 ? 11.907  -12.896 18.186  1.00 51.21  ? 169 ARG   B NH2  1 
ATOM   7206 H H    . ARG   B 1 184 ? 7.392   -8.102  16.495  1.00 42.93  ? 169 ARG   B H    1 
ATOM   7207 H HA   . ARG   B 1 184 ? 8.915   -6.643  17.997  1.00 42.60  ? 169 ARG   B HA   1 
ATOM   7208 H HB2  . ARG   B 1 184 ? 9.022   -8.932  18.180  1.00 46.41  ? 169 ARG   B HB2  1 
ATOM   7209 H HB3  . ARG   B 1 184 ? 9.570   -9.057  16.694  1.00 46.41  ? 169 ARG   B HB3  1 
ATOM   7210 H HG2  . ARG   B 1 184 ? 11.604  -8.704  17.303  1.00 48.00  ? 169 ARG   B HG2  1 
ATOM   7211 H HG3  . ARG   B 1 184 ? 11.188  -7.569  18.334  1.00 48.00  ? 169 ARG   B HG3  1 
ATOM   7212 H HD2  . ARG   B 1 184 ? 12.095  -9.296  19.538  1.00 68.22  ? 169 ARG   B HD2  1 
ATOM   7213 H HD3  . ARG   B 1 184 ? 10.538  -9.266  19.852  1.00 68.22  ? 169 ARG   B HD3  1 
ATOM   7214 H HE   . ARG   B 1 184 ? 10.311  -11.164 18.689  1.00 69.57  ? 169 ARG   B HE   1 
ATOM   7215 H HH11 . ARG   B 1 184 ? 13.539  -10.371 18.803  1.00 72.24  ? 169 ARG   B HH11 1 
ATOM   7216 H HH12 . ARG   B 1 184 ? 14.035  -11.722 18.417  1.00 72.24  ? 169 ARG   B HH12 1 
ATOM   7217 H HH21 . ARG   B 1 184 ? 11.100  -13.191 18.142  1.00 61.46  ? 169 ARG   B HH21 1 
ATOM   7218 H HH22 . ARG   B 1 184 ? 12.567  -13.421 18.019  1.00 61.46  ? 169 ARG   B HH22 1 
ATOM   7219 N N    . LEU   B 1 185 ? 9.951   -6.771  14.956  1.00 34.57  ? 170 LEU   B N    1 
ATOM   7220 C CA   . LEU   B 1 185 ? 10.766  -6.038  13.994  1.00 33.95  ? 170 LEU   B CA   1 
ATOM   7221 C C    . LEU   B 1 185 ? 10.316  -4.584  13.892  1.00 38.29  ? 170 LEU   B C    1 
ATOM   7222 O O    . LEU   B 1 185 ? 11.145  -3.674  13.791  1.00 36.24  ? 170 LEU   B O    1 
ATOM   7223 C CB   . LEU   B 1 185 ? 10.708  -6.726  12.631  1.00 37.10  ? 170 LEU   B CB   1 
ATOM   7224 C CG   . LEU   B 1 185 ? 11.308  -8.139  12.568  1.00 35.34  ? 170 LEU   B CG   1 
ATOM   7225 C CD1  . LEU   B 1 185 ? 10.992  -8.781  11.223  1.00 36.98  ? 170 LEU   B CD1  1 
ATOM   7226 C CD2  . LEU   B 1 185 ? 12.815  -8.124  12.806  1.00 33.85  ? 170 LEU   B CD2  1 
ATOM   7227 H H    . LEU   B 1 185 ? 9.529   -7.447  14.634  1.00 41.49  ? 170 LEU   B H    1 
ATOM   7228 H HA   . LEU   B 1 185 ? 11.691  -6.043  14.288  1.00 40.74  ? 170 LEU   B HA   1 
ATOM   7229 H HB2  . LEU   B 1 185 ? 9.778   -6.797  12.366  1.00 44.51  ? 170 LEU   B HB2  1 
ATOM   7230 H HB3  . LEU   B 1 185 ? 11.194  -6.179  11.994  1.00 44.51  ? 170 LEU   B HB3  1 
ATOM   7231 H HG   . LEU   B 1 185 ? 10.911  -8.673  13.274  1.00 42.41  ? 170 LEU   B HG   1 
ATOM   7232 H HD11 . LEU   B 1 185 ? 11.383  -9.668  11.197  1.00 44.37  ? 170 LEU   B HD11 1 
ATOM   7233 H HD12 . LEU   B 1 185 ? 10.030  -8.840  11.121  1.00 44.37  ? 170 LEU   B HD12 1 
ATOM   7234 H HD13 . LEU   B 1 185 ? 11.367  -8.233  10.516  1.00 44.37  ? 170 LEU   B HD13 1 
ATOM   7235 H HD21 . LEU   B 1 185 ? 13.161  -9.023  12.697  1.00 40.62  ? 170 LEU   B HD21 1 
ATOM   7236 H HD22 . LEU   B 1 185 ? 13.230  -7.529  12.161  1.00 40.62  ? 170 LEU   B HD22 1 
ATOM   7237 H HD23 . LEU   B 1 185 ? 12.989  -7.809  13.706  1.00 40.62  ? 170 LEU   B HD23 1 
ATOM   7238 N N    . GLU   B 1 186 ? 9.005   -4.344  13.960  1.00 40.43  ? 171 GLU   B N    1 
ATOM   7239 C CA   . GLU   B 1 186 ? 8.487   -2.987  13.820  1.00 37.35  ? 171 GLU   B CA   1 
ATOM   7240 C C    . GLU   B 1 186 ? 8.826   -2.133  15.035  1.00 33.08  ? 171 GLU   B C    1 
ATOM   7241 O O    . GLU   B 1 186 ? 9.278   -0.990  14.896  1.00 38.09  ? 171 GLU   B O    1 
ATOM   7242 C CB   . GLU   B 1 186 ? 6.972   -3.037  13.598  1.00 37.89  ? 171 GLU   B CB   1 
ATOM   7243 C CG   . GLU   B 1 186 ? 6.315   -1.674  13.507  1.00 41.91  ? 171 GLU   B CG   1 
ATOM   7244 C CD   . GLU   B 1 186 ? 4.833   -1.758  13.197  1.00 51.22  ? 171 GLU   B CD   1 
ATOM   7245 O OE1  . GLU   B 1 186 ? 4.293   -2.886  13.132  1.00 43.86  ? 171 GLU   B OE1  1 
ATOM   7246 O OE2  . GLU   B 1 186 ? 4.203   -0.691  13.029  1.00 40.62  ? 171 GLU   B OE2  1 
ATOM   7247 H H    . GLU   B 1 186 ? 8.401   -4.944  14.085  1.00 48.51  ? 171 GLU   B H    1 
ATOM   7248 H HA   . GLU   B 1 186 ? 8.897   -2.571  13.045  1.00 44.82  ? 171 GLU   B HA   1 
ATOM   7249 H HB2  . GLU   B 1 186 ? 6.795   -3.507  12.768  1.00 45.47  ? 171 GLU   B HB2  1 
ATOM   7250 H HB3  . GLU   B 1 186 ? 6.565   -3.511  14.341  1.00 45.47  ? 171 GLU   B HB3  1 
ATOM   7251 H HG2  . GLU   B 1 186 ? 6.419   -1.215  14.355  1.00 50.29  ? 171 GLU   B HG2  1 
ATOM   7252 H HG3  . GLU   B 1 186 ? 6.741   -1.165  12.799  1.00 50.29  ? 171 GLU   B HG3  1 
ATOM   7253 N N    . PHE   B 1 187 ? 8.621   -2.662  16.237  1.00 33.70  ? 172 PHE   B N    1 
ATOM   7254 C CA   . PHE   B 1 187 ? 8.770   -1.866  17.447  1.00 41.40  ? 172 PHE   B CA   1 
ATOM   7255 C C    . PHE   B 1 187 ? 10.218  -1.823  17.924  1.00 44.01  ? 172 PHE   B C    1 
ATOM   7256 O O    . PHE   B 1 187 ? 10.711  -0.755  18.305  1.00 35.67  ? 172 PHE   B O    1 
ATOM   7257 C CB   . PHE   B 1 187 ? 7.858   -2.416  18.554  1.00 34.54  ? 172 PHE   B CB   1 
ATOM   7258 C CG   . PHE   B 1 187 ? 6.393   -2.378  18.209  1.00 34.88  ? 172 PHE   B CG   1 
ATOM   7259 C CD1  . PHE   B 1 187 ? 5.871   -1.354  17.440  1.00 38.09  ? 172 PHE   B CD1  1 
ATOM   7260 C CD2  . PHE   B 1 187 ? 5.539   -3.371  18.649  1.00 35.54  ? 172 PHE   B CD2  1 
ATOM   7261 C CE1  . PHE   B 1 187 ? 4.528   -1.319  17.124  1.00 38.02  ? 172 PHE   B CE1  1 
ATOM   7262 C CE2  . PHE   B 1 187 ? 4.193   -3.343  18.332  1.00 35.88  ? 172 PHE   B CE2  1 
ATOM   7263 C CZ   . PHE   B 1 187 ? 3.687   -2.318  17.574  1.00 36.31  ? 172 PHE   B CZ   1 
ATOM   7264 H H    . PHE   B 1 187 ? 8.394   -3.479  16.378  1.00 40.44  ? 172 PHE   B H    1 
ATOM   7265 H HA   . PHE   B 1 187 ? 8.491   -0.954  17.266  1.00 49.68  ? 172 PHE   B HA   1 
ATOM   7266 H HB2  . PHE   B 1 187 ? 8.098   -3.340  18.725  1.00 41.44  ? 172 PHE   B HB2  1 
ATOM   7267 H HB3  . PHE   B 1 187 ? 7.987   -1.886  19.356  1.00 41.44  ? 172 PHE   B HB3  1 
ATOM   7268 H HD1  . PHE   B 1 187 ? 6.433   -0.681  17.131  1.00 45.71  ? 172 PHE   B HD1  1 
ATOM   7269 H HD2  . PHE   B 1 187 ? 5.874   -4.068  19.165  1.00 42.64  ? 172 PHE   B HD2  1 
ATOM   7270 H HE1  . PHE   B 1 187 ? 4.190   -0.622  16.608  1.00 45.62  ? 172 PHE   B HE1  1 
ATOM   7271 H HE2  . PHE   B 1 187 ? 3.630   -4.019  18.633  1.00 43.05  ? 172 PHE   B HE2  1 
ATOM   7272 H HZ   . PHE   B 1 187 ? 2.781   -2.296  17.364  1.00 43.57  ? 172 PHE   B HZ   1 
ATOM   7273 N N    . ILE   B 1 188 ? 10.907  -2.966  17.912  1.00 35.98  ? 173 ILE   B N    1 
ATOM   7274 C CA   . ILE   B 1 188 ? 12.308  -2.990  18.326  1.00 36.58  ? 173 ILE   B CA   1 
ATOM   7275 C C    . ILE   B 1 188 ? 13.221  -2.569  17.176  1.00 37.67  ? 173 ILE   B C    1 
ATOM   7276 O O    . ILE   B 1 188 ? 14.257  -1.937  17.406  1.00 43.70  ? 173 ILE   B O    1 
ATOM   7277 C CB   . ILE   B 1 188 ? 12.688  -4.387  18.855  1.00 46.06  ? 173 ILE   B CB   1 
ATOM   7278 C CG1  . ILE   B 1 188 ? 11.677  -4.843  19.908  1.00 47.04  ? 173 ILE   B CG1  1 
ATOM   7279 C CG2  . ILE   B 1 188 ? 14.106  -4.387  19.438  1.00 42.59  ? 173 ILE   B CG2  1 
ATOM   7280 C CD1  . ILE   B 1 188 ? 12.169  -5.957  20.798  1.00 43.33  ? 173 ILE   B CD1  1 
ATOM   7281 H H    . ILE   B 1 188 ? 10.591  -3.729  17.672  1.00 43.17  ? 173 ILE   B H    1 
ATOM   7282 H HA   . ILE   B 1 188 ? 12.424  -2.354  19.049  1.00 43.90  ? 173 ILE   B HA   1 
ATOM   7283 H HB   . ILE   B 1 188 ? 12.669  -5.008  18.111  1.00 55.28  ? 173 ILE   B HB   1 
ATOM   7284 H HG12 . ILE   B 1 188 ? 11.458  -4.088  20.476  1.00 56.44  ? 173 ILE   B HG12 1 
ATOM   7285 H HG13 . ILE   B 1 188 ? 10.879  -5.159  19.455  1.00 56.44  ? 173 ILE   B HG13 1 
ATOM   7286 H HG21 . ILE   B 1 188 ? 14.403  -5.304  19.544  1.00 51.11  ? 173 ILE   B HG21 1 
ATOM   7287 H HG22 . ILE   B 1 188 ? 14.697  -3.915  18.830  1.00 51.11  ? 173 ILE   B HG22 1 
ATOM   7288 H HG23 . ILE   B 1 188 ? 14.093  -3.941  20.300  1.00 51.11  ? 173 ILE   B HG23 1 
ATOM   7289 H HD11 . ILE   B 1 188 ? 11.407  -6.384  21.220  1.00 52.00  ? 173 ILE   B HD11 1 
ATOM   7290 H HD12 . ILE   B 1 188 ? 12.652  -6.602  20.258  1.00 52.00  ? 173 ILE   B HD12 1 
ATOM   7291 H HD13 . ILE   B 1 188 ? 12.757  -5.585  21.474  1.00 52.00  ? 173 ILE   B HD13 1 
ATOM   7292 N N    . GLY   B 1 189 ? 12.868  -2.916  15.939  1.00 34.12  ? 174 GLY   B N    1 
ATOM   7293 C CA   . GLY   B 1 189 ? 13.642  -2.513  14.782  1.00 31.53  ? 174 GLY   B CA   1 
ATOM   7294 C C    . GLY   B 1 189 ? 14.197  -3.676  13.986  1.00 32.26  ? 174 GLY   B C    1 
ATOM   7295 O O    . GLY   B 1 189 ? 14.416  -4.766  14.528  1.00 32.25  ? 174 GLY   B O    1 
ATOM   7296 H H    . GLY   B 1 189 ? 12.176  -3.389  15.747  1.00 40.95  ? 174 GLY   B H    1 
ATOM   7297 H HA2  . GLY   B 1 189 ? 13.079  -1.987  14.193  1.00 37.84  ? 174 GLY   B HA2  1 
ATOM   7298 H HA3  . GLY   B 1 189 ? 14.389  -1.967  15.076  1.00 37.84  ? 174 GLY   B HA3  1 
ATOM   7299 N N    . THR   B 1 190 ? 14.419  -3.466  12.695  1.00 33.60  ? 175 THR   B N    1 
ATOM   7300 C CA   . THR   B 1 190 ? 15.131  -4.453  11.906  1.00 32.42  ? 175 THR   B CA   1 
ATOM   7301 C C    . THR   B 1 190 ? 16.592  -4.492  12.347  1.00 30.65  ? 175 THR   B C    1 
ATOM   7302 O O    . THR   B 1 190 ? 17.085  -3.549  12.966  1.00 32.74  ? 175 THR   B O    1 
ATOM   7303 C CB   . THR   B 1 190 ? 15.028  -4.129  10.421  1.00 35.04  ? 175 THR   B CB   1 
ATOM   7304 O OG1  . THR   B 1 190 ? 15.319  -2.743  10.219  1.00 41.28  ? 175 THR   B OG1  1 
ATOM   7305 C CG2  . THR   B 1 190 ? 13.631  -4.429  9.906   1.00 41.21  ? 175 THR   B CG2  1 
ATOM   7306 H H    . THR   B 1 190 ? 14.169  -2.767  12.259  1.00 40.32  ? 175 THR   B H    1 
ATOM   7307 H HA   . THR   B 1 190 ? 14.743  -5.333  12.035  1.00 38.91  ? 175 THR   B HA   1 
ATOM   7308 H HB   . THR   B 1 190 ? 15.659  -4.672  9.923   1.00 42.04  ? 175 THR   B HB   1 
ATOM   7309 H HG1  . THR   B 1 190 ? 15.265  -2.554  9.402   1.00 49.53  ? 175 THR   B HG1  1 
ATOM   7310 H HG21 . THR   B 1 190 ? 13.572  -4.216  8.961   1.00 49.46  ? 175 THR   B HG21 1 
ATOM   7311 H HG22 . THR   B 1 190 ? 13.426  -5.369  10.030  1.00 49.46  ? 175 THR   B HG22 1 
ATOM   7312 H HG23 . THR   B 1 190 ? 12.978  -3.898  10.389  1.00 49.46  ? 175 THR   B HG23 1 
ATOM   7313 N N    . PRO   B 1 191 ? 17.301  -5.588  12.059  1.00 30.93  ? 176 PRO   B N    1 
ATOM   7314 C CA   . PRO   B 1 191 ? 18.689  -5.704  12.525  1.00 32.27  ? 176 PRO   B CA   1 
ATOM   7315 C C    . PRO   B 1 191 ? 19.719  -5.045  11.627  1.00 29.73  ? 176 PRO   B C    1 
ATOM   7316 O O    . PRO   B 1 191 ? 20.859  -4.859  12.067  1.00 29.50  ? 176 PRO   B O    1 
ATOM   7317 C CB   . PRO   B 1 191 ? 18.920  -7.221  12.550  1.00 31.64  ? 176 PRO   B CB   1 
ATOM   7318 C CG   . PRO   B 1 191 ? 18.029  -7.732  11.474  1.00 33.42  ? 176 PRO   B CG   1 
ATOM   7319 C CD   . PRO   B 1 191 ? 16.804  -6.856  11.496  1.00 31.60  ? 176 PRO   B CD   1 
ATOM   7320 H HA   . PRO   B 1 191 ? 18.758  -5.332  13.418  1.00 38.72  ? 176 PRO   B HA   1 
ATOM   7321 H HB2  . PRO   B 1 191 ? 19.850  -7.422  12.362  1.00 37.96  ? 176 PRO   B HB2  1 
ATOM   7322 H HB3  . PRO   B 1 191 ? 18.671  -7.583  13.415  1.00 37.96  ? 176 PRO   B HB3  1 
ATOM   7323 H HG2  . PRO   B 1 191 ? 18.481  -7.669  10.618  1.00 40.10  ? 176 PRO   B HG2  1 
ATOM   7324 H HG3  . PRO   B 1 191 ? 17.793  -8.655  11.657  1.00 40.10  ? 176 PRO   B HG3  1 
ATOM   7325 H HD2  . PRO   B 1 191 ? 16.459  -6.723  10.599  1.00 37.91  ? 176 PRO   B HD2  1 
ATOM   7326 H HD3  . PRO   B 1 191 ? 16.116  -7.239  12.063  1.00 37.91  ? 176 PRO   B HD3  1 
ATOM   7327 N N    . TYR   B 1 192 ? 19.366  -4.716  10.388  1.00 29.09  ? 177 TYR   B N    1 
ATOM   7328 C CA   . TYR   B 1 192 ? 20.388  -4.518  9.364   1.00 28.18  ? 177 TYR   B CA   1 
ATOM   7329 C C    . TYR   B 1 192 ? 21.317  -3.354  9.694   1.00 27.28  ? 177 TYR   B C    1 
ATOM   7330 O O    . TYR   B 1 192 ? 22.504  -3.405  9.370   1.00 26.76  ? 177 TYR   B O    1 
ATOM   7331 C CB   . TYR   B 1 192 ? 19.711  -4.329  8.011   1.00 27.69  ? 177 TYR   B CB   1 
ATOM   7332 C CG   . TYR   B 1 192 ? 18.799  -5.489  7.666   1.00 28.65  ? 177 TYR   B CG   1 
ATOM   7333 C CD1  . TYR   B 1 192 ? 19.323  -6.691  7.210   1.00 29.09  ? 177 TYR   B CD1  1 
ATOM   7334 C CD2  . TYR   B 1 192 ? 17.426  -5.390  7.818   1.00 29.15  ? 177 TYR   B CD2  1 
ATOM   7335 C CE1  . TYR   B 1 192 ? 18.505  -7.757  6.904   1.00 31.94  ? 177 TYR   B CE1  1 
ATOM   7336 C CE2  . TYR   B 1 192 ? 16.595  -6.455  7.517   1.00 31.86  ? 177 TYR   B CE2  1 
ATOM   7337 C CZ   . TYR   B 1 192 ? 17.142  -7.637  7.059   1.00 35.73  ? 177 TYR   B CZ   1 
ATOM   7338 O OH   . TYR   B 1 192 ? 16.334  -8.706  6.754   1.00 38.22  ? 177 TYR   B OH   1 
ATOM   7339 H H    . TYR   B 1 192 ? 18.557  -4.603  10.118  1.00 34.91  ? 177 TYR   B H    1 
ATOM   7340 H HA   . TYR   B 1 192 ? 20.949  -5.308  9.312   1.00 33.82  ? 177 TYR   B HA   1 
ATOM   7341 H HB2  . TYR   B 1 192 ? 19.177  -3.520  8.032   1.00 33.23  ? 177 TYR   B HB2  1 
ATOM   7342 H HB3  . TYR   B 1 192 ? 20.390  -4.261  7.321   1.00 33.23  ? 177 TYR   B HB3  1 
ATOM   7343 H HD1  . TYR   B 1 192 ? 20.244  -6.778  7.110   1.00 34.91  ? 177 TYR   B HD1  1 
ATOM   7344 H HD2  . TYR   B 1 192 ? 17.056  -4.595  8.127   1.00 34.98  ? 177 TYR   B HD2  1 
ATOM   7345 H HE1  . TYR   B 1 192 ? 18.872  -8.553  6.594   1.00 38.32  ? 177 TYR   B HE1  1 
ATOM   7346 H HE2  . TYR   B 1 192 ? 15.675  -6.374  7.622   1.00 38.23  ? 177 TYR   B HE2  1 
ATOM   7347 H HH   . TYR   B 1 192 ? 16.802  -9.363  6.521   1.00 45.86  ? 177 TYR   B HH   1 
ATOM   7348 N N    . TRP   B 1 193 ? 20.818  -2.331  10.379  1.00 27.14  ? 178 TRP   B N    1 
ATOM   7349 C CA   . TRP   B 1 193 ? 21.638  -1.194  10.771  1.00 29.31  ? 178 TRP   B CA   1 
ATOM   7350 C C    . TRP   B 1 193 ? 22.097  -1.263  12.218  1.00 28.83  ? 178 TRP   B C    1 
ATOM   7351 O O    . TRP   B 1 193 ? 22.782  -0.338  12.678  1.00 26.58  ? 178 TRP   B O    1 
ATOM   7352 C CB   . TRP   B 1 193 ? 20.871  0.113   10.557  1.00 25.74  ? 178 TRP   B CB   1 
ATOM   7353 C CG   . TRP   B 1 193 ? 20.602  0.473   9.110   1.00 24.84  ? 178 TRP   B CG   1 
ATOM   7354 C CD1  . TRP   B 1 193 ? 21.357  1.293   8.319   1.00 23.58  ? 178 TRP   B CD1  1 
ATOM   7355 C CD2  . TRP   B 1 193 ? 19.493  0.053   8.304   1.00 26.72  ? 178 TRP   B CD2  1 
ATOM   7356 N NE1  . TRP   B 1 193 ? 20.792  1.407   7.080   1.00 23.06  ? 178 TRP   B NE1  1 
ATOM   7357 C CE2  . TRP   B 1 193 ? 19.647  0.659   7.040   1.00 24.03  ? 178 TRP   B CE2  1 
ATOM   7358 C CE3  . TRP   B 1 193 ? 18.386  -0.779  8.526   1.00 27.38  ? 178 TRP   B CE3  1 
ATOM   7359 C CZ2  . TRP   B 1 193 ? 18.746  0.457   6.001   1.00 24.06  ? 178 TRP   B CZ2  1 
ATOM   7360 C CZ3  . TRP   B 1 193 ? 17.487  -0.975  7.497   1.00 26.23  ? 178 TRP   B CZ3  1 
ATOM   7361 C CH2  . TRP   B 1 193 ? 17.676  -0.366  6.244   1.00 26.88  ? 178 TRP   B CH2  1 
ATOM   7362 H H    . TRP   B 1 193 ? 19.998  -2.274  10.631  1.00 32.57  ? 178 TRP   B H    1 
ATOM   7363 H HA   . TRP   B 1 193 ? 22.425  -1.181  10.203  1.00 35.17  ? 178 TRP   B HA   1 
ATOM   7364 H HB2  . TRP   B 1 193 ? 20.013  0.040   11.003  1.00 30.89  ? 178 TRP   B HB2  1 
ATOM   7365 H HB3  . TRP   B 1 193 ? 21.386  0.837   10.945  1.00 30.89  ? 178 TRP   B HB3  1 
ATOM   7366 H HD1  . TRP   B 1 193 ? 22.143  1.713   8.586   1.00 28.30  ? 178 TRP   B HD1  1 
ATOM   7367 H HE1  . TRP   B 1 193 ? 21.106  1.874   6.430   1.00 27.67  ? 178 TRP   B HE1  1 
ATOM   7368 H HE3  . TRP   B 1 193 ? 18.260  -1.191  9.351   1.00 32.85  ? 178 TRP   B HE3  1 
ATOM   7369 H HZ2  . TRP   B 1 193 ? 18.864  0.864   5.173   1.00 28.87  ? 178 TRP   B HZ2  1 
ATOM   7370 H HZ3  . TRP   B 1 193 ? 16.744  -1.518  7.635   1.00 31.48  ? 178 TRP   B HZ3  1 
ATOM   7371 H HH2  . TRP   B 1 193 ? 17.061  -0.524  5.564   1.00 32.26  ? 178 TRP   B HH2  1 
ATOM   7372 N N    . MET   B 1 194 ? 21.733  -2.312  12.951  1.00 28.19  ? 179 MET   B N    1 
ATOM   7373 C CA   . MET   B 1 194 ? 22.072  -2.400  14.360  1.00 28.91  ? 179 MET   B CA   1 
ATOM   7374 C C    . MET   B 1 194 ? 23.541  -2.764  14.543  1.00 28.88  ? 179 MET   B C    1 
ATOM   7375 O O    . MET   B 1 194 ? 24.082  -3.610  13.824  1.00 28.86  ? 179 MET   B O    1 
ATOM   7376 C CB   . MET   B 1 194 ? 21.218  -3.455  15.075  1.00 30.08  ? 179 MET   B CB   1 
ATOM   7377 C CG   . MET   B 1 194 ? 19.733  -3.182  15.140  1.00 34.07  ? 179 MET   B CG   1 
ATOM   7378 S SD   . MET   B 1 194 ? 18.906  -4.370  16.240  1.00 32.49  ? 179 MET   B SD   1 
ATOM   7379 C CE   . MET   B 1 194 ? 17.229  -3.733  16.233  1.00 31.71  ? 179 MET   B CE   1 
ATOM   7380 H H    . MET   B 1 194 ? 21.289  -2.985  12.652  1.00 33.83  ? 179 MET   B H    1 
ATOM   7381 H HA   . MET   B 1 194 ? 21.890  -1.535  14.760  1.00 34.70  ? 179 MET   B HA   1 
ATOM   7382 H HB2  . MET   B 1 194 ? 21.333  -4.300  14.613  1.00 36.10  ? 179 MET   B HB2  1 
ATOM   7383 H HB3  . MET   B 1 194 ? 21.535  -3.531  15.989  1.00 36.10  ? 179 MET   B HB3  1 
ATOM   7384 H HG2  . MET   B 1 194 ? 19.584  -2.287  15.484  1.00 40.88  ? 179 MET   B HG2  1 
ATOM   7385 H HG3  . MET   B 1 194 ? 19.350  -3.265  14.253  1.00 40.88  ? 179 MET   B HG3  1 
ATOM   7386 H HE1  . MET   B 1 194 ? 16.708  -4.209  16.899  1.00 38.05  ? 179 MET   B HE1  1 
ATOM   7387 H HE2  . MET   B 1 194 ? 17.249  -2.787  16.444  1.00 38.05  ? 179 MET   B HE2  1 
ATOM   7388 H HE3  . MET   B 1 194 ? 16.843  -3.868  15.353  1.00 38.05  ? 179 MET   B HE3  1 
ATOM   7389 N N    . ALA   B 1 195 ? 24.169  -2.144  15.535  1.00 28.97  ? 180 ALA   B N    1 
ATOM   7390 C CA   . ALA   B 1 195 ? 25.465  -2.609  15.987  1.00 29.26  ? 180 ALA   B CA   1 
ATOM   7391 C C    . ALA   B 1 195 ? 25.313  -3.956  16.690  1.00 34.76  ? 180 ALA   B C    1 
ATOM   7392 O O    . ALA   B 1 195 ? 24.257  -4.249  17.252  1.00 31.15  ? 180 ALA   B O    1 
ATOM   7393 C CB   . ALA   B 1 195 ? 26.080  -1.604  16.942  1.00 29.30  ? 180 ALA   B CB   1 
ATOM   7394 H H    . ALA   B 1 195 ? 23.866  -1.459  15.958  1.00 34.76  ? 180 ALA   B H    1 
ATOM   7395 H HA   . ALA   B 1 195 ? 26.062  -2.716  15.230  1.00 35.11  ? 180 ALA   B HA   1 
ATOM   7396 H HB1  . ALA   B 1 195 ? 26.954  -1.923  17.218  1.00 35.16  ? 180 ALA   B HB1  1 
ATOM   7397 H HB2  . ALA   B 1 195 ? 26.169  -0.751  16.488  1.00 35.16  ? 180 ALA   B HB2  1 
ATOM   7398 H HB3  . ALA   B 1 195 ? 25.503  -1.509  17.715  1.00 35.16  ? 180 ALA   B HB3  1 
ATOM   7399 N N    . PRO   B 1 196 ? 26.364  -4.787  16.694  1.00 30.94  ? 181 PRO   B N    1 
ATOM   7400 C CA   . PRO   B 1 196 ? 26.231  -6.112  17.311  1.00 33.18  ? 181 PRO   B CA   1 
ATOM   7401 C C    . PRO   B 1 196 ? 25.793  -6.059  18.764  1.00 32.87  ? 181 PRO   B C    1 
ATOM   7402 O O    . PRO   B 1 196 ? 24.994  -6.904  19.192  1.00 33.64  ? 181 PRO   B O    1 
ATOM   7403 C CB   . PRO   B 1 196 ? 27.638  -6.716  17.157  1.00 33.83  ? 181 PRO   B CB   1 
ATOM   7404 C CG   . PRO   B 1 196 ? 28.245  -5.975  16.020  1.00 30.95  ? 181 PRO   B CG   1 
ATOM   7405 C CD   . PRO   B 1 196 ? 27.702  -4.583  16.103  1.00 30.18  ? 181 PRO   B CD   1 
ATOM   7406 H HA   . PRO   B 1 196 ? 25.598  -6.646  16.806  1.00 39.81  ? 181 PRO   B HA   1 
ATOM   7407 H HB2  . PRO   B 1 196 ? 28.148  -6.582  17.971  1.00 40.60  ? 181 PRO   B HB2  1 
ATOM   7408 H HB3  . PRO   B 1 196 ? 27.572  -7.664  16.959  1.00 40.60  ? 181 PRO   B HB3  1 
ATOM   7409 H HG2  . PRO   B 1 196 ? 29.211  -5.972  16.109  1.00 37.13  ? 181 PRO   B HG2  1 
ATOM   7410 H HG3  . PRO   B 1 196 ? 27.991  -6.393  15.183  1.00 37.13  ? 181 PRO   B HG3  1 
ATOM   7411 H HD2  . PRO   B 1 196 ? 28.253  -4.029  16.677  1.00 36.21  ? 181 PRO   B HD2  1 
ATOM   7412 H HD3  . PRO   B 1 196 ? 27.634  -4.184  15.222  1.00 36.21  ? 181 PRO   B HD3  1 
ATOM   7413 N N    . GLU   B 1 197 ? 26.288  -5.093  19.543  1.00 32.75  ? 182 GLU   B N    1 
ATOM   7414 C CA   . GLU   B 1 197 ? 25.861  -5.006  20.935  1.00 33.58  ? 182 GLU   B CA   1 
ATOM   7415 C C    . GLU   B 1 197 ? 24.385  -4.645  21.035  1.00 33.54  ? 182 GLU   B C    1 
ATOM   7416 O O    . GLU   B 1 197 ? 23.697  -5.101  21.955  1.00 34.33  ? 182 GLU   B O    1 
ATOM   7417 C CB   . GLU   B 1 197 ? 26.731  -4.008  21.705  1.00 33.50  ? 182 GLU   B CB   1 
ATOM   7418 C CG   . GLU   B 1 197 ? 26.528  -2.520  21.355  1.00 32.53  ? 182 GLU   B CG   1 
ATOM   7419 C CD   . GLU   B 1 197 ? 27.443  -2.027  20.237  1.00 35.90  ? 182 GLU   B CD   1 
ATOM   7420 O OE1  . GLU   B 1 197 ? 27.997  -2.862  19.489  1.00 33.70  ? 182 GLU   B OE1  1 
ATOM   7421 O OE2  . GLU   B 1 197 ? 27.617  -0.794  20.120  1.00 30.69  ? 182 GLU   B OE2  1 
ATOM   7422 H H    . GLU   B 1 197 ? 26.854  -4.495  19.294  1.00 39.30  ? 182 GLU   B H    1 
ATOM   7423 H HA   . GLU   B 1 197 ? 25.986  -5.869  21.360  1.00 40.29  ? 182 GLU   B HA   1 
ATOM   7424 H HB2  . GLU   B 1 197 ? 26.541  -4.108  22.651  1.00 40.20  ? 182 GLU   B HB2  1 
ATOM   7425 H HB3  . GLU   B 1 197 ? 27.661  -4.219  21.529  1.00 40.20  ? 182 GLU   B HB3  1 
ATOM   7426 H HG2  . GLU   B 1 197 ? 25.611  -2.388  21.068  1.00 39.03  ? 182 GLU   B HG2  1 
ATOM   7427 H HG3  . GLU   B 1 197 ? 26.709  -1.985  22.145  1.00 39.03  ? 182 GLU   B HG3  1 
ATOM   7428 N N    . VAL   B 1 198 ? 23.872  -3.860  20.084  1.00 32.63  ? 183 VAL   B N    1 
ATOM   7429 C CA   . VAL   B 1 198 ? 22.446  -3.545  20.079  1.00 32.62  ? 183 VAL   B CA   1 
ATOM   7430 C C    . VAL   B 1 198 ? 21.636  -4.776  19.683  1.00 34.63  ? 183 VAL   B C    1 
ATOM   7431 O O    . VAL   B 1 198 ? 20.608  -5.083  20.299  1.00 35.04  ? 183 VAL   B O    1 
ATOM   7432 C CB   . VAL   B 1 198 ? 22.160  -2.352  19.148  1.00 32.80  ? 183 VAL   B CB   1 
ATOM   7433 C CG1  . VAL   B 1 198 ? 20.654  -2.099  19.021  1.00 31.61  ? 183 VAL   B CG1  1 
ATOM   7434 C CG2  . VAL   B 1 198 ? 22.859  -1.096  19.656  1.00 37.51  ? 183 VAL   B CG2  1 
ATOM   7435 H H    . VAL   B 1 198 ? 24.321  -3.504  19.442  1.00 39.15  ? 183 VAL   B H    1 
ATOM   7436 H HA   . VAL   B 1 198 ? 22.185  -3.288  20.977  1.00 39.15  ? 183 VAL   B HA   1 
ATOM   7437 H HB   . VAL   B 1 198 ? 22.505  -2.566  18.267  1.00 39.36  ? 183 VAL   B HB   1 
ATOM   7438 H HG11 . VAL   B 1 198 ? 20.513  -1.234  18.606  1.00 37.93  ? 183 VAL   B HG11 1 
ATOM   7439 H HG12 . VAL   B 1 198 ? 20.262  -2.797  18.474  1.00 37.93  ? 183 VAL   B HG12 1 
ATOM   7440 H HG13 . VAL   B 1 198 ? 20.257  -2.110  19.906  1.00 37.93  ? 183 VAL   B HG13 1 
ATOM   7441 H HG21 . VAL   B 1 198 ? 22.653  -0.358  19.062  1.00 45.01  ? 183 VAL   B HG21 1 
ATOM   7442 H HG22 . VAL   B 1 198 ? 22.542  -0.899  20.552  1.00 45.01  ? 183 VAL   B HG22 1 
ATOM   7443 H HG23 . VAL   B 1 198 ? 23.816  -1.252  19.671  1.00 45.01  ? 183 VAL   B HG23 1 
ATOM   7444 N N    . ALA   B 1 199 ? 22.091  -5.504  18.661  1.00 34.86  ? 184 ALA   B N    1 
ATOM   7445 C CA   . ALA   B 1 199 ? 21.367  -6.688  18.212  1.00 33.36  ? 184 ALA   B CA   1 
ATOM   7446 C C    . ALA   B 1 199 ? 21.249  -7.719  19.328  1.00 34.44  ? 184 ALA   B C    1 
ATOM   7447 O O    . ALA   B 1 199 ? 20.215  -8.383  19.464  1.00 40.31  ? 184 ALA   B O    1 
ATOM   7448 C CB   . ALA   B 1 199 ? 22.066  -7.290  16.994  1.00 33.02  ? 184 ALA   B CB   1 
ATOM   7449 H H    . ALA   B 1 199 ? 22.808  -5.335  18.217  1.00 41.83  ? 184 ALA   B H    1 
ATOM   7450 H HA   . ALA   B 1 199 ? 20.470  -6.429  17.950  1.00 40.03  ? 184 ALA   B HA   1 
ATOM   7451 H HB1  . ALA   B 1 199 ? 21.581  -8.081  16.711  1.00 39.62  ? 184 ALA   B HB1  1 
ATOM   7452 H HB2  . ALA   B 1 199 ? 22.075  -6.634  16.279  1.00 39.62  ? 184 ALA   B HB2  1 
ATOM   7453 H HB3  . ALA   B 1 199 ? 22.974  -7.528  17.237  1.00 39.62  ? 184 ALA   B HB3  1 
ATOM   7454 N N    . ALA   B 1 200 ? 22.299  -7.870  20.135  1.00 36.72  ? 185 ALA   B N    1 
ATOM   7455 C CA   . ALA   B 1 200 ? 22.263  -8.856  21.210  1.00 36.58  ? 185 ALA   B CA   1 
ATOM   7456 C C    . ALA   B 1 200 ? 21.163  -8.534  22.214  1.00 43.85  ? 185 ALA   B C    1 
ATOM   7457 O O    . ALA   B 1 200 ? 20.518  -9.441  22.752  1.00 43.15  ? 185 ALA   B O    1 
ATOM   7458 C CB   . ALA   B 1 200 ? 23.622  -8.922  21.907  1.00 36.20  ? 185 ALA   B CB   1 
ATOM   7459 H H    . ALA   B 1 200 ? 23.031  -7.423  20.082  1.00 44.06  ? 185 ALA   B H    1 
ATOM   7460 H HA   . ALA   B 1 200 ? 22.078  -9.728  20.829  1.00 43.89  ? 185 ALA   B HA   1 
ATOM   7461 H HB1  . ALA   B 1 200 ? 23.581  -9.582  22.616  1.00 43.44  ? 185 ALA   B HB1  1 
ATOM   7462 H HB2  . ALA   B 1 200 ? 24.297  -9.175  21.258  1.00 43.44  ? 185 ALA   B HB2  1 
ATOM   7463 H HB3  . ALA   B 1 200 ? 23.829  -8.050  22.278  1.00 43.44  ? 185 ALA   B HB3  1 
ATOM   7464 N N    . VAL   B 1 201 ? 20.939  -7.247  22.489  1.00 41.58  ? 186 VAL   B N    1 
ATOM   7465 C CA   . VAL   B 1 201 ? 19.845  -6.866  23.376  1.00 46.15  ? 186 VAL   B CA   1 
ATOM   7466 C C    . VAL   B 1 201 ? 18.501  -7.185  22.728  1.00 46.90  ? 186 VAL   B C    1 
ATOM   7467 O O    . VAL   B 1 201 ? 17.609  -7.761  23.359  1.00 46.36  ? 186 VAL   B O    1 
ATOM   7468 C CB   . VAL   B 1 201 ? 19.951  -5.377  23.749  1.00 41.89  ? 186 VAL   B CB   1 
ATOM   7469 C CG1  . VAL   B 1 201 ? 18.757  -4.965  24.602  1.00 47.13  ? 186 VAL   B CG1  1 
ATOM   7470 C CG2  . VAL   B 1 201 ? 21.262  -5.106  24.475  1.00 43.20  ? 186 VAL   B CG2  1 
ATOM   7471 H H    . VAL   B 1 201 ? 21.398  -6.589  22.179  1.00 49.90  ? 186 VAL   B H    1 
ATOM   7472 H HA   . VAL   B 1 201 ? 19.915  -7.385  24.192  1.00 55.38  ? 186 VAL   B HA   1 
ATOM   7473 H HB   . VAL   B 1 201 ? 19.942  -4.842  22.940  1.00 50.26  ? 186 VAL   B HB   1 
ATOM   7474 H HG11 . VAL   B 1 201 ? 18.984  -4.161  25.094  1.00 56.55  ? 186 VAL   B HG11 1 
ATOM   7475 H HG12 . VAL   B 1 201 ? 17.998  -4.796  24.022  1.00 56.55  ? 186 VAL   B HG12 1 
ATOM   7476 H HG13 . VAL   B 1 201 ? 18.547  -5.684  25.219  1.00 56.55  ? 186 VAL   B HG13 1 
ATOM   7477 H HG21 . VAL   B 1 201 ? 21.290  -4.172  24.737  1.00 51.84  ? 186 VAL   B HG21 1 
ATOM   7478 H HG22 . VAL   B 1 201 ? 21.310  -5.672  25.261  1.00 51.84  ? 186 VAL   B HG22 1 
ATOM   7479 H HG23 . VAL   B 1 201 ? 22.000  -5.304  23.878  1.00 51.84  ? 186 VAL   B HG23 1 
ATOM   7480 N N    . ALA   B 1 202 ? 18.343  -6.819  21.454  1.00 43.94  ? 187 ALA   B N    1 
ATOM   7481 C CA   . ALA   B 1 202 ? 17.089  -7.055  20.749  1.00 40.28  ? 187 ALA   B CA   1 
ATOM   7482 C C    . ALA   B 1 202 ? 16.752  -8.534  20.634  1.00 45.58  ? 187 ALA   B C    1 
ATOM   7483 O O    . ALA   B 1 202 ? 15.579  -8.882  20.468  1.00 48.15  ? 187 ALA   B O    1 
ATOM   7484 C CB   . ALA   B 1 202 ? 17.158  -6.442  19.349  1.00 46.78  ? 187 ALA   B CB   1 
ATOM   7485 H H    . ALA   B 1 202 ? 18.947  -6.433  20.978  1.00 52.72  ? 187 ALA   B H    1 
ATOM   7486 H HA   . ALA   B 1 202 ? 16.375  -6.623  21.244  1.00 48.34  ? 187 ALA   B HA   1 
ATOM   7487 H HB1  . ALA   B 1 202 ? 16.320  -6.607  18.890  1.00 56.14  ? 187 ALA   B HB1  1 
ATOM   7488 H HB2  . ALA   B 1 202 ? 17.309  -5.487  19.429  1.00 56.14  ? 187 ALA   B HB2  1 
ATOM   7489 H HB3  . ALA   B 1 202 ? 17.889  -6.852  18.860  1.00 56.14  ? 187 ALA   B HB3  1 
ATOM   7490 N N    . LEU   B 1 203 ? 17.752  -9.410  20.709  1.00 50.72  ? 188 LEU   B N    1 
ATOM   7491 C CA   . LEU   B 1 203 ? 17.518  -10.833 20.489  1.00 58.59  ? 188 LEU   B CA   1 
ATOM   7492 C C    . LEU   B 1 203 ? 16.962  -11.501 21.741  1.00 59.34  ? 188 LEU   B C    1 
ATOM   7493 O O    . LEU   B 1 203 ? 15.948  -12.205 21.679  1.00 57.07  ? 188 LEU   B O    1 
ATOM   7494 C CB   . LEU   B 1 203 ? 18.820  -11.508 20.047  1.00 53.13  ? 188 LEU   B CB   1 
ATOM   7495 C CG   . LEU   B 1 203 ? 18.732  -12.909 19.432  1.00 61.00  ? 188 LEU   B CG   1 
ATOM   7496 C CD1  . LEU   B 1 203 ? 17.816  -12.927 18.219  1.00 52.10  ? 188 LEU   B CD1  1 
ATOM   7497 C CD2  . LEU   B 1 203 ? 20.124  -13.398 19.057  1.00 62.97  ? 188 LEU   B CD2  1 
ATOM   7498 H H    . LEU   B 1 203 ? 18.569  -9.207  20.885  1.00 60.87  ? 188 LEU   B H    1 
ATOM   7499 H HA   . LEU   B 1 203 ? 16.866  -10.942 19.779  1.00 70.31  ? 188 LEU   B HA   1 
ATOM   7500 H HB2  . LEU   B 1 203 ? 19.236  -10.938 19.381  1.00 63.75  ? 188 LEU   B HB2  1 
ATOM   7501 H HB3  . LEU   B 1 203 ? 19.393  -11.581 20.826  1.00 63.75  ? 188 LEU   B HB3  1 
ATOM   7502 H HG   . LEU   B 1 203 ? 18.353  -13.514 20.088  1.00 73.20  ? 188 LEU   B HG   1 
ATOM   7503 H HD11 . LEU   B 1 203 ? 18.027  -13.702 17.675  1.00 62.52  ? 188 LEU   B HD11 1 
ATOM   7504 H HD12 . LEU   B 1 203 ? 16.895  -12.975 18.520  1.00 62.52  ? 188 LEU   B HD12 1 
ATOM   7505 H HD13 . LEU   B 1 203 ? 17.954  -12.115 17.707  1.00 62.52  ? 188 LEU   B HD13 1 
ATOM   7506 H HD21 . LEU   B 1 203 ? 20.055  -14.290 18.680  1.00 75.57  ? 188 LEU   B HD21 1 
ATOM   7507 H HD22 . LEU   B 1 203 ? 20.507  -12.792 18.404  1.00 75.57  ? 188 LEU   B HD22 1 
ATOM   7508 H HD23 . LEU   B 1 203 ? 20.677  -13.418 19.854  1.00 75.57  ? 188 LEU   B HD23 1 
ATOM   7509 N N    . LYS   B 1 204 ? 17.609  -11.287 22.884  1.00 62.90  ? 189 LYS   B N    1 
ATOM   7510 C CA   . LYS   B 1 204 ? 17.190  -11.885 24.143  1.00 68.01  ? 189 LYS   B CA   1 
ATOM   7511 C C    . LYS   B 1 204 ? 16.265  -10.986 24.950  1.00 69.51  ? 189 LYS   B C    1 
ATOM   7512 O O    . LYS   B 1 204 ? 15.833  -11.380 26.039  1.00 74.44  ? 189 LYS   B O    1 
ATOM   7513 C CB   . LYS   B 1 204 ? 18.418  -12.234 24.993  1.00 67.64  ? 189 LYS   B CB   1 
ATOM   7514 H H    . LYS   B 1 204 ? 18.307  -10.789 22.954  1.00 75.48  ? 189 LYS   B H    1 
ATOM   7515 H HA   . LYS   B 1 204 ? 16.712  -12.706 23.947  1.00 81.61  ? 189 LYS   B HA   1 
ATOM   7516 N N    . GLY   B 1 205 ? 15.941  -9.799  24.448  1.00 60.94  ? 190 GLY   B N    1 
ATOM   7517 C CA   . GLY   B 1 205 ? 15.242  -8.819  25.243  1.00 60.16  ? 190 GLY   B CA   1 
ATOM   7518 C C    . GLY   B 1 205 ? 16.127  -8.054  26.199  1.00 51.36  ? 190 GLY   B C    1 
ATOM   7519 O O    . GLY   B 1 205 ? 15.678  -7.046  26.755  1.00 54.00  ? 190 GLY   B O    1 
ATOM   7520 H H    . GLY   B 1 205 ? 16.119  -9.544  23.646  1.00 73.13  ? 190 GLY   B H    1 
ATOM   7521 H HA2  . GLY   B 1 205 ? 14.819  -8.179  24.650  1.00 72.19  ? 190 GLY   B HA2  1 
ATOM   7522 H HA3  . GLY   B 1 205 ? 14.558  -9.268  25.763  1.00 72.19  ? 190 GLY   B HA3  1 
ATOM   7523 N N    . GLY   B 1 206 ? 17.361  -8.509  26.422  1.00 54.41  ? 191 GLY   B N    1 
ATOM   7524 C CA   . GLY   B 1 206 ? 18.335  -7.752  27.181  1.00 44.32  ? 191 GLY   B CA   1 
ATOM   7525 C C    . GLY   B 1 206 ? 18.293  -7.932  28.680  1.00 68.33  ? 191 GLY   B C    1 
ATOM   7526 O O    . GLY   B 1 206 ? 18.728  -7.035  29.410  1.00 64.68  ? 191 GLY   B O    1 
ATOM   7527 H H    . GLY   B 1 206 ? 17.656  -9.265  26.138  1.00 65.30  ? 191 GLY   B H    1 
ATOM   7528 H HA2  . GLY   B 1 206 ? 19.222  -8.008  26.883  1.00 53.18  ? 191 GLY   B HA2  1 
ATOM   7529 H HA3  . GLY   B 1 206 ? 18.200  -6.809  26.998  1.00 53.18  ? 191 GLY   B HA3  1 
ATOM   7530 N N    . TYR   B 1 207 ? 17.793  -9.067  29.168  1.00 64.99  ? 192 TYR   B N    1 
ATOM   7531 C CA   . TYR   B 1 207 ? 17.624  -9.282  30.599  1.00 59.53  ? 192 TYR   B CA   1 
ATOM   7532 C C    . TYR   B 1 207 ? 17.731  -10.776 30.882  1.00 59.19  ? 192 TYR   B C    1 
ATOM   7533 O O    . TYR   B 1 207 ? 18.013  -11.575 29.984  1.00 49.04  ? 192 TYR   B O    1 
ATOM   7534 C CB   . TYR   B 1 207 ? 16.287  -8.700  31.070  1.00 49.85  ? 192 TYR   B CB   1 
ATOM   7535 C CG   . TYR   B 1 207 ? 15.107  -9.157  30.246  1.00 51.18  ? 192 TYR   B CG   1 
ATOM   7536 C CD1  . TYR   B 1 207 ? 14.434  -10.338 30.545  1.00 53.56  ? 192 TYR   B CD1  1 
ATOM   7537 C CD2  . TYR   B 1 207 ? 14.663  -8.408  29.170  1.00 52.01  ? 192 TYR   B CD2  1 
ATOM   7538 C CE1  . TYR   B 1 207 ? 13.347  -10.755 29.789  1.00 47.37  ? 192 TYR   B CE1  1 
ATOM   7539 C CE2  . TYR   B 1 207 ? 13.578  -8.815  28.411  1.00 55.89  ? 192 TYR   B CE2  1 
ATOM   7540 C CZ   . TYR   B 1 207 ? 12.925  -9.986  28.723  1.00 52.22  ? 192 TYR   B CZ   1 
ATOM   7541 O OH   . TYR   B 1 207 ? 11.851  -10.377 27.959  1.00 51.33  ? 192 TYR   B OH   1 
ATOM   7542 H H    . TYR   B 1 207 ? 17.543  -9.732  28.684  1.00 77.99  ? 192 TYR   B H    1 
ATOM   7543 H HA   . TYR   B 1 207 ? 18.344  -8.832  31.068  1.00 71.44  ? 192 TYR   B HA   1 
ATOM   7544 H HB2  . TYR   B 1 207 ? 16.132  -8.974  31.988  1.00 59.82  ? 192 TYR   B HB2  1 
ATOM   7545 H HB3  . TYR   B 1 207 ? 16.330  -7.732  31.016  1.00 59.82  ? 192 TYR   B HB3  1 
ATOM   7546 H HD1  . TYR   B 1 207 ? 14.716  -10.855 31.264  1.00 64.27  ? 192 TYR   B HD1  1 
ATOM   7547 H HD2  . TYR   B 1 207 ? 15.101  -7.616  28.953  1.00 62.41  ? 192 TYR   B HD2  1 
ATOM   7548 H HE1  . TYR   B 1 207 ? 12.906  -11.547 29.999  1.00 56.85  ? 192 TYR   B HE1  1 
ATOM   7549 H HE2  . TYR   B 1 207 ? 13.292  -8.299  27.692  1.00 67.06  ? 192 TYR   B HE2  1 
ATOM   7550 H HH   . TYR   B 1 207 ? 11.705  -9.808  27.358  1.00 61.60  ? 192 TYR   B HH   1 
ATOM   7551 N N    . ASN   B 1 208 ? 17.481  -11.151 32.133  1.00 45.31  ? 193 ASN   B N    1 
ATOM   7552 C CA   . ASN   B 1 208 ? 17.720  -12.486 32.650  1.00 47.47  ? 193 ASN   B CA   1 
ATOM   7553 C C    . ASN   B 1 208 ? 16.419  -13.100 33.168  1.00 58.24  ? 193 ASN   B C    1 
ATOM   7554 O O    . ASN   B 1 208 ? 15.363  -12.462 33.181  1.00 57.37  ? 193 ASN   B O    1 
ATOM   7555 C CB   . ASN   B 1 208 ? 18.759  -12.441 33.770  1.00 62.51  ? 193 ASN   B CB   1 
ATOM   7556 C CG   . ASN   B 1 208 ? 18.265  -11.668 34.975  1.00 62.97  ? 193 ASN   B CG   1 
ATOM   7557 O OD1  . ASN   B 1 208 ? 17.476  -10.726 34.848  1.00 65.67  ? 193 ASN   B OD1  1 
ATOM   7558 N ND2  . ASN   B 1 208 ? 18.724  -12.060 36.151  1.00 69.85  ? 193 ASN   B ND2  1 
ATOM   7559 H H    . ASN   B 1 208 ? 17.156  -10.619 32.727  1.00 54.37  ? 193 ASN   B H    1 
ATOM   7560 H HA   . ASN   B 1 208 ? 18.047  -13.042 31.925  1.00 56.96  ? 193 ASN   B HA   1 
ATOM   7561 H HB2  . ASN   B 1 208 ? 18.962  -13.346 34.054  1.00 75.01  ? 193 ASN   B HB2  1 
ATOM   7562 H HB3  . ASN   B 1 208 ? 19.562  -12.008 33.442  1.00 75.01  ? 193 ASN   B HB3  1 
ATOM   7563 H HD21 . ASN   B 1 208 ? 18.474  -11.655 36.867  1.00 83.82  ? 193 ASN   B HD21 1 
ATOM   7564 H HD22 . ASN   B 1 208 ? 19.272  -12.721 36.200  1.00 83.82  ? 193 ASN   B HD22 1 
ATOM   7565 N N    . GLU   B 1 209 ? 16.515  -14.351 33.629  1.00 43.83  ? 194 GLU   B N    1 
ATOM   7566 C CA   . GLU   B 1 209 ? 15.332  -15.109 34.017  1.00 42.75  ? 194 GLU   B CA   1 
ATOM   7567 C C    . GLU   B 1 209 ? 14.764  -14.682 35.364  1.00 40.12  ? 194 GLU   B C    1 
ATOM   7568 O O    . GLU   B 1 209 ? 13.605  -14.994 35.662  1.00 35.06  ? 194 GLU   B O    1 
ATOM   7569 C CB   . GLU   B 1 209 ? 15.654  -16.611 34.038  1.00 36.35  ? 194 GLU   B CB   1 
ATOM   7570 C CG   . GLU   B 1 209 ? 16.513  -17.097 35.203  1.00 42.07  ? 194 GLU   B CG   1 
ATOM   7571 C CD   . GLU   B 1 209 ? 18.004  -16.903 34.991  1.00 61.90  ? 194 GLU   B CD   1 
ATOM   7572 O OE1  . GLU   B 1 209 ? 18.403  -16.240 34.006  1.00 67.43  ? 194 GLU   B OE1  1 
ATOM   7573 O OE2  . GLU   B 1 209 ? 18.783  -17.421 35.820  1.00 63.14  ? 194 GLU   B OE2  1 
ATOM   7574 H H    . GLU   B 1 209 ? 17.255  -14.778 33.726  1.00 52.59  ? 194 GLU   B H    1 
ATOM   7575 H HA   . GLU   B 1 209 ? 14.641  -14.962 33.353  1.00 51.30  ? 194 GLU   B HA   1 
ATOM   7576 H HB2  . GLU   B 1 209 ? 14.816  -17.099 34.077  1.00 43.62  ? 194 GLU   B HB2  1 
ATOM   7577 H HB3  . GLU   B 1 209 ? 16.128  -16.831 33.221  1.00 43.62  ? 194 GLU   B HB3  1 
ATOM   7578 H HG2  . GLU   B 1 209 ? 16.262  -16.606 36.001  1.00 50.48  ? 194 GLU   B HG2  1 
ATOM   7579 H HG3  . GLU   B 1 209 ? 16.354  -18.045 35.332  1.00 50.48  ? 194 GLU   B HG3  1 
ATOM   7580 N N    . LEU   B 1 210 ? 15.539  -13.976 36.184  1.00 38.04  ? 195 LEU   B N    1 
ATOM   7581 C CA   . LEU   B 1 210 ? 15.007  -13.477 37.445  1.00 37.67  ? 195 LEU   B CA   1 
ATOM   7582 C C    . LEU   B 1 210 ? 13.867  -12.486 37.241  1.00 36.53  ? 195 LEU   B C    1 
ATOM   7583 O O    . LEU   B 1 210 ? 13.175  -12.157 38.209  1.00 38.88  ? 195 LEU   B O    1 
ATOM   7584 C CB   . LEU   B 1 210 ? 16.134  -12.850 38.261  1.00 35.93  ? 195 LEU   B CB   1 
ATOM   7585 C CG   . LEU   B 1 210 ? 17.259  -13.841 38.555  1.00 41.13  ? 195 LEU   B CG   1 
ATOM   7586 C CD1  . LEU   B 1 210 ? 18.419  -13.183 39.275  1.00 39.85  ? 195 LEU   B CD1  1 
ATOM   7587 C CD2  . LEU   B 1 210 ? 16.712  -15.023 39.361  1.00 40.90  ? 195 LEU   B CD2  1 
ATOM   7588 H H    . LEU   B 1 210 ? 16.362  -13.776 36.035  1.00 45.65  ? 195 LEU   B H    1 
ATOM   7589 H HA   . LEU   B 1 210 ? 14.651  -14.216 37.963  1.00 45.20  ? 195 LEU   B HA   1 
ATOM   7590 H HB2  . LEU   B 1 210 ? 16.508  -12.105 37.764  1.00 43.12  ? 195 LEU   B HB2  1 
ATOM   7591 H HB3  . LEU   B 1 210 ? 15.777  -12.537 39.107  1.00 43.12  ? 195 LEU   B HB3  1 
ATOM   7592 H HG   . LEU   B 1 210 ? 17.610  -14.172 37.714  1.00 49.36  ? 195 LEU   B HG   1 
ATOM   7593 H HD11 . LEU   B 1 210 ? 19.138  -13.826 39.369  1.00 47.82  ? 195 LEU   B HD11 1 
ATOM   7594 H HD12 . LEU   B 1 210 ? 18.722  -12.422 38.755  1.00 47.82  ? 195 LEU   B HD12 1 
ATOM   7595 H HD13 . LEU   B 1 210 ? 18.122  -12.888 40.150  1.00 47.82  ? 195 LEU   B HD13 1 
ATOM   7596 H HD21 . LEU   B 1 210 ? 17.454  -15.501 39.764  1.00 49.08  ? 195 LEU   B HD21 1 
ATOM   7597 H HD22 . LEU   B 1 210 ? 16.121  -14.687 40.053  1.00 49.08  ? 195 LEU   B HD22 1 
ATOM   7598 H HD23 . LEU   B 1 210 ? 16.224  -15.612 38.765  1.00 49.08  ? 195 LEU   B HD23 1 
ATOM   7599 N N    A CYS   B 1 211 ? 13.638  -12.015 36.013  0.43 34.87  ? 196 CYS   B N    1 
ATOM   7600 N N    B CYS   B 1 211 ? 13.657  -12.003 36.015  0.57 35.11  ? 196 CYS   B N    1 
ATOM   7601 C CA   A CYS   B 1 211 ? 12.486  -11.155 35.769  0.43 35.94  ? 196 CYS   B CA   1 
ATOM   7602 C CA   B CYS   B 1 211 ? 12.494  -11.169 35.745  0.57 35.93  ? 196 CYS   B CA   1 
ATOM   7603 C C    A CYS   B 1 211 ? 11.174  -11.899 35.988  0.43 34.28  ? 196 CYS   B C    1 
ATOM   7604 C C    B CYS   B 1 211 ? 11.203  -11.911 36.064  0.57 34.44  ? 196 CYS   B C    1 
ATOM   7605 O O    A CYS   B 1 211 ? 10.158  -11.276 36.318  0.43 29.86  ? 196 CYS   B O    1 
ATOM   7606 O O    B CYS   B 1 211 ? 10.230  -11.310 36.532  0.57 29.94  ? 196 CYS   B O    1 
ATOM   7607 C CB   A CYS   B 1 211 ? 12.540  -10.592 34.352  0.43 35.29  ? 196 CYS   B CB   1 
ATOM   7608 C CB   B CYS   B 1 211 ? 12.497  -10.728 34.285  0.57 35.20  ? 196 CYS   B CB   1 
ATOM   7609 S SG   A CYS   B 1 211 ? 14.049  -9.684  33.989  0.43 40.96  ? 196 CYS   B SG   1 
ATOM   7610 S SG   B CYS   B 1 211 ? 12.131  -12.082 33.145  0.57 41.50  ? 196 CYS   B SG   1 
ATOM   7611 H H    A CYS   B 1 211 ? 14.123  -12.177 35.322  0.43 41.84  ? 196 CYS   B H    1 
ATOM   7612 H H    B CYS   B 1 211 ? 14.166  -12.143 35.336  0.57 42.13  ? 196 CYS   B H    1 
ATOM   7613 H HA   A CYS   B 1 211 ? 12.518  -10.410 36.390  0.43 43.12  ? 196 CYS   B HA   1 
ATOM   7614 H HA   B CYS   B 1 211 ? 12.540  -10.377 36.304  0.57 43.12  ? 196 CYS   B HA   1 
ATOM   7615 H HB2  A CYS   B 1 211 ? 12.479  -11.327 33.723  0.43 42.34  ? 196 CYS   B HB2  1 
ATOM   7616 H HB2  B CYS   B 1 211 ? 11.824  -10.040 34.162  0.57 42.24  ? 196 CYS   B HB2  1 
ATOM   7617 H HB3  A CYS   B 1 211 ? 11.793  -9.986  34.229  0.43 42.34  ? 196 CYS   B HB3  1 
ATOM   7618 H HB3  B CYS   B 1 211 ? 13.374  -10.377 34.064  0.57 42.24  ? 196 CYS   B HB3  1 
ATOM   7619 H HG   A CYS   B 1 211 ? 14.051  -8.663  34.620  0.43 49.15  ? 196 CYS   B HG   1 
ATOM   7620 H HG   B CYS   B 1 211 ? 12.950  -12.947 33.291  0.57 49.80  ? 196 CYS   B HG   1 
ATOM   7621 N N    . ASP   B 1 212 ? 11.172  -13.221 35.799  1.00 30.52  ? 197 ASP   B N    1 
ATOM   7622 C CA   . ASP   B 1 212 ? 9.978   -14.004 36.095  1.00 32.60  ? 197 ASP   B CA   1 
ATOM   7623 C C    . ASP   B 1 212 ? 9.683   -14.010 37.592  1.00 28.87  ? 197 ASP   B C    1 
ATOM   7624 O O    . ASP   B 1 212 ? 8.523   -14.134 37.996  1.00 27.99  ? 197 ASP   B O    1 
ATOM   7625 C CB   . ASP   B 1 212 ? 10.134  -15.448 35.592  1.00 32.70  ? 197 ASP   B CB   1 
ATOM   7626 C CG   . ASP   B 1 212 ? 10.158  -15.566 34.057  1.00 36.08  ? 197 ASP   B CG   1 
ATOM   7627 O OD1  . ASP   B 1 212 ? 9.612   -14.688 33.346  1.00 30.27  ? 197 ASP   B OD1  1 
ATOM   7628 O OD2  . ASP   B 1 212 ? 10.711  -16.575 33.562  1.00 30.74  ? 197 ASP   B OD2  1 
ATOM   7629 H H    A ASP   B 1 212 ? 11.838  -13.679 35.506  0.43 36.63  ? 197 ASP   B H    1 
ATOM   7630 H H    B ASP   B 1 212 ? 11.819  -13.670 35.454  0.57 36.63  ? 197 ASP   B H    1 
ATOM   7631 H HA   . ASP   B 1 212 ? 9.228   -13.606 35.626  1.00 39.12  ? 197 ASP   B HA   1 
ATOM   7632 H HB2  . ASP   B 1 212 ? 10.969  -15.809 35.930  1.00 39.24  ? 197 ASP   B HB2  1 
ATOM   7633 H HB3  . ASP   B 1 212 ? 9.388   -15.976 35.919  1.00 39.24  ? 197 ASP   B HB3  1 
ATOM   7634 N N    . ILE   B 1 213 ? 10.719  -13.900 38.427  1.00 31.95  ? 198 ILE   B N    1 
ATOM   7635 C CA   . ILE   B 1 213 ? 10.521  -13.888 39.874  1.00 29.80  ? 198 ILE   B CA   1 
ATOM   7636 C C    . ILE   B 1 213 ? 9.875   -12.575 40.310  1.00 31.18  ? 198 ILE   B C    1 
ATOM   7637 O O    . ILE   B 1 213 ? 9.001   -12.557 41.182  1.00 30.03  ? 198 ILE   B O    1 
ATOM   7638 C CB   . ILE   B 1 213 ? 11.865  -14.130 40.585  1.00 31.25  ? 198 ILE   B CB   1 
ATOM   7639 C CG1  . ILE   B 1 213 ? 12.444  -15.499 40.209  1.00 38.30  ? 198 ILE   B CG1  1 
ATOM   7640 C CG2  . ILE   B 1 213 ? 11.714  -14.015 42.082  1.00 32.71  ? 198 ILE   B CG2  1 
ATOM   7641 C CD1  . ILE   B 1 213 ? 11.499  -16.678 40.406  1.00 38.26  ? 198 ILE   B CD1  1 
ATOM   7642 H H    . ILE   B 1 213 ? 11.540  -13.832 38.181  1.00 38.34  ? 198 ILE   B H    1 
ATOM   7643 H HA   . ILE   B 1 213 ? 9.917   -14.607 40.117  1.00 35.76  ? 198 ILE   B HA   1 
ATOM   7644 H HB   . ILE   B 1 213 ? 12.482  -13.444 40.286  1.00 37.49  ? 198 ILE   B HB   1 
ATOM   7645 H HG12 . ILE   B 1 213 ? 12.691  -15.479 39.271  1.00 45.96  ? 198 ILE   B HG12 1 
ATOM   7646 H HG13 . ILE   B 1 213 ? 13.228  -15.660 40.756  1.00 45.96  ? 198 ILE   B HG13 1 
ATOM   7647 H HG21 . ILE   B 1 213 ? 12.510  -14.371 42.508  1.00 39.26  ? 198 ILE   B HG21 1 
ATOM   7648 H HG22 . ILE   B 1 213 ? 11.603  -13.081 42.317  1.00 39.26  ? 198 ILE   B HG22 1 
ATOM   7649 H HG23 . ILE   B 1 213 ? 10.935  -14.521 42.361  1.00 39.26  ? 198 ILE   B HG23 1 
ATOM   7650 H HD11 . ILE   B 1 213 ? 12.006  -17.503 40.340  1.00 45.92  ? 198 ILE   B HD11 1 
ATOM   7651 H HD12 . ILE   B 1 213 ? 11.090  -16.612 41.283  1.00 45.92  ? 198 ILE   B HD12 1 
ATOM   7652 H HD13 . ILE   B 1 213 ? 10.815  -16.654 39.719  1.00 45.92  ? 198 ILE   B HD13 1 
ATOM   7653 N N    . TRP   B 1 214 ? 10.294  -11.456 39.715  1.00 29.55  ? 199 TRP   B N    1 
ATOM   7654 C CA   . TRP   B 1 214 ? 9.596   -10.197 39.951  1.00 30.92  ? 199 TRP   B CA   1 
ATOM   7655 C C    . TRP   B 1 214 ? 8.137   -10.303 39.513  1.00 30.32  ? 199 TRP   B C    1 
ATOM   7656 O O    . TRP   B 1 214 ? 7.219   -10.027 40.294  1.00 27.55  ? 199 TRP   B O    1 
ATOM   7657 C CB   . TRP   B 1 214 ? 10.310  -9.055  39.216  1.00 30.56  ? 199 TRP   B CB   1 
ATOM   7658 C CG   . TRP   B 1 214 ? 9.636   -7.711  39.386  1.00 34.25  ? 199 TRP   B CG   1 
ATOM   7659 C CD1  . TRP   B 1 214 ? 8.518   -7.269  38.739  1.00 29.05  ? 199 TRP   B CD1  1 
ATOM   7660 C CD2  . TRP   B 1 214 ? 10.036  -6.651  40.263  1.00 30.13  ? 199 TRP   B CD2  1 
ATOM   7661 N NE1  . TRP   B 1 214 ? 8.197   -6.003  39.159  1.00 31.32  ? 199 TRP   B NE1  1 
ATOM   7662 C CE2  . TRP   B 1 214 ? 9.112   -5.602  40.096  1.00 29.70  ? 199 TRP   B CE2  1 
ATOM   7663 C CE3  . TRP   B 1 214 ? 11.085  -6.487  41.172  1.00 32.21  ? 199 TRP   B CE3  1 
ATOM   7664 C CZ2  . TRP   B 1 214 ? 9.207   -4.402  40.800  1.00 30.57  ? 199 TRP   B CZ2  1 
ATOM   7665 C CZ3  . TRP   B 1 214 ? 11.176  -5.296  41.874  1.00 35.05  ? 199 TRP   B CZ3  1 
ATOM   7666 C CH2  . TRP   B 1 214 ? 10.243  -4.268  41.682  1.00 31.65  ? 199 TRP   B CH2  1 
ATOM   7667 H H    . TRP   B 1 214 ? 10.966  -11.401 39.181  1.00 35.46  ? 199 TRP   B H    1 
ATOM   7668 H HA   . TRP   B 1 214 ? 9.613   -9.993  40.899  1.00 37.11  ? 199 TRP   B HA   1 
ATOM   7669 H HB2  . TRP   B 1 214 ? 11.214  -8.979  39.561  1.00 36.68  ? 199 TRP   B HB2  1 
ATOM   7670 H HB3  . TRP   B 1 214 ? 10.333  -9.259  38.268  1.00 36.68  ? 199 TRP   B HB3  1 
ATOM   7671 H HD1  . TRP   B 1 214 ? 8.043   -7.756  38.105  1.00 34.86  ? 199 TRP   B HD1  1 
ATOM   7672 H HE1  . TRP   B 1 214 ? 7.530   -5.538  38.880  1.00 37.58  ? 199 TRP   B HE1  1 
ATOM   7673 H HE3  . TRP   B 1 214 ? 11.709  -7.164  41.304  1.00 38.65  ? 199 TRP   B HE3  1 
ATOM   7674 H HZ2  . TRP   B 1 214 ? 8.588   -3.719  40.675  1.00 36.68  ? 199 TRP   B HZ2  1 
ATOM   7675 H HZ3  . TRP   B 1 214 ? 11.869  -5.176  42.484  1.00 42.06  ? 199 TRP   B HZ3  1 
ATOM   7676 H HH2  . TRP   B 1 214 ? 10.331  -3.477  42.163  1.00 37.98  ? 199 TRP   B HH2  1 
ATOM   7677 N N    . SER   B 1 215 ? 7.904   -10.743 38.271  1.00 27.58  ? 200 SER   B N    1 
ATOM   7678 C CA   . SER   B 1 215 ? 6.539   -10.813 37.763  1.00 26.75  ? 200 SER   B CA   1 
ATOM   7679 C C    . SER   B 1 215 ? 5.650   -11.675 38.654  1.00 26.53  ? 200 SER   B C    1 
ATOM   7680 O O    . SER   B 1 215 ? 4.444   -11.419 38.754  1.00 27.84  ? 200 SER   B O    1 
ATOM   7681 C CB   . SER   B 1 215 ? 6.524   -11.357 36.337  1.00 26.71  ? 200 SER   B CB   1 
ATOM   7682 O OG   . SER   B 1 215 ? 7.193   -10.505 35.421  1.00 32.38  ? 200 SER   B OG   1 
ATOM   7683 H H    . SER   B 1 215 ? 8.509   -11.000 37.717  1.00 33.10  ? 200 SER   B H    1 
ATOM   7684 H HA   . SER   B 1 215 ? 6.178   -9.914  37.745  1.00 32.10  ? 200 SER   B HA   1 
ATOM   7685 H HB2  . SER   B 1 215 ? 6.964   -12.222 36.332  1.00 32.05  ? 200 SER   B HB2  1 
ATOM   7686 H HB3  . SER   B 1 215 ? 5.601   -11.453 36.053  1.00 32.05  ? 200 SER   B HB3  1 
ATOM   7687 H HG   . SER   B 1 215 ? 6.814   -9.755  35.397  1.00 38.85  ? 200 SER   B HG   1 
ATOM   7688 N N    . LEU   B 1 216 ? 6.214   -12.695 39.306  1.00 26.65  ? 201 LEU   B N    1 
ATOM   7689 C CA   . LEU   B 1 216 ? 5.398   -13.543 40.174  1.00 27.40  ? 201 LEU   B CA   1 
ATOM   7690 C C    . LEU   B 1 216 ? 4.996   -12.804 41.444  1.00 26.58  ? 201 LEU   B C    1 
ATOM   7691 O O    . LEU   B 1 216 ? 3.865   -12.946 41.918  1.00 28.74  ? 201 LEU   B O    1 
ATOM   7692 C CB   . LEU   B 1 216 ? 6.145   -14.832 40.519  1.00 26.92  ? 201 LEU   B CB   1 
ATOM   7693 C CG   . LEU   B 1 216 ? 5.423   -15.765 41.492  1.00 27.58  ? 201 LEU   B CG   1 
ATOM   7694 C CD1  . LEU   B 1 216 ? 4.078   -16.192 40.937  1.00 30.14  ? 201 LEU   B CD1  1 
ATOM   7695 C CD2  . LEU   B 1 216 ? 6.275   -16.964 41.793  1.00 31.37  ? 201 LEU   B CD2  1 
ATOM   7696 H H    . LEU   B 1 216 ? 7.045   -12.912 39.264  1.00 31.97  ? 201 LEU   B H    1 
ATOM   7697 H HA   . LEU   B 1 216 ? 4.590   -13.787 39.695  1.00 32.87  ? 201 LEU   B HA   1 
ATOM   7698 H HB2  . LEU   B 1 216 ? 6.294   -15.328 39.698  1.00 32.30  ? 201 LEU   B HB2  1 
ATOM   7699 H HB3  . LEU   B 1 216 ? 6.995   -14.594 40.921  1.00 32.30  ? 201 LEU   B HB3  1 
ATOM   7700 H HG   . LEU   B 1 216 ? 5.261   -15.288 42.321  1.00 33.10  ? 201 LEU   B HG   1 
ATOM   7701 H HD11 . LEU   B 1 216 ? 3.697   -16.868 41.519  1.00 36.17  ? 201 LEU   B HD11 1 
ATOM   7702 H HD12 . LEU   B 1 216 ? 3.493   -15.420 40.899  1.00 36.17  ? 201 LEU   B HD12 1 
ATOM   7703 H HD13 . LEU   B 1 216 ? 4.205   -16.556 40.047  1.00 36.17  ? 201 LEU   B HD13 1 
ATOM   7704 H HD21 . LEU   B 1 216 ? 5.799   -17.542 42.410  1.00 37.64  ? 201 LEU   B HD21 1 
ATOM   7705 H HD22 . LEU   B 1 216 ? 6.455   -17.439 40.966  1.00 37.64  ? 201 LEU   B HD22 1 
ATOM   7706 H HD23 . LEU   B 1 216 ? 7.107   -16.668 42.192  1.00 37.64  ? 201 LEU   B HD23 1 
ATOM   7707 N N    . GLY   B 1 217 ? 5.910   -12.017 42.010  1.00 27.18  ? 202 GLY   B N    1 
ATOM   7708 C CA   . GLY   B 1 217 ? 5.544   -11.187 43.146  1.00 27.52  ? 202 GLY   B CA   1 
ATOM   7709 C C    . GLY   B 1 217 ? 4.396   -10.251 42.822  1.00 28.09  ? 202 GLY   B C    1 
ATOM   7710 O O    . GLY   B 1 217 ? 3.446   -10.120 43.596  1.00 33.59  ? 202 GLY   B O    1 
ATOM   7711 H H    . GLY   B 1 217 ? 6.730   -11.949 41.760  1.00 32.62  ? 202 GLY   B H    1 
ATOM   7712 H HA2  . GLY   B 1 217 ? 5.279   -11.754 43.887  1.00 33.03  ? 202 GLY   B HA2  1 
ATOM   7713 H HA3  . GLY   B 1 217 ? 6.308   -10.653 43.414  1.00 33.03  ? 202 GLY   B HA3  1 
ATOM   7714 N N    . ILE   B 1 218 ? 4.461   -9.595  41.662  1.00 26.77  ? 203 ILE   B N    1 
ATOM   7715 C CA   . ILE   B 1 218 ? 3.361   -8.731  41.247  1.00 27.97  ? 203 ILE   B CA   1 
ATOM   7716 C C    . ILE   B 1 218 ? 2.078   -9.544  41.102  1.00 26.08  ? 203 ILE   B C    1 
ATOM   7717 O O    . ILE   B 1 218 ? 0.996   -9.116  41.527  1.00 26.23  ? 203 ILE   B O    1 
ATOM   7718 C CB   . ILE   B 1 218 ? 3.718   -8.001  39.939  1.00 28.45  ? 203 ILE   B CB   1 
ATOM   7719 C CG1  . ILE   B 1 218 ? 5.012   -7.197  40.096  1.00 27.39  ? 203 ILE   B CG1  1 
ATOM   7720 C CG2  . ILE   B 1 218 ? 2.582   -7.075  39.526  1.00 26.36  ? 203 ILE   B CG2  1 
ATOM   7721 C CD1  . ILE   B 1 218 ? 4.890   -5.977  41.018  1.00 27.63  ? 203 ILE   B CD1  1 
ATOM   7722 H H    . ILE   B 1 218 ? 5.119   -9.633  41.109  1.00 32.12  ? 203 ILE   B H    1 
ATOM   7723 H HA   . ILE   B 1 218 ? 3.218   -8.060  41.934  1.00 33.56  ? 203 ILE   B HA   1 
ATOM   7724 H HB   . ILE   B 1 218 ? 3.853   -8.672  39.252  1.00 34.14  ? 203 ILE   B HB   1 
ATOM   7725 H HG12 . ILE   B 1 218 ? 5.695   -7.778  40.466  1.00 32.86  ? 203 ILE   B HG12 1 
ATOM   7726 H HG13 . ILE   B 1 218 ? 5.286   -6.878  39.222  1.00 32.86  ? 203 ILE   B HG13 1 
ATOM   7727 H HG21 . ILE   B 1 218 ? 2.912   -6.447  38.865  1.00 31.63  ? 203 ILE   B HG21 1 
ATOM   7728 H HG22 . ILE   B 1 218 ? 1.863   -7.606  39.148  1.00 31.63  ? 203 ILE   B HG22 1 
ATOM   7729 H HG23 . ILE   B 1 218 ? 2.264   -6.597  40.307  1.00 31.63  ? 203 ILE   B HG23 1 
ATOM   7730 H HD11 . ILE   B 1 218 ? 5.770   -5.592  41.151  1.00 33.15  ? 203 ILE   B HD11 1 
ATOM   7731 H HD12 . ILE   B 1 218 ? 4.303   -5.326  40.604  1.00 33.15  ? 203 ILE   B HD12 1 
ATOM   7732 H HD13 . ILE   B 1 218 ? 4.521   -6.261  41.869  1.00 33.15  ? 203 ILE   B HD13 1 
ATOM   7733 N N    . THR   B 1 219 ? 2.181   -10.722 40.490  1.00 25.73  ? 204 THR   B N    1 
ATOM   7734 C CA   . THR   B 1 219 ? 1.015   -11.575 40.287  1.00 25.49  ? 204 THR   B CA   1 
ATOM   7735 C C    . THR   B 1 219 ? 0.381   -11.968 41.613  1.00 25.81  ? 204 THR   B C    1 
ATOM   7736 O O    . THR   B 1 219 ? -0.847  -12.063 41.719  1.00 25.93  ? 204 THR   B O    1 
ATOM   7737 C CB   . THR   B 1 219 ? 1.430   -12.821 39.499  1.00 25.27  ? 204 THR   B CB   1 
ATOM   7738 O OG1  . THR   B 1 219 ? 1.987   -12.420 38.241  1.00 25.19  ? 204 THR   B OG1  1 
ATOM   7739 C CG2  . THR   B 1 219 ? 0.236   -13.732 39.259  1.00 26.31  ? 204 THR   B CG2  1 
ATOM   7740 H H    . THR   B 1 219 ? 2.914   -11.051 40.183  1.00 30.88  ? 204 THR   B H    1 
ATOM   7741 H HA   . THR   B 1 219 ? 0.350   -11.090 39.774  1.00 30.59  ? 204 THR   B HA   1 
ATOM   7742 H HB   . THR   B 1 219 ? 2.090   -13.321 40.004  1.00 30.32  ? 204 THR   B HB   1 
ATOM   7743 H HG1  . THR   B 1 219 ? 2.663   -11.938 38.367  1.00 30.23  ? 204 THR   B HG1  1 
ATOM   7744 H HG21 . THR   B 1 219 ? 0.463   -14.410 38.603  1.00 31.57  ? 204 THR   B HG21 1 
ATOM   7745 H HG22 . THR   B 1 219 ? -0.020  -14.167 40.087  1.00 31.57  ? 204 THR   B HG22 1 
ATOM   7746 H HG23 . THR   B 1 219 ? -0.515  -13.214 38.930  1.00 31.57  ? 204 THR   B HG23 1 
ATOM   7747 N N    . ALA   B 1 220 ? 1.204   -12.201 42.638  1.00 26.17  ? 205 ALA   B N    1 
ATOM   7748 C CA   . ALA   B 1 220 ? 0.667   -12.508 43.958  1.00 26.72  ? 205 ALA   B CA   1 
ATOM   7749 C C    . ALA   B 1 220 ? -0.168  -11.352 44.485  1.00 31.35  ? 205 ALA   B C    1 
ATOM   7750 O O    . ALA   B 1 220 ? -1.247  -11.560 45.050  1.00 27.56  ? 205 ALA   B O    1 
ATOM   7751 C CB   . ALA   B 1 220 ? 1.805   -12.828 44.926  1.00 28.74  ? 205 ALA   B CB   1 
ATOM   7752 H H    . ALA   B 1 220 ? 2.063   -12.188 42.593  1.00 31.41  ? 205 ALA   B H    1 
ATOM   7753 H HA   . ALA   B 1 220 ? 0.099   -13.291 43.894  1.00 32.06  ? 205 ALA   B HA   1 
ATOM   7754 H HB1  . ALA   B 1 220 ? 1.431   -13.021 45.800  1.00 34.49  ? 205 ALA   B HB1  1 
ATOM   7755 H HB2  . ALA   B 1 220 ? 2.292   -13.599 44.596  1.00 34.49  ? 205 ALA   B HB2  1 
ATOM   7756 H HB3  . ALA   B 1 220 ? 2.396   -12.061 44.982  1.00 34.49  ? 205 ALA   B HB3  1 
ATOM   7757 N N    . ILE   B 1 221 ? 0.314   -10.118 44.307  1.00 31.36  ? 206 ILE   B N    1 
ATOM   7758 C CA   . ILE   B 1 221 ? -0.501  -8.958  44.660  1.00 28.22  ? 206 ILE   B CA   1 
ATOM   7759 C C    . ILE   B 1 221 ? -1.758  -8.927  43.801  1.00 27.53  ? 206 ILE   B C    1 
ATOM   7760 O O    . ILE   B 1 221 ? -2.864  -8.706  44.299  1.00 30.09  ? 206 ILE   B O    1 
ATOM   7761 C CB   . ILE   B 1 221 ? 0.320   -7.661  44.520  1.00 33.07  ? 206 ILE   B CB   1 
ATOM   7762 C CG1  . ILE   B 1 221 ? 1.606   -7.742  45.355  1.00 28.42  ? 206 ILE   B CG1  1 
ATOM   7763 C CG2  . ILE   B 1 221 ? -0.528  -6.464  44.937  1.00 30.88  ? 206 ILE   B CG2  1 
ATOM   7764 C CD1  . ILE   B 1 221 ? 2.495   -6.495  45.259  1.00 34.47  ? 206 ILE   B CD1  1 
ATOM   7765 H H    . ILE   B 1 221 ? 1.092   -9.931  43.990  1.00 37.64  ? 206 ILE   B H    1 
ATOM   7766 H HA   . ILE   B 1 221 ? -0.771  -9.035  45.589  1.00 33.87  ? 206 ILE   B HA   1 
ATOM   7767 H HB   . ILE   B 1 221 ? 0.576   -7.553  43.591  1.00 39.69  ? 206 ILE   B HB   1 
ATOM   7768 H HG12 . ILE   B 1 221 ? 1.365   -7.860  46.287  1.00 34.10  ? 206 ILE   B HG12 1 
ATOM   7769 H HG13 . ILE   B 1 221 ? 2.128   -8.500  45.049  1.00 34.10  ? 206 ILE   B HG13 1 
ATOM   7770 H HG21 . ILE   B 1 221 ? 0.001   -5.656  44.847  1.00 37.06  ? 206 ILE   B HG21 1 
ATOM   7771 H HG22 . ILE   B 1 221 ? -1.308  -6.414  44.362  1.00 37.06  ? 206 ILE   B HG22 1 
ATOM   7772 H HG23 . ILE   B 1 221 ? -0.804  -6.578  45.860  1.00 37.06  ? 206 ILE   B HG23 1 
ATOM   7773 H HD11 . ILE   B 1 221 ? 3.362   -6.695  45.647  1.00 41.36  ? 206 ILE   B HD11 1 
ATOM   7774 H HD12 . ILE   B 1 221 ? 2.598   -6.252  44.326  1.00 41.36  ? 206 ILE   B HD12 1 
ATOM   7775 H HD13 . ILE   B 1 221 ? 2.074   -5.769  45.746  1.00 41.36  ? 206 ILE   B HD13 1 
ATOM   7776 N N    . GLU   B 1 222 ? -1.607  -9.176  42.500  1.00 31.36  ? 207 GLU   B N    1 
ATOM   7777 C CA   . GLU   B 1 222 ? -2.746  -9.209  41.586  1.00 28.54  ? 207 GLU   B CA   1 
ATOM   7778 C C    . GLU   B 1 222 ? -3.831  -10.152 42.091  1.00 30.50  ? 207 GLU   B C    1 
ATOM   7779 O O    . GLU   B 1 222 ? -5.019  -9.810  42.097  1.00 27.79  ? 207 GLU   B O    1 
ATOM   7780 C CB   . GLU   B 1 222 ? -2.258  -9.633  40.195  1.00 26.16  ? 207 GLU   B CB   1 
ATOM   7781 C CG   . GLU   B 1 222 ? -3.359  -9.844  39.172  1.00 26.26  ? 207 GLU   B CG   1 
ATOM   7782 C CD   . GLU   B 1 222 ? -2.889  -10.613 37.950  1.00 27.57  ? 207 GLU   B CD   1 
ATOM   7783 O OE1  . GLU   B 1 222 ? -1.696  -10.973 37.887  1.00 25.44  ? 207 GLU   B OE1  1 
ATOM   7784 O OE2  . GLU   B 1 222 ? -3.725  -10.868 37.060  1.00 29.33  ? 207 GLU   B OE2  1 
ATOM   7785 H H    . GLU   B 1 222 ? -0.851  -9.330  42.119  1.00 37.63  ? 207 GLU   B H    1 
ATOM   7786 H HA   . GLU   B 1 222 ? -3.135  -8.322  41.522  1.00 34.25  ? 207 GLU   B HA   1 
ATOM   7787 H HB2  . GLU   B 1 222 ? -1.670  -8.943  39.851  1.00 31.39  ? 207 GLU   B HB2  1 
ATOM   7788 H HB3  . GLU   B 1 222 ? -1.775  -10.469 40.280  1.00 31.39  ? 207 GLU   B HB3  1 
ATOM   7789 H HG2  . GLU   B 1 222 ? -4.080  -10.346 39.583  1.00 31.51  ? 207 GLU   B HG2  1 
ATOM   7790 H HG3  . GLU   B 1 222 ? -3.685  -8.980  38.875  1.00 31.51  ? 207 GLU   B HG3  1 
ATOM   7791 N N    . LEU   B 1 223 ? -3.440  -11.360 42.499  1.00 31.72  ? 208 LEU   B N    1 
ATOM   7792 C CA   . LEU   B 1 223 ? -4.421  -12.338 42.951  1.00 27.39  ? 208 LEU   B CA   1 
ATOM   7793 C C    . LEU   B 1 223 ? -5.027  -11.932 44.285  1.00 28.69  ? 208 LEU   B C    1 
ATOM   7794 O O    . LEU   B 1 223 ? -6.183  -12.261 44.567  1.00 33.61  ? 208 LEU   B O    1 
ATOM   7795 C CB   . LEU   B 1 223 ? -3.772  -13.721 43.058  1.00 28.42  ? 208 LEU   B CB   1 
ATOM   7796 C CG   . LEU   B 1 223 ? -3.134  -14.278 41.774  1.00 26.32  ? 208 LEU   B CG   1 
ATOM   7797 C CD1  . LEU   B 1 223 ? -2.415  -15.583 42.039  1.00 29.68  ? 208 LEU   B CD1  1 
ATOM   7798 C CD2  . LEU   B 1 223 ? -4.175  -14.460 40.683  1.00 26.38  ? 208 LEU   B CD2  1 
ATOM   7799 H H    . LEU   B 1 223 ? -2.624  -11.633 42.523  1.00 38.07  ? 208 LEU   B H    1 
ATOM   7800 H HA   . LEU   B 1 223 ? -5.136  -12.395 42.298  1.00 32.87  ? 208 LEU   B HA   1 
ATOM   7801 H HB2  . LEU   B 1 223 ? -3.072  -13.674 43.728  1.00 34.10  ? 208 LEU   B HB2  1 
ATOM   7802 H HB3  . LEU   B 1 223 ? -4.454  -14.353 43.335  1.00 34.10  ? 208 LEU   B HB3  1 
ATOM   7803 H HG   . LEU   B 1 223 ? -2.478  -13.635 41.460  1.00 31.59  ? 208 LEU   B HG   1 
ATOM   7804 H HD11 . LEU   B 1 223 ? -2.022  -15.901 41.212  1.00 35.61  ? 208 LEU   B HD11 1 
ATOM   7805 H HD12 . LEU   B 1 223 ? -1.720  -15.432 42.699  1.00 35.61  ? 208 LEU   B HD12 1 
ATOM   7806 H HD13 . LEU   B 1 223 ? -3.053  -16.232 42.374  1.00 35.61  ? 208 LEU   B HD13 1 
ATOM   7807 H HD21 . LEU   B 1 223 ? -3.760  -14.890 39.919  1.00 31.66  ? 208 LEU   B HD21 1 
ATOM   7808 H HD22 . LEU   B 1 223 ? -4.895  -15.012 41.023  1.00 31.66  ? 208 LEU   B HD22 1 
ATOM   7809 H HD23 . LEU   B 1 223 ? -4.518  -13.590 40.426  1.00 31.66  ? 208 LEU   B HD23 1 
ATOM   7810 N N    . ALA   B 1 224 ? -4.267  -11.217 45.112  1.00 28.58  ? 209 ALA   B N    1 
ATOM   7811 C CA   . ALA   B 1 224 ? -4.768  -10.770 46.405  1.00 31.87  ? 209 ALA   B CA   1 
ATOM   7812 C C    . ALA   B 1 224 ? -5.671  -9.551  46.297  1.00 31.60  ? 209 ALA   B C    1 
ATOM   7813 O O    . ALA   B 1 224 ? -6.537  -9.355  47.152  1.00 35.29  ? 209 ALA   B O    1 
ATOM   7814 C CB   . ALA   B 1 224 ? -3.595  -10.456 47.334  1.00 35.37  ? 209 ALA   B CB   1 
ATOM   7815 H H    . ALA   B 1 224 ? -3.457  -10.978 44.947  1.00 34.30  ? 209 ALA   B H    1 
ATOM   7816 H HA   . ALA   B 1 224 ? -5.290  -11.490 46.792  1.00 38.24  ? 209 ALA   B HA   1 
ATOM   7817 H HB1  . ALA   B 1 224 ? -3.937  -10.060 48.151  1.00 42.45  ? 209 ALA   B HB1  1 
ATOM   7818 H HB2  . ALA   B 1 224 ? -3.123  -11.279 47.537  1.00 42.45  ? 209 ALA   B HB2  1 
ATOM   7819 H HB3  . ALA   B 1 224 ? -2.998  -9.833  46.889  1.00 42.45  ? 209 ALA   B HB3  1 
ATOM   7820 N N    . GLU   B 1 225 ? -5.497  -8.722  45.263  1.00 36.07  ? 210 GLU   B N    1 
ATOM   7821 C CA   . GLU   B 1 225 ? -6.169  -7.429  45.220  1.00 34.15  ? 210 GLU   B CA   1 
ATOM   7822 C C    . GLU   B 1 225 ? -6.943  -7.178  43.936  1.00 30.61  ? 210 GLU   B C    1 
ATOM   7823 O O    . GLU   B 1 225 ? -7.602  -6.143  43.830  1.00 34.48  ? 210 GLU   B O    1 
ATOM   7824 C CB   . GLU   B 1 225 ? -5.142  -6.303  45.419  1.00 36.96  ? 210 GLU   B CB   1 
ATOM   7825 C CG   . GLU   B 1 225 ? -4.256  -6.506  46.643  1.00 37.86  ? 210 GLU   B CG   1 
ATOM   7826 C CD   . GLU   B 1 225 ? -3.311  -5.344  46.903  1.00 40.04  ? 210 GLU   B CD   1 
ATOM   7827 O OE1  . GLU   B 1 225 ? -3.130  -4.488  46.007  1.00 37.87  ? 210 GLU   B OE1  1 
ATOM   7828 O OE2  . GLU   B 1 225 ? -2.745  -5.286  48.014  1.00 49.02  ? 210 GLU   B OE2  1 
ATOM   7829 H H    . GLU   B 1 225 ? -4.999  -8.888  44.582  1.00 43.29  ? 210 GLU   B H    1 
ATOM   7830 H HA   . GLU   B 1 225 ? -6.808  -7.390  45.949  1.00 40.98  ? 210 GLU   B HA   1 
ATOM   7831 H HB2  . GLU   B 1 225 ? -4.567  -6.261  44.639  1.00 44.36  ? 210 GLU   B HB2  1 
ATOM   7832 H HB3  . GLU   B 1 225 ? -5.614  -5.463  45.528  1.00 44.36  ? 210 GLU   B HB3  1 
ATOM   7833 H HG2  . GLU   B 1 225 ? -4.821  -6.610  47.425  1.00 45.43  ? 210 GLU   B HG2  1 
ATOM   7834 H HG3  . GLU   B 1 225 ? -3.719  -7.303  46.513  1.00 45.43  ? 210 GLU   B HG3  1 
ATOM   7835 N N    . LEU   B 1 226 ? -6.875  -8.080  42.966  1.00 34.57  ? 211 LEU   B N    1 
ATOM   7836 C CA   . LEU   B 1 226 ? -7.571  -8.050  41.686  1.00 31.68  ? 211 LEU   B CA   1 
ATOM   7837 C C    . LEU   B 1 226 ? -6.913  -7.097  40.696  1.00 33.08  ? 211 LEU   B C    1 
ATOM   7838 O O    . LEU   B 1 226 ? -7.384  -7.007  39.555  1.00 33.45  ? 211 LEU   B O    1 
ATOM   7839 C CB   . LEU   B 1 226 ? -9.055  -7.681  41.820  1.00 31.17  ? 211 LEU   B CB   1 
ATOM   7840 C CG   . LEU   B 1 226 ? -9.895  -8.597  42.718  1.00 38.01  ? 211 LEU   B CG   1 
ATOM   7841 C CD1  . LEU   B 1 226 ? -11.369 -8.285  42.548  1.00 50.24  ? 211 LEU   B CD1  1 
ATOM   7842 C CD2  . LEU   B 1 226 ? -9.634  -10.065 42.435  1.00 39.04  ? 211 LEU   B CD2  1 
ATOM   7843 H H    . LEU   B 1 226 ? -6.386  -8.784  43.036  1.00 41.48  ? 211 LEU   B H    1 
ATOM   7844 H HA   . LEU   B 1 226 ? -7.525  -8.940  41.302  1.00 38.01  ? 211 LEU   B HA   1 
ATOM   7845 H HB2  . LEU   B 1 226 ? -9.113  -6.785  42.189  1.00 37.40  ? 211 LEU   B HB2  1 
ATOM   7846 H HB3  . LEU   B 1 226 ? -9.454  -7.701  40.936  1.00 37.40  ? 211 LEU   B HB3  1 
ATOM   7847 H HG   . LEU   B 1 226 ? -9.638  -8.433  43.639  1.00 45.61  ? 211 LEU   B HG   1 
ATOM   7848 H HD11 . LEU   B 1 226 ? -11.883 -8.872  43.124  1.00 60.28  ? 211 LEU   B HD11 1 
ATOM   7849 H HD12 . LEU   B 1 226 ? -11.526 -7.360  42.793  1.00 60.28  ? 211 LEU   B HD12 1 
ATOM   7850 H HD13 . LEU   B 1 226 ? -11.617 -8.430  41.622  1.00 60.28  ? 211 LEU   B HD13 1 
ATOM   7851 H HD21 . LEU   B 1 226 ? -10.254 -10.601 42.953  1.00 46.85  ? 211 LEU   B HD21 1 
ATOM   7852 H HD22 . LEU   B 1 226 ? -9.764  -10.232 41.488  1.00 46.85  ? 211 LEU   B HD22 1 
ATOM   7853 H HD23 . LEU   B 1 226 ? -8.722  -10.278 42.687  1.00 46.85  ? 211 LEU   B HD23 1 
ATOM   7854 N N    . GLN   B 1 227 ? -5.843  -6.403  41.073  1.00 35.88  ? 212 GLN   B N    1 
ATOM   7855 C CA   . GLN   B 1 227 ? -5.108  -5.549  40.149  1.00 28.64  ? 212 GLN   B CA   1 
ATOM   7856 C C    . GLN   B 1 227 ? -3.640  -5.556  40.537  1.00 28.02  ? 212 GLN   B C    1 
ATOM   7857 O O    . GLN   B 1 227 ? -3.317  -5.605  41.728  1.00 29.86  ? 212 GLN   B O    1 
ATOM   7858 C CB   . GLN   B 1 227 ? -5.626  -4.101  40.165  1.00 37.51  ? 212 GLN   B CB   1 
ATOM   7859 C CG   . GLN   B 1 227 ? -7.027  -3.904  39.609  1.00 45.32  ? 212 GLN   B CG   1 
ATOM   7860 C CD   . GLN   B 1 227 ? -7.086  -4.044  38.103  1.00 46.68  ? 212 GLN   B CD   1 
ATOM   7861 O OE1  . GLN   B 1 227 ? -6.062  -4.221  37.447  1.00 49.43  ? 212 GLN   B OE1  1 
ATOM   7862 N NE2  . GLN   B 1 227 ? -8.291  -3.960  37.545  1.00 47.80  ? 212 GLN   B NE2  1 
ATOM   7863 H H    . GLN   B 1 227 ? -5.519  -6.412  41.870  1.00 43.06  ? 212 GLN   B H    1 
ATOM   7864 H HA   . GLN   B 1 227 ? -5.202  -5.907  39.252  1.00 34.36  ? 212 GLN   B HA   1 
ATOM   7865 H HB2  . GLN   B 1 227 ? -5.632  -3.788  41.083  1.00 45.02  ? 212 GLN   B HB2  1 
ATOM   7866 H HB3  . GLN   B 1 227 ? -5.025  -3.556  39.633  1.00 45.02  ? 212 GLN   B HB3  1 
ATOM   7867 H HG2  . GLN   B 1 227 ? -7.616  -4.571  39.996  1.00 54.38  ? 212 GLN   B HG2  1 
ATOM   7868 H HG3  . GLN   B 1 227 ? -7.336  -3.015  39.840  1.00 54.38  ? 212 GLN   B HG3  1 
ATOM   7869 H HE21 . GLN   B 1 227 ? -8.985  -3.833  38.037  1.00 57.36  ? 212 GLN   B HE21 1 
ATOM   7870 H HE22 . GLN   B 1 227 ? -8.376  -4.033  36.692  1.00 57.36  ? 212 GLN   B HE22 1 
ATOM   7871 N N    . PRO   B 1 228 ? -2.732  -5.480  39.571  1.00 31.49  ? 213 PRO   B N    1 
ATOM   7872 C CA   . PRO   B 1 228 ? -1.333  -5.206  39.901  1.00 32.72  ? 213 PRO   B CA   1 
ATOM   7873 C C    . PRO   B 1 228 ? -1.198  -3.811  40.484  1.00 34.09  ? 213 PRO   B C    1 
ATOM   7874 O O    . PRO   B 1 228 ? -2.087  -2.969  40.296  1.00 29.56  ? 213 PRO   B O    1 
ATOM   7875 C CB   . PRO   B 1 228 ? -0.623  -5.320  38.547  1.00 26.82  ? 213 PRO   B CB   1 
ATOM   7876 C CG   . PRO   B 1 228 ? -1.660  -4.944  37.566  1.00 28.49  ? 213 PRO   B CG   1 
ATOM   7877 C CD   . PRO   B 1 228 ? -2.955  -5.487  38.115  1.00 32.62  ? 213 PRO   B CD   1 
ATOM   7878 H HA   . PRO   B 1 228 ? -0.971  -5.865  40.515  1.00 39.26  ? 213 PRO   B HA   1 
ATOM   7879 H HB2  . PRO   B 1 228 ? 0.130   -4.709  38.512  1.00 32.19  ? 213 PRO   B HB2  1 
ATOM   7880 H HB3  . PRO   B 1 228 ? -0.319  -6.230  38.404  1.00 32.19  ? 213 PRO   B HB3  1 
ATOM   7881 H HG2  . PRO   B 1 228 ? -1.699  -3.978  37.483  1.00 34.19  ? 213 PRO   B HG2  1 
ATOM   7882 H HG3  . PRO   B 1 228 ? -1.457  -5.343  36.705  1.00 34.19  ? 213 PRO   B HG3  1 
ATOM   7883 H HD2  . PRO   B 1 228 ? -3.699  -4.911  37.877  1.00 39.14  ? 213 PRO   B HD2  1 
ATOM   7884 H HD3  . PRO   B 1 228 ? -3.117  -6.388  37.794  1.00 39.14  ? 213 PRO   B HD3  1 
ATOM   7885 N N    . PRO   B 1 229 ? -0.117  -3.525  41.208  1.00 28.18  ? 214 PRO   B N    1 
ATOM   7886 C CA   . PRO   B 1 229 ? 0.094   -2.155  41.696  1.00 35.01  ? 214 PRO   B CA   1 
ATOM   7887 C C    . PRO   B 1 229 ? 0.196   -1.160  40.546  1.00 31.43  ? 214 PRO   B C    1 
ATOM   7888 O O    . PRO   B 1 229 ? 0.642   -1.489  39.449  1.00 29.17  ? 214 PRO   B O    1 
ATOM   7889 C CB   . PRO   B 1 229 ? 1.416   -2.252  42.468  1.00 40.00  ? 214 PRO   B CB   1 
ATOM   7890 C CG   . PRO   B 1 229 ? 1.533   -3.706  42.840  1.00 28.64  ? 214 PRO   B CG   1 
ATOM   7891 C CD   . PRO   B 1 229 ? 0.903   -4.463  41.714  1.00 27.84  ? 214 PRO   B CD   1 
ATOM   7892 H HA   . PRO   B 1 229 ? -0.620  -1.889  42.295  1.00 42.01  ? 214 PRO   B HA   1 
ATOM   7893 H HB2  . PRO   B 1 229 ? 2.153   -1.978  41.900  1.00 48.00  ? 214 PRO   B HB2  1 
ATOM   7894 H HB3  . PRO   B 1 229 ? 1.380   -1.692  43.259  1.00 48.00  ? 214 PRO   B HB3  1 
ATOM   7895 H HG2  . PRO   B 1 229 ? 2.468   -3.946  42.935  1.00 34.37  ? 214 PRO   B HG2  1 
ATOM   7896 H HG3  . PRO   B 1 229 ? 1.062   -3.871  43.672  1.00 34.37  ? 214 PRO   B HG3  1 
ATOM   7897 H HD2  . PRO   B 1 229 ? 1.556   -4.667  41.027  1.00 33.41  ? 214 PRO   B HD2  1 
ATOM   7898 H HD3  . PRO   B 1 229 ? 0.491   -5.280  42.034  1.00 33.41  ? 214 PRO   B HD3  1 
ATOM   7899 N N    . LEU   B 1 230 ? -0.239  0.073   40.812  1.00 30.51  ? 215 LEU   B N    1 
ATOM   7900 C CA   . LEU   B 1 230 ? -0.173  1.185   39.861  1.00 33.90  ? 215 LEU   B CA   1 
ATOM   7901 C C    . LEU   B 1 230 ? -1.063  0.975   38.640  1.00 30.34  ? 215 LEU   B C    1 
ATOM   7902 O O    . LEU   B 1 230 ? -0.899  1.659   37.626  1.00 30.64  ? 215 LEU   B O    1 
ATOM   7903 C CB   . LEU   B 1 230 ? 1.270   1.439   39.417  1.00 33.39  ? 215 LEU   B CB   1 
ATOM   7904 C CG   . LEU   B 1 230 ? 2.231   1.870   40.529  1.00 35.19  ? 215 LEU   B CG   1 
ATOM   7905 C CD1  . LEU   B 1 230 ? 3.673   1.816   40.068  1.00 31.08  ? 215 LEU   B CD1  1 
ATOM   7906 C CD2  . LEU   B 1 230 ? 1.896   3.271   41.015  1.00 38.08  ? 215 LEU   B CD2  1 
ATOM   7907 H H    . LEU   B 1 230 ? -0.589  0.298   41.564  1.00 36.61  ? 215 LEU   B H    1 
ATOM   7908 H HA   . LEU   B 1 230 ? -0.498  1.980   40.311  1.00 40.68  ? 215 LEU   B HA   1 
ATOM   7909 H HB2  . LEU   B 1 230 ? 1.620   0.620   39.032  1.00 40.07  ? 215 LEU   B HB2  1 
ATOM   7910 H HB3  . LEU   B 1 230 ? 1.264   2.143   38.750  1.00 40.07  ? 215 LEU   B HB3  1 
ATOM   7911 H HG   . LEU   B 1 230 ? 2.131   1.250   41.268  1.00 42.23  ? 215 LEU   B HG   1 
ATOM   7912 H HD11 . LEU   B 1 230 ? 4.248   2.092   40.799  1.00 37.30  ? 215 LEU   B HD11 1 
ATOM   7913 H HD12 . LEU   B 1 230 ? 3.886   0.907   39.804  1.00 37.30  ? 215 LEU   B HD12 1 
ATOM   7914 H HD13 . LEU   B 1 230 ? 3.786   2.415   39.314  1.00 37.30  ? 215 LEU   B HD13 1 
ATOM   7915 H HD21 . LEU   B 1 230 ? 2.561   3.547   41.664  1.00 45.70  ? 215 LEU   B HD21 1 
ATOM   7916 H HD22 . LEU   B 1 230 ? 1.901   3.877   40.258  1.00 45.70  ? 215 LEU   B HD22 1 
ATOM   7917 H HD23 . LEU   B 1 230 ? 1.017   3.261   41.425  1.00 45.70  ? 215 LEU   B HD23 1 
ATOM   7918 N N    . PHE   B 1 231 ? -2.038  0.064   38.742  1.00 32.79  ? 216 PHE   B N    1 
ATOM   7919 C CA   . PHE   B 1 231 ? -2.871  -0.285  37.596  1.00 32.69  ? 216 PHE   B CA   1 
ATOM   7920 C C    . PHE   B 1 231 ? -3.652  0.908   37.066  1.00 31.03  ? 216 PHE   B C    1 
ATOM   7921 O O    . PHE   B 1 231 ? -4.008  0.938   35.886  1.00 31.19  ? 216 PHE   B O    1 
ATOM   7922 C CB   . PHE   B 1 231 ? -3.869  -1.384  37.980  1.00 31.09  ? 216 PHE   B CB   1 
ATOM   7923 C CG   . PHE   B 1 231 ? -5.098  -0.852  38.678  1.00 40.56  ? 216 PHE   B CG   1 
ATOM   7924 C CD1  . PHE   B 1 231 ? -5.098  -0.652  40.052  1.00 42.57  ? 216 PHE   B CD1  1 
ATOM   7925 C CD2  . PHE   B 1 231 ? -6.242  -0.515  37.956  1.00 39.62  ? 216 PHE   B CD2  1 
ATOM   7926 C CE1  . PHE   B 1 231 ? -6.220  -0.143  40.699  1.00 46.75  ? 216 PHE   B CE1  1 
ATOM   7927 C CE2  . PHE   B 1 231 ? -7.370  -0.002  38.595  1.00 39.38  ? 216 PHE   B CE2  1 
ATOM   7928 C CZ   . PHE   B 1 231 ? -7.358  0.183   39.967  1.00 43.24  ? 216 PHE   B CZ   1 
ATOM   7929 H H    . PHE   B 1 231 ? -2.235  -0.362  39.462  1.00 39.35  ? 216 PHE   B H    1 
ATOM   7930 H HA   . PHE   B 1 231 ? -2.283  -0.611  36.897  1.00 39.23  ? 216 PHE   B HA   1 
ATOM   7931 H HB2  . PHE   B 1 231 ? -4.157  -1.841  37.174  1.00 37.31  ? 216 PHE   B HB2  1 
ATOM   7932 H HB3  . PHE   B 1 231 ? -3.432  -2.010  38.578  1.00 37.31  ? 216 PHE   B HB3  1 
ATOM   7933 H HD1  . PHE   B 1 231 ? -4.339  -0.861  40.547  1.00 51.08  ? 216 PHE   B HD1  1 
ATOM   7934 H HD2  . PHE   B 1 231 ? -6.252  -0.634  37.033  1.00 47.54  ? 216 PHE   B HD2  1 
ATOM   7935 H HE1  . PHE   B 1 231 ? -6.209  -0.021  41.621  1.00 56.09  ? 216 PHE   B HE1  1 
ATOM   7936 H HE2  . PHE   B 1 231 ? -8.127  0.215   38.101  1.00 47.26  ? 216 PHE   B HE2  1 
ATOM   7937 H HZ   . PHE   B 1 231 ? -8.108  0.525   40.398  1.00 51.88  ? 216 PHE   B HZ   1 
ATOM   7938 N N    . ASP   B 1 232 ? -3.996  1.859   37.933  1.00 31.97  ? 217 ASP   B N    1 
ATOM   7939 C CA   . ASP   B 1 232 ? -4.764  3.030   37.529  1.00 33.25  ? 217 ASP   B CA   1 
ATOM   7940 C C    . ASP   B 1 232 ? -3.878  4.172   37.041  1.00 37.56  ? 217 ASP   B C    1 
ATOM   7941 O O    . ASP   B 1 232 ? -4.396  5.254   36.733  1.00 35.11  ? 217 ASP   B O    1 
ATOM   7942 C CB   . ASP   B 1 232 ? -5.651  3.508   38.687  1.00 34.38  ? 217 ASP   B CB   1 
ATOM   7943 C CG   . ASP   B 1 232 ? -4.877  3.733   39.989  1.00 34.40  ? 217 ASP   B CG   1 
ATOM   7944 O OD1  . ASP   B 1 232 ? -3.863  3.042   40.229  1.00 33.34  ? 217 ASP   B OD1  1 
ATOM   7945 O OD2  . ASP   B 1 232 ? -5.302  4.597   40.788  1.00 42.49  ? 217 ASP   B OD2  1 
ATOM   7946 H H    . ASP   B 1 232 ? -3.793  1.846   38.769  1.00 38.36  ? 217 ASP   B H    1 
ATOM   7947 H HA   . ASP   B 1 232 ? -5.352  2.783   36.798  1.00 39.90  ? 217 ASP   B HA   1 
ATOM   7948 H HB2  . ASP   B 1 232 ? -6.066  4.348   38.438  1.00 41.26  ? 217 ASP   B HB2  1 
ATOM   7949 H HB3  . ASP   B 1 232 ? -6.332  2.839   38.857  1.00 41.26  ? 217 ASP   B HB3  1 
ATOM   7950 N N    . VAL   B 1 233 ? -2.572  3.951   36.957  1.00 32.88  ? 218 VAL   B N    1 
ATOM   7951 C CA   . VAL   B 1 233 ? -1.604  4.973   36.596  1.00 33.38  ? 218 VAL   B CA   1 
ATOM   7952 C C    . VAL   B 1 233 ? -1.181  4.769   35.148  1.00 33.08  ? 218 VAL   B C    1 
ATOM   7953 O O    . VAL   B 1 233 ? -1.044  3.635   34.675  1.00 32.15  ? 218 VAL   B O    1 
ATOM   7954 C CB   . VAL   B 1 233 ? -0.390  4.931   37.545  1.00 33.10  ? 218 VAL   B CB   1 
ATOM   7955 C CG1  . VAL   B 1 233 ? 0.656   5.946   37.116  1.00 38.53  ? 218 VAL   B CG1  1 
ATOM   7956 C CG2  . VAL   B 1 233 ? -0.834  5.207   38.982  1.00 35.57  ? 218 VAL   B CG2  1 
ATOM   7957 H H    . VAL   B 1 233 ? -2.211  3.186   37.112  1.00 39.45  ? 218 VAL   B H    1 
ATOM   7958 H HA   . VAL   B 1 233 ? -2.018  5.848   36.665  1.00 40.06  ? 218 VAL   B HA   1 
ATOM   7959 H HB   . VAL   B 1 233 ? 0.007   4.047   37.506  1.00 39.72  ? 218 VAL   B HB   1 
ATOM   7960 H HG11 . VAL   B 1 233 ? 1.305   6.052   37.830  1.00 46.24  ? 218 VAL   B HG11 1 
ATOM   7961 H HG12 . VAL   B 1 233 ? 1.097   5.626   36.314  1.00 46.24  ? 218 VAL   B HG12 1 
ATOM   7962 H HG13 . VAL   B 1 233 ? 0.220   6.794   36.938  1.00 46.24  ? 218 VAL   B HG13 1 
ATOM   7963 H HG21 . VAL   B 1 233 ? -0.052  5.220   39.557  1.00 42.69  ? 218 VAL   B HG21 1 
ATOM   7964 H HG22 . VAL   B 1 233 ? -1.282  6.067   39.015  1.00 42.69  ? 218 VAL   B HG22 1 
ATOM   7965 H HG23 . VAL   B 1 233 ? -1.441  4.506   39.265  1.00 42.69  ? 218 VAL   B HG23 1 
ATOM   7966 N N    . HIS   B 1 234 ? -0.978  5.877   34.446  1.00 35.42  ? 219 HIS   B N    1 
ATOM   7967 C CA   . HIS   B 1 234 ? -0.608  5.827   33.042  1.00 34.12  ? 219 HIS   B CA   1 
ATOM   7968 C C    . HIS   B 1 234 ? 0.596   4.907   32.852  1.00 33.93  ? 219 HIS   B C    1 
ATOM   7969 O O    . HIS   B 1 234 ? 1.582   5.024   33.589  1.00 34.53  ? 219 HIS   B O    1 
ATOM   7970 C CB   . HIS   B 1 234 ? -0.286  7.237   32.547  1.00 35.45  ? 219 HIS   B CB   1 
ATOM   7971 C CG   . HIS   B 1 234 ? -0.105  7.335   31.068  1.00 39.53  ? 219 HIS   B CG   1 
ATOM   7972 N ND1  . HIS   B 1 234 ? 0.969   6.775   30.411  1.00 38.86  ? 219 HIS   B ND1  1 
ATOM   7973 C CD2  . HIS   B 1 234 ? -0.846  7.952   30.117  1.00 40.93  ? 219 HIS   B CD2  1 
ATOM   7974 C CE1  . HIS   B 1 234 ? 0.874   7.030   29.118  1.00 36.28  ? 219 HIS   B CE1  1 
ATOM   7975 N NE2  . HIS   B 1 234 ? -0.218  7.742   28.914  1.00 37.77  ? 219 HIS   B NE2  1 
ATOM   7976 H H    . HIS   B 1 234 ? -1.049  6.673   34.762  1.00 42.51  ? 219 HIS   B H    1 
ATOM   7977 H HA   . HIS   B 1 234 ? -1.343  5.475   32.516  1.00 40.95  ? 219 HIS   B HA   1 
ATOM   7978 H HB2  . HIS   B 1 234 ? -1.015  7.827   32.794  1.00 42.53  ? 219 HIS   B HB2  1 
ATOM   7979 H HB3  . HIS   B 1 234 ? 0.537   7.533   32.965  1.00 42.53  ? 219 HIS   B HB3  1 
ATOM   7980 H HD2  . HIS   B 1 234 ? -1.633  8.429   30.254  1.00 49.11  ? 219 HIS   B HD2  1 
ATOM   7981 H HE1  . HIS   B 1 234 ? 1.474   6.754   28.464  1.00 43.54  ? 219 HIS   B HE1  1 
ATOM   7982 H HE2  . HIS   B 1 234 ? -0.492  8.028   28.151  1.00 45.32  ? 219 HIS   B HE2  1 
ATOM   7983 N N    . PRO   B 1 235 ? 0.562   3.999   31.871  1.00 35.57  ? 220 PRO   B N    1 
ATOM   7984 C CA   . PRO   B 1 235 ? 1.626   2.985   31.794  1.00 31.88  ? 220 PRO   B CA   1 
ATOM   7985 C C    . PRO   B 1 235 ? 2.996   3.557   31.499  1.00 32.51  ? 220 PRO   B C    1 
ATOM   7986 O O    . PRO   B 1 235 ? 3.996   3.048   32.020  1.00 32.08  ? 220 PRO   B O    1 
ATOM   7987 C CB   . PRO   B 1 235 ? 1.134   2.056   30.676  1.00 31.62  ? 220 PRO   B CB   1 
ATOM   7988 C CG   . PRO   B 1 235 ? 0.200   2.873   29.866  1.00 32.62  ? 220 PRO   B CG   1 
ATOM   7989 C CD   . PRO   B 1 235 ? -0.447  3.836   30.813  1.00 36.83  ? 220 PRO   B CD   1 
ATOM   7990 H HA   . PRO   B 1 235 ? 1.669   2.493   32.629  1.00 38.25  ? 220 PRO   B HA   1 
ATOM   7991 H HB2  . PRO   B 1 235 ? 1.887   1.760   30.140  1.00 37.95  ? 220 PRO   B HB2  1 
ATOM   7992 H HB3  . PRO   B 1 235 ? 0.680   1.291   31.061  1.00 37.95  ? 220 PRO   B HB3  1 
ATOM   7993 H HG2  . PRO   B 1 235 ? 0.695   3.348   29.180  1.00 39.14  ? 220 PRO   B HG2  1 
ATOM   7994 H HG3  . PRO   B 1 235 ? -0.464  2.296   29.458  1.00 39.14  ? 220 PRO   B HG3  1 
ATOM   7995 H HD2  . PRO   B 1 235 ? -0.628  4.682   30.375  1.00 44.20  ? 220 PRO   B HD2  1 
ATOM   7996 H HD3  . PRO   B 1 235 ? -1.268  3.467   31.174  1.00 44.20  ? 220 PRO   B HD3  1 
ATOM   7997 N N    . LEU   B 1 236 ? 3.083   4.597   30.665  1.00 33.56  ? 221 LEU   B N    1 
ATOM   7998 C CA   . LEU   B 1 236 ? 4.375   5.226   30.415  1.00 34.37  ? 221 LEU   B CA   1 
ATOM   7999 C C    . LEU   B 1 236 ? 4.922   5.838   31.699  1.00 34.55  ? 221 LEU   B C    1 
ATOM   8000 O O    . LEU   B 1 236 ? 6.089   5.636   32.050  1.00 34.65  ? 221 LEU   B O    1 
ATOM   8001 C CB   . LEU   B 1 236 ? 4.237   6.289   29.315  1.00 39.09  ? 221 LEU   B CB   1 
ATOM   8002 C CG   . LEU   B 1 236 ? 5.512   6.822   28.658  1.00 36.81  ? 221 LEU   B CG   1 
ATOM   8003 C CD1  . LEU   B 1 236 ? 6.356   5.695   28.062  1.00 44.11  ? 221 LEU   B CD1  1 
ATOM   8004 C CD2  . LEU   B 1 236 ? 5.171   7.855   27.574  1.00 38.22  ? 221 LEU   B CD2  1 
ATOM   8005 H H    . LEU   B 1 236 ? 2.422   4.948   30.242  1.00 40.27  ? 221 LEU   B H    1 
ATOM   8006 H HA   . LEU   B 1 236 ? 5.004   4.559   30.101  1.00 41.24  ? 221 LEU   B HA   1 
ATOM   8007 H HB2  . LEU   B 1 236 ? 3.698   5.908   28.604  1.00 46.91  ? 221 LEU   B HB2  1 
ATOM   8008 H HB3  . LEU   B 1 236 ? 3.783   7.055   29.701  1.00 46.91  ? 221 LEU   B HB3  1 
ATOM   8009 H HG   . LEU   B 1 236 ? 6.043   7.254   29.346  1.00 44.17  ? 221 LEU   B HG   1 
ATOM   8010 H HD11 . LEU   B 1 236 ? 7.076   6.082   27.540  1.00 52.93  ? 221 LEU   B HD11 1 
ATOM   8011 H HD12 . LEU   B 1 236 ? 6.722   5.159   28.783  1.00 52.93  ? 221 LEU   B HD12 1 
ATOM   8012 H HD13 . LEU   B 1 236 ? 5.793   5.146   27.494  1.00 52.93  ? 221 LEU   B HD13 1 
ATOM   8013 H HD21 . LEU   B 1 236 ? 5.995   8.177   27.176  1.00 45.86  ? 221 LEU   B HD21 1 
ATOM   8014 H HD22 . LEU   B 1 236 ? 4.620   7.432   26.898  1.00 45.86  ? 221 LEU   B HD22 1 
ATOM   8015 H HD23 . LEU   B 1 236 ? 4.690   8.592   27.981  1.00 45.86  ? 221 LEU   B HD23 1 
ATOM   8016 N N    . ARG   B 1 237 ? 4.085   6.586   32.416  1.00 34.81  ? 222 ARG   B N    1 
ATOM   8017 C CA   . ARG   B 1 237 ? 4.485   7.109   33.715  1.00 35.10  ? 222 ARG   B CA   1 
ATOM   8018 C C    . ARG   B 1 237 ? 4.992   5.991   34.617  1.00 37.42  ? 222 ARG   B C    1 
ATOM   8019 O O    . ARG   B 1 237 ? 5.995   6.153   35.320  1.00 35.79  ? 222 ARG   B O    1 
ATOM   8020 C CB   . ARG   B 1 237 ? 3.300   7.845   34.350  1.00 39.69  ? 222 ARG   B CB   1 
ATOM   8021 C CG   . ARG   B 1 237 ? 3.635   8.644   35.577  1.00 36.27  ? 222 ARG   B CG   1 
ATOM   8022 C CD   . ARG   B 1 237 ? 2.536   9.649   35.912  1.00 37.99  ? 222 ARG   B CD   1 
ATOM   8023 N NE   . ARG   B 1 237 ? 2.719   10.924  35.225  1.00 38.60  ? 222 ARG   B NE   1 
ATOM   8024 C CZ   . ARG   B 1 237 ? 1.819   11.513  34.440  1.00 44.57  ? 222 ARG   B CZ   1 
ATOM   8025 N NH1  . ARG   B 1 237 ? 0.635   10.968  34.206  1.00 41.83  ? 222 ARG   B NH1  1 
ATOM   8026 N NH2  . ARG   B 1 237 ? 2.111   12.685  33.889  1.00 44.54  ? 222 ARG   B NH2  1 
ATOM   8027 H H    . ARG   B 1 237 ? 3.288   6.801   32.175  1.00 41.78  ? 222 ARG   B H    1 
ATOM   8028 H HA   . ARG   B 1 237 ? 5.208   7.748   33.607  1.00 42.12  ? 222 ARG   B HA   1 
ATOM   8029 H HB2  . ARG   B 1 237 ? 2.932   8.459   33.695  1.00 47.63  ? 222 ARG   B HB2  1 
ATOM   8030 H HB3  . ARG   B 1 237 ? 2.631   7.190   34.603  1.00 47.63  ? 222 ARG   B HB3  1 
ATOM   8031 H HG2  . ARG   B 1 237 ? 3.739   8.044   36.332  1.00 43.52  ? 222 ARG   B HG2  1 
ATOM   8032 H HG3  . ARG   B 1 237 ? 4.459   9.133   35.426  1.00 43.52  ? 222 ARG   B HG3  1 
ATOM   8033 H HD2  . ARG   B 1 237 ? 1.678   9.283   35.644  1.00 45.58  ? 222 ARG   B HD2  1 
ATOM   8034 H HD3  . ARG   B 1 237 ? 2.541   9.819   36.867  1.00 45.58  ? 222 ARG   B HD3  1 
ATOM   8035 H HE   . ARG   B 1 237 ? 3.470   11.329  35.336  1.00 46.32  ? 222 ARG   B HE   1 
ATOM   8036 H HH11 . ARG   B 1 237 ? 0.430   10.213  34.564  1.00 50.19  ? 222 ARG   B HH11 1 
ATOM   8037 H HH12 . ARG   B 1 237 ? 0.071   11.368  33.695  1.00 50.19  ? 222 ARG   B HH12 1 
ATOM   8038 H HH21 . ARG   B 1 237 ? 2.873   13.054  34.040  1.00 53.45  ? 222 ARG   B HH21 1 
ATOM   8039 H HH22 . ARG   B 1 237 ? 1.538   13.076  33.380  1.00 53.45  ? 222 ARG   B HH22 1 
ATOM   8040 N N    . VAL   B 1 238 ? 4.334   4.828   34.586  1.00 34.10  ? 223 VAL   B N    1 
ATOM   8041 C CA   . VAL   B 1 238 ? 4.789   3.716   35.419  1.00 34.84  ? 223 VAL   B CA   1 
ATOM   8042 C C    . VAL   B 1 238 ? 6.214   3.333   35.043  1.00 32.38  ? 223 VAL   B C    1 
ATOM   8043 O O    . VAL   B 1 238 ? 7.072   3.140   35.918  1.00 32.56  ? 223 VAL   B O    1 
ATOM   8044 C CB   . VAL   B 1 238 ? 3.820   2.524   35.297  1.00 31.09  ? 223 VAL   B CB   1 
ATOM   8045 C CG1  . VAL   B 1 238 ? 4.453   1.255   35.866  1.00 30.34  ? 223 VAL   B CG1  1 
ATOM   8046 C CG2  . VAL   B 1 238 ? 2.521   2.840   36.015  1.00 31.13  ? 223 VAL   B CG2  1 
ATOM   8047 H H    . VAL   B 1 238 ? 3.641   4.662   34.104  1.00 40.92  ? 223 VAL   B H    1 
ATOM   8048 H HA   . VAL   B 1 238 ? 4.790   3.999   36.346  1.00 41.81  ? 223 VAL   B HA   1 
ATOM   8049 H HB   . VAL   B 1 238 ? 3.626   2.366   34.360  1.00 37.31  ? 223 VAL   B HB   1 
ATOM   8050 H HG11 . VAL   B 1 238 ? 3.758   0.598   36.023  1.00 36.41  ? 223 VAL   B HG11 1 
ATOM   8051 H HG12 . VAL   B 1 238 ? 5.097   0.910   35.228  1.00 36.41  ? 223 VAL   B HG12 1 
ATOM   8052 H HG13 . VAL   B 1 238 ? 4.898   1.472   36.701  1.00 36.41  ? 223 VAL   B HG13 1 
ATOM   8053 H HG21 . VAL   B 1 238 ? 1.918   2.085   35.924  1.00 37.36  ? 223 VAL   B HG21 1 
ATOM   8054 H HG22 . VAL   B 1 238 ? 2.710   3.000   36.953  1.00 37.36  ? 223 VAL   B HG22 1 
ATOM   8055 H HG23 . VAL   B 1 238 ? 2.124   3.630   35.618  1.00 37.36  ? 223 VAL   B HG23 1 
ATOM   8056 N N    . LEU   B 1 239 ? 6.500   3.246   33.743  1.00 32.59  ? 224 LEU   B N    1 
ATOM   8057 C CA   . LEU   B 1 239 ? 7.854   2.940   33.295  1.00 36.36  ? 224 LEU   B CA   1 
ATOM   8058 C C    . LEU   B 1 239 ? 8.847   3.989   33.779  1.00 39.91  ? 224 LEU   B C    1 
ATOM   8059 O O    . LEU   B 1 239 ? 9.961   3.655   34.202  1.00 38.65  ? 224 LEU   B O    1 
ATOM   8060 C CB   . LEU   B 1 239 ? 7.895   2.849   31.768  1.00 42.40  ? 224 LEU   B CB   1 
ATOM   8061 C CG   . LEU   B 1 239 ? 7.209   1.649   31.122  1.00 35.26  ? 224 LEU   B CG   1 
ATOM   8062 C CD1  . LEU   B 1 239 ? 6.921   1.935   29.663  1.00 34.55  ? 224 LEU   B CD1  1 
ATOM   8063 C CD2  . LEU   B 1 239 ? 8.077   0.422   31.254  1.00 32.25  ? 224 LEU   B CD2  1 
ATOM   8064 H H    . LEU   B 1 239 ? 5.932   3.359   33.107  1.00 39.11  ? 224 LEU   B H    1 
ATOM   8065 H HA   . LEU   B 1 239 ? 8.111   2.080   33.662  1.00 43.63  ? 224 LEU   B HA   1 
ATOM   8066 H HB2  . LEU   B 1 239 ? 7.469   3.644   31.411  1.00 50.88  ? 224 LEU   B HB2  1 
ATOM   8067 H HB3  . LEU   B 1 239 ? 8.826   2.821   31.497  1.00 50.88  ? 224 LEU   B HB3  1 
ATOM   8068 H HG   . LEU   B 1 239 ? 6.367   1.479   31.572  1.00 42.31  ? 224 LEU   B HG   1 
ATOM   8069 H HD11 . LEU   B 1 239 ? 6.503   1.155   29.266  1.00 41.46  ? 224 LEU   B HD11 1 
ATOM   8070 H HD12 . LEU   B 1 239 ? 6.324   2.697   29.603  1.00 41.46  ? 224 LEU   B HD12 1 
ATOM   8071 H HD13 . LEU   B 1 239 ? 7.755   2.131   29.209  1.00 41.46  ? 224 LEU   B HD13 1 
ATOM   8072 H HD21 . LEU   B 1 239 ? 7.655   -0.315  30.785  1.00 38.70  ? 224 LEU   B HD21 1 
ATOM   8073 H HD22 . LEU   B 1 239 ? 8.947   0.607   30.866  1.00 38.70  ? 224 LEU   B HD22 1 
ATOM   8074 H HD23 . LEU   B 1 239 ? 8.174   0.203   32.194  1.00 38.70  ? 224 LEU   B HD23 1 
ATOM   8075 N N    . PHE   B 1 240 ? 8.470   5.268   33.703  1.00 37.34  ? 225 PHE   B N    1 
ATOM   8076 C CA   . PHE   B 1 240 ? 9.356   6.325   34.172  1.00 36.44  ? 225 PHE   B CA   1 
ATOM   8077 C C    . PHE   B 1 240 ? 9.647   6.172   35.662  1.00 36.38  ? 225 PHE   B C    1 
ATOM   8078 O O    . PHE   B 1 240 ? 10.800  6.287   36.092  1.00 37.89  ? 225 PHE   B O    1 
ATOM   8079 C CB   . PHE   B 1 240 ? 8.738   7.694   33.877  1.00 37.85  ? 225 PHE   B CB   1 
ATOM   8080 C CG   . PHE   B 1 240 ? 8.641   8.033   32.397  1.00 45.01  ? 225 PHE   B CG   1 
ATOM   8081 C CD1  . PHE   B 1 240 ? 9.421   7.379   31.450  1.00 37.99  ? 225 PHE   B CD1  1 
ATOM   8082 C CD2  . PHE   B 1 240 ? 7.764   9.020   31.962  1.00 45.96  ? 225 PHE   B CD2  1 
ATOM   8083 C CE1  . PHE   B 1 240 ? 9.327   7.698   30.108  1.00 38.71  ? 225 PHE   B CE1  1 
ATOM   8084 C CE2  . PHE   B 1 240 ? 7.670   9.345   30.611  1.00 47.46  ? 225 PHE   B CE2  1 
ATOM   8085 C CZ   . PHE   B 1 240 ? 8.453   8.682   29.688  1.00 39.25  ? 225 PHE   B CZ   1 
ATOM   8086 H H    . PHE   B 1 240 ? 7.718   5.543   33.389  1.00 44.81  ? 225 PHE   B H    1 
ATOM   8087 H HA   . PHE   B 1 240 ? 10.198  6.269   33.694  1.00 43.72  ? 225 PHE   B HA   1 
ATOM   8088 H HB2  . PHE   B 1 240 ? 7.839   7.713   34.242  1.00 45.42  ? 225 PHE   B HB2  1 
ATOM   8089 H HB3  . PHE   B 1 240 ? 9.282   8.377   34.299  1.00 45.42  ? 225 PHE   B HB3  1 
ATOM   8090 H HD1  . PHE   B 1 240 ? 10.016  6.718   31.724  1.00 45.59  ? 225 PHE   B HD1  1 
ATOM   8091 H HD2  . PHE   B 1 240 ? 7.235   9.470   32.580  1.00 55.16  ? 225 PHE   B HD2  1 
ATOM   8092 H HE1  . PHE   B 1 240 ? 9.852   7.248   29.486  1.00 46.45  ? 225 PHE   B HE1  1 
ATOM   8093 H HE2  . PHE   B 1 240 ? 7.080   10.007  30.331  1.00 56.95  ? 225 PHE   B HE2  1 
ATOM   8094 H HZ   . PHE   B 1 240 ? 8.393   8.898   28.785  1.00 47.11  ? 225 PHE   B HZ   1 
ATOM   8095 N N    . LEU   B 1 241 ? 8.619   5.894   36.465  1.00 35.51  ? 226 LEU   B N    1 
ATOM   8096 C CA   . LEU   B 1 241 ? 8.825   5.761   37.905  1.00 36.81  ? 226 LEU   B CA   1 
ATOM   8097 C C    . LEU   B 1 241 ? 9.738   4.586   38.237  1.00 40.07  ? 226 LEU   B C    1 
ATOM   8098 O O    . LEU   B 1 241 ? 10.597  4.691   39.119  1.00 36.20  ? 226 LEU   B O    1 
ATOM   8099 C CB   . LEU   B 1 241 ? 7.481   5.599   38.616  1.00 40.59  ? 226 LEU   B CB   1 
ATOM   8100 C CG   . LEU   B 1 241 ? 6.599   6.846   38.698  1.00 42.36  ? 226 LEU   B CG   1 
ATOM   8101 C CD1  . LEU   B 1 241 ? 5.206   6.466   39.159  1.00 49.12  ? 226 LEU   B CD1  1 
ATOM   8102 C CD2  . LEU   B 1 241 ? 7.196   7.877   39.638  1.00 44.47  ? 226 LEU   B CD2  1 
ATOM   8103 H H    . LEU   B 1 241 ? 7.807   5.779   36.206  1.00 42.61  ? 226 LEU   B H    1 
ATOM   8104 H HA   . LEU   B 1 241 ? 9.248   6.572   38.228  1.00 44.18  ? 226 LEU   B HA   1 
ATOM   8105 H HB2  . LEU   B 1 241 ? 6.973   4.921   38.145  1.00 48.71  ? 226 LEU   B HB2  1 
ATOM   8106 H HB3  . LEU   B 1 241 ? 7.655   5.313   39.526  1.00 48.71  ? 226 LEU   B HB3  1 
ATOM   8107 H HG   . LEU   B 1 241 ? 6.541   7.246   37.816  1.00 50.84  ? 226 LEU   B HG   1 
ATOM   8108 H HD11 . LEU   B 1 241 ? 4.662   7.267   39.214  1.00 58.94  ? 226 LEU   B HD11 1 
ATOM   8109 H HD12 . LEU   B 1 241 ? 4.820   5.847   38.520  1.00 58.94  ? 226 LEU   B HD12 1 
ATOM   8110 H HD13 . LEU   B 1 241 ? 5.266   6.047   40.032  1.00 58.94  ? 226 LEU   B HD13 1 
ATOM   8111 H HD21 . LEU   B 1 241 ? 6.576   8.618   39.729  1.00 53.36  ? 226 LEU   B HD21 1 
ATOM   8112 H HD22 . LEU   B 1 241 ? 7.348   7.465   40.503  1.00 53.36  ? 226 LEU   B HD22 1 
ATOM   8113 H HD23 . LEU   B 1 241 ? 8.036   8.193   39.269  1.00 53.36  ? 226 LEU   B HD23 1 
ATOM   8114 N N    . MET   B 1 242 ? 9.561   3.451   37.549  1.00 35.01  ? 227 MET   B N    1 
ATOM   8115 C CA   . MET   B 1 242 ? 10.424  2.298   37.784  1.00 45.93  ? 227 MET   B CA   1 
ATOM   8116 C C    . MET   B 1 242 ? 11.889  2.593   37.503  1.00 44.07  ? 227 MET   B C    1 
ATOM   8117 O O    . MET   B 1 242 ? 12.762  1.888   38.021  1.00 53.27  ? 227 MET   B O    1 
ATOM   8118 C CB   . MET   B 1 242 ? 10.006  1.120   36.907  1.00 43.15  ? 227 MET   B CB   1 
ATOM   8119 C CG   . MET   B 1 242 ? 8.688   0.515   37.270  1.00 52.90  ? 227 MET   B CG   1 
ATOM   8120 S SD   . MET   B 1 242 ? 8.314   -0.903  36.218  1.00 56.29  ? 227 MET   B SD   1 
ATOM   8121 C CE   . MET   B 1 242 ? 6.794   -1.467  36.973  1.00 53.84  ? 227 MET   B CE   1 
ATOM   8122 H H    . MET   B 1 242 ? 8.957   3.329   36.949  1.00 42.01  ? 227 MET   B H    1 
ATOM   8123 H HA   . MET   B 1 242 ? 10.313  2.050   38.716  1.00 55.11  ? 227 MET   B HA   1 
ATOM   8124 H HB2  . MET   B 1 242 ? 9.946   1.425   35.989  1.00 51.78  ? 227 MET   B HB2  1 
ATOM   8125 H HB3  . MET   B 1 242 ? 10.678  0.425   36.983  1.00 51.78  ? 227 MET   B HB3  1 
ATOM   8126 H HG2  . MET   B 1 242 ? 8.713   0.215   38.192  1.00 63.48  ? 227 MET   B HG2  1 
ATOM   8127 H HG3  . MET   B 1 242 ? 7.987   1.176   37.155  1.00 63.48  ? 227 MET   B HG3  1 
ATOM   8128 H HE1  . MET   B 1 242 ? 6.479   -2.252  36.499  1.00 64.61  ? 227 MET   B HE1  1 
ATOM   8129 H HE2  . MET   B 1 242 ? 6.966   -1.688  37.902  1.00 64.61  ? 227 MET   B HE2  1 
ATOM   8130 H HE3  . MET   B 1 242 ? 6.133   -0.760  36.918  1.00 64.61  ? 227 MET   B HE3  1 
ATOM   8131 N N    . THR   B 1 243 ? 12.169  3.588   36.661  1.00 48.44  ? 228 THR   B N    1 
ATOM   8132 C CA   . THR   B 1 243 ? 13.536  3.931   36.292  1.00 54.82  ? 228 THR   B CA   1 
ATOM   8133 C C    . THR   B 1 243 ? 14.221  4.782   37.353  1.00 61.18  ? 228 THR   B C    1 
ATOM   8134 O O    . THR   B 1 243 ? 15.449  4.733   37.480  1.00 67.46  ? 228 THR   B O    1 
ATOM   8135 C CB   . THR   B 1 243 ? 13.533  4.687   34.959  1.00 53.74  ? 228 THR   B CB   1 
ATOM   8136 O OG1  . THR   B 1 243 ? 12.752  3.961   34.004  1.00 46.92  ? 228 THR   B OG1  1 
ATOM   8137 C CG2  . THR   B 1 243 ? 14.950  4.887   34.434  1.00 66.84  ? 228 THR   B CG2  1 
ATOM   8138 H H    . THR   B 1 243 ? 11.576  4.086   36.286  1.00 58.13  ? 228 THR   B H    1 
ATOM   8139 H HA   . THR   B 1 243 ? 14.046  3.112   36.188  1.00 65.79  ? 228 THR   B HA   1 
ATOM   8140 H HB   . THR   B 1 243 ? 13.146  5.566   35.089  1.00 64.49  ? 228 THR   B HB   1 
ATOM   8141 H HG1  . THR   B 1 243 ? 11.949  3.937   34.247  1.00 56.31  ? 228 THR   B HG1  1 
ATOM   8142 H HG21 . THR   B 1 243 ? 14.923  5.277   33.546  1.00 80.20  ? 228 THR   B HG21 1 
ATOM   8143 H HG22 . THR   B 1 243 ? 15.442  5.481   35.023  1.00 80.20  ? 228 THR   B HG22 1 
ATOM   8144 H HG23 . THR   B 1 243 ? 15.412  4.035   34.389  1.00 80.20  ? 228 THR   B HG23 1 
ATOM   8145 N N    . LYS   B 1 244 ? 13.452  5.575   38.103  1.00 59.44  ? 229 LYS   B N    1 
ATOM   8146 C CA   . LYS   B 1 244 ? 14.024  6.462   39.106  1.00 50.62  ? 229 LYS   B CA   1 
ATOM   8147 C C    . LYS   B 1 244 ? 14.949  5.694   40.042  1.00 54.94  ? 229 LYS   B C    1 
ATOM   8148 O O    . LYS   B 1 244 ? 14.763  4.499   40.291  1.00 53.02  ? 229 LYS   B O    1 
ATOM   8149 C CB   . LYS   B 1 244 ? 12.911  7.135   39.913  1.00 54.64  ? 229 LYS   B CB   1 
ATOM   8150 C CG   . LYS   B 1 244 ? 12.624  8.588   39.531  1.00 58.08  ? 229 LYS   B CG   1 
ATOM   8151 C CD   . LYS   B 1 244 ? 12.061  8.712   38.125  1.00 55.13  ? 229 LYS   B CD   1 
ATOM   8152 C CE   . LYS   B 1 244 ? 11.579  10.133  37.849  1.00 70.92  ? 229 LYS   B CE   1 
ATOM   8153 N NZ   . LYS   B 1 244 ? 11.180  10.343  36.427  1.00 68.23  ? 229 LYS   B NZ   1 
ATOM   8154 H H    . LYS   B 1 244 ? 12.595  5.615   38.047  1.00 71.33  ? 229 LYS   B H    1 
ATOM   8155 H HA   . LYS   B 1 244 ? 14.544  7.152   38.664  1.00 60.75  ? 229 LYS   B HA   1 
ATOM   8156 H HB2  . LYS   B 1 244 ? 12.091  6.633   39.784  1.00 65.57  ? 229 LYS   B HB2  1 
ATOM   8157 H HB3  . LYS   B 1 244 ? 13.162  7.126   40.850  1.00 65.57  ? 229 LYS   B HB3  1 
ATOM   8158 H HG2  . LYS   B 1 244 ? 11.975  8.958   40.149  1.00 69.70  ? 229 LYS   B HG2  1 
ATOM   8159 H HG3  . LYS   B 1 244 ? 13.449  9.097   39.571  1.00 69.70  ? 229 LYS   B HG3  1 
ATOM   8160 H HD2  . LYS   B 1 244 ? 12.751  8.491   37.480  1.00 66.15  ? 229 LYS   B HD2  1 
ATOM   8161 H HD3  . LYS   B 1 244 ? 11.308  8.108   38.025  1.00 66.15  ? 229 LYS   B HD3  1 
ATOM   8162 H HE2  . LYS   B 1 244 ? 10.808  10.319  38.407  1.00 85.11  ? 229 LYS   B HE2  1 
ATOM   8163 H HE3  . LYS   B 1 244 ? 12.295  10.754  38.054  1.00 85.11  ? 229 LYS   B HE3  1 
ATOM   8164 H HZ1  . LYS   B 1 244 ? 10.775  11.131  36.337  1.00 81.88  ? 229 LYS   B HZ1  1 
ATOM   8165 H HZ2  . LYS   B 1 244 ? 11.899  10.326  35.903  1.00 81.88  ? 229 LYS   B HZ2  1 
ATOM   8166 H HZ3  . LYS   B 1 244 ? 10.620  9.700   36.169  1.00 81.88  ? 229 LYS   B HZ3  1 
ATOM   8167 N N    . SER   B 1 245 ? 15.957  6.395   40.567  1.00 53.54  ? 230 SER   B N    1 
ATOM   8168 C CA   . SER   B 1 245 ? 16.917  5.753   41.457  1.00 52.55  ? 230 SER   B CA   1 
ATOM   8169 C C    . SER   B 1 245 ? 16.254  5.293   42.748  1.00 46.45  ? 230 SER   B C    1 
ATOM   8170 O O    . SER   B 1 245 ? 16.547  4.200   43.249  1.00 53.55  ? 230 SER   B O    1 
ATOM   8171 C CB   . SER   B 1 245 ? 18.064  6.712   41.767  1.00 46.73  ? 230 SER   B CB   1 
ATOM   8172 O OG   . SER   B 1 245 ? 18.441  7.436   40.610  1.00 70.66  ? 230 SER   B OG   1 
ATOM   8173 H H    . SER   B 1 245 ? 16.103  7.230   40.424  1.00 64.24  ? 230 SER   B H    1 
ATOM   8174 H HA   . SER   B 1 245 ? 17.283  4.974   41.009  1.00 63.06  ? 230 SER   B HA   1 
ATOM   8175 H HB2  . SER   B 1 245 ? 17.776  7.338   42.451  1.00 56.07  ? 230 SER   B HB2  1 
ATOM   8176 H HB3  . SER   B 1 245 ? 18.826  6.202   42.083  1.00 56.07  ? 230 SER   B HB3  1 
ATOM   8177 H HG   . SER   B 1 245 ? 19.052  7.981   40.799  1.00 84.79  ? 230 SER   B HG   1 
ATOM   8178 N N    . GLY   B 1 246 ? 15.367  6.114   43.305  1.00 47.94  ? 231 GLY   B N    1 
ATOM   8179 C CA   . GLY   B 1 246 ? 14.715  5.790   44.557  1.00 48.86  ? 231 GLY   B CA   1 
ATOM   8180 C C    . GLY   B 1 246 ? 13.373  5.107   44.386  1.00 49.45  ? 231 GLY   B C    1 
ATOM   8181 O O    . GLY   B 1 246 ? 12.479  5.275   45.221  1.00 49.77  ? 231 GLY   B O    1 
ATOM   8182 H H    . GLY   B 1 246 ? 15.127  6.869   42.971  1.00 57.53  ? 231 GLY   B H    1 
ATOM   8183 H HA2  . GLY   B 1 246 ? 15.290  5.199   45.068  1.00 58.63  ? 231 GLY   B HA2  1 
ATOM   8184 H HA3  . GLY   B 1 246 ? 14.575  6.607   45.061  1.00 58.63  ? 231 GLY   B HA3  1 
ATOM   8185 N N    . TYR   B 1 247 ? 13.213  4.335   43.314  1.00 50.10  ? 232 TYR   B N    1 
ATOM   8186 C CA   . TYR   B 1 247 ? 11.981  3.580   43.131  1.00 46.95  ? 232 TYR   B CA   1 
ATOM   8187 C C    . TYR   B 1 247 ? 11.762  2.663   44.324  1.00 40.67  ? 232 TYR   B C    1 
ATOM   8188 O O    . TYR   B 1 247 ? 12.684  1.973   44.767  1.00 46.27  ? 232 TYR   B O    1 
ATOM   8189 C CB   . TYR   B 1 247 ? 12.038  2.768   41.842  1.00 41.07  ? 232 TYR   B CB   1 
ATOM   8190 C CG   . TYR   B 1 247 ? 10.830  1.885   41.627  1.00 42.87  ? 232 TYR   B CG   1 
ATOM   8191 C CD1  . TYR   B 1 247 ? 9.563   2.432   41.548  1.00 43.38  ? 232 TYR   B CD1  1 
ATOM   8192 C CD2  . TYR   B 1 247 ? 10.957  0.506   41.487  1.00 45.89  ? 232 TYR   B CD2  1 
ATOM   8193 C CE1  . TYR   B 1 247 ? 8.456   1.646   41.348  1.00 40.52  ? 232 TYR   B CE1  1 
ATOM   8194 C CE2  . TYR   B 1 247 ? 9.839   -0.296  41.284  1.00 43.84  ? 232 TYR   B CE2  1 
ATOM   8195 C CZ   . TYR   B 1 247 ? 8.594   0.291   41.216  1.00 43.07  ? 232 TYR   B CZ   1 
ATOM   8196 O OH   . TYR   B 1 247 ? 7.468   -0.465  41.016  1.00 52.27  ? 232 TYR   B OH   1 
ATOM   8197 H H    . TYR   B 1 247 ? 13.794  4.233   42.689  1.00 60.12  ? 232 TYR   B H    1 
ATOM   8198 H HA   . TYR   B 1 247 ? 11.232  4.193   43.061  1.00 56.34  ? 232 TYR   B HA   1 
ATOM   8199 H HB2  . TYR   B 1 247 ? 12.097  3.378   41.091  1.00 49.29  ? 232 TYR   B HB2  1 
ATOM   8200 H HB3  . TYR   B 1 247 ? 12.822  2.197   41.868  1.00 49.29  ? 232 TYR   B HB3  1 
ATOM   8201 H HD1  . TYR   B 1 247 ? 9.459   3.352   41.633  1.00 52.06  ? 232 TYR   B HD1  1 
ATOM   8202 H HD2  . TYR   B 1 247 ? 11.800  0.116   41.529  1.00 55.07  ? 232 TYR   B HD2  1 
ATOM   8203 H HE1  . TYR   B 1 247 ? 7.612   2.034   41.301  1.00 48.62  ? 232 TYR   B HE1  1 
ATOM   8204 H HE2  . TYR   B 1 247 ? 9.931   -1.217  41.196  1.00 52.61  ? 232 TYR   B HE2  1 
ATOM   8205 H HH   . TYR   B 1 247 ? 7.674   -1.277  40.950  1.00 62.72  ? 232 TYR   B HH   1 
ATOM   8206 N N    . GLN   B 1 248 ? 10.540  2.673   44.856  1.00 48.70  ? 233 GLN   B N    1 
ATOM   8207 C CA   . GLN   B 1 248 ? 10.170  1.810   45.968  1.00 48.64  ? 233 GLN   B CA   1 
ATOM   8208 C C    . GLN   B 1 248 ? 9.337   0.658   45.438  1.00 49.53  ? 233 GLN   B C    1 
ATOM   8209 O O    . GLN   B 1 248 ? 8.276   0.905   44.842  1.00 50.46  ? 233 GLN   B O    1 
ATOM   8210 C CB   . GLN   B 1 248 ? 9.378   2.585   47.013  1.00 46.79  ? 233 GLN   B CB   1 
ATOM   8211 C CG   . GLN   B 1 248 ? 10.122  3.754   47.616  1.00 63.19  ? 233 GLN   B CG   1 
ATOM   8212 C CD   . GLN   B 1 248 ? 11.083  3.333   48.704  1.00 70.51  ? 233 GLN   B CD   1 
ATOM   8213 O OE1  . GLN   B 1 248 ? 12.274  3.135   48.453  1.00 73.14  ? 233 GLN   B OE1  1 
ATOM   8214 N NE2  . GLN   B 1 248 ? 10.573  3.202   49.928  1.00 71.85  ? 233 GLN   B NE2  1 
ATOM   8215 H H    . GLN   B 1 248 ? 9.901   3.180   44.584  1.00 58.45  ? 233 GLN   B H    1 
ATOM   8216 H HA   . GLN   B 1 248 ? 10.970  1.460   46.390  1.00 58.37  ? 233 GLN   B HA   1 
ATOM   8217 H HB2  . GLN   B 1 248 ? 8.573   2.932   46.597  1.00 56.15  ? 233 GLN   B HB2  1 
ATOM   8218 H HB3  . GLN   B 1 248 ? 9.144   1.981   47.735  1.00 56.15  ? 233 GLN   B HB3  1 
ATOM   8219 H HG2  . GLN   B 1 248 ? 10.632  4.197   46.920  1.00 75.83  ? 233 GLN   B HG2  1 
ATOM   8220 H HG3  . GLN   B 1 248 ? 9.481   4.371   48.003  1.00 75.83  ? 233 GLN   B HG3  1 
ATOM   8221 H HE21 . GLN   B 1 248 ? 9.738   3.354   50.064  1.00 86.22  ? 233 GLN   B HE21 1 
ATOM   8222 H HE22 . GLN   B 1 248 ? 11.079  2.964   50.581  1.00 86.22  ? 233 GLN   B HE22 1 
ATOM   8223 N N    . PRO   B 1 249 ? 9.763   -0.592  45.609  1.00 43.99  ? 234 PRO   B N    1 
ATOM   8224 C CA   . PRO   B 1 249 ? 8.952   -1.705  45.115  1.00 43.79  ? 234 PRO   B CA   1 
ATOM   8225 C C    . PRO   B 1 249 ? 7.590   -1.712  45.765  1.00 37.59  ? 234 PRO   B C    1 
ATOM   8226 O O    . PRO   B 1 249 ? 7.428   -1.284  46.922  1.00 38.82  ? 234 PRO   B O    1 
ATOM   8227 C CB   . PRO   B 1 249 ? 9.776   -2.941  45.517  1.00 34.93  ? 234 PRO   B CB   1 
ATOM   8228 C CG   . PRO   B 1 249 ? 11.164  -2.450  45.642  1.00 42.32  ? 234 PRO   B CG   1 
ATOM   8229 C CD   . PRO   B 1 249 ? 11.060  -1.039  46.142  1.00 40.41  ? 234 PRO   B CD   1 
ATOM   8230 H HA   . PRO   B 1 249 ? 8.855   -1.663  44.151  1.00 52.55  ? 234 PRO   B HA   1 
ATOM   8231 H HB2  . PRO   B 1 249 ? 9.454   -3.291  46.362  1.00 41.91  ? 234 PRO   B HB2  1 
ATOM   8232 H HB3  . PRO   B 1 249 ? 9.708   -3.620  44.828  1.00 41.91  ? 234 PRO   B HB3  1 
ATOM   8233 H HG2  . PRO   B 1 249 ? 11.650  -3.003  46.274  1.00 50.78  ? 234 PRO   B HG2  1 
ATOM   8234 H HG3  . PRO   B 1 249 ? 11.599  -2.476  44.775  1.00 50.78  ? 234 PRO   B HG3  1 
ATOM   8235 H HD2  . PRO   B 1 249 ? 11.062  -1.014  47.112  1.00 48.50  ? 234 PRO   B HD2  1 
ATOM   8236 H HD3  . PRO   B 1 249 ? 11.783  -0.494  45.795  1.00 48.50  ? 234 PRO   B HD3  1 
ATOM   8237 N N    . PRO   B 1 250 ? 6.571   -2.213  45.067  1.00 45.27  ? 235 PRO   B N    1 
ATOM   8238 C CA   . PRO   B 1 250 ? 5.228   -2.245  45.650  1.00 42.27  ? 235 PRO   B CA   1 
ATOM   8239 C C    . PRO   B 1 250 ? 5.165   -3.132  46.886  1.00 42.51  ? 235 PRO   B C    1 
ATOM   8240 O O    . PRO   B 1 250 ? 6.092   -3.871  47.233  1.00 33.68  ? 235 PRO   B O    1 
ATOM   8241 C CB   . PRO   B 1 250 ? 4.350   -2.807  44.523  1.00 47.01  ? 235 PRO   B CB   1 
ATOM   8242 C CG   . PRO   B 1 250 ? 5.158   -2.661  43.280  1.00 44.58  ? 235 PRO   B CG   1 
ATOM   8243 C CD   . PRO   B 1 250 ? 6.586   -2.761  43.699  1.00 38.49  ? 235 PRO   B CD   1 
ATOM   8244 H HA   . PRO   B 1 250 ? 4.943   -1.345  45.877  1.00 50.72  ? 235 PRO   B HA   1 
ATOM   8245 H HB2  . PRO   B 1 250 ? 4.150   -3.741  44.697  1.00 56.41  ? 235 PRO   B HB2  1 
ATOM   8246 H HB3  . PRO   B 1 250 ? 3.527   -2.298  44.462  1.00 56.41  ? 235 PRO   B HB3  1 
ATOM   8247 H HG2  . PRO   B 1 250 ? 4.933   -3.371  42.658  1.00 53.50  ? 235 PRO   B HG2  1 
ATOM   8248 H HG3  . PRO   B 1 250 ? 4.980   -1.797  42.875  1.00 53.50  ? 235 PRO   B HG3  1 
ATOM   8249 H HD2  . PRO   B 1 250 ? 6.882   -3.685  43.700  1.00 46.19  ? 235 PRO   B HD2  1 
ATOM   8250 H HD3  . PRO   B 1 250 ? 7.155   -2.231  43.120  1.00 46.19  ? 235 PRO   B HD3  1 
ATOM   8251 N N    . ARG   B 1 251 ? 4.024   -3.035  47.563  1.00 37.93  ? 236 ARG   B N    1 
ATOM   8252 C CA   . ARG   B 1 251 ? 3.718   -3.854  48.724  1.00 35.23  ? 236 ARG   B CA   1 
ATOM   8253 C C    . ARG   B 1 251 ? 2.220   -4.117  48.732  1.00 42.71  ? 236 ARG   B C    1 
ATOM   8254 O O    . ARG   B 1 251 ? 1.444   -3.433  48.057  1.00 37.15  ? 236 ARG   B O    1 
ATOM   8255 C CB   . ARG   B 1 251 ? 4.141   -3.180  50.033  1.00 44.27  ? 236 ARG   B CB   1 
ATOM   8256 C CG   . ARG   B 1 251 ? 5.637   -2.990  50.198  1.00 47.09  ? 236 ARG   B CG   1 
ATOM   8257 C CD   . ARG   B 1 251 ? 5.974   -2.449  51.585  1.00 60.24  ? 236 ARG   B CD   1 
ATOM   8258 N NE   . ARG   B 1 251 ? 5.378   -1.140  51.831  1.00 65.40  ? 236 ARG   B NE   1 
ATOM   8259 C CZ   . ARG   B 1 251 ? 5.291   -0.564  53.025  1.00 72.02  ? 236 ARG   B CZ   1 
ATOM   8260 N NH1  . ARG   B 1 251 ? 5.754   -1.156  54.116  1.00 70.16  ? 236 ARG   B NH1  1 
ATOM   8261 N NH2  . ARG   B 1 251 ? 4.717   0.632   53.127  1.00 70.26  ? 236 ARG   B NH2  1 
ATOM   8262 H H    . ARG   B 1 251 ? 3.395   -2.485  47.362  1.00 45.52  ? 236 ARG   B H    1 
ATOM   8263 H HA   . ARG   B 1 251 ? 4.193   -4.697  48.657  1.00 42.28  ? 236 ARG   B HA   1 
ATOM   8264 H HB2  . ARG   B 1 251 ? 3.729   -2.303  50.074  1.00 53.12  ? 236 ARG   B HB2  1 
ATOM   8265 H HB3  . ARG   B 1 251 ? 3.833   -3.727  50.773  1.00 53.12  ? 236 ARG   B HB3  1 
ATOM   8266 H HG2  . ARG   B 1 251 ? 6.085   -3.843  50.084  1.00 56.50  ? 236 ARG   B HG2  1 
ATOM   8267 H HG3  . ARG   B 1 251 ? 5.957   -2.357  49.536  1.00 56.50  ? 236 ARG   B HG3  1 
ATOM   8268 H HD2  . ARG   B 1 251 ? 5.638   -3.064  52.256  1.00 72.29  ? 236 ARG   B HD2  1 
ATOM   8269 H HD3  . ARG   B 1 251 ? 6.937   -2.362  51.667  1.00 72.29  ? 236 ARG   B HD3  1 
ATOM   8270 H HE   . ARG   B 1 251 ? 5.061   -0.712  51.156  1.00 78.48  ? 236 ARG   B HE   1 
ATOM   8271 H HH11 . ARG   B 1 251 ? 6.122   -1.932  54.061  1.00 84.19  ? 236 ARG   B HH11 1 
ATOM   8272 H HH12 . ARG   B 1 251 ? 5.688   -0.765  54.878  1.00 84.19  ? 236 ARG   B HH12 1 
ATOM   8273 H HH21 . ARG   B 1 251 ? 4.408   1.022   52.426  1.00 84.32  ? 236 ARG   B HH21 1 
ATOM   8274 H HH22 . ARG   B 1 251 ? 4.656   1.015   53.895  1.00 84.32  ? 236 ARG   B HH22 1 
ATOM   8275 N N    . LEU   B 1 252 ? 1.821   -5.124  49.504  1.00 46.03  ? 237 LEU   B N    1 
ATOM   8276 C CA   . LEU   B 1 252 ? 0.401   -5.380  49.703  1.00 42.73  ? 237 LEU   B CA   1 
ATOM   8277 C C    . LEU   B 1 252 ? -0.244  -4.182  50.391  1.00 33.96  ? 237 LEU   B C    1 
ATOM   8278 O O    . LEU   B 1 252 ? 0.350   -3.562  51.275  1.00 37.03  ? 237 LEU   B O    1 
ATOM   8279 C CB   . LEU   B 1 252 ? 0.204   -6.651  50.528  1.00 32.95  ? 237 LEU   B CB   1 
ATOM   8280 C CG   . LEU   B 1 252 ? 0.559   -7.947  49.800  1.00 31.77  ? 237 LEU   B CG   1 
ATOM   8281 C CD1  . LEU   B 1 252 ? 0.771   -9.074  50.778  1.00 38.52  ? 237 LEU   B CD1  1 
ATOM   8282 C CD2  . LEU   B 1 252 ? -0.538  -8.306  48.798  1.00 33.43  ? 237 LEU   B CD2  1 
ATOM   8283 H H    . LEU   B 1 252 ? 2.345   -5.666  49.918  1.00 55.23  ? 237 LEU   B H    1 
ATOM   8284 H HA   . LEU   B 1 252 ? -0.037  -5.517  48.848  1.00 51.27  ? 237 LEU   B HA   1 
ATOM   8285 H HB2  . LEU   B 1 252 ? 0.765   -6.595  51.318  1.00 39.54  ? 237 LEU   B HB2  1 
ATOM   8286 H HB3  . LEU   B 1 252 ? -0.729  -6.707  50.788  1.00 39.54  ? 237 LEU   B HB3  1 
ATOM   8287 H HG   . LEU   B 1 252 ? 1.389   -7.817  49.315  1.00 38.12  ? 237 LEU   B HG   1 
ATOM   8288 H HD11 . LEU   B 1 252 ? 1.039   -9.869  50.291  1.00 46.22  ? 237 LEU   B HD11 1 
ATOM   8289 H HD12 . LEU   B 1 252 ? 1.467   -8.821  51.405  1.00 46.22  ? 237 LEU   B HD12 1 
ATOM   8290 H HD13 . LEU   B 1 252 ? -0.058  -9.241  51.253  1.00 46.22  ? 237 LEU   B HD13 1 
ATOM   8291 H HD21 . LEU   B 1 252 ? -0.315  -9.150  48.375  1.00 40.12  ? 237 LEU   B HD21 1 
ATOM   8292 H HD22 . LEU   B 1 252 ? -1.382  -8.384  49.269  1.00 40.12  ? 237 LEU   B HD22 1 
ATOM   8293 H HD23 . LEU   B 1 252 ? -0.595  -7.606  48.129  1.00 40.12  ? 237 LEU   B HD23 1 
ATOM   8294 N N    . LYS   B 1 253 ? -1.472  -3.862  49.971  1.00 36.61  ? 238 LYS   B N    1 
ATOM   8295 C CA   . LYS   B 1 253 ? -2.169  -2.684  50.486  1.00 40.17  ? 238 LYS   B CA   1 
ATOM   8296 C C    . LYS   B 1 253 ? -2.588  -2.870  51.945  1.00 49.46  ? 238 LYS   B C    1 
ATOM   8297 O O    . LYS   B 1 253 ? -2.271  -2.031  52.800  1.00 49.97  ? 238 LYS   B O    1 
ATOM   8298 C CB   . LYS   B 1 253 ? -3.385  -2.389  49.598  1.00 42.76  ? 238 LYS   B CB   1 
ATOM   8299 C CG   . LYS   B 1 253 ? -4.139  -1.103  49.921  1.00 44.73  ? 238 LYS   B CG   1 
ATOM   8300 C CD   . LYS   B 1 253 ? -3.694  0.031   49.018  1.00 65.76  ? 238 LYS   B CD   1 
ATOM   8301 C CE   . LYS   B 1 253 ? -4.472  1.321   49.292  1.00 67.89  ? 238 LYS   B CE   1 
ATOM   8302 N NZ   . LYS   B 1 253 ? -4.045  2.435   48.381  1.00 72.05  ? 238 LYS   B NZ   1 
ATOM   8303 H H    . LYS   B 1 253 ? -1.922  -4.309  49.391  1.00 43.93  ? 238 LYS   B H    1 
ATOM   8304 H HA   . LYS   B 1 253 ? -1.570  -1.922  50.454  1.00 48.20  ? 238 LYS   B HA   1 
ATOM   8305 H HB2  . LYS   B 1 253 ? -3.082  -2.323  48.679  1.00 51.31  ? 238 LYS   B HB2  1 
ATOM   8306 H HB3  . LYS   B 1 253 ? -4.014  -3.122  49.689  1.00 51.31  ? 238 LYS   B HB3  1 
ATOM   8307 H HG2  . LYS   B 1 253 ? -5.089  -1.244  49.790  1.00 53.68  ? 238 LYS   B HG2  1 
ATOM   8308 H HG3  . LYS   B 1 253 ? -3.965  -0.849  50.841  1.00 53.68  ? 238 LYS   B HG3  1 
ATOM   8309 H HD2  . LYS   B 1 253 ? -2.752  0.208   49.168  1.00 78.91  ? 238 LYS   B HD2  1 
ATOM   8310 H HD3  . LYS   B 1 253 ? -3.841  -0.221  48.093  1.00 78.91  ? 238 LYS   B HD3  1 
ATOM   8311 H HE2  . LYS   B 1 253 ? -5.418  1.159   49.151  1.00 81.47  ? 238 LYS   B HE2  1 
ATOM   8312 H HE3  . LYS   B 1 253 ? -4.315  1.601   50.207  1.00 81.47  ? 238 LYS   B HE3  1 
ATOM   8313 H HZ1  . LYS   B 1 253 ? -4.516  3.169   48.557  1.00 86.45  ? 238 LYS   B HZ1  1 
ATOM   8314 H HZ2  . LYS   B 1 253 ? -3.181  2.610   48.499  1.00 86.45  ? 238 LYS   B HZ2  1 
ATOM   8315 H HZ3  . LYS   B 1 253 ? -4.179  2.202   47.532  1.00 86.45  ? 238 LYS   B HZ3  1 
ATOM   8316 N N    . GLU   B 1 254 ? -3.311  -3.955  52.249  1.00 41.15  ? 239 GLU   B N    1 
ATOM   8317 C CA   . GLU   B 1 254 ? -3.811  -4.221  53.598  1.00 38.81  ? 239 GLU   B CA   1 
ATOM   8318 C C    . GLU   B 1 254 ? -2.780  -5.022  54.386  1.00 48.08  ? 239 GLU   B C    1 
ATOM   8319 O O    . GLU   B 1 254 ? -2.582  -6.214  54.130  1.00 56.07  ? 239 GLU   B O    1 
ATOM   8320 C CB   . GLU   B 1 254 ? -5.129  -4.990  53.554  1.00 53.24  ? 239 GLU   B CB   1 
ATOM   8321 C CG   . GLU   B 1 254 ? -6.292  -4.222  52.963  1.00 56.49  ? 239 GLU   B CG   1 
ATOM   8322 C CD   . GLU   B 1 254 ? -7.625  -4.836  53.321  1.00 57.49  ? 239 GLU   B CD   1 
ATOM   8323 O OE1  . GLU   B 1 254 ? -7.980  -4.825  54.519  1.00 55.31  ? 239 GLU   B OE1  1 
ATOM   8324 O OE2  . GLU   B 1 254 ? -8.309  -5.341  52.408  1.00 64.34  ? 239 GLU   B OE2  1 
ATOM   8325 H H    . GLU   B 1 254 ? -3.528  -4.560  51.678  1.00 49.38  ? 239 GLU   B H    1 
ATOM   8326 H HA   . GLU   B 1 254 ? -3.947  -3.367  54.036  1.00 46.57  ? 239 GLU   B HA   1 
ATOM   8327 H HB2  . GLU   B 1 254 ? -5.003  -5.788  53.017  1.00 63.89  ? 239 GLU   B HB2  1 
ATOM   8328 H HB3  . GLU   B 1 254 ? -5.372  -5.236  54.460  1.00 63.89  ? 239 GLU   B HB3  1 
ATOM   8329 H HG2  . GLU   B 1 254 ? -6.278  -3.313  53.301  1.00 67.78  ? 239 GLU   B HG2  1 
ATOM   8330 H HG3  . GLU   B 1 254 ? -6.212  -4.218  51.996  1.00 67.78  ? 239 GLU   B HG3  1 
ATOM   8331 N N    . LYS   B 1 255 ? -2.162  -4.389  55.378  1.00 50.57  ? 240 LYS   B N    1 
ATOM   8332 C CA   . LYS   B 1 255 ? -1.118  -5.061  56.140  1.00 49.95  ? 240 LYS   B CA   1 
ATOM   8333 C C    . LYS   B 1 255 ? -1.682  -6.224  56.949  1.00 49.34  ? 240 LYS   B C    1 
ATOM   8334 O O    . LYS   B 1 255 ? -1.217  -7.361  56.831  1.00 48.76  ? 240 LYS   B O    1 
ATOM   8335 C CB   . LYS   B 1 255 ? -0.418  -4.057  57.056  1.00 54.60  ? 240 LYS   B CB   1 
ATOM   8336 C CG   . LYS   B 1 255 ? 1.086   -4.249  57.163  1.00 63.41  ? 240 LYS   B CG   1 
ATOM   8337 C CD   . LYS   B 1 255 ? 1.739   -3.078  57.888  1.00 70.71  ? 240 LYS   B CD   1 
ATOM   8338 C CE   . LYS   B 1 255 ? 3.239   -3.007  57.609  1.00 78.05  ? 240 LYS   B CE   1 
ATOM   8339 N NZ   . LYS   B 1 255 ? 3.991   -4.160  58.195  1.00 79.70  ? 240 LYS   B NZ   1 
ATOM   8340 H H    . LYS   B 1 255 ? -2.327  -3.583  55.627  1.00 60.69  ? 240 LYS   B H    1 
ATOM   8341 H HA   . LYS   B 1 255 ? -0.461  -5.420  55.522  1.00 59.94  ? 240 LYS   B HA   1 
ATOM   8342 H HB2  . LYS   B 1 255 ? -0.577  -3.163  56.713  1.00 65.52  ? 240 LYS   B HB2  1 
ATOM   8343 H HB3  . LYS   B 1 255 ? -0.790  -4.141  57.948  1.00 65.52  ? 240 LYS   B HB3  1 
ATOM   8344 H HG2  . LYS   B 1 255 ? 1.273   -5.061  57.661  1.00 76.09  ? 240 LYS   B HG2  1 
ATOM   8345 H HG3  . LYS   B 1 255 ? 1.468   -4.311  56.273  1.00 76.09  ? 240 LYS   B HG3  1 
ATOM   8346 H HD2  . LYS   B 1 255 ? 1.334   -2.249  57.587  1.00 84.85  ? 240 LYS   B HD2  1 
ATOM   8347 H HD3  . LYS   B 1 255 ? 1.612   -3.182  58.844  1.00 84.85  ? 240 LYS   B HD3  1 
ATOM   8348 H HE2  . LYS   B 1 255 ? 3.384   -3.012  56.650  1.00 93.66  ? 240 LYS   B HE2  1 
ATOM   8349 H HE3  . LYS   B 1 255 ? 3.594   -2.191  57.994  1.00 93.66  ? 240 LYS   B HE3  1 
ATOM   8350 H HZ1  . LYS   B 1 255 ? 4.858   -4.084  58.010  1.00 95.64  ? 240 LYS   B HZ1  1 
ATOM   8351 H HZ2  . LYS   B 1 255 ? 3.884   -4.176  59.079  1.00 95.64  ? 240 LYS   B HZ2  1 
ATOM   8352 H HZ3  . LYS   B 1 255 ? 3.689   -4.925  57.855  1.00 95.64  ? 240 LYS   B HZ3  1 
ATOM   8353 N N    . GLY   B 1 256 ? -2.701  -5.951  57.771  1.00 43.92  ? 241 GLY   B N    1 
ATOM   8354 C CA   . GLY   B 1 256 ? -3.205  -6.913  58.734  1.00 46.17  ? 241 GLY   B CA   1 
ATOM   8355 C C    . GLY   B 1 256 ? -3.929  -8.100  58.143  1.00 47.45  ? 241 GLY   B C    1 
ATOM   8356 O O    . GLY   B 1 256 ? -4.139  -9.092  58.847  1.00 46.30  ? 241 GLY   B O    1 
ATOM   8357 H H    . GLY   B 1 256 ? -3.120  -5.200  57.786  1.00 52.70  ? 241 GLY   B H    1 
ATOM   8358 H HA2  . GLY   B 1 256 ? -2.458  -7.253  59.251  1.00 55.41  ? 241 GLY   B HA2  1 
ATOM   8359 H HA3  . GLY   B 1 256 ? -3.821  -6.460  59.330  1.00 55.41  ? 241 GLY   B HA3  1 
ATOM   8360 N N    . LYS   B 1 257 ? -4.322  -8.022  56.868  1.00 41.91  ? 242 LYS   B N    1 
ATOM   8361 C CA   . LYS   B 1 257 ? -5.046  -9.115  56.237  1.00 42.48  ? 242 LYS   B CA   1 
ATOM   8362 C C    . LYS   B 1 257 ? -4.146  -10.305 55.935  1.00 49.03  ? 242 LYS   B C    1 
ATOM   8363 O O    . LYS   B 1 257 ? -4.654  -11.409 55.721  1.00 45.75  ? 242 LYS   B O    1 
ATOM   8364 C CB   . LYS   B 1 257 ? -5.697  -8.622  54.941  1.00 44.53  ? 242 LYS   B CB   1 
ATOM   8365 C CG   . LYS   B 1 257 ? -6.617  -9.633  54.282  1.00 53.03  ? 242 LYS   B CG   1 
ATOM   8366 C CD   . LYS   B 1 257 ? -7.295  -9.074  53.031  1.00 46.89  ? 242 LYS   B CD   1 
ATOM   8367 C CE   . LYS   B 1 257 ? -8.219  -10.121 52.401  1.00 49.95  ? 242 LYS   B CE   1 
ATOM   8368 N NZ   . LYS   B 1 257 ? -9.061  -9.565  51.310  1.00 48.15  ? 242 LYS   B NZ   1 
ATOM   8369 H H    . LYS   B 1 257 ? -4.180  -7.348  56.353  1.00 50.29  ? 242 LYS   B H    1 
ATOM   8370 H HA   . LYS   B 1 257 ? -5.746  -9.415  56.838  1.00 50.97  ? 242 LYS   B HA   1 
ATOM   8371 H HB2  . LYS   B 1 257 ? -6.222  -7.831  55.139  1.00 53.43  ? 242 LYS   B HB2  1 
ATOM   8372 H HB3  . LYS   B 1 257 ? -4.996  -8.404  54.306  1.00 53.43  ? 242 LYS   B HB3  1 
ATOM   8373 H HG2  . LYS   B 1 257 ? -6.101  -10.412 54.022  1.00 63.64  ? 242 LYS   B HG2  1 
ATOM   8374 H HG3  . LYS   B 1 257 ? -7.310  -9.890  54.911  1.00 63.64  ? 242 LYS   B HG3  1 
ATOM   8375 H HD2  . LYS   B 1 257 ? -7.826  -8.298  53.269  1.00 56.26  ? 242 LYS   B HD2  1 
ATOM   8376 H HD3  . LYS   B 1 257 ? -6.620  -8.827  52.379  1.00 56.26  ? 242 LYS   B HD3  1 
ATOM   8377 H HE2  . LYS   B 1 257 ? -7.680  -10.835 52.028  1.00 59.94  ? 242 LYS   B HE2  1 
ATOM   8378 H HE3  . LYS   B 1 257 ? -8.810  -10.473 53.085  1.00 59.94  ? 242 LYS   B HE3  1 
ATOM   8379 H HZ1  . LYS   B 1 257 ? -9.585  -10.202 50.976  1.00 57.78  ? 242 LYS   B HZ1  1 
ATOM   8380 H HZ2  . LYS   B 1 257 ? -9.572  -8.907  51.625  1.00 57.78  ? 242 LYS   B HZ2  1 
ATOM   8381 H HZ3  . LYS   B 1 257 ? -8.545  -9.245  50.660  1.00 57.78  ? 242 LYS   B HZ3  1 
ATOM   8382 N N    . TRP   B 1 258 ? -2.831  -10.109 55.913  1.00 42.83  ? 243 TRP   B N    1 
ATOM   8383 C CA   . TRP   B 1 258 ? -1.907  -11.118 55.418  1.00 37.59  ? 243 TRP   B CA   1 
ATOM   8384 C C    . TRP   B 1 258 ? -0.852  -11.428 56.464  1.00 40.02  ? 243 TRP   B C    1 
ATOM   8385 O O    . TRP   B 1 258 ? -0.515  -10.589 57.306  1.00 40.06  ? 243 TRP   B O    1 
ATOM   8386 C CB   . TRP   B 1 258 ? -1.231  -10.644 54.122  1.00 39.52  ? 243 TRP   B CB   1 
ATOM   8387 C CG   . TRP   B 1 258 ? -2.196  -10.092 53.116  1.00 35.06  ? 243 TRP   B CG   1 
ATOM   8388 C CD1  . TRP   B 1 258 ? -2.357  -8.779  52.760  1.00 35.07  ? 243 TRP   B CD1  1 
ATOM   8389 C CD2  . TRP   B 1 258 ? -3.144  -10.837 52.342  1.00 35.82  ? 243 TRP   B CD2  1 
ATOM   8390 N NE1  . TRP   B 1 258 ? -3.341  -8.665  51.811  1.00 34.40  ? 243 TRP   B NE1  1 
ATOM   8391 C CE2  . TRP   B 1 258 ? -3.838  -9.911  51.534  1.00 37.39  ? 243 TRP   B CE2  1 
ATOM   8392 C CE3  . TRP   B 1 258 ? -3.475  -12.195 52.253  1.00 39.02  ? 243 TRP   B CE3  1 
ATOM   8393 C CZ2  . TRP   B 1 258 ? -4.838  -10.300 50.647  1.00 33.40  ? 243 TRP   B CZ2  1 
ATOM   8394 C CZ3  . TRP   B 1 258 ? -4.471  -12.579 51.368  1.00 33.48  ? 243 TRP   B CZ3  1 
ATOM   8395 C CH2  . TRP   B 1 258 ? -5.138  -11.630 50.574  1.00 38.48  ? 243 TRP   B CH2  1 
ATOM   8396 H H    . TRP   B 1 258 ? -2.447  -9.389  56.184  1.00 51.40  ? 243 TRP   B H    1 
ATOM   8397 H HA   . TRP   B 1 258 ? -2.389  -11.941 55.242  1.00 45.10  ? 243 TRP   B HA   1 
ATOM   8398 H HB2  . TRP   B 1 258 ? -0.594  -9.944  54.338  1.00 47.42  ? 243 TRP   B HB2  1 
ATOM   8399 H HB3  . TRP   B 1 258 ? -0.773  -11.395 53.714  1.00 47.42  ? 243 TRP   B HB3  1 
ATOM   8400 H HD1  . TRP   B 1 258 ? -1.870  -8.068  53.111  1.00 42.09  ? 243 TRP   B HD1  1 
ATOM   8401 H HE1  . TRP   B 1 258 ? -3.604  -7.931  51.449  1.00 41.28  ? 243 TRP   B HE1  1 
ATOM   8402 H HE3  . TRP   B 1 258 ? -3.035  -12.826 52.776  1.00 46.83  ? 243 TRP   B HE3  1 
ATOM   8403 H HZ2  . TRP   B 1 258 ? -5.286  -9.676  50.123  1.00 40.08  ? 243 TRP   B HZ2  1 
ATOM   8404 H HZ3  . TRP   B 1 258 ? -4.702  -13.477 51.299  1.00 40.18  ? 243 TRP   B HZ3  1 
ATOM   8405 H HH2  . TRP   B 1 258 ? -5.799  -11.915 49.986  1.00 46.17  ? 243 TRP   B HH2  1 
ATOM   8406 N N    . SER   B 1 259 ? -0.331  -12.649 56.398  1.00 38.62  ? 244 SER   B N    1 
ATOM   8407 C CA   . SER   B 1 259 ? 0.679   -13.097 57.339  1.00 39.89  ? 244 SER   B CA   1 
ATOM   8408 C C    . SER   B 1 259 ? 2.031   -12.471 57.019  1.00 39.26  ? 244 SER   B C    1 
ATOM   8409 O O    . SER   B 1 259 ? 2.267   -11.966 55.917  1.00 38.52  ? 244 SER   B O    1 
ATOM   8410 C CB   . SER   B 1 259 ? 0.825   -14.614 57.303  1.00 39.40  ? 244 SER   B CB   1 
ATOM   8411 O OG   . SER   B 1 259 ? 1.687   -14.993 56.240  1.00 40.99  ? 244 SER   B OG   1 
ATOM   8412 H H    . SER   B 1 259 ? -0.549  -13.240 55.812  1.00 46.35  ? 244 SER   B H    1 
ATOM   8413 H HA   . SER   B 1 259 ? 0.408   -12.829 58.231  1.00 47.87  ? 244 SER   B HA   1 
ATOM   8414 H HB2  . SER   B 1 259 ? 1.201   -14.919 58.144  1.00 47.28  ? 244 SER   B HB2  1 
ATOM   8415 H HB3  . SER   B 1 259 ? -0.048  -15.015 57.166  1.00 47.28  ? 244 SER   B HB3  1 
ATOM   8416 H HG   . SER   B 1 259 ? 1.378   -14.719 55.508  1.00 49.19  ? 244 SER   B HG   1 
ATOM   8417 N N    . ALA   B 1 260 ? 2.941   -12.555 57.992  1.00 40.80  ? 245 ALA   B N    1 
ATOM   8418 C CA   . ALA   B 1 260 ? 4.279   -12.005 57.798  1.00 44.23  ? 245 ALA   B CA   1 
ATOM   8419 C C    . ALA   B 1 260 ? 5.020   -12.748 56.692  1.00 43.41  ? 245 ALA   B C    1 
ATOM   8420 O O    . ALA   B 1 260 ? 5.761   -12.140 55.908  1.00 39.09  ? 245 ALA   B O    1 
ATOM   8421 C CB   . ALA   B 1 260 ? 5.063   -12.064 59.109  1.00 43.17  ? 245 ALA   B CB   1 
ATOM   8422 H H    . ALA   B 1 260 ? 2.810   -12.919 58.760  1.00 48.96  ? 245 ALA   B H    1 
ATOM   8423 H HA   . ALA   B 1 260 ? 4.205   -11.074 57.536  1.00 53.08  ? 245 ALA   B HA   1 
ATOM   8424 H HB1  . ALA   B 1 260 ? 5.949   -11.697 58.964  1.00 51.80  ? 245 ALA   B HB1  1 
ATOM   8425 H HB2  . ALA   B 1 260 ? 4.595   -11.543 59.780  1.00 51.80  ? 245 ALA   B HB2  1 
ATOM   8426 H HB3  . ALA   B 1 260 ? 5.130   -12.988 59.396  1.00 51.80  ? 245 ALA   B HB3  1 
ATOM   8427 N N    . ALA   B 1 261 ? 4.819   -14.063 56.603  1.00 39.21  ? 246 ALA   B N    1 
ATOM   8428 C CA   . ALA   B 1 261 ? 5.449   -14.836 55.539  1.00 41.46  ? 246 ALA   B CA   1 
ATOM   8429 C C    . ALA   B 1 261 ? 5.070   -14.289 54.168  1.00 36.16  ? 246 ALA   B C    1 
ATOM   8430 O O    . ALA   B 1 261 ? 5.924   -14.154 53.288  1.00 35.56  ? 246 ALA   B O    1 
ATOM   8431 C CB   . ALA   B 1 261 ? 5.057   -16.310 55.659  1.00 38.08  ? 246 ALA   B CB   1 
ATOM   8432 H H    . ALA   B 1 261 ? 4.329   -14.524 57.139  1.00 47.05  ? 246 ALA   B H    1 
ATOM   8433 H HA   . ALA   B 1 261 ? 6.412   -14.774 55.632  1.00 49.75  ? 246 ALA   B HA   1 
ATOM   8434 H HB1  . ALA   B 1 261 ? 5.484   -16.809 54.945  1.00 45.69  ? 246 ALA   B HB1  1 
ATOM   8435 H HB2  . ALA   B 1 261 ? 5.352   -16.646 56.519  1.00 45.69  ? 246 ALA   B HB2  1 
ATOM   8436 H HB3  . ALA   B 1 261 ? 4.093   -16.388 55.586  1.00 45.69  ? 246 ALA   B HB3  1 
ATOM   8437 N N    . PHE   B 1 262 ? 3.791   -13.964 53.971  1.00 35.50  ? 247 PHE   B N    1 
ATOM   8438 C CA   . PHE   B 1 262 ? 3.349   -13.441 52.683  1.00 33.93  ? 247 PHE   B CA   1 
ATOM   8439 C C    . PHE   B 1 262 ? 4.034   -12.112 52.385  1.00 37.70  ? 247 PHE   B C    1 
ATOM   8440 O O    . PHE   B 1 262 ? 4.606   -11.924 51.301  1.00 35.95  ? 247 PHE   B O    1 
ATOM   8441 C CB   . PHE   B 1 262 ? 1.827   -13.297 52.693  1.00 36.57  ? 247 PHE   B CB   1 
ATOM   8442 C CG   . PHE   B 1 262 ? 1.203   -13.107 51.330  1.00 33.96  ? 247 PHE   B CG   1 
ATOM   8443 C CD1  . PHE   B 1 262 ? 1.945   -13.236 50.167  1.00 37.08  ? 247 PHE   B CD1  1 
ATOM   8444 C CD2  . PHE   B 1 262 ? -0.143  -12.783 51.223  1.00 33.63  ? 247 PHE   B CD2  1 
ATOM   8445 C CE1  . PHE   B 1 262 ? 1.359   -13.056 48.937  1.00 31.03  ? 247 PHE   B CE1  1 
ATOM   8446 C CE2  . PHE   B 1 262 ? -0.732  -12.601 49.994  1.00 31.48  ? 247 PHE   B CE2  1 
ATOM   8447 C CZ   . PHE   B 1 262 ? 0.018   -12.741 48.848  1.00 32.18  ? 247 PHE   B CZ   1 
ATOM   8448 H H    . PHE   B 1 262 ? 3.169   -14.037 54.560  1.00 42.60  ? 247 PHE   B H    1 
ATOM   8449 H HA   . PHE   B 1 262 ? 3.583   -14.060 51.974  1.00 40.71  ? 247 PHE   B HA   1 
ATOM   8450 H HB2  . PHE   B 1 262 ? 1.444   -14.099 53.081  1.00 43.88  ? 247 PHE   B HB2  1 
ATOM   8451 H HB3  . PHE   B 1 262 ? 1.594   -12.524 53.232  1.00 43.88  ? 247 PHE   B HB3  1 
ATOM   8452 H HD1  . PHE   B 1 262 ? 2.850   -13.447 50.219  1.00 44.49  ? 247 PHE   B HD1  1 
ATOM   8453 H HD2  . PHE   B 1 262 ? -0.654  -12.687 51.994  1.00 40.36  ? 247 PHE   B HD2  1 
ATOM   8454 H HE1  . PHE   B 1 262 ? 1.867   -13.147 48.163  1.00 37.24  ? 247 PHE   B HE1  1 
ATOM   8455 H HE2  . PHE   B 1 262 ? -1.634  -12.384 49.938  1.00 37.78  ? 247 PHE   B HE2  1 
ATOM   8456 H HZ   . PHE   B 1 262 ? -0.378  -12.623 48.015  1.00 38.61  ? 247 PHE   B HZ   1 
ATOM   8457 N N    . HIS   B 1 263 ? 4.019   -11.187 53.353  1.00 35.81  ? 248 HIS   B N    1 
ATOM   8458 C CA   . HIS   B 1 263 ? 4.689   -9.901  53.176  1.00 37.11  ? 248 HIS   B CA   1 
ATOM   8459 C C    . HIS   B 1 263 ? 6.167   -10.089 52.855  1.00 36.65  ? 248 HIS   B C    1 
ATOM   8460 O O    . HIS   B 1 263 ? 6.718   -9.398  51.990  1.00 34.99  ? 248 HIS   B O    1 
ATOM   8461 C CB   . HIS   B 1 263 ? 4.544   -9.044  54.439  1.00 37.02  ? 248 HIS   B CB   1 
ATOM   8462 C CG   . HIS   B 1 263 ? 3.171   -8.485  54.653  1.00 40.01  ? 248 HIS   B CG   1 
ATOM   8463 N ND1  . HIS   B 1 263 ? 2.610   -7.541  53.820  1.00 40.23  ? 248 HIS   B ND1  1 
ATOM   8464 C CD2  . HIS   B 1 263 ? 2.265   -8.704  55.636  1.00 38.20  ? 248 HIS   B CD2  1 
ATOM   8465 C CE1  . HIS   B 1 263 ? 1.408   -7.220  54.267  1.00 38.66  ? 248 HIS   B CE1  1 
ATOM   8466 N NE2  . HIS   B 1 263 ? 1.173   -7.915  55.367  1.00 40.22  ? 248 HIS   B NE2  1 
ATOM   8467 H H    . HIS   B 1 263 ? 3.629   -11.282 54.114  1.00 42.97  ? 248 HIS   B H    1 
ATOM   8468 H HA   . HIS   B 1 263 ? 4.265   -9.437  52.437  1.00 44.53  ? 248 HIS   B HA   1 
ATOM   8469 H HB2  . HIS   B 1 263 ? 4.761   -9.591  55.210  1.00 44.43  ? 248 HIS   B HB2  1 
ATOM   8470 H HB3  . HIS   B 1 263 ? 5.159   -8.297  54.378  1.00 44.43  ? 248 HIS   B HB3  1 
ATOM   8471 H HD2  . HIS   B 1 263 ? 2.363   -9.282  56.358  1.00 45.84  ? 248 HIS   B HD2  1 
ATOM   8472 H HE1  . HIS   B 1 263 ? 0.826   -6.609  53.875  1.00 46.39  ? 248 HIS   B HE1  1 
ATOM   8473 H HE2  . HIS   B 1 263 ? 0.454   -7.879  55.837  1.00 48.27  ? 248 HIS   B HE2  1 
ATOM   8474 N N    . ASN   B 1 264 ? 6.831   -11.015 53.556  1.00 36.90  ? 249 ASN   B N    1 
ATOM   8475 C CA   . ASN   B 1 264 ? 8.239   -11.274 53.280  1.00 36.99  ? 249 ASN   B CA   1 
ATOM   8476 C C    . ASN   B 1 264 ? 8.421   -11.922 51.914  1.00 36.96  ? 249 ASN   B C    1 
ATOM   8477 O O    . ASN   B 1 264 ? 9.432   -11.684 51.246  1.00 37.68  ? 249 ASN   B O    1 
ATOM   8478 C CB   . ASN   B 1 264 ? 8.841   -12.155 54.375  1.00 38.70  ? 249 ASN   B CB   1 
ATOM   8479 C CG   . ASN   B 1 264 ? 10.307  -12.467 54.133  1.00 46.65  ? 249 ASN   B CG   1 
ATOM   8480 O OD1  . ASN   B 1 264 ? 10.645  -13.437 53.452  1.00 43.92  ? 249 ASN   B OD1  1 
ATOM   8481 N ND2  . ASN   B 1 264 ? 11.186  -11.644 54.691  1.00 45.04  ? 249 ASN   B ND2  1 
ATOM   8482 H H    . ASN   B 1 264 ? 6.492   -11.495 54.184  1.00 44.28  ? 249 ASN   B H    1 
ATOM   8483 H HA   . ASN   B 1 264 ? 8.721   -10.432 53.284  1.00 44.38  ? 249 ASN   B HA   1 
ATOM   8484 H HB2  . ASN   B 1 264 ? 8.768   -11.697 55.227  1.00 46.45  ? 249 ASN   B HB2  1 
ATOM   8485 H HB3  . ASN   B 1 264 ? 8.356   -12.995 54.408  1.00 46.45  ? 249 ASN   B HB3  1 
ATOM   8486 H HD21 . ASN   B 1 264 ? 12.029  -11.778 54.583  1.00 54.05  ? 249 ASN   B HD21 1 
ATOM   8487 H HD22 . ASN   B 1 264 ? 10.913  -10.977 55.160  1.00 54.05  ? 249 ASN   B HD22 1 
ATOM   8488 N N    . PHE   B 1 265 ? 7.457   -12.732 51.480  1.00 36.66  ? 250 PHE   B N    1 
ATOM   8489 C CA   . PHE   B 1 265 ? 7.518   -13.280 50.131  1.00 35.82  ? 250 PHE   B CA   1 
ATOM   8490 C C    . PHE   B 1 265 ? 7.505   -12.156 49.105  1.00 38.28  ? 250 PHE   B C    1 
ATOM   8491 O O    . PHE   B 1 265 ? 8.337   -12.118 48.190  1.00 35.45  ? 250 PHE   B O    1 
ATOM   8492 C CB   . PHE   B 1 265 ? 6.349   -14.243 49.911  1.00 39.19  ? 250 PHE   B CB   1 
ATOM   8493 C CG   . PHE   B 1 265 ? 6.385   -14.960 48.587  1.00 32.82  ? 250 PHE   B CG   1 
ATOM   8494 C CD1  . PHE   B 1 265 ? 7.089   -16.147 48.443  1.00 34.17  ? 250 PHE   B CD1  1 
ATOM   8495 C CD2  . PHE   B 1 265 ? 5.704   -14.455 47.492  1.00 32.03  ? 250 PHE   B CD2  1 
ATOM   8496 C CE1  . PHE   B 1 265 ? 7.121   -16.812 47.230  1.00 32.24  ? 250 PHE   B CE1  1 
ATOM   8497 C CE2  . PHE   B 1 265 ? 5.728   -15.117 46.272  1.00 32.59  ? 250 PHE   B CE2  1 
ATOM   8498 C CZ   . PHE   B 1 265 ? 6.442   -16.298 46.141  1.00 29.60  ? 250 PHE   B CZ   1 
ATOM   8499 H H    . PHE   B 1 265 ? 6.772   -12.974 51.939  1.00 43.99  ? 250 PHE   B H    1 
ATOM   8500 H HA   . PHE   B 1 265 ? 8.339   -13.784 50.019  1.00 42.98  ? 250 PHE   B HA   1 
ATOM   8501 H HB2  . PHE   B 1 265 ? 6.364   -14.915 50.610  1.00 47.02  ? 250 PHE   B HB2  1 
ATOM   8502 H HB3  . PHE   B 1 265 ? 5.521   -13.740 49.951  1.00 47.02  ? 250 PHE   B HB3  1 
ATOM   8503 H HD1  . PHE   B 1 265 ? 7.546   -16.500 49.172  1.00 41.00  ? 250 PHE   B HD1  1 
ATOM   8504 H HD2  . PHE   B 1 265 ? 5.224   -13.663 47.574  1.00 38.43  ? 250 PHE   B HD2  1 
ATOM   8505 H HE1  . PHE   B 1 265 ? 7.600   -17.605 47.148  1.00 38.69  ? 250 PHE   B HE1  1 
ATOM   8506 H HE2  . PHE   B 1 265 ? 5.266   -14.769 45.544  1.00 39.11  ? 250 PHE   B HE2  1 
ATOM   8507 H HZ   . PHE   B 1 265 ? 6.463   -16.742 45.324  1.00 35.52  ? 250 PHE   B HZ   1 
ATOM   8508 N N    . ILE   B 1 266 ? 6.578   -11.211 49.265  1.00 41.18  ? 251 ILE   B N    1 
ATOM   8509 C CA   . ILE   B 1 266 ? 6.489   -10.077 48.350  1.00 31.33  ? 251 ILE   B CA   1 
ATOM   8510 C C    . ILE   B 1 266 ? 7.800   -9.302  48.343  1.00 32.19  ? 251 ILE   B C    1 
ATOM   8511 O O    . ILE   B 1 266 ? 8.388   -9.046  47.287  1.00 35.77  ? 251 ILE   B O    1 
ATOM   8512 C CB   . ILE   B 1 266 ? 5.305   -9.174  48.746  1.00 37.87  ? 251 ILE   B CB   1 
ATOM   8513 C CG1  . ILE   B 1 266 ? 3.985   -9.954  48.657  1.00 34.91  ? 251 ILE   B CG1  1 
ATOM   8514 C CG2  . ILE   B 1 266 ? 5.271   -7.920  47.881  1.00 31.58  ? 251 ILE   B CG2  1 
ATOM   8515 C CD1  . ILE   B 1 266 ? 3.621   -10.414 47.263  1.00 30.00  ? 251 ILE   B CD1  1 
ATOM   8516 H H    . ILE   B 1 266 ? 5.990   -11.204 49.892  1.00 49.41  ? 251 ILE   B H    1 
ATOM   8517 H HA   . ILE   B 1 266 ? 6.333   -10.408 47.452  1.00 37.60  ? 251 ILE   B HA   1 
ATOM   8518 H HB   . ILE   B 1 266 ? 5.426   -8.895  49.667  1.00 45.44  ? 251 ILE   B HB   1 
ATOM   8519 H HG12 . ILE   B 1 266 ? 4.054   -10.743 49.217  1.00 41.89  ? 251 ILE   B HG12 1 
ATOM   8520 H HG13 . ILE   B 1 266 ? 3.268   -9.383  48.974  1.00 41.89  ? 251 ILE   B HG13 1 
ATOM   8521 H HG21 . ILE   B 1 266 ? 4.402   -7.499  47.971  1.00 37.89  ? 251 ILE   B HG21 1 
ATOM   8522 H HG22 . ILE   B 1 266 ? 5.965   -7.312  48.178  1.00 37.89  ? 251 ILE   B HG22 1 
ATOM   8523 H HG23 . ILE   B 1 266 ? 5.423   -8.171  46.956  1.00 37.89  ? 251 ILE   B HG23 1 
ATOM   8524 H HD11 . ILE   B 1 266 ? 2.741   -10.821 47.284  1.00 36.00  ? 251 ILE   B HD11 1 
ATOM   8525 H HD12 . ILE   B 1 266 ? 3.616   -9.647  46.668  1.00 36.00  ? 251 ILE   B HD12 1 
ATOM   8526 H HD13 . ILE   B 1 266 ? 4.278   -11.061 46.962  1.00 36.00  ? 251 ILE   B HD13 1 
ATOM   8527 N N    . LYS   B 1 267 ? 8.280   -8.931  49.530  1.00 33.58  ? 252 LYS   B N    1 
ATOM   8528 C CA   . LYS   B 1 267 ? 9.498   -8.139  49.637  1.00 34.70  ? 252 LYS   B CA   1 
ATOM   8529 C C    . LYS   B 1 267 ? 10.671  -8.825  48.953  1.00 37.82  ? 252 LYS   B C    1 
ATOM   8530 O O    . LYS   B 1 267 ? 11.480  -8.173  48.282  1.00 40.56  ? 252 LYS   B O    1 
ATOM   8531 C CB   . LYS   B 1 267 ? 9.811   -7.886  51.110  1.00 39.17  ? 252 LYS   B CB   1 
ATOM   8532 C CG   . LYS   B 1 267 ? 11.056  -7.056  51.381  1.00 43.84  ? 252 LYS   B CG   1 
ATOM   8533 C CD   . LYS   B 1 267 ? 11.042  -6.569  52.826  1.00 51.23  ? 252 LYS   B CD   1 
ATOM   8534 C CE   . LYS   B 1 267 ? 12.331  -5.860  53.218  1.00 61.65  ? 252 LYS   B CE   1 
ATOM   8535 N NZ   . LYS   B 1 267 ? 13.412  -6.822  53.568  1.00 64.45  ? 252 LYS   B NZ   1 
ATOM   8536 H H    . LYS   B 1 267 ? 7.919   -9.124  50.286  1.00 40.29  ? 252 LYS   B H    1 
ATOM   8537 H HA   . LYS   B 1 267 ? 9.361   -7.285  49.197  1.00 41.64  ? 252 LYS   B HA   1 
ATOM   8538 H HB2  . LYS   B 1 267 ? 9.059   -7.418  51.505  1.00 47.00  ? 252 LYS   B HB2  1 
ATOM   8539 H HB3  . LYS   B 1 267 ? 9.934   -8.744  51.547  1.00 47.00  ? 252 LYS   B HB3  1 
ATOM   8540 H HG2  . LYS   B 1 267 ? 11.849  -7.597  51.241  1.00 52.61  ? 252 LYS   B HG2  1 
ATOM   8541 H HG3  . LYS   B 1 267 ? 11.072  -6.286  50.791  1.00 52.61  ? 252 LYS   B HG3  1 
ATOM   8542 H HD2  . LYS   B 1 267 ? 10.309  -5.944  52.943  1.00 61.47  ? 252 LYS   B HD2  1 
ATOM   8543 H HD3  . LYS   B 1 267 ? 10.926  -7.330  53.416  1.00 61.47  ? 252 LYS   B HD3  1 
ATOM   8544 H HE2  . LYS   B 1 267 ? 12.637  -5.319  52.474  1.00 73.98  ? 252 LYS   B HE2  1 
ATOM   8545 H HE3  . LYS   B 1 267 ? 12.165  -5.298  53.991  1.00 73.98  ? 252 LYS   B HE3  1 
ATOM   8546 H HZ1  . LYS   B 1 267 ? 14.151  -6.381  53.794  1.00 77.33  ? 252 LYS   B HZ1  1 
ATOM   8547 H HZ2  . LYS   B 1 267 ? 13.157  -7.330  54.253  1.00 77.33  ? 252 LYS   B HZ2  1 
ATOM   8548 H HZ3  . LYS   B 1 267 ? 13.590  -7.346  52.871  1.00 77.33  ? 252 LYS   B HZ3  1 
ATOM   8549 N N    . VAL   B 1 268 ? 10.779  -10.139 49.109  1.00 34.90  ? 253 VAL   B N    1 
ATOM   8550 C CA   . VAL   B 1 268 ? 11.932  -10.860 48.583  1.00 36.49  ? 253 VAL   B CA   1 
ATOM   8551 C C    . VAL   B 1 268 ? 11.832  -11.023 47.070  1.00 36.05  ? 253 VAL   B C    1 
ATOM   8552 O O    . VAL   B 1 268 ? 12.832  -10.887 46.357  1.00 35.99  ? 253 VAL   B O    1 
ATOM   8553 C CB   . VAL   B 1 268 ? 12.057  -12.210 49.314  1.00 45.49  ? 253 VAL   B CB   1 
ATOM   8554 C CG1  . VAL   B 1 268 ? 12.960  -13.153 48.565  1.00 49.87  ? 253 VAL   B CG1  1 
ATOM   8555 C CG2  . VAL   B 1 268 ? 12.588  -11.986 50.722  1.00 43.03  ? 253 VAL   B CG2  1 
ATOM   8556 H H    . VAL   B 1 268 ? 10.204  -10.635 49.512  1.00 41.88  ? 253 VAL   B H    1 
ATOM   8557 H HA   . VAL   B 1 268 ? 12.737  -10.346 48.754  1.00 43.79  ? 253 VAL   B HA   1 
ATOM   8558 H HB   . VAL   B 1 268 ? 11.179  -12.618 49.364  1.00 54.59  ? 253 VAL   B HB   1 
ATOM   8559 H HG11 . VAL   B 1 268 ? 13.201  -13.889 49.149  1.00 59.84  ? 253 VAL   B HG11 1 
ATOM   8560 H HG12 . VAL   B 1 268 ? 12.489  -13.488 47.786  1.00 59.84  ? 253 VAL   B HG12 1 
ATOM   8561 H HG13 . VAL   B 1 268 ? 13.757  -12.675 48.290  1.00 59.84  ? 253 VAL   B HG13 1 
ATOM   8562 H HG21 . VAL   B 1 268 ? 12.642  -12.840 51.179  1.00 51.64  ? 253 VAL   B HG21 1 
ATOM   8563 H HG22 . VAL   B 1 268 ? 13.469  -11.583 50.667  1.00 51.64  ? 253 VAL   B HG22 1 
ATOM   8564 H HG23 . VAL   B 1 268 ? 11.983  -11.395 51.197  1.00 51.64  ? 253 VAL   B HG23 1 
ATOM   8565 N N    . THR   B 1 269 ? 10.633  -11.300 46.548  1.00 37.04  ? 254 THR   B N    1 
ATOM   8566 C CA   . THR   B 1 269 ? 10.488  -11.460 45.106  1.00 31.68  ? 254 THR   B CA   1 
ATOM   8567 C C    . THR   B 1 269 ? 10.652  -10.129 44.383  1.00 40.42  ? 254 THR   B C    1 
ATOM   8568 O O    . THR   B 1 269 ? 11.189  -10.090 43.267  1.00 34.27  ? 254 THR   B O    1 
ATOM   8569 C CB   . THR   B 1 269 ? 9.130   -12.069 44.765  1.00 31.09  ? 254 THR   B CB   1 
ATOM   8570 O OG1  . THR   B 1 269 ? 8.085   -11.337 45.414  1.00 33.74  ? 254 THR   B OG1  1 
ATOM   8571 C CG2  . THR   B 1 269 ? 9.066   -13.520 45.200  1.00 34.91  ? 254 THR   B CG2  1 
ATOM   8572 H H    . THR   B 1 269 ? 9.908   -11.398 46.999  1.00 44.45  ? 254 THR   B H    1 
ATOM   8573 H HA   . THR   B 1 269 ? 11.175  -12.071 44.796  1.00 38.02  ? 254 THR   B HA   1 
ATOM   8574 H HB   . THR   B 1 269 ? 9.001   -12.030 43.804  1.00 37.30  ? 254 THR   B HB   1 
ATOM   8575 H HG1  . THR   B 1 269 ? 8.143   -11.432 46.246  1.00 40.48  ? 254 THR   B HG1  1 
ATOM   8576 H HG21 . THR   B 1 269 ? 8.201   -13.896 44.973  1.00 41.89  ? 254 THR   B HG21 1 
ATOM   8577 H HG22 . THR   B 1 269 ? 9.759   -14.031 44.753  1.00 41.89  ? 254 THR   B HG22 1 
ATOM   8578 H HG23 . THR   B 1 269 ? 9.196   -13.585 46.159  1.00 41.89  ? 254 THR   B HG23 1 
ATOM   8579 N N    . LEU   B 1 270 ? 10.206  -9.040  44.997  1.00 33.78  ? 255 LEU   B N    1 
ATOM   8580 C CA   . LEU   B 1 270 ? 10.296  -7.706  44.401  1.00 33.93  ? 255 LEU   B CA   1 
ATOM   8581 C C    . LEU   B 1 270 ? 11.587  -7.006  44.807  1.00 33.20  ? 255 LEU   B C    1 
ATOM   8582 O O    . LEU   B 1 270 ? 11.590  -5.846  45.216  1.00 33.77  ? 255 LEU   B O    1 
ATOM   8583 C CB   . LEU   B 1 270 ? 9.082   -6.874  44.796  1.00 35.09  ? 255 LEU   B CB   1 
ATOM   8584 C CG   . LEU   B 1 270 ? 7.739   -7.482  44.395  1.00 31.32  ? 255 LEU   B CG   1 
ATOM   8585 C CD1  . LEU   B 1 270 ? 6.605   -6.514  44.672  1.00 35.15  ? 255 LEU   B CD1  1 
ATOM   8586 C CD2  . LEU   B 1 270 ? 7.754   -7.883  42.934  1.00 30.84  ? 255 LEU   B CD2  1 
ATOM   8587 H H    . LEU   B 1 270 ? 9.839   -9.044  45.774  1.00 40.54  ? 255 LEU   B H    1 
ATOM   8588 H HA   . LEU   B 1 270 ? 10.291  -7.798  43.436  1.00 40.72  ? 255 LEU   B HA   1 
ATOM   8589 H HB2  . LEU   B 1 270 ? 9.081   -6.769  45.760  1.00 42.10  ? 255 LEU   B HB2  1 
ATOM   8590 H HB3  . LEU   B 1 270 ? 9.151   -6.006  44.368  1.00 42.10  ? 255 LEU   B HB3  1 
ATOM   8591 H HG   . LEU   B 1 270 ? 7.585   -8.279  44.925  1.00 37.58  ? 255 LEU   B HG   1 
ATOM   8592 H HD11 . LEU   B 1 270 ? 5.772   -7.009  44.721  1.00 42.17  ? 255 LEU   B HD11 1 
ATOM   8593 H HD12 . LEU   B 1 270 ? 6.772   -6.065  45.515  1.00 42.17  ? 255 LEU   B HD12 1 
ATOM   8594 H HD13 . LEU   B 1 270 ? 6.562   -5.863  43.954  1.00 42.17  ? 255 LEU   B HD13 1 
ATOM   8595 H HD21 . LEU   B 1 270 ? 6.843   -8.039  42.640  1.00 37.00  ? 255 LEU   B HD21 1 
ATOM   8596 H HD22 . LEU   B 1 270 ? 8.151   -7.168  42.413  1.00 37.00  ? 255 LEU   B HD22 1 
ATOM   8597 H HD23 . LEU   B 1 270 ? 8.277   -8.694  42.835  1.00 37.00  ? 255 LEU   B HD23 1 
ATOM   8598 N N    . THR   B 1 271 ? 12.699  -7.727  44.702  1.00 36.61  ? 256 THR   B N    1 
ATOM   8599 C CA   . THR   B 1 271 ? 14.015  -7.149  44.936  1.00 37.61  ? 256 THR   B CA   1 
ATOM   8600 C C    . THR   B 1 271 ? 14.447  -6.358  43.711  1.00 37.22  ? 256 THR   B C    1 
ATOM   8601 O O    . THR   B 1 271 ? 14.454  -6.887  42.594  1.00 36.69  ? 256 THR   B O    1 
ATOM   8602 C CB   . THR   B 1 271 ? 15.030  -8.246  45.243  1.00 38.45  ? 256 THR   B CB   1 
ATOM   8603 O OG1  . THR   B 1 271 ? 14.718  -8.845  46.507  1.00 39.46  ? 256 THR   B OG1  1 
ATOM   8604 C CG2  . THR   B 1 271 ? 16.445  -7.679  45.272  1.00 43.55  ? 256 THR   B CG2  1 
ATOM   8605 H H    . THR   B 1 271 ? 12.717  -8.562  44.494  1.00 43.93  ? 256 THR   B H    1 
ATOM   8606 H HA   . THR   B 1 271 ? 13.979  -6.549  45.698  1.00 45.13  ? 256 THR   B HA   1 
ATOM   8607 H HB   . THR   B 1 271 ? 14.995  -8.925  44.551  1.00 46.14  ? 256 THR   B HB   1 
ATOM   8608 H HG1  . THR   B 1 271 ? 13.954  -9.193  46.480  1.00 47.35  ? 256 THR   B HG1  1 
ATOM   8609 H HG21 . THR   B 1 271 ? 17.040  -8.294  45.730  1.00 52.26  ? 256 THR   B HG21 1 
ATOM   8610 H HG22 . THR   B 1 271 ? 16.767  -7.546  44.367  1.00 52.26  ? 256 THR   B HG22 1 
ATOM   8611 H HG23 . THR   B 1 271 ? 16.453  -6.828  45.737  1.00 52.26  ? 256 THR   B HG23 1 
ATOM   8612 N N    . LYS   B 1 272 ? 14.818  -5.094  43.925  1.00 42.62  ? 257 LYS   B N    1 
ATOM   8613 C CA   . LYS   B 1 272 ? 15.118  -4.206  42.808  1.00 40.89  ? 257 LYS   B CA   1 
ATOM   8614 C C    . LYS   B 1 272 ? 16.264  -4.743  41.965  1.00 37.82  ? 257 LYS   B C    1 
ATOM   8615 O O    . LYS   B 1 272 ? 16.141  -4.876  40.743  1.00 43.94  ? 257 LYS   B O    1 
ATOM   8616 C CB   . LYS   B 1 272 ? 15.457  -2.809  43.327  1.00 46.51  ? 257 LYS   B CB   1 
ATOM   8617 C CG   . LYS   B 1 272 ? 14.259  -1.899  43.465  1.00 56.84  ? 257 LYS   B CG   1 
ATOM   8618 C CD   . LYS   B 1 272 ? 14.634  -0.522  44.031  1.00 59.27  ? 257 LYS   B CD   1 
ATOM   8619 C CE   . LYS   B 1 272 ? 15.656  0.191   43.173  1.00 55.20  ? 257 LYS   B CE   1 
ATOM   8620 N NZ   . LYS   B 1 272 ? 15.847  1.611   43.597  1.00 63.78  ? 257 LYS   B NZ   1 
ATOM   8621 H H    . LYS   B 1 272 ? 14.901  -4.731  44.700  1.00 51.14  ? 257 LYS   B H    1 
ATOM   8622 H HA   . LYS   B 1 272 ? 14.330  -4.145  42.246  1.00 49.06  ? 257 LYS   B HA   1 
ATOM   8623 H HB2  . LYS   B 1 272 ? 15.866  -2.894  44.203  1.00 55.81  ? 257 LYS   B HB2  1 
ATOM   8624 H HB3  . LYS   B 1 272 ? 16.078  -2.390  42.710  1.00 55.81  ? 257 LYS   B HB3  1 
ATOM   8625 H HG2  . LYS   B 1 272 ? 13.858  -1.766  42.592  1.00 68.21  ? 257 LYS   B HG2  1 
ATOM   8626 H HG3  . LYS   B 1 272 ? 13.616  -2.307  44.066  1.00 68.21  ? 257 LYS   B HG3  1 
ATOM   8627 H HD2  . LYS   B 1 272 ? 13.839  0.031   44.077  1.00 71.13  ? 257 LYS   B HD2  1 
ATOM   8628 H HD3  . LYS   B 1 272 ? 15.011  -0.635  44.918  1.00 71.13  ? 257 LYS   B HD3  1 
ATOM   8629 H HE2  . LYS   B 1 272 ? 16.509  -0.265  43.246  1.00 66.24  ? 257 LYS   B HE2  1 
ATOM   8630 H HE3  . LYS   B 1 272 ? 15.356  0.187   42.250  1.00 66.24  ? 257 LYS   B HE3  1 
ATOM   8631 H HZ1  . LYS   B 1 272 ? 16.451  2.006   43.077  1.00 76.53  ? 257 LYS   B HZ1  1 
ATOM   8632 H HZ2  . LYS   B 1 272 ? 15.077  2.054   43.533  1.00 76.53  ? 257 LYS   B HZ2  1 
ATOM   8633 H HZ3  . LYS   B 1 272 ? 16.128  1.642   44.441  1.00 76.53  ? 257 LYS   B HZ3  1 
ATOM   8634 N N    . SER   B 1 273 ? 17.387  -5.036  42.593  1.00 43.86  ? 258 SER   B N    1 
ATOM   8635 C CA   . SER   B 1 273 ? 18.561  -5.467  41.849  1.00 40.88  ? 258 SER   B CA   1 
ATOM   8636 C C    . SER   B 1 273 ? 18.394  -6.917  41.413  1.00 50.95  ? 258 SER   B C    1 
ATOM   8637 O O    . SER   B 1 273 ? 18.119  -7.780  42.250  1.00 50.63  ? 258 SER   B O    1 
ATOM   8638 C CB   . SER   B 1 273 ? 19.818  -5.328  42.700  1.00 52.52  ? 258 SER   B CB   1 
ATOM   8639 O OG   . SER   B 1 273 ? 20.956  -5.820  42.009  1.00 54.65  ? 258 SER   B OG   1 
ATOM   8640 H H    . SER   B 1 273 ? 17.498  -4.995  43.445  1.00 52.63  ? 258 SER   B H    1 
ATOM   8641 H HA   . SER   B 1 273 ? 18.664  -4.914  41.059  1.00 49.05  ? 258 SER   B HA   1 
ATOM   8642 H HB2  . SER   B 1 273 ? 19.956  -4.390  42.908  1.00 63.03  ? 258 SER   B HB2  1 
ATOM   8643 H HB3  . SER   B 1 273 ? 19.702  -5.835  43.519  1.00 63.03  ? 258 SER   B HB3  1 
ATOM   8644 H HG   . SER   B 1 273 ? 21.640  -5.740  42.489  1.00 65.58  ? 258 SER   B HG   1 
ATOM   8645 N N    . PRO   B 1 274 ? 18.549  -7.227  40.124  1.00 50.83  ? 259 PRO   B N    1 
ATOM   8646 C CA   . PRO   B 1 274 ? 18.496  -8.639  39.718  1.00 44.47  ? 259 PRO   B CA   1 
ATOM   8647 C C    . PRO   B 1 274 ? 19.604  -9.463  40.343  1.00 50.37  ? 259 PRO   B C    1 
ATOM   8648 O O    . PRO   B 1 274 ? 19.423  -10.664 40.579  1.00 54.88  ? 259 PRO   B O    1 
ATOM   8649 C CB   . PRO   B 1 274 ? 18.632  -8.581  38.189  1.00 54.82  ? 259 PRO   B CB   1 
ATOM   8650 C CG   . PRO   B 1 274 ? 18.427  -7.160  37.812  1.00 45.24  ? 259 PRO   B CG   1 
ATOM   8651 C CD   . PRO   B 1 274 ? 18.831  -6.337  38.987  1.00 43.11  ? 259 PRO   B CD   1 
ATOM   8652 H HA   . PRO   B 1 274 ? 17.632  -9.019  39.941  1.00 53.36  ? 259 PRO   B HA   1 
ATOM   8653 H HB2  . PRO   B 1 274 ? 19.517  -8.881  37.930  1.00 65.78  ? 259 PRO   B HB2  1 
ATOM   8654 H HB3  . PRO   B 1 274 ? 17.957  -9.146  37.780  1.00 65.78  ? 259 PRO   B HB3  1 
ATOM   8655 H HG2  . PRO   B 1 274 ? 18.978  -6.948  37.043  1.00 54.29  ? 259 PRO   B HG2  1 
ATOM   8656 H HG3  . PRO   B 1 274 ? 17.492  -7.014  37.600  1.00 54.29  ? 259 PRO   B HG3  1 
ATOM   8657 H HD2  . PRO   B 1 274 ? 19.774  -6.114  38.947  1.00 51.73  ? 259 PRO   B HD2  1 
ATOM   8658 H HD3  . PRO   B 1 274 ? 18.301  -5.526  39.042  1.00 51.73  ? 259 PRO   B HD3  1 
ATOM   8659 N N    . LYS   B 1 275 ? 20.754  -8.845  40.622  1.00 52.10  ? 260 LYS   B N    1 
ATOM   8660 C CA   . LYS   B 1 275 ? 21.865  -9.553  41.241  1.00 56.92  ? 260 LYS   B CA   1 
ATOM   8661 C C    . LYS   B 1 275 ? 21.589  -9.946  42.683  1.00 52.74  ? 260 LYS   B C    1 
ATOM   8662 O O    . LYS   B 1 275 ? 22.414  -10.643 43.282  1.00 60.58  ? 260 LYS   B O    1 
ATOM   8663 C CB   . LYS   B 1 275 ? 23.126  -8.692  41.187  1.00 65.71  ? 260 LYS   B CB   1 
ATOM   8664 C CG   . LYS   B 1 275 ? 23.737  -8.576  39.795  1.00 69.42  ? 260 LYS   B CG   1 
ATOM   8665 C CD   . LYS   B 1 275 ? 25.079  -7.856  39.814  1.00 69.16  ? 260 LYS   B CD   1 
ATOM   8666 C CE   . LYS   B 1 275 ? 26.134  -8.611  40.623  1.00 70.01  ? 260 LYS   B CE   1 
ATOM   8667 N NZ   . LYS   B 1 275 ? 27.439  -7.887  40.656  1.00 71.03  ? 260 LYS   B NZ   1 
ATOM   8668 H H    . LYS   B 1 275 ? 20.912  -8.016  40.460  1.00 62.52  ? 260 LYS   B H    1 
ATOM   8669 H HA   . LYS   B 1 275 ? 22.027  -10.365 40.736  1.00 68.30  ? 260 LYS   B HA   1 
ATOM   8670 H HB2  . LYS   B 1 275 ? 22.904  -7.797  41.487  1.00 78.85  ? 260 LYS   B HB2  1 
ATOM   8671 H HB3  . LYS   B 1 275 ? 23.794  -9.083  41.771  1.00 78.85  ? 260 LYS   B HB3  1 
ATOM   8672 H HG2  . LYS   B 1 275 ? 23.877  -9.465  39.433  1.00 83.30  ? 260 LYS   B HG2  1 
ATOM   8673 H HG3  . LYS   B 1 275 ? 23.134  -8.076  39.223  1.00 83.30  ? 260 LYS   B HG3  1 
ATOM   8674 H HD2  . LYS   B 1 275 ? 25.405  -7.766  38.904  1.00 82.99  ? 260 LYS   B HD2  1 
ATOM   8675 H HD3  . LYS   B 1 275 ? 24.964  -6.979  40.213  1.00 82.99  ? 260 LYS   B HD3  1 
ATOM   8676 H HE2  . LYS   B 1 275 ? 25.822  -8.714  41.536  1.00 84.02  ? 260 LYS   B HE2  1 
ATOM   8677 H HE3  . LYS   B 1 275 ? 26.281  -9.482  40.222  1.00 84.02  ? 260 LYS   B HE3  1 
ATOM   8678 H HZ1  . LYS   B 1 275 ? 28.031  -8.349  41.134  1.00 85.24  ? 260 LYS   B HZ1  1 
ATOM   8679 H HZ2  . LYS   B 1 275 ? 27.752  -7.786  39.829  1.00 85.24  ? 260 LYS   B HZ2  1 
ATOM   8680 H HZ3  . LYS   B 1 275 ? 27.333  -7.084  41.025  1.00 85.24  ? 260 LYS   B HZ3  1 
ATOM   8681 N N    . LYS   B 1 276 ? 20.469  -9.510  43.254  1.00 48.10  ? 261 LYS   B N    1 
ATOM   8682 C CA   . LYS   B 1 276 ? 20.072  -9.901  44.598  1.00 50.74  ? 261 LYS   B CA   1 
ATOM   8683 C C    . LYS   B 1 276 ? 18.700  -10.555 44.625  1.00 49.52  ? 261 LYS   B C    1 
ATOM   8684 O O    . LYS   B 1 276 ? 18.254  -10.984 45.697  1.00 47.73  ? 261 LYS   B O    1 
ATOM   8685 C CB   . LYS   B 1 276 ? 20.090  -8.683  45.530  1.00 54.43  ? 261 LYS   B CB   1 
ATOM   8686 C CG   . LYS   B 1 276 ? 21.484  -8.105  45.749  1.00 53.52  ? 261 LYS   B CG   1 
ATOM   8687 C CD   . LYS   B 1 276 ? 21.446  -6.798  46.532  1.00 65.19  ? 261 LYS   B CD   1 
ATOM   8688 C CE   . LYS   B 1 276 ? 22.814  -6.456  47.108  1.00 61.95  ? 261 LYS   B CE   1 
ATOM   8689 N NZ   . LYS   B 1 276 ? 23.260  -7.470  48.108  1.00 74.85  ? 261 LYS   B NZ   1 
ATOM   8690 H H    . LYS   B 1 276 ? 19.913  -8.976  42.873  1.00 57.72  ? 261 LYS   B H    1 
ATOM   8691 H HA   . LYS   B 1 276 ? 20.714  -10.539 44.948  1.00 60.89  ? 261 LYS   B HA   1 
ATOM   8692 H HB2  . LYS   B 1 276 ? 19.537  -7.985  45.144  1.00 65.31  ? 261 LYS   B HB2  1 
ATOM   8693 H HB3  . LYS   B 1 276 ? 19.737  -8.945  46.395  1.00 65.31  ? 261 LYS   B HB3  1 
ATOM   8694 H HG2  . LYS   B 1 276 ? 22.018  -8.742  46.250  1.00 64.23  ? 261 LYS   B HG2  1 
ATOM   8695 H HG3  . LYS   B 1 276 ? 21.897  -7.931  44.889  1.00 64.23  ? 261 LYS   B HG3  1 
ATOM   8696 H HD2  . LYS   B 1 276 ? 21.174  -6.078  45.942  1.00 78.23  ? 261 LYS   B HD2  1 
ATOM   8697 H HD3  . LYS   B 1 276 ? 20.817  -6.881  47.266  1.00 78.23  ? 261 LYS   B HD3  1 
ATOM   8698 H HE2  . LYS   B 1 276 ? 23.467  -6.429  46.391  1.00 74.35  ? 261 LYS   B HE2  1 
ATOM   8699 H HE3  . LYS   B 1 276 ? 22.770  -5.593  47.549  1.00 74.35  ? 261 LYS   B HE3  1 
ATOM   8700 H HZ1  . LYS   B 1 276 ? 23.999  -7.190  48.517  1.00 89.82  ? 261 LYS   B HZ1  1 
ATOM   8701 H HZ2  . LYS   B 1 276 ? 22.624  -7.597  48.717  1.00 89.82  ? 261 LYS   B HZ2  1 
ATOM   8702 H HZ3  . LYS   B 1 276 ? 23.431  -8.244  47.702  1.00 89.82  ? 261 LYS   B HZ3  1 
ATOM   8703 N N    . ARG   B 1 277 ? 18.020  -10.640 43.487  1.00 43.01  ? 262 ARG   B N    1 
ATOM   8704 C CA   . ARG   B 1 277 ? 16.718  -11.297 43.442  1.00 46.91  ? 262 ARG   B CA   1 
ATOM   8705 C C    . ARG   B 1 277 ? 16.916  -12.811 43.458  1.00 40.97  ? 262 ARG   B C    1 
ATOM   8706 O O    . ARG   B 1 277 ? 17.718  -13.333 42.680  1.00 39.23  ? 262 ARG   B O    1 
ATOM   8707 C CB   . ARG   B 1 277 ? 15.947  -10.868 42.195  1.00 45.06  ? 262 ARG   B CB   1 
ATOM   8708 C CG   . ARG   B 1 277 ? 14.463  -11.191 42.246  1.00 44.62  ? 262 ARG   B CG   1 
ATOM   8709 C CD   . ARG   B 1 277 ? 13.707  -10.667 41.020  1.00 39.71  ? 262 ARG   B CD   1 
ATOM   8710 N NE   . ARG   B 1 277 ? 13.950  -9.249  40.779  1.00 35.59  ? 262 ARG   B NE   1 
ATOM   8711 C CZ   . ARG   B 1 277 ? 14.348  -8.727  39.622  1.00 33.92  ? 262 ARG   B CZ   1 
ATOM   8712 N NH1  . ARG   B 1 277 ? 14.494  -9.469  38.538  1.00 35.72  ? 262 ARG   B NH1  1 
ATOM   8713 N NH2  . ARG   B 1 277 ? 14.601  -7.423  39.554  1.00 35.81  ? 262 ARG   B NH2  1 
ATOM   8714 H H    . ARG   B 1 277 ? 18.288  -10.328 42.732  1.00 51.61  ? 262 ARG   B H    1 
ATOM   8715 H HA   . ARG   B 1 277 ? 16.189  -11.049 44.216  1.00 56.29  ? 262 ARG   B HA   1 
ATOM   8716 H HB2  . ARG   B 1 277 ? 16.037  -9.908  42.089  1.00 54.07  ? 262 ARG   B HB2  1 
ATOM   8717 H HB3  . ARG   B 1 277 ? 16.323  -11.323 41.425  1.00 54.07  ? 262 ARG   B HB3  1 
ATOM   8718 H HG2  . ARG   B 1 277 ? 14.349  -12.154 42.281  1.00 53.54  ? 262 ARG   B HG2  1 
ATOM   8719 H HG3  . ARG   B 1 277 ? 14.076  -10.782 43.035  1.00 53.54  ? 262 ARG   B HG3  1 
ATOM   8720 H HD2  . ARG   B 1 277 ? 13.994  -11.160 40.235  1.00 47.65  ? 262 ARG   B HD2  1 
ATOM   8721 H HD3  . ARG   B 1 277 ? 12.755  -10.790 41.158  1.00 47.65  ? 262 ARG   B HD3  1 
ATOM   8722 H HE   . ARG   B 1 277 ? 13.827  -8.709  41.436  1.00 42.70  ? 262 ARG   B HE   1 
ATOM   8723 H HH11 . ARG   B 1 277 ? 14.331  -10.312 38.569  1.00 42.86  ? 262 ARG   B HH11 1 
ATOM   8724 H HH12 . ARG   B 1 277 ? 14.752  -9.107  37.801  1.00 42.86  ? 262 ARG   B HH12 1 
ATOM   8725 H HH21 . ARG   B 1 277 ? 14.507  -6.929  40.252  1.00 42.97  ? 262 ARG   B HH21 1 
ATOM   8726 H HH22 . ARG   B 1 277 ? 14.858  -7.073  38.812  1.00 42.97  ? 262 ARG   B HH22 1 
ATOM   8727 N N    . PRO   B 1 278 ? 16.225  -13.541 44.335  1.00 40.83  ? 263 PRO   B N    1 
ATOM   8728 C CA   . PRO   B 1 278 ? 16.470  -14.984 44.437  1.00 38.35  ? 263 PRO   B CA   1 
ATOM   8729 C C    . PRO   B 1 278 ? 15.983  -15.760 43.223  1.00 37.81  ? 263 PRO   B C    1 
ATOM   8730 O O    . PRO   B 1 278 ? 14.993  -15.405 42.578  1.00 38.60  ? 263 PRO   B O    1 
ATOM   8731 C CB   . PRO   B 1 278 ? 15.681  -15.395 45.689  1.00 37.98  ? 263 PRO   B CB   1 
ATOM   8732 C CG   . PRO   B 1 278 ? 15.404  -14.143 46.417  1.00 43.03  ? 263 PRO   B CG   1 
ATOM   8733 C CD   . PRO   B 1 278 ? 15.298  -13.073 45.378  1.00 40.07  ? 263 PRO   B CD   1 
ATOM   8734 H HA   . PRO   B 1 278 ? 17.419  -15.145 44.559  1.00 46.01  ? 263 PRO   B HA   1 
ATOM   8735 H HB2  . PRO   B 1 278 ? 14.855  -15.831 45.427  1.00 45.58  ? 263 PRO   B HB2  1 
ATOM   8736 H HB3  . PRO   B 1 278 ? 16.217  -15.996 46.231  1.00 45.58  ? 263 PRO   B HB3  1 
ATOM   8737 H HG2  . PRO   B 1 278 ? 14.571  -14.228 46.906  1.00 51.64  ? 263 PRO   B HG2  1 
ATOM   8738 H HG3  . PRO   B 1 278 ? 16.131  -13.954 47.030  1.00 51.64  ? 263 PRO   B HG3  1 
ATOM   8739 H HD2  . PRO   B 1 278 ? 14.392  -13.010 45.036  1.00 48.08  ? 263 PRO   B HD2  1 
ATOM   8740 H HD3  . PRO   B 1 278 ? 15.578  -12.215 45.734  1.00 48.08  ? 263 PRO   B HD3  1 
ATOM   8741 N N    . SER   B 1 279 ? 16.687  -16.855 42.941  1.00 44.90  ? 264 SER   B N    1 
ATOM   8742 C CA   . SER   B 1 279 ? 16.321  -17.769 41.873  1.00 41.35  ? 264 SER   B CA   1 
ATOM   8743 C C    . SER   B 1 279 ? 15.001  -18.465 42.195  1.00 47.57  ? 264 SER   B C    1 
ATOM   8744 O O    . SER   B 1 279 ? 14.496  -18.415 43.320  1.00 46.89  ? 264 SER   B O    1 
ATOM   8745 C CB   . SER   B 1 279 ? 17.407  -18.822 41.680  1.00 39.65  ? 264 SER   B CB   1 
ATOM   8746 O OG   . SER   B 1 279 ? 17.425  -19.699 42.792  1.00 41.86  ? 264 SER   B OG   1 
ATOM   8747 H H    . SER   B 1 279 ? 17.397  -17.093 43.365  1.00 53.88  ? 264 SER   B H    1 
ATOM   8748 H HA   . SER   B 1 279 ? 16.218  -17.264 41.051  1.00 49.62  ? 264 SER   B HA   1 
ATOM   8749 H HB2  . SER   B 1 279 ? 17.221  -19.330 40.874  1.00 47.58  ? 264 SER   B HB2  1 
ATOM   8750 H HB3  . SER   B 1 279 ? 18.269  -18.384 41.604  1.00 47.58  ? 264 SER   B HB3  1 
ATOM   8751 H HG   . SER   B 1 279 ? 18.035  -20.269 42.699  1.00 50.23  ? 264 SER   B HG   1 
ATOM   8752 N N    . ALA   B 1 280 ? 14.450  -19.146 41.189  1.00 38.90  ? 265 ALA   B N    1 
ATOM   8753 C CA   . ALA   B 1 280 ? 13.218  -19.895 41.410  1.00 39.96  ? 265 ALA   B CA   1 
ATOM   8754 C C    . ALA   B 1 280 ? 13.432  -21.017 42.419  1.00 41.77  ? 265 ALA   B C    1 
ATOM   8755 O O    . ALA   B 1 280 ? 12.576  -21.265 43.276  1.00 37.35  ? 265 ALA   B O    1 
ATOM   8756 C CB   . ALA   B 1 280 ? 12.704  -20.457 40.089  1.00 37.25  ? 265 ALA   B CB   1 
ATOM   8757 H H    . ALA   B 1 280 ? 14.763  -19.189 40.389  1.00 46.68  ? 265 ALA   B H    1 
ATOM   8758 H HA   . ALA   B 1 280 ? 12.545  -19.294 41.765  1.00 47.95  ? 265 ALA   B HA   1 
ATOM   8759 H HB1  . ALA   B 1 280 ? 11.885  -20.950 40.253  1.00 44.70  ? 265 ALA   B HB1  1 
ATOM   8760 H HB2  . ALA   B 1 280 ? 12.532  -19.723 39.479  1.00 44.70  ? 265 ALA   B HB2  1 
ATOM   8761 H HB3  . ALA   B 1 280 ? 13.376  -21.048 39.714  1.00 44.70  ? 265 ALA   B HB3  1 
ATOM   8762 N N    . THR   B 1 281 ? 14.570  -21.709 42.331  1.00 48.24  ? 266 THR   B N    1 
ATOM   8763 C CA   . THR   B 1 281 ? 14.843  -22.795 43.265  1.00 47.39  ? 266 THR   B CA   1 
ATOM   8764 C C    . THR   B 1 281 ? 14.960  -22.279 44.692  1.00 42.61  ? 266 THR   B C    1 
ATOM   8765 O O    . THR   B 1 281 ? 14.422  -22.886 45.626  1.00 51.01  ? 266 THR   B O    1 
ATOM   8766 C CB   . THR   B 1 281 ? 16.120  -23.524 42.857  1.00 47.53  ? 266 THR   B CB   1 
ATOM   8767 O OG1  . THR   B 1 281 ? 15.915  -24.170 41.595  1.00 40.42  ? 266 THR   B OG1  1 
ATOM   8768 C CG2  . THR   B 1 281 ? 16.494  -24.548 43.902  1.00 49.85  ? 266 THR   B CG2  1 
ATOM   8769 H H    . THR   B 1 281 ? 15.188  -21.570 41.750  1.00 57.89  ? 266 THR   B H    1 
ATOM   8770 H HA   . THR   B 1 281 ? 14.108  -23.427 43.232  1.00 56.86  ? 266 THR   B HA   1 
ATOM   8771 H HB   . THR   B 1 281 ? 16.852  -22.893 42.777  1.00 57.04  ? 266 THR   B HB   1 
ATOM   8772 H HG1  . THR   B 1 281 ? 16.617  -24.563 41.356  1.00 48.50  ? 266 THR   B HG1  1 
ATOM   8773 H HG21 . THR   B 1 281 ? 17.107  -25.199 43.525  1.00 59.82  ? 266 THR   B HG21 1 
ATOM   8774 H HG22 . THR   B 1 281 ? 16.923  -24.112 44.655  1.00 59.82  ? 266 THR   B HG22 1 
ATOM   8775 H HG23 . THR   B 1 281 ? 15.700  -25.008 44.216  1.00 59.82  ? 266 THR   B HG23 1 
ATOM   8776 N N    . LYS   B 1 282 ? 15.663  -21.163 44.882  1.00 42.46  ? 267 LYS   B N    1 
ATOM   8777 C CA   . LYS   B 1 282 ? 15.811  -20.609 46.222  1.00 47.58  ? 267 LYS   B CA   1 
ATOM   8778 C C    . LYS   B 1 282 ? 14.465  -20.201 46.806  1.00 45.19  ? 267 LYS   B C    1 
ATOM   8779 O O    . LYS   B 1 282 ? 14.259  -20.302 48.018  1.00 50.85  ? 267 LYS   B O    1 
ATOM   8780 C CB   . LYS   B 1 282 ? 16.767  -19.415 46.188  1.00 56.71  ? 267 LYS   B CB   1 
ATOM   8781 C CG   . LYS   B 1 282 ? 17.018  -18.761 47.544  1.00 63.19  ? 267 LYS   B CG   1 
ATOM   8782 C CD   . LYS   B 1 282 ? 17.398  -19.789 48.603  1.00 70.66  ? 267 LYS   B CD   1 
ATOM   8783 C CE   . LYS   B 1 282 ? 17.982  -19.132 49.846  1.00 68.91  ? 267 LYS   B CE   1 
ATOM   8784 N NZ   . LYS   B 1 282 ? 19.356  -18.597 49.607  1.00 78.08  ? 267 LYS   B NZ   1 
ATOM   8785 H H    . LYS   B 1 282 ? 16.057  -20.715 44.262  1.00 50.95  ? 267 LYS   B H    1 
ATOM   8786 H HA   . LYS   B 1 282 ? 16.195  -21.283 46.805  1.00 57.10  ? 267 LYS   B HA   1 
ATOM   8787 H HB2  . LYS   B 1 282 ? 17.623  -19.716 45.845  1.00 68.05  ? 267 LYS   B HB2  1 
ATOM   8788 H HB3  . LYS   B 1 282 ? 16.394  -18.739 45.602  1.00 68.05  ? 267 LYS   B HB3  1 
ATOM   8789 H HG2  . LYS   B 1 282 ? 17.746  -18.125 47.463  1.00 75.83  ? 267 LYS   B HG2  1 
ATOM   8790 H HG3  . LYS   B 1 282 ? 16.212  -18.308 47.835  1.00 75.83  ? 267 LYS   B HG3  1 
ATOM   8791 H HD2  . LYS   B 1 282 ? 16.607  -20.286 48.865  1.00 84.79  ? 267 LYS   B HD2  1 
ATOM   8792 H HD3  . LYS   B 1 282 ? 18.064  -20.394 48.238  1.00 84.79  ? 267 LYS   B HD3  1 
ATOM   8793 H HE2  . LYS   B 1 282 ? 17.412  -18.394 50.114  1.00 82.69  ? 267 LYS   B HE2  1 
ATOM   8794 H HE3  . LYS   B 1 282 ? 18.033  -19.788 50.559  1.00 82.69  ? 267 LYS   B HE3  1 
ATOM   8795 H HZ1  . LYS   B 1 282 ? 19.673  -18.229 50.353  1.00 93.70  ? 267 LYS   B HZ1  1 
ATOM   8796 H HZ2  . LYS   B 1 282 ? 19.900  -19.255 49.355  1.00 93.70  ? 267 LYS   B HZ2  1 
ATOM   8797 H HZ3  . LYS   B 1 282 ? 19.335  -17.979 48.967  1.00 93.70  ? 267 LYS   B HZ3  1 
ATOM   8798 N N    . MET   B 1 283 ? 13.536  -19.747 45.964  1.00 41.27  ? 268 MET   B N    1 
ATOM   8799 C CA   . MET   B 1 283 ? 12.245  -19.301 46.472  1.00 36.42  ? 268 MET   B CA   1 
ATOM   8800 C C    . MET   B 1 283 ? 11.378  -20.475 46.902  1.00 44.46  ? 268 MET   B C    1 
ATOM   8801 O O    . MET   B 1 283 ? 10.523  -20.321 47.781  1.00 40.81  ? 268 MET   B O    1 
ATOM   8802 C CB   . MET   B 1 283 ? 11.524  -18.471 45.414  1.00 45.10  ? 268 MET   B CB   1 
ATOM   8803 C CG   . MET   B 1 283 ? 12.132  -17.081 45.187  1.00 42.08  ? 268 MET   B CG   1 
ATOM   8804 S SD   . MET   B 1 283 ? 12.134  -16.058 46.678  1.00 41.38  ? 268 MET   B SD   1 
ATOM   8805 C CE   . MET   B 1 283 ? 10.413  -16.144 47.158  1.00 36.69  ? 268 MET   B CE   1 
ATOM   8806 H H    . MET   B 1 283 ? 13.628  -19.688 45.111  1.00 49.52  ? 268 MET   B H    1 
ATOM   8807 H HA   . MET   B 1 283 ? 12.398  -18.731 47.242  1.00 43.71  ? 268 MET   B HA   1 
ATOM   8808 H HB2  . MET   B 1 283 ? 11.556  -18.948 44.570  1.00 54.13  ? 268 MET   B HB2  1 
ATOM   8809 H HB3  . MET   B 1 283 ? 10.602  -18.348 45.691  1.00 54.13  ? 268 MET   B HB3  1 
ATOM   8810 H HG2  . MET   B 1 283 ? 13.051  -17.183 44.893  1.00 50.50  ? 268 MET   B HG2  1 
ATOM   8811 H HG3  . MET   B 1 283 ? 11.616  -16.618 44.508  1.00 50.50  ? 268 MET   B HG3  1 
ATOM   8812 H HE1  . MET   B 1 283 ? 10.245  -15.486 47.850  1.00 44.03  ? 268 MET   B HE1  1 
ATOM   8813 H HE2  . MET   B 1 283 ? 9.860   -15.957 46.383  1.00 44.03  ? 268 MET   B HE2  1 
ATOM   8814 H HE3  . MET   B 1 283 ? 10.223  -17.034 47.494  1.00 44.03  ? 268 MET   B HE3  1 
ATOM   8815 N N    . LEU   B 1 284 ? 11.573  -21.648 46.301  1.00 39.63  ? 269 LEU   B N    1 
ATOM   8816 C CA   . LEU   B 1 284 ? 10.842  -22.823 46.753  1.00 38.42  ? 269 LEU   B CA   1 
ATOM   8817 C C    . LEU   B 1 284 ? 11.207  -23.216 48.175  1.00 39.50  ? 269 LEU   B C    1 
ATOM   8818 O O    . LEU   B 1 284 ? 10.495  -24.028 48.776  1.00 40.56  ? 269 LEU   B O    1 
ATOM   8819 C CB   . LEU   B 1 284 ? 11.094  -23.985 45.794  1.00 40.64  ? 269 LEU   B CB   1 
ATOM   8820 C CG   . LEU   B 1 284 ? 10.349  -23.830 44.466  1.00 36.83  ? 269 LEU   B CG   1 
ATOM   8821 C CD1  . LEU   B 1 284 ? 10.944  -24.720 43.395  1.00 35.05  ? 269 LEU   B CD1  1 
ATOM   8822 C CD2  . LEU   B 1 284 ? 8.864   -24.129 44.657  1.00 34.05  ? 269 LEU   B CD2  1 
ATOM   8823 H H    . LEU   B 1 284 ? 12.112  -21.784 45.645  1.00 47.55  ? 269 LEU   B H    1 
ATOM   8824 H HA   . LEU   B 1 284 ? 9.891   -22.634 46.739  1.00 46.10  ? 269 LEU   B HA   1 
ATOM   8825 H HB2  . LEU   B 1 284 ? 12.043  -24.034 45.602  1.00 48.77  ? 269 LEU   B HB2  1 
ATOM   8826 H HB3  . LEU   B 1 284 ? 10.796  -24.808 46.212  1.00 48.77  ? 269 LEU   B HB3  1 
ATOM   8827 H HG   . LEU   B 1 284 ? 10.439  -22.913 44.162  1.00 44.19  ? 269 LEU   B HG   1 
ATOM   8828 H HD11 . LEU   B 1 284 ? 10.444  -24.602 42.572  1.00 42.06  ? 269 LEU   B HD11 1 
ATOM   8829 H HD12 . LEU   B 1 284 ? 11.871  -24.472 43.257  1.00 42.06  ? 269 LEU   B HD12 1 
ATOM   8830 H HD13 . LEU   B 1 284 ? 10.889  -25.644 43.685  1.00 42.06  ? 269 LEU   B HD13 1 
ATOM   8831 H HD21 . LEU   B 1 284 ? 8.426   -24.121 43.791  1.00 40.86  ? 269 LEU   B HD21 1 
ATOM   8832 H HD22 . LEU   B 1 284 ? 8.768   -25.002 45.068  1.00 40.86  ? 269 LEU   B HD22 1 
ATOM   8833 H HD23 . LEU   B 1 284 ? 8.476   -23.449 45.230  1.00 40.86  ? 269 LEU   B HD23 1 
ATOM   8834 N N    . SER   B 1 285 ? 12.291  -22.665 48.724  1.00 39.33  ? 270 SER   B N    1 
ATOM   8835 C CA   . SER   B 1 285 ? 12.620  -22.848 50.129  1.00 39.67  ? 270 SER   B CA   1 
ATOM   8836 C C    . SER   B 1 285 ? 11.824  -21.930 51.045  1.00 39.22  ? 270 SER   B C    1 
ATOM   8837 O O    . SER   B 1 285 ? 11.841  -22.132 52.264  1.00 42.79  ? 270 SER   B O    1 
ATOM   8838 C CB   . SER   B 1 285 ? 14.110  -22.591 50.358  1.00 44.51  ? 270 SER   B CB   1 
ATOM   8839 O OG   . SER   B 1 285 ? 14.900  -23.291 49.419  1.00 61.70  ? 270 SER   B OG   1 
ATOM   8840 H H    . SER   B 1 285 ? 12.855  -22.177 48.296  1.00 47.19  ? 270 SER   B H    1 
ATOM   8841 H HA   . SER   B 1 285 ? 12.426  -23.768 50.371  1.00 47.60  ? 270 SER   B HA   1 
ATOM   8842 H HB2  . SER   B 1 285 ? 14.282  -21.640 50.266  1.00 53.41  ? 270 SER   B HB2  1 
ATOM   8843 H HB3  . SER   B 1 285 ? 14.347  -22.886 51.251  1.00 53.41  ? 270 SER   B HB3  1 
ATOM   8844 H HG   . SER   B 1 285 ? 15.713  -23.115 49.539  1.00 74.04  ? 270 SER   B HG   1 
ATOM   8845 N N    . HIS   B 1 286 ? 11.136  -20.936 50.496  1.00 37.63  ? 271 HIS   B N    1 
ATOM   8846 C CA   . HIS   B 1 286 ? 10.517  -19.907 51.319  1.00 37.47  ? 271 HIS   B CA   1 
ATOM   8847 C C    . HIS   B 1 286 ? 9.338   -20.458 52.111  1.00 37.40  ? 271 HIS   B C    1 
ATOM   8848 O O    . HIS   B 1 286 ? 8.541   -21.250 51.605  1.00 36.52  ? 271 HIS   B O    1 
ATOM   8849 C CB   . HIS   B 1 286 ? 10.050  -18.749 50.444  1.00 38.89  ? 271 HIS   B CB   1 
ATOM   8850 C CG   . HIS   B 1 286 ? 9.719   -17.512 51.212  1.00 38.04  ? 271 HIS   B CG   1 
ATOM   8851 N ND1  . HIS   B 1 286 ? 8.509   -17.328 51.843  1.00 38.76  ? 271 HIS   B ND1  1 
ATOM   8852 C CD2  . HIS   B 1 286 ? 10.443  -16.391 51.447  1.00 39.81  ? 271 HIS   B CD2  1 
ATOM   8853 C CE1  . HIS   B 1 286 ? 8.499   -16.147 52.436  1.00 43.92  ? 271 HIS   B CE1  1 
ATOM   8854 N NE2  . HIS   B 1 286 ? 9.661   -15.558 52.211  1.00 40.68  ? 271 HIS   B NE2  1 
ATOM   8855 H H    . HIS   B 1 286 ? 11.014  -20.834 49.651  1.00 45.16  ? 271 HIS   B H    1 
ATOM   8856 H HA   . HIS   B 1 286 ? 11.173  -19.580 51.955  1.00 44.97  ? 271 HIS   B HA   1 
ATOM   8857 H HB2  . HIS   B 1 286 ? 10.755  -18.529 49.815  1.00 46.67  ? 271 HIS   B HB2  1 
ATOM   8858 H HB3  . HIS   B 1 286 ? 9.252   -19.023 49.964  1.00 46.67  ? 271 HIS   B HB3  1 
ATOM   8859 H HD2  . HIS   B 1 286 ? 11.306  -16.218 51.148  1.00 47.78  ? 271 HIS   B HD2  1 
ATOM   8860 H HE1  . HIS   B 1 286 ? 7.795   -15.790 52.927  1.00 52.71  ? 271 HIS   B HE1  1 
ATOM   8861 H HE2  . HIS   B 1 286 ? 9.891   -14.781 52.497  1.00 48.82  ? 271 HIS   B HE2  1 
ATOM   8862 N N    . GLN   B 1 287 ? 9.207   -19.983 53.353  1.00 41.89  ? 272 GLN   B N    1 
ATOM   8863 C CA   . GLN   B 1 287 ? 8.157   -20.470 54.245  1.00 40.07  ? 272 GLN   B CA   1 
ATOM   8864 C C    . GLN   B 1 287 ? 6.791   -20.477 53.565  1.00 42.70  ? 272 GLN   B C    1 
ATOM   8865 O O    . GLN   B 1 287 ? 6.018   -21.427 53.726  1.00 41.31  ? 272 GLN   B O    1 
ATOM   8866 C CB   . GLN   B 1 287 ? 8.139   -19.607 55.511  1.00 46.54  ? 272 GLN   B CB   1 
ATOM   8867 C CG   . GLN   B 1 287 ? 7.006   -19.890 56.483  1.00 49.58  ? 272 GLN   B CG   1 
ATOM   8868 C CD   . GLN   B 1 287 ? 7.043   -18.977 57.715  1.00 60.91  ? 272 GLN   B CD   1 
ATOM   8869 O OE1  . GLN   B 1 287 ? 7.903   -18.099 57.831  1.00 59.45  ? 272 GLN   B OE1  1 
ATOM   8870 N NE2  . GLN   B 1 287 ? 6.106   -19.186 58.637  1.00 54.44  ? 272 GLN   B NE2  1 
ATOM   8871 H H    . GLN   B 1 287 ? 9.712   -19.381 53.701  1.00 50.27  ? 272 GLN   B H    1 
ATOM   8872 H HA   . GLN   B 1 287 ? 8.350   -21.386 54.499  1.00 48.09  ? 272 GLN   B HA   1 
ATOM   8873 H HB2  . GLN   B 1 287 ? 8.971   -19.751 55.990  1.00 55.85  ? 272 GLN   B HB2  1 
ATOM   8874 H HB3  . GLN   B 1 287 ? 8.065   -18.678 55.246  1.00 55.85  ? 272 GLN   B HB3  1 
ATOM   8875 H HG2  . GLN   B 1 287 ? 6.159   -19.751 56.030  1.00 59.49  ? 272 GLN   B HG2  1 
ATOM   8876 H HG3  . GLN   B 1 287 ? 7.072   -20.809 56.787  1.00 59.49  ? 272 GLN   B HG3  1 
ATOM   8877 H HE21 . GLN   B 1 287 ? 5.522   -19.807 58.524  1.00 65.33  ? 272 GLN   B HE21 1 
ATOM   8878 H HE22 . GLN   B 1 287 ? 6.085   -18.700 59.347  1.00 65.33  ? 272 GLN   B HE22 1 
ATOM   8879 N N    . LEU   B 1 288 ? 6.486   -19.442 52.774  1.00 40.66  ? 273 LEU   B N    1 
ATOM   8880 C CA   . LEU   B 1 288 ? 5.143   -19.319 52.216  1.00 37.69  ? 273 LEU   B CA   1 
ATOM   8881 C C    . LEU   B 1 288 ? 4.795   -20.501 51.324  1.00 34.80  ? 273 LEU   B C    1 
ATOM   8882 O O    . LEU   B 1 288 ? 3.676   -21.024 51.382  1.00 38.21  ? 273 LEU   B O    1 
ATOM   8883 C CB   . LEU   B 1 288 ? 5.003   -18.024 51.420  1.00 33.90  ? 273 LEU   B CB   1 
ATOM   8884 C CG   . LEU   B 1 288 ? 3.562   -17.749 50.973  1.00 32.75  ? 273 LEU   B CG   1 
ATOM   8885 C CD1  . LEU   B 1 288 ? 2.702   -17.309 52.173  1.00 33.67  ? 273 LEU   B CD1  1 
ATOM   8886 C CD2  . LEU   B 1 288 ? 3.520   -16.719 49.864  1.00 39.82  ? 273 LEU   B CD2  1 
ATOM   8887 H H    . LEU   B 1 288 ? 7.029   -18.813 52.551  1.00 48.79  ? 273 LEU   B H    1 
ATOM   8888 H HA   . LEU   B 1 288 ? 4.519   -19.293 52.958  1.00 45.23  ? 273 LEU   B HA   1 
ATOM   8889 H HB2  . LEU   B 1 288 ? 5.292   -17.282 51.973  1.00 40.69  ? 273 LEU   B HB2  1 
ATOM   8890 H HB3  . LEU   B 1 288 ? 5.557   -18.081 50.626  1.00 40.69  ? 273 LEU   B HB3  1 
ATOM   8891 H HG   . LEU   B 1 288 ? 3.184   -18.568 50.617  1.00 39.30  ? 273 LEU   B HG   1 
ATOM   8892 H HD11 . LEU   B 1 288 ? 1.830   -17.031 51.851  1.00 40.40  ? 273 LEU   B HD11 1 
ATOM   8893 H HD12 . LEU   B 1 288 ? 2.606   -18.056 52.784  1.00 40.40  ? 273 LEU   B HD12 1 
ATOM   8894 H HD13 . LEU   B 1 288 ? 3.140   -16.568 52.621  1.00 40.40  ? 273 LEU   B HD13 1 
ATOM   8895 H HD21 . LEU   B 1 288 ? 2.597   -16.575 49.603  1.00 47.79  ? 273 LEU   B HD21 1 
ATOM   8896 H HD22 . LEU   B 1 288 ? 3.905   -15.890 50.188  1.00 47.79  ? 273 LEU   B HD22 1 
ATOM   8897 H HD23 . LEU   B 1 288 ? 4.030   -17.048 49.108  1.00 47.79  ? 273 LEU   B HD23 1 
ATOM   8898 N N    . VAL   B 1 289 ? 5.726   -20.918 50.465  1.00 34.07  ? 274 VAL   B N    1 
ATOM   8899 C CA   . VAL   B 1 289 ? 5.454   -22.002 49.528  1.00 36.33  ? 274 VAL   B CA   1 
ATOM   8900 C C    . VAL   B 1 289 ? 5.943   -23.350 50.036  1.00 38.88  ? 274 VAL   B C    1 
ATOM   8901 O O    . VAL   B 1 289 ? 5.794   -24.356 49.333  1.00 38.90  ? 274 VAL   B O    1 
ATOM   8902 C CB   . VAL   B 1 289 ? 6.061   -21.698 48.143  1.00 32.86  ? 274 VAL   B CB   1 
ATOM   8903 C CG1  . VAL   B 1 289 ? 5.331   -20.535 47.502  1.00 34.23  ? 274 VAL   B CG1  1 
ATOM   8904 C CG2  . VAL   B 1 289 ? 7.547   -21.405 48.253  1.00 33.21  ? 274 VAL   B CG2  1 
ATOM   8905 H H    . VAL   B 1 289 ? 6.519   -20.589 50.409  1.00 40.88  ? 274 VAL   B H    1 
ATOM   8906 H HA   . VAL   B 1 289 ? 4.492   -22.071 49.424  1.00 43.59  ? 274 VAL   B HA   1 
ATOM   8907 H HB   . VAL   B 1 289 ? 5.959   -22.479 47.576  1.00 39.43  ? 274 VAL   B HB   1 
ATOM   8908 H HG11 . VAL   B 1 289 ? 5.718   -20.361 46.630  1.00 41.08  ? 274 VAL   B HG11 1 
ATOM   8909 H HG12 . VAL   B 1 289 ? 4.394   -20.764 47.409  1.00 41.08  ? 274 VAL   B HG12 1 
ATOM   8910 H HG13 . VAL   B 1 289 ? 5.426   -19.753 48.068  1.00 41.08  ? 274 VAL   B HG13 1 
ATOM   8911 H HG21 . VAL   B 1 289 ? 7.925   -21.351 47.361  1.00 39.85  ? 274 VAL   B HG21 1 
ATOM   8912 H HG22 . VAL   B 1 289 ? 7.668   -20.560 48.715  1.00 39.85  ? 274 VAL   B HG22 1 
ATOM   8913 H HG23 . VAL   B 1 289 ? 7.974   -22.119 48.751  1.00 39.85  ? 274 VAL   B HG23 1 
ATOM   8914 N N    . SER   B 1 290 ? 6.509   -23.402 51.245  1.00 43.96  ? 275 SER   B N    1 
ATOM   8915 C CA   . SER   B 1 290 ? 7.010   -24.635 51.834  1.00 45.37  ? 275 SER   B CA   1 
ATOM   8916 C C    . SER   B 1 290 ? 6.036   -25.273 52.815  1.00 49.79  ? 275 SER   B C    1 
ATOM   8917 O O    . SER   B 1 290 ? 6.178   -26.462 53.114  1.00 49.71  ? 275 SER   B O    1 
ATOM   8918 C CB   . SER   B 1 290 ? 8.331   -24.376 52.575  1.00 42.88  ? 275 SER   B CB   1 
ATOM   8919 O OG   . SER   B 1 290 ? 9.282   -23.775 51.720  1.00 54.74  ? 275 SER   B OG   1 
ATOM   8920 H H    . SER   B 1 290 ? 6.614   -22.716 51.753  1.00 52.76  ? 275 SER   B H    1 
ATOM   8921 H HA   . SER   B 1 290 ? 7.180   -25.266 51.117  1.00 54.44  ? 275 SER   B HA   1 
ATOM   8922 H HB2  . SER   B 1 290 ? 8.162   -23.783 53.323  1.00 51.45  ? 275 SER   B HB2  1 
ATOM   8923 H HB3  . SER   B 1 290 ? 8.684   -25.221 52.894  1.00 51.45  ? 275 SER   B HB3  1 
ATOM   8924 H HG   . SER   B 1 290 ? 9.006   -23.023 51.466  1.00 65.69  ? 275 SER   B HG   1 
ATOM   8925 N N    . GLN   B 1 291 ? 5.062   -24.517 53.319  1.00 52.40  ? 276 GLN   B N    1 
ATOM   8926 C CA   . GLN   B 1 291 ? 4.195   -25.016 54.375  1.00 49.38  ? 276 GLN   B CA   1 
ATOM   8927 C C    . GLN   B 1 291 ? 3.408   -26.235 53.896  1.00 41.52  ? 276 GLN   B C    1 
ATOM   8928 O O    . GLN   B 1 291 ? 3.143   -26.389 52.699  1.00 43.02  ? 276 GLN   B O    1 
ATOM   8929 C CB   . GLN   B 1 291 ? 3.237   -23.917 54.849  1.00 45.61  ? 276 GLN   B CB   1 
ATOM   8930 C CG   . GLN   B 1 291 ? 2.407   -23.256 53.761  1.00 36.50  ? 276 GLN   B CG   1 
ATOM   8931 C CD   . GLN   B 1 291 ? 1.614   -22.045 54.266  1.00 43.45  ? 276 GLN   B CD   1 
ATOM   8932 O OE1  . GLN   B 1 291 ? 0.995   -22.093 55.331  1.00 39.90  ? 276 GLN   B OE1  1 
ATOM   8933 N NE2  . GLN   B 1 291 ? 1.635   -20.954 53.499  1.00 35.31  ? 276 GLN   B NE2  1 
ATOM   8934 H H    . GLN   B 1 291 ? 4.885   -23.714 53.067  1.00 62.88  ? 276 GLN   B H    1 
ATOM   8935 H HA   . GLN   B 1 291 ? 4.739   -25.291 55.130  1.00 59.25  ? 276 GLN   B HA   1 
ATOM   8936 H HB2  . GLN   B 1 291 ? 2.618   -24.307 55.487  1.00 54.73  ? 276 GLN   B HB2  1 
ATOM   8937 H HB3  . GLN   B 1 291 ? 3.759   -23.221 55.277  1.00 54.73  ? 276 GLN   B HB3  1 
ATOM   8938 H HG2  . GLN   B 1 291 ? 2.998   -22.952 53.054  1.00 43.80  ? 276 GLN   B HG2  1 
ATOM   8939 H HG3  . GLN   B 1 291 ? 1.774   -23.902 53.410  1.00 43.80  ? 276 GLN   B HG3  1 
ATOM   8940 H HE21 . GLN   B 1 291 ? 2.079   -20.954 52.763  1.00 42.37  ? 276 GLN   B HE21 1 
ATOM   8941 H HE22 . GLN   B 1 291 ? 1.205   -20.250 53.742  1.00 42.37  ? 276 GLN   B HE22 1 
ATOM   8942 N N    . PRO   B 1 292 ? 3.034   -27.127 54.807  1.00 40.86  ? 277 PRO   B N    1 
ATOM   8943 C CA   . PRO   B 1 292 ? 2.137   -28.225 54.439  1.00 39.68  ? 277 PRO   B CA   1 
ATOM   8944 C C    . PRO   B 1 292 ? 0.748   -27.698 54.113  1.00 45.75  ? 277 PRO   B C    1 
ATOM   8945 O O    . PRO   B 1 292 ? 0.444   -26.513 54.265  1.00 53.04  ? 277 PRO   B O    1 
ATOM   8946 C CB   . PRO   B 1 292 ? 2.128   -29.116 55.684  1.00 46.30  ? 277 PRO   B CB   1 
ATOM   8947 C CG   . PRO   B 1 292 ? 2.475   -28.190 56.811  1.00 46.19  ? 277 PRO   B CG   1 
ATOM   8948 C CD   . PRO   B 1 292 ? 3.426   -27.186 56.229  1.00 45.60  ? 277 PRO   B CD   1 
ATOM   8949 H HA   . PRO   B 1 292 ? 2.485   -28.730 53.687  1.00 47.61  ? 277 PRO   B HA   1 
ATOM   8950 H HB2  . PRO   B 1 292 ? 1.247   -29.503 55.810  1.00 55.56  ? 277 PRO   B HB2  1 
ATOM   8951 H HB3  . PRO   B 1 292 ? 2.789   -29.819 55.594  1.00 55.56  ? 277 PRO   B HB3  1 
ATOM   8952 H HG2  . PRO   B 1 292 ? 1.672   -27.754 57.137  1.00 55.43  ? 277 PRO   B HG2  1 
ATOM   8953 H HG3  . PRO   B 1 292 ? 2.897   -28.689 57.528  1.00 55.43  ? 277 PRO   B HG3  1 
ATOM   8954 H HD2  . PRO   B 1 292 ? 3.316   -26.321 56.654  1.00 54.72  ? 277 PRO   B HD2  1 
ATOM   8955 H HD3  . PRO   B 1 292 ? 4.344   -27.487 56.322  1.00 54.72  ? 277 PRO   B HD3  1 
ATOM   8956 N N    . GLY   B 1 293 ? -0.105  -28.608 53.648  1.00 44.79  ? 278 GLY   B N    1 
ATOM   8957 C CA   . GLY   B 1 293 ? -1.485  -28.284 53.368  1.00 44.82  ? 278 GLY   B CA   1 
ATOM   8958 C C    . GLY   B 1 293 ? -1.751  -27.616 52.039  1.00 39.50  ? 278 GLY   B C    1 
ATOM   8959 O O    . GLY   B 1 293 ? -2.921  -27.439 51.678  1.00 47.83  ? 278 GLY   B O    1 
ATOM   8960 H H    . GLY   B 1 293 ? 0.102   -29.427 53.487  1.00 53.75  ? 278 GLY   B H    1 
ATOM   8961 H HA2  . GLY   B 1 293 ? -2.003  -29.105 53.390  1.00 53.79  ? 278 GLY   B HA2  1 
ATOM   8962 H HA3  . GLY   B 1 293 ? -1.808  -27.689 54.063  1.00 53.79  ? 278 GLY   B HA3  1 
ATOM   8963 N N    . LEU   B 1 294 ? -0.721  -27.238 51.287  1.00 45.14  ? 279 LEU   B N    1 
ATOM   8964 C CA   . LEU   B 1 294 ? -0.927  -26.639 49.971  1.00 37.38  ? 279 LEU   B CA   1 
ATOM   8965 C C    . LEU   B 1 294 ? -1.160  -27.753 48.959  1.00 39.92  ? 279 LEU   B C    1 
ATOM   8966 O O    . LEU   B 1 294 ? -0.260  -28.557 48.697  1.00 46.03  ? 279 LEU   B O    1 
ATOM   8967 C CB   . LEU   B 1 294 ? 0.270   -25.781 49.583  1.00 37.28  ? 279 LEU   B CB   1 
ATOM   8968 C CG   . LEU   B 1 294 ? 0.575   -24.606 50.518  1.00 37.73  ? 279 LEU   B CG   1 
ATOM   8969 C CD1  . LEU   B 1 294 ? 1.780   -23.817 50.030  1.00 36.16  ? 279 LEU   B CD1  1 
ATOM   8970 C CD2  . LEU   B 1 294 ? -0.635  -23.695 50.649  1.00 36.95  ? 279 LEU   B CD2  1 
ATOM   8971 H H    . LEU   B 1 294 ? 0.104   -27.317 51.516  1.00 54.17  ? 279 LEU   B H    1 
ATOM   8972 H HA   . LEU   B 1 294 ? -1.713  -26.071 49.992  1.00 44.85  ? 279 LEU   B HA   1 
ATOM   8973 H HB2  . LEU   B 1 294 ? 1.057   -26.347 49.565  1.00 44.74  ? 279 LEU   B HB2  1 
ATOM   8974 H HB3  . LEU   B 1 294 ? 0.106   -25.412 48.700  1.00 44.74  ? 279 LEU   B HB3  1 
ATOM   8975 H HG   . LEU   B 1 294 ? 0.785   -24.961 51.396  1.00 45.27  ? 279 LEU   B HG   1 
ATOM   8976 H HD11 . LEU   B 1 294 ? 1.951   -23.088 50.647  1.00 43.39  ? 279 LEU   B HD11 1 
ATOM   8977 H HD12 . LEU   B 1 294 ? 2.550   -24.406 49.994  1.00 43.39  ? 279 LEU   B HD12 1 
ATOM   8978 H HD13 . LEU   B 1 294 ? 1.591   -23.465 49.147  1.00 43.39  ? 279 LEU   B HD13 1 
ATOM   8979 H HD21 . LEU   B 1 294 ? -0.371  -22.885 51.113  1.00 44.34  ? 279 LEU   B HD21 1 
ATOM   8980 H HD22 . LEU   B 1 294 ? -0.963  -23.477 49.763  1.00 44.34  ? 279 LEU   B HD22 1 
ATOM   8981 H HD23 . LEU   B 1 294 ? -1.324  -24.156 51.153  1.00 44.34  ? 279 LEU   B HD23 1 
ATOM   8982 N N    . ASN   B 1 295 ? -2.362  -27.801 48.385  1.00 38.87  ? 280 ASN   B N    1 
ATOM   8983 C CA   . ASN   B 1 295 ? -2.697  -28.826 47.404  1.00 37.49  ? 280 ASN   B CA   1 
ATOM   8984 C C    . ASN   B 1 295 ? -3.818  -28.321 46.507  1.00 32.86  ? 280 ASN   B C    1 
ATOM   8985 O O    . ASN   B 1 295 ? -4.429  -27.282 46.766  1.00 33.03  ? 280 ASN   B O    1 
ATOM   8986 C CB   . ASN   B 1 295 ? -3.105  -30.133 48.086  1.00 34.89  ? 280 ASN   B CB   1 
ATOM   8987 C CG   . ASN   B 1 295 ? -4.297  -29.955 49.001  1.00 35.75  ? 280 ASN   B CG   1 
ATOM   8988 O OD1  . ASN   B 1 295 ? -5.421  -29.753 48.546  1.00 37.77  ? 280 ASN   B OD1  1 
ATOM   8989 N ND2  . ASN   B 1 295 ? -4.055  -30.028 50.299  1.00 39.99  ? 280 ASN   B ND2  1 
ATOM   8990 H H    . ASN   B 1 295 ? -3.001  -27.249 48.548  1.00 46.65  ? 280 ASN   B H    1 
ATOM   8991 H HA   . ASN   B 1 295 ? -1.918  -28.988 46.849  1.00 44.99  ? 280 ASN   B HA   1 
ATOM   8992 H HB2  . ASN   B 1 295 ? -3.341  -30.785 47.408  1.00 41.87  ? 280 ASN   B HB2  1 
ATOM   8993 H HB3  . ASN   B 1 295 ? -2.363  -30.459 48.618  1.00 41.87  ? 280 ASN   B HB3  1 
ATOM   8994 H HD21 . ASN   B 1 295 ? -4.699  -29.934 50.862  1.00 47.99  ? 280 ASN   B HD21 1 
ATOM   8995 H HD22 . ASN   B 1 295 ? -3.255  -30.170 50.580  1.00 47.99  ? 280 ASN   B HD22 1 
ATOM   8996 N N    . ARG   B 1 296 ? -4.097  -29.090 45.454  1.00 33.41  ? 281 ARG   B N    1 
ATOM   8997 C CA   . ARG   B 1 296 ? -5.088  -28.676 44.468  1.00 32.42  ? 281 ARG   B CA   1 
ATOM   8998 C C    . ARG   B 1 296 ? -6.489  -28.563 45.054  1.00 33.26  ? 281 ARG   B C    1 
ATOM   8999 O O    . ARG   B 1 296 ? -7.349  -27.918 44.444  1.00 33.06  ? 281 ARG   B O    1 
ATOM   9000 C CB   . ARG   B 1 296 ? -5.099  -29.651 43.290  1.00 32.57  ? 281 ARG   B CB   1 
ATOM   9001 C CG   . ARG   B 1 296 ? -5.601  -31.059 43.637  1.00 35.90  ? 281 ARG   B CG   1 
ATOM   9002 C CD   . ARG   B 1 296 ? -5.354  -32.036 42.491  1.00 34.14  ? 281 ARG   B CD   1 
ATOM   9003 N NE   . ARG   B 1 296 ? -5.808  -33.390 42.797  1.00 40.95  ? 281 ARG   B NE   1 
ATOM   9004 C CZ   . ARG   B 1 296 ? -7.020  -33.855 42.524  1.00 36.39  ? 281 ARG   B CZ   1 
ATOM   9005 N NH1  . ARG   B 1 296 ? -7.939  -33.096 41.951  1.00 36.11  ? 281 ARG   B NH1  1 
ATOM   9006 N NH2  . ARG   B 1 296 ? -7.320  -35.112 42.843  1.00 39.34  ? 281 ARG   B NH2  1 
ATOM   9007 H H    . ARG   B 1 296 ? -3.728  -29.849 45.290  1.00 40.09  ? 281 ARG   B H    1 
ATOM   9008 H HA   . ARG   B 1 296 ? -4.837  -27.800 44.136  1.00 38.91  ? 281 ARG   B HA   1 
ATOM   9009 H HB2  . ARG   B 1 296 ? -5.678  -29.295 42.599  1.00 39.09  ? 281 ARG   B HB2  1 
ATOM   9010 H HB3  . ARG   B 1 296 ? -4.194  -29.737 42.953  1.00 39.09  ? 281 ARG   B HB3  1 
ATOM   9011 H HG2  . ARG   B 1 296 ? -5.133  -31.383 44.422  1.00 43.08  ? 281 ARG   B HG2  1 
ATOM   9012 H HG3  . ARG   B 1 296 ? -6.555  -31.026 43.811  1.00 43.08  ? 281 ARG   B HG3  1 
ATOM   9013 H HD2  . ARG   B 1 296 ? -5.833  -31.729 41.705  1.00 40.97  ? 281 ARG   B HD2  1 
ATOM   9014 H HD3  . ARG   B 1 296 ? -4.403  -32.073 42.307  1.00 40.97  ? 281 ARG   B HD3  1 
ATOM   9015 H HE   . ARG   B 1 296 ? -5.252  -33.922 43.180  1.00 49.14  ? 281 ARG   B HE   1 
ATOM   9016 H HH11 . ARG   B 1 296 ? -7.758  -32.281 41.746  1.00 43.33  ? 281 ARG   B HH11 1 
ATOM   9017 H HH12 . ARG   B 1 296 ? -8.719  -33.418 41.783  1.00 43.33  ? 281 ARG   B HH12 1 
ATOM   9018 H HH21 . ARG   B 1 296 ? -6.731  -35.612 43.221  1.00 47.20  ? 281 ARG   B HH21 1 
ATOM   9019 H HH22 . ARG   B 1 296 ? -8.102  -35.425 42.671  1.00 47.20  ? 281 ARG   B HH22 1 
ATOM   9020 N N    . GLY   B 1 297 ? -6.749  -29.180 46.207  1.00 34.39  ? 282 GLY   B N    1 
ATOM   9021 C CA   . GLY   B 1 297 ? -8.035  -28.989 46.854  1.00 35.42  ? 282 GLY   B CA   1 
ATOM   9022 C C    . GLY   B 1 297 ? -8.340  -27.530 47.131  1.00 34.97  ? 282 GLY   B C    1 
ATOM   9023 O O    . GLY   B 1 297 ? -9.505  -27.122 47.138  1.00 35.62  ? 282 GLY   B O    1 
ATOM   9024 H H    . GLY   B 1 297 ? -6.207  -29.703 46.624  1.00 41.27  ? 282 GLY   B H    1 
ATOM   9025 H HA2  . GLY   B 1 297 ? -8.736  -29.343 46.284  1.00 42.50  ? 282 GLY   B HA2  1 
ATOM   9026 H HA3  . GLY   B 1 297 ? -8.043  -29.467 47.698  1.00 42.50  ? 282 GLY   B HA3  1 
ATOM   9027 N N    . LEU   B 1 298 ? -7.302  -26.720 47.354  1.00 37.66  ? 283 LEU   B N    1 
ATOM   9028 C CA   . LEU   B 1 298 ? -7.508  -25.293 47.586  1.00 33.66  ? 283 LEU   B CA   1 
ATOM   9029 C C    . LEU   B 1 298 ? -8.135  -24.626 46.373  1.00 33.99  ? 283 LEU   B C    1 
ATOM   9030 O O    . LEU   B 1 298 ? -8.999  -23.753 46.513  1.00 35.90  ? 283 LEU   B O    1 
ATOM   9031 C CB   . LEU   B 1 298 ? -6.181  -24.623 47.931  1.00 32.86  ? 283 LEU   B CB   1 
ATOM   9032 C CG   . LEU   B 1 298 ? -5.572  -25.068 49.258  1.00 33.77  ? 283 LEU   B CG   1 
ATOM   9033 C CD1  . LEU   B 1 298 ? -4.219  -24.427 49.457  1.00 36.71  ? 283 LEU   B CD1  1 
ATOM   9034 C CD2  . LEU   B 1 298 ? -6.492  -24.727 50.415  1.00 38.18  ? 283 LEU   B CD2  1 
ATOM   9035 H H    . LEU   B 1 298 ? -6.479  -26.970 47.375  1.00 45.20  ? 283 LEU   B H    1 
ATOM   9036 H HA   . LEU   B 1 298 ? -8.109  -25.182 48.339  1.00 40.39  ? 283 LEU   B HA   1 
ATOM   9037 H HB2  . LEU   B 1 298 ? -5.541  -24.828 47.231  1.00 39.43  ? 283 LEU   B HB2  1 
ATOM   9038 H HB3  . LEU   B 1 298 ? -6.323  -23.665 47.980  1.00 39.43  ? 283 LEU   B HB3  1 
ATOM   9039 H HG   . LEU   B 1 298 ? -5.456  -26.031 49.242  1.00 40.53  ? 283 LEU   B HG   1 
ATOM   9040 H HD11 . LEU   B 1 298 ? -3.847  -24.731 50.299  1.00 44.05  ? 283 LEU   B HD11 1 
ATOM   9041 H HD12 . LEU   B 1 298 ? -3.637  -24.686 48.725  1.00 44.05  ? 283 LEU   B HD12 1 
ATOM   9042 H HD13 . LEU   B 1 298 ? -4.325  -23.463 49.470  1.00 44.05  ? 283 LEU   B HD13 1 
ATOM   9043 H HD21 . LEU   B 1 298 ? -6.005  -24.832 51.247  1.00 45.81  ? 283 LEU   B HD21 1 
ATOM   9044 H HD22 . LEU   B 1 298 ? -6.791  -23.809 50.320  1.00 45.81  ? 283 LEU   B HD22 1 
ATOM   9045 H HD23 . LEU   B 1 298 ? -7.254  -25.326 50.399  1.00 45.81  ? 283 LEU   B HD23 1 
ATOM   9046 N N    . ILE   B 1 299 ? -7.716  -25.031 45.172  1.00 34.07  ? 284 ILE   B N    1 
ATOM   9047 C CA   . ILE   B 1 299 ? -8.283  -24.463 43.956  1.00 31.75  ? 284 ILE   B CA   1 
ATOM   9048 C C    . ILE   B 1 299 ? -9.610  -25.128 43.598  1.00 37.26  ? 284 ILE   B C    1 
ATOM   9049 O O    . ILE   B 1 299 ? -10.479 -24.483 43.001  1.00 33.11  ? 284 ILE   B O    1 
ATOM   9050 C CB   . ILE   B 1 299 ? -7.273  -24.567 42.801  1.00 39.04  ? 284 ILE   B CB   1 
ATOM   9051 C CG1  . ILE   B 1 299 ? -5.988  -23.805 43.144  1.00 39.13  ? 284 ILE   B CG1  1 
ATOM   9052 C CG2  . ILE   B 1 299 ? -7.870  -24.015 41.514  1.00 30.42  ? 284 ILE   B CG2  1 
ATOM   9053 C CD1  . ILE   B 1 299 ? -6.213  -22.363 43.536  1.00 38.03  ? 284 ILE   B CD1  1 
ATOM   9054 H H    . ILE   B 1 299 ? -7.110  -25.627 45.038  1.00 40.88  ? 284 ILE   B H    1 
ATOM   9055 H HA   . ILE   B 1 299 ? -8.463  -23.523 44.115  1.00 38.10  ? 284 ILE   B HA   1 
ATOM   9056 H HB   . ILE   B 1 299 ? -7.062  -25.505 42.673  1.00 46.85  ? 284 ILE   B HB   1 
ATOM   9057 H HG12 . ILE   B 1 299 ? -5.553  -24.249 43.889  1.00 46.96  ? 284 ILE   B HG12 1 
ATOM   9058 H HG13 . ILE   B 1 299 ? -5.406  -23.813 42.368  1.00 46.96  ? 284 ILE   B HG13 1 
ATOM   9059 H HG21 . ILE   B 1 299 ? -7.155  -23.858 40.877  1.00 36.51  ? 284 ILE   B HG21 1 
ATOM   9060 H HG22 . ILE   B 1 299 ? -8.497  -24.661 41.154  1.00 36.51  ? 284 ILE   B HG22 1 
ATOM   9061 H HG23 . ILE   B 1 299 ? -8.328  -23.183 41.709  1.00 36.51  ? 284 ILE   B HG23 1 
ATOM   9062 H HD11 . ILE   B 1 299 ? -5.362  -21.898 43.532  1.00 45.63  ? 284 ILE   B HD11 1 
ATOM   9063 H HD12 . ILE   B 1 299 ? -6.817  -21.952 42.897  1.00 45.63  ? 284 ILE   B HD12 1 
ATOM   9064 H HD13 . ILE   B 1 299 ? -6.602  -22.334 44.424  1.00 45.63  ? 284 ILE   B HD13 1 
ATOM   9065 N N    . LEU   B 1 300 ? -9.805  -26.406 43.939  1.00 33.76  ? 285 LEU   B N    1 
ATOM   9066 C CA   . LEU   B 1 300 ? -11.136 -26.985 43.788  1.00 35.15  ? 285 LEU   B CA   1 
ATOM   9067 C C    . LEU   B 1 300 ? -12.155 -26.170 44.575  1.00 36.11  ? 285 LEU   B C    1 
ATOM   9068 O O    . LEU   B 1 300 ? -13.291 -25.978 44.133  1.00 41.26  ? 285 LEU   B O    1 
ATOM   9069 C CB   . LEU   B 1 300 ? -11.151 -28.444 44.249  1.00 36.30  ? 285 LEU   B CB   1 
ATOM   9070 C CG   . LEU   B 1 300 ? -10.408 -29.508 43.434  1.00 35.78  ? 285 LEU   B CG   1 
ATOM   9071 C CD1  . LEU   B 1 300 ? -10.703 -30.885 44.020  1.00 43.86  ? 285 LEU   B CD1  1 
ATOM   9072 C CD2  . LEU   B 1 300 ? -10.786 -29.476 41.973  1.00 37.26  ? 285 LEU   B CD2  1 
ATOM   9073 H H    . LEU   B 1 300 ? -9.204  -26.938 44.248  1.00 40.52  ? 285 LEU   B H    1 
ATOM   9074 H HA   . LEU   B 1 300 ? -11.378 -26.978 42.848  1.00 42.18  ? 285 LEU   B HA   1 
ATOM   9075 H HB2  . LEU   B 1 300 ? -10.767 -28.468 45.139  1.00 43.56  ? 285 LEU   B HB2  1 
ATOM   9076 H HB3  . LEU   B 1 300 ? -12.079 -28.726 44.280  1.00 43.56  ? 285 LEU   B HB3  1 
ATOM   9077 H HG   . LEU   B 1 300 ? -9.457  -29.324 43.481  1.00 42.93  ? 285 LEU   B HG   1 
ATOM   9078 H HD11 . LEU   B 1 300 ? -10.224 -31.556 43.508  1.00 52.63  ? 285 LEU   B HD11 1 
ATOM   9079 H HD12 . LEU   B 1 300 ? -10.411 -30.904 44.945  1.00 52.63  ? 285 LEU   B HD12 1 
ATOM   9080 H HD13 . LEU   B 1 300 ? -11.657 -31.052 43.971  1.00 52.63  ? 285 LEU   B HD13 1 
ATOM   9081 H HD21 . LEU   B 1 300 ? -10.358 -30.220 41.520  1.00 44.71  ? 285 LEU   B HD21 1 
ATOM   9082 H HD22 . LEU   B 1 300 ? -11.750 -29.551 41.894  1.00 44.71  ? 285 LEU   B HD22 1 
ATOM   9083 H HD23 . LEU   B 1 300 ? -10.487 -28.638 41.588  1.00 44.71  ? 285 LEU   B HD23 1 
ATOM   9084 N N    . ASP   B 1 301 ? -11.752 -25.677 45.746  1.00 36.11  ? 286 ASP   B N    1 
ATOM   9085 C CA   . ASP   B 1 301 ? -12.616 -24.808 46.539  1.00 39.55  ? 286 ASP   B CA   1 
ATOM   9086 C C    . ASP   B 1 301 ? -12.925 -23.515 45.790  1.00 42.94  ? 286 ASP   B C    1 
ATOM   9087 O O    . ASP   B 1 301 ? -14.043 -22.989 45.866  1.00 40.65  ? 286 ASP   B O    1 
ATOM   9088 C CB   . ASP   B 1 301 ? -11.929 -24.526 47.876  1.00 43.27  ? 286 ASP   B CB   1 
ATOM   9089 C CG   . ASP   B 1 301 ? -12.874 -24.008 48.938  1.00 46.59  ? 286 ASP   B CG   1 
ATOM   9090 O OD1  . ASP   B 1 301 ? -13.922 -24.644 49.181  1.00 56.94  ? 286 ASP   B OD1  1 
ATOM   9091 O OD2  . ASP   B 1 301 ? -12.538 -22.977 49.555  1.00 48.45  ? 286 ASP   B OD2  1 
ATOM   9092 H H    . ASP   B 1 301 ? -10.985 -25.830 46.103  1.00 43.33  ? 286 ASP   B H    1 
ATOM   9093 H HA   . ASP   B 1 301 ? -13.463 -25.246 46.714  1.00 47.46  ? 286 ASP   B HA   1 
ATOM   9094 H HB2  . ASP   B 1 301 ? -11.534 -25.348 48.206  1.00 51.93  ? 286 ASP   B HB2  1 
ATOM   9095 H HB3  . ASP   B 1 301 ? -11.240 -23.857 47.741  1.00 51.93  ? 286 ASP   B HB3  1 
ATOM   9096 N N    . LEU   B 1 302 ? -11.952 -22.995 45.043  1.00 34.94  ? 287 LEU   B N    1 
ATOM   9097 C CA   . LEU   B 1 302 ? -12.182 -21.779 44.266  1.00 39.41  ? 287 LEU   B CA   1 
ATOM   9098 C C    . LEU   B 1 302 ? -13.133 -22.047 43.104  1.00 36.40  ? 287 LEU   B C    1 
ATOM   9099 O O    . LEU   B 1 302 ? -14.012 -21.228 42.815  1.00 35.79  ? 287 LEU   B O    1 
ATOM   9100 C CB   . LEU   B 1 302 ? -10.842 -21.225 43.774  1.00 32.78  ? 287 LEU   B CB   1 
ATOM   9101 C CG   . LEU   B 1 302 ? -10.794 -19.830 43.143  1.00 36.38  ? 287 LEU   B CG   1 
ATOM   9102 C CD1  . LEU   B 1 302 ? -11.209 -18.734 44.126  1.00 38.24  ? 287 LEU   B CD1  1 
ATOM   9103 C CD2  . LEU   B 1 302 ? -9.402  -19.560 42.616  1.00 36.88  ? 287 LEU   B CD2  1 
ATOM   9104 H H    . LEU   B 1 302 ? -11.160 -23.321 44.969  1.00 41.93  ? 287 LEU   B H    1 
ATOM   9105 H HA   . LEU   B 1 302 ? -12.592 -21.104 44.830  1.00 47.30  ? 287 LEU   B HA   1 
ATOM   9106 H HB2  . LEU   B 1 302 ? -10.242 -21.201 44.535  1.00 39.33  ? 287 LEU   B HB2  1 
ATOM   9107 H HB3  . LEU   B 1 302 ? -10.504 -21.839 43.103  1.00 39.33  ? 287 LEU   B HB3  1 
ATOM   9108 H HG   . LEU   B 1 302 ? -11.430 -19.804 42.411  1.00 43.65  ? 287 LEU   B HG   1 
ATOM   9109 H HD11 . LEU   B 1 302 ? -11.093 -17.869 43.702  1.00 45.89  ? 287 LEU   B HD11 1 
ATOM   9110 H HD12 . LEU   B 1 302 ? -12.140 -18.862 44.368  1.00 45.89  ? 287 LEU   B HD12 1 
ATOM   9111 H HD13 . LEU   B 1 302 ? -10.651 -18.791 44.918  1.00 45.89  ? 287 LEU   B HD13 1 
ATOM   9112 H HD21 . LEU   B 1 302 ? -9.380  -18.675 42.220  1.00 44.25  ? 287 LEU   B HD21 1 
ATOM   9113 H HD22 . LEU   B 1 302 ? -8.771  -19.610 43.351  1.00 44.25  ? 287 LEU   B HD22 1 
ATOM   9114 H HD23 . LEU   B 1 302 ? -9.183  -20.227 41.947  1.00 44.25  ? 287 LEU   B HD23 1 
ATOM   9115 N N    . LEU   B 1 303 ? -12.995 -23.206 42.447  1.00 38.17  ? 288 LEU   B N    1 
ATOM   9116 C CA   . LEU   B 1 303 ? -13.860 -23.536 41.317  1.00 39.35  ? 288 LEU   B CA   1 
ATOM   9117 C C    . LEU   B 1 303 ? -15.287 -23.822 41.763  1.00 42.91  ? 288 LEU   B C    1 
ATOM   9118 O O    . LEU   B 1 303 ? -16.237 -23.542 41.024  1.00 39.62  ? 288 LEU   B O    1 
ATOM   9119 C CB   . LEU   B 1 303 ? -13.315 -24.747 40.558  1.00 35.38  ? 288 LEU   B CB   1 
ATOM   9120 C CG   . LEU   B 1 303 ? -11.914 -24.625 39.962  1.00 37.16  ? 288 LEU   B CG   1 
ATOM   9121 C CD1  . LEU   B 1 303 ? -11.585 -25.879 39.168  1.00 33.84  ? 288 LEU   B CD1  1 
ATOM   9122 C CD2  . LEU   B 1 303 ? -11.788 -23.370 39.088  1.00 33.00  ? 288 LEU   B CD2  1 
ATOM   9123 H H    . LEU   B 1 303 ? -12.413 -23.811 42.636  1.00 45.81  ? 288 LEU   B H    1 
ATOM   9124 H HA   . LEU   B 1 303 ? -13.868 -22.775 40.715  1.00 47.22  ? 288 LEU   B HA   1 
ATOM   9125 H HB2  . LEU   B 1 303 ? -13.296 -25.498 41.171  1.00 42.46  ? 288 LEU   B HB2  1 
ATOM   9126 H HB3  . LEU   B 1 303 ? -13.919 -24.933 39.823  1.00 42.46  ? 288 LEU   B HB3  1 
ATOM   9127 H HG   . LEU   B 1 303 ? -11.268 -24.535 40.680  1.00 44.59  ? 288 LEU   B HG   1 
ATOM   9128 H HD11 . LEU   B 1 303 ? -10.695 -25.791 38.793  1.00 40.60  ? 288 LEU   B HD11 1 
ATOM   9129 H HD12 . LEU   B 1 303 ? -11.619 -26.646 39.761  1.00 40.60  ? 288 LEU   B HD12 1 
ATOM   9130 H HD13 . LEU   B 1 303 ? -12.236 -25.982 38.456  1.00 40.60  ? 288 LEU   B HD13 1 
ATOM   9131 H HD21 . LEU   B 1 303 ? -10.934 -23.390 38.628  1.00 39.60  ? 288 LEU   B HD21 1 
ATOM   9132 H HD22 . LEU   B 1 303 ? -12.511 -23.360 38.442  1.00 39.60  ? 288 LEU   B HD22 1 
ATOM   9133 H HD23 . LEU   B 1 303 ? -11.839 -22.584 39.654  1.00 39.60  ? 288 LEU   B HD23 1 
ATOM   9134 N N    . ASP   B 1 304 ? -15.458 -24.405 42.950  1.00 45.07  ? 289 ASP   B N    1 
ATOM   9135 C CA   . ASP   B 1 304 ? -16.800 -24.603 43.476  1.00 45.85  ? 289 ASP   B CA   1 
ATOM   9136 C C    . ASP   B 1 304 ? -17.494 -23.266 43.703  1.00 46.13  ? 289 ASP   B C    1 
ATOM   9137 O O    . ASP   B 1 304 ? -18.684 -23.116 43.402  1.00 60.45  ? 289 ASP   B O    1 
ATOM   9138 C CB   . ASP   B 1 304 ? -16.741 -25.407 44.769  1.00 45.46  ? 289 ASP   B CB   1 
ATOM   9139 C CG   . ASP   B 1 304 ? -18.086 -25.514 45.436  1.00 55.83  ? 289 ASP   B CG   1 
ATOM   9140 O OD1  . ASP   B 1 304 ? -19.007 -26.075 44.807  1.00 54.18  ? 289 ASP   B OD1  1 
ATOM   9141 O OD2  . ASP   B 1 304 ? -18.224 -25.029 46.582  1.00 55.54  ? 289 ASP   B OD2  1 
ATOM   9142 H H    . ASP   B 1 304 ? -14.824 -24.689 43.457  1.00 54.09  ? 289 ASP   B H    1 
ATOM   9143 H HA   . ASP   B 1 304 ? -17.322 -25.110 42.834  1.00 55.03  ? 289 ASP   B HA   1 
ATOM   9144 H HB2  . ASP   B 1 304 ? -16.431 -26.305 44.571  1.00 54.55  ? 289 ASP   B HB2  1 
ATOM   9145 H HB3  . ASP   B 1 304 ? -16.132 -24.973 45.386  1.00 54.55  ? 289 ASP   B HB3  1 
ATOM   9146 N N    . LYS   B 1 305 ? -16.765 -22.281 44.236  1.00 47.80  ? 290 LYS   B N    1 
ATOM   9147 C CA   . LYS   B 1 305 ? -17.327 -20.945 44.393  1.00 50.96  ? 290 LYS   B CA   1 
ATOM   9148 C C    . LYS   B 1 305 ? -17.650 -20.321 43.044  1.00 50.03  ? 290 LYS   B C    1 
ATOM   9149 O O    . LYS   B 1 305 ? -18.627 -19.573 42.920  1.00 56.42  ? 290 LYS   B O    1 
ATOM   9150 C CB   . LYS   B 1 305 ? -16.353 -20.052 45.161  1.00 51.93  ? 290 LYS   B CB   1 
ATOM   9151 C CG   . LYS   B 1 305 ? -16.830 -18.615 45.327  1.00 52.06  ? 290 LYS   B CG   1 
ATOM   9152 C CD   . LYS   B 1 305 ? -15.798 -17.758 46.046  1.00 52.47  ? 290 LYS   B CD   1 
ATOM   9153 C CE   . LYS   B 1 305 ? -16.295 -16.332 46.212  1.00 47.73  ? 290 LYS   B CE   1 
ATOM   9154 N NZ   . LYS   B 1 305 ? -15.317 -15.471 46.925  1.00 53.05  ? 290 LYS   B NZ   1 
ATOM   9155 H H    . LYS   B 1 305 ? -15.954 -22.362 44.510  1.00 57.36  ? 290 LYS   B H    1 
ATOM   9156 H HA   . LYS   B 1 305 ? -18.147 -21.008 44.906  1.00 61.15  ? 290 LYS   B HA   1 
ATOM   9157 H HB2  . LYS   B 1 305 ? -16.224 -20.424 46.048  1.00 62.31  ? 290 LYS   B HB2  1 
ATOM   9158 H HB3  . LYS   B 1 305 ? -15.509 -20.030 44.684  1.00 62.31  ? 290 LYS   B HB3  1 
ATOM   9159 H HG2  . LYS   B 1 305 ? -16.990 -18.228 44.452  1.00 62.48  ? 290 LYS   B HG2  1 
ATOM   9160 H HG3  . LYS   B 1 305 ? -17.648 -18.607 45.848  1.00 62.48  ? 290 LYS   B HG3  1 
ATOM   9161 H HD2  . LYS   B 1 305 ? -15.628 -18.128 46.926  1.00 62.96  ? 290 LYS   B HD2  1 
ATOM   9162 H HD3  . LYS   B 1 305 ? -14.977 -17.739 45.530  1.00 62.96  ? 290 LYS   B HD3  1 
ATOM   9163 H HE2  . LYS   B 1 305 ? -16.453 -15.947 45.335  1.00 57.28  ? 290 LYS   B HE2  1 
ATOM   9164 H HE3  . LYS   B 1 305 ? -17.119 -16.340 46.724  1.00 57.28  ? 290 LYS   B HE3  1 
ATOM   9165 H HZ1  . LYS   B 1 305 ? -15.643 -14.647 47.013  1.00 63.66  ? 290 LYS   B HZ1  1 
ATOM   9166 H HZ2  . LYS   B 1 305 ? -15.152 -15.804 47.734  1.00 63.66  ? 290 LYS   B HZ2  1 
ATOM   9167 H HZ3  . LYS   B 1 305 ? -14.555 -15.432 46.467  1.00 63.66  ? 290 LYS   B HZ3  1 
ATOM   9168 N N    . LEU   B 1 306 ? -16.839 -20.609 42.028  1.00 48.27  ? 291 LEU   B N    1 
ATOM   9169 C CA   . LEU   B 1 306 ? -17.117 -20.108 40.687  1.00 44.61  ? 291 LEU   B CA   1 
ATOM   9170 C C    . LEU   B 1 306 ? -18.453 -20.632 40.180  1.00 55.82  ? 291 LEU   B C    1 
ATOM   9171 O O    . LEU   B 1 306 ? -19.270 -19.871 39.650  1.00 57.24  ? 291 LEU   B O    1 
ATOM   9172 C CB   . LEU   B 1 306 ? -15.979 -20.516 39.754  1.00 45.50  ? 291 LEU   B CB   1 
ATOM   9173 C CG   . LEU   B 1 306 ? -16.088 -20.205 38.266  1.00 48.38  ? 291 LEU   B CG   1 
ATOM   9174 C CD1  . LEU   B 1 306 ? -15.976 -18.711 38.015  1.00 50.53  ? 291 LEU   B CD1  1 
ATOM   9175 C CD2  . LEU   B 1 306 ? -15.000 -20.968 37.511  1.00 40.44  ? 291 LEU   B CD2  1 
ATOM   9176 H H    . LEU   B 1 306 ? -16.127 -21.088 42.088  1.00 57.92  ? 291 LEU   B H    1 
ATOM   9177 H HA   . LEU   B 1 306 ? -17.167 -19.140 40.705  1.00 53.53  ? 291 LEU   B HA   1 
ATOM   9178 H HB2  . LEU   B 1 306 ? -15.175 -20.073 40.067  1.00 54.60  ? 291 LEU   B HB2  1 
ATOM   9179 H HB3  . LEU   B 1 306 ? -15.877 -21.478 39.825  1.00 54.60  ? 291 LEU   B HB3  1 
ATOM   9180 H HG   . LEU   B 1 306 ? -16.956 -20.487 37.935  1.00 58.05  ? 291 LEU   B HG   1 
ATOM   9181 H HD11 . LEU   B 1 306 ? -16.049 -18.545 37.062  1.00 60.64  ? 291 LEU   B HD11 1 
ATOM   9182 H HD12 . LEU   B 1 306 ? -16.691 -18.257 38.487  1.00 60.64  ? 291 LEU   B HD12 1 
ATOM   9183 H HD13 . LEU   B 1 306 ? -15.116 -18.401 38.340  1.00 60.64  ? 291 LEU   B HD13 1 
ATOM   9184 H HD21 . LEU   B 1 306 ? -15.060 -20.752 36.567  1.00 48.53  ? 291 LEU   B HD21 1 
ATOM   9185 H HD22 . LEU   B 1 306 ? -14.133 -20.705 37.857  1.00 48.53  ? 291 LEU   B HD22 1 
ATOM   9186 H HD23 . LEU   B 1 306 ? -15.133 -21.920 37.642  1.00 48.53  ? 291 LEU   B HD23 1 
ATOM   9187 N N    . LYS   B 1 307 ? -18.704 -21.932 40.359  1.00 50.75  ? 292 LYS   B N    1 
ATOM   9188 C CA   . LYS   B 1 307 ? -19.877 -22.565 39.767  1.00 57.07  ? 292 LYS   B CA   1 
ATOM   9189 C C    . LYS   B 1 307 ? -21.161 -22.267 40.532  1.00 66.82  ? 292 LYS   B C    1 
ATOM   9190 O O    . LYS   B 1 307 ? -22.242 -22.256 39.931  1.00 69.28  ? 292 LYS   B O    1 
ATOM   9191 C CB   . LYS   B 1 307 ? -19.669 -24.081 39.694  1.00 64.93  ? 292 LYS   B CB   1 
ATOM   9192 C CG   . LYS   B 1 307 ? -19.568 -24.642 38.284  1.00 63.72  ? 292 LYS   B CG   1 
ATOM   9193 C CD   . LYS   B 1 307 ? -20.910 -24.604 37.569  1.00 76.17  ? 292 LYS   B CD   1 
ATOM   9194 C CE   . LYS   B 1 307 ? -20.809 -25.152 36.147  1.00 72.34  ? 292 LYS   B CE   1 
ATOM   9195 N NZ   . LYS   B 1 307 ? -22.144 -25.187 35.472  1.00 79.05  ? 292 LYS   B NZ   1 
ATOM   9196 H H    . LYS   B 1 307 ? -18.210 -22.466 40.819  1.00 60.90  ? 292 LYS   B H    1 
ATOM   9197 H HA   . LYS   B 1 307 ? -19.982 -22.219 38.867  1.00 68.49  ? 292 LYS   B HA   1 
ATOM   9198 H HB2  . LYS   B 1 307 ? -18.846 -24.302 40.156  1.00 77.92  ? 292 LYS   B HB2  1 
ATOM   9199 H HB3  . LYS   B 1 307 ? -20.420 -24.516 40.128  1.00 77.92  ? 292 LYS   B HB3  1 
ATOM   9200 H HG2  . LYS   B 1 307 ? -18.936 -24.112 37.772  1.00 76.47  ? 292 LYS   B HG2  1 
ATOM   9201 H HG3  . LYS   B 1 307 ? -19.271 -25.564 38.325  1.00 76.47  ? 292 LYS   B HG3  1 
ATOM   9202 H HD2  . LYS   B 1 307 ? -21.549 -25.145 38.059  1.00 91.41  ? 292 LYS   B HD2  1 
ATOM   9203 H HD3  . LYS   B 1 307 ? -21.221 -23.687 37.520  1.00 91.41  ? 292 LYS   B HD3  1 
ATOM   9204 H HE2  . LYS   B 1 307 ? -20.219 -24.585 35.626  1.00 86.81  ? 292 LYS   B HE2  1 
ATOM   9205 H HE3  . LYS   B 1 307 ? -20.460 -26.057 36.176  1.00 86.81  ? 292 LYS   B HE3  1 
ATOM   9206 H HZ1  . LYS   B 1 307 ? -22.059 -25.508 34.646  1.00 94.86  ? 292 LYS   B HZ1  1 
ATOM   9207 H HZ2  . LYS   B 1 307 ? -22.703 -25.708 35.929  1.00 94.86  ? 292 LYS   B HZ2  1 
ATOM   9208 H HZ3  . LYS   B 1 307 ? -22.485 -24.365 35.429  1.00 94.86  ? 292 LYS   B HZ3  1 
ATOM   9209 N N    . ASN   B 1 308 ? -21.075 -22.030 41.841  1.00 66.75  ? 293 ASN   B N    1 
ATOM   9210 C CA   . ASN   B 1 308 ? -22.252 -21.903 42.697  1.00 69.98  ? 293 ASN   B CA   1 
ATOM   9211 C C    . ASN   B 1 308 ? -22.168 -20.592 43.465  1.00 76.16  ? 293 ASN   B C    1 
ATOM   9212 O O    . ASN   B 1 308 ? -21.363 -20.459 44.393  1.00 69.62  ? 293 ASN   B O    1 
ATOM   9213 C CB   . ASN   B 1 308 ? -22.351 -23.095 43.646  1.00 69.98  ? 293 ASN   B CB   1 
ATOM   9214 C CG   . ASN   B 1 308 ? -22.026 -24.407 42.956  1.00 63.30  ? 293 ASN   B CG   1 
ATOM   9215 O OD1  . ASN   B 1 308 ? -21.060 -25.084 43.307  1.00 60.76  ? 293 ASN   B OD1  1 
ATOM   9216 N ND2  . ASN   B 1 308 ? -22.825 -24.761 41.955  1.00 66.96  ? 293 ASN   B ND2  1 
ATOM   9217 H H    . ASN   B 1 308 ? -20.331 -21.937 42.263  1.00 80.10  ? 293 ASN   B H    1 
ATOM   9218 H HA   . ASN   B 1 308 ? -23.051 -21.868 42.148  1.00 83.98  ? 293 ASN   B HA   1 
ATOM   9219 H HB2  . ASN   B 1 308 ? -21.724 -22.974 44.376  1.00 83.98  ? 293 ASN   B HB2  1 
ATOM   9220 H HB3  . ASN   B 1 308 ? -23.256 -23.151 43.992  1.00 83.98  ? 293 ASN   B HB3  1 
ATOM   9221 H HD21 . ASN   B 1 308 ? -22.683 -25.496 41.532  1.00 80.36  ? 293 ASN   B HD21 1 
ATOM   9222 H HD22 . ASN   B 1 308 ? -23.483 -24.256 41.731  1.00 80.36  ? 293 ASN   B HD22 1 
ATOM   9223 N N    . GLY   B 1 309 ? -22.996 -19.627 43.071  1.00 91.10  ? 294 GLY   B N    1 
ATOM   9224 C CA   . GLY   B 1 309 ? -23.038 -18.335 43.726  1.00 86.06  ? 294 GLY   B CA   1 
ATOM   9225 C C    . GLY   B 1 309 ? -21.693 -17.642 43.687  1.00 81.87  ? 294 GLY   B C    1 
ATOM   9226 O O    . GLY   B 1 309 ? -20.871 -17.824 44.585  1.00 89.57  ? 294 GLY   B O    1 
ATOM   9227 H H    . GLY   B 1 309 ? -23.548 -19.703 42.416  1.00 109.31 ? 294 GLY   B H    1 
ATOM   9228 H HA2  . GLY   B 1 309 ? -23.690 -17.770 43.282  1.00 103.27 ? 294 GLY   B HA2  1 
ATOM   9229 H HA3  . GLY   B 1 309 ? -23.299 -18.451 44.652  1.00 103.27 ? 294 GLY   B HA3  1 
HETATM 9230 C C1   . EDO   C 2 .   ? -2.010  5.345   27.638  1.00 41.41  ? 301 EDO   A C1   1 
HETATM 9231 O O1   . EDO   C 2 .   ? -3.414  5.530   27.445  1.00 43.10  ? 301 EDO   A O1   1 
HETATM 9232 C C2   . EDO   C 2 .   ? -1.532  4.139   26.843  1.00 35.89  ? 301 EDO   A C2   1 
HETATM 9233 O O2   . EDO   C 2 .   ? -1.633  4.422   25.444  1.00 44.73  ? 301 EDO   A O2   1 
HETATM 9234 H H11  . EDO   C 2 .   ? -1.472  6.238   27.312  1.00 49.70  ? 301 EDO   A H11  1 
HETATM 9235 H H12  . EDO   C 2 .   ? -1.799  5.195   28.699  1.00 49.70  ? 301 EDO   A H12  1 
HETATM 9236 H HO1  . EDO   C 2 .   ? -3.708  6.307   27.940  1.00 51.71  ? 301 EDO   A HO1  1 
HETATM 9237 H H21  . EDO   C 2 .   ? -2.141  3.267   27.090  1.00 43.06  ? 301 EDO   A H21  1 
HETATM 9238 H H22  . EDO   C 2 .   ? -0.497  3.909   27.102  1.00 43.06  ? 301 EDO   A H22  1 
HETATM 9239 H HO2  . EDO   C 2 .   ? -1.348  3.649   24.938  1.00 53.68  ? 301 EDO   A HO2  1 
HETATM 9240 C C1   . EDO   D 2 .   ? 16.254  9.993   19.106  1.00 35.29  ? 302 EDO   A C1   1 
HETATM 9241 O O1   . EDO   D 2 .   ? 14.921  9.797   18.623  1.00 48.90  ? 302 EDO   A O1   1 
HETATM 9242 C C2   . EDO   D 2 .   ? 16.382  9.363   20.486  1.00 42.27  ? 302 EDO   A C2   1 
HETATM 9243 O O2   . EDO   D 2 .   ? 16.309  7.934   20.385  1.00 47.86  ? 302 EDO   A O2   1 
HETATM 9244 H H11  . EDO   D 2 .   ? 16.970  9.536   18.420  1.00 42.34  ? 302 EDO   A H11  1 
HETATM 9245 H H12  . EDO   D 2 .   ? 16.477  11.061  19.162  1.00 42.34  ? 302 EDO   A H12  1 
HETATM 9246 H HO1  . EDO   D 2 .   ? 14.827  10.218  17.757  1.00 58.68  ? 302 EDO   A HO1  1 
HETATM 9247 H H21  . EDO   D 2 .   ? 17.335  9.651   20.935  1.00 50.72  ? 302 EDO   A H21  1 
HETATM 9248 H H22  . EDO   D 2 .   ? 15.582  9.727   21.133  1.00 50.72  ? 302 EDO   A H22  1 
HETATM 9249 H HO2  . EDO   D 2 .   ? 16.169  7.556   21.264  1.00 57.44  ? 302 EDO   A HO2  1 
HETATM 9250 C C1   . EDO   E 2 .   ? 7.948   14.026  0.196   1.00 46.14  ? 303 EDO   A C1   1 
HETATM 9251 O O1   . EDO   E 2 .   ? 6.624   13.572  0.501   1.00 50.10  ? 303 EDO   A O1   1 
HETATM 9252 C C2   . EDO   E 2 .   ? 8.658   14.456  1.476   1.00 39.11  ? 303 EDO   A C2   1 
HETATM 9253 O O2   . EDO   E 2 .   ? 9.318   15.709  1.244   1.00 46.41  ? 303 EDO   A O2   1 
HETATM 9254 H H11  . EDO   E 2 .   ? 8.511   13.225  -0.287  1.00 55.37  ? 303 EDO   A H11  1 
HETATM 9255 H H12  . EDO   E 2 .   ? 7.898   14.868  -0.499  1.00 55.37  ? 303 EDO   A H12  1 
HETATM 9256 H HO1  . EDO   E 2 .   ? 6.182   13.296  -0.313  1.00 60.11  ? 303 EDO   A HO1  1 
HETATM 9257 H H21  . EDO   E 2 .   ? 9.387   13.699  1.771   1.00 46.94  ? 303 EDO   A H21  1 
HETATM 9258 H H22  . EDO   E 2 .   ? 7.934   14.560  2.287   1.00 46.94  ? 303 EDO   A H22  1 
HETATM 9259 H HO2  . EDO   E 2 .   ? 9.741   16.007  2.061   1.00 55.69  ? 303 EDO   A HO2  1 
HETATM 9260 C C1   . EDO   F 2 .   ? 9.836   29.787  11.008  1.00 42.13  ? 304 EDO   A C1   1 
HETATM 9261 O O1   . EDO   F 2 .   ? 11.097  29.117  10.867  1.00 57.48  ? 304 EDO   A O1   1 
HETATM 9262 C C2   . EDO   F 2 .   ? 8.880   28.927  11.826  1.00 42.24  ? 304 EDO   A C2   1 
HETATM 9263 O O2   . EDO   F 2 .   ? 7.581   29.533  11.860  1.00 45.48  ? 304 EDO   A O2   1 
HETATM 9264 H H11  . EDO   F 2 .   ? 9.983   30.749  11.504  1.00 50.56  ? 304 EDO   A H11  1 
HETATM 9265 H H12  . EDO   F 2 .   ? 9.408   29.979  10.022  1.00 50.56  ? 304 EDO   A H12  1 
HETATM 9266 H HO1  . EDO   F 2 .   ? 11.693  29.662  10.335  1.00 68.98  ? 304 EDO   A HO1  1 
HETATM 9267 H H21  . EDO   F 2 .   ? 9.261   28.817  12.844  1.00 50.69  ? 304 EDO   A H21  1 
HETATM 9268 H H22  . EDO   F 2 .   ? 8.810   27.930  11.384  1.00 50.69  ? 304 EDO   A H22  1 
HETATM 9269 H HO2  . EDO   F 2 .   ? 7.094   29.209  12.631  1.00 54.58  ? 304 EDO   A HO2  1 
HETATM 9270 C C1   . EDO   G 2 .   ? 27.558  -8.481  3.225   1.00 46.70  ? 305 EDO   A C1   1 
HETATM 9271 O O1   . EDO   G 2 .   ? 27.730  -9.136  4.489   1.00 43.89  ? 305 EDO   A O1   1 
HETATM 9272 C C2   . EDO   G 2 .   ? 26.170  -8.801  2.684   1.00 30.07  ? 305 EDO   A C2   1 
HETATM 9273 O O2   . EDO   G 2 .   ? 25.789  -7.902  1.636   1.00 43.48  ? 305 EDO   A O2   1 
HETATM 9274 H H11  . EDO   G 2 .   ? 27.672  -7.402  3.345   1.00 56.04  ? 305 EDO   A H11  1 
HETATM 9275 H H12  . EDO   G 2 .   ? 28.320  -8.823  2.522   1.00 56.04  ? 305 EDO   A H12  1 
HETATM 9276 H HO1  . EDO   G 2 .   ? 28.594  -8.904  4.857   1.00 52.66  ? 305 EDO   A HO1  1 
HETATM 9277 H H21  . EDO   G 2 .   ? 26.158  -9.824  2.303   1.00 36.08  ? 305 EDO   A H21  1 
HETATM 9278 H H22  . EDO   G 2 .   ? 25.443  -8.737  3.497   1.00 36.08  ? 305 EDO   A H22  1 
HETATM 9279 H HO2  . EDO   G 2 .   ? 24.923  -8.158  1.291   1.00 52.17  ? 305 EDO   A HO2  1 
HETATM 9280 C C1   . EDO   H 2 .   ? 27.170  -10.498 -2.178  1.00 54.03  ? 306 EDO   A C1   1 
HETATM 9281 O O1   . EDO   H 2 .   ? 27.693  -9.944  -0.962  1.00 55.97  ? 306 EDO   A O1   1 
HETATM 9282 C C2   . EDO   H 2 .   ? 25.663  -10.716 -2.071  1.00 46.95  ? 306 EDO   A C2   1 
HETATM 9283 O O2   . EDO   H 2 .   ? 24.972  -9.584  -2.619  1.00 57.76  ? 306 EDO   A O2   1 
HETATM 9284 H H11  . EDO   H 2 .   ? 27.383  -9.821  -3.008  1.00 64.84  ? 306 EDO   A H11  1 
HETATM 9285 H H12  . EDO   H 2 .   ? 27.663  -11.450 -2.386  1.00 64.84  ? 306 EDO   A H12  1 
HETATM 9286 H HO1  . EDO   H 2 .   ? 28.647  -9.817  -1.049  1.00 67.17  ? 306 EDO   A HO1  1 
HETATM 9287 H H21  . EDO   H 2 .   ? 25.381  -10.851 -1.024  1.00 56.34  ? 306 EDO   A H21  1 
HETATM 9288 H H22  . EDO   H 2 .   ? 25.380  -11.621 -2.613  1.00 56.34  ? 306 EDO   A H22  1 
HETATM 9289 H HO2  . EDO   H 2 .   ? 24.018  -9.727  -2.555  1.00 69.32  ? 306 EDO   A HO2  1 
HETATM 9290 C C1   . EDO   I 2 .   ? 13.915  -8.639  4.812   1.00 51.43  ? 307 EDO   A C1   1 
HETATM 9291 O O1   . EDO   I 2 .   ? 14.632  -7.496  4.316   1.00 42.06  ? 307 EDO   A O1   1 
HETATM 9292 C C2   . EDO   I 2 .   ? 14.287  -9.877  3.997   1.00 42.08  ? 307 EDO   A C2   1 
HETATM 9293 O O2   . EDO   I 2 .   ? 13.713  -11.046 4.589   1.00 52.36  ? 307 EDO   A O2   1 
HETATM 9294 H H11  . EDO   I 2 .   ? 14.161  -8.801  5.864   1.00 61.71  ? 307 EDO   A H11  1 
HETATM 9295 H H12  . EDO   I 2 .   ? 12.840  -8.459  4.743   1.00 61.71  ? 307 EDO   A H12  1 
HETATM 9296 H HO1  . EDO   I 2 .   ? 14.406  -6.719  4.844   1.00 50.47  ? 307 EDO   A HO1  1 
HETATM 9297 H H21  . EDO   I 2 .   ? 15.373  -9.979  3.959   1.00 50.49  ? 307 EDO   A H21  1 
HETATM 9298 H H22  . EDO   I 2 .   ? 13.924  -9.766  2.973   1.00 50.49  ? 307 EDO   A H22  1 
HETATM 9299 H HO2  . EDO   I 2 .   ? 13.952  -11.823 4.065   1.00 62.83  ? 307 EDO   A HO2  1 
HETATM 9300 C C1   . GOL   J 3 .   ? 15.636  1.021   0.391   1.00 42.77  ? 308 GOL   A C1   1 
HETATM 9301 O O1   . GOL   J 3 .   ? 15.131  0.690   -0.875  1.00 44.81  ? 308 GOL   A O1   1 
HETATM 9302 C C2   . GOL   J 3 .   ? 15.956  -0.308  1.134   1.00 37.84  ? 308 GOL   A C2   1 
HETATM 9303 O O2   . GOL   J 3 .   ? 16.704  -1.177  0.362   1.00 40.69  ? 308 GOL   A O2   1 
HETATM 9304 C C3   . GOL   J 3 .   ? 16.721  0.117   2.414   1.00 42.69  ? 308 GOL   A C3   1 
HETATM 9305 O O3   . GOL   J 3 .   ? 18.018  0.455   2.023   1.00 33.68  ? 308 GOL   A O3   1 
HETATM 9306 H H11  . GOL   J 3 .   ? 15.007  1.536   0.919   1.00 51.32  ? 308 GOL   A H11  1 
HETATM 9307 H H12  . GOL   J 3 .   ? 16.442  1.558   0.340   1.00 51.32  ? 308 GOL   A H12  1 
HETATM 9308 H HO1  . GOL   J 3 .   ? 15.790  0.703   -1.413  1.00 53.77  ? 308 GOL   A HO1  1 
HETATM 9309 H H2   . GOL   J 3 .   ? 15.132  -0.772  1.348   1.00 45.41  ? 308 GOL   A H2   1 
HETATM 9310 H HO2  . GOL   J 3 .   ? 17.300  -0.720  -0.034  1.00 48.83  ? 308 GOL   A HO2  1 
HETATM 9311 H H31  . GOL   J 3 .   ? 16.690  -0.612  3.053   1.00 51.23  ? 308 GOL   A H31  1 
HETATM 9312 H H32  . GOL   J 3 .   ? 16.244  0.848   2.836   1.00 51.23  ? 308 GOL   A H32  1 
HETATM 9313 H HO3  . GOL   J 3 .   ? 18.016  1.287   1.852   1.00 40.41  ? 308 GOL   A HO3  1 
HETATM 9314 S S    . DMS   K 4 .   ? 4.909   31.600  15.011  1.00 82.06  ? 309 DMS   A S    1 
HETATM 9315 O O    . DMS   K 4 .   ? 4.659   30.156  15.315  1.00 53.70  ? 309 DMS   A O    1 
HETATM 9316 C C1   . DMS   K 4 .   ? 6.645   31.858  14.561  1.00 51.92  ? 309 DMS   A C1   1 
HETATM 9317 C C2   . DMS   K 4 .   ? 4.103   32.045  13.448  1.00 59.66  ? 309 DMS   A C2   1 
HETATM 9318 H H11  . DMS   K 4 .   ? 6.901   31.218  13.758  1.00 62.31  ? 309 DMS   A H11  1 
HETATM 9319 H H12  . DMS   K 4 .   ? 7.263   31.643  15.394  1.00 62.31  ? 309 DMS   A H12  1 
HETATM 9320 H H13  . DMS   K 4 .   ? 6.788   32.866  14.267  1.00 62.31  ? 309 DMS   A H13  1 
HETATM 9321 H H21  . DMS   K 4 .   ? 4.288   31.291  12.727  1.00 71.59  ? 309 DMS   A H21  1 
HETATM 9322 H H22  . DMS   K 4 .   ? 3.059   32.137  13.601  1.00 71.59  ? 309 DMS   A H22  1 
HETATM 9323 H H23  . DMS   K 4 .   ? 4.490   32.967  13.100  1.00 71.59  ? 309 DMS   A H23  1 
HETATM 9324 S S    . DMS   L 4 .   ? 9.782   10.263  8.175   1.00 74.74  ? 310 DMS   A S    1 
HETATM 9325 O O    . DMS   L 4 .   ? 10.588  9.000   8.235   1.00 65.56  ? 310 DMS   A O    1 
HETATM 9326 C C1   . DMS   L 4 .   ? 8.231   9.906   7.307   1.00 48.25  ? 310 DMS   A C1   1 
HETATM 9327 C C2   . DMS   L 4 .   ? 9.106   10.683  9.807   1.00 47.25  ? 310 DMS   A C2   1 
HETATM 9328 H H11  . DMS   L 4 .   ? 8.426   9.779   6.273   1.00 57.90  ? 310 DMS   A H11  1 
HETATM 9329 H H12  . DMS   L 4 .   ? 7.557   10.712  7.442   1.00 57.90  ? 310 DMS   A H12  1 
HETATM 9330 H H13  . DMS   L 4 .   ? 7.803   9.020   7.696   1.00 57.90  ? 310 DMS   A H13  1 
HETATM 9331 H H21  . DMS   L 4 .   ? 8.479   11.533  9.722   1.00 56.70  ? 310 DMS   A H21  1 
HETATM 9332 H H22  . DMS   L 4 .   ? 9.900   10.897  10.474  1.00 56.70  ? 310 DMS   A H22  1 
HETATM 9333 H H23  . DMS   L 4 .   ? 8.543   9.866   10.178  1.00 56.70  ? 310 DMS   A H23  1 
HETATM 9334 C C4   . A1BWC M 5 .   ? 10.167  -5.112  24.950  1.00 47.24  ? 311 A1BWC A C4   1 
HETATM 9335 C C5   . A1BWC M 5 .   ? 9.524   -6.098  24.063  1.00 43.80  ? 311 A1BWC A C5   1 
HETATM 9336 C C6   . A1BWC M 5 .   ? 8.961   -7.256  24.603  1.00 41.45  ? 311 A1BWC A C6   1 
HETATM 9337 C C7   . A1BWC M 5 .   ? 9.027   -7.478  26.023  1.00 39.87  ? 311 A1BWC A C7   1 
HETATM 9338 C C10  . A1BWC M 5 .   ? 10.167  -5.298  26.289  1.00 42.04  ? 311 A1BWC A C10  1 
HETATM 9339 C C13  . A1BWC M 5 .   ? 13.100  -4.565  24.203  1.00 45.35  ? 311 A1BWC A C13  1 
HETATM 9340 C C20  . A1BWC M 5 .   ? 9.720   -1.444  23.001  1.00 57.00  ? 311 A1BWC A C20  1 
HETATM 9341 C C21  . A1BWC M 5 .   ? 7.960   -9.783  25.933  1.00 47.45  ? 311 A1BWC A C21  1 
HETATM 9342 C C24  . A1BWC M 5 .   ? 6.757   -12.061 26.265  1.00 51.21  ? 311 A1BWC A C24  1 
HETATM 9343 C C26  . A1BWC M 5 .   ? 4.544   -10.968 25.569  1.00 46.36  ? 311 A1BWC A C26  1 
HETATM 9344 C C28  . A1BWC M 5 .   ? 2.585   -9.933  24.826  1.00 50.99  ? 311 A1BWC A C28  1 
HETATM 9345 C C1   . A1BWC M 5 .   ? 12.121  -2.570  23.142  1.00 49.97  ? 311 A1BWC A C1   1 
HETATM 9346 C C14  . A1BWC M 5 .   ? 14.372  -4.170  23.624  1.00 59.55  ? 311 A1BWC A C14  1 
HETATM 9347 C C16  . A1BWC M 5 .   ? 13.368  -2.273  22.639  1.00 42.06  ? 311 A1BWC A C16  1 
HETATM 9348 C C18  . A1BWC M 5 .   ? 12.008  -0.675  21.930  1.00 47.57  ? 311 A1BWC A C18  1 
HETATM 9349 C C19  . A1BWC M 5 .   ? 11.246  -1.569  22.705  1.00 39.29  ? 311 A1BWC A C19  1 
HETATM 9350 C C2   . A1BWC M 5 .   ? 11.963  -3.730  23.928  1.00 46.11  ? 311 A1BWC A C2   1 
HETATM 9351 C C25  . A1BWC M 5 .   ? 5.828   -11.723 25.085  1.00 49.94  ? 311 A1BWC A C25  1 
HETATM 9352 C C29  . A1BWC M 5 .   ? 2.947   -12.131 24.227  1.00 51.35  ? 311 A1BWC A C29  1 
HETATM 9353 C C30  . A1BWC M 5 .   ? 2.062   -11.958 22.996  1.00 49.09  ? 311 A1BWC A C30  1 
HETATM 9354 C C32  . A1BWC M 5 .   ? 1.650   -9.749  23.633  1.00 55.64  ? 311 A1BWC A C32  1 
HETATM 9355 C C9   . A1BWC M 5 .   ? 9.579   -6.514  26.853  1.00 35.79  ? 311 A1BWC A C9   1 
HETATM 9356 F F11  . A1BWC M 5 .   ? 10.707  -4.435  27.091  1.00 46.00  ? 311 A1BWC A F11  1 
HETATM 9357 F F12  . A1BWC M 5 .   ? 9.513   -5.865  22.721  1.00 53.21  ? 311 A1BWC A F12  1 
HETATM 9358 F F33  . A1BWC M 5 .   ? 9.186   -0.305  22.394  1.00 62.77  ? 311 A1BWC A F33  1 
HETATM 9359 F F34  . A1BWC M 5 .   ? 9.080   -2.502  22.506  1.00 61.53  ? 311 A1BWC A F34  1 
HETATM 9360 F F35  . A1BWC M 5 .   ? 9.520   -1.371  24.418  1.00 61.04  ? 311 A1BWC A F35  1 
HETATM 9361 N N15  . A1BWC M 5 .   ? 14.505  -3.109  22.899  1.00 50.25  ? 311 A1BWC A N15  1 
HETATM 9362 N N17  . A1BWC M 5 .   ? 13.268  -1.111  21.902  1.00 50.95  ? 311 A1BWC A N17  1 
HETATM 9363 N N22  . A1BWC M 5 .   ? 7.258   -10.818 26.821  1.00 45.13  ? 311 A1BWC A N22  1 
HETATM 9364 N N27  . A1BWC M 5 .   ? 3.530   -10.887 24.525  1.00 48.46  ? 311 A1BWC A N27  1 
HETATM 9365 N N8   . A1BWC M 5 .   ? 8.420   -8.588  26.635  1.00 49.14  ? 311 A1BWC A N8   1 
HETATM 9366 O O23  . A1BWC M 5 .   ? 8.136   -9.980  24.743  1.00 46.76  ? 311 A1BWC A O23  1 
HETATM 9367 O O3   . A1BWC M 5 .   ? 10.686  -3.897  24.382  1.00 49.43  ? 311 A1BWC A O3   1 
HETATM 9368 O O31  . A1BWC M 5 .   ? 1.119   -10.958 23.164  1.00 51.97  ? 311 A1BWC A O31  1 
HETATM 9369 H H61  . A1BWC M 5 .   ? 8.479   -7.980  23.958  1.00 49.74  ? 311 A1BWC A H61  1 
HETATM 9370 H H131 . A1BWC M 5 .   ? 13.013  -5.454  24.818  1.00 54.41  ? 311 A1BWC A H131 1 
HETATM 9371 H H242 . A1BWC M 5 .   ? 7.626   -12.700 25.897  1.00 61.45  ? 311 A1BWC A H242 1 
HETATM 9372 H H241 . A1BWC M 5 .   ? 6.174   -12.635 27.059  1.00 61.45  ? 311 A1BWC A H241 1 
HETATM 9373 H H262 . A1BWC M 5 .   ? 4.107   -11.518 26.456  1.00 55.64  ? 311 A1BWC A H262 1 
HETATM 9374 H H261 . A1BWC M 5 .   ? 4.829   -9.919  25.880  1.00 55.64  ? 311 A1BWC A H261 1 
HETATM 9375 H H281 . A1BWC M 5 .   ? 2.016   -10.249 25.685  1.00 61.19  ? 311 A1BWC A H281 1 
HETATM 9376 H H282 . A1BWC M 5 .   ? 3.075   -8.999  25.047  1.00 61.19  ? 311 A1BWC A H282 1 
HETATM 9377 H H141 . A1BWC M 5 .   ? 15.281  -4.817  23.816  1.00 71.46  ? 311 A1BWC A H141 1 
HETATM 9378 H H181 . A1BWC M 5 .   ? 11.663  0.147   21.477  1.00 57.09  ? 311 A1BWC A H181 1 
HETATM 9379 H H251 . A1BWC M 5 .   ? 6.319   -11.148 24.436  1.00 59.93  ? 311 A1BWC A H251 1 
HETATM 9380 H H252 . A1BWC M 5 .   ? 5.559   -12.566 24.629  1.00 59.93  ? 311 A1BWC A H252 1 
HETATM 9381 H H292 . A1BWC M 5 .   ? 3.772   -12.914 24.011  1.00 61.62  ? 311 A1BWC A H292 1 
HETATM 9382 H H291 . A1BWC M 5 .   ? 2.308   -12.493 25.122  1.00 61.62  ? 311 A1BWC A H291 1 
HETATM 9383 H H301 . A1BWC M 5 .   ? 2.679   -11.716 22.163  1.00 58.91  ? 311 A1BWC A H301 1 
HETATM 9384 H H302 . A1BWC M 5 .   ? 1.561   -12.878 22.803  1.00 58.91  ? 311 A1BWC A H302 1 
HETATM 9385 H H321 . A1BWC M 5 .   ? 0.816   -9.093  23.937  1.00 66.77  ? 311 A1BWC A H321 1 
HETATM 9386 H H322 . A1BWC M 5 .   ? 2.213   -9.271  22.813  1.00 66.77  ? 311 A1BWC A H322 1 
HETATM 9387 H H91  . A1BWC M 5 .   ? 9.574   -6.672  27.999  1.00 42.94  ? 311 A1BWC A H91  1 
HETATM 9388 H H171 . A1BWC M 5 .   ? 14.036  -0.658  21.414  1.00 61.14  ? 311 A1BWC A H171 1 
HETATM 9389 H H221 . A1BWC M 5 .   ? 7.145   -10.638 27.782  1.00 54.15  ? 311 A1BWC A H221 1 
HETATM 9390 H H81  . A1BWC M 5 .   ? 8.278   -8.554  27.741  1.00 58.97  ? 311 A1BWC A H81  1 
HETATM 9391 C C4   . A1BWC N 5 .   ? -5.461  19.533  3.175   0.50 37.23  ? 312 A1BWC A C4   1 
HETATM 9392 C C5   . A1BWC N 5 .   ? -6.683  20.368  3.114   0.50 40.87  ? 312 A1BWC A C5   1 
HETATM 9393 C C6   . A1BWC N 5 .   ? -6.602  21.700  2.696   0.50 41.15  ? 312 A1BWC A C6   1 
HETATM 9394 C C7   . A1BWC N 5 .   ? -5.338  22.261  2.311   0.50 38.00  ? 312 A1BWC A C7   1 
HETATM 9395 C C10  . A1BWC N 5 .   ? -4.274  20.069  2.802   0.50 37.72  ? 312 A1BWC A C10  1 
HETATM 9396 C C13  . A1BWC N 5 .   ? -5.766  19.040  5.886   0.50 33.06  ? 312 A1BWC A C13  1 
HETATM 9397 C C20  . A1BWC N 5 .   ? -5.329  15.032  3.360   0.50 37.92  ? 312 A1BWC A C20  1 
HETATM 9398 C C1   . A1BWC N 5 .   ? -5.590  16.622  5.447   0.50 32.02  ? 312 A1BWC A C1   1 
HETATM 9399 C C14  . A1BWC N 5 .   ? -5.873  18.745  7.299   0.50 28.78  ? 312 A1BWC A C14  1 
HETATM 9400 C C16  . A1BWC N 5 .   ? -5.694  16.437  6.813   0.50 31.88  ? 312 A1BWC A C16  1 
HETATM 9401 C C18  . A1BWC N 5 .   ? -5.501  14.407  5.933   0.50 32.22  ? 312 A1BWC A C18  1 
HETATM 9402 C C19  . A1BWC N 5 .   ? -5.462  15.347  4.879   0.50 27.99  ? 312 A1BWC A C19  1 
HETATM 9403 C C2   . A1BWC N 5 .   ? -5.624  17.951  4.949   0.50 35.59  ? 312 A1BWC A C2   1 
HETATM 9404 C C9   . A1BWC N 5 .   ? -4.192  21.474  2.358   0.50 36.62  ? 312 A1BWC A C9   1 
HETATM 9405 F F11  . A1BWC N 5 .   ? -3.203  19.342  2.842   0.50 38.74  ? 312 A1BWC A F11  1 
HETATM 9406 F F12  . A1BWC N 5 .   ? -7.889  19.853  3.477   0.50 43.03  ? 312 A1BWC A F12  1 
HETATM 9407 F F33  . A1BWC N 5 .   ? -4.938  13.725  3.106   0.50 38.64  ? 312 A1BWC A F33  1 
HETATM 9408 F F34  . A1BWC N 5 .   ? -6.520  15.119  2.814   0.50 43.36  ? 312 A1BWC A F34  1 
HETATM 9409 F F35  . A1BWC N 5 .   ? -4.446  15.970  2.733   0.50 38.89  ? 312 A1BWC A F35  1 
HETATM 9410 N N15  . A1BWC N 5 .   ? -5.842  17.535  7.735   0.50 32.05  ? 312 A1BWC A N15  1 
HETATM 9411 N N17  . A1BWC N 5 .   ? -5.639  15.079  7.075   0.50 37.12  ? 312 A1BWC A N17  1 
HETATM 9412 O O3   . A1BWC N 5 .   ? -5.518  18.145  3.588   0.50 36.17  ? 312 A1BWC A O3   1 
HETATM 9413 H H61  . A1BWC N 5 .   ? -7.496  22.309  2.663   0.50 49.38  ? 312 A1BWC A H61  1 
HETATM 9414 H H91  . A1BWC N 5 .   ? -3.171  21.923  2.049   0.50 43.94  ? 312 A1BWC A H91  1 
HETATM 9415 C C4   . A1BWC O 5 .   ? 8.834   13.154  5.637   1.00 28.31  ? 313 A1BWC A C4   1 
HETATM 9416 C C5   . A1BWC O 5 .   ? 7.577   12.516  5.216   1.00 32.57  ? 313 A1BWC A C5   1 
HETATM 9417 C C6   . A1BWC O 5 .   ? 7.596   11.531  4.234   1.00 27.99  ? 313 A1BWC A C6   1 
HETATM 9418 C C7   . A1BWC O 5 .   ? 8.866   11.154  3.670   1.00 29.14  ? 313 A1BWC A C7   1 
HETATM 9419 C C10  . A1BWC O 5 .   ? 10.020  12.786  5.102   1.00 34.48  ? 313 A1BWC A C10  1 
HETATM 9420 C C13  . A1BWC O 5 .   ? 9.201   15.933  5.090   1.00 21.66  ? 313 A1BWC A C13  1 
HETATM 9421 C C20  . A1BWC O 5 .   ? 9.712   14.640  9.664   1.00 27.14  ? 313 A1BWC A C20  1 
HETATM 9422 C C21  . A1BWC O 5 .   ? 7.916   9.333   2.223   1.00 30.31  ? 313 A1BWC A C21  1 
HETATM 9423 C C24  . A1BWC O 5 .   ? 7.354   7.438   0.568   1.00 36.89  ? 313 A1BWC A C24  1 
HETATM 9424 C C26  . A1BWC O 5 .   ? 7.061   5.898   -1.385  1.00 56.92  ? 313 A1BWC A C26  1 
HETATM 9425 C C28  . A1BWC O 5 .   ? 7.993   5.282   -3.450  1.00 59.43  ? 313 A1BWC A C28  1 
HETATM 9426 C C1   . A1BWC O 5 .   ? 9.849   16.097  7.455   1.00 26.38  ? 313 A1BWC A C1   1 
HETATM 9427 C C14  . A1BWC O 5 .   ? 9.768   17.242  4.890   1.00 31.86  ? 313 A1BWC A C14  1 
HETATM 9428 C C16  . A1BWC O 5 .   ? 10.359  17.352  7.158   1.00 26.35  ? 313 A1BWC A C16  1 
HETATM 9429 C C18  . A1BWC O 5 .   ? 10.736  17.043  9.304   1.00 28.38  ? 313 A1BWC A C18  1 
HETATM 9430 C C19  . A1BWC O 5 .   ? 10.079  15.891  8.816   1.00 21.89  ? 313 A1BWC A C19  1 
HETATM 9431 C C2   . A1BWC O 5 .   ? 9.256   15.361  6.402   1.00 27.77  ? 313 A1BWC A C2   1 
HETATM 9432 C C25  . A1BWC O 5 .   ? 8.088   6.539   -0.416  1.00 50.25  ? 313 A1BWC A C25  1 
HETATM 9433 C C29  . A1BWC O 5 .   ? 7.536   3.629   -1.775  1.00 51.27  ? 313 A1BWC A C29  1 
HETATM 9434 C C30  . A1BWC O 5 .   ? 8.546   2.704   -2.446  1.00 52.78  ? 313 A1BWC A C30  1 
HETATM 9435 C C32  . A1BWC O 5 .   ? 9.015   4.338   -4.070  1.00 64.08  ? 313 A1BWC A C32  1 
HETATM 9436 C C9   . A1BWC O 5 .   ? 10.050  11.751  4.074   1.00 28.15  ? 313 A1BWC A C9   1 
HETATM 9437 F F11  . A1BWC O 5 .   ? 11.136  13.323  5.463   1.00 33.83  ? 313 A1BWC A F11  1 
HETATM 9438 F F12  . A1BWC O 5 .   ? 6.423   12.921  5.807   1.00 35.84  ? 313 A1BWC A F12  1 
HETATM 9439 F F33  . A1BWC O 5 .   ? 10.120  14.851  10.971  1.00 31.88  ? 313 A1BWC A F33  1 
HETATM 9440 F F34  . A1BWC O 5 .   ? 8.406   14.400  9.615   1.00 29.52  ? 313 A1BWC A F34  1 
HETATM 9441 F F35  . A1BWC O 5 .   ? 10.450  13.522  9.175   1.00 28.58  ? 313 A1BWC A F35  1 
HETATM 9442 N N15  . A1BWC O 5 .   ? 10.303  17.904  5.848   1.00 25.46  ? 313 A1BWC A N15  1 
HETATM 9443 N N17  . A1BWC O 5 .   ? 10.896  17.902  8.298   1.00 25.83  ? 313 A1BWC A N17  1 
HETATM 9444 N N22  . A1BWC O 5 .   ? 8.321   8.332   1.143   1.00 35.97  ? 313 A1BWC A N22  1 
HETATM 9445 N N27  . A1BWC O 5 .   ? 7.827   4.947   -2.132  1.00 58.32  ? 313 A1BWC A N27  1 
HETATM 9446 N N8   . A1BWC O 5 .   ? 9.003   10.178  2.683   1.00 25.85  ? 313 A1BWC A N8   1 
HETATM 9447 O O23  . A1BWC O 5 .   ? 6.776   9.404   2.644   1.00 36.39  ? 313 A1BWC A O23  1 
HETATM 9448 O O3   . A1BWC O 5 .   ? 8.728   14.132  6.675   1.00 33.19  ? 313 A1BWC A O3   1 
HETATM 9449 O O31  . A1BWC O 5 .   ? 8.750   2.988   -3.790  1.00 61.70  ? 313 A1BWC A O31  1 
HETATM 9450 H H61  . A1BWC O 5 .   ? 6.678   11.061  3.903   1.00 33.59  ? 313 A1BWC A H61  1 
HETATM 9451 H H131 . A1BWC O 5 .   ? 8.744   15.394  4.267   1.00 25.99  ? 313 A1BWC A H131 1 
HETATM 9452 H H242 . A1BWC O 5 .   ? 6.872   6.805   1.384   1.00 44.27  ? 313 A1BWC A H242 1 
HETATM 9453 H H241 . A1BWC O 5 .   ? 6.547   8.031   0.023   1.00 44.27  ? 313 A1BWC A H241 1 
HETATM 9454 H H262 . A1BWC O 5 .   ? 6.614   6.678   -2.071  1.00 68.31  ? 313 A1BWC A H262 1 
HETATM 9455 H H261 . A1BWC O 5 .   ? 6.234   5.382   -0.811  1.00 68.31  ? 313 A1BWC A H261 1 
HETATM 9456 H H281 . A1BWC O 5 .   ? 8.345   6.298   -3.525  1.00 71.32  ? 313 A1BWC A H281 1 
HETATM 9457 H H282 . A1BWC O 5 .   ? 7.053   5.192   -3.969  1.00 71.32  ? 313 A1BWC A H282 1 
HETATM 9458 H H141 . A1BWC O 5 .   ? 9.739   17.699  3.855   1.00 38.23  ? 313 A1BWC A H141 1 
HETATM 9459 H H181 . A1BWC O 5 .   ? 11.031  17.189  10.249  1.00 34.05  ? 313 A1BWC A H181 1 
HETATM 9460 H H251 . A1BWC O 5 .   ? 8.747   7.076   -0.934  1.00 60.30  ? 313 A1BWC A H251 1 
HETATM 9461 H H252 . A1BWC O 5 .   ? 8.572   5.824   0.079   1.00 60.30  ? 313 A1BWC A H252 1 
HETATM 9462 H H292 . A1BWC O 5 .   ? 7.602   3.509   -0.626  1.00 61.52  ? 313 A1BWC A H292 1 
HETATM 9463 H H291 . A1BWC O 5 .   ? 6.466   3.354   -2.123  1.00 61.52  ? 313 A1BWC A H291 1 
HETATM 9464 H H301 . A1BWC O 5 .   ? 8.195   1.702   -2.359  1.00 63.33  ? 313 A1BWC A H301 1 
HETATM 9465 H H302 . A1BWC O 5 .   ? 9.476   2.792   -1.934  1.00 63.33  ? 313 A1BWC A H302 1 
HETATM 9466 H H321 . A1BWC O 5 .   ? 9.007   4.478   -5.165  1.00 76.89  ? 313 A1BWC A H321 1 
HETATM 9467 H H322 . A1BWC O 5 .   ? 10.014  4.590   -3.675  1.00 76.89  ? 313 A1BWC A H322 1 
HETATM 9468 H H91  . A1BWC O 5 .   ? 11.055  11.430  3.599   1.00 33.78  ? 313 A1BWC A H91  1 
HETATM 9469 H H171 . A1BWC O 5 .   ? 11.342  18.813  8.362   1.00 31.00  ? 313 A1BWC A H171 1 
HETATM 9470 H H221 . A1BWC O 5 .   ? 9.255   8.299   0.836   1.00 43.16  ? 313 A1BWC A H221 1 
HETATM 9471 H H81  . A1BWC O 5 .   ? 10.008  10.039  2.218   1.00 31.02  ? 313 A1BWC A H81  1 
HETATM 9472 C C4   . A1BWC P 5 .   ? 16.561  13.791  20.242  1.00 32.33  ? 314 A1BWC A C4   1 
HETATM 9473 C C5   . A1BWC P 5 .   ? 15.103  13.806  20.489  1.00 37.38  ? 314 A1BWC A C5   1 
HETATM 9474 C C6   . A1BWC P 5 .   ? 14.604  13.180  21.631  1.00 40.40  ? 314 A1BWC A C6   1 
HETATM 9475 C C7   . A1BWC P 5 .   ? 15.489  12.520  22.547  1.00 42.71  ? 314 A1BWC A C7   1 
HETATM 9476 C C10  . A1BWC P 5 .   ? 17.388  13.158  21.106  1.00 37.47  ? 314 A1BWC A C10  1 
HETATM 9477 C C13  . A1BWC P 5 .   ? 16.570  16.701  19.614  1.00 29.72  ? 314 A1BWC A C13  1 
HETATM 9478 C C20  . A1BWC P 5 .   ? 17.031  13.599  16.047  1.00 27.18  ? 314 A1BWC A C20  1 
HETATM 9479 C C21  . A1BWC P 5 .   ? 15.692  11.232  24.723  1.00 46.68  ? 314 A1BWC A C21  1 
HETATM 9480 C C24  . A1BWC P 5 .   ? 15.650  9.935   26.940  1.00 59.69  ? 314 A1BWC A C24  1 
HETATM 9481 C C26  . A1BWC P 5 .   ? 16.385  7.464   27.234  1.00 60.86  ? 314 A1BWC A C26  1 
HETATM 9482 C C28  . A1BWC P 5 .   ? 15.622  6.749   29.324  1.00 57.74  ? 314 A1BWC A C28  1 
HETATM 9483 C C1   . A1BWC P 5 .   ? 16.547  15.863  17.314  1.00 29.11  ? 314 A1BWC A C1   1 
HETATM 9484 C C14  . A1BWC P 5 .   ? 16.158  17.984  19.100  1.00 30.86  ? 314 A1BWC A C14  1 
HETATM 9485 C C16  . A1BWC P 5 .   ? 16.152  17.127  16.918  1.00 30.93  ? 314 A1BWC A C16  1 
HETATM 9486 C C18  . A1BWC P 5 .   ? 16.276  15.925  15.069  1.00 25.89  ? 314 A1BWC A C18  1 
HETATM 9487 C C19  . A1BWC P 5 .   ? 16.633  15.096  16.151  1.00 27.66  ? 314 A1BWC A C19  1 
HETATM 9488 C C2   . A1BWC P 5 .   ? 16.754  15.621  18.689  1.00 29.38  ? 314 A1BWC A C2   1 
HETATM 9489 C C25  . A1BWC P 5 .   ? 15.252  8.457   26.825  1.00 57.17  ? 314 A1BWC A C25  1 
HETATM 9490 C C29  . A1BWC P 5 .   ? 17.898  7.062   28.986  1.00 54.85  ? 314 A1BWC A C29  1 
HETATM 9491 C C30  . A1BWC P 5 .   ? 18.108  5.563   28.758  1.00 62.17  ? 314 A1BWC A C30  1 
HETATM 9492 C C32  . A1BWC P 5 .   ? 15.827  5.232   29.301  1.00 58.89  ? 314 A1BWC A C32  1 
HETATM 9493 C C9   . A1BWC P 5 .   ? 16.859  12.502  22.302  1.00 40.89  ? 314 A1BWC A C9   1 
HETATM 9494 F F11  . A1BWC P 5 .   ? 18.665  13.130  20.896  1.00 42.34  ? 314 A1BWC A F11  1 
HETATM 9495 F F12  . A1BWC P 5 .   ? 14.236  14.418  19.636  1.00 46.11  ? 314 A1BWC A F12  1 
HETATM 9496 F F33  . A1BWC P 5 .   ? 17.084  13.255  14.706  1.00 31.10  ? 314 A1BWC A F33  1 
HETATM 9497 F F34  . A1BWC P 5 .   ? 18.225  13.383  16.595  1.00 29.68  ? 314 A1BWC A F34  1 
HETATM 9498 F F35  . A1BWC P 5 .   ? 16.025  12.815  16.702  1.00 28.60  ? 314 A1BWC A F35  1 
HETATM 9499 N N15  . A1BWC P 5 .   ? 15.959  18.195  17.850  1.00 26.83  ? 314 A1BWC A N15  1 
HETATM 9500 N N17  . A1BWC P 5 .   ? 15.997  17.132  15.548  1.00 26.57  ? 314 A1BWC A N17  1 
HETATM 9501 N N22  . A1BWC P 5 .   ? 14.916  10.632  25.904  1.00 49.73  ? 314 A1BWC A N22  1 
HETATM 9502 N N27  . A1BWC P 5 .   ? 16.595  7.476   28.673  1.00 54.60  ? 314 A1BWC A N27  1 
HETATM 9503 N N8   . A1BWC P 5 .   ? 14.918  11.912  23.684  1.00 45.71  ? 314 A1BWC A N8   1 
HETATM 9504 O O23  . A1BWC P 5 .   ? 16.901  11.124  24.691  1.00 44.40  ? 314 A1BWC A O23  1 
HETATM 9505 O O3   . A1BWC P 5 .   ? 17.171  14.381  19.081  1.00 30.40  ? 314 A1BWC A O3   1 
HETATM 9506 O O31  . A1BWC P 5 .   ? 17.153  4.788   29.402  1.00 69.35  ? 314 A1BWC A O31  1 
HETATM 9507 H H61  . A1BWC P 5 .   ? 13.539  13.193  21.827  1.00 48.48  ? 314 A1BWC A H61  1 
HETATM 9508 H H131 . A1BWC P 5 .   ? 16.736  16.557  20.677  1.00 35.67  ? 314 A1BWC A H131 1 
HETATM 9509 H H242 . A1BWC P 5 .   ? 15.369  10.339  27.968  1.00 71.62  ? 314 A1BWC A H242 1 
HETATM 9510 H H241 . A1BWC P 5 .   ? 16.772  10.054  26.781  1.00 71.62  ? 314 A1BWC A H241 1 
HETATM 9511 H H262 . A1BWC P 5 .   ? 17.347  7.764   26.720  1.00 73.04  ? 314 A1BWC A H262 1 
HETATM 9512 H H261 . A1BWC P 5 .   ? 16.097  6.418   26.913  1.00 73.04  ? 314 A1BWC A H261 1 
HETATM 9513 H H281 . A1BWC P 5 .   ? 14.674  6.967   28.860  1.00 69.28  ? 314 A1BWC A H281 1 
HETATM 9514 H H282 . A1BWC P 5 .   ? 15.598  7.069   30.353  1.00 69.28  ? 314 A1BWC A H282 1 
HETATM 9515 H H141 . A1BWC P 5 .   ? 16.003  18.837  19.828  1.00 37.03  ? 314 A1BWC A H141 1 
HETATM 9516 H H181 . A1BWC P 5 .   ? 16.239  15.653  14.108  1.00 31.07  ? 314 A1BWC A H181 1 
HETATM 9517 H H251 . A1BWC P 5 .   ? 14.995  8.271   25.881  1.00 68.61  ? 314 A1BWC A H251 1 
HETATM 9518 H H252 . A1BWC P 5 .   ? 14.464  8.295   27.411  1.00 68.61  ? 314 A1BWC A H252 1 
HETATM 9519 H H292 . A1BWC P 5 .   ? 18.112  7.303   30.098  1.00 65.82  ? 314 A1BWC A H292 1 
HETATM 9520 H H291 . A1BWC P 5 .   ? 18.647  7.646   28.323  1.00 65.82  ? 314 A1BWC A H291 1 
HETATM 9521 H H301 . A1BWC P 5 .   ? 18.063  5.368   27.713  1.00 74.60  ? 314 A1BWC A H301 1 
HETATM 9522 H H302 . A1BWC P 5 .   ? 19.072  5.295   29.122  1.00 74.60  ? 314 A1BWC A H302 1 
HETATM 9523 H H321 . A1BWC P 5 .   ? 15.263  4.801   30.146  1.00 70.67  ? 314 A1BWC A H321 1 
HETATM 9524 H H322 . A1BWC P 5 .   ? 15.415  4.849   28.351  1.00 70.67  ? 314 A1BWC A H322 1 
HETATM 9525 H H91  . A1BWC P 5 .   ? 17.575  11.972  23.040  1.00 49.07  ? 314 A1BWC A H91  1 
HETATM 9526 H H171 . A1BWC P 5 .   ? 15.714  17.935  14.992  1.00 31.89  ? 314 A1BWC A H171 1 
HETATM 9527 H H221 . A1BWC P 5 .   ? 13.937  10.719  25.957  1.00 59.68  ? 314 A1BWC A H221 1 
HETATM 9528 H H81  . A1BWC P 5 .   ? 13.809  11.951  23.798  1.00 54.85  ? 314 A1BWC A H81  1 
HETATM 9529 C C1   . EDO   Q 2 .   ? -6.189  -7.361  36.299  1.00 41.29  ? 301 EDO   B C1   1 
HETATM 9530 O O1   . EDO   Q 2 .   ? -7.279  -8.154  35.819  1.00 51.30  ? 301 EDO   B O1   1 
HETATM 9531 C C2   . EDO   Q 2 .   ? -5.554  -6.640  35.119  1.00 39.94  ? 301 EDO   B C2   1 
HETATM 9532 O O2   . EDO   Q 2 .   ? -4.912  -7.587  34.256  1.00 53.11  ? 301 EDO   B O2   1 
HETATM 9533 H H11  . EDO   Q 2 .   ? -5.451  -7.998  36.791  1.00 49.54  ? 301 EDO   B H11  1 
HETATM 9534 H H12  . EDO   Q 2 .   ? -6.548  -6.636  37.032  1.00 49.54  ? 301 EDO   B H12  1 
HETATM 9535 H HO1  . EDO   Q 2 .   ? -7.704  -8.602  36.563  1.00 61.56  ? 301 EDO   B HO1  1 
HETATM 9536 H H21  . EDO   Q 2 .   ? -6.320  -6.094  34.563  1.00 47.93  ? 301 EDO   B H21  1 
HETATM 9537 H H22  . EDO   Q 2 .   ? -4.822  -5.914  35.481  1.00 47.93  ? 301 EDO   B H22  1 
HETATM 9538 H HO2  . EDO   Q 2 .   ? -4.517  -7.123  33.505  1.00 63.74  ? 301 EDO   B HO2  1 
HETATM 9539 C C1   . EDO   R 2 .   ? -11.738 -22.838 29.158  1.00 47.52  ? 302 EDO   B C1   1 
HETATM 9540 O O1   . EDO   R 2 .   ? -13.005 -22.215 29.391  1.00 62.76  ? 302 EDO   B O1   1 
HETATM 9541 C C2   . EDO   R 2 .   ? -10.856 -21.896 28.353  1.00 44.43  ? 302 EDO   B C2   1 
HETATM 9542 O O2   . EDO   R 2 .   ? -11.146 -20.525 28.664  1.00 60.82  ? 302 EDO   B O2   1 
HETATM 9543 H H11  . EDO   R 2 .   ? -11.259 -23.074 30.110  1.00 57.02  ? 302 EDO   B H11  1 
HETATM 9544 H H12  . EDO   R 2 .   ? -11.879 -23.774 28.613  1.00 57.02  ? 302 EDO   B H12  1 
HETATM 9545 H HO1  . EDO   R 2 .   ? -13.567 -22.810 29.905  1.00 75.31  ? 302 EDO   B HO1  1 
HETATM 9546 H H21  . EDO   R 2 .   ? -9.807  -22.105 28.571  1.00 53.32  ? 302 EDO   B H21  1 
HETATM 9547 H H22  . EDO   R 2 .   ? -11.018 -22.069 27.286  1.00 53.32  ? 302 EDO   B H22  1 
HETATM 9548 H HO2  . EDO   R 2 .   ? -10.550 -19.949 28.166  1.00 72.98  ? 302 EDO   B HO2  1 
HETATM 9549 C C4   . A1BWC S 5 .   ? -7.001  -19.812 26.863  1.00 39.17  ? 303 A1BWC B C4   1 
HETATM 9550 C C5   . A1BWC S 5 .   ? -7.903  -19.111 25.931  1.00 40.43  ? 303 A1BWC B C5   1 
HETATM 9551 C C6   . A1BWC S 5 .   ? -8.805  -18.165 26.404  1.00 36.51  ? 303 A1BWC B C6   1 
HETATM 9552 C C7   . A1BWC S 5 .   ? -8.824  -17.875 27.808  1.00 44.65  ? 303 A1BWC B C7   1 
HETATM 9553 C C10  . A1BWC S 5 .   ? -7.037  -19.531 28.188  1.00 41.86  ? 303 A1BWC B C10  1 
HETATM 9554 C C13  . A1BWC S 5 .   ? -7.593  -22.508 27.196  1.00 30.65  ? 303 A1BWC B C13  1 
HETATM 9555 C C20  . A1BWC S 5 .   ? -3.212  -21.673 25.754  1.00 36.97  ? 303 A1BWC B C20  1 
HETATM 9556 C C21  . A1BWC S 5 .   ? -10.261 -15.844 27.558  1.00 42.34  ? 303 A1BWC B C21  1 
HETATM 9557 C C24  . A1BWC S 5 .   ? -11.799 -13.805 27.579  1.00 50.68  ? 303 A1BWC B C24  1 
HETATM 9558 C C26  . A1BWC S 5 .   ? -13.167 -11.707 27.942  1.00 60.32  ? 303 A1BWC B C26  1 
HETATM 9559 C C28  . A1BWC S 5 .   ? -13.996 -10.924 29.999  1.00 52.64  ? 303 A1BWC B C28  1 
HETATM 9560 C C1   . A1BWC S 5 .   ? -5.255  -22.994 26.680  1.00 29.70  ? 303 A1BWC B C1   1 
HETATM 9561 C C14  . A1BWC S 5 .   ? -7.732  -23.885 27.612  1.00 39.72  ? 303 A1BWC B C14  1 
HETATM 9562 C C16  . A1BWC S 5 .   ? -5.479  -24.290 27.094  1.00 31.03  ? 303 A1BWC B C16  1 
HETATM 9563 C C18  . A1BWC S 5 .   ? -3.364  -24.218 26.487  1.00 31.72  ? 303 A1BWC B C18  1 
HETATM 9564 C C19  . A1BWC S 5 .   ? -3.926  -22.933 26.304  1.00 31.83  ? 303 A1BWC B C19  1 
HETATM 9565 C C2   . A1BWC S 5 .   ? -6.315  -22.062 26.727  1.00 34.89  ? 303 A1BWC B C2   1 
HETATM 9566 C C25  . A1BWC S 5 .   ? -12.742 -13.082 28.529  1.00 50.43  ? 303 A1BWC B C25  1 
HETATM 9567 C C29  . A1BWC S 5 .   ? -13.015 -9.446  28.488  1.00 56.29  ? 303 A1BWC B C29  1 
HETATM 9568 C C30  . A1BWC S 5 .   ? -12.725 -8.466  29.625  1.00 63.98  ? 303 A1BWC B C30  1 
HETATM 9569 C C32  . A1BWC S 5 .   ? -13.645 -10.004 31.163  1.00 54.85  ? 303 A1BWC B C32  1 
HETATM 9570 C C9   . A1BWC S 5 .   ? -7.982  -18.537 28.689  1.00 40.04  ? 303 A1BWC B C9   1 
HETATM 9571 F F11  . A1BWC S 5 .   ? -6.263  -20.121 29.038  1.00 48.52  ? 303 A1BWC B F11  1 
HETATM 9572 F F12  . A1BWC S 5 .   ? -7.842  -19.408 24.610  1.00 44.55  ? 303 A1BWC B F12  1 
HETATM 9573 F F33  . A1BWC S 5 .   ? -1.865  -21.972 25.602  1.00 36.62  ? 303 A1BWC B F33  1 
HETATM 9574 F F34  . A1BWC S 5 .   ? -3.792  -21.367 24.604  1.00 36.70  ? 303 A1BWC B F34  1 
HETATM 9575 F F35  . A1BWC S 5 .   ? -3.356  -20.562 26.638  1.00 37.75  ? 303 A1BWC B F35  1 
HETATM 9576 N N15  . A1BWC S 5 .   ? -6.754  -24.714 27.560  1.00 34.51  ? 303 A1BWC B N15  1 
HETATM 9577 N N17  . A1BWC S 5 .   ? -4.316  -25.013 26.969  1.00 33.57  ? 303 A1BWC B N17  1 
HETATM 9578 N N22  . A1BWC S 5 .   ? -11.228 -14.919 28.292  1.00 46.86  ? 303 A1BWC B N22  1 
HETATM 9579 N N27  . A1BWC S 5 .   ? -13.059 -10.743 29.011  1.00 65.06  ? 303 A1BWC B N27  1 
HETATM 9580 N N8   . A1BWC S 5 .   ? -9.717  -16.941 28.344  1.00 39.09  ? 303 A1BWC B N8   1 
HETATM 9581 O O23  . A1BWC S 5 .   ? -9.985  -15.650 26.391  1.00 55.73  ? 303 A1BWC B O23  1 
HETATM 9582 O O3   . A1BWC S 5 .   ? -6.082  -20.774 26.312  1.00 43.15  ? 303 A1BWC B O3   1 
HETATM 9583 O O31  . A1BWC S 5 .   ? -13.494 -8.668  30.769  1.00 61.16  ? 303 A1BWC B O31  1 
HETATM 9584 H H61  . A1BWC S 5 .   ? -9.479  -17.657 25.725  1.00 43.81  ? 303 A1BWC B H61  1 
HETATM 9585 H H131 . A1BWC S 5 .   ? -8.438  -21.829 27.239  1.00 36.78  ? 303 A1BWC B H131 1 
HETATM 9586 H H242 . A1BWC S 5 .   ? -12.377 -14.178 26.670  1.00 60.81  ? 303 A1BWC B H242 1 
HETATM 9587 H H241 . A1BWC S 5 .   ? -10.975 -13.095 27.237  1.00 60.81  ? 303 A1BWC B H241 1 
HETATM 9588 H H262 . A1BWC S 5 .   ? -12.483 -11.417 27.089  1.00 72.38  ? 303 A1BWC B H262 1 
HETATM 9589 H H261 . A1BWC S 5 .   ? -14.234 -11.753 27.570  1.00 72.38  ? 303 A1BWC B H261 1 
HETATM 9590 H H281 . A1BWC S 5 .   ? -14.976 -10.680 29.622  1.00 63.16  ? 303 A1BWC B H281 1 
HETATM 9591 H H282 . A1BWC S 5 .   ? -13.986 -11.951 30.328  1.00 63.16  ? 303 A1BWC B H282 1 
HETATM 9592 H H141 . A1BWC S 5 .   ? -8.736  -24.242 27.996  1.00 47.66  ? 303 A1BWC B H141 1 
HETATM 9593 H H181 . A1BWC S 5 .   ? -2.420  -24.482 26.291  1.00 38.07  ? 303 A1BWC B H181 1 
HETATM 9594 H H251 . A1BWC S 5 .   ? -12.284 -12.940 29.402  1.00 60.51  ? 303 A1BWC B H251 1 
HETATM 9595 H H252 . A1BWC S 5 .   ? -13.552 -13.641 28.677  1.00 60.51  ? 303 A1BWC B H252 1 
HETATM 9596 H H292 . A1BWC S 5 .   ? -12.180 -9.373  27.689  1.00 67.54  ? 303 A1BWC B H292 1 
HETATM 9597 H H291 . A1BWC S 5 .   ? -14.031 -9.185  27.998  1.00 67.54  ? 303 A1BWC B H291 1 
HETATM 9598 H H301 . A1BWC S 5 .   ? -11.698 -8.556  29.889  1.00 76.78  ? 303 A1BWC B H301 1 
HETATM 9599 H H302 . A1BWC S 5 .   ? -12.906 -7.479  29.267  1.00 76.78  ? 303 A1BWC B H302 1 
HETATM 9600 H H321 . A1BWC S 5 .   ? -12.697 -10.348 31.613  1.00 65.82  ? 303 A1BWC B H321 1 
HETATM 9601 H H322 . A1BWC S 5 .   ? -14.450 -10.062 31.915  1.00 65.82  ? 303 A1BWC B H322 1 
HETATM 9602 H H91  . A1BWC S 5 .   ? -8.030  -18.302 29.821  1.00 48.05  ? 303 A1BWC B H91  1 
HETATM 9603 H H171 . A1BWC S 5 .   ? -4.203  -25.996 27.206  1.00 40.29  ? 303 A1BWC B H171 1 
HETATM 9604 H H221 . A1BWC S 5 .   ? -11.458 -15.079 29.236  1.00 56.24  ? 303 A1BWC B H221 1 
HETATM 9605 H H81  . A1BWC S 5 .   ? -10.023 -17.041 29.412  1.00 46.91  ? 303 A1BWC B H81  1 
HETATM 9606 O O    . HOH   T 6 .   ? 0.114   -4.661  19.763  1.00 42.88  ? 401 HOH   A O    1 
HETATM 9607 O O    . HOH   T 6 .   ? -5.764  14.219  9.222   1.00 35.20  ? 402 HOH   A O    1 
HETATM 9608 O O    . HOH   T 6 .   ? 36.886  10.654  20.851  1.00 45.77  ? 403 HOH   A O    1 
HETATM 9609 O O    . HOH   T 6 .   ? -1.846  5.935   23.600  1.00 35.24  ? 404 HOH   A O    1 
HETATM 9610 O O    . HOH   T 6 .   ? 12.200  33.927  8.065   1.00 43.27  ? 405 HOH   A O    1 
HETATM 9611 O O    . HOH   T 6 .   ? 11.848  14.100  16.915  1.00 50.45  ? 406 HOH   A O    1 
HETATM 9612 O O    . HOH   T 6 .   ? 23.153  23.111  22.758  1.00 38.80  ? 407 HOH   A O    1 
HETATM 9613 O O    . HOH   T 6 .   ? 30.195  22.285  3.622   1.00 35.61  ? 408 HOH   A O    1 
HETATM 9614 O O    . HOH   T 6 .   ? 20.459  1.280   15.952  1.00 32.86  ? 409 HOH   A O    1 
HETATM 9615 O O    . HOH   T 6 .   ? 11.867  12.739  18.749  1.00 48.09  ? 410 HOH   A O    1 
HETATM 9616 O O    . HOH   T 6 .   ? 6.488   10.650  15.189  1.00 34.13  ? 411 HOH   A O    1 
HETATM 9617 O O    . HOH   T 6 .   ? 13.583  6.941   14.915  1.00 36.33  ? 412 HOH   A O    1 
HETATM 9618 O O    . HOH   T 6 .   ? 11.475  5.712   0.736   1.00 32.23  ? 413 HOH   A O    1 
HETATM 9619 O O    . HOH   T 6 .   ? 5.587   7.789   4.354   1.00 36.44  ? 414 HOH   A O    1 
HETATM 9620 O O    . HOH   T 6 .   ? 4.680   -9.897  22.455  1.00 48.15  ? 415 HOH   A O    1 
HETATM 9621 O O    . HOH   T 6 .   ? -6.275  28.444  18.700  1.00 54.05  ? 416 HOH   A O    1 
HETATM 9622 O O    . HOH   T 6 .   ? 2.206   9.582   26.280  1.00 31.87  ? 417 HOH   A O    1 
HETATM 9623 O O    . HOH   T 6 .   ? 15.693  7.468   16.942  1.00 30.85  ? 418 HOH   A O    1 
HETATM 9624 O O    . HOH   T 6 .   ? 6.312   -4.311  37.996  1.00 27.33  ? 419 HOH   A O    1 
HETATM 9625 O O    . HOH   T 6 .   ? -5.913  9.574   8.236   1.00 36.95  ? 420 HOH   A O    1 
HETATM 9626 O O    . HOH   T 6 .   ? 35.410  5.686   21.102  1.00 28.29  ? 421 HOH   A O    1 
HETATM 9627 O O    . HOH   T 6 .   ? 18.621  22.862  11.284  1.00 27.76  ? 422 HOH   A O    1 
HETATM 9628 O O    . HOH   T 6 .   ? 27.897  -4.682  1.049   1.00 28.43  ? 423 HOH   A O    1 
HETATM 9629 O O    . HOH   T 6 .   ? -4.432  22.453  24.580  1.00 31.56  ? 424 HOH   A O    1 
HETATM 9630 O O    . HOH   T 6 .   ? 39.228  9.196   12.251  1.00 27.84  ? 425 HOH   A O    1 
HETATM 9631 O O    . HOH   T 6 .   ? -0.290  -7.267  26.312  1.00 49.99  ? 426 HOH   A O    1 
HETATM 9632 O O    . HOH   T 6 .   ? 40.301  0.709   -3.862  1.00 37.94  ? 427 HOH   A O    1 
HETATM 9633 O O    . HOH   T 6 .   ? 11.770  9.026   5.809   1.00 34.66  ? 428 HOH   A O    1 
HETATM 9634 O O    . HOH   T 6 .   ? 35.150  -7.852  7.888   1.00 42.96  ? 429 HOH   A O    1 
HETATM 9635 O O    . HOH   T 6 .   ? 36.347  -1.901  4.375   1.00 29.22  ? 430 HOH   A O    1 
HETATM 9636 O O    . HOH   T 6 .   ? 3.897   -6.110  32.579  1.00 35.12  ? 431 HOH   A O    1 
HETATM 9637 O O    . HOH   T 6 .   ? 12.287  28.056  16.180  1.00 44.76  ? 432 HOH   A O    1 
HETATM 9638 O O    . HOH   T 6 .   ? 33.490  18.742  10.137  1.00 27.77  ? 433 HOH   A O    1 
HETATM 9639 O O    . HOH   T 6 .   ? 12.425  10.343  9.655   1.00 39.05  ? 434 HOH   A O    1 
HETATM 9640 O O    . HOH   T 6 .   ? 35.395  -3.597  10.485  1.00 25.02  ? 435 HOH   A O    1 
HETATM 9641 O O    . HOH   T 6 .   ? 22.869  16.476  -11.936 1.00 39.41  ? 436 HOH   A O    1 
HETATM 9642 O O    . HOH   T 6 .   ? 35.448  18.011  4.675   1.00 30.02  ? 437 HOH   A O    1 
HETATM 9643 O O    . HOH   T 6 .   ? 16.919  0.193   -2.860  1.00 37.20  ? 438 HOH   A O    1 
HETATM 9644 O O    . HOH   T 6 .   ? 30.222  -1.720  -3.582  1.00 34.62  ? 439 HOH   A O    1 
HETATM 9645 O O    . HOH   T 6 .   ? -0.341  9.175   26.471  1.00 35.52  ? 440 HOH   A O    1 
HETATM 9646 O O    . HOH   T 6 .   ? 23.322  -6.558  0.506   1.00 36.60  ? 441 HOH   A O    1 
HETATM 9647 O O    . HOH   T 6 .   ? 25.611  -6.037  9.441   1.00 35.56  ? 442 HOH   A O    1 
HETATM 9648 O O    . HOH   T 6 .   ? 30.556  22.179  -5.201  1.00 33.04  ? 443 HOH   A O    1 
HETATM 9649 O O    . HOH   T 6 .   ? -1.282  8.219   10.230  1.00 47.43  ? 444 HOH   A O    1 
HETATM 9650 O O    . HOH   T 6 .   ? -6.859  22.289  14.099  1.00 46.51  ? 445 HOH   A O    1 
HETATM 9651 O O    . HOH   T 6 .   ? 2.361   22.613  27.871  1.00 41.01  ? 446 HOH   A O    1 
HETATM 9652 O O    . HOH   T 6 .   ? -7.262  18.346  22.774  1.00 31.83  ? 447 HOH   A O    1 
HETATM 9653 O O    . HOH   T 6 .   ? 30.776  10.000  19.883  1.00 24.42  ? 448 HOH   A O    1 
HETATM 9654 O O    . HOH   T 6 .   ? 12.522  26.257  9.595   1.00 33.76  ? 449 HOH   A O    1 
HETATM 9655 O O    . HOH   T 6 .   ? 36.478  -4.295  1.063   1.00 46.11  ? 450 HOH   A O    1 
HETATM 9656 O O    . HOH   T 6 .   ? 4.357   18.907  28.599  1.00 52.36  ? 451 HOH   A O    1 
HETATM 9657 O O    . HOH   T 6 .   ? 16.920  3.685   5.160   1.00 20.59  ? 452 HOH   A O    1 
HETATM 9658 O O    . HOH   T 6 .   ? 15.573  23.329  19.855  1.00 41.78  ? 453 HOH   A O    1 
HETATM 9659 O O    . HOH   T 6 .   ? 23.793  -5.363  7.855   1.00 29.81  ? 454 HOH   A O    1 
HETATM 9660 O O    . HOH   T 6 .   ? -3.686  7.933   17.149  1.00 46.57  ? 455 HOH   A O    1 
HETATM 9661 O O    . HOH   T 6 .   ? 24.657  -3.927  0.600   1.00 27.30  ? 456 HOH   A O    1 
HETATM 9662 O O    . HOH   T 6 .   ? 15.649  23.131  5.673   1.00 29.59  ? 457 HOH   A O    1 
HETATM 9663 O O    . HOH   T 6 .   ? 34.934  -2.175  2.144   1.00 28.80  ? 458 HOH   A O    1 
HETATM 9664 O O    . HOH   T 6 .   ? -8.042  23.665  25.264  1.00 48.85  ? 459 HOH   A O    1 
HETATM 9665 O O    . HOH   T 6 .   ? 29.203  18.917  15.915  1.00 38.84  ? 460 HOH   A O    1 
HETATM 9666 O O    . HOH   T 6 .   ? 31.516  9.029   22.306  1.00 34.59  ? 461 HOH   A O    1 
HETATM 9667 O O    . HOH   T 6 .   ? 27.351  0.574   -6.299  1.00 40.65  ? 462 HOH   A O    1 
HETATM 9668 O O    . HOH   T 6 .   ? 10.371  12.086  -0.502  1.00 34.92  ? 463 HOH   A O    1 
HETATM 9669 O O    . HOH   T 6 .   ? -8.602  11.960  18.596  1.00 37.77  ? 464 HOH   A O    1 
HETATM 9670 O O    . HOH   T 6 .   ? 31.285  21.486  8.069   1.00 33.66  ? 465 HOH   A O    1 
HETATM 9671 O O    . HOH   T 6 .   ? 11.932  25.190  7.445   1.00 28.12  ? 466 HOH   A O    1 
HETATM 9672 O O    . HOH   T 6 .   ? -1.745  11.420  12.308  1.00 41.00  ? 467 HOH   A O    1 
HETATM 9673 O O    . HOH   T 6 .   ? 3.731   -2.542  39.217  1.00 39.39  ? 468 HOH   A O    1 
HETATM 9674 O O    . HOH   T 6 .   ? 30.208  -7.683  3.411   1.00 32.14  ? 469 HOH   A O    1 
HETATM 9675 O O    . HOH   T 6 .   ? -4.310  8.013   31.237  1.00 44.08  ? 470 HOH   A O    1 
HETATM 9676 O O    . HOH   T 6 .   ? 35.399  19.971  2.149   1.00 32.85  ? 471 HOH   A O    1 
HETATM 9677 O O    . HOH   T 6 .   ? 10.344  13.549  13.686  1.00 47.05  ? 472 HOH   A O    1 
HETATM 9678 O O    . HOH   T 6 .   ? 36.995  10.493  -1.742  1.00 37.57  ? 473 HOH   A O    1 
HETATM 9679 O O    . HOH   T 6 .   ? 28.013  5.315   -7.181  1.00 32.09  ? 474 HOH   A O    1 
HETATM 9680 O O    . HOH   T 6 .   ? 22.609  2.678   -8.759  1.00 39.07  ? 475 HOH   A O    1 
HETATM 9681 O O    . HOH   T 6 .   ? 13.546  22.402  1.520   1.00 24.59  ? 476 HOH   A O    1 
HETATM 9682 O O    . HOH   T 6 .   ? 26.694  22.131  9.920   1.00 38.18  ? 477 HOH   A O    1 
HETATM 9683 O O    . HOH   T 6 .   ? 27.938  -9.155  7.298   1.00 38.26  ? 478 HOH   A O    1 
HETATM 9684 O O    . HOH   T 6 .   ? 42.786  2.047   9.998   1.00 42.64  ? 479 HOH   A O    1 
HETATM 9685 O O    . HOH   T 6 .   ? 24.313  20.210  5.312   1.00 26.16  ? 480 HOH   A O    1 
HETATM 9686 O O    . HOH   T 6 .   ? 42.229  4.660   -3.362  1.00 41.57  ? 481 HOH   A O    1 
HETATM 9687 O O    . HOH   T 6 .   ? 35.307  16.821  9.067   1.00 33.10  ? 482 HOH   A O    1 
HETATM 9688 O O    . HOH   T 6 .   ? 21.519  2.134   29.527  1.00 49.55  ? 483 HOH   A O    1 
HETATM 9689 O O    . HOH   T 6 .   ? 29.803  -6.277  19.842  1.00 40.04  ? 484 HOH   A O    1 
HETATM 9690 O O    . HOH   T 6 .   ? 0.610   7.537   17.607  1.00 35.97  ? 485 HOH   A O    1 
HETATM 9691 O O    . HOH   T 6 .   ? 21.950  4.475   15.086  1.00 25.17  ? 486 HOH   A O    1 
HETATM 9692 O O    . HOH   T 6 .   ? 23.567  -1.651  -6.095  1.00 40.75  ? 487 HOH   A O    1 
HETATM 9693 O O    . HOH   T 6 .   ? 42.115  6.955   -0.419  1.00 37.50  ? 488 HOH   A O    1 
HETATM 9694 O O    . HOH   T 6 .   ? 19.120  9.450   24.125  1.00 30.35  ? 489 HOH   A O    1 
HETATM 9695 O O    . HOH   T 6 .   ? 27.947  23.298  1.811   1.00 31.09  ? 490 HOH   A O    1 
HETATM 9696 O O    . HOH   T 6 .   ? -2.123  17.457  -0.108  1.00 49.15  ? 491 HOH   A O    1 
HETATM 9697 O O    . HOH   T 6 .   ? -9.121  21.866  22.066  1.00 41.74  ? 492 HOH   A O    1 
HETATM 9698 O O    . HOH   T 6 .   ? 17.862  21.870  -5.500  1.00 41.50  ? 493 HOH   A O    1 
HETATM 9699 O O    . HOH   T 6 .   ? 32.960  10.386  -5.882  1.00 35.26  ? 494 HOH   A O    1 
HETATM 9700 O O    . HOH   T 6 .   ? 30.914  14.526  20.943  1.00 29.05  ? 495 HOH   A O    1 
HETATM 9701 O O    . HOH   T 6 .   ? -7.128  5.500   25.228  1.00 41.77  ? 496 HOH   A O    1 
HETATM 9702 O O    . HOH   T 6 .   ? 5.514   27.241  16.078  1.00 37.58  ? 497 HOH   A O    1 
HETATM 9703 O O    . HOH   T 6 .   ? -5.236  35.309  20.082  1.00 58.45  ? 498 HOH   A O    1 
HETATM 9704 O O    . HOH   T 6 .   ? 27.801  -11.362 2.654   1.00 33.49  ? 499 HOH   A O    1 
HETATM 9705 O O    . HOH   T 6 .   ? 24.331  12.979  -8.814  1.00 37.73  ? 500 HOH   A O    1 
HETATM 9706 O O    . HOH   T 6 .   ? 34.769  6.420   -5.944  1.00 36.76  ? 501 HOH   A O    1 
HETATM 9707 O O    . HOH   T 6 .   ? -7.741  13.282  16.694  1.00 32.52  ? 502 HOH   A O    1 
HETATM 9708 O O    . HOH   T 6 .   ? 9.130   -9.243  29.399  1.00 45.37  ? 503 HOH   A O    1 
HETATM 9709 O O    . HOH   T 6 .   ? 12.496  14.972  14.018  1.00 43.76  ? 504 HOH   A O    1 
HETATM 9710 O O    . HOH   T 6 .   ? -6.710  21.315  11.585  1.00 51.15  ? 505 HOH   A O    1 
HETATM 9711 O O    . HOH   T 6 .   ? 16.162  21.182  17.212  1.00 25.63  ? 506 HOH   A O    1 
HETATM 9712 O O    . HOH   T 6 .   ? 18.211  21.863  15.466  1.00 20.59  ? 507 HOH   A O    1 
HETATM 9713 O O    . HOH   T 6 .   ? 10.832  12.169  21.004  1.00 47.92  ? 508 HOH   A O    1 
HETATM 9714 O O    . HOH   T 6 .   ? 16.688  -1.364  24.453  1.00 53.69  ? 509 HOH   A O    1 
HETATM 9715 O O    . HOH   T 6 .   ? 31.007  5.992   25.460  1.00 57.37  ? 510 HOH   A O    1 
HETATM 9716 O O    . HOH   T 6 .   ? 11.010  28.734  3.496   1.00 36.06  ? 511 HOH   A O    1 
HETATM 9717 O O    . HOH   T 6 .   ? 29.324  21.272  14.484  1.00 43.67  ? 512 HOH   A O    1 
HETATM 9718 O O    . HOH   T 6 .   ? 28.521  -1.581  -5.278  1.00 37.12  ? 513 HOH   A O    1 
HETATM 9719 O O    . HOH   T 6 .   ? 32.134  7.349   -6.817  1.00 33.17  ? 514 HOH   A O    1 
HETATM 9720 O O    . HOH   T 6 .   ? -0.486  12.422  0.905   1.00 40.76  ? 515 HOH   A O    1 
HETATM 9721 O O    . HOH   T 6 .   ? 37.355  7.378   19.764  1.00 27.74  ? 516 HOH   A O    1 
HETATM 9722 O O    . HOH   T 6 .   ? 24.768  10.128  -7.974  1.00 36.74  ? 517 HOH   A O    1 
HETATM 9723 O O    . HOH   T 6 .   ? 13.949  -0.365  6.775   1.00 40.20  ? 518 HOH   A O    1 
HETATM 9724 O O    . HOH   T 6 .   ? -4.600  25.725  6.834   1.00 43.43  ? 519 HOH   A O    1 
HETATM 9725 O O    . HOH   T 6 .   ? 41.499  0.060   5.277   1.00 32.09  ? 520 HOH   A O    1 
HETATM 9726 O O    . HOH   T 6 .   ? 41.754  0.889   3.144   1.00 34.71  ? 521 HOH   A O    1 
HETATM 9727 O O    . HOH   T 6 .   ? 42.370  6.910   5.519   1.00 36.65  ? 522 HOH   A O    1 
HETATM 9728 O O    . HOH   T 6 .   ? -10.654 17.988  12.302  1.00 42.23  ? 523 HOH   A O    1 
HETATM 9729 O O    . HOH   T 6 .   ? -1.937  9.736   14.399  1.00 28.04  ? 524 HOH   A O    1 
HETATM 9730 O O    . HOH   T 6 .   ? 27.947  -15.119 11.660  1.00 42.21  ? 525 HOH   A O    1 
HETATM 9731 O O    . HOH   T 6 .   ? -6.047  20.698  15.548  1.00 38.96  ? 526 HOH   A O    1 
HETATM 9732 O O    . HOH   T 6 .   ? 11.650  7.573   3.908   1.00 33.96  ? 527 HOH   A O    1 
HETATM 9733 O O    . HOH   T 6 .   ? 7.126   3.489   23.583  1.00 48.55  ? 528 HOH   A O    1 
HETATM 9734 O O    . HOH   T 6 .   ? 25.047  24.411  14.341  1.00 39.01  ? 529 HOH   A O    1 
HETATM 9735 O O    . HOH   T 6 .   ? 2.615   8.249   2.992   1.00 38.02  ? 530 HOH   A O    1 
HETATM 9736 O O    . HOH   T 6 .   ? 23.994  22.852  7.140   1.00 36.24  ? 531 HOH   A O    1 
HETATM 9737 O O    . HOH   T 6 .   ? 19.635  21.433  -7.717  1.00 35.42  ? 532 HOH   A O    1 
HETATM 9738 O O    . HOH   T 6 .   ? 5.711   25.144  21.870  1.00 43.62  ? 533 HOH   A O    1 
HETATM 9739 O O    . HOH   T 6 .   ? 32.186  12.301  19.897  1.00 32.83  ? 534 HOH   A O    1 
HETATM 9740 O O    . HOH   T 6 .   ? 4.536   24.642  30.440  1.00 55.08  ? 535 HOH   A O    1 
HETATM 9741 O O    . HOH   T 6 .   ? 8.843   14.121  16.827  1.00 41.30  ? 536 HOH   A O    1 
HETATM 9742 O O    . HOH   T 6 .   ? 16.253  24.614  1.376   1.00 28.86  ? 537 HOH   A O    1 
HETATM 9743 O O    . HOH   T 6 .   ? -14.012 12.373  22.136  1.00 40.98  ? 538 HOH   A O    1 
HETATM 9744 O O    . HOH   T 6 .   ? 36.085  -5.354  14.220  1.00 32.53  ? 539 HOH   A O    1 
HETATM 9745 O O    . HOH   T 6 .   ? 24.621  0.603   -7.422  1.00 45.08  ? 540 HOH   A O    1 
HETATM 9746 O O    . HOH   T 6 .   ? 18.588  23.992  13.951  1.00 28.31  ? 541 HOH   A O    1 
HETATM 9747 O O    . HOH   T 6 .   ? 16.481  1.064   16.138  1.00 53.21  ? 542 HOH   A O    1 
HETATM 9748 O O    . HOH   T 6 .   ? 13.704  10.783  -12.061 1.00 47.84  ? 543 HOH   A O    1 
HETATM 9749 O O    . HOH   T 6 .   ? 20.898  25.379  14.535  1.00 37.30  ? 544 HOH   A O    1 
HETATM 9750 O O    . HOH   T 6 .   ? 10.664  7.069   -3.534  1.00 42.70  ? 545 HOH   A O    1 
HETATM 9751 O O    . HOH   T 6 .   ? -0.278  34.826  18.610  1.00 55.72  ? 546 HOH   A O    1 
HETATM 9752 O O    . HOH   T 6 .   ? 21.205  4.666   27.380  1.00 43.10  ? 547 HOH   A O    1 
HETATM 9753 O O    . HOH   T 6 .   ? 20.409  8.668   26.583  1.00 51.89  ? 548 HOH   A O    1 
HETATM 9754 O O    . HOH   T 6 .   ? 38.076  11.147  -3.641  1.00 49.81  ? 549 HOH   A O    1 
HETATM 9755 O O    . HOH   T 6 .   ? -1.637  -2.439  26.896  1.00 33.86  ? 550 HOH   A O    1 
HETATM 9756 O O    . HOH   T 6 .   ? 40.500  9.553   -1.304  1.00 41.07  ? 551 HOH   A O    1 
HETATM 9757 O O    . HOH   T 6 .   ? 30.917  13.767  23.535  1.00 42.46  ? 552 HOH   A O    1 
HETATM 9758 O O    . HOH   T 6 .   ? 16.183  26.254  -0.621  1.00 43.23  ? 553 HOH   A O    1 
HETATM 9759 O O    . HOH   T 6 .   ? 39.194  -2.714  4.309   1.00 45.30  ? 554 HOH   A O    1 
HETATM 9760 O O    . HOH   T 6 .   ? 10.367  6.061   4.830   1.00 44.17  ? 555 HOH   A O    1 
HETATM 9761 O O    . HOH   T 6 .   ? 8.138   6.434   5.402   1.00 52.27  ? 556 HOH   A O    1 
HETATM 9762 O O    . HOH   T 6 .   ? -2.273  22.289  26.228  1.00 32.80  ? 557 HOH   A O    1 
HETATM 9763 O O    . HOH   T 6 .   ? -2.586  -5.486  26.984  1.00 48.97  ? 558 HOH   A O    1 
HETATM 9764 O O    . HOH   U 6 .   ? -6.051  -37.064 43.102  1.00 44.16  ? 401 HOH   B O    1 
HETATM 9765 O O    . HOH   U 6 .   ? -14.793 -26.854 49.329  1.00 56.59  ? 402 HOH   B O    1 
HETATM 9766 O O    . HOH   U 6 .   ? -0.602  -3.155  46.657  1.00 30.19  ? 403 HOH   B O    1 
HETATM 9767 O O    . HOH   U 6 .   ? 12.482  7.784   34.948  1.00 47.38  ? 404 HOH   B O    1 
HETATM 9768 O O    . HOH   U 6 .   ? 4.355   -10.603 33.267  1.00 36.02  ? 405 HOH   B O    1 
HETATM 9769 O O    . HOH   U 6 .   ? -1.748  -34.364 36.895  1.00 43.17  ? 406 HOH   B O    1 
HETATM 9770 O O    . HOH   U 6 .   ? 16.095  -23.714 37.696  1.00 42.46  ? 407 HOH   B O    1 
HETATM 9771 O O    . HOH   U 6 .   ? -7.381  -29.508 50.186  1.00 36.82  ? 408 HOH   B O    1 
HETATM 9772 O O    . HOH   U 6 .   ? -2.113  -7.778  30.919  1.00 44.26  ? 409 HOH   B O    1 
HETATM 9773 O O    . HOH   U 6 .   ? 7.791   -5.962  10.891  1.00 39.98  ? 410 HOH   B O    1 
HETATM 9774 O O    . HOH   U 6 .   ? 24.397  -3.969  11.261  1.00 23.35  ? 411 HOH   B O    1 
HETATM 9775 O O    . HOH   U 6 .   ? 5.542   1.516   13.458  1.00 39.25  ? 412 HOH   B O    1 
HETATM 9776 O O    . HOH   U 6 .   ? 7.679   -27.400 45.984  1.00 47.95  ? 413 HOH   B O    1 
HETATM 9777 O O    . HOH   U 6 .   ? 1.842   -19.219 30.487  1.00 34.26  ? 414 HOH   B O    1 
HETATM 9778 O O    . HOH   U 6 .   ? 18.574  -1.587  12.016  1.00 26.35  ? 415 HOH   B O    1 
HETATM 9779 O O    . HOH   U 6 .   ? 2.098   -23.172 4.570   1.00 51.06  ? 416 HOH   B O    1 
HETATM 9780 O O    . HOH   U 6 .   ? -0.566  -28.104 40.133  1.00 29.73  ? 417 HOH   B O    1 
HETATM 9781 O O    . HOH   U 6 .   ? 6.677   -12.760 10.853  1.00 39.44  ? 418 HOH   B O    1 
HETATM 9782 O O    . HOH   U 6 .   ? -3.272  -3.609  43.484  1.00 35.70  ? 419 HOH   B O    1 
HETATM 9783 O O    . HOH   U 6 .   ? 15.587  -19.462 38.408  1.00 35.61  ? 420 HOH   B O    1 
HETATM 9784 O O    . HOH   U 6 .   ? 4.503   -26.569 50.069  1.00 36.20  ? 421 HOH   B O    1 
HETATM 9785 O O    . HOH   U 6 .   ? -15.917 -35.005 18.203  1.00 63.33  ? 422 HOH   B O    1 
HETATM 9786 O O    . HOH   U 6 .   ? -7.348  -14.505 30.688  1.00 42.99  ? 423 HOH   B O    1 
HETATM 9787 O O    . HOH   U 6 .   ? 1.421   -30.620 52.719  1.00 53.16  ? 424 HOH   B O    1 
HETATM 9788 O O    . HOH   U 6 .   ? -3.441  -11.019 34.385  1.00 20.59  ? 425 HOH   B O    1 
HETATM 9789 O O    . HOH   U 6 .   ? 5.887   -18.986 27.469  1.00 47.72  ? 426 HOH   B O    1 
HETATM 9790 O O    . HOH   U 6 .   ? -3.474  3.170   45.823  1.00 50.02  ? 427 HOH   B O    1 
HETATM 9791 O O    . HOH   U 6 .   ? -13.149 -19.656 34.297  1.00 56.57  ? 428 HOH   B O    1 
HETATM 9792 O O    . HOH   U 6 .   ? -6.507  7.033   40.487  1.00 32.88  ? 429 HOH   B O    1 
HETATM 9793 O O    . HOH   U 6 .   ? 5.181   -16.337 27.625  1.00 41.73  ? 430 HOH   B O    1 
HETATM 9794 O O    . HOH   U 6 .   ? 0.429   -30.839 46.484  1.00 40.21  ? 431 HOH   B O    1 
HETATM 9795 O O    . HOH   U 6 .   ? -7.760  -8.110  49.359  1.00 45.90  ? 432 HOH   B O    1 
HETATM 9796 O O    . HOH   U 6 .   ? -11.091 -17.557 47.653  1.00 40.13  ? 433 HOH   B O    1 
HETATM 9797 O O    . HOH   U 6 .   ? 14.013  -0.758  11.705  1.00 46.72  ? 434 HOH   B O    1 
HETATM 9798 O O    . HOH   U 6 .   ? -0.189  -24.438 56.332  1.00 43.28  ? 435 HOH   B O    1 
HETATM 9799 O O    . HOH   U 6 .   ? -9.668  -29.338 32.426  1.00 36.38  ? 436 HOH   B O    1 
HETATM 9800 O O    . HOH   U 6 .   ? 0.421   -10.042 28.266  1.00 48.92  ? 437 HOH   B O    1 
HETATM 9801 O O    . HOH   U 6 .   ? 7.487   -12.872 33.731  1.00 30.06  ? 438 HOH   B O    1 
HETATM 9802 O O    . HOH   U 6 .   ? 3.673   -6.450  51.429  1.00 33.84  ? 439 HOH   B O    1 
HETATM 9803 O O    . HOH   U 6 .   ? -2.374  -12.952 27.878  1.00 54.17  ? 440 HOH   B O    1 
HETATM 9804 O O    . HOH   U 6 .   ? 7.907   -4.905  49.176  1.00 45.67  ? 441 HOH   B O    1 
HETATM 9805 O O    . HOH   U 6 .   ? -3.977  -6.210  50.482  1.00 37.79  ? 442 HOH   B O    1 
HETATM 9806 O O    . HOH   U 6 .   ? -5.749  -32.514 27.005  1.00 47.56  ? 443 HOH   B O    1 
HETATM 9807 O O    . HOH   U 6 .   ? 5.995   -6.662  51.351  1.00 36.51  ? 444 HOH   B O    1 
HETATM 9808 O O    . HOH   U 6 .   ? -9.940  -7.152  38.190  1.00 42.36  ? 445 HOH   B O    1 
HETATM 9809 O O    . HOH   U 6 .   ? -7.132  -12.172 57.075  1.00 43.08  ? 446 HOH   B O    1 
HETATM 9810 O O    . HOH   U 6 .   ? -4.182  -14.338 55.591  1.00 45.11  ? 447 HOH   B O    1 
HETATM 9811 O O    . HOH   U 6 .   ? -5.584  -18.293 53.611  1.00 46.41  ? 448 HOH   B O    1 
HETATM 9812 O O    . HOH   U 6 .   ? 2.636   -14.622 15.788  1.00 45.76  ? 449 HOH   B O    1 
HETATM 9813 O O    . HOH   U 6 .   ? 23.172  0.528   16.287  1.00 20.59  ? 450 HOH   B O    1 
HETATM 9814 O O    . HOH   U 6 .   ? 9.474   -8.998  34.291  1.00 31.49  ? 451 HOH   B O    1 
HETATM 9815 O O    . HOH   U 6 .   ? -6.377  -6.056  50.280  1.00 47.51  ? 452 HOH   B O    1 
HETATM 9816 O O    . HOH   U 6 .   ? 19.763  -15.400 42.032  1.00 47.04  ? 453 HOH   B O    1 
HETATM 9817 O O    . HOH   U 6 .   ? -0.091  -30.775 38.813  1.00 33.08  ? 454 HOH   B O    1 
HETATM 9818 O O    . HOH   U 6 .   ? 10.043  6.194   41.643  1.00 41.49  ? 455 HOH   B O    1 
HETATM 9819 O O    . HOH   U 6 .   ? 8.117   -9.218  32.002  1.00 42.13  ? 456 HOH   B O    1 
HETATM 9820 O O    . HOH   U 6 .   ? 7.401   -11.669 21.875  1.00 50.08  ? 457 HOH   B O    1 
HETATM 9821 O O    . HOH   U 6 .   ? -0.968  -30.368 42.773  1.00 41.00  ? 458 HOH   B O    1 
HETATM 9822 O O    . HOH   U 6 .   ? 11.156  -27.813 27.609  1.00 54.04  ? 459 HOH   B O    1 
HETATM 9823 O O    . HOH   U 6 .   ? -1.253  -30.932 51.230  1.00 49.81  ? 460 HOH   B O    1 
HETATM 9824 O O    . HOH   U 6 .   ? 2.398   -0.453  46.938  1.00 37.84  ? 461 HOH   B O    1 
HETATM 9825 O O    . HOH   U 6 .   ? 5.452   1.257   43.567  1.00 41.96  ? 462 HOH   B O    1 
HETATM 9826 O O    . HOH   U 6 .   ? -8.646  -37.602 41.500  1.00 34.54  ? 463 HOH   B O    1 
HETATM 9827 O O    . HOH   U 6 .   ? 16.216  -21.578 39.655  1.00 44.12  ? 464 HOH   B O    1 
HETATM 9828 O O    . HOH   U 6 .   ? 10.739  -28.097 39.365  1.00 46.21  ? 465 HOH   B O    1 
HETATM 9829 O O    . HOH   U 6 .   ? 1.806   -13.533 60.787  1.00 42.85  ? 466 HOH   B O    1 
HETATM 9830 O O    . HOH   U 6 .   ? 0.230   -14.785 13.823  1.00 50.42  ? 467 HOH   B O    1 
HETATM 9831 O O    . HOH   U 6 .   ? 18.094  -4.512  45.687  1.00 41.75  ? 468 HOH   B O    1 
HETATM 9832 O O    . HOH   U 6 .   ? -13.041 -30.217 12.429  1.00 53.29  ? 469 HOH   B O    1 
HETATM 9833 O O    . HOH   U 6 .   ? -3.411  -17.263 28.134  1.00 44.52  ? 470 HOH   B O    1 
HETATM 9834 O O    . HOH   U 6 .   ? 19.252  0.172   13.766  1.00 31.31  ? 471 HOH   B O    1 
HETATM 9835 O O    . HOH   U 6 .   ? 10.990  -19.636 25.542  1.00 52.56  ? 472 HOH   B O    1 
HETATM 9836 O O    . HOH   U 6 .   ? -4.619  3.399   32.855  1.00 47.33  ? 473 HOH   B O    1 
HETATM 9837 O O    . HOH   U 6 .   ? -3.749  5.327   31.627  1.00 43.39  ? 474 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . PRO A 21  ? 0.9598 0.8544 0.7256 -0.0220 0.0132  -0.2303 6   PRO A N   
2    C CA  . PRO A 21  ? 0.9271 0.8354 0.7258 -0.0121 0.0215  -0.2063 6   PRO A CA  
3    C C   . PRO A 21  ? 0.8805 0.8228 0.7010 -0.0185 0.0067  -0.1899 6   PRO A C   
4    O O   . PRO A 21  ? 0.8696 0.8144 0.7176 -0.0261 0.0008  -0.1833 6   PRO A O   
5    C CB  . PRO A 21  ? 0.9982 0.8804 0.8193 -0.0145 0.0294  -0.2086 6   PRO A CB  
6    C CG  . PRO A 21  ? 1.0858 0.9523 0.8993 -0.0324 0.0169  -0.2287 6   PRO A CG  
7    C CD  . PRO A 21  ? 1.0906 0.9563 0.8630 -0.0351 0.0107  -0.2466 6   PRO A CD  
15   N N   . ASP A 22  ? 0.9152 0.8823 0.7225 -0.0144 0.0021  -0.1829 7   ASP A N   
16   C CA  . ASP A 22  ? 0.8668 0.8642 0.6930 -0.0186 -0.0094 -0.1666 7   ASP A CA  
17   C C   . ASP A 22  ? 0.8206 0.8235 0.6796 -0.0133 -0.0031 -0.1482 7   ASP A C   
18   O O   . ASP A 22  ? 0.7710 0.7786 0.6528 -0.0210 -0.0107 -0.1422 7   ASP A O   
19   C CB  . ASP A 22  ? 0.9678 0.9879 0.7745 -0.0117 -0.0106 -0.1603 7   ASP A CB  
20   C CG  . ASP A 22  ? 1.0494 1.0964 0.8617 -0.0204 -0.0265 -0.1530 7   ASP A CG  
21   O OD1 . ASP A 22  ? 1.0497 1.0966 0.8580 -0.0334 -0.0399 -0.1639 7   ASP A OD1 
22   O OD2 . ASP A 22  ? 1.0262 1.0947 0.8480 -0.0142 -0.0251 -0.1357 7   ASP A OD2 
27   N N   . ILE A 23  ? 0.6478 0.6509 0.5090 0.0001  0.0108  -0.1389 8   ILE A N   
28   C CA  . ILE A 23  ? 0.5057 0.5143 0.3959 0.0054  0.0168  -0.1226 8   ILE A CA  
29   C C   . ILE A 23  ? 0.5610 0.5478 0.4533 0.0144  0.0322  -0.1254 8   ILE A C   
30   O O   . ILE A 23  ? 0.5553 0.5297 0.4261 0.0224  0.0429  -0.1334 8   ILE A O   
31   C CB  . ILE A 23  ? 0.5067 0.5388 0.4035 0.0127  0.0192  -0.1060 8   ILE A CB  
32   C CG1 . ILE A 23  ? 0.6198 0.6719 0.5148 0.0053  0.0061  -0.1019 8   ILE A CG1 
33   C CG2 . ILE A 23  ? 0.4561 0.4941 0.3818 0.0167  0.0239  -0.0908 8   ILE A CG2 
34   C CD1 . ILE A 23  ? 0.5047 0.5770 0.4024 0.0123  0.0099  -0.0873 8   ILE A CD1 
46   N N   . PHE A 24  ? 0.5451 0.5274 0.4625 0.0142  0.0344  -0.1181 9   PHE A N   
47   C CA  . PHE A 24  ? 0.5253 0.4879 0.4484 0.0235  0.0499  -0.1181 9   PHE A CA  
48   C C   . PHE A 24  ? 0.5158 0.4915 0.4472 0.0374  0.0619  -0.1027 9   PHE A C   
49   O O   . PHE A 24  ? 0.4840 0.4828 0.4349 0.0377  0.0572  -0.0871 9   PHE A O   
50   C CB  . PHE A 24  ? 0.5098 0.4662 0.4579 0.0198  0.0485  -0.1130 9   PHE A CB  
51   C CG  . PHE A 24  ? 0.5263 0.4638 0.4699 0.0078  0.0418  -0.1280 9   PHE A CG  
52   C CD1 . PHE A 24  ? 0.6080 0.5191 0.5294 0.0059  0.0471  -0.1471 9   PHE A CD1 
53   C CD2 . PHE A 24  ? 0.5627 0.5083 0.5242 -0.0017 0.0303  -0.1232 9   PHE A CD2 
54   C CE1 . PHE A 24  ? 0.6844 0.5785 0.6044 -0.0073 0.0398  -0.1613 9   PHE A CE1 
55   C CE2 . PHE A 24  ? 0.6505 0.5807 0.6120 -0.0133 0.0243  -0.1352 9   PHE A CE2 
56   C CZ  . PHE A 24  ? 0.5588 0.4636 0.5008 -0.0170 0.0284  -0.1544 9   PHE A CZ  
66   N N   . ASN A 25  ? 0.5471 0.5071 0.4635 0.0487  0.0778  -0.1073 10  ASN A N   
67   C CA  . ASN A 25  ? 0.5509 0.5213 0.4791 0.0635  0.0924  -0.0913 10  ASN A CA  
68   C C   . ASN A 25  ? 0.5815 0.5464 0.5359 0.0693  0.1011  -0.0809 10  ASN A C   
69   O O   . ASN A 25  ? 0.5621 0.5104 0.5151 0.0815  0.1187  -0.0800 10  ASN A O   
70   C CB  . ASN A 25  ? 0.5929 0.5487 0.4929 0.0750  0.1076  -0.0993 10  ASN A CB  
71   C CG  . ASN A 25  ? 0.5799 0.5485 0.4938 0.0911  0.1239  -0.0806 10  ASN A CG  
72   O OD1 . ASN A 25  ? 0.5495 0.5463 0.4880 0.0911  0.1192  -0.0626 10  ASN A OD1 
73   N ND2 . ASN A 25  ? 0.6171 0.5643 0.5159 0.1049  0.1436  -0.0847 10  ASN A ND2 
80   N N   . ARG A 26  ? 0.5522 0.5315 0.5298 0.0614  0.0890  -0.0722 11  ARG A N   
81   C CA  . ARG A 26  ? 0.5330 0.5095 0.5346 0.0652  0.0938  -0.0624 11  ARG A CA  
82   C C   . ARG A 26  ? 0.5103 0.5160 0.5365 0.0608  0.0815  -0.0463 11  ARG A C   
83   O O   . ARG A 26  ? 0.4392 0.4576 0.4624 0.0504  0.0667  -0.0483 11  ARG A O   
84   C CB  . ARG A 26  ? 0.6187 0.5703 0.6168 0.0575  0.0914  -0.0756 11  ARG A CB  
85   C CG  . ARG A 26  ? 0.7530 0.6703 0.7362 0.0636  0.1075  -0.0887 11  ARG A CG  
86   C CD  . ARG A 26  ? 0.8062 0.7012 0.7940 0.0546  0.1045  -0.0985 11  ARG A CD  
87   N NE  . ARG A 26  ? 0.9821 0.8487 0.9743 0.0646  0.1241  -0.0995 11  ARG A NE  
88   C CZ  . ARG A 26  ? 0.8745 0.7471 0.8921 0.0761  0.1351  -0.0808 11  ARG A CZ  
89   N NH1 . ARG A 26  ? 0.8608 0.7673 0.9003 0.0783  0.1271  -0.0609 11  ARG A NH1 
90   N NH2 . ARG A 26  ? 0.9322 0.7760 0.9528 0.0859  0.1547  -0.0821 11  ARG A NH2 
104  N N   . ASP A 27  ? 0.4707 0.4861 0.5202 0.0690  0.0879  -0.0306 12  ASP A N   
105  C CA  . ASP A 27  ? 0.4857 0.5254 0.5566 0.0644  0.0757  -0.0172 12  ASP A CA  
106  C C   . ASP A 27  ? 0.4370 0.4658 0.5086 0.0565  0.0675  -0.0231 12  ASP A C   
107  O O   . ASP A 27  ? 0.4401 0.4507 0.5157 0.0613  0.0770  -0.0243 12  ASP A O   
108  C CB  . ASP A 27  ? 0.5731 0.6288 0.6683 0.0761  0.0848  0.0021  12  ASP A CB  
109  C CG  . ASP A 27  ? 0.5140 0.5970 0.6290 0.0713  0.0711  0.0154  12  ASP A CG  
110  O OD1 . ASP A 27  ? 0.4731 0.5594 0.5817 0.0596  0.0561  0.0092  12  ASP A OD1 
111  O OD2 . ASP A 27  ? 0.6122 0.7134 0.7485 0.0795  0.0754  0.0324  12  ASP A OD2 
116  N N   . PRO A 28  ? 0.4020 0.4405 0.4711 0.0452  0.0517  -0.0258 13  PRO A N   
117  C CA  . PRO A 28  ? 0.4393 0.4681 0.5103 0.0389  0.0454  -0.0296 13  PRO A CA  
118  C C   . PRO A 28  ? 0.3871 0.4211 0.4777 0.0459  0.0493  -0.0159 13  PRO A C   
119  O O   . PRO A 28  ? 0.3929 0.4132 0.4871 0.0447  0.0509  -0.0178 13  PRO A O   
120  C CB  . PRO A 28  ? 0.3701 0.4130 0.4365 0.0284  0.0295  -0.0308 13  PRO A CB  
121  C CG  . PRO A 28  ? 0.3628 0.4266 0.4336 0.0303  0.0272  -0.0225 13  PRO A CG  
122  C CD  . PRO A 28  ? 0.3880 0.4465 0.4550 0.0387  0.0403  -0.0234 13  PRO A CD  
130  N N   . ARG A 29  ? 0.3774 0.4331 0.4823 0.0531  0.0507  -0.0008 14  ARG A N   
131  C CA  . ARG A 29  ? 0.3952 0.4602 0.5187 0.0614  0.0545  0.0144  14  ARG A CA  
132  C C   . ARG A 29  ? 0.4031 0.4462 0.5320 0.0717  0.0725  0.0154  14  ARG A C   
133  O O   . ARG A 29  ? 0.4106 0.4572 0.5546 0.0792  0.0775  0.0278  14  ARG A O   
134  C CB  . ARG A 29  ? 0.4688 0.5639 0.6074 0.0665  0.0520  0.0303  14  ARG A CB  
135  C CG  . ARG A 29  ? 0.5854 0.7007 0.7210 0.0559  0.0352  0.0297  14  ARG A CG  
136  C CD  . ARG A 29  ? 0.5961 0.7337 0.7426 0.0552  0.0242  0.0416  14  ARG A CD  
137  N NE  . ARG A 29  ? 0.7571 0.9206 0.9115 0.0504  0.0141  0.0481  14  ARG A NE  
138  C CZ  . ARG A 29  ? 0.7163 0.9034 0.8805 0.0491  0.0034  0.0585  14  ARG A CZ  
139  N NH1 . ARG A 29  ? 0.6174 0.8076 0.7837 0.0540  0.0020  0.0652  14  ARG A NH1 
140  N NH2 . ARG A 29  ? 0.6473 0.8560 0.8196 0.0424  -0.0062 0.0624  14  ARG A NH2 
154  N N   . ASP A 30  ? 0.4379 0.4582 0.5538 0.0730  0.0831  0.0029  15  ASP A N   
155  C CA  . ASP A 30  ? 0.4800 0.4719 0.5976 0.0810  0.1006  -0.0003 15  ASP A CA  
156  C C   . ASP A 30  ? 0.5260 0.4975 0.6422 0.0730  0.0976  -0.0092 15  ASP A C   
157  O O   . ASP A 30  ? 0.5136 0.4663 0.6399 0.0796  0.1109  -0.0058 15  ASP A O   
158  C CB  . ASP A 30  ? 0.6067 0.5769 0.7056 0.0835  0.1119  -0.0143 15  ASP A CB  
159  C CG  . ASP A 30  ? 0.6666 0.6554 0.7698 0.0938  0.1188  -0.0030 15  ASP A CG  
160  O OD1 . ASP A 30  ? 0.7338 0.7480 0.8593 0.1015  0.1196  0.0172  15  ASP A OD1 
161  O OD2 . ASP A 30  ? 0.6971 0.6767 0.7819 0.0943  0.1235  -0.0135 15  ASP A OD2 
166  N N   . HIS A 31  ? 0.4406 0.4155 0.5464 0.0592  0.0815  -0.0192 16  HIS A N   
167  C CA  . HIS A 31  ? 0.4468 0.4054 0.5533 0.0504  0.0776  -0.0267 16  HIS A CA  
168  C C   . HIS A 31  ? 0.4361 0.4144 0.5540 0.0481  0.0666  -0.0145 16  HIS A C   
169  O O   . HIS A 31  ? 0.4622 0.4291 0.5882 0.0454  0.0679  -0.0139 16  HIS A O   
170  C CB  . HIS A 31  ? 0.4905 0.4375 0.5771 0.0366  0.0683  -0.0468 16  HIS A CB  
171  C CG  . HIS A 31  ? 0.5648 0.4869 0.6352 0.0372  0.0784  -0.0626 16  HIS A CG  
172  N ND1 . HIS A 31  ? 0.6793 0.5928 0.7285 0.0262  0.0704  -0.0809 16  HIS A ND1 
173  C CD2 . HIS A 31  ? 0.6760 0.5796 0.7465 0.0483  0.0964  -0.0628 16  HIS A CD2 
174  C CE1 . HIS A 31  ? 0.7399 0.6298 0.7742 0.0299  0.0822  -0.0932 16  HIS A CE1 
175  N NE2 . HIS A 31  ? 0.6785 0.5604 0.7253 0.0436  0.0990  -0.0827 16  HIS A NE2 
183  N N   . TYR A 32  ? 0.3970 0.4032 0.5153 0.0489  0.0564  -0.0052 17  TYR A N   
184  C CA  . TYR A 32  ? 0.3773 0.4003 0.4998 0.0460  0.0450  0.0032  17  TYR A CA  
185  C C   . TYR A 32  ? 0.3659 0.4147 0.4990 0.0550  0.0434  0.0206  17  TYR A C   
186  O O   . TYR A 32  ? 0.3650 0.4260 0.5006 0.0595  0.0455  0.0248  17  TYR A O   
187  C CB  . TYR A 32  ? 0.3629 0.3929 0.4709 0.0342  0.0304  -0.0062 17  TYR A CB  
188  C CG  . TYR A 32  ? 0.3732 0.3836 0.4716 0.0244  0.0291  -0.0218 17  TYR A CG  
189  C CD1 . TYR A 32  ? 0.3745 0.3759 0.4779 0.0192  0.0270  -0.0228 17  TYR A CD1 
190  C CD2 . TYR A 32  ? 0.3832 0.3860 0.4681 0.0204  0.0298  -0.0346 17  TYR A CD2 
191  C CE1 . TYR A 32  ? 0.3848 0.3716 0.4820 0.0088  0.0242  -0.0363 17  TYR A CE1 
192  C CE2 . TYR A 32  ? 0.4425 0.4304 0.5175 0.0107  0.0267  -0.0490 17  TYR A CE2 
193  C CZ  . TYR A 32  ? 0.3955 0.3761 0.4778 0.0042  0.0232  -0.0500 17  TYR A CZ  
194  O OH  . TYR A 32  ? 0.5184 0.4871 0.5932 -0.0068 0.0186  -0.0638 17  TYR A OH  
204  N N   . ASP A 33  ? 0.4006 0.4590 0.5401 0.0578  0.0397  0.0313  18  ASP A N   
205  C CA  . ASP A 33  ? 0.4100 0.4962 0.5554 0.0638  0.0333  0.0464  18  ASP A CA  
206  C C   . ASP A 33  ? 0.3574 0.4555 0.4893 0.0543  0.0169  0.0417  18  ASP A C   
207  O O   . ASP A 33  ? 0.3320 0.4216 0.4573 0.0502  0.0135  0.0382  18  ASP A O   
208  C CB  . ASP A 33  ? 0.3552 0.4448 0.5135 0.0748  0.0405  0.0622  18  ASP A CB  
209  C CG  . ASP A 33  ? 0.4601 0.5369 0.6335 0.0857  0.0589  0.0689  18  ASP A CG  
210  O OD1 . ASP A 33  ? 0.5011 0.5878 0.6809 0.0916  0.0637  0.0741  18  ASP A OD1 
211  O OD2 . ASP A 33  ? 0.4920 0.5479 0.6721 0.0883  0.0694  0.0693  18  ASP A OD2 
216  N N   . LEU A 34  ? 0.3856 0.5022 0.5146 0.0510  0.0080  0.0421  19  LEU A N   
217  C CA  . LEU A 34  ? 0.3744 0.5007 0.4908 0.0424  -0.0065 0.0379  19  LEU A CA  
218  C C   . LEU A 34  ? 0.3158 0.4562 0.4313 0.0474  -0.0123 0.0488  19  LEU A C   
219  O O   . LEU A 34  ? 0.3276 0.4872 0.4532 0.0546  -0.0125 0.0613  19  LEU A O   
220  C CB  . LEU A 34  ? 0.3332 0.4743 0.4497 0.0370  -0.0135 0.0359  19  LEU A CB  
221  C CG  . LEU A 34  ? 0.4293 0.5598 0.5439 0.0330  -0.0083 0.0263  19  LEU A CG  
222  C CD1 . LEU A 34  ? 0.3948 0.5415 0.5106 0.0268  -0.0163 0.0262  19  LEU A CD1 
223  C CD2 . LEU A 34  ? 0.4025 0.5122 0.5036 0.0266  -0.0080 0.0133  19  LEU A CD2 
235  N N   . LEU A 35  ? 0.3150 0.4476 0.4181 0.0442  -0.0168 0.0450  20  LEU A N   
236  C CA  . LEU A 35  ? 0.4012 0.5449 0.4991 0.0502  -0.0211 0.0548  20  LEU A CA  
237  C C   . LEU A 35  ? 0.3875 0.5432 0.4693 0.0436  -0.0355 0.0507  20  LEU A C   
238  O O   . LEU A 35  ? 0.4076 0.5815 0.4861 0.0480  -0.0422 0.0590  20  LEU A O   
239  C CB  . LEU A 35  ? 0.3706 0.4979 0.4653 0.0531  -0.0148 0.0557  20  LEU A CB  
240  C CG  . LEU A 35  ? 0.4646 0.5780 0.5762 0.0594  -0.0002 0.0607  20  LEU A CG  
241  C CD1 . LEU A 35  ? 0.3329 0.4342 0.4441 0.0616  0.0048  0.0641  20  LEU A CD1 
242  C CD2 . LEU A 35  ? 0.3895 0.5163 0.5158 0.0711  0.0066  0.0755  20  LEU A CD2 
254  N N   . GLN A 36  ? 0.4394 0.5853 0.5110 0.0332  -0.0405 0.0380  21  GLN A N   
255  C CA  . GLN A 36  ? 0.3786 0.5277 0.4323 0.0271  -0.0518 0.0325  21  GLN A CA  
256  C C   . GLN A 36  ? 0.3328 0.4718 0.3818 0.0163  -0.0543 0.0203  21  GLN A C   
257  O O   . GLN A 36  ? 0.3051 0.4298 0.3562 0.0147  -0.0476 0.0155  21  GLN A O   
258  C CB  . GLN A 36  ? 0.3949 0.5350 0.4339 0.0322  -0.0503 0.0346  21  GLN A CB  
259  C CG  . GLN A 36  ? 0.5734 0.7156 0.5903 0.0292  -0.0603 0.0303  21  GLN A CG  
260  C CD  . GLN A 36  ? 0.6767 0.8098 0.6790 0.0373  -0.0558 0.0347  21  GLN A CD  
261  O OE1 . GLN A 36  ? 0.6166 0.7340 0.6193 0.0377  -0.0482 0.0332  21  GLN A OE1 
262  N NE2 . GLN A 36  ? 0.8407 0.9858 0.8308 0.0442  -0.0605 0.0413  21  GLN A NE2 
271  N N   . ARG A 37  ? 0.3391 0.4862 0.3827 0.0088  -0.0641 0.0160  22  ARG A N   
272  C CA  . ARG A 37  ? 0.3624 0.4991 0.4000 -0.0008 -0.0660 0.0058  22  ARG A CA  
273  C C   . ARG A 37  ? 0.3182 0.4397 0.3356 -0.0017 -0.0670 0.0007  22  ARG A C   
274  O O   . ARG A 37  ? 0.3471 0.4709 0.3504 -0.0014 -0.0736 0.0002  22  ARG A O   
275  C CB  . ARG A 37  ? 0.3896 0.5394 0.4322 -0.0091 -0.0749 0.0039  22  ARG A CB  
276  C CG  . ARG A 37  ? 0.3429 0.4826 0.3838 -0.0183 -0.0748 -0.0045 22  ARG A CG  
277  C CD  . ARG A 37  ? 0.3423 0.4963 0.3931 -0.0270 -0.0832 -0.0046 22  ARG A CD  
278  N NE  . ARG A 37  ? 0.4793 0.6253 0.5329 -0.0352 -0.0816 -0.0102 22  ARG A NE  
279  C CZ  . ARG A 37  ? 0.4646 0.5976 0.5056 -0.0427 -0.0852 -0.0179 22  ARG A CZ  
280  N NH1 . ARG A 37  ? 0.4463 0.5706 0.4679 -0.0429 -0.0905 -0.0227 22  ARG A NH1 
281  N NH2 . ARG A 37  ? 0.4373 0.5647 0.4849 -0.0491 -0.0821 -0.0204 22  ARG A NH2 
295  N N   . LEU A 38  ? 0.3125 0.4193 0.3278 -0.0022 -0.0603 -0.0028 23  LEU A N   
296  C CA  . LEU A 38  ? 0.3193 0.4123 0.3185 -0.0012 -0.0586 -0.0051 23  LEU A CA  
297  C C   . LEU A 38  ? 0.3481 0.4326 0.3363 -0.0088 -0.0619 -0.0129 23  LEU A C   
298  O O   . LEU A 38  ? 0.3382 0.4118 0.3092 -0.0076 -0.0619 -0.0151 23  LEU A O   
299  C CB  . LEU A 38  ? 0.3111 0.3952 0.3162 0.0016  -0.0502 -0.0032 23  LEU A CB  
300  C CG  . LEU A 38  ? 0.3194 0.4065 0.3361 0.0086  -0.0450 0.0040  23  LEU A CG  
301  C CD1 . LEU A 38  ? 0.3754 0.4536 0.3990 0.0080  -0.0387 0.0038  23  LEU A CD1 
302  C CD2 . LEU A 38  ? 0.3270 0.4169 0.3356 0.0167  -0.0452 0.0112  23  LEU A CD2 
314  N N   . GLY A 39  ? 0.3792 0.4670 0.3772 -0.0157 -0.0630 -0.0163 24  GLY A N   
315  C CA  . GLY A 39  ? 0.3953 0.4742 0.3864 -0.0229 -0.0644 -0.0224 24  GLY A CA  
316  C C   . GLY A 39  ? 0.4222 0.5081 0.4289 -0.0284 -0.0635 -0.0228 24  GLY A C   
317  O O   . GLY A 39  ? 0.3178 0.4133 0.3375 -0.0258 -0.0608 -0.0192 24  GLY A O   
321  N N   . GLY A 40  ? 0.3782 0.4575 0.3827 -0.0354 -0.0644 -0.0269 25  GLY A N   
322  C CA  . GLY A 40  ? 0.3342 0.4199 0.3534 -0.0401 -0.0622 -0.0259 25  GLY A CA  
323  C C   . GLY A 40  ? 0.4283 0.5006 0.4428 -0.0456 -0.0594 -0.0292 25  GLY A C   
324  O O   . GLY A 40  ? 0.4016 0.4612 0.4032 -0.0489 -0.0622 -0.0343 25  GLY A O   
328  N N   . GLY A 41  ? 0.3670 0.4411 0.3907 -0.0458 -0.0529 -0.0260 26  GLY A N   
329  C CA  . GLY A 41  ? 0.4135 0.4758 0.4361 -0.0498 -0.0480 -0.0266 26  GLY A CA  
330  C C   . GLY A 41  ? 0.4468 0.5170 0.4811 -0.0479 -0.0408 -0.0206 26  GLY A C   
331  O O   . GLY A 41  ? 0.4323 0.5171 0.4768 -0.0458 -0.0409 -0.0176 26  GLY A O   
335  N N   . THR A 42  ? 0.3816 0.4421 0.4135 -0.0474 -0.0334 -0.0180 27  THR A N   
336  C CA  . THR A 42  ? 0.4003 0.4693 0.4406 -0.0441 -0.0258 -0.0109 27  THR A CA  
337  C C   . THR A 42  ? 0.3424 0.4213 0.3777 -0.0367 -0.0249 -0.0092 27  THR A C   
338  O O   . THR A 42  ? 0.3700 0.4598 0.4102 -0.0336 -0.0210 -0.0051 27  THR A O   
339  C CB  . THR A 42  ? 0.4289 0.4859 0.4673 -0.0435 -0.0172 -0.0066 27  THR A CB  
340  O OG1 . THR A 42  ? 0.4054 0.4530 0.4297 -0.0383 -0.0151 -0.0066 27  THR A OG1 
341  C CG2 . THR A 42  ? 0.4235 0.4669 0.4674 -0.0523 -0.0173 -0.0099 27  THR A CG2 
349  N N   . TYR A 43  ? 0.3714 0.4462 0.3967 -0.0340 -0.0283 -0.0122 28  TYR A N   
350  C CA  . TYR A 43  ? 0.4362 0.5187 0.4582 -0.0292 -0.0287 -0.0121 28  TYR A CA  
351  C C   . TYR A 43  ? 0.4021 0.4930 0.4296 -0.0287 -0.0320 -0.0150 28  TYR A C   
352  O O   . TYR A 43  ? 0.4396 0.5342 0.4646 -0.0256 -0.0319 -0.0165 28  TYR A O   
353  C CB  . TYR A 43  ? 0.3977 0.4729 0.4111 -0.0269 -0.0303 -0.0127 28  TYR A CB  
354  C CG  . TYR A 43  ? 0.4339 0.5016 0.4436 -0.0281 -0.0349 -0.0166 28  TYR A CG  
355  C CD1 . TYR A 43  ? 0.4590 0.5320 0.4712 -0.0270 -0.0392 -0.0187 28  TYR A CD1 
356  C CD2 . TYR A 43  ? 0.4521 0.5068 0.4542 -0.0298 -0.0343 -0.0178 28  TYR A CD2 
357  C CE1 . TYR A 43  ? 0.4838 0.5529 0.4916 -0.0269 -0.0434 -0.0206 28  TYR A CE1 
358  C CE2 . TYR A 43  ? 0.4522 0.5011 0.4470 -0.0305 -0.0392 -0.0219 28  TYR A CE2 
359  C CZ  . TYR A 43  ? 0.5515 0.6093 0.5493 -0.0288 -0.0442 -0.0225 28  TYR A CZ  
360  O OH  . TYR A 43  ? 0.5539 0.6086 0.5435 -0.0283 -0.0491 -0.0250 28  TYR A OH  
370  N N   . GLY A 44  ? 0.4152 0.5091 0.4508 -0.0319 -0.0347 -0.0156 29  GLY A N   
371  C CA  . GLY A 44  ? 0.4267 0.5290 0.4692 -0.0300 -0.0366 -0.0162 29  GLY A CA  
372  C C   . GLY A 44  ? 0.4363 0.5371 0.4781 -0.0311 -0.0431 -0.0179 29  GLY A C   
373  O O   . GLY A 44  ? 0.4025 0.4958 0.4378 -0.0343 -0.0468 -0.0197 29  GLY A O   
377  N N   . GLU A 45  ? 0.2845 0.3923 0.3320 -0.0274 -0.0436 -0.0168 30  GLU A N   
378  C CA  . GLU A 45  ? 0.3264 0.4361 0.3739 -0.0261 -0.0488 -0.0162 30  GLU A CA  
379  C C   . GLU A 45  ? 0.2845 0.3897 0.3286 -0.0200 -0.0457 -0.0164 30  GLU A C   
380  O O   . GLU A 45  ? 0.2971 0.4028 0.3451 -0.0168 -0.0404 -0.0168 30  GLU A O   
381  C CB  . GLU A 45  ? 0.3025 0.4271 0.3643 -0.0268 -0.0517 -0.0117 30  GLU A CB  
382  C CG  . GLU A 45  ? 0.4990 0.6278 0.5644 -0.0354 -0.0587 -0.0122 30  GLU A CG  
383  C CD  . GLU A 45  ? 0.6799 0.8268 0.7651 -0.0378 -0.0605 -0.0061 30  GLU A CD  
384  O OE1 . GLU A 45  ? 0.6172 0.7712 0.7123 -0.0320 -0.0532 -0.0013 30  GLU A OE1 
385  O OE2 . GLU A 45  ? 0.6460 0.8001 0.7369 -0.0456 -0.0691 -0.0062 30  GLU A OE2 
392  N N   . VAL A 46  ? 0.2873 0.3866 0.3236 -0.0184 -0.0483 -0.0162 31  VAL A N   
393  C CA  . VAL A 46  ? 0.2866 0.3800 0.3216 -0.0135 -0.0449 -0.0155 31  VAL A CA  
394  C C   . VAL A 46  ? 0.3249 0.4233 0.3639 -0.0084 -0.0461 -0.0105 31  VAL A C   
395  O O   . VAL A 46  ? 0.2946 0.3962 0.3277 -0.0085 -0.0514 -0.0087 31  VAL A O   
396  C CB  . VAL A 46  ? 0.3111 0.3949 0.3362 -0.0141 -0.0444 -0.0162 31  VAL A CB  
397  C CG1 . VAL A 46  ? 0.3024 0.3818 0.3301 -0.0100 -0.0412 -0.0138 31  VAL A CG1 
398  C CG2 . VAL A 46  ? 0.3482 0.4298 0.3708 -0.0178 -0.0425 -0.0188 31  VAL A CG2 
408  N N   . PHE A 47  ? 0.2892 0.3871 0.3367 -0.0036 -0.0408 -0.0083 32  PHE A N   
409  C CA  . PHE A 47  ? 0.2926 0.3962 0.3469 0.0031  -0.0396 -0.0012 32  PHE A CA  
410  C C   . PHE A 47  ? 0.2953 0.3888 0.3514 0.0074  -0.0339 0.0010  32  PHE A C   
411  O O   . PHE A 47  ? 0.3162 0.3999 0.3743 0.0051  -0.0298 -0.0038 32  PHE A O   
412  C CB  . PHE A 47  ? 0.2930 0.4050 0.3605 0.0065  -0.0355 0.0021  32  PHE A CB  
413  C CG  . PHE A 47  ? 0.2908 0.4165 0.3621 0.0027  -0.0407 0.0032  32  PHE A CG  
414  C CD1 . PHE A 47  ? 0.2878 0.4120 0.3586 -0.0024 -0.0398 -0.0020 32  PHE A CD1 
415  C CD2 . PHE A 47  ? 0.2977 0.4395 0.3742 0.0041  -0.0469 0.0102  32  PHE A CD2 
416  C CE1 . PHE A 47  ? 0.3242 0.4611 0.4020 -0.0064 -0.0438 0.0003  32  PHE A CE1 
417  C CE2 . PHE A 47  ? 0.3481 0.5039 0.4316 -0.0013 -0.0527 0.0115  32  PHE A CE2 
418  C CZ  . PHE A 47  ? 0.2884 0.4410 0.3738 -0.0066 -0.0505 0.0067  32  PHE A CZ  
428  N N   . LYS A 48  ? 0.2995 0.3965 0.3553 0.0135  -0.0341 0.0086  33  LYS A N   
429  C CA  . LYS A 48  ? 0.3035 0.3933 0.3670 0.0194  -0.0268 0.0142  33  LYS A CA  
430  C C   . LYS A 48  ? 0.3069 0.3983 0.3848 0.0244  -0.0199 0.0180  33  LYS A C   
431  O O   . LYS A 48  ? 0.3072 0.4120 0.3889 0.0278  -0.0217 0.0229  33  LYS A O   
432  C CB  . LYS A 48  ? 0.3604 0.4544 0.4173 0.0259  -0.0281 0.0229  33  LYS A CB  
433  C CG  . LYS A 48  ? 0.3141 0.4022 0.3812 0.0333  -0.0193 0.0318  33  LYS A CG  
434  C CD  . LYS A 48  ? 0.3215 0.4159 0.3790 0.0415  -0.0202 0.0416  33  LYS A CD  
435  C CE  . LYS A 48  ? 0.4273 0.5156 0.4966 0.0494  -0.0100 0.0524  33  LYS A CE  
436  N NZ  . LYS A 48  ? 0.5708 0.6674 0.6296 0.0601  -0.0095 0.0641  33  LYS A NZ  
450  N N   . ALA A 49  ? 0.3115 0.3891 0.3981 0.0246  -0.0117 0.0157  34  ALA A N   
451  C CA  . ALA A 49  ? 0.3352 0.4086 0.4342 0.0297  -0.0025 0.0176  34  ALA A CA  
452  C C   . ALA A 49  ? 0.3289 0.3863 0.4387 0.0321  0.0069  0.0196  34  ALA A C   
453  O O   . ALA A 49  ? 0.3284 0.3776 0.4371 0.0268  0.0055  0.0165  34  ALA A O   
454  C CB  . ALA A 49  ? 0.3200 0.3889 0.4159 0.0245  -0.0017 0.0070  34  ALA A CB  
460  N N   . ARG A 50  ? 0.3390 0.3922 0.4616 0.0401  0.0175  0.0260  35  ARG A N   
461  C CA  . ARG A 50  ? 0.3521 0.3877 0.4881 0.0429  0.0287  0.0286  35  ARG A CA  
462  C C   . ARG A 50  ? 0.3674 0.3844 0.5079 0.0418  0.0384  0.0193  35  ARG A C   
463  O O   . ARG A 50  ? 0.3712 0.3928 0.5135 0.0486  0.0437  0.0223  35  ARG A O   
464  C CB  . ARG A 50  ? 0.3562 0.4000 0.5044 0.0559  0.0360  0.0470  35  ARG A CB  
465  C CG  . ARG A 50  ? 0.4402 0.4640 0.6058 0.0591  0.0498  0.0513  35  ARG A CG  
466  C CD  . ARG A 50  ? 0.4571 0.4899 0.6359 0.0741  0.0592  0.0720  35  ARG A CD  
467  N NE  . ARG A 50  ? 0.6063 0.6571 0.7779 0.0781  0.0516  0.0826  35  ARG A NE  
468  C CZ  . ARG A 50  ? 0.6124 0.6877 0.7759 0.0859  0.0451  0.0929  35  ARG A CZ  
469  N NH1 . ARG A 50  ? 0.6198 0.7083 0.7850 0.0904  0.0445  0.0960  35  ARG A NH1 
470  N NH2 . ARG A 50  ? 0.6115 0.6989 0.7648 0.0894  0.0391  0.1005  35  ARG A NH2 
484  N N   . ASP A 51  ? 0.3784 0.3747 0.5207 0.0334  0.0410  0.0083  36  ASP A N   
485  C CA  . ASP A 51  ? 0.4090 0.3823 0.5535 0.0321  0.0513  -0.0022 36  ASP A CA  
486  C C   . ASP A 51  ? 0.4325 0.3983 0.5935 0.0452  0.0673  0.0104  36  ASP A C   
487  O O   . ASP A 51  ? 0.4143 0.3810 0.5897 0.0506  0.0722  0.0235  36  ASP A O   
488  C CB  . ASP A 51  ? 0.4760 0.4298 0.6216 0.0192  0.0493  -0.0153 36  ASP A CB  
489  C CG  . ASP A 51  ? 0.4976 0.4256 0.6385 0.0149  0.0571  -0.0315 36  ASP A CG  
490  O OD1 . ASP A 51  ? 0.6194 0.5348 0.7666 0.0247  0.0714  -0.0279 36  ASP A OD1 
491  O OD2 . ASP A 51  ? 0.6070 0.5274 0.7370 0.0022  0.0492  -0.0475 36  ASP A OD2 
496  N N   . LYS A 52  ? 0.4268 0.3858 0.5861 0.0517  0.0767  0.0081  37  LYS A N   
497  C CA  . LYS A 52  ? 0.4666 0.4201 0.6423 0.0662  0.0936  0.0222  37  LYS A CA  
498  C C   . LYS A 52  ? 0.4708 0.3918 0.6589 0.0649  0.1075  0.0180  37  LYS A C   
499  O O   . LYS A 52  ? 0.5106 0.4273 0.7170 0.0766  0.1215  0.0336  37  LYS A O   
500  C CB  . LYS A 52  ? 0.4491 0.4041 0.6204 0.0743  0.1015  0.0217  37  LYS A CB  
501  C CG  . LYS A 52  ? 0.4275 0.4176 0.5994 0.0813  0.0937  0.0358  37  LYS A CG  
502  C CD  . LYS A 52  ? 0.5093 0.5012 0.6782 0.0880  0.1016  0.0350  37  LYS A CD  
503  C CE  . LYS A 52  ? 0.6131 0.6422 0.7880 0.0938  0.0934  0.0508  37  LYS A CE  
504  N NZ  . LYS A 52  ? 0.5727 0.6074 0.7471 0.0996  0.1003  0.0517  37  LYS A NZ  
518  N N   . VAL A 53  ? 0.5143 0.4127 0.6937 0.0506  0.1041  -0.0023 38  VAL A N   
519  C CA  . VAL A 53  ? 0.6035 0.4684 0.7950 0.0463  0.1162  -0.0091 38  VAL A CA  
520  C C   . VAL A 53  ? 0.5017 0.3694 0.7079 0.0389  0.1104  -0.0031 38  VAL A C   
521  O O   . VAL A 53  ? 0.6097 0.4698 0.8374 0.0462  0.1226  0.0112  38  VAL A O   
522  C CB  . VAL A 53  ? 0.6666 0.5045 0.8405 0.0339  0.1153  -0.0354 38  VAL A CB  
523  C CG1 . VAL A 53  ? 0.7033 0.5065 0.8900 0.0246  0.1239  -0.0454 38  VAL A CG1 
524  C CG2 . VAL A 53  ? 0.6806 0.5104 0.8422 0.0446  0.1269  -0.0391 38  VAL A CG2 
534  N N   . SER A 54  ? 0.6006 0.4803 0.7964 0.0255  0.0929  -0.0120 39  SER A N   
535  C CA  . SER A 54  ? 0.5614 0.4426 0.7713 0.0172  0.0876  -0.0076 39  SER A CA  
536  C C   . SER A 54  ? 0.5427 0.4505 0.7603 0.0280  0.0854  0.0149  39  SER A C   
537  O O   . SER A 54  ? 0.6097 0.5165 0.8449 0.0275  0.0886  0.0255  39  SER A O   
538  C CB  . SER A 54  ? 0.5290 0.4146 0.7257 -0.0001 0.0704  -0.0241 39  SER A CB  
539  O OG  . SER A 54  ? 0.6093 0.5216 0.7878 0.0018  0.0578  -0.0224 39  SER A OG  
545  N N   . GLY A 55  ? 0.5273 0.4589 0.7317 0.0372  0.0801  0.0223  40  GLY A N   
546  C CA  . GLY A 55  ? 0.4184 0.3752 0.6233 0.0454  0.0750  0.0398  40  GLY A CA  
547  C C   . GLY A 55  ? 0.4259 0.3966 0.6187 0.0360  0.0595  0.0352  40  GLY A C   
548  O O   . GLY A 55  ? 0.4148 0.4039 0.6044 0.0426  0.0554  0.0481  40  GLY A O   
552  N N   . ASP A 56  ? 0.4380 0.4003 0.6230 0.0215  0.0513  0.0177  41  ASP A N   
553  C CA  . ASP A 56  ? 0.4139 0.3901 0.5881 0.0135  0.0376  0.0143  41  ASP A CA  
554  C C   . ASP A 56  ? 0.4079 0.4044 0.5628 0.0185  0.0291  0.0160  41  ASP A C   
555  O O   . ASP A 56  ? 0.3658 0.3643 0.5123 0.0214  0.0295  0.0114  41  ASP A O   
556  C CB  . ASP A 56  ? 0.5173 0.4833 0.6862 -0.0022 0.0303  -0.0044 41  ASP A CB  
557  C CG  . ASP A 56  ? 0.5601 0.5116 0.7485 -0.0118 0.0330  -0.0063 41  ASP A CG  
558  O OD1 . ASP A 56  ? 0.7286 0.6882 0.9297 -0.0113 0.0326  0.0061  41  ASP A OD1 
559  O OD2 . ASP A 56  ? 0.6815 0.6131 0.8724 -0.0203 0.0357  -0.0204 41  ASP A OD2 
564  N N   . LEU A 57  ? 0.3693 0.3799 0.5176 0.0191  0.0220  0.0226  42  LEU A N   
565  C CA  . LEU A 57  ? 0.3770 0.4033 0.5064 0.0200  0.0124  0.0208  42  LEU A CA  
566  C C   . LEU A 57  ? 0.3361 0.3613 0.4548 0.0084  0.0039  0.0064  42  LEU A C   
567  O O   . LEU A 57  ? 0.3372 0.3560 0.4613 -0.0003 0.0021  0.0013  42  LEU A O   
568  C CB  . LEU A 57  ? 0.3445 0.3827 0.4681 0.0259  0.0095  0.0324  42  LEU A CB  
569  C CG  . LEU A 57  ? 0.4311 0.4749 0.5608 0.0393  0.0168  0.0482  42  LEU A CG  
570  C CD1 . LEU A 57  ? 0.4142 0.4690 0.5316 0.0453  0.0132  0.0574  42  LEU A CD1 
571  C CD2 . LEU A 57  ? 0.4168 0.4684 0.5443 0.0454  0.0175  0.0496  42  LEU A CD2 
583  N N   . VAL A 58  ? 0.3274 0.3607 0.4325 0.0082  -0.0012 0.0011  43  VAL A N   
584  C CA  . VAL A 58  ? 0.3228 0.3584 0.4163 -0.0005 -0.0087 -0.0098 43  VAL A CA  
585  C C   . VAL A 58  ? 0.3115 0.3606 0.3922 0.0018  -0.0148 -0.0074 43  VAL A C   
586  O O   . VAL A 58  ? 0.3093 0.3659 0.3894 0.0088  -0.0144 0.0003  43  VAL A O   
587  C CB  . VAL A 58  ? 0.3393 0.3658 0.4301 -0.0044 -0.0063 -0.0219 43  VAL A CB  
588  C CG1 . VAL A 58  ? 0.3500 0.3592 0.4519 -0.0082 -0.0003 -0.0269 43  VAL A CG1 
589  C CG2 . VAL A 58  ? 0.3340 0.3646 0.4234 0.0035  -0.0019 -0.0193 43  VAL A CG2 
599  N N   . ALA A 59  ? 0.3066 0.3590 0.3775 -0.0045 -0.0207 -0.0141 44  ALA A N   
600  C CA  . ALA A 59  ? 0.2991 0.3611 0.3593 -0.0043 -0.0255 -0.0142 44  ALA A CA  
601  C C   . ALA A 59  ? 0.3178 0.3804 0.3747 -0.0070 -0.0250 -0.0220 44  ALA A C   
602  O O   . ALA A 59  ? 0.3265 0.3835 0.3815 -0.0117 -0.0247 -0.0295 44  ALA A O   
603  C CB  . ALA A 59  ? 0.3422 0.4070 0.3944 -0.0077 -0.0302 -0.0133 44  ALA A CB  
609  N N   . LEU A 60  ? 0.2989 0.3690 0.3554 -0.0038 -0.0250 -0.0198 45  LEU A N   
610  C CA  . LEU A 60  ? 0.3009 0.3738 0.3548 -0.0046 -0.0233 -0.0245 45  LEU A CA  
611  C C   . LEU A 60  ? 0.2955 0.3779 0.3437 -0.0077 -0.0286 -0.0233 45  LEU A C   
612  O O   . LEU A 60  ? 0.2891 0.3786 0.3393 -0.0067 -0.0321 -0.0181 45  LEU A O   
613  C CB  . LEU A 60  ? 0.3059 0.3810 0.3686 0.0021  -0.0172 -0.0206 45  LEU A CB  
614  C CG  . LEU A 60  ? 0.3644 0.4259 0.4321 0.0056  -0.0086 -0.0236 45  LEU A CG  
615  C CD1 . LEU A 60  ? 0.3237 0.3893 0.4022 0.0144  -0.0011 -0.0160 45  LEU A CD1 
616  C CD2 . LEU A 60  ? 0.4529 0.5044 0.5110 0.0015  -0.0062 -0.0352 45  LEU A CD2 
628  N N   . LYS A 61  ? 0.2933 0.3755 0.3343 -0.0116 -0.0293 -0.0281 46  LYS A N   
629  C CA  . LYS A 61  ? 0.3254 0.4147 0.3630 -0.0141 -0.0319 -0.0264 46  LYS A CA  
630  C C   . LYS A 61  ? 0.3360 0.4310 0.3762 -0.0122 -0.0275 -0.0267 46  LYS A C   
631  O O   . LYS A 61  ? 0.3366 0.4280 0.3719 -0.0107 -0.0233 -0.0315 46  LYS A O   
632  C CB  . LYS A 61  ? 0.3501 0.4380 0.3797 -0.0178 -0.0339 -0.0280 46  LYS A CB  
633  C CG  . LYS A 61  ? 0.4346 0.5275 0.4622 -0.0198 -0.0345 -0.0251 46  LYS A CG  
634  C CD  . LYS A 61  ? 0.4082 0.5015 0.4290 -0.0215 -0.0345 -0.0246 46  LYS A CD  
635  C CE  . LYS A 61  ? 0.3472 0.4356 0.3659 -0.0221 -0.0366 -0.0221 46  LYS A CE  
636  N NZ  . LYS A 61  ? 0.5449 0.6367 0.5595 -0.0228 -0.0360 -0.0192 46  LYS A NZ  
650  N N   . MET A 62  ? 0.2878 0.3916 0.3354 -0.0123 -0.0286 -0.0216 47  MET A N   
651  C CA  . MET A 62  ? 0.3045 0.4163 0.3588 -0.0097 -0.0236 -0.0187 47  MET A CA  
652  C C   . MET A 62  ? 0.2876 0.4049 0.3421 -0.0137 -0.0244 -0.0164 47  MET A C   
653  O O   . MET A 62  ? 0.2839 0.4016 0.3397 -0.0188 -0.0299 -0.0150 47  MET A O   
654  C CB  . MET A 62  ? 0.2906 0.4117 0.3590 -0.0068 -0.0237 -0.0121 47  MET A CB  
655  C CG  . MET A 62  ? 0.3555 0.4858 0.4340 -0.0022 -0.0165 -0.0069 47  MET A CG  
656  S SD  . MET A 62  ? 0.3539 0.4983 0.4437 -0.0079 -0.0192 -0.0005 47  MET A SD  
657  C CE  . MET A 62  ? 0.2841 0.4428 0.3902 -0.0113 -0.0282 0.0065  47  MET A CE  
667  N N   . VAL A 63  ? 0.2925 0.4125 0.3445 -0.0108 -0.0180 -0.0161 48  VAL A N   
668  C CA  . VAL A 63  ? 0.2918 0.4178 0.3462 -0.0129 -0.0160 -0.0117 48  VAL A CA  
669  C C   . VAL A 63  ? 0.2953 0.4316 0.3613 -0.0084 -0.0089 -0.0052 48  VAL A C   
670  O O   . VAL A 63  ? 0.3035 0.4387 0.3645 -0.0014 -0.0019 -0.0066 48  VAL A O   
671  C CB  . VAL A 63  ? 0.2962 0.4187 0.3358 -0.0119 -0.0139 -0.0146 48  VAL A CB  
672  C CG1 . VAL A 63  ? 0.2965 0.4255 0.3402 -0.0126 -0.0100 -0.0076 48  VAL A CG1 
673  C CG2 . VAL A 63  ? 0.3886 0.5032 0.4198 -0.0156 -0.0201 -0.0190 48  VAL A CG2 
683  N N   . LYS A 64  ? 0.2916 0.4369 0.3732 -0.0126 -0.0100 0.0021  49  LYS A N   
684  C CA  . LYS A 64  ? 0.2942 0.4523 0.3918 -0.0088 -0.0029 0.0111  49  LYS A CA  
685  C C   . LYS A 64  ? 0.3008 0.4608 0.3930 -0.0040 0.0066  0.0148  49  LYS A C   
686  O O   . LYS A 64  ? 0.3002 0.4572 0.3875 -0.0076 0.0058  0.0150  49  LYS A O   
687  C CB  . LYS A 64  ? 0.2911 0.4598 0.4105 -0.0169 -0.0090 0.0177  49  LYS A CB  
688  C CG  . LYS A 64  ? 0.2854 0.4529 0.4059 -0.0223 -0.0202 0.0137  49  LYS A CG  
689  C CD  . LYS A 64  ? 0.2850 0.4637 0.4248 -0.0321 -0.0282 0.0185  49  LYS A CD  
690  C CE  . LYS A 64  ? 0.3216 0.4957 0.4543 -0.0383 -0.0404 0.0121  49  LYS A CE  
691  N NZ  . LYS A 64  ? 0.3665 0.5503 0.5145 -0.0496 -0.0503 0.0141  49  LYS A NZ  
705  N N   . MET A 65  ? 0.2935 0.4530 0.3344 -0.0087 0.0546  0.0409  50  MET A N   
706  C CA  . MET A 65  ? 0.3377 0.5107 0.3635 -0.0102 0.0546  0.0452  50  MET A CA  
707  C C   . MET A 65  ? 0.3744 0.5618 0.4004 -0.0161 0.0562  0.0609  50  MET A C   
708  O O   . MET A 65  ? 0.3041 0.4981 0.3393 -0.0162 0.0613  0.0659  50  MET A O   
709  C CB  . MET A 65  ? 0.3379 0.5213 0.3528 -0.0032 0.0617  0.0339  50  MET A CB  
710  C CG  . MET A 65  ? 0.3520 0.5214 0.3636 0.0020  0.0591  0.0185  50  MET A CG  
711  S SD  . MET A 65  ? 0.3577 0.5171 0.3589 -0.0018 0.0484  0.0176  50  MET A SD  
712  C CE  . MET A 65  ? 0.3114 0.4523 0.3301 -0.0058 0.0407  0.0214  50  MET A CE  
722  N N   . GLU A 66  ? 0.3742 0.5664 0.3898 -0.0216 0.0509  0.0694  51  GLU A N   
723  C CA  . GLU A 66  ? 0.3266 0.5345 0.3389 -0.0279 0.0518  0.0846  51  GLU A CA  
724  C C   . GLU A 66  ? 0.3832 0.6131 0.3828 -0.0251 0.0603  0.0825  51  GLU A C   
725  O O   . GLU A 66  ? 0.3738 0.6040 0.3640 -0.0192 0.0632  0.0698  51  GLU A O   
726  C CB  . GLU A 66  ? 0.4439 0.6454 0.4510 -0.0356 0.0409  0.0951  51  GLU A CB  
727  C CG  . GLU A 66  ? 0.4300 0.6092 0.4483 -0.0373 0.0323  0.0959  51  GLU A CG  
728  C CD  . GLU A 66  ? 0.4674 0.6416 0.4995 -0.0391 0.0338  0.1022  51  GLU A CD  
729  O OE1 . GLU A 66  ? 0.5643 0.7491 0.5965 -0.0446 0.0343  0.1154  51  GLU A OE1 
730  O OE2 . GLU A 66  ? 0.5718 0.7316 0.6143 -0.0355 0.0340  0.0942  51  GLU A OE2 
737  N N   . PRO A 67  ? 0.4604 0.7094 0.4587 -0.0295 0.0643  0.0949  52  PRO A N   
738  C CA  . PRO A 67  ? 0.5099 0.7821 0.4960 -0.0266 0.0736  0.0928  52  PRO A CA  
739  C C   . PRO A 67  ? 0.4393 0.7134 0.4060 -0.0277 0.0705  0.0890  52  PRO A C   
740  O O   . PRO A 67  ? 0.5293 0.8146 0.4844 -0.0218 0.0781  0.0795  52  PRO A O   
741  C CB  . PRO A 67  ? 0.4511 0.7423 0.4404 -0.0338 0.0759  0.1103  52  PRO A CB  
742  C CG  . PRO A 67  ? 0.4427 0.7198 0.4492 -0.0373 0.0708  0.1175  52  PRO A CG  
743  C CD  . PRO A 67  ? 0.4272 0.6779 0.4354 -0.0371 0.0611  0.1110  52  PRO A CD  
751  N N   . ASP A 68  ? 0.4773 0.7399 0.4398 -0.0347 0.0592  0.0957  53  ASP A N   
752  C CA  . ASP A 68  ? 0.5268 0.7903 0.4712 -0.0371 0.0547  0.0936  53  ASP A CA  
753  C C   . ASP A 68  ? 0.5077 0.7512 0.4501 -0.0323 0.0493  0.0797  53  ASP A C   
754  O O   . ASP A 68  ? 0.4342 0.6762 0.3621 -0.0345 0.0443  0.0778  53  ASP A O   
755  C CB  . ASP A 68  ? 0.5871 0.8508 0.5274 -0.0482 0.0443  0.1100  53  ASP A CB  
756  C CG  . ASP A 68  ? 0.6685 0.9556 0.6040 -0.0546 0.0488  0.1242  53  ASP A CG  
757  O OD1 . ASP A 68  ? 0.6439 0.9505 0.5739 -0.0502 0.0605  0.1200  53  ASP A OD1 
758  O OD2 . ASP A 68  ? 0.8156 1.1019 0.7529 -0.0640 0.0404  0.1396  53  ASP A OD2 
763  N N   . ASP A 69  ? 0.3980 0.6266 0.3543 -0.0266 0.0497  0.0707  54  ASP A N   
764  C CA  . ASP A 69  ? 0.3777 0.5879 0.3333 -0.0233 0.0435  0.0593  54  ASP A CA  
765  C C   . ASP A 69  ? 0.4645 0.6788 0.4043 -0.0175 0.0482  0.0460  54  ASP A C   
766  O O   . ASP A 69  ? 0.4453 0.6723 0.3805 -0.0121 0.0584  0.0405  54  ASP A O   
767  C CB  . ASP A 69  ? 0.4049 0.5996 0.3786 -0.0192 0.0433  0.0530  54  ASP A CB  
768  C CG  . ASP A 69  ? 0.4287 0.6103 0.4146 -0.0249 0.0342  0.0625  54  ASP A CG  
769  O OD1 . ASP A 69  ? 0.3868 0.5651 0.3672 -0.0302 0.0255  0.0692  54  ASP A OD1 
770  O OD2 . ASP A 69  ? 0.3851 0.5593 0.3859 -0.0239 0.0355  0.0631  54  ASP A OD2 
775  N N   . ASP A 70  ? 0.4849 0.6878 0.4163 -0.0185 0.0402  0.0408  55  ASP A N   
776  C CA  . ASP A 70  ? 0.4711 0.6747 0.3846 -0.0144 0.0420  0.0291  55  ASP A CA  
777  C C   . ASP A 70  ? 0.4259 0.6094 0.3441 -0.0114 0.0352  0.0182  55  ASP A C   
778  O O   . ASP A 70  ? 0.4281 0.6017 0.3468 -0.0161 0.0249  0.0218  55  ASP A O   
779  C CB  . ASP A 70  ? 0.4360 0.6483 0.3307 -0.0211 0.0378  0.0363  55  ASP A CB  
780  C CG  . ASP A 70  ? 0.5747 0.7866 0.4485 -0.0176 0.0392  0.0245  55  ASP A CG  
781  O OD1 . ASP A 70  ? 0.5031 0.7077 0.3770 -0.0096 0.0432  0.0104  55  ASP A OD1 
782  O OD2 . ASP A 70  ? 0.5033 0.7212 0.3597 -0.0233 0.0355  0.0293  55  ASP A OD2 
787  N N   . VAL A 71  ? 0.4463 0.6241 0.3686 -0.0036 0.0404  0.0054  56  VAL A N   
788  C CA  . VAL A 71  ? 0.4013 0.5607 0.3292 -0.0013 0.0340  -0.0044 56  VAL A CA  
789  C C   . VAL A 71  ? 0.4185 0.5718 0.3293 -0.0026 0.0270  -0.0099 56  VAL A C   
790  O O   . VAL A 71  ? 0.4142 0.5533 0.3299 -0.0034 0.0189  -0.0140 56  VAL A O   
791  C CB  . VAL A 71  ? 0.4530 0.6075 0.3873 0.0068  0.0405  -0.0168 56  VAL A CB  
792  C CG1 . VAL A 71  ? 0.4509 0.6057 0.4057 0.0070  0.0442  -0.0115 56  VAL A CG1 
793  C CG2 . VAL A 71  ? 0.4959 0.6615 0.4143 0.0130  0.0496  -0.0247 56  VAL A CG2 
803  N N   . SER A 72  ? 0.4389 0.6029 0.3293 -0.0032 0.0300  -0.0100 57  SER A N   
804  C CA  . SER A 72  ? 0.4573 0.6147 0.3296 -0.0053 0.0228  -0.0147 57  SER A CA  
805  C C   . SER A 72  ? 0.4562 0.6078 0.3329 -0.0135 0.0108  -0.0044 57  SER A C   
806  O O   . SER A 72  ? 0.4632 0.6048 0.3322 -0.0155 0.0022  -0.0082 57  SER A O   
807  C CB  . SER A 72  ? 0.5104 0.6813 0.3587 -0.0049 0.0289  -0.0161 57  SER A CB  
808  O OG  . SER A 72  ? 0.4973 0.6832 0.3433 -0.0116 0.0299  -0.0018 57  SER A OG  
814  N N   . THR A 73  ? 0.4419 0.5990 0.3313 -0.0182 0.0096  0.0087  58  THR A N   
815  C CA  . THR A 73  ? 0.4380 0.5883 0.3342 -0.0248 -0.0021 0.0182  58  THR A CA  
816  C C   . THR A 73  ? 0.4503 0.5850 0.3638 -0.0228 -0.0083 0.0134  58  THR A C   
817  O O   . THR A 73  ? 0.4198 0.5482 0.3402 -0.0271 -0.0183 0.0196  58  THR A O   
818  C CB  . THR A 73  ? 0.4393 0.5977 0.3443 -0.0299 -0.0023 0.0331  58  THR A CB  
819  O OG1 . THR A 73  ? 0.4104 0.5669 0.3342 -0.0263 0.0032  0.0330  58  THR A OG1 
820  C CG2 . THR A 73  ? 0.4453 0.6213 0.3339 -0.0329 0.0039  0.0393  58  THR A CG2 
828  N N   . LEU A 74  ? 0.4471 0.5763 0.3683 -0.0165 -0.0028 0.0028  59  LEU A N   
829  C CA  . LEU A 74  ? 0.3991 0.5148 0.3361 -0.0148 -0.0078 -0.0025 59  LEU A CA  
830  C C   . LEU A 74  ? 0.4522 0.5589 0.3795 -0.0130 -0.0124 -0.0138 59  LEU A C   
831  O O   . LEU A 74  ? 0.4644 0.5608 0.4035 -0.0116 -0.0161 -0.0192 59  LEU A O   
832  C CB  . LEU A 74  ? 0.4542 0.5683 0.4062 -0.0102 0.0000  -0.0064 59  LEU A CB  
833  C CG  . LEU A 74  ? 0.5182 0.6387 0.4822 -0.0119 0.0044  0.0042  59  LEU A CG  
834  C CD1 . LEU A 74  ? 0.5311 0.6494 0.5072 -0.0072 0.0120  -0.0014 59  LEU A CD1 
835  C CD2 . LEU A 74  ? 0.4632 0.5778 0.4400 -0.0164 -0.0040 0.0135  59  LEU A CD2 
847  N N   . GLN A 75  ? 0.4697 0.5798 0.3749 -0.0134 -0.0125 -0.0171 60  GLN A N   
848  C CA  . GLN A 75  ? 0.5534 0.6540 0.4466 -0.0111 -0.0159 -0.0290 60  GLN A CA  
849  C C   . GLN A 75  ? 0.5229 0.6128 0.4239 -0.0149 -0.0280 -0.0281 60  GLN A C   
850  O O   . GLN A 75  ? 0.4389 0.5186 0.3432 -0.0128 -0.0311 -0.0370 60  GLN A O   
851  C CB  . GLN A 75  ? 0.5977 0.7038 0.4640 -0.0116 -0.0143 -0.0317 60  GLN A CB  
852  C CG  . GLN A 75  ? 0.7101 0.8061 0.5607 -0.0077 -0.0156 -0.0457 60  GLN A CG  
853  C CD  . GLN A 75  ? 0.8456 0.9466 0.6679 -0.0081 -0.0135 -0.0485 60  GLN A CD  
854  O OE1 . GLN A 75  ? 0.8659 0.9745 0.6794 -0.0142 -0.0165 -0.0390 60  GLN A OE1 
855  N NE2 . GLN A 75  ? 0.8279 0.9245 0.6351 -0.0016 -0.0086 -0.0616 60  GLN A NE2 
864  N N   . LYS A 76  ? 0.5184 0.6108 0.4231 -0.0208 -0.0354 -0.0171 61  LYS A N   
865  C CA  . LYS A 76  ? 0.5749 0.6589 0.4877 -0.0242 -0.0470 -0.0156 61  LYS A CA  
866  C C   . LYS A 76  ? 0.5358 0.6150 0.4741 -0.0223 -0.0475 -0.0156 61  LYS A C   
867  O O   . LYS A 76  ? 0.4982 0.5699 0.4439 -0.0228 -0.0541 -0.0197 61  LYS A O   
868  C CB  . LYS A 76  ? 0.6027 0.6907 0.5117 -0.0307 -0.0553 -0.0039 61  LYS A CB  
869  C CG  . LYS A 76  ? 0.7211 0.8076 0.6058 -0.0344 -0.0612 -0.0059 61  LYS A CG  
870  C CD  . LYS A 76  ? 0.7632 0.8575 0.6372 -0.0406 -0.0649 0.0056  61  LYS A CD  
871  C CE  . LYS A 76  ? 0.7546 0.8475 0.6013 -0.0444 -0.0692 0.0026  61  LYS A CE  
872  N NZ  . LYS A 76  ? 0.8486 0.9514 0.6803 -0.0501 -0.0693 0.0124  61  LYS A NZ  
886  N N   . GLU A 77  ? 0.4831 0.5667 0.4348 -0.0206 -0.0408 -0.0110 62  GLU A N   
887  C CA  . GLU A 77  ? 0.4883 0.5668 0.4625 -0.0188 -0.0404 -0.0119 62  GLU A CA  
888  C C   . GLU A 77  ? 0.4567 0.5290 0.4320 -0.0147 -0.0362 -0.0239 62  GLU A C   
889  O O   . GLU A 77  ? 0.4321 0.4981 0.4210 -0.0146 -0.0396 -0.0272 62  GLU A O   
890  C CB  . GLU A 77  ? 0.5126 0.5957 0.4986 -0.0184 -0.0347 -0.0040 62  GLU A CB  
891  C CG  . GLU A 77  ? 0.5651 0.6519 0.5535 -0.0226 -0.0407 0.0086  62  GLU A CG  
892  C CD  . GLU A 77  ? 0.5997 0.6807 0.6045 -0.0238 -0.0495 0.0118  62  GLU A CD  
893  O OE1 . GLU A 77  ? 0.4850 0.5608 0.5049 -0.0212 -0.0481 0.0068  62  GLU A OE1 
894  O OE2 . GLU A 77  ? 0.5390 0.6211 0.5420 -0.0273 -0.0579 0.0195  62  GLU A OE2 
901  N N   . ILE A 78  ? 0.4867 0.5611 0.4478 -0.0114 -0.0291 -0.0305 63  ILE A N   
902  C CA  . ILE A 78  ? 0.3912 0.4586 0.3522 -0.0073 -0.0258 -0.0420 63  ILE A CA  
903  C C   . ILE A 78  ? 0.4648 0.5232 0.4180 -0.0088 -0.0346 -0.0490 63  ILE A C   
904  O O   . ILE A 78  ? 0.4212 0.4716 0.3824 -0.0079 -0.0367 -0.0556 63  ILE A O   
905  C CB  . ILE A 78  ? 0.4800 0.5524 0.4278 -0.0026 -0.0160 -0.0472 63  ILE A CB  
906  C CG1 . ILE A 78  ? 0.4894 0.5703 0.4483 -0.0014 -0.0075 -0.0403 63  ILE A CG1 
907  C CG2 . ILE A 78  ? 0.5904 0.6538 0.5346 0.0019  -0.0146 -0.0602 63  ILE A CG2 
908  C CD1 . ILE A 78  ? 0.5589 0.6343 0.5367 0.0003  -0.0046 -0.0425 63  ILE A CD1 
920  N N   . LEU A 79  ? 0.4937 0.5530 0.4308 -0.0117 -0.0405 -0.0471 64  LEU A N   
921  C CA  . LEU A 79  ? 0.5267 0.5770 0.4558 -0.0140 -0.0502 -0.0524 64  LEU A CA  
922  C C   . LEU A 79  ? 0.5724 0.6195 0.5220 -0.0174 -0.0581 -0.0485 64  LEU A C   
923  O O   . LEU A 79  ? 0.5194 0.5585 0.4710 -0.0183 -0.0637 -0.0546 64  LEU A O   
924  C CB  . LEU A 79  ? 0.5853 0.6375 0.4937 -0.0175 -0.0556 -0.0493 64  LEU A CB  
925  C CG  . LEU A 79  ? 0.7632 0.8052 0.6592 -0.0205 -0.0661 -0.0547 64  LEU A CG  
926  C CD1 . LEU A 79  ? 0.7193 0.7520 0.6019 -0.0158 -0.0631 -0.0681 64  LEU A CD1 
927  C CD2 . LEU A 79  ? 0.7006 0.7447 0.5774 -0.0252 -0.0721 -0.0496 64  LEU A CD2 
939  N N   . ILE A 80  ? 0.3973 0.4508 0.3621 -0.0194 -0.0588 -0.0383 65  ILE A N   
940  C CA  . ILE A 80  ? 0.4628 0.5150 0.4487 -0.0215 -0.0650 -0.0347 65  ILE A CA  
941  C C   . ILE A 80  ? 0.4413 0.4897 0.4419 -0.0189 -0.0601 -0.0406 65  ILE A C   
942  O O   . ILE A 80  ? 0.4967 0.5412 0.5072 -0.0206 -0.0655 -0.0434 65  ILE A O   
943  C CB  . ILE A 80  ? 0.4150 0.4739 0.4132 -0.0229 -0.0662 -0.0231 65  ILE A CB  
944  C CG1 . ILE A 80  ? 0.3912 0.4524 0.3778 -0.0271 -0.0747 -0.0166 65  ILE A CG1 
945  C CG2 . ILE A 80  ? 0.4709 0.5293 0.4938 -0.0229 -0.0685 -0.0207 65  ILE A CG2 
946  C CD1 . ILE A 80  ? 0.4881 0.5549 0.4839 -0.0286 -0.0766 -0.0050 65  ILE A CD1 
958  N N   . LEU A 81  ? 0.3728 0.4228 0.3756 -0.0154 -0.0502 -0.0420 66  LEU A N   
959  C CA  . LEU A 81  ? 0.3447 0.3905 0.3601 -0.0135 -0.0456 -0.0475 66  LEU A CA  
960  C C   . LEU A 81  ? 0.3743 0.4117 0.3811 -0.0132 -0.0487 -0.0580 66  LEU A C   
961  O O   . LEU A 81  ? 0.3785 0.4113 0.3971 -0.0141 -0.0499 -0.0617 66  LEU A O   
962  C CB  . LEU A 81  ? 0.3361 0.3850 0.3527 -0.0101 -0.0351 -0.0469 66  LEU A CB  
963  C CG  . LEU A 81  ? 0.3907 0.4447 0.4211 -0.0108 -0.0320 -0.0372 66  LEU A CG  
964  C CD1 . LEU A 81  ? 0.3785 0.4363 0.4066 -0.0082 -0.0225 -0.0355 66  LEU A CD1 
965  C CD2 . LEU A 81  ? 0.4361 0.4868 0.4868 -0.0119 -0.0335 -0.0367 66  LEU A CD2 
977  N N   . LYS A 82  ? 0.3770 0.4118 0.3625 -0.0122 -0.0501 -0.0629 67  LYS A N   
978  C CA  . LYS A 82  ? 0.3840 0.4087 0.3589 -0.0116 -0.0540 -0.0732 67  LYS A CA  
979  C C   . LYS A 82  ? 0.4916 0.5118 0.4688 -0.0167 -0.0658 -0.0728 67  LYS A C   
980  O O   . LYS A 82  ? 0.5679 0.5800 0.5472 -0.0180 -0.0701 -0.0790 67  LYS A O   
981  C CB  . LYS A 82  ? 0.5467 0.5694 0.4967 -0.0083 -0.0517 -0.0791 67  LYS A CB  
982  C CG  . LYS A 82  ? 0.6061 0.6319 0.5524 -0.0022 -0.0402 -0.0828 67  LYS A CG  
983  C CD  . LYS A 82  ? 0.6467 0.6690 0.5678 0.0017  -0.0388 -0.0912 67  LYS A CD  
984  C CE  . LYS A 82  ? 0.8165 0.8420 0.7353 0.0087  -0.0275 -0.0963 67  LYS A CE  
985  N NZ  . LYS A 82  ? 0.9473 0.9679 0.8419 0.0137  -0.0263 -0.1065 67  LYS A NZ  
999  N N   . THR A 83  ? 0.4445 0.4697 0.4211 -0.0201 -0.0717 -0.0651 68  THR A N   
1000 C CA  . THR A 83  ? 0.5079 0.5294 0.4837 -0.0252 -0.0836 -0.0642 68  THR A CA  
1001 C C   . THR A 83  ? 0.5262 0.5528 0.5271 -0.0282 -0.0875 -0.0581 68  THR A C   
1002 O O   . THR A 83  ? 0.6178 0.6413 0.6227 -0.0323 -0.0963 -0.0590 68  THR A O   
1003 C CB  . THR A 83  ? 0.5545 0.5781 0.5144 -0.0277 -0.0892 -0.0593 68  THR A CB  
1004 O OG1 . THR A 83  ? 0.6911 0.7247 0.6600 -0.0275 -0.0858 -0.0496 68  THR A OG1 
1005 C CG2 . THR A 83  ? 0.6573 0.6757 0.5903 -0.0249 -0.0859 -0.0664 68  THR A CG2 
1013 N N   . CYS A 84  ? 0.4766 0.5108 0.4940 -0.0265 -0.0813 -0.0519 69  CYS A N   
1014 C CA  . CYS A 84  ? 0.3993 0.4388 0.4407 -0.0282 -0.0835 -0.0469 69  CYS A CA  
1015 C C   . CYS A 84  ? 0.4127 0.4491 0.4652 -0.0275 -0.0787 -0.0526 69  CYS A C   
1016 O O   . CYS A 84  ? 0.4603 0.4956 0.5137 -0.0242 -0.0696 -0.0548 69  CYS A O   
1017 C CB  . CYS A 84  ? 0.4673 0.5145 0.5201 -0.0264 -0.0798 -0.0380 69  CYS A CB  
1018 S SG  . CYS A 84  ? 0.5838 0.6362 0.6352 -0.0293 -0.0899 -0.0286 69  CYS A SG  
1024 N N   . ARG A 85  ? 0.3344 0.3698 0.3957 -0.0312 -0.0852 -0.0543 70  ARG A N   
1025 C CA  . ARG A 85  ? 0.3654 0.3977 0.4366 -0.0319 -0.0821 -0.0594 70  ARG A CA  
1026 C C   . ARG A 85  ? 0.3142 0.3529 0.4046 -0.0360 -0.0876 -0.0558 70  ARG A C   
1027 O O   . ARG A 85  ? 0.3233 0.3639 0.4127 -0.0396 -0.0971 -0.0533 70  ARG A O   
1028 C CB  . ARG A 85  ? 0.3404 0.3614 0.3948 -0.0326 -0.0846 -0.0686 70  ARG A CB  
1029 C CG  . ARG A 85  ? 0.4341 0.4502 0.4941 -0.0317 -0.0785 -0.0743 70  ARG A CG  
1030 C CD  . ARG A 85  ? 0.4267 0.4310 0.4675 -0.0300 -0.0794 -0.0835 70  ARG A CD  
1031 N NE  . ARG A 85  ? 0.4963 0.4958 0.5419 -0.0282 -0.0728 -0.0883 70  ARG A NE  
1032 C CZ  . ARG A 85  ? 0.5778 0.5787 0.6230 -0.0233 -0.0629 -0.0886 70  ARG A CZ  
1033 N NH1 . ARG A 85  ? 0.5083 0.5156 0.5483 -0.0197 -0.0580 -0.0842 70  ARG A NH1 
1034 N NH2 . ARG A 85  ? 0.5781 0.5741 0.6285 -0.0225 -0.0584 -0.0928 70  ARG A NH2 
1048 N N   . HIS A 86  ? 0.3101 0.3526 0.4178 -0.0356 -0.0816 -0.0552 71  HIS A N   
1049 C CA  . HIS A 86  ? 0.2875 0.3378 0.4149 -0.0390 -0.0849 -0.0522 71  HIS A CA  
1050 C C   . HIS A 86  ? 0.2718 0.3224 0.4115 -0.0387 -0.0767 -0.0545 71  HIS A C   
1051 O O   . HIS A 86  ? 0.2654 0.3131 0.4037 -0.0350 -0.0682 -0.0550 71  HIS A O   
1052 C CB  . HIS A 86  ? 0.3131 0.3738 0.4529 -0.0375 -0.0872 -0.0439 71  HIS A CB  
1053 C CG  . HIS A 86  ? 0.2858 0.3566 0.4464 -0.0403 -0.0907 -0.0408 71  HIS A CG  
1054 N ND1 . HIS A 86  ? 0.2609 0.3381 0.4397 -0.0384 -0.0837 -0.0395 71  HIS A ND1 
1055 C CD2 . HIS A 86  ? 0.3058 0.3822 0.4718 -0.0448 -0.1003 -0.0385 71  HIS A CD2 
1056 C CE1 . HIS A 86  ? 0.2573 0.3447 0.4523 -0.0412 -0.0881 -0.0368 71  HIS A CE1 
1057 N NE2 . HIS A 86  ? 0.2694 0.3570 0.4577 -0.0454 -0.0984 -0.0358 71  HIS A NE2 
1065 N N   . ALA A 87  ? 0.2664 0.3206 0.4179 -0.0434 -0.0797 -0.0554 72  ALA A N   
1066 C CA  . ALA A 87  ? 0.2863 0.3401 0.4480 -0.0446 -0.0727 -0.0579 72  ALA A CA  
1067 C C   . ALA A 87  ? 0.2408 0.2994 0.4138 -0.0399 -0.0636 -0.0541 72  ALA A C   
1068 O O   . ALA A 87  ? 0.2332 0.2867 0.4064 -0.0388 -0.0560 -0.0563 72  ALA A O   
1069 C CB  . ALA A 87  ? 0.2900 0.3504 0.4645 -0.0509 -0.0777 -0.0577 72  ALA A CB  
1075 N N   . ASN A 88  ? 0.2400 0.3070 0.4218 -0.0371 -0.0650 -0.0481 73  ASN A N   
1076 C CA  . ASN A 88  ? 0.2409 0.3120 0.4347 -0.0327 -0.0579 -0.0443 73  ASN A CA  
1077 C C   . ASN A 88  ? 0.2537 0.3198 0.4378 -0.0278 -0.0542 -0.0416 73  ASN A C   
1078 O O   . ASN A 88  ? 0.2311 0.2998 0.4237 -0.0240 -0.0507 -0.0372 73  ASN A O   
1079 C CB  . ASN A 88  ? 0.2892 0.3726 0.5003 -0.0319 -0.0616 -0.0392 73  ASN A CB  
1080 C CG  . ASN A 88  ? 0.2215 0.3127 0.4463 -0.0365 -0.0625 -0.0410 73  ASN A CG  
1081 O OD1 . ASN A 88  ? 0.2259 0.3249 0.4561 -0.0398 -0.0701 -0.0392 73  ASN A OD1 
1082 N ND2 . ASN A 88  ? 0.2495 0.3391 0.4798 -0.0373 -0.0548 -0.0439 73  ASN A ND2 
1089 N N   . ILE A 89  ? 0.2610 0.3199 0.4272 -0.0277 -0.0552 -0.0440 74  ILE A N   
1090 C CA  . ILE A 89  ? 0.2438 0.2986 0.4001 -0.0239 -0.0504 -0.0417 74  ILE A CA  
1091 C C   . ILE A 89  ? 0.2538 0.3003 0.3988 -0.0242 -0.0452 -0.0474 74  ILE A C   
1092 O O   . ILE A 89  ? 0.2607 0.3032 0.3978 -0.0267 -0.0485 -0.0531 74  ILE A O   
1093 C CB  . ILE A 89  ? 0.2568 0.3132 0.4018 -0.0228 -0.0563 -0.0379 74  ILE A CB  
1094 C CG1 . ILE A 89  ? 0.2699 0.3218 0.3982 -0.0252 -0.0613 -0.0431 74  ILE A CG1 
1095 C CG2 . ILE A 89  ? 0.2573 0.3218 0.4150 -0.0227 -0.0628 -0.0321 74  ILE A CG2 
1096 C CD1 . ILE A 89  ? 0.3095 0.3625 0.4249 -0.0249 -0.0669 -0.0395 74  ILE A CD1 
1108 N N   . VAL A 90  ? 0.2378 0.2815 0.3825 -0.0217 -0.0377 -0.0456 75  VAL A N   
1109 C CA  . VAL A 90  ? 0.2365 0.2733 0.3734 -0.0216 -0.0323 -0.0503 75  VAL A CA  
1110 C C   . VAL A 90  ? 0.2738 0.3076 0.3938 -0.0212 -0.0355 -0.0548 75  VAL A C   
1111 O O   . VAL A 90  ? 0.2597 0.2961 0.3696 -0.0193 -0.0377 -0.0521 75  VAL A O   
1112 C CB  . VAL A 90  ? 0.2685 0.3040 0.4057 -0.0189 -0.0250 -0.0458 75  VAL A CB  
1113 C CG1 . VAL A 90  ? 0.4021 0.4322 0.5301 -0.0183 -0.0200 -0.0496 75  VAL A CG1 
1114 C CG2 . VAL A 90  ? 0.4192 0.4544 0.5714 -0.0196 -0.0215 -0.0433 75  VAL A CG2 
1124 N N   . ALA A 91  ? 0.2802 0.3079 0.3961 -0.0229 -0.0360 -0.0618 76  ALA A N   
1125 C CA  . ALA A 91  ? 0.2663 0.2895 0.3658 -0.0221 -0.0398 -0.0674 76  ALA A CA  
1126 C C   . ALA A 91  ? 0.2712 0.2930 0.3589 -0.0176 -0.0335 -0.0681 76  ALA A C   
1127 O O   . ALA A 91  ? 0.2785 0.2986 0.3705 -0.0163 -0.0266 -0.0680 76  ALA A O   
1128 C CB  . ALA A 91  ? 0.3298 0.3457 0.4292 -0.0254 -0.0434 -0.0747 76  ALA A CB  
1134 N N   . TYR A 92  ? 0.3864 0.4096 0.4591 -0.0155 -0.0358 -0.0685 77  TYR A N   
1135 C CA  . TYR A 92  ? 0.3492 0.3730 0.4090 -0.0112 -0.0299 -0.0696 77  TYR A CA  
1136 C C   . TYR A 92  ? 0.3044 0.3202 0.3522 -0.0092 -0.0308 -0.0795 77  TYR A C   
1137 O O   . TYR A 92  ? 0.3879 0.3988 0.4271 -0.0107 -0.0383 -0.0843 77  TYR A O   
1138 C CB  . TYR A 92  ? 0.3834 0.4133 0.4321 -0.0103 -0.0319 -0.0647 77  TYR A CB  
1139 C CG  . TYR A 92  ? 0.3163 0.3484 0.3488 -0.0062 -0.0267 -0.0665 77  TYR A CG  
1140 C CD1 . TYR A 92  ? 0.4177 0.4558 0.4527 -0.0041 -0.0186 -0.0613 77  TYR A CD1 
1141 C CD2 . TYR A 92  ? 0.4662 0.4948 0.4805 -0.0046 -0.0299 -0.0732 77  TYR A CD2 
1142 C CE1 . TYR A 92  ? 0.3644 0.4069 0.3854 -0.0004 -0.0132 -0.0624 77  TYR A CE1 
1143 C CE2 . TYR A 92  ? 0.4142 0.4461 0.4132 -0.0003 -0.0241 -0.0753 77  TYR A CE2 
1144 C CZ  . TYR A 92  ? 0.3944 0.4344 0.3976 0.0017  -0.0155 -0.0697 77  TYR A CZ  
1145 O OH  . TYR A 92  ? 0.4053 0.4510 0.3946 0.0058  -0.0092 -0.0712 77  TYR A OH  
1155 N N   . HIS A 93  ? 0.3396 0.3538 0.3869 -0.0058 -0.0236 -0.0823 78  HIS A N   
1156 C CA  . HIS A 93  ? 0.3314 0.3373 0.3687 -0.0029 -0.0242 -0.0920 78  HIS A CA  
1157 C C   . HIS A 93  ? 0.4371 0.4460 0.4589 0.0033  -0.0188 -0.0949 78  HIS A C   
1158 O O   . HIS A 93  ? 0.5795 0.5811 0.5893 0.0066  -0.0207 -0.1039 78  HIS A O   
1159 C CB  . HIS A 93  ? 0.4097 0.4100 0.4592 -0.0037 -0.0213 -0.0946 78  HIS A CB  
1160 C CG  . HIS A 93  ? 0.3092 0.3058 0.3720 -0.0100 -0.0266 -0.0935 78  HIS A CG  
1161 N ND1 . HIS A 93  ? 0.4306 0.4223 0.4903 -0.0137 -0.0358 -0.0971 78  HIS A ND1 
1162 C CD2 . HIS A 93  ? 0.3554 0.3532 0.4342 -0.0135 -0.0239 -0.0891 78  HIS A CD2 
1163 C CE1 . HIS A 93  ? 0.3726 0.3640 0.4466 -0.0192 -0.0382 -0.0948 78  HIS A CE1 
1164 N NE2 . HIS A 93  ? 0.3779 0.3727 0.4632 -0.0190 -0.0308 -0.0903 78  HIS A NE2 
1172 N N   . GLY A 94  ? 0.4327 0.4519 0.4541 0.0050  -0.0125 -0.0878 79  GLY A N   
1173 C CA  . GLY A 94  ? 0.3522 0.3770 0.3589 0.0104  -0.0069 -0.0898 79  GLY A CA  
1174 C C   . GLY A 94  ? 0.3424 0.3783 0.3555 0.0115  0.0018  -0.0812 79  GLY A C   
1175 O O   . GLY A 94  ? 0.3267 0.3636 0.3554 0.0086  0.0036  -0.0748 79  GLY A O   
1179 N N   . SER A 95  ? 0.3389 0.3832 0.3390 0.0155  0.0070  -0.0809 80  SER A N   
1180 C CA  . SER A 95  ? 0.3439 0.4002 0.3476 0.0162  0.0150  -0.0723 80  SER A CA  
1181 C C   . SER A 95  ? 0.3681 0.4297 0.3653 0.0229  0.0231  -0.0775 80  SER A C   
1182 O O   . SER A 95  ? 0.3577 0.4161 0.3408 0.0276  0.0227  -0.0871 80  SER A O   
1183 C CB  . SER A 95  ? 0.3398 0.4052 0.3349 0.0135  0.0136  -0.0640 80  SER A CB  
1184 O OG  . SER A 95  ? 0.5387 0.5995 0.5398 0.0082  0.0056  -0.0598 80  SER A OG  
1190 N N   . TYR A 96  ? 0.3301 0.3997 0.3375 0.0235  0.0303  -0.0709 81  TYR A N   
1191 C CA  . TYR A 96  ? 0.4010 0.4784 0.4058 0.0299  0.0388  -0.0741 81  TYR A CA  
1192 C C   . TYR A 96  ? 0.3638 0.4578 0.3695 0.0288  0.0455  -0.0627 81  TYR A C   
1193 O O   . TYR A 96  ? 0.3202 0.4159 0.3361 0.0230  0.0443  -0.0520 81  TYR A O   
1194 C CB  . TYR A 96  ? 0.3564 0.4269 0.3761 0.0316  0.0406  -0.0776 81  TYR A CB  
1195 C CG  . TYR A 96  ? 0.3637 0.4179 0.3837 0.0322  0.0339  -0.0884 81  TYR A CG  
1196 C CD1 . TYR A 96  ? 0.3901 0.4342 0.4165 0.0259  0.0260  -0.0873 81  TYR A CD1 
1197 C CD2 . TYR A 96  ? 0.4159 0.4651 0.4299 0.0392  0.0351  -0.0996 81  TYR A CD2 
1198 C CE1 . TYR A 96  ? 0.4243 0.4545 0.4510 0.0255  0.0194  -0.0962 81  TYR A CE1 
1199 C CE2 . TYR A 96  ? 0.4325 0.4658 0.4462 0.0390  0.0278  -0.1089 81  TYR A CE2 
1200 C CZ  . TYR A 96  ? 0.4898 0.5140 0.5098 0.0316  0.0198  -0.1068 81  TYR A CZ  
1201 O OH  . TYR A 96  ? 0.5659 0.5752 0.5857 0.0304  0.0120  -0.1151 81  TYR A OH  
1211 N N   . LEU A 97  ? 0.3468 0.4527 0.3415 0.0342  0.0525  -0.0648 82  LEU A N   
1212 C CA  . LEU A 97  ? 0.3451 0.4686 0.3414 0.0334  0.0599  -0.0542 82  LEU A CA  
1213 C C   . LEU A 97  ? 0.3463 0.4776 0.3475 0.0405  0.0687  -0.0582 82  LEU A C   
1214 O O   . LEU A 97  ? 0.3720 0.5029 0.3630 0.0480  0.0714  -0.0696 82  LEU A O   
1215 C CB  . LEU A 97  ? 0.3615 0.4965 0.3398 0.0324  0.0608  -0.0508 82  LEU A CB  
1216 C CG  . LEU A 97  ? 0.3725 0.5274 0.3516 0.0307  0.0681  -0.0389 82  LEU A CG  
1217 C CD1 . LEU A 97  ? 0.3435 0.4978 0.3374 0.0229  0.0649  -0.0250 82  LEU A CD1 
1218 C CD2 . LEU A 97  ? 0.3804 0.5473 0.3394 0.0299  0.0695  -0.0370 82  LEU A CD2 
1230 N N   . TRP A 98  ? 0.3320 0.4699 0.3485 0.0384  0.0726  -0.0490 83  TRP A N   
1231 C CA  . TRP A 98  ? 0.3321 0.4786 0.3557 0.0448  0.0807  -0.0514 83  TRP A CA  
1232 C C   . TRP A 98  ? 0.3197 0.4789 0.3561 0.0403  0.0850  -0.0367 83  TRP A C   
1233 O O   . TRP A 98  ? 0.3193 0.4703 0.3674 0.0334  0.0804  -0.0289 83  TRP A O   
1234 C CB  . TRP A 98  ? 0.4003 0.5305 0.4335 0.0483  0.0777  -0.0615 83  TRP A CB  
1235 C CG  . TRP A 98  ? 0.4041 0.5415 0.4426 0.0567  0.0850  -0.0670 83  TRP A CG  
1236 C CD1 . TRP A 98  ? 0.4961 0.6359 0.5522 0.0567  0.0881  -0.0622 83  TRP A CD1 
1237 C CD2 . TRP A 98  ? 0.5180 0.6610 0.5442 0.0668  0.0900  -0.0784 83  TRP A CD2 
1238 N NE1 . TRP A 98  ? 0.5314 0.6789 0.5884 0.0664  0.0946  -0.0695 83  TRP A NE1 
1239 C CE2 . TRP A 98  ? 0.5031 0.6525 0.5417 0.0731  0.0962  -0.0800 83  TRP A CE2 
1240 C CE3 . TRP A 98  ? 0.5147 0.6573 0.5202 0.0712  0.0897  -0.0876 83  TRP A CE3 
1241 C CZ2 . TRP A 98  ? 0.5141 0.6700 0.5458 0.0846  0.1024  -0.0909 83  TRP A CZ2 
1242 C CZ3 . TRP A 98  ? 0.5027 0.6507 0.4996 0.0821  0.0959  -0.0986 83  TRP A CZ3 
1243 C CH2 . TRP A 98  ? 0.4442 0.5991 0.4546 0.0891  0.1024  -0.1004 83  TRP A CH2 
1254 N N   . LEU A 99  ? 0.2962 0.5318 0.4990 0.0714  0.0880  -0.0234 84  LEU A N   
1255 C CA  . LEU A 99  ? 0.3112 0.5629 0.5367 0.0671  0.0880  -0.0104 84  LEU A CA  
1256 C C   . LEU A 99  ? 0.2696 0.5201 0.4912 0.0558  0.0816  -0.0025 84  LEU A C   
1257 O O   . LEU A 99  ? 0.3067 0.5569 0.5426 0.0489  0.0729  0.0038  84  LEU A O   
1258 C CB  . LEU A 99  ? 0.2988 0.5495 0.5457 0.0682  0.0809  -0.0083 84  LEU A CB  
1259 C CG  . LEU A 99  ? 0.4682 0.7214 0.7247 0.0798  0.0872  -0.0139 84  LEU A CG  
1260 C CD1 . LEU A 99  ? 0.3330 0.5879 0.6122 0.0802  0.0794  -0.0089 84  LEU A CD1 
1261 C CD2 . LEU A 99  ? 0.2966 0.5694 0.5594 0.0872  0.1020  -0.0120 84  LEU A CD2 
1273 N N   . GLN A 100 ? 0.2751 0.5246 0.4770 0.0542  0.0858  -0.0036 85  GLN A N   
1274 C CA  . GLN A 100 ? 0.2869 0.5370 0.4855 0.0448  0.0824  0.0048  85  GLN A CA  
1275 C C   . GLN A 100 ? 0.2761 0.5081 0.4693 0.0369  0.0689  0.0029  85  GLN A C   
1276 O O   . GLN A 100 ? 0.2510 0.4829 0.4490 0.0285  0.0641  0.0104  85  GLN A O   
1277 C CB  . GLN A 100 ? 0.2644 0.5327 0.4879 0.0409  0.0859  0.0181  85  GLN A CB  
1278 C CG  . GLN A 100 ? 0.2745 0.5630 0.5062 0.0489  0.1004  0.0221  85  GLN A CG  
1279 C CD  . GLN A 100 ? 0.3567 0.6636 0.6152 0.0440  0.1039  0.0366  85  GLN A CD  
1280 O OE1 . GLN A 100 ? 0.4129 0.7171 0.6790 0.0340  0.0970  0.0438  85  GLN A OE1 
1281 N NE2 . GLN A 100 ? 0.3941 0.7197 0.6686 0.0509  0.1148  0.0409  85  GLN A NE2 
1290 N N   . LYS A 101 ? 0.2585 0.4752 0.4426 0.0397  0.0633  -0.0068 86  LYS A N   
1291 C CA  . LYS A 101 ? 0.2510 0.4502 0.4263 0.0337  0.0520  -0.0093 86  LYS A CA  
1292 C C   . LYS A 101 ? 0.2861 0.4725 0.4386 0.0362  0.0523  -0.0191 86  LYS A C   
1293 O O   . LYS A 101 ? 0.2665 0.4499 0.4153 0.0436  0.0561  -0.0277 86  LYS A O   
1294 C CB  . LYS A 101 ? 0.3004 0.4939 0.4889 0.0343  0.0440  -0.0099 86  LYS A CB  
1295 C CG  . LYS A 101 ? 0.3031 0.5082 0.5138 0.0301  0.0403  -0.0008 86  LYS A CG  
1296 C CD  . LYS A 101 ? 0.3377 0.5487 0.5667 0.0359  0.0390  -0.0006 86  LYS A CD  
1297 C CE  . LYS A 101 ? 0.4515 0.6485 0.6778 0.0357  0.0283  -0.0035 86  LYS A CE  
1298 N NZ  . LYS A 101 ? 0.5875 0.7921 0.8330 0.0412  0.0263  -0.0013 86  LYS A NZ  
1312 N N   . LEU A 102 ? 0.2553 0.4343 0.3939 0.0302  0.0483  -0.0182 87  LEU A N   
1313 C CA  . LEU A 102 ? 0.2680 0.4350 0.3865 0.0311  0.0467  -0.0269 87  LEU A CA  
1314 C C   . LEU A 102 ? 0.2533 0.4034 0.3705 0.0274  0.0367  -0.0293 87  LEU A C   
1315 O O   . LEU A 102 ? 0.2718 0.4188 0.3922 0.0210  0.0306  -0.0231 87  LEU A O   
1316 C CB  . LEU A 102 ? 0.2637 0.4349 0.3681 0.0276  0.0489  -0.0234 87  LEU A CB  
1317 C CG  . LEU A 102 ? 0.3124 0.4725 0.3969 0.0279  0.0459  -0.0322 87  LEU A CG  
1318 C CD1 . LEU A 102 ? 0.2838 0.4466 0.3596 0.0361  0.0519  -0.0430 87  LEU A CD1 
1319 C CD2 . LEU A 102 ? 0.3360 0.4989 0.4090 0.0230  0.0453  -0.0264 87  LEU A CD2 
1331 N N   . TRP A 103 ? 0.2581 0.3975 0.3714 0.0317  0.0353  -0.0383 88  TRP A N   
1332 C CA  . TRP A 103 ? 0.2528 0.3767 0.3657 0.0293  0.0272  -0.0399 88  TRP A CA  
1333 C C   . TRP A 103 ? 0.2575 0.3701 0.3546 0.0280  0.0251  -0.0472 88  TRP A C   
1334 O O   . TRP A 103 ? 0.3178 0.4307 0.4076 0.0323  0.0293  -0.0557 88  TRP A O   
1335 C CB  . TRP A 103 ? 0.2549 0.3746 0.3799 0.0350  0.0268  -0.0426 88  TRP A CB  
1336 C CG  . TRP A 103 ? 0.2513 0.3822 0.3937 0.0372  0.0279  -0.0362 88  TRP A CG  
1337 C CD1 . TRP A 103 ? 0.2559 0.4011 0.4073 0.0419  0.0355  -0.0354 88  TRP A CD1 
1338 C CD2 . TRP A 103 ? 0.2436 0.3735 0.3972 0.0355  0.0210  -0.0298 88  TRP A CD2 
1339 N NE1 . TRP A 103 ? 0.2505 0.4039 0.4199 0.0425  0.0335  -0.0286 88  TRP A NE1 
1340 C CE2 . TRP A 103 ? 0.2432 0.3875 0.4136 0.0386  0.0241  -0.0255 88  TRP A CE2 
1341 C CE3 . TRP A 103 ? 0.2954 0.4147 0.4461 0.0319  0.0126  -0.0273 88  TRP A CE3 
1342 C CZ2 . TRP A 103 ? 0.3315 0.4799 0.5158 0.0379  0.0178  -0.0192 88  TRP A CZ2 
1343 C CZ3 . TRP A 103 ? 0.2333 0.3566 0.3958 0.0318  0.0070  -0.0213 88  TRP A CZ3 
1344 C CH2 . TRP A 103 ? 0.2332 0.3709 0.4123 0.0346  0.0090  -0.0176 88  TRP A CH2 
1355 N N   . ILE A 104 ? 0.2638 0.3669 0.3563 0.0224  0.0183  -0.0444 89  ILE A N   
1356 C CA  . ILE A 104 ? 0.2716 0.3637 0.3526 0.0206  0.0152  -0.0503 89  ILE A CA  
1357 C C   . ILE A 104 ? 0.2505 0.3291 0.3373 0.0206  0.0100  -0.0505 89  ILE A C   
1358 O O   . ILE A 104 ? 0.3004 0.3771 0.3919 0.0180  0.0059  -0.0434 89  ILE A O   
1359 C CB  . ILE A 104 ? 0.3372 0.4304 0.4077 0.0146  0.0127  -0.0457 89  ILE A CB  
1360 C CG1 . ILE A 104 ? 0.4397 0.5471 0.5052 0.0149  0.0183  -0.0430 89  ILE A CG1 
1361 C CG2 . ILE A 104 ? 0.3471 0.4304 0.4076 0.0130  0.0091  -0.0518 89  ILE A CG2 
1362 C CD1 . ILE A 104 ? 0.4686 0.5850 0.5442 0.0123  0.0195  -0.0329 89  ILE A CD1 
1374 N N   . CYS A 105 ? 0.3000 0.3696 0.3866 0.0234  0.0101  -0.0586 90  CYS A N   
1375 C CA  . CYS A 105 ? 0.2709 0.3277 0.3647 0.0240  0.0064  -0.0579 90  CYS A CA  
1376 C C   . CYS A 105 ? 0.2820 0.3295 0.3684 0.0191  0.0020  -0.0587 90  CYS A C   
1377 O O   . CYS A 105 ? 0.2939 0.3399 0.3732 0.0181  0.0022  -0.0663 90  CYS A O   
1378 C CB  . CYS A 105 ? 0.2812 0.3325 0.3837 0.0302  0.0094  -0.0656 90  CYS A CB  
1379 S SG  . CYS A 105 ? 0.3637 0.4005 0.4781 0.0315  0.0058  -0.0617 90  CYS A SG  
1385 N N   . MET A 106 ? 0.2762 0.3183 0.3645 0.0165  -0.0020 -0.0511 91  MET A N   
1386 C CA  . MET A 106 ? 0.3078 0.3429 0.3901 0.0119  -0.0056 -0.0498 91  MET A CA  
1387 C C   . MET A 106 ? 0.2922 0.3172 0.3818 0.0127  -0.0079 -0.0450 91  MET A C   
1388 O O   . MET A 106 ? 0.2518 0.2766 0.3490 0.0163  -0.0076 -0.0405 91  MET A O   
1389 C CB  . MET A 106 ? 0.2377 0.2786 0.3116 0.0074  -0.0074 -0.0437 91  MET A CB  
1390 C CG  . MET A 106 ? 0.3380 0.3894 0.4049 0.0063  -0.0049 -0.0458 91  MET A CG  
1391 S SD  . MET A 106 ? 0.4804 0.5372 0.5423 0.0015  -0.0067 -0.0369 91  MET A SD  
1392 C CE  . MET A 106 ? 0.3409 0.4015 0.4132 0.0033  -0.0071 -0.0316 91  MET A CE  
1402 N N   . GLU A 107 ? 0.3143 0.3320 0.4018 0.0095  -0.0100 -0.0453 92  GLU A N   
1403 C CA  . GLU A 107 ? 0.3692 0.3785 0.4620 0.0096  -0.0116 -0.0386 92  GLU A CA  
1404 C C   . GLU A 107 ? 0.3620 0.3751 0.4517 0.0103  -0.0130 -0.0295 92  GLU A C   
1405 O O   . GLU A 107 ? 0.3176 0.3376 0.3996 0.0080  -0.0140 -0.0282 92  GLU A O   
1406 C CB  . GLU A 107 ? 0.4374 0.4421 0.5272 0.0050  -0.0135 -0.0392 92  GLU A CB  
1407 C CG  . GLU A 107 ? 0.4051 0.4014 0.5013 0.0050  -0.0140 -0.0322 92  GLU A CG  
1408 C CD  . GLU A 107 ? 0.4394 0.4333 0.5340 0.0002  -0.0157 -0.0325 92  GLU A CD  
1409 O OE1 . GLU A 107 ? 0.3430 0.3415 0.4313 -0.0028 -0.0171 -0.0388 92  GLU A OE1 
1410 O OE2 . GLU A 107 ? 0.4094 0.3978 0.5096 0.0000  -0.0154 -0.0258 92  GLU A OE2 
1417 N N   . PHE A 108 ? 0.2697 0.2781 0.3656 0.0137  -0.0133 -0.0233 93  PHE A N   
1418 C CA  . PHE A 108 ? 0.3767 0.3888 0.4689 0.0154  -0.0155 -0.0154 93  PHE A CA  
1419 C C   . PHE A 108 ? 0.2881 0.2958 0.3741 0.0136  -0.0167 -0.0097 93  PHE A C   
1420 O O   . PHE A 108 ? 0.3276 0.3280 0.4185 0.0139  -0.0153 -0.0074 93  PHE A O   
1421 C CB  . PHE A 108 ? 0.2715 0.2831 0.3728 0.0213  -0.0152 -0.0109 93  PHE A CB  
1422 C CG  . PHE A 108 ? 0.2835 0.2996 0.3803 0.0237  -0.0184 -0.0033 93  PHE A CG  
1423 C CD1 . PHE A 108 ? 0.2739 0.2991 0.3658 0.0224  -0.0214 -0.0042 93  PHE A CD1 
1424 C CD2 . PHE A 108 ? 0.2685 0.2802 0.3664 0.0275  -0.0186 0.0048  93  PHE A CD2 
1425 C CE1 . PHE A 108 ? 0.2401 0.2695 0.3277 0.0246  -0.0256 0.0012  93  PHE A CE1 
1426 C CE2 . PHE A 108 ? 0.2454 0.2623 0.3369 0.0304  -0.0222 0.0111  93  PHE A CE2 
1427 C CZ  . PHE A 108 ? 0.2553 0.2809 0.3415 0.0289  -0.0262 0.0084  93  PHE A CZ  
1437 N N   . CYS A 109 ? 0.3167 0.3289 0.3932 0.0119  -0.0191 -0.0075 94  CYS A N   
1438 C CA  . CYS A 109 ? 0.3247 0.3337 0.3938 0.0110  -0.0199 -0.0025 94  CYS A CA  
1439 C C   . CYS A 109 ? 0.2819 0.2945 0.3453 0.0144  -0.0228 0.0023  94  CYS A C   
1440 O O   . CYS A 109 ? 0.3032 0.3207 0.3609 0.0126  -0.0256 0.0002  94  CYS A O   
1441 C CB  . CYS A 109 ? 0.3457 0.3558 0.4079 0.0060  -0.0202 -0.0058 94  CYS A CB  
1442 S SG  . CYS A 109 ? 0.3809 0.3887 0.4479 0.0023  -0.0183 -0.0121 94  CYS A SG  
1448 N N   . GLY A 110 ? 0.2504 0.2606 0.3158 0.0194  -0.0222 0.0088  95  GLY A N   
1449 C CA  . GLY A 110 ? 0.2629 0.2782 0.3243 0.0240  -0.0256 0.0129  95  GLY A CA  
1450 C C   . GLY A 110 ? 0.3539 0.3711 0.4020 0.0239  -0.0286 0.0139  95  GLY A C   
1451 O O   . GLY A 110 ? 0.3756 0.3984 0.4191 0.0268  -0.0331 0.0146  95  GLY A O   
1455 N N   . ALA A 111 ? 0.2473 0.2602 0.2895 0.0211  -0.0266 0.0134  96  ALA A N   
1456 C CA  . ALA A 111 ? 0.3000 0.3135 0.3298 0.0217  -0.0288 0.0135  96  ALA A CA  
1457 C C   . ALA A 111 ? 0.2625 0.2775 0.2896 0.0163  -0.0313 0.0066  96  ALA A C   
1458 O O   . ALA A 111 ? 0.3925 0.4068 0.4105 0.0164  -0.0333 0.0052  96  ALA A O   
1459 C CB  . ALA A 111 ? 0.3277 0.3360 0.3532 0.0230  -0.0243 0.0184  96  ALA A CB  
1465 N N   . GLY A 112 ? 0.2787 0.2956 0.3138 0.0120  -0.0309 0.0024  97  GLY A N   
1466 C CA  . GLY A 112 ? 0.3770 0.3961 0.4114 0.0072  -0.0328 -0.0023 97  GLY A CA  
1467 C C   . GLY A 112 ? 0.3219 0.3367 0.3527 0.0039  -0.0302 -0.0027 97  GLY A C   
1468 O O   . GLY A 112 ? 0.2852 0.2965 0.3172 0.0041  -0.0268 -0.0006 97  GLY A O   
1472 N N   . SER A 113 ? 0.3007 0.3158 0.3286 0.0010  -0.0321 -0.0052 98  SER A N   
1473 C CA  . SER A 113 ? 0.2396 0.2514 0.2651 -0.0018 -0.0300 -0.0051 98  SER A CA  
1474 C C   . SER A 113 ? 0.2287 0.2354 0.2456 0.0013  -0.0297 -0.0033 98  SER A C   
1475 O O   . SER A 113 ? 0.2583 0.2648 0.2696 0.0051  -0.0322 -0.0035 98  SER A O   
1476 C CB  . SER A 113 ? 0.2795 0.2936 0.3078 -0.0062 -0.0314 -0.0075 98  SER A CB  
1477 O OG  . SER A 113 ? 0.3272 0.3392 0.3521 -0.0059 -0.0350 -0.0094 98  SER A OG  
1483 N N   . LEU A 114 ? 0.2321 0.2357 0.2480 0.0003  -0.0267 -0.0015 99  LEU A N   
1484 C CA  . LEU A 114 ? 0.3008 0.3002 0.3093 0.0035  -0.0254 0.0001  99  LEU A CA  
1485 C C   . LEU A 114 ? 0.2521 0.2495 0.2554 0.0038  -0.0289 -0.0042 99  LEU A C   
1486 O O   . LEU A 114 ? 0.2760 0.2706 0.2706 0.0083  -0.0292 -0.0048 99  LEU A O   
1487 C CB  . LEU A 114 ? 0.2895 0.2872 0.3006 0.0019  -0.0217 0.0029  99  LEU A CB  
1488 C CG  . LEU A 114 ? 0.2703 0.2684 0.2858 0.0030  -0.0183 0.0073  99  LEU A CG  
1489 C CD1 . LEU A 114 ? 0.3114 0.3096 0.3314 0.0007  -0.0160 0.0095  99  LEU A CD1 
1490 C CD2 . LEU A 114 ? 0.2496 0.2460 0.2596 0.0088  -0.0162 0.0113  99  LEU A CD2 
1502 N N   . GLN A 115 ? 0.2381 0.2369 0.2469 -0.0008 -0.0314 -0.0072 100 GLN A N   
1503 C CA  . GLN A 115 ? 0.2792 0.2756 0.2861 -0.0013 -0.0356 -0.0120 100 GLN A CA  
1504 C C   . GLN A 115 ? 0.3604 0.3592 0.3630 0.0019  -0.0403 -0.0150 100 GLN A C   
1505 O O   . GLN A 115 ? 0.3198 0.3156 0.3147 0.0049  -0.0434 -0.0190 100 GLN A O   
1506 C CB  . GLN A 115 ? 0.2559 0.2541 0.2726 -0.0072 -0.0368 -0.0131 100 GLN A CB  
1507 C CG  . GLN A 115 ? 0.3405 0.3354 0.3592 -0.0088 -0.0414 -0.0181 100 GLN A CG  
1508 C CD  . GLN A 115 ? 0.3736 0.3705 0.4044 -0.0148 -0.0414 -0.0171 100 GLN A CD  
1509 O OE1 . GLN A 115 ? 0.3680 0.3624 0.4017 -0.0167 -0.0381 -0.0138 100 GLN A OE1 
1510 N NE2 . GLN A 115 ? 0.4132 0.4155 0.4520 -0.0175 -0.0450 -0.0189 100 GLN A NE2 
1519 N N   . ASP A 116 ? 0.2824 0.2872 0.2897 0.0018  -0.0411 -0.0134 101 ASP A N   
1520 C CA  . ASP A 116 ? 0.3329 0.3414 0.3366 0.0055  -0.0458 -0.0149 101 ASP A CA  
1521 C C   . ASP A 116 ? 0.3506 0.3567 0.3415 0.0123  -0.0446 -0.0128 101 ASP A C   
1522 O O   . ASP A 116 ? 0.3712 0.3789 0.3541 0.0163  -0.0493 -0.0156 101 ASP A O   
1523 C CB  . ASP A 116 ? 0.4018 0.4166 0.4134 0.0054  -0.0455 -0.0121 101 ASP A CB  
1524 C CG  . ASP A 116 ? 0.4268 0.4461 0.4507 -0.0002 -0.0460 -0.0138 101 ASP A CG  
1525 O OD1 . ASP A 116 ? 0.3664 0.3857 0.3941 -0.0040 -0.0490 -0.0172 101 ASP A OD1 
1526 O OD2 . ASP A 116 ? 0.3708 0.3938 0.4012 -0.0005 -0.0432 -0.0115 101 ASP A OD2 
1531 N N   . ILE A 117 ? 0.3166 0.3197 0.3059 0.0139  -0.0383 -0.0075 102 ILE A N   
1532 C CA  . ILE A 117 ? 0.2651 0.2673 0.2442 0.0207  -0.0355 -0.0033 102 ILE A CA  
1533 C C   . ILE A 117 ? 0.2916 0.2894 0.2596 0.0237  -0.0354 -0.0067 102 ILE A C   
1534 O O   . ILE A 117 ? 0.3848 0.3837 0.3408 0.0297  -0.0375 -0.0081 102 ILE A O   
1535 C CB  . ILE A 117 ? 0.2883 0.2895 0.2732 0.0208  -0.0288 0.0040  102 ILE A CB  
1536 C CG1 . ILE A 117 ? 0.3437 0.3483 0.3392 0.0188  -0.0292 0.0060  102 ILE A CG1 
1537 C CG2 . ILE A 117 ? 0.3251 0.3260 0.3017 0.0277  -0.0248 0.0102  102 ILE A CG2 
1538 C CD1 . ILE A 117 ? 0.2626 0.2653 0.2666 0.0173  -0.0238 0.0108  102 ILE A CD1 
1550 N N   . TYR A 118 ? 0.3223 0.3153 0.2936 0.0203  -0.0329 -0.0083 103 TYR A N   
1551 C CA  . TYR A 118 ? 0.2815 0.2696 0.2429 0.0242  -0.0316 -0.0113 103 TYR A CA  
1552 C C   . TYR A 118 ? 0.2934 0.2797 0.2492 0.0245  -0.0388 -0.0208 103 TYR A C   
1553 O O   . TYR A 118 ? 0.3367 0.3197 0.2807 0.0299  -0.0389 -0.0249 103 TYR A O   
1554 C CB  . TYR A 118 ? 0.2758 0.2594 0.2432 0.0214  -0.0269 -0.0097 103 TYR A CB  
1555 C CG  . TYR A 118 ? 0.3349 0.3165 0.3127 0.0143  -0.0293 -0.0130 103 TYR A CG  
1556 C CD1 . TYR A 118 ? 0.2799 0.2576 0.2574 0.0127  -0.0343 -0.0204 103 TYR A CD1 
1557 C CD2 . TYR A 118 ? 0.3025 0.2859 0.2906 0.0096  -0.0265 -0.0084 103 TYR A CD2 
1558 C CE1 . TYR A 118 ? 0.3101 0.2861 0.2987 0.0065  -0.0356 -0.0215 103 TYR A CE1 
1559 C CE2 . TYR A 118 ? 0.2570 0.2396 0.2535 0.0040  -0.0280 -0.0098 103 TYR A CE2 
1560 C CZ  . TYR A 118 ? 0.2734 0.2523 0.2707 0.0025  -0.0321 -0.0155 103 TYR A CZ  
1561 O OH  . TYR A 118 ? 0.2962 0.2746 0.3036 -0.0030 -0.0327 -0.0152 103 TYR A OH  
1571 N N   . GLN A 119 ? 0.3472 0.3360 0.3116 0.0192  -0.0447 -0.0246 104 GLN A N   
1572 C CA  . GLN A 119 ? 0.3872 0.3753 0.3482 0.0192  -0.0526 -0.0338 104 GLN A CA  
1573 C C   . GLN A 119 ? 0.3657 0.3583 0.3123 0.0265  -0.0564 -0.0354 104 GLN A C   
1574 O O   . GLN A 119 ? 0.4004 0.3917 0.3392 0.0287  -0.0628 -0.0442 104 GLN A O   
1575 C CB  . GLN A 119 ? 0.3283 0.3199 0.3041 0.0118  -0.0578 -0.0361 104 GLN A CB  
1576 C CG  . GLN A 119 ? 0.3827 0.3697 0.3711 0.0050  -0.0552 -0.0356 104 GLN A CG  
1577 C CD  . GLN A 119 ? 0.4278 0.4199 0.4319 -0.0019 -0.0585 -0.0357 104 GLN A CD  
1578 O OE1 . GLN A 119 ? 0.4835 0.4834 0.4911 -0.0020 -0.0609 -0.0343 104 GLN A OE1 
1579 N NE2 . GLN A 119 ? 0.4222 0.4104 0.4367 -0.0073 -0.0578 -0.0365 104 GLN A NE2 
1588 N N   . VAL A 120 ? 0.3801 0.3780 0.3233 0.0307  -0.0528 -0.0271 105 VAL A N   
1589 C CA  . VAL A 120 ? 0.4027 0.4061 0.3315 0.0387  -0.0552 -0.0260 105 VAL A CA  
1590 C C   . VAL A 120 ? 0.3827 0.3840 0.2978 0.0465  -0.0477 -0.0210 105 VAL A C   
1591 O O   . VAL A 120 ? 0.4962 0.4991 0.3947 0.0538  -0.0497 -0.0244 105 VAL A O   
1592 C CB  . VAL A 120 ? 0.4251 0.4362 0.3606 0.0390  -0.0560 -0.0187 105 VAL A CB  
1593 C CG1 . VAL A 120 ? 0.4282 0.4453 0.3488 0.0485  -0.0565 -0.0140 105 VAL A CG1 
1594 C CG2 . VAL A 120 ? 0.4496 0.4650 0.3970 0.0331  -0.0640 -0.0240 105 VAL A CG2 
1604 N N   . THR A 121 ? 0.4084 0.4072 0.3305 0.0451  -0.0391 -0.0130 106 THR A N   
1605 C CA  . THR A 121 ? 0.3946 0.3933 0.3074 0.0522  -0.0309 -0.0059 106 THR A CA  
1606 C C   . THR A 121 ? 0.3745 0.3668 0.2810 0.0542  -0.0274 -0.0107 106 THR A C   
1607 O O   . THR A 121 ? 0.3466 0.3398 0.2410 0.0621  -0.0218 -0.0073 106 THR A O   
1608 C CB  . THR A 121 ? 0.3651 0.3644 0.2910 0.0496  -0.0237 0.0049  106 THR A CB  
1609 O OG1 . THR A 121 ? 0.3829 0.3773 0.3212 0.0422  -0.0222 0.0028  106 THR A OG1 
1610 C CG2 . THR A 121 ? 0.3954 0.3995 0.3294 0.0479  -0.0263 0.0094  106 THR A CG2 
1618 N N   . GLY A 122 ? 0.3977 0.3840 0.3129 0.0477  -0.0299 -0.0176 107 GLY A N   
1619 C CA  . GLY A 122 ? 0.4177 0.3974 0.3312 0.0490  -0.0253 -0.0202 107 GLY A CA  
1620 C C   . GLY A 122 ? 0.3646 0.3439 0.2909 0.0458  -0.0178 -0.0112 107 GLY A C   
1621 O O   . GLY A 122 ? 0.3523 0.3355 0.2887 0.0418  -0.0166 -0.0043 107 GLY A O   
1625 N N   . SER A 123 ? 0.3241 0.2988 0.2500 0.0479  -0.0128 -0.0116 108 SER A N   
1626 C CA  . SER A 123 ? 0.3941 0.3686 0.3339 0.0438  -0.0074 -0.0046 108 SER A CA  
1627 C C   . SER A 123 ? 0.3481 0.3289 0.2916 0.0457  -0.0013 0.0065  108 SER A C   
1628 O O   . SER A 123 ? 0.3829 0.3670 0.3163 0.0528  0.0023  0.0105  108 SER A O   
1629 C CB  . SER A 123 ? 0.4278 0.3969 0.3670 0.0469  -0.0030 -0.0067 108 SER A CB  
1630 O OG  . SER A 123 ? 0.4354 0.4053 0.3610 0.0566  0.0024  -0.0059 108 SER A OG  
1636 N N   . LEU A 124 ? 0.3506 0.3331 0.3091 0.0393  -0.0001 0.0117  109 LEU A N   
1637 C CA  . LEU A 124 ? 0.3896 0.3769 0.3557 0.0398  0.0052  0.0216  109 LEU A CA  
1638 C C   . LEU A 124 ? 0.3795 0.3679 0.3473 0.0443  0.0130  0.0275  109 LEU A C   
1639 O O   . LEU A 124 ? 0.3770 0.3621 0.3444 0.0452  0.0142  0.0243  109 LEU A O   
1640 C CB  . LEU A 124 ? 0.3320 0.3209 0.3135 0.0314  0.0028  0.0233  109 LEU A CB  
1641 C CG  . LEU A 124 ? 0.3354 0.3256 0.3184 0.0280  -0.0024 0.0210  109 LEU A CG  
1642 C CD1 . LEU A 124 ? 0.3503 0.3381 0.3256 0.0271  -0.0088 0.0123  109 LEU A CD1 
1643 C CD2 . LEU A 124 ? 0.3029 0.2948 0.3002 0.0209  -0.0035 0.0223  109 LEU A CD2 
1655 N N   . SER A 125 ? 0.3622 0.3553 0.3337 0.0474  0.0189  0.0370  110 SER A N   
1656 C CA  . SER A 125 ? 0.2914 0.2874 0.2688 0.0510  0.0270  0.0445  110 SER A CA  
1657 C C   . SER A 125 ? 0.2776 0.2750 0.2738 0.0435  0.0264  0.0469  110 SER A C   
1658 O O   . SER A 125 ? 0.2774 0.2743 0.2817 0.0361  0.0207  0.0443  110 SER A O   
1659 C CB  . SER A 125 ? 0.3635 0.3649 0.3418 0.0560  0.0336  0.0553  110 SER A CB  
1660 O OG  . SER A 125 ? 0.3193 0.3223 0.3131 0.0494  0.0318  0.0599  110 SER A OG  
1666 N N   . GLU A 126 ? 0.2852 0.2851 0.2880 0.0461  0.0323  0.0518  111 GLU A N   
1667 C CA  . GLU A 126 ? 0.2771 0.2798 0.2976 0.0396  0.0311  0.0543  111 GLU A CA  
1668 C C   . GLU A 126 ? 0.2845 0.2910 0.3195 0.0334  0.0294  0.0589  111 GLU A C   
1669 O O   . GLU A 126 ? 0.2849 0.2920 0.3294 0.0260  0.0238  0.0559  111 GLU A O   
1670 C CB  . GLU A 126 ? 0.2713 0.2779 0.2986 0.0442  0.0384  0.0605  111 GLU A CB  
1671 C CG  . GLU A 126 ? 0.2713 0.2825 0.3174 0.0379  0.0364  0.0635  111 GLU A CG  
1672 C CD  . GLU A 126 ? 0.3586 0.3741 0.4122 0.0429  0.0431  0.0693  111 GLU A CD  
1673 O OE1 . GLU A 126 ? 0.3925 0.4044 0.4342 0.0505  0.0475  0.0670  111 GLU A OE1 
1674 O OE2 . GLU A 126 ? 0.3106 0.3333 0.3828 0.0392  0.0436  0.0757  111 GLU A OE2 
1681 N N   . LEU A 127 ? 0.3072 0.3161 0.3441 0.0365  0.0341  0.0662  112 LEU A N   
1682 C CA  . LEU A 127 ? 0.3008 0.3120 0.3543 0.0308  0.0329  0.0706  112 LEU A CA  
1683 C C   . LEU A 127 ? 0.2519 0.2590 0.3020 0.0259  0.0255  0.0633  112 LEU A C   
1684 O O   . LEU A 127 ? 0.2953 0.3029 0.3584 0.0190  0.0214  0.0616  112 LEU A O   
1685 C CB  . LEU A 127 ? 0.2907 0.3051 0.3486 0.0359  0.0408  0.0818  112 LEU A CB  
1686 C CG  . LEU A 127 ? 0.3171 0.3379 0.3873 0.0387  0.0489  0.0914  112 LEU A CG  
1687 C CD1 . LEU A 127 ? 0.4310 0.4553 0.5019 0.0455  0.0580  0.1033  112 LEU A CD1 
1688 C CD2 . LEU A 127 ? 0.3339 0.3582 0.4281 0.0302  0.0458  0.0928  112 LEU A CD2 
1700 N N   . GLN A 128 ? 0.3069 0.3105 0.3401 0.0295  0.0235  0.0586  113 GLN A N   
1701 C CA  . GLN A 128 ? 0.2614 0.2620 0.2919 0.0251  0.0165  0.0514  113 GLN A CA  
1702 C C   . GLN A 128 ? 0.2876 0.2876 0.3212 0.0188  0.0109  0.0440  113 GLN A C   
1703 O O   . GLN A 128 ? 0.2651 0.2653 0.3061 0.0130  0.0065  0.0405  113 GLN A O   
1704 C CB  . GLN A 128 ? 0.3298 0.3282 0.3426 0.0304  0.0148  0.0478  113 GLN A CB  
1705 C CG  . GLN A 128 ? 0.3405 0.3408 0.3485 0.0372  0.0196  0.0558  113 GLN A CG  
1706 C CD  . GLN A 128 ? 0.3949 0.3947 0.3829 0.0437  0.0177  0.0519  113 GLN A CD  
1707 O OE1 . GLN A 128 ? 0.3905 0.3881 0.3680 0.0448  0.0152  0.0443  113 GLN A OE1 
1708 N NE2 . GLN A 128 ? 0.3919 0.3938 0.3754 0.0482  0.0186  0.0570  113 GLN A NE2 
1717 N N   . ILE A 129 ? 0.2448 0.2441 0.2729 0.0203  0.0113  0.0417  114 ILE A N   
1718 C CA  . ILE A 129 ? 0.2378 0.2372 0.2693 0.0149  0.0068  0.0368  114 ILE A CA  
1719 C C   . ILE A 129 ? 0.3023 0.3065 0.3495 0.0099  0.0061  0.0399  114 ILE A C   
1720 O O   . ILE A 129 ? 0.2813 0.2871 0.3323 0.0044  0.0011  0.0357  114 ILE A O   
1721 C CB  . ILE A 129 ? 0.2424 0.2394 0.2671 0.0183  0.0082  0.0352  114 ILE A CB  
1722 C CG1 . ILE A 129 ? 0.3462 0.3380 0.3558 0.0223  0.0068  0.0295  114 ILE A CG1 
1723 C CG2 . ILE A 129 ? 0.2648 0.2629 0.2952 0.0133  0.0044  0.0327  114 ILE A CG2 
1724 C CD1 . ILE A 129 ? 0.2916 0.2790 0.2946 0.0261  0.0080  0.0261  114 ILE A CD1 
1736 N N   . SER A 130 ? 0.2326 0.2403 0.2894 0.0118  0.0111  0.0472  115 SER A N   
1737 C CA  . SER A 130 ? 0.2905 0.3035 0.3643 0.0066  0.0096  0.0498  115 SER A CA  
1738 C C   . SER A 130 ? 0.2569 0.2693 0.3376 0.0016  0.0056  0.0466  115 SER A C   
1739 O O   . SER A 130 ? 0.2394 0.2549 0.3279 -0.0040 0.0005  0.0428  115 SER A O   
1740 C CB  . SER A 130 ? 0.2507 0.2679 0.3358 0.0097  0.0161  0.0591  115 SER A CB  
1741 O OG  . SER A 130 ? 0.3399 0.3572 0.4178 0.0159  0.0211  0.0618  115 SER A OG  
1747 N N   . TYR A 131 ? 0.2614 0.2702 0.3391 0.0040  0.0077  0.0481  116 TYR A N   
1748 C CA  . TYR A 131 ? 0.3266 0.3336 0.4113 0.0000  0.0043  0.0448  116 TYR A CA  
1749 C C   . TYR A 131 ? 0.2706 0.2766 0.3473 -0.0033 -0.0018 0.0353  116 TYR A C   
1750 O O   . TYR A 131 ? 0.2242 0.2313 0.3084 -0.0082 -0.0059 0.0304  116 TYR A O   
1751 C CB  . TYR A 131 ? 0.2647 0.2681 0.3469 0.0044  0.0082  0.0494  116 TYR A CB  
1752 C CG  . TYR A 131 ? 0.3101 0.3102 0.3975 0.0016  0.0049  0.0454  116 TYR A CG  
1753 C CD1 . TYR A 131 ? 0.2428 0.2427 0.3483 -0.0032 0.0037  0.0452  116 TYR A CD1 
1754 C CD2 . TYR A 131 ? 0.2658 0.2632 0.3415 0.0039  0.0030  0.0415  116 TYR A CD2 
1755 C CE1 . TYR A 131 ? 0.3391 0.3349 0.4500 -0.0050 0.0011  0.0408  116 TYR A CE1 
1756 C CE2 . TYR A 131 ? 0.2837 0.2783 0.3651 0.0022  0.0007  0.0383  116 TYR A CE2 
1757 C CZ  . TYR A 131 ? 0.3000 0.2934 0.3987 -0.0020 0.0001  0.0378  116 TYR A CZ  
1758 O OH  . TYR A 131 ? 0.3209 0.3104 0.4255 -0.0031 -0.0019 0.0336  116 TYR A OH  
1768 N N   . VAL A 132 ? 0.2227 0.2268 0.2847 -0.0006 -0.0023 0.0326  117 VAL A N   
1769 C CA  . VAL A 132 ? 0.2646 0.2686 0.3203 -0.0035 -0.0072 0.0251  117 VAL A CA  
1770 C C   . VAL A 132 ? 0.2641 0.2726 0.3240 -0.0080 -0.0105 0.0224  117 VAL A C   
1771 O O   . VAL A 132 ? 0.2461 0.2567 0.3077 -0.0116 -0.0142 0.0171  117 VAL A O   
1772 C CB  . VAL A 132 ? 0.2616 0.2629 0.3036 -0.0002 -0.0073 0.0232  117 VAL A CB  
1773 C CG1 . VAL A 132 ? 0.2858 0.2884 0.3241 -0.0037 -0.0116 0.0171  117 VAL A CG1 
1774 C CG2 . VAL A 132 ? 0.2591 0.2576 0.2957 0.0040  -0.0059 0.0244  117 VAL A CG2 
1784 N N   . CYS A 133 ? 0.2677 0.2785 0.3287 -0.0070 -0.0090 0.0263  118 CYS A N   
1785 C CA  . CYS A 133 ? 0.2524 0.2688 0.3172 -0.0105 -0.0124 0.0251  118 CYS A CA  
1786 C C   . CYS A 133 ? 0.2608 0.2815 0.3373 -0.0148 -0.0156 0.0232  118 CYS A C   
1787 O O   . CYS A 133 ? 0.2557 0.2808 0.3316 -0.0182 -0.0202 0.0184  118 CYS A O   
1788 C CB  . CYS A 133 ? 0.2246 0.2426 0.2909 -0.0079 -0.0097 0.0307  118 CYS A CB  
1789 S SG  . CYS A 133 ? 0.3713 0.3834 0.4243 -0.0035 -0.0075 0.0302  118 CYS A SG  
1795 N N   . ARG A 134 ? 0.2380 0.2580 0.3257 -0.0146 -0.0132 0.0270  119 ARG A N   
1796 C CA  . ARG A 134 ? 0.2136 0.2367 0.3148 -0.0193 -0.0169 0.0241  119 ARG A CA  
1797 C C   . ARG A 134 ? 0.2610 0.2819 0.3584 -0.0216 -0.0206 0.0154  119 ARG A C   
1798 O O   . ARG A 134 ? 0.2515 0.2767 0.3509 -0.0252 -0.0259 0.0091  119 ARG A O   
1799 C CB  . ARG A 134 ? 0.2362 0.2575 0.3520 -0.0187 -0.0129 0.0303  119 ARG A CB  
1800 C CG  . ARG A 134 ? 0.2388 0.2631 0.3727 -0.0243 -0.0173 0.0273  119 ARG A CG  
1801 C CD  . ARG A 134 ? 0.3084 0.3295 0.4589 -0.0242 -0.0129 0.0339  119 ARG A CD  
1802 N NE  . ARG A 134 ? 0.3005 0.3136 0.4470 -0.0220 -0.0103 0.0331  119 ARG A NE  
1803 C CZ  . ARG A 134 ? 0.2637 0.2728 0.4222 -0.0207 -0.0056 0.0399  119 ARG A CZ  
1804 N NH1 . ARG A 134 ? 0.2929 0.3051 0.4688 -0.0216 -0.0021 0.0484  119 ARG A NH1 
1805 N NH2 . ARG A 134 ? 0.3543 0.3566 0.5083 -0.0183 -0.0039 0.0392  119 ARG A NH2 
1819 N N   . GLU A 135 ? 0.2445 0.2591 0.3357 -0.0189 -0.0180 0.0150  120 GLU A N   
1820 C CA  . GLU A 135 ? 0.2658 0.2782 0.3547 -0.0202 -0.0205 0.0073  120 GLU A CA  
1821 C C   . GLU A 135 ? 0.2156 0.2324 0.2932 -0.0212 -0.0238 0.0016  120 GLU A C   
1822 O O   . GLU A 135 ? 0.2508 0.2695 0.3283 -0.0233 -0.0270 -0.0059 120 GLU A O   
1823 C CB  . GLU A 135 ? 0.2692 0.2754 0.3543 -0.0163 -0.0169 0.0096  120 GLU A CB  
1824 C CG  . GLU A 135 ? 0.2748 0.2770 0.3712 -0.0146 -0.0130 0.0165  120 GLU A CG  
1825 C CD  . GLU A 135 ? 0.2763 0.2773 0.3894 -0.0186 -0.0151 0.0133  120 GLU A CD  
1826 O OE1 . GLU A 135 ? 0.3389 0.3366 0.4538 -0.0193 -0.0170 0.0069  120 GLU A OE1 
1827 O OE2 . GLU A 135 ? 0.3490 0.3524 0.4743 -0.0210 -0.0151 0.0168  120 GLU A OE2 
1834 N N   . VAL A 136 ? 0.2463 0.2647 0.3145 -0.0195 -0.0225 0.0050  121 VAL A N   
1835 C CA  . VAL A 136 ? 0.2133 0.2363 0.2724 -0.0204 -0.0247 0.0018  121 VAL A CA  
1836 C C   . VAL A 136 ? 0.2554 0.2861 0.3172 -0.0233 -0.0287 0.0001  121 VAL A C   
1837 O O   . VAL A 136 ? 0.2726 0.3085 0.3291 -0.0245 -0.0314 -0.0050 121 VAL A O   
1838 C CB  . VAL A 136 ? 0.2719 0.2933 0.3231 -0.0180 -0.0224 0.0064  121 VAL A CB  
1839 C CG1 . VAL A 136 ? 0.2650 0.2921 0.3102 -0.0194 -0.0242 0.0055  121 VAL A CG1 
1840 C CG2 . VAL A 136 ? 0.3012 0.3168 0.3480 -0.0154 -0.0202 0.0060  121 VAL A CG2 
1850 N N   . LEU A 137 ? 0.2131 0.2460 0.2830 -0.0239 -0.0291 0.0046  122 LEU A N   
1851 C CA  . LEU A 137 ? 0.2152 0.2569 0.2890 -0.0265 -0.0340 0.0032  122 LEU A CA  
1852 C C   . LEU A 137 ? 0.2584 0.3019 0.3376 -0.0296 -0.0385 -0.0055 122 LEU A C   
1853 O O   . LEU A 137 ? 0.2509 0.3022 0.3268 -0.0313 -0.0435 -0.0103 122 LEU A O   
1854 C CB  . LEU A 137 ? 0.2137 0.2577 0.2979 -0.0264 -0.0333 0.0102  122 LEU A CB  
1855 C CG  . LEU A 137 ? 0.2980 0.3428 0.3768 -0.0233 -0.0304 0.0176  122 LEU A CG  
1856 C CD1 . LEU A 137 ? 0.3160 0.3618 0.4058 -0.0219 -0.0278 0.0247  122 LEU A CD1 
1857 C CD2 . LEU A 137 ? 0.2601 0.3134 0.3330 -0.0241 -0.0344 0.0173  122 LEU A CD2 
1869 N N   . GLN A 138 ? 0.2288 0.2650 0.3162 -0.0300 -0.0369 -0.0077 123 GLN A N   
1870 C CA  . GLN A 138 ? 0.2274 0.2633 0.3210 -0.0327 -0.0411 -0.0172 123 GLN A CA  
1871 C C   . GLN A 138 ? 0.2308 0.2687 0.3111 -0.0316 -0.0422 -0.0249 123 GLN A C   
1872 O O   . GLN A 138 ? 0.2547 0.2986 0.3323 -0.0332 -0.0472 -0.0329 123 GLN A O   
1873 C CB  . GLN A 138 ? 0.2828 0.3094 0.3890 -0.0328 -0.0381 -0.0163 123 GLN A CB  
1874 C CG  . GLN A 138 ? 0.2836 0.3104 0.4062 -0.0346 -0.0375 -0.0096 123 GLN A CG  
1875 C CD  . GLN A 138 ? 0.3129 0.3310 0.4455 -0.0329 -0.0319 -0.0037 123 GLN A CD  
1876 O OE1 . GLN A 138 ? 0.2835 0.2951 0.4117 -0.0305 -0.0293 -0.0054 123 GLN A OE1 
1877 N NE2 . GLN A 138 ? 0.2443 0.2633 0.3912 -0.0337 -0.0297 0.0042  123 GLN A NE2 
1886 N N   . GLY A 139 ? 0.2382 0.2721 0.3100 -0.0286 -0.0376 -0.0226 124 GLY A N   
1887 C CA  . GLY A 139 ? 0.2898 0.3269 0.3501 -0.0273 -0.0375 -0.0281 124 GLY A CA  
1888 C C   . GLY A 139 ? 0.3145 0.3621 0.3650 -0.0276 -0.0401 -0.0278 124 GLY A C   
1889 O O   . GLY A 139 ? 0.2441 0.2978 0.2880 -0.0275 -0.0426 -0.0351 124 GLY A O   
1893 N N   . LEU A 140 ? 0.2294 0.2795 0.2787 -0.0274 -0.0393 -0.0191 125 LEU A N   
1894 C CA  . LEU A 140 ? 0.2612 0.3212 0.3020 -0.0272 -0.0412 -0.0165 125 LEU A CA  
1895 C C   . LEU A 140 ? 0.2561 0.3248 0.2988 -0.0291 -0.0477 -0.0213 125 LEU A C   
1896 O O   . LEU A 140 ? 0.3246 0.4030 0.3576 -0.0284 -0.0503 -0.0238 125 LEU A O   
1897 C CB  . LEU A 140 ? 0.2240 0.2832 0.2655 -0.0262 -0.0388 -0.0061 125 LEU A CB  
1898 C CG  . LEU A 140 ? 0.2690 0.3222 0.3061 -0.0243 -0.0337 -0.0017 125 LEU A CG  
1899 C CD1 . LEU A 140 ? 0.3225 0.3737 0.3619 -0.0232 -0.0318 0.0071  125 LEU A CD1 
1900 C CD2 . LEU A 140 ? 0.2226 0.2812 0.2506 -0.0237 -0.0326 -0.0028 125 LEU A CD2 
1912 N N   . ALA A 141 ? 0.2486 0.3149 0.3042 -0.0315 -0.0506 -0.0224 126 ALA A N   
1913 C CA  . ALA A 141 ? 0.2952 0.3699 0.3548 -0.0339 -0.0581 -0.0285 126 ALA A CA  
1914 C C   . ALA A 141 ? 0.2804 0.3570 0.3331 -0.0339 -0.0611 -0.0413 126 ALA A C   
1915 O O   . ALA A 141 ? 0.2632 0.3505 0.3083 -0.0339 -0.0667 -0.0466 126 ALA A O   
1916 C CB  . ALA A 141 ? 0.2788 0.3495 0.3570 -0.0370 -0.0601 -0.0278 126 ALA A CB  
1922 N N   . TYR A 142 ? 0.2814 0.3482 0.3362 -0.0333 -0.0575 -0.0463 127 TYR A N   
1923 C CA  . TYR A 142 ? 0.3170 0.3847 0.3653 -0.0323 -0.0593 -0.0588 127 TYR A CA  
1924 C C   . TYR A 142 ? 0.2981 0.3748 0.3280 -0.0288 -0.0572 -0.0584 127 TYR A C   
1925 O O   . TYR A 142 ? 0.3287 0.4146 0.3490 -0.0278 -0.0613 -0.0664 127 TYR A O   
1926 C CB  . TYR A 142 ? 0.3324 0.3876 0.3882 -0.0316 -0.0551 -0.0627 127 TYR A CB  
1927 C CG  . TYR A 142 ? 0.2795 0.3353 0.3280 -0.0294 -0.0555 -0.0753 127 TYR A CG  
1928 C CD1 . TYR A 142 ? 0.3525 0.4071 0.4070 -0.0311 -0.0614 -0.0885 127 TYR A CD1 
1929 C CD2 . TYR A 142 ? 0.2893 0.3472 0.3257 -0.0254 -0.0501 -0.0744 127 TYR A CD2 
1930 C CE1 . TYR A 142 ? 0.3413 0.3961 0.3883 -0.0282 -0.0613 -0.1011 127 TYR A CE1 
1931 C CE2 . TYR A 142 ? 0.3751 0.4345 0.4049 -0.0226 -0.0495 -0.0856 127 TYR A CE2 
1932 C CZ  . TYR A 142 ? 0.3148 0.3724 0.3489 -0.0236 -0.0549 -0.0991 127 TYR A CZ  
1933 O OH  . TYR A 142 ? 0.3954 0.4541 0.4220 -0.0198 -0.0537 -0.1109 127 TYR A OH  
1943 N N   . LEU A 143 ? 0.3082 0.3829 0.3335 -0.0267 -0.0507 -0.0493 128 LEU A N   
1944 C CA  . LEU A 143 ? 0.3708 0.4542 0.3815 -0.0237 -0.0477 -0.0469 128 LEU A CA  
1945 C C   . LEU A 143 ? 0.2904 0.3873 0.2925 -0.0234 -0.0522 -0.0447 128 LEU A C   
1946 O O   . LEU A 143 ? 0.3447 0.4517 0.3343 -0.0209 -0.0533 -0.0498 128 LEU A O   
1947 C CB  . LEU A 143 ? 0.2859 0.3650 0.2967 -0.0227 -0.0413 -0.0361 128 LEU A CB  
1948 C CG  . LEU A 143 ? 0.2637 0.3328 0.2795 -0.0219 -0.0368 -0.0383 128 LEU A CG  
1949 C CD1 . LEU A 143 ? 0.2388 0.3047 0.2550 -0.0213 -0.0322 -0.0285 128 LEU A CD1 
1950 C CD2 . LEU A 143 ? 0.3226 0.3951 0.3322 -0.0193 -0.0351 -0.0472 128 LEU A CD2 
1962 N N   . HIS A 144 ? 0.2643 0.3624 0.2728 -0.0253 -0.0549 -0.0368 129 HIS A N   
1963 C CA  . HIS A 144 ? 0.2962 0.4077 0.2978 -0.0246 -0.0594 -0.0328 129 HIS A CA  
1964 C C   . HIS A 144 ? 0.3468 0.4667 0.3448 -0.0252 -0.0676 -0.0450 129 HIS A C   
1965 O O   . HIS A 144 ? 0.3495 0.4830 0.3345 -0.0228 -0.0708 -0.0455 129 HIS A O   
1966 C CB  . HIS A 144 ? 0.3511 0.4613 0.3632 -0.0262 -0.0605 -0.0223 129 HIS A CB  
1967 C CG  . HIS A 144 ? 0.2803 0.3832 0.2942 -0.0251 -0.0532 -0.0112 129 HIS A CG  
1968 N ND1 . HIS A 144 ? 0.3085 0.4085 0.3311 -0.0254 -0.0524 -0.0018 129 HIS A ND1 
1969 C CD2 . HIS A 144 ? 0.2953 0.3935 0.3042 -0.0235 -0.0468 -0.0088 129 HIS A CD2 
1970 C CE1 . HIS A 144 ? 0.3668 0.4597 0.3887 -0.0241 -0.0461 0.0049  129 HIS A CE1 
1971 N NE2 . HIS A 144 ? 0.3053 0.3972 0.3196 -0.0233 -0.0430 0.0010  129 HIS A NE2 
1979 N N   . SER A 145 ? 0.2951 0.4072 0.3046 -0.0282 -0.0712 -0.0550 130 SER A N   
1980 C CA  . SER A 145 ? 0.3216 0.4403 0.3291 -0.0292 -0.0798 -0.0687 130 SER A CA  
1981 C C   . SER A 145 ? 0.3130 0.4371 0.3031 -0.0250 -0.0783 -0.0784 130 SER A C   
1982 O O   . SER A 145 ? 0.3817 0.5172 0.3614 -0.0237 -0.0850 -0.0873 130 SER A O   
1983 C CB  . SER A 145 ? 0.3631 0.4704 0.3892 -0.0335 -0.0831 -0.0774 130 SER A CB  
1984 O OG  . SER A 145 ? 0.3663 0.4612 0.3949 -0.0325 -0.0771 -0.0824 130 SER A OG  
1990 N N   . GLN A 146 ? 0.3422 0.4591 0.3290 -0.0226 -0.0697 -0.0768 131 GLN A N   
1991 C CA  . GLN A 146 ? 0.3546 0.4772 0.3256 -0.0178 -0.0660 -0.0834 131 GLN A CA  
1992 C C   . GLN A 146 ? 0.4302 0.5661 0.3859 -0.0141 -0.0619 -0.0720 131 GLN A C   
1993 O O   . GLN A 146 ? 0.3883 0.5297 0.3317 -0.0097 -0.0566 -0.0740 131 GLN A O   
1994 C CB  . GLN A 146 ? 0.3531 0.4631 0.3301 -0.0169 -0.0585 -0.0855 131 GLN A CB  
1995 C CG  . GLN A 146 ? 0.4064 0.5022 0.4001 -0.0201 -0.0612 -0.0944 131 GLN A CG  
1996 C CD  . GLN A 146 ? 0.4467 0.5441 0.4387 -0.0199 -0.0681 -0.1121 131 GLN A CD  
1997 O OE1 . GLN A 146 ? 0.4970 0.5977 0.4776 -0.0156 -0.0660 -0.1218 131 GLN A OE1 
1998 N NE2 . GLN A 146 ? 0.4768 0.5723 0.4805 -0.0245 -0.0763 -0.1166 131 GLN A NE2 
2007 N N   . LYS A 147 ? 0.3504 0.4912 0.3081 -0.0154 -0.0635 -0.0593 132 LYS A N   
2008 C CA  . LYS A 147 ? 0.3271 0.4802 0.2729 -0.0120 -0.0599 -0.0467 132 LYS A CA  
2009 C C   . LYS A 147 ? 0.3425 0.4905 0.2887 -0.0106 -0.0496 -0.0378 132 LYS A C   
2010 O O   . LYS A 147 ? 0.3943 0.5524 0.3294 -0.0069 -0.0447 -0.0310 132 LYS A O   
2011 C CB  . LYS A 147 ? 0.4133 0.5832 0.3399 -0.0076 -0.0634 -0.0532 132 LYS A CB  
2012 C CG  . LYS A 147 ? 0.4840 0.6591 0.4102 -0.0092 -0.0750 -0.0657 132 LYS A CG  
2013 C CD  . LYS A 147 ? 0.6212 0.8086 0.5462 -0.0095 -0.0816 -0.0562 132 LYS A CD  
2014 C CE  . LYS A 147 ? 0.7533 0.9609 0.6557 -0.0034 -0.0828 -0.0540 132 LYS A CE  
2015 N NZ  . LYS A 147 ? 0.7755 0.9972 0.6742 -0.0035 -0.0949 -0.0565 132 LYS A NZ  
2029 N N   . LYS A 148 ? 0.3179 0.4508 0.2776 -0.0134 -0.0465 -0.0374 133 LYS A N   
2030 C CA  . LYS A 148 ? 0.2849 0.4119 0.2482 -0.0129 -0.0382 -0.0295 133 LYS A CA  
2031 C C   . LYS A 148 ? 0.3188 0.4385 0.2926 -0.0155 -0.0373 -0.0176 133 LYS A C   
2032 O O   . LYS A 148 ? 0.3956 0.5116 0.3766 -0.0179 -0.0421 -0.0171 133 LYS A O   
2033 C CB  . LYS A 148 ? 0.2814 0.3975 0.2511 -0.0131 -0.0355 -0.0386 133 LYS A CB  
2034 C CG  . LYS A 148 ? 0.3975 0.5174 0.3594 -0.0104 -0.0371 -0.0532 133 LYS A CG  
2035 C CD  . LYS A 148 ? 0.4469 0.5796 0.3948 -0.0056 -0.0316 -0.0521 133 LYS A CD  
2036 C CE  . LYS A 148 ? 0.4683 0.6032 0.4089 -0.0019 -0.0318 -0.0678 133 LYS A CE  
2037 N NZ  . LYS A 148 ? 0.5691 0.7125 0.4989 -0.0009 -0.0396 -0.0777 133 LYS A NZ  
2051 N N   . ILE A 149 ? 0.3758 0.4935 0.3515 -0.0151 -0.0310 -0.0085 134 ILE A N   
2052 C CA  . ILE A 149 ? 0.2666 0.3759 0.2520 -0.0171 -0.0294 0.0013  134 ILE A CA  
2053 C C   . ILE A 149 ? 0.2824 0.3815 0.2747 -0.0179 -0.0249 0.0006  134 ILE A C   
2054 O O   . ILE A 149 ? 0.3262 0.4289 0.3155 -0.0165 -0.0207 -0.0005 134 ILE A O   
2055 C CB  . ILE A 149 ? 0.3310 0.4479 0.3139 -0.0159 -0.0272 0.0144  134 ILE A CB  
2056 C CG1 . ILE A 149 ? 0.3846 0.5155 0.3578 -0.0139 -0.0315 0.0155  134 ILE A CG1 
2057 C CG2 . ILE A 149 ? 0.2497 0.3568 0.2434 -0.0177 -0.0268 0.0225  134 ILE A CG2 
2058 C CD1 . ILE A 149 ? 0.3925 0.5331 0.3622 -0.0117 -0.0286 0.0296  134 ILE A CD1 
2070 N N   . HIS A 150 ? 0.2644 0.3517 0.2657 -0.0198 -0.0256 0.0016  135 HIS A N   
2071 C CA  . HIS A 150 ? 0.2779 0.3564 0.2850 -0.0203 -0.0223 0.0011  135 HIS A CA  
2072 C C   . HIS A 150 ? 0.2909 0.3704 0.3002 -0.0206 -0.0184 0.0099  135 HIS A C   
2073 O O   . HIS A 150 ? 0.2870 0.3681 0.2977 -0.0203 -0.0151 0.0097  135 HIS A O   
2074 C CB  . HIS A 150 ? 0.2829 0.3497 0.2972 -0.0214 -0.0240 -0.0002 135 HIS A CB  
2075 C CG  . HIS A 150 ? 0.2215 0.2805 0.2402 -0.0212 -0.0218 -0.0018 135 HIS A CG  
2076 N ND1 . HIS A 150 ? 0.3055 0.3612 0.3273 -0.0217 -0.0197 0.0035  135 HIS A ND1 
2077 C CD2 . HIS A 150 ? 0.2239 0.2784 0.2450 -0.0205 -0.0218 -0.0081 135 HIS A CD2 
2078 C CE1 . HIS A 150 ? 0.2381 0.2886 0.2631 -0.0213 -0.0191 0.0002  135 HIS A CE1 
2079 N NE2 . HIS A 150 ? 0.2423 0.2921 0.2669 -0.0203 -0.0201 -0.0062 135 HIS A NE2 
2087 N N   . ARG A 151 ? 0.3348 0.4130 0.3465 -0.0211 -0.0188 0.0179  136 ARG A N   
2088 C CA  . ARG A 151 ? 0.2982 0.3769 0.3141 -0.0216 -0.0157 0.0276  136 ARG A CA  
2089 C C   . ARG A 151 ? 0.3514 0.4182 0.3758 -0.0232 -0.0149 0.0280  136 ARG A C   
2090 O O   . ARG A 151 ? 0.2979 0.3621 0.3280 -0.0240 -0.0132 0.0352  136 ARG A O   
2091 C CB  . ARG A 151 ? 0.3001 0.3894 0.3130 -0.0209 -0.0116 0.0312  136 ARG A CB  
2092 C CG  . ARG A 151 ? 0.3312 0.4341 0.3336 -0.0185 -0.0121 0.0326  136 ARG A CG  
2093 C CD  . ARG A 151 ? 0.4588 0.5733 0.4579 -0.0169 -0.0067 0.0381  136 ARG A CD  
2094 N NE  . ARG A 151 ? 0.4477 0.5762 0.4346 -0.0137 -0.0073 0.0403  136 ARG A NE  
2095 C CZ  . ARG A 151 ? 0.4862 0.6219 0.4621 -0.0114 -0.0092 0.0306  136 ARG A CZ  
2096 N NH1 . ARG A 151 ? 0.4762 0.6057 0.4530 -0.0118 -0.0101 0.0188  136 ARG A NH1 
2097 N NH2 . ARG A 151 ? 0.5883 0.7376 0.5520 -0.0082 -0.0104 0.0327  136 ARG A NH2 
2111 N N   . ASP A 152 ? 0.3005 0.3601 0.3262 -0.0233 -0.0162 0.0207  137 ASP A N   
2112 C CA  . ASP A 152 ? 0.2633 0.3135 0.2953 -0.0243 -0.0160 0.0201  137 ASP A CA  
2113 C C   . ASP A 152 ? 0.2646 0.3062 0.2959 -0.0232 -0.0183 0.0146  137 ASP A C   
2114 O O   . ASP A 152 ? 0.2493 0.2866 0.2822 -0.0230 -0.0188 0.0105  137 ASP A O   
2115 C CB  . ASP A 152 ? 0.3693 0.4231 0.4047 -0.0251 -0.0142 0.0187  137 ASP A CB  
2116 C CG  . ASP A 152 ? 0.3443 0.3912 0.3879 -0.0269 -0.0146 0.0198  137 ASP A CG  
2117 O OD1 . ASP A 152 ? 0.4360 0.4754 0.4821 -0.0273 -0.0156 0.0224  137 ASP A OD1 
2118 O OD2 . ASP A 152 ? 0.5362 0.5852 0.5845 -0.0277 -0.0142 0.0176  137 ASP A OD2 
2123 N N   . ILE A 153 ? 0.2151 0.2548 0.2448 -0.0223 -0.0196 0.0156  138 ILE A N   
2124 C CA  . ILE A 153 ? 0.2625 0.2948 0.2925 -0.0210 -0.0206 0.0124  138 ILE A CA  
2125 C C   . ILE A 153 ? 0.2568 0.2803 0.2888 -0.0202 -0.0202 0.0135  138 ILE A C   
2126 O O   . ILE A 153 ? 0.2575 0.2788 0.2916 -0.0202 -0.0195 0.0179  138 ILE A O   
2127 C CB  . ILE A 153 ? 0.2658 0.2999 0.2959 -0.0204 -0.0217 0.0141  138 ILE A CB  
2128 C CG1 . ILE A 153 ? 0.3098 0.3516 0.3381 -0.0213 -0.0235 0.0101  138 ILE A CG1 
2129 C CG2 . ILE A 153 ? 0.2977 0.3242 0.3298 -0.0186 -0.0214 0.0136  138 ILE A CG2 
2130 C CD1 . ILE A 153 ? 0.2552 0.2940 0.2841 -0.0210 -0.0237 0.0036  138 ILE A CD1 
2142 N N   . LYS A 154 ? 0.3022 0.3209 0.3334 -0.0191 -0.0208 0.0094  139 LYS A N   
2143 C CA  . LYS A 154 ? 0.2685 0.2793 0.2995 -0.0177 -0.0213 0.0084  139 LYS A CA  
2144 C C   . LYS A 154 ? 0.2683 0.2766 0.2965 -0.0156 -0.0223 0.0043  139 LYS A C   
2145 O O   . LYS A 154 ? 0.2716 0.2837 0.2999 -0.0157 -0.0223 0.0026  139 LYS A O   
2146 C CB  . LYS A 154 ? 0.2785 0.2887 0.3138 -0.0199 -0.0219 0.0090  139 LYS A CB  
2147 C CG  . LYS A 154 ? 0.2460 0.2619 0.2839 -0.0218 -0.0225 0.0070  139 LYS A CG  
2148 C CD  . LYS A 154 ? 0.2854 0.3035 0.3308 -0.0249 -0.0221 0.0099  139 LYS A CD  
2149 C CE  . LYS A 154 ? 0.3694 0.3797 0.4188 -0.0255 -0.0247 0.0071  139 LYS A CE  
2150 N NZ  . LYS A 154 ? 0.4498 0.4610 0.5098 -0.0291 -0.0242 0.0108  139 LYS A NZ  
2164 N N   . GLY A 155 ? 0.2768 0.2787 0.3021 -0.0132 -0.0231 0.0026  140 GLY A N   
2165 C CA  . GLY A 155 ? 0.2663 0.2665 0.2876 -0.0102 -0.0241 0.0000  140 GLY A CA  
2166 C C   . GLY A 155 ? 0.3146 0.3193 0.3385 -0.0115 -0.0261 -0.0025 140 GLY A C   
2167 O O   . GLY A 155 ? 0.2258 0.2318 0.2489 -0.0095 -0.0260 -0.0030 140 GLY A O   
2171 N N   . ALA A 156 ? 0.2334 0.2406 0.2620 -0.0146 -0.0275 -0.0035 141 ALA A N   
2172 C CA  . ALA A 156 ? 0.3016 0.3142 0.3344 -0.0156 -0.0291 -0.0055 141 ALA A CA  
2173 C C   . ALA A 156 ? 0.2567 0.2753 0.2916 -0.0160 -0.0267 -0.0049 141 ALA A C   
2174 O O   . ALA A 156 ? 0.2381 0.2609 0.2762 -0.0155 -0.0273 -0.0066 141 ALA A O   
2175 C CB  . ALA A 156 ? 0.2849 0.2996 0.3249 -0.0192 -0.0306 -0.0056 141 ALA A CB  
2181 N N   . ASN A 157 ? 0.2226 0.2420 0.2559 -0.0168 -0.0244 -0.0030 142 ASN A N   
2182 C CA  . ASN A 157 ? 0.2767 0.3016 0.3110 -0.0171 -0.0228 -0.0041 142 ASN A CA  
2183 C C   . ASN A 157 ? 0.3250 0.3468 0.3579 -0.0153 -0.0224 -0.0050 142 ASN A C   
2184 O O   . ASN A 157 ? 0.2725 0.2975 0.3063 -0.0158 -0.0216 -0.0070 142 ASN A O   
2185 C CB  . ASN A 157 ? 0.2208 0.2511 0.2549 -0.0195 -0.0212 -0.0018 142 ASN A CB  
2186 C CG  . ASN A 157 ? 0.2969 0.3328 0.3351 -0.0213 -0.0203 -0.0002 142 ASN A CG  
2187 O OD1 . ASN A 157 ? 0.3412 0.3795 0.3832 -0.0210 -0.0205 -0.0022 142 ASN A OD1 
2188 N ND2 . ASN A 157 ? 0.2727 0.3112 0.3115 -0.0232 -0.0190 0.0044  142 ASN A ND2 
2195 N N   . ILE A 158 ? 0.2601 0.2760 0.2912 -0.0130 -0.0228 -0.0036 143 ILE A N   
2196 C CA  . ILE A 158 ? 0.2931 0.3061 0.3255 -0.0113 -0.0218 -0.0030 143 ILE A CA  
2197 C C   . ILE A 158 ? 0.2499 0.2605 0.2827 -0.0080 -0.0221 -0.0031 143 ILE A C   
2198 O O   . ILE A 158 ? 0.2890 0.2971 0.3176 -0.0057 -0.0230 -0.0017 143 ILE A O   
2199 C CB  . ILE A 158 ? 0.2758 0.2852 0.3064 -0.0106 -0.0207 0.0007  143 ILE A CB  
2200 C CG1 . ILE A 158 ? 0.2474 0.2602 0.2785 -0.0133 -0.0208 0.0017  143 ILE A CG1 
2201 C CG2 . ILE A 158 ? 0.2318 0.2390 0.2665 -0.0090 -0.0192 0.0025  143 ILE A CG2 
2202 C CD1 . ILE A 158 ? 0.2362 0.2460 0.2664 -0.0121 -0.0196 0.0057  143 ILE A CD1 
2214 N N   . LEU A 159 ? 0.3306 0.3424 0.3683 -0.0075 -0.0217 -0.0051 144 LEU A N   
2215 C CA  . LEU A 159 ? 0.2932 0.3038 0.3329 -0.0040 -0.0220 -0.0045 144 LEU A CA  
2216 C C   . LEU A 159 ? 0.2708 0.2766 0.3134 -0.0015 -0.0201 -0.0007 144 LEU A C   
2217 O O   . LEU A 159 ? 0.2769 0.2810 0.3235 -0.0033 -0.0187 -0.0003 144 LEU A O   
2218 C CB  . LEU A 159 ? 0.2586 0.2730 0.3038 -0.0042 -0.0219 -0.0084 144 LEU A CB  
2219 C CG  . LEU A 159 ? 0.2664 0.2871 0.3106 -0.0066 -0.0225 -0.0110 144 LEU A CG  
2220 C CD1 . LEU A 159 ? 0.3028 0.3282 0.3527 -0.0054 -0.0216 -0.0143 144 LEU A CD1 
2221 C CD2 . LEU A 159 ? 0.2608 0.2821 0.3018 -0.0068 -0.0249 -0.0091 144 LEU A CD2 
2233 N N   . ILE A 160 ? 0.2943 0.2988 0.3359 0.0027  -0.0202 0.0027  145 ILE A N   
2234 C CA  . ILE A 160 ? 0.2891 0.2897 0.3337 0.0061  -0.0177 0.0086  145 ILE A CA  
2235 C C   . ILE A 160 ? 0.2859 0.2865 0.3363 0.0095  -0.0178 0.0099  145 ILE A C   
2236 O O   . ILE A 160 ? 0.2857 0.2899 0.3327 0.0117  -0.0203 0.0092  145 ILE A O   
2237 C CB  . ILE A 160 ? 0.2362 0.2362 0.2714 0.0096  -0.0171 0.0135  145 ILE A CB  
2238 C CG1 . ILE A 160 ? 0.2291 0.2289 0.2591 0.0068  -0.0170 0.0117  145 ILE A CG1 
2239 C CG2 . ILE A 160 ? 0.2597 0.2569 0.2983 0.0135  -0.0132 0.0214  145 ILE A CG2 
2240 C CD1 . ILE A 160 ? 0.2829 0.2814 0.3200 0.0036  -0.0146 0.0128  145 ILE A CD1 
2252 N N   . ASN A 161 ? 0.2954 0.2920 0.3562 0.0101  -0.0152 0.0122  146 ASN A N   
2253 C CA  . ASN A 161 ? 0.3115 0.3070 0.3794 0.0142  -0.0146 0.0148  146 ASN A CA  
2254 C C   . ASN A 161 ? 0.3113 0.3051 0.3781 0.0194  -0.0123 0.0250  146 ASN A C   
2255 O O   . ASN A 161 ? 0.3056 0.2991 0.3663 0.0198  -0.0106 0.0294  146 ASN A O   
2256 C CB  . ASN A 161 ? 0.2858 0.2771 0.3673 0.0123  -0.0132 0.0106  146 ASN A CB  
2257 C CG  . ASN A 161 ? 0.3018 0.2872 0.3927 0.0103  -0.0106 0.0135  146 ASN A CG  
2258 O OD1 . ASN A 161 ? 0.3277 0.3123 0.4169 0.0115  -0.0085 0.0212  146 ASN A OD1 
2259 N ND2 . ASN A 161 ? 0.2956 0.2773 0.3975 0.0074  -0.0106 0.0071  146 ASN A ND2 
2266 N N   . ASP A 162 ? 0.3194 0.3130 0.3919 0.0241  -0.0120 0.0295  147 ASP A N   
2267 C CA  . ASP A 162 ? 0.3857 0.3797 0.4552 0.0303  -0.0099 0.0404  147 ASP A CA  
2268 C C   . ASP A 162 ? 0.3709 0.3593 0.4497 0.0302  -0.0045 0.0480  147 ASP A C   
2269 O O   . ASP A 162 ? 0.3500 0.3397 0.4247 0.0352  -0.0015 0.0582  147 ASP A O   
2270 C CB  . ASP A 162 ? 0.3802 0.3762 0.4544 0.0357  -0.0111 0.0442  147 ASP A CB  
2271 C CG  . ASP A 162 ? 0.4498 0.4533 0.5156 0.0363  -0.0167 0.0384  147 ASP A CG  
2272 O OD1 . ASP A 162 ? 0.4943 0.5019 0.5461 0.0364  -0.0196 0.0370  147 ASP A OD1 
2273 O OD2 . ASP A 162 ? 0.5456 0.5507 0.6197 0.0366  -0.0182 0.0348  147 ASP A OD2 
2278 N N   . ALA A 163 ? 0.2815 0.2649 0.3728 0.0246  -0.0033 0.0432  148 ALA A N   
2279 C CA  . ALA A 163 ? 0.2611 0.2399 0.3636 0.0229  0.0010  0.0493  148 ALA A CA  
2280 C C   . ALA A 163 ? 0.2709 0.2523 0.3656 0.0201  0.0017  0.0490  148 ALA A C   
2281 O O   . ALA A 163 ? 0.2987 0.2779 0.4032 0.0186  0.0054  0.0546  148 ALA A O   
2282 C CB  . ALA A 163 ? 0.4179 0.3902 0.5386 0.0181  0.0008  0.0429  148 ALA A CB  
2288 N N   . GLY A 164 ? 0.3079 0.2938 0.3870 0.0194  -0.0015 0.0432  149 GLY A N   
2289 C CA  . GLY A 164 ? 0.3085 0.2965 0.3806 0.0173  -0.0007 0.0427  149 GLY A CA  
2290 C C   . GLY A 164 ? 0.3125 0.2998 0.3906 0.0103  -0.0028 0.0349  149 GLY A C   
2291 O O   . GLY A 164 ? 0.2397 0.2286 0.3160 0.0085  -0.0017 0.0359  149 GLY A O   
2295 N N   . GLU A 165 ? 0.2651 0.2509 0.3499 0.0069  -0.0056 0.0271  150 GLU A N   
2296 C CA  . GLU A 165 ? 0.2921 0.2785 0.3814 0.0009  -0.0082 0.0190  150 GLU A CA  
2297 C C   . GLU A 165 ? 0.2332 0.2243 0.3097 -0.0007 -0.0115 0.0122  150 GLU A C   
2298 O O   . GLU A 165 ? 0.2607 0.2537 0.3288 0.0019  -0.0126 0.0113  150 GLU A O   
2299 C CB  . GLU A 165 ? 0.2378 0.2202 0.3405 -0.0011 -0.0092 0.0135  150 GLU A CB  
2300 C CG  . GLU A 165 ? 0.3657 0.3425 0.4849 -0.0006 -0.0060 0.0202  150 GLU A CG  
2301 C CD  . GLU A 165 ? 0.3894 0.3603 0.5225 -0.0013 -0.0067 0.0150  150 GLU A CD  
2302 O OE1 . GLU A 165 ? 0.4144 0.3851 0.5433 0.0017  -0.0075 0.0115  150 GLU A OE1 
2303 O OE2 . GLU A 165 ? 0.5998 0.5661 0.7491 -0.0047 -0.0066 0.0140  150 GLU A OE2 
2310 N N   . VAL A 166 ? 0.2598 0.3659 0.4230 0.1063  0.0078  -0.0159 151 VAL A N   
2311 C CA  . VAL A 166 ? 0.1915 0.2923 0.3398 0.0936  -0.0030 -0.0123 151 VAL A CA  
2312 C C   . VAL A 166 ? 0.2413 0.3341 0.3734 0.0847  0.0094  -0.0133 151 VAL A C   
2313 O O   . VAL A 166 ? 0.2485 0.3283 0.3663 0.0830  0.0169  -0.0203 151 VAL A O   
2314 C CB  . VAL A 166 ? 0.2679 0.3510 0.3996 0.0900  -0.0219 -0.0152 151 VAL A CB  
2315 C CG1 . VAL A 166 ? 0.3410 0.4188 0.4586 0.0779  -0.0297 -0.0106 151 VAL A CG1 
2316 C CG2 . VAL A 166 ? 0.2994 0.3872 0.4467 0.0979  -0.0337 -0.0145 151 VAL A CG2 
2326 N N   . ARG A 167 ? 0.2336 0.3341 0.3669 0.0776  0.0112  -0.0070 152 ARG A N   
2327 C CA  . ARG A 167 ? 0.2383 0.3322 0.3591 0.0693  0.0236  -0.0069 152 ARG A CA  
2328 C C   . ARG A 167 ? 0.2477 0.3385 0.3571 0.0591  0.0141  -0.0033 152 ARG A C   
2329 O O   . ARG A 167 ? 0.2526 0.3569 0.3740 0.0588  0.0103  0.0027  152 ARG A O   
2330 C CB  . ARG A 167 ? 0.2722 0.3804 0.4114 0.0738  0.0436  -0.0015 152 ARG A CB  
2331 C CG  . ARG A 167 ? 0.3462 0.4610 0.5020 0.0856  0.0576  -0.0030 152 ARG A CG  
2332 C CD  . ARG A 167 ? 0.3152 0.4117 0.4556 0.0826  0.0721  -0.0119 152 ARG A CD  
2333 N NE  . ARG A 167 ? 0.3287 0.4308 0.4859 0.0943  0.0896  -0.0137 152 ARG A NE  
2334 C CZ  . ARG A 167 ? 0.2841 0.3807 0.4406 0.1015  0.0858  -0.0218 152 ARG A CZ  
2335 N NH1 . ARG A 167 ? 0.2486 0.3345 0.3890 0.0984  0.0639  -0.0277 152 ARG A NH1 
2336 N NH2 . ARG A 167 ? 0.3164 0.4165 0.4846 0.1100  0.1025  -0.0238 152 ARG A NH2 
2350 N N   . LEU A 168 ? 0.3188 0.3940 0.4056 0.0504  0.0125  -0.0066 153 LEU A N   
2351 C CA  . LEU A 168 ? 0.2827 0.3546 0.3591 0.0417  0.0069  -0.0030 153 LEU A CA  
2352 C C   . LEU A 168 ? 0.2817 0.3592 0.3636 0.0386  0.0199  0.0005  153 LEU A C   
2353 O O   . LEU A 168 ? 0.2885 0.3637 0.3711 0.0386  0.0352  -0.0011 153 LEU A O   
2354 C CB  . LEU A 168 ? 0.2912 0.3486 0.3433 0.0339  0.0027  -0.0060 153 LEU A CB  
2355 C CG  . LEU A 168 ? 0.2875 0.3386 0.3309 0.0356  -0.0104 -0.0072 153 LEU A CG  
2356 C CD1 . LEU A 168 ? 0.3269 0.3695 0.3468 0.0270  -0.0120 -0.0080 153 LEU A CD1 
2357 C CD2 . LEU A 168 ? 0.3407 0.3940 0.3917 0.0375  -0.0228 -0.0017 153 LEU A CD2 
2369 N N   . ALA A 169 ? 0.2804 0.3643 0.3659 0.0354  0.0151  0.0051  154 ALA A N   
2370 C CA  . ALA A 169 ? 0.2874 0.3751 0.3756 0.0316  0.0249  0.0089  154 ALA A CA  
2371 C C   . ALA A 169 ? 0.3435 0.4221 0.4168 0.0237  0.0179  0.0089  154 ALA A C   
2372 O O   . ALA A 169 ? 0.2998 0.3712 0.3628 0.0217  0.0071  0.0074  154 ALA A O   
2373 C CB  . ALA A 169 ? 0.2728 0.3831 0.3838 0.0364  0.0283  0.0154  154 ALA A CB  
2379 N N   . ASP A 170 ? 0.3968 0.4760 0.4700 0.0198  0.0254  0.0114  155 ASP A N   
2380 C CA  . ASP A 170 ? 0.3830 0.4542 0.4440 0.0134  0.0212  0.0112  155 ASP A CA  
2381 C C   . ASP A 170 ? 0.4212 0.5027 0.4920 0.0122  0.0269  0.0150  155 ASP A C   
2382 O O   . ASP A 170 ? 0.4147 0.5109 0.5014 0.0159  0.0338  0.0193  155 ASP A O   
2383 C CB  . ASP A 170 ? 0.4805 0.5349 0.5227 0.0080  0.0248  0.0082  155 ASP A CB  
2384 C CG  . ASP A 170 ? 0.4947 0.5446 0.5380 0.0061  0.0393  0.0083  155 ASP A CG  
2385 O OD1 . ASP A 170 ? 0.5883 0.6447 0.6440 0.0106  0.0481  0.0096  155 ASP A OD1 
2386 O OD2 . ASP A 170 ? 0.6801 0.7192 0.7123 0.0002  0.0433  0.0075  155 ASP A OD2 
2391 N N   . PHE A 171 ? 0.5619 0.6370 0.6235 0.0071  0.0248  0.0142  156 PHE A N   
2392 C CA  . PHE A 171 ? 0.3731 0.4566 0.4411 0.0049  0.0303  0.0168  156 PHE A CA  
2393 C C   . PHE A 171 ? 0.3974 0.4775 0.4679 0.0056  0.0422  0.0198  156 PHE A C   
2394 O O   . PHE A 171 ? 0.3605 0.4552 0.4441 0.0070  0.0487  0.0254  156 PHE A O   
2395 C CB  . PHE A 171 ? 0.3709 0.4443 0.4267 -0.0001 0.0278  0.0140  156 PHE A CB  
2396 C CG  . PHE A 171 ? 0.4311 0.5125 0.4916 -0.0029 0.0331  0.0151  156 PHE A CG  
2397 C CD1 . PHE A 171 ? 0.3607 0.4609 0.4312 -0.0053 0.0316  0.0157  156 PHE A CD1 
2398 C CD2 . PHE A 171 ? 0.4739 0.5445 0.5284 -0.0042 0.0401  0.0154  156 PHE A CD2 
2399 C CE1 . PHE A 171 ? 0.4222 0.5323 0.4960 -0.0091 0.0369  0.0164  156 PHE A CE1 
2400 C CE2 . PHE A 171 ? 0.5219 0.5997 0.5801 -0.0066 0.0448  0.0166  156 PHE A CE2 
2401 C CZ  . PHE A 171 ? 0.4124 0.5111 0.4801 -0.0091 0.0433  0.0170  156 PHE A CZ  
2411 N N   . GLY A 172 ? 0.4906 0.5526 0.5486 0.0037  0.0464  0.0171  157 GLY A N   
2412 C CA  . GLY A 172 ? 0.5041 0.5596 0.5644 0.0033  0.0603  0.0197  157 GLY A CA  
2413 C C   . GLY A 172 ? 0.5318 0.5720 0.5815 -0.0021 0.0654  0.0192  157 GLY A C   
2414 O O   . GLY A 172 ? 0.4995 0.5349 0.5403 -0.0047 0.0584  0.0165  157 GLY A O   
2418 N N   . ILE A 173 ? 0.5840 0.6155 0.6355 -0.0035 0.0796  0.0221  158 ILE A N   
2419 C CA  . ILE A 173 ? 0.5409 0.5545 0.5825 -0.0091 0.0862  0.0217  158 ILE A CA  
2420 C C   . ILE A 173 ? 0.4648 0.4843 0.5116 -0.0077 0.0843  0.0254  158 ILE A C   
2421 O O   . ILE A 173 ? 0.4141 0.4177 0.4519 -0.0115 0.0875  0.0242  158 ILE A O   
2422 C CB  . ILE A 173 ? 0.6227 0.6251 0.6675 -0.0114 0.1051  0.0254  158 ILE A CB  
2423 C CG1 . ILE A 173 ? 0.5088 0.5295 0.5762 -0.0040 0.1151  0.0360  158 ILE A CG1 
2424 C CG2 . ILE A 173 ? 0.6603 0.6531 0.6950 -0.0162 0.1094  0.0189  158 ILE A CG2 
2425 C CD1 . ILE A 173 ? 0.5102 0.5350 0.5859 -0.0027 0.1201  0.0446  158 ILE A CD1 
2437 N N   . SER A 174 ? 0.4890 0.5314 0.5499 -0.0032 0.0799  0.0297  159 SER A N   
2438 C CA  . SER A 174 ? 0.5080 0.5586 0.5724 -0.0037 0.0788  0.0322  159 SER A CA  
2439 C C   . SER A 174 ? 0.5119 0.5482 0.5604 -0.0074 0.0711  0.0241  159 SER A C   
2440 O O   . SER A 174 ? 0.5534 0.5853 0.5992 -0.0089 0.0735  0.0240  159 SER A O   
2441 C CB  . SER A 174 ? 0.6288 0.7098 0.7088 -0.0010 0.0742  0.0364  159 SER A CB  
2442 O OG  . SER A 174 ? 0.5415 0.6316 0.6219 -0.0038 0.0730  0.0368  159 SER A OG  
2448 N N   . ALA A 175 ? 0.4484 0.4779 0.4866 -0.0084 0.0630  0.0180  160 ALA A N   
2449 C CA  . ALA A 175 ? 0.5099 0.5269 0.5344 -0.0107 0.0583  0.0122  160 ALA A CA  
2450 C C   . ALA A 175 ? 0.4002 0.3951 0.4125 -0.0139 0.0635  0.0103  160 ALA A C   
2451 O O   . ALA A 175 ? 0.5052 0.4900 0.5079 -0.0149 0.0617  0.0066  160 ALA A O   
2452 C CB  . ALA A 175 ? 0.5263 0.5448 0.5449 -0.0104 0.0495  0.0092  160 ALA A CB  
2458 N N   . GLN A 176 ? 0.4039 0.3907 0.4165 -0.0158 0.0713  0.0127  161 GLN A N   
2459 C CA  . GLN A 176 ? 0.4342 0.3995 0.4351 -0.0211 0.0777  0.0106  161 GLN A CA  
2460 C C   . GLN A 176 ? 0.4166 0.3721 0.4221 -0.0215 0.0878  0.0148  161 GLN A C   
2461 O O   . GLN A 176 ? 0.4455 0.3807 0.4417 -0.0265 0.0939  0.0131  161 GLN A O   
2462 C CB  . GLN A 176 ? 0.5418 0.5013 0.5377 -0.0259 0.0831  0.0096  161 GLN A CB  
2463 C CG  . GLN A 176 ? 0.6805 0.6509 0.6729 -0.0253 0.0740  0.0069  161 GLN A CG  
2464 C CD  . GLN A 176 ? 0.6635 0.6296 0.6410 -0.0285 0.0658  0.0031  161 GLN A CD  
2465 O OE1 . GLN A 176 ? 0.7846 0.7424 0.7495 -0.0360 0.0685  0.0003  161 GLN A OE1 
2466 N NE2 . GLN A 176 ? 0.8250 0.7983 0.8041 -0.0237 0.0573  0.0035  161 GLN A NE2 
2475 N N   . ILE A 177 ? 0.4066 0.3771 0.4266 -0.0170 0.0903  0.0210  162 ILE A N   
2476 C CA  . ILE A 177 ? 0.4096 0.3734 0.4357 -0.0169 0.1011  0.0278  162 ILE A CA  
2477 C C   . ILE A 177 ? 0.3971 0.3844 0.4361 -0.0126 0.0988  0.0331  162 ILE A C   
2478 O O   . ILE A 177 ? 0.4924 0.5012 0.5370 -0.0107 0.0907  0.0316  162 ILE A O   
2479 C CB  . ILE A 177 ? 0.4140 0.3722 0.4473 -0.0183 0.1158  0.0349  162 ILE A CB  
2480 C CG1 . ILE A 177 ? 0.4391 0.3799 0.4741 -0.0201 0.1291  0.0418  162 ILE A CG1 
2481 C CG2 . ILE A 177 ? 0.4787 0.4639 0.5303 -0.0125 0.1182  0.0428  162 ILE A CG2 
2482 C CD1 . ILE A 177 ? 0.4725 0.3979 0.5098 -0.0243 0.1476  0.0469  162 ILE A CD1 
2494 N N   . GLY A 178 ? 0.3989 0.3831 0.4421 -0.0123 0.1061  0.0393  163 GLY A N   
2495 C CA  . GLY A 178 ? 0.3977 0.4085 0.4534 -0.0098 0.1057  0.0459  163 GLY A CA  
2496 C C   . GLY A 178 ? 0.4825 0.4991 0.5308 -0.0113 0.0963  0.0368  163 GLY A C   
2497 O O   . GLY A 178 ? 0.3930 0.3889 0.4270 -0.0126 0.0923  0.0270  163 GLY A O   
2501 N N   . ALA A 179 ? 0.4487 0.4960 0.5076 -0.0116 0.0946  0.0405  164 ALA A N   
2502 C CA  . ALA A 179 ? 0.4950 0.5501 0.5477 -0.0148 0.0895  0.0318  164 ALA A CA  
2503 C C   . ALA A 179 ? 0.3970 0.4476 0.4414 -0.0159 0.0815  0.0207  164 ALA A C   
2504 O O   . ALA A 179 ? 0.4033 0.4459 0.4380 -0.0179 0.0803  0.0115  164 ALA A O   
2505 C CB  . ALA A 179 ? 0.5126 0.6055 0.5785 -0.0175 0.0908  0.0385  164 ALA A CB  
2511 N N   . GLU A 180 ? 0.3678 0.4231 0.4163 -0.0144 0.0775  0.0222  165 GLU A N   
2512 C CA  . GLU A 180 ? 0.3829 0.4334 0.4238 -0.0151 0.0705  0.0139  165 GLU A CA  
2513 C C   . GLU A 180 ? 0.3963 0.4174 0.4219 -0.0142 0.0700  0.0078  165 GLU A C   
2514 O O   . GLU A 180 ? 0.3994 0.4145 0.4171 -0.0149 0.0685  0.0010  165 GLU A O   
2515 C CB  . GLU A 180 ? 0.4209 0.4820 0.4694 -0.0132 0.0661  0.0174  165 GLU A CB  
2516 C CG  . GLU A 180 ? 0.5178 0.5772 0.5606 -0.0140 0.0589  0.0112  165 GLU A CG  
2517 C CD  . GLU A 180 ? 0.6358 0.7115 0.6813 -0.0185 0.0580  0.0071  165 GLU A CD  
2518 O OE1 . GLU A 180 ? 0.5005 0.5918 0.5515 -0.0219 0.0623  0.0081  165 GLU A OE1 
2519 O OE2 . GLU A 180 ? 0.5623 0.6357 0.6043 -0.0195 0.0542  0.0033  165 GLU A OE2 
2526 N N   . LEU A 181 ? 0.4070 0.4107 0.4289 -0.0132 0.0730  0.0107  166 LEU A N   
2527 C CA  . LEU A 181 ? 0.4000 0.3786 0.4077 -0.0136 0.0730  0.0056  166 LEU A CA  
2528 C C   . LEU A 181 ? 0.4041 0.3732 0.4057 -0.0132 0.0756  0.0006  166 LEU A C   
2529 O O   . LEU A 181 ? 0.4093 0.3677 0.4016 -0.0123 0.0740  -0.0052 166 LEU A O   
2530 C CB  . LEU A 181 ? 0.4084 0.3703 0.4135 -0.0153 0.0787  0.0093  166 LEU A CB  
2531 C CG  . LEU A 181 ? 0.4384 0.3756 0.4291 -0.0176 0.0797  0.0045  166 LEU A CG  
2532 C CD1 . LEU A 181 ? 0.4239 0.3614 0.4057 -0.0186 0.0731  0.0007  166 LEU A CD1 
2533 C CD2 . LEU A 181 ? 0.4317 0.3511 0.4207 -0.0215 0.0886  0.0081  166 LEU A CD2 
2545 N N   . ALA A 182 ? 0.4017 0.3754 0.4091 -0.0134 0.0804  0.0034  167 ALA A N   
2546 C CA  . ALA A 182 ? 0.4055 0.3696 0.4068 -0.0129 0.0836  -0.0023 167 ALA A CA  
2547 C C   . ALA A 182 ? 0.4172 0.3924 0.4166 -0.0136 0.0825  -0.0098 167 ALA A C   
2548 O O   . ALA A 182 ? 0.4672 0.4285 0.4581 -0.0119 0.0851  -0.0169 167 ALA A O   
2549 C CB  . ALA A 182 ? 0.4041 0.3752 0.4125 -0.0136 0.0889  0.0037  167 ALA A CB  
2555 N N   . ARG A 183 ? 0.3930 0.3925 0.4008 -0.0163 0.0801  -0.0082 168 ARG A N   
2556 C CA  . ARG A 183 ? 0.4026 0.4112 0.4087 -0.0189 0.0817  -0.0152 168 ARG A CA  
2557 C C   . ARG A 183 ? 0.4451 0.4396 0.4439 -0.0159 0.0799  -0.0181 168 ARG A C   
2558 O O   . ARG A 183 ? 0.4208 0.4095 0.4144 -0.0156 0.0857  -0.0242 168 ARG A O   
2559 C CB  . ARG A 183 ? 0.4539 0.4914 0.4709 -0.0238 0.0797  -0.0124 168 ARG A CB  
2560 C CG  . ARG A 183 ? 0.4554 0.5145 0.4798 -0.0281 0.0832  -0.0094 168 ARG A CG  
2561 C CD  . ARG A 183 ? 0.5914 0.6784 0.6220 -0.0360 0.0842  -0.0122 168 ARG A CD  
2562 N NE  . ARG A 183 ? 0.5607 0.6567 0.5983 -0.0352 0.0775  -0.0080 168 ARG A NE  
2563 C CZ  . ARG A 183 ? 0.4821 0.5900 0.5218 -0.0407 0.0771  -0.0119 168 ARG A CZ  
2564 N NH1 . ARG A 183 ? 0.4982 0.6106 0.5333 -0.0486 0.0849  -0.0205 168 ARG A NH1 
2565 N NH2 . ARG A 183 ? 0.3812 0.4951 0.4276 -0.0387 0.0701  -0.0075 168 ARG A NH2 
2579 N N   . ARG A 184 ? 0.3966 0.3869 0.3951 -0.0138 0.0737  -0.0130 169 ARG A N   
2580 C CA  . ARG A 184 ? 0.4013 0.3824 0.3930 -0.0114 0.0716  -0.0134 169 ARG A CA  
2581 C C   . ARG A 184 ? 0.5055 0.4669 0.4875 -0.0081 0.0756  -0.0165 169 ARG A C   
2582 O O   . ARG A 184 ? 0.4336 0.3911 0.4117 -0.0056 0.0796  -0.0183 169 ARG A O   
2583 C CB  . ARG A 184 ? 0.5027 0.4856 0.4951 -0.0112 0.0643  -0.0079 169 ARG A CB  
2584 C CG  . ARG A 184 ? 0.5256 0.5275 0.5289 -0.0129 0.0605  -0.0047 169 ARG A CG  
2585 C CD  . ARG A 184 ? 0.4739 0.4784 0.4770 -0.0120 0.0539  -0.0012 169 ARG A CD  
2586 N NE  . ARG A 184 ? 0.6226 0.6455 0.6371 -0.0128 0.0507  0.0010  169 ARG A NE  
2587 C CZ  . ARG A 184 ? 0.5643 0.5932 0.5808 -0.0122 0.0451  0.0024  169 ARG A CZ  
2588 N NH1 . ARG A 184 ? 0.5408 0.5603 0.5485 -0.0109 0.0423  0.0032  169 ARG A NH1 
2589 N NH2 . ARG A 184 ? 0.5134 0.5594 0.5412 -0.0130 0.0425  0.0040  169 ARG A NH2 
2603 N N   . LEU A 185 ? 0.4814 0.4301 0.4604 -0.0079 0.0762  -0.0163 170 LEU A N   
2604 C CA  . LEU A 185 ? 0.4689 0.3985 0.4390 -0.0051 0.0793  -0.0192 170 LEU A CA  
2605 C C   . LEU A 185 ? 0.5146 0.4404 0.4836 -0.0022 0.0872  -0.0259 170 LEU A C   
2606 O O   . LEU A 185 ? 0.5271 0.4435 0.4908 0.0021  0.0914  -0.0282 170 LEU A O   
2607 C CB  . LEU A 185 ? 0.4782 0.3930 0.4457 -0.0068 0.0793  -0.0177 170 LEU A CB  
2608 C CG  . LEU A 185 ? 0.4808 0.3961 0.4479 -0.0108 0.0753  -0.0123 170 LEU A CG  
2609 C CD1 . LEU A 185 ? 0.5360 0.4362 0.5026 -0.0136 0.0795  -0.0103 170 LEU A CD1 
2610 C CD2 . LEU A 185 ? 0.5103 0.4228 0.4689 -0.0116 0.0721  -0.0119 170 LEU A CD2 
2622 N N   . GLU A 186 ? 0.5633 0.4982 0.5373 -0.0047 0.0906  -0.0289 171 GLU A N   
2623 C CA  . GLU A 186 ? 0.5835 0.5171 0.5557 -0.0037 0.1002  -0.0369 171 GLU A CA  
2624 C C   . GLU A 186 ? 0.6060 0.5453 0.5786 -0.0027 0.1056  -0.0384 171 GLU A C   
2625 O O   . GLU A 186 ? 0.6142 0.5444 0.5832 0.0011  0.1157  -0.0435 171 GLU A O   
2626 C CB  . GLU A 186 ? 0.6063 0.5552 0.5837 -0.0093 0.1028  -0.0391 171 GLU A CB  
2627 C CG  . GLU A 186 ? 0.7262 0.6739 0.7001 -0.0102 0.1146  -0.0493 171 GLU A CG  
2628 C CD  . GLU A 186 ? 0.8351 0.8064 0.8138 -0.0189 0.1179  -0.0517 171 GLU A CD  
2629 O OE1 . GLU A 186 ? 0.7281 0.7202 0.7134 -0.0246 0.1149  -0.0483 171 GLU A OE1 
2630 O OE2 . GLU A 186 ? 0.8989 0.8692 0.8747 -0.0205 0.1235  -0.0568 171 GLU A OE2 
2637 N N   . PHE A 187 ? 0.4781 0.4313 0.4554 -0.0056 0.1004  -0.0332 172 PHE A N   
2638 C CA  . PHE A 187 ? 0.5422 0.5005 0.5209 -0.0056 0.1070  -0.0331 172 PHE A CA  
2639 C C   . PHE A 187 ? 0.6169 0.5641 0.5911 0.0015  0.1091  -0.0287 172 PHE A C   
2640 O O   . PHE A 187 ? 0.5382 0.4827 0.5125 0.0045  0.1212  -0.0297 172 PHE A O   
2641 C CB  . PHE A 187 ? 0.5462 0.5205 0.5312 -0.0102 0.1001  -0.0282 172 PHE A CB  
2642 C CG  . PHE A 187 ? 0.4767 0.4534 0.4632 -0.0104 0.1073  -0.0264 172 PHE A CG  
2643 C CD1 . PHE A 187 ? 0.5199 0.5001 0.5082 -0.0153 0.1212  -0.0329 172 PHE A CD1 
2644 C CD2 . PHE A 187 ? 0.5782 0.5537 0.5641 -0.0066 0.1019  -0.0178 172 PHE A CD2 
2645 C CE1 . PHE A 187 ? 0.6205 0.6005 0.6109 -0.0162 0.1310  -0.0302 172 PHE A CE1 
2646 C CE2 . PHE A 187 ? 0.5787 0.5556 0.5669 -0.0064 0.1100  -0.0139 172 PHE A CE2 
2647 C CZ  . PHE A 187 ? 0.5721 0.5498 0.5629 -0.0110 0.1252  -0.0198 172 PHE A CZ  
2657 N N   . ILE A 188 ? 0.4695 0.4121 0.4402 0.0036  0.0990  -0.0230 173 ILE A N   
2658 C CA  . ILE A 188 ? 0.4864 0.4241 0.4529 0.0091  0.1002  -0.0174 173 ILE A CA  
2659 C C   . ILE A 188 ? 0.5056 0.4290 0.4676 0.0144  0.1071  -0.0215 173 ILE A C   
2660 O O   . ILE A 188 ? 0.5303 0.4521 0.4897 0.0194  0.1092  -0.0162 173 ILE A O   
2661 C CB  . ILE A 188 ? 0.4617 0.4032 0.4250 0.0069  0.0878  -0.0103 173 ILE A CB  
2662 C CG1 . ILE A 188 ? 0.5374 0.4683 0.4964 0.0041  0.0825  -0.0133 173 ILE A CG1 
2663 C CG2 . ILE A 188 ? 0.5594 0.5140 0.5277 0.0027  0.0809  -0.0070 173 ILE A CG2 
2664 C CD1 . ILE A 188 ? 0.6463 0.5804 0.6013 -0.0005 0.0733  -0.0081 173 ILE A CD1 
2676 N N   . GLY A 189 ? 0.5556 0.4700 0.5170 0.0138  0.1108  -0.0300 174 GLY A N   
2677 C CA  . GLY A 189 ? 0.5984 0.4969 0.5555 0.0194  0.1171  -0.0350 174 GLY A CA  
2678 C C   . GLY A 189 ? 0.6944 0.5807 0.6461 0.0186  0.1083  -0.0338 174 GLY A C   
2679 O O   . GLY A 189 ? 0.6188 0.4922 0.5666 0.0237  0.1119  -0.0358 174 GLY A O   
2683 N N   . THR A 190 ? 0.5217 0.4108 0.4734 0.0121  0.0984  -0.0307 175 THR A N   
2684 C CA  . THR A 190 ? 0.4469 0.3248 0.3933 0.0088  0.0920  -0.0284 175 THR A CA  
2685 C C   . THR A 190 ? 0.5213 0.4041 0.4632 0.0091  0.0893  -0.0226 175 THR A C   
2686 O O   . THR A 190 ? 0.4604 0.3541 0.4044 0.0138  0.0930  -0.0193 175 THR A O   
2687 C CB  . THR A 190 ? 0.5765 0.4333 0.5193 0.0108  0.0956  -0.0341 175 THR A CB  
2688 O OG1 . THR A 190 ? 0.6438 0.4919 0.5829 0.0174  0.1008  -0.0366 175 THR A OG1 
2689 C CG2 . THR A 190 ? 0.6421 0.4989 0.5891 0.0115  0.1003  -0.0395 175 THR A CG2 
2697 N N   . PRO A 191 ? 0.4854 0.3626 0.4214 0.0031  0.0840  -0.0201 176 PRO A N   
2698 C CA  . PRO A 191 ? 0.4856 0.3720 0.4163 0.0012  0.0813  -0.0143 176 PRO A CA  
2699 C C   . PRO A 191 ? 0.4817 0.3572 0.4068 0.0029  0.0842  -0.0156 176 PRO A C   
2700 O O   . PRO A 191 ? 0.4958 0.3832 0.4167 0.0007  0.0823  -0.0098 176 PRO A O   
2701 C CB  . PRO A 191 ? 0.5174 0.4064 0.4443 -0.0093 0.0751  -0.0121 176 PRO A CB  
2702 C CG  . PRO A 191 ? 0.5148 0.3854 0.4428 -0.0122 0.0772  -0.0169 176 PRO A CG  
2703 C CD  . PRO A 191 ? 0.5036 0.3717 0.4387 -0.0043 0.0811  -0.0208 176 PRO A CD  
2711 N N   . TYR A 192 ? 0.5223 0.3776 0.4473 0.0065  0.0885  -0.0225 177 TYR A N   
2712 C CA  . TYR A 192 ? 0.4770 0.3184 0.3961 0.0063  0.0899  -0.0245 177 TYR A CA  
2713 C C   . TYR A 192 ? 0.4732 0.3269 0.3939 0.0147  0.0943  -0.0204 177 TYR A C   
2714 O O   . TYR A 192 ? 0.4780 0.3350 0.3938 0.0115  0.0929  -0.0171 177 TYR A O   
2715 C CB  . TYR A 192 ? 0.4743 0.2897 0.3933 0.0092  0.0935  -0.0325 177 TYR A CB  
2716 C CG  . TYR A 192 ? 0.4758 0.2811 0.3945 0.0009  0.0909  -0.0331 177 TYR A CG  
2717 C CD1 . TYR A 192 ? 0.4836 0.2800 0.3963 -0.0104 0.0889  -0.0311 177 TYR A CD1 
2718 C CD2 . TYR A 192 ? 0.4799 0.2875 0.4050 0.0033  0.0922  -0.0346 177 TYR A CD2 
2719 C CE1 . TYR A 192 ? 0.4978 0.2855 0.4120 -0.0171 0.0898  -0.0298 177 TYR A CE1 
2720 C CE2 . TYR A 192 ? 0.5025 0.3050 0.4296 -0.0032 0.0913  -0.0324 177 TYR A CE2 
2721 C CZ  . TYR A 192 ? 0.5375 0.3290 0.4597 -0.0126 0.0909  -0.0295 177 TYR A CZ  
2722 O OH  . TYR A 192 ? 0.5420 0.3282 0.4679 -0.0182 0.0934  -0.0257 177 TYR A OH  
2732 N N   . TRP A 193 ? 0.4675 0.3299 0.3955 0.0247  0.1013  -0.0197 178 TRP A N   
2733 C CA  . TRP A 193 ? 0.4666 0.3423 0.3986 0.0342  0.1091  -0.0135 178 TRP A CA  
2734 C C   . TRP A 193 ? 0.5121 0.4151 0.4465 0.0326  0.1071  -0.0013 178 TRP A C   
2735 O O   . TRP A 193 ? 0.4642 0.3816 0.4043 0.0412  0.1158  0.0070  178 TRP A O   
2736 C CB  . TRP A 193 ? 0.4626 0.3310 0.4016 0.0458  0.1223  -0.0192 178 TRP A CB  
2737 C CG  . TRP A 193 ? 0.4632 0.3061 0.4000 0.0495  0.1258  -0.0308 178 TRP A CG  
2738 C CD1 . TRP A 193 ? 0.4639 0.2965 0.4014 0.0587  0.1336  -0.0339 178 TRP A CD1 
2739 C CD2 . TRP A 193 ? 0.4827 0.3082 0.4168 0.0446  0.1222  -0.0400 178 TRP A CD2 
2740 N NE1 . TRP A 193 ? 0.4641 0.2715 0.3985 0.0597  0.1343  -0.0455 178 TRP A NE1 
2741 C CE2 . TRP A 193 ? 0.5290 0.3326 0.4612 0.0509  0.1275  -0.0486 178 TRP A CE2 
2742 C CE3 . TRP A 193 ? 0.4988 0.3267 0.4326 0.0360  0.1154  -0.0406 178 TRP A CE3 
2743 C CZ2 . TRP A 193 ? 0.5417 0.3258 0.4711 0.0483  0.1260  -0.0569 178 TRP A CZ2 
2744 C CZ3 . TRP A 193 ? 0.5438 0.3549 0.4761 0.0338  0.1147  -0.0479 178 TRP A CZ3 
2745 C CH2 . TRP A 193 ? 0.4770 0.2666 0.4068 0.0396  0.1198  -0.0556 178 TRP A CH2 
2756 N N   . MET A 194 ? 0.4704 0.3804 0.4011 0.0223  0.0973  0.0008  179 MET A N   
2757 C CA  . MET A 194 ? 0.5040 0.4373 0.4369 0.0207  0.0947  0.0112  179 MET A CA  
2758 C C   . MET A 194 ? 0.4689 0.4219 0.3964 0.0157  0.0903  0.0214  179 MET A C   
2759 O O   . MET A 194 ? 0.4876 0.4361 0.4066 0.0060  0.0845  0.0182  179 MET A O   
2760 C CB  . MET A 194 ? 0.5176 0.4490 0.4493 0.0126  0.0866  0.0077  179 MET A CB  
2761 C CG  . MET A 194 ? 0.4924 0.4411 0.4285 0.0133  0.0853  0.0153  179 MET A CG  
2762 S SD  . MET A 194 ? 0.5574 0.5027 0.4939 0.0053  0.0766  0.0098  179 MET A SD  
2763 C CE  . MET A 194 ? 0.5381 0.4704 0.4826 0.0109  0.0843  0.0007  179 MET A CE  
2773 N N   . ALA A 195 ? 0.4671 0.4431 0.3994 0.0213  0.0945  0.0344  180 ALA A N   
2774 C CA  . ALA A 195 ? 0.4708 0.4723 0.3983 0.0157  0.0902  0.0463  180 ALA A CA  
2775 C C   . ALA A 195 ? 0.5015 0.5118 0.4208 0.0023  0.0787  0.0467  180 ALA A C   
2776 O O   . ALA A 195 ? 0.4823 0.4848 0.4035 0.0013  0.0756  0.0424  180 ALA A O   
2777 C CB  . ALA A 195 ? 0.4679 0.4934 0.4044 0.0265  0.0996  0.0629  180 ALA A CB  
2783 N N   . PRO A 196 ? 0.4792 0.5073 0.3893 -0.0088 0.0732  0.0516  181 PRO A N   
2784 C CA  . PRO A 196 ? 0.4826 0.5177 0.3838 -0.0226 0.0642  0.0500  181 PRO A CA  
2785 C C   . PRO A 196 ? 0.5033 0.5514 0.4093 -0.0185 0.0619  0.0579  181 PRO A C   
2786 O O   . PRO A 196 ? 0.4847 0.5225 0.3895 -0.0228 0.0570  0.0509  181 PRO A O   
2787 C CB  . PRO A 196 ? 0.4904 0.5494 0.3814 -0.0348 0.0617  0.0563  181 PRO A CB  
2788 C CG  . PRO A 196 ? 0.5535 0.6046 0.4463 -0.0305 0.0673  0.0542  181 PRO A CG  
2789 C CD  . PRO A 196 ? 0.5264 0.5676 0.4331 -0.0111 0.0754  0.0566  181 PRO A CD  
2797 N N   . GLU A 197 ? 0.5361 0.6060 0.4487 -0.0096 0.0663  0.0733  182 GLU A N   
2798 C CA  . GLU A 197 ? 0.4690 0.5496 0.3858 -0.0063 0.0644  0.0820  182 GLU A CA  
2799 C C   . GLU A 197 ? 0.4796 0.5363 0.4044 0.0002  0.0665  0.0729  182 GLU A C   
2800 O O   . GLU A 197 ? 0.5166 0.5737 0.4419 -0.0019 0.0611  0.0728  182 GLU A O   
2801 C CB  . GLU A 197 ? 0.5039 0.6105 0.4282 0.0031  0.0721  0.1024  182 GLU A CB  
2802 C CG  . GLU A 197 ? 0.5568 0.6543 0.4938 0.0183  0.0869  0.1057  182 GLU A CG  
2803 C CD  . GLU A 197 ? 0.5015 0.6018 0.4383 0.0207  0.0923  0.1053  182 GLU A CD  
2804 O OE1 . GLU A 197 ? 0.5939 0.6904 0.5203 0.0096  0.0841  0.0956  182 GLU A OE1 
2805 O OE2 . GLU A 197 ? 0.4653 0.5712 0.4127 0.0335  0.1062  0.1149  182 GLU A OE2 
2812 N N   . VAL A 198 ? 0.4875 0.5245 0.4183 0.0076  0.0745  0.0648  183 VAL A N   
2813 C CA  . VAL A 198 ? 0.5110 0.5284 0.4481 0.0111  0.0766  0.0550  183 VAL A CA  
2814 C C   . VAL A 198 ? 0.4789 0.4838 0.4102 0.0014  0.0669  0.0428  183 VAL A C   
2815 O O   . VAL A 198 ? 0.5054 0.5066 0.4402 0.0005  0.0634  0.0395  183 VAL A O   
2816 C CB  . VAL A 198 ? 0.5334 0.5347 0.4769 0.0200  0.0885  0.0487  183 VAL A CB  
2817 C CG1 . VAL A 198 ? 0.5517 0.5378 0.5012 0.0217  0.0917  0.0393  183 VAL A CG1 
2818 C CG2 . VAL A 198 ? 0.5644 0.5786 0.5148 0.0303  0.1013  0.0618  183 VAL A CG2 
2828 N N   . ALA A 199 ? 0.5214 0.5200 0.4446 -0.0060 0.0638  0.0367  184 ALA A N   
2829 C CA  . ALA A 199 ? 0.5289 0.5155 0.4474 -0.0153 0.0581  0.0270  184 ALA A CA  
2830 C C   . ALA A 199 ? 0.4622 0.4624 0.3777 -0.0215 0.0510  0.0306  184 ALA A C   
2831 O O   . ALA A 199 ? 0.4852 0.4776 0.4030 -0.0240 0.0482  0.0246  184 ALA A O   
2832 C CB  . ALA A 199 ? 0.4721 0.4503 0.3816 -0.0240 0.0584  0.0218  184 ALA A CB  
2838 N N   . ALA A 200 ? 0.5270 0.5490 0.4379 -0.0236 0.0486  0.0412  185 ALA A N   
2839 C CA  . ALA A 200 ? 0.5167 0.5520 0.4239 -0.0292 0.0419  0.0447  185 ALA A CA  
2840 C C   . ALA A 200 ? 0.5337 0.5653 0.4509 -0.0212 0.0406  0.0458  185 ALA A C   
2841 O O   . ALA A 200 ? 0.5315 0.5601 0.4489 -0.0247 0.0357  0.0409  185 ALA A O   
2842 C CB  . ALA A 200 ? 0.4846 0.5471 0.3854 -0.0322 0.0401  0.0580  185 ALA A CB  
2848 N N   . VAL A 201 ? 0.5153 0.5466 0.4414 -0.0109 0.0464  0.0517  186 VAL A N   
2849 C CA  . VAL A 201 ? 0.5726 0.6000 0.5081 -0.0053 0.0467  0.0523  186 VAL A CA  
2850 C C   . VAL A 201 ? 0.5948 0.6053 0.5350 -0.0062 0.0462  0.0392  186 VAL A C   
2851 O O   . VAL A 201 ? 0.5637 0.5737 0.5081 -0.0071 0.0416  0.0367  186 VAL A O   
2852 C CB  . VAL A 201 ? 0.6113 0.6410 0.5549 0.0043  0.0572  0.0614  186 VAL A CB  
2853 C CG1 . VAL A 201 ? 0.6143 0.6389 0.5667 0.0076  0.0591  0.0615  186 VAL A CG1 
2854 C CG2 . VAL A 201 ? 0.6775 0.7281 0.6182 0.0060  0.0588  0.0778  186 VAL A CG2 
2864 N N   . ALA A 202 ? 0.5499 0.5478 0.4898 -0.0061 0.0509  0.0315  187 ALA A N   
2865 C CA  . ALA A 202 ? 0.5293 0.5144 0.4742 -0.0070 0.0512  0.0214  187 ALA A CA  
2866 C C   . ALA A 202 ? 0.5724 0.5577 0.5152 -0.0137 0.0447  0.0176  187 ALA A C   
2867 O O   . ALA A 202 ? 0.5493 0.5304 0.4990 -0.0135 0.0444  0.0128  187 ALA A O   
2868 C CB  . ALA A 202 ? 0.5450 0.5163 0.4885 -0.0063 0.0569  0.0150  187 ALA A CB  
2874 N N   . LEU A 203 ? 0.5439 0.5353 0.4773 -0.0201 0.0411  0.0200  188 LEU A N   
2875 C CA  . LEU A 203 ? 0.5833 0.5753 0.5144 -0.0266 0.0377  0.0164  188 LEU A CA  
2876 C C   . LEU A 203 ? 0.6054 0.6105 0.5374 -0.0256 0.0314  0.0214  188 LEU A C   
2877 O O   . LEU A 203 ? 0.5785 0.5865 0.5068 -0.0310 0.0290  0.0190  188 LEU A O   
2878 C CB  . LEU A 203 ? 0.5866 0.5764 0.5056 -0.0369 0.0399  0.0139  188 LEU A CB  
2879 C CG  . LEU A 203 ? 0.5937 0.5669 0.5111 -0.0394 0.0463  0.0085  188 LEU A CG  
2880 C CD1 . LEU A 203 ? 0.5447 0.5166 0.4491 -0.0519 0.0493  0.0063  188 LEU A CD1 
2881 C CD2 . LEU A 203 ? 0.5588 0.5185 0.4853 -0.0374 0.0502  0.0032  188 LEU A CD2 
2893 N N   . LYS A 204 ? 0.7231 0.7349 0.6601 -0.0188 0.0301  0.0284  189 LYS A N   
2894 C CA  . LYS A 204 ? 0.7494 0.7700 0.6897 -0.0163 0.0246  0.0336  189 LYS A CA  
2895 C C   . LYS A 204 ? 0.7696 0.8041 0.6994 -0.0208 0.0200  0.0408  189 LYS A C   
2896 O O   . LYS A 204 ? 0.8049 0.8445 0.7329 -0.0227 0.0143  0.0408  189 LYS A O   
2897 C CB  . LYS A 204 ? 0.7778 0.7943 0.7252 -0.0165 0.0215  0.0268  189 LYS A CB  
2898 C CG  . LYS A 204 ? 0.7544 0.7635 0.7132 -0.0127 0.0255  0.0218  189 LYS A CG  
2899 C CD  . LYS A 204 ? 0.7547 0.7648 0.7223 -0.0125 0.0231  0.0171  189 LYS A CD  
2900 C CE  . LYS A 204 ? 0.8440 0.8507 0.8075 -0.0173 0.0252  0.0126  189 LYS A CE  
2901 N NZ  . LYS A 204 ? 0.9785 0.9886 0.9523 -0.0156 0.0248  0.0100  189 LYS A NZ  
2915 N N   . GLY A 205 ? 0.5950 0.6378 0.5180 -0.0223 0.0227  0.0475  190 GLY A N   
2916 C CA  . GLY A 205 ? 0.4406 0.5027 0.3549 -0.0258 0.0191  0.0580  190 GLY A CA  
2917 C C   . GLY A 205 ? 0.6440 0.7149 0.5648 -0.0171 0.0209  0.0726  190 GLY A C   
2918 O O   . GLY A 205 ? 0.6341 0.6944 0.5657 -0.0094 0.0251  0.0729  190 GLY A O   
2922 N N   . GLY A 206 ? 0.7750 0.8670 0.6890 -0.0194 0.0192  0.0856  191 GLY A N   
2923 C CA  . GLY A 206 ? 0.6997 0.8024 0.6201 -0.0111 0.0235  0.1031  191 GLY A CA  
2924 C C   . GLY A 206 ? 0.7091 0.8143 0.6320 -0.0085 0.0181  0.1104  191 GLY A C   
2925 O O   . GLY A 206 ? 0.6146 0.7243 0.5448 -0.0011 0.0238  0.1256  191 GLY A O   
2929 N N   . TYR A 207 ? 0.6828 0.7841 0.6007 -0.0139 0.0090  0.1006  192 TYR A N   
2930 C CA  . TYR A 207 ? 0.6906 0.7927 0.6101 -0.0115 0.0026  0.1060  192 TYR A CA  
2931 C C   . TYR A 207 ? 0.6042 0.7071 0.5142 -0.0196 -0.0060 0.0938  192 TYR A C   
2932 O O   . TYR A 207 ? 0.6039 0.7027 0.5086 -0.0265 -0.0049 0.0808  192 TYR A O   
2933 C CB  . TYR A 207 ? 0.6054 0.6880 0.5388 -0.0037 0.0055  0.1035  192 TYR A CB  
2934 C CG  . TYR A 207 ? 0.6477 0.7132 0.5862 -0.0047 0.0057  0.0854  192 TYR A CG  
2935 C CD1 . TYR A 207 ? 0.5209 0.5804 0.4596 -0.0072 -0.0018 0.0741  192 TYR A CD1 
2936 C CD2 . TYR A 207 ? 0.5882 0.6450 0.5321 -0.0028 0.0143  0.0806  192 TYR A CD2 
2937 C CE1 . TYR A 207 ? 0.6067 0.6543 0.5517 -0.0075 -0.0003 0.0605  192 TYR A CE1 
2938 C CE2 . TYR A 207 ? 0.5959 0.6401 0.5447 -0.0039 0.0146  0.0661  192 TYR A CE2 
2939 C CZ  . TYR A 207 ? 0.4791 0.5200 0.4289 -0.0062 0.0074  0.0571  192 TYR A CZ  
2940 O OH  . TYR A 207 ? 0.6289 0.6609 0.5852 -0.0068 0.0090  0.0456  192 TYR A OH  
2950 N N   . ASN A 208 ? 0.4834 0.5904 0.3917 -0.0188 -0.0129 0.0983  193 ASN A N   
2951 C CA  . ASN A 208 ? 0.5281 0.6402 0.4255 -0.0267 -0.0193 0.0892  193 ASN A CA  
2952 C C   . ASN A 208 ? 0.4678 0.5633 0.3730 -0.0218 -0.0243 0.0797  193 ASN A C   
2953 O O   . ASN A 208 ? 0.4807 0.5618 0.3992 -0.0137 -0.0235 0.0796  193 ASN A O   
2954 C CB  . ASN A 208 ? 0.5700 0.7069 0.4554 -0.0315 -0.0235 0.1030  193 ASN A CB  
2955 C CG  . ASN A 208 ? 0.6215 0.7582 0.5131 -0.0228 -0.0280 0.1173  193 ASN A CG  
2956 O OD1 . ASN A 208 ? 0.7004 0.8176 0.6050 -0.0141 -0.0277 0.1161  193 ASN A OD1 
2957 N ND2 . ASN A 208 ? 0.6556 0.8150 0.5377 -0.0262 -0.0317 0.1314  193 ASN A ND2 
2964 N N   . GLU A 209 ? 0.4097 0.5087 0.3060 -0.0274 -0.0284 0.0714  194 GLU A N   
2965 C CA  . GLU A 209 ? 0.3995 0.4839 0.3034 -0.0232 -0.0315 0.0599  194 GLU A CA  
2966 C C   . GLU A 209 ? 0.3885 0.4674 0.3004 -0.0141 -0.0386 0.0681  194 GLU A C   
2967 O O   . GLU A 209 ? 0.3777 0.4437 0.3000 -0.0086 -0.0411 0.0601  194 GLU A O   
2968 C CB  . GLU A 209 ? 0.4082 0.4978 0.3000 -0.0320 -0.0308 0.0484  194 GLU A CB  
2969 C CG  . GLU A 209 ? 0.4346 0.5394 0.3134 -0.0359 -0.0370 0.0551  194 GLU A CG  
2970 C CD  . GLU A 209 ? 0.5459 0.6739 0.4091 -0.0471 -0.0351 0.0635  194 GLU A CD  
2971 O OE1 . GLU A 209 ? 0.6052 0.7367 0.4695 -0.0492 -0.0301 0.0675  194 GLU A OE1 
2972 O OE2 . GLU A 209 ? 0.7572 0.9016 0.6068 -0.0542 -0.0384 0.0660  194 GLU A OE2 
2979 N N   . LEU A 210 ? 0.3907 0.4796 0.2991 -0.0125 -0.0410 0.0850  195 LEU A N   
2980 C CA  . LEU A 210 ? 0.4024 0.4833 0.3186 -0.0044 -0.0464 0.0941  195 LEU A CA  
2981 C C   . LEU A 210 ? 0.3739 0.4378 0.3066 0.0025  -0.0422 0.0946  195 LEU A C   
2982 O O   . LEU A 210 ? 0.3653 0.4185 0.3061 0.0080  -0.0456 0.0990  195 LEU A O   
2983 C CB  . LEU A 210 ? 0.4145 0.5116 0.3231 -0.0047 -0.0478 0.1147  195 LEU A CB  
2984 C CG  . LEU A 210 ? 0.3918 0.5074 0.2835 -0.0123 -0.0537 0.1143  195 LEU A CG  
2985 C CD1 . LEU A 210 ? 0.4170 0.5553 0.3014 -0.0136 -0.0540 0.1371  195 LEU A CD1 
2986 C CD2 . LEU A 210 ? 0.3970 0.5011 0.2887 -0.0094 -0.0618 0.1046  195 LEU A CD2 
2998 N N   . CYS A 211 ? 0.3889 0.4498 0.3263 0.0013  -0.0345 0.0894  196 CYS A N   
2999 C CA  . CYS A 211 ? 0.3783 0.4248 0.3303 0.0056  -0.0296 0.0866  196 CYS A CA  
3000 C C   . CYS A 211 ? 0.3590 0.3956 0.3197 0.0076  -0.0350 0.0734  196 CYS A C   
3001 O O   . CYS A 211 ? 0.3510 0.3778 0.3234 0.0106  -0.0341 0.0736  196 CYS A O   
3002 C CB  . CYS A 211 ? 0.4281 0.4747 0.3819 0.0035  -0.0205 0.0822  196 CYS A CB  
3003 S SG  . CYS A 211 ? 0.5042 0.5496 0.4565 -0.0010 -0.0208 0.0634  196 CYS A SG  
3009 N N   . ASP A 212 ? 0.3579 0.3981 0.3138 0.0054  -0.0389 0.0623  197 ASP A N   
3010 C CA  . ASP A 212 ? 0.3460 0.3797 0.3115 0.0087  -0.0426 0.0512  197 ASP A CA  
3011 C C   . ASP A 212 ? 0.3363 0.3642 0.3053 0.0137  -0.0508 0.0558  197 ASP A C   
3012 O O   . ASP A 212 ? 0.3243 0.3455 0.3058 0.0176  -0.0534 0.0505  197 ASP A O   
3013 C CB  . ASP A 212 ? 0.3486 0.3869 0.3078 0.0055  -0.0415 0.0397  197 ASP A CB  
3014 C CG  . ASP A 212 ? 0.3563 0.3964 0.3149 0.0008  -0.0326 0.0335  197 ASP A CG  
3015 O OD1 . ASP A 212 ? 0.3548 0.3916 0.3223 0.0020  -0.0285 0.0340  197 ASP A OD1 
3016 O OD2 . ASP A 212 ? 0.3644 0.4084 0.3132 -0.0049 -0.0287 0.0275  197 ASP A OD2 
3021 N N   . ILE A 213 ? 0.3411 0.3729 0.2994 0.0133  -0.0549 0.0663  198 ILE A N   
3022 C CA  . ILE A 213 ? 0.3325 0.3569 0.2933 0.0182  -0.0628 0.0721  198 ILE A CA  
3023 C C   . ILE A 213 ? 0.3277 0.3404 0.3007 0.0209  -0.0599 0.0805  198 ILE A C   
3024 O O   . ILE A 213 ? 0.3163 0.3182 0.2993 0.0244  -0.0642 0.0772  198 ILE A O   
3025 C CB  . ILE A 213 ? 0.3399 0.3739 0.2855 0.0164  -0.0669 0.0834  198 ILE A CB  
3026 C CG1 . ILE A 213 ? 0.3449 0.3904 0.2776 0.0113  -0.0683 0.0723  198 ILE A CG1 
3027 C CG2 . ILE A 213 ? 0.3316 0.3561 0.2798 0.0219  -0.0746 0.0917  198 ILE A CG2 
3028 C CD1 . ILE A 213 ? 0.3776 0.4153 0.3154 0.0147  -0.0715 0.0566  198 ILE A CD1 
3040 N N   . TRP A 214 ? 0.3368 0.3513 0.3092 0.0188  -0.0511 0.0910  199 TRP A N   
3041 C CA  . TRP A 214 ? 0.3346 0.3371 0.3184 0.0194  -0.0438 0.0972  199 TRP A CA  
3042 C C   . TRP A 214 ? 0.3255 0.3228 0.3216 0.0181  -0.0428 0.0826  199 TRP A C   
3043 O O   . TRP A 214 ? 0.3171 0.3040 0.3231 0.0184  -0.0435 0.0820  199 TRP A O   
3044 C CB  . TRP A 214 ? 0.3467 0.3534 0.3284 0.0175  -0.0311 0.1084  199 TRP A CB  
3045 C CG  . TRP A 214 ? 0.3468 0.3408 0.3396 0.0165  -0.0191 0.1129  199 TRP A CG  
3046 C CD1 . TRP A 214 ? 0.3436 0.3327 0.3455 0.0129  -0.0130 0.1010  199 TRP A CD1 
3047 C CD2 . TRP A 214 ? 0.3514 0.3370 0.3472 0.0178  -0.0093 0.1307  199 TRP A CD2 
3048 N NE1 . TRP A 214 ? 0.3465 0.3242 0.3557 0.0106  0.0002  0.1085  199 TRP A NE1 
3049 C CE2 . TRP A 214 ? 0.3516 0.3253 0.3578 0.0139  0.0037  0.1271  199 TRP A CE2 
3050 C CE3 . TRP A 214 ? 0.3559 0.3440 0.3469 0.0213  -0.0087 0.1505  199 TRP A CE3 
3051 C CZ2 . TRP A 214 ? 0.3902 0.3516 0.4020 0.0132  0.0190  0.1416  199 TRP A CZ2 
3052 C CZ3 . TRP A 214 ? 0.3604 0.3370 0.3581 0.0221  0.0055  0.1669  199 TRP A CZ3 
3053 C CH2 . TRP A 214 ? 0.3691 0.3311 0.3772 0.0179  0.0202  0.1620  199 TRP A CH2 
3064 N N   . SER A 215 ? 0.3272 0.3328 0.3229 0.0161  -0.0408 0.0713  200 SER A N   
3065 C CA  . SER A 215 ? 0.3187 0.3243 0.3266 0.0147  -0.0392 0.0596  200 SER A CA  
3066 C C   . SER A 215 ? 0.3044 0.3080 0.3202 0.0184  -0.0485 0.0530  200 SER A C   
3067 O O   . SER A 215 ? 0.2949 0.2979 0.3234 0.0172  -0.0479 0.0482  200 SER A O   
3068 C CB  . SER A 215 ? 0.3232 0.3381 0.3289 0.0128  -0.0354 0.0507  200 SER A CB  
3069 O OG  . SER A 215 ? 0.3351 0.3510 0.3352 0.0098  -0.0265 0.0555  200 SER A OG  
3075 N N   . LEU A 216 ? 0.3024 0.3068 0.3113 0.0223  -0.0565 0.0524  201 LEU A N   
3076 C CA  . LEU A 216 ? 0.2881 0.2897 0.3051 0.0273  -0.0646 0.0460  201 LEU A CA  
3077 C C   . LEU A 216 ? 0.2813 0.2703 0.3046 0.0282  -0.0682 0.0532  201 LEU A C   
3078 O O   . LEU A 216 ? 0.2799 0.2668 0.3160 0.0295  -0.0713 0.0477  201 LEU A O   
3079 C CB  . LEU A 216 ? 0.2888 0.2930 0.2956 0.0308  -0.0703 0.0428  201 LEU A CB  
3080 C CG  . LEU A 216 ? 0.2791 0.2796 0.2940 0.0375  -0.0778 0.0358  201 LEU A CG  
3081 C CD1 . LEU A 216 ? 0.2768 0.2845 0.3083 0.0396  -0.0746 0.0262  201 LEU A CD1 
3082 C CD2 . LEU A 216 ? 0.3684 0.3714 0.3710 0.0396  -0.0806 0.0315  201 LEU A CD2 
3094 N N   . GLY A 217 ? 0.3201 0.3013 0.3353 0.0271  -0.0665 0.0664  202 GLY A N   
3095 C CA  . GLY A 217 ? 0.3455 0.3117 0.3666 0.0268  -0.0667 0.0750  202 GLY A CA  
3096 C C   . GLY A 217 ? 0.2829 0.2459 0.3166 0.0207  -0.0583 0.0714  202 GLY A C   
3097 O O   . GLY A 217 ? 0.2880 0.2423 0.3315 0.0197  -0.0610 0.0696  202 GLY A O   
3101 N N   . ILE A 218 ? 0.3040 0.2745 0.3372 0.0157  -0.0478 0.0699  203 ILE A N   
3102 C CA  . ILE A 218 ? 0.2899 0.2606 0.3336 0.0081  -0.0386 0.0648  203 ILE A CA  
3103 C C   . ILE A 218 ? 0.2754 0.2571 0.3304 0.0082  -0.0455 0.0518  203 ILE A C   
3104 O O   . ILE A 218 ? 0.2683 0.2499 0.3340 0.0022  -0.0430 0.0483  203 ILE A O   
3105 C CB  . ILE A 218 ? 0.3077 0.2850 0.3475 0.0037  -0.0261 0.0647  203 ILE A CB  
3106 C CG1 . ILE A 218 ? 0.3158 0.2853 0.3464 0.0049  -0.0176 0.0793  203 ILE A CG1 
3107 C CG2 . ILE A 218 ? 0.3009 0.2805 0.3503 -0.0056 -0.0157 0.0580  203 ILE A CG2 
3108 C CD1 . ILE A 218 ? 0.3479 0.3015 0.3826 0.0010  -0.0070 0.0897  203 ILE A CD1 
3120 N N   . THR A 219 ? 0.2713 0.2646 0.3248 0.0142  -0.0524 0.0452  204 THR A N   
3121 C CA  . THR A 219 ? 0.2572 0.2640 0.3235 0.0160  -0.0567 0.0352  204 THR A CA  
3122 C C   . THR A 219 ? 0.2430 0.2433 0.3177 0.0197  -0.0659 0.0344  204 THR A C   
3123 O O   . THR A 219 ? 0.2308 0.2408 0.3195 0.0175  -0.0669 0.0291  204 THR A O   
3124 C CB  . THR A 219 ? 0.2576 0.2753 0.3204 0.0220  -0.0586 0.0297  204 THR A CB  
3125 O OG1 . THR A 219 ? 0.2879 0.3102 0.3433 0.0180  -0.0503 0.0302  204 THR A OG1 
3126 C CG2 . THR A 219 ? 0.2430 0.2765 0.3213 0.0252  -0.0603 0.0220  204 THR A CG2 
3134 N N   . ALA A 220 ? 0.2440 0.2294 0.3105 0.0251  -0.0726 0.0401  205 ALA A N   
3135 C CA  . ALA A 220 ? 0.2751 0.2505 0.3487 0.0291  -0.0816 0.0400  205 ALA A CA  
3136 C C   . ALA A 220 ? 0.2479 0.2141 0.3297 0.0202  -0.0771 0.0433  205 ALA A C   
3137 O O   . ALA A 220 ? 0.2886 0.2558 0.3827 0.0198  -0.0820 0.0387  205 ALA A O   
3138 C CB  . ALA A 220 ? 0.2644 0.2251 0.3254 0.0356  -0.0886 0.0470  205 ALA A CB  
3144 N N   . ILE A 221 ? 0.2585 0.2163 0.3340 0.0123  -0.0660 0.0511  206 ILE A N   
3145 C CA  . ILE A 221 ? 0.2435 0.1930 0.3264 0.0011  -0.0571 0.0527  206 ILE A CA  
3146 C C   . ILE A 221 ? 0.2687 0.2396 0.3631 -0.0068 -0.0532 0.0418  206 ILE A C   
3147 O O   . ILE A 221 ? 0.2565 0.2290 0.3616 -0.0143 -0.0528 0.0381  206 ILE A O   
3148 C CB  . ILE A 221 ? 0.2613 0.1974 0.3355 -0.0050 -0.0423 0.0639  206 ILE A CB  
3149 C CG1 . ILE A 221 ? 0.2665 0.1845 0.3314 0.0025  -0.0461 0.0779  206 ILE A CG1 
3150 C CG2 . ILE A 221 ? 0.2646 0.1924 0.3462 -0.0190 -0.0285 0.0637  206 ILE A CG2 
3151 C CD1 . ILE A 221 ? 0.3094 0.2172 0.3669 -0.0009 -0.0300 0.0924  206 ILE A CD1 
3163 N N   . GLU A 222 ? 0.2403 0.2297 0.3327 -0.0053 -0.0507 0.0370  207 GLU A N   
3164 C CA  . GLU A 222 ? 0.2343 0.2476 0.3373 -0.0121 -0.0467 0.0286  207 GLU A CA  
3165 C C   . GLU A 222 ? 0.2363 0.2644 0.3538 -0.0078 -0.0570 0.0230  207 GLU A C   
3166 O O   . GLU A 222 ? 0.2068 0.2519 0.3361 -0.0168 -0.0543 0.0186  207 GLU A O   
3167 C CB  . GLU A 222 ? 0.2951 0.3222 0.3926 -0.0091 -0.0428 0.0263  207 GLU A CB  
3168 C CG  . GLU A 222 ? 0.2614 0.3162 0.3697 -0.0135 -0.0398 0.0194  207 GLU A CG  
3169 C CD  . GLU A 222 ? 0.2384 0.3046 0.3434 -0.0063 -0.0394 0.0179  207 GLU A CD  
3170 O OE1 . GLU A 222 ? 0.2474 0.3005 0.3404 0.0003  -0.0409 0.0207  207 GLU A OE1 
3171 O OE2 . GLU A 222 ? 0.2337 0.3231 0.3482 -0.0082 -0.0368 0.0145  207 GLU A OE2 
3178 N N   . LEU A 223 ? 0.2273 0.2517 0.3444 0.0056  -0.0678 0.0229  208 LEU A N   
3179 C CA  . LEU A 223 ? 0.1921 0.2305 0.3245 0.0119  -0.0762 0.0180  208 LEU A CA  
3180 C C   . LEU A 223 ? 0.2621 0.2882 0.4015 0.0077  -0.0811 0.0187  208 LEU A C   
3181 O O   . LEU A 223 ? 0.2427 0.2850 0.3977 0.0079  -0.0854 0.0146  208 LEU A O   
3182 C CB  . LEU A 223 ? 0.1979 0.2339 0.3273 0.0271  -0.0835 0.0165  208 LEU A CB  
3183 C CG  . LEU A 223 ? 0.2328 0.2800 0.3559 0.0309  -0.0777 0.0151  208 LEU A CG  
3184 C CD1 . LEU A 223 ? 0.2119 0.2555 0.3319 0.0436  -0.0824 0.0124  208 LEU A CD1 
3185 C CD2 . LEU A 223 ? 0.2220 0.2978 0.3587 0.0270  -0.0710 0.0124  208 LEU A CD2 
3197 N N   . ALA A 224 ? 0.2504 0.2489 0.3793 0.0038  -0.0796 0.0250  209 ALA A N   
3198 C CA  . ALA A 224 ? 0.2779 0.2590 0.4120 -0.0011 -0.0826 0.0270  209 ALA A CA  
3199 C C   . ALA A 224 ? 0.2186 0.2038 0.3580 -0.0198 -0.0709 0.0257  209 ALA A C   
3200 O O   . ALA A 224 ? 0.3678 0.3518 0.5175 -0.0264 -0.0734 0.0233  209 ALA A O   
3201 C CB  . ALA A 224 ? 0.2753 0.2242 0.3961 0.0034  -0.0843 0.0367  209 ALA A CB  
3207 N N   . GLU A 225 ? 0.2638 0.2544 0.3964 -0.0292 -0.0575 0.0264  210 GLU A N   
3208 C CA  . GLU A 225 ? 0.2251 0.2149 0.3593 -0.0486 -0.0426 0.0252  210 GLU A CA  
3209 C C   . GLU A 225 ? 0.2366 0.2581 0.3752 -0.0587 -0.0344 0.0179  210 GLU A C   
3210 O O   . GLU A 225 ? 0.2413 0.2660 0.3809 -0.0769 -0.0208 0.0148  210 GLU A O   
3211 C CB  . GLU A 225 ? 0.2679 0.2283 0.3890 -0.0526 -0.0293 0.0344  210 GLU A CB  
3212 C CG  . GLU A 225 ? 0.3411 0.2703 0.4585 -0.0444 -0.0359 0.0442  210 GLU A CG  
3213 C CD  . GLU A 225 ? 0.3660 0.2690 0.4726 -0.0470 -0.0210 0.0569  210 GLU A CD  
3214 O OE1 . GLU A 225 ? 0.3899 0.2970 0.4922 -0.0554 -0.0044 0.0571  210 GLU A OE1 
3215 O OE2 . GLU A 225 ? 0.4338 0.3126 0.5366 -0.0401 -0.0252 0.0677  210 GLU A OE2 
3222 N N   . LEU A 226 ? 0.2701 0.3149 0.3013 0.0142  -0.0407 -0.0578 211 LEU A N   
3223 C CA  . LEU A 226 ? 0.2703 0.3291 0.3125 0.0113  -0.0505 -0.0713 211 LEU A CA  
3224 C C   . LEU A 226 ? 0.3063 0.3706 0.3684 0.0014  -0.0434 -0.0780 211 LEU A C   
3225 O O   . LEU A 226 ? 0.2644 0.3418 0.3399 -0.0032 -0.0490 -0.0917 211 LEU A O   
3226 C CB  . LEU A 226 ? 0.2905 0.3484 0.3201 0.0132  -0.0587 -0.0834 211 LEU A CB  
3227 C CG  . LEU A 226 ? 0.3371 0.3854 0.3404 0.0231  -0.0650 -0.0774 211 LEU A CG  
3228 C CD1 . LEU A 226 ? 0.3617 0.4092 0.3499 0.0254  -0.0742 -0.0904 211 LEU A CD1 
3229 C CD2 . LEU A 226 ? 0.3960 0.4505 0.3996 0.0303  -0.0742 -0.0706 211 LEU A CD2 
3241 N N   . GLN A 227 ? 0.2588 0.3132 0.3231 -0.0019 -0.0311 -0.0692 212 GLN A N   
3242 C CA  . GLN A 227 ? 0.3226 0.3783 0.4017 -0.0110 -0.0227 -0.0729 212 GLN A CA  
3243 C C   . GLN A 227 ? 0.2683 0.3120 0.3433 -0.0094 -0.0126 -0.0583 212 GLN A C   
3244 O O   . GLN A 227 ? 0.2882 0.3223 0.3521 -0.0031 -0.0104 -0.0494 212 GLN A O   
3245 C CB  . GLN A 227 ? 0.3841 0.4340 0.4666 -0.0194 -0.0176 -0.0863 212 GLN A CB  
3246 C CG  . GLN A 227 ? 0.4051 0.4342 0.4735 -0.0182 -0.0089 -0.0827 212 GLN A CG  
3247 C CD  . GLN A 227 ? 0.5987 0.6195 0.6720 -0.0282 -0.0017 -0.0966 212 GLN A CD  
3248 O OE1 . GLN A 227 ? 0.6147 0.6489 0.6991 -0.0345 -0.0079 -0.1126 212 GLN A OE1 
3249 N NE2 . GLN A 227 ? 0.5789 0.5777 0.6455 -0.0296 0.0114  -0.0914 212 GLN A NE2 
3258 N N   . PRO A 228 ? 0.2743 0.3188 0.3576 -0.0144 -0.0064 -0.0558 213 PRO A N   
3259 C CA  . PRO A 228 ? 0.3613 0.3934 0.4380 -0.0116 0.0018  -0.0424 213 PRO A CA  
3260 C C   . PRO A 228 ? 0.2723 0.2837 0.3413 -0.0127 0.0120  -0.0413 213 PRO A C   
3261 O O   . PRO A 228 ? 0.2831 0.2897 0.3537 -0.0187 0.0147  -0.0525 213 PRO A O   
3262 C CB  . PRO A 228 ? 0.3172 0.3539 0.4014 -0.0177 0.0062  -0.0426 213 PRO A CB  
3263 C CG  . PRO A 228 ? 0.2517 0.2963 0.3482 -0.0272 0.0068  -0.0582 213 PRO A CG  
3264 C CD  . PRO A 228 ? 0.2753 0.3312 0.3736 -0.0232 -0.0054 -0.0664 213 PRO A CD  
3272 N N   . PRO A 229 ? 0.2735 0.2726 0.3347 -0.0064 0.0174  -0.0290 214 PRO A N   
3273 C CA  . PRO A 229 ? 0.3068 0.2834 0.3607 -0.0060 0.0279  -0.0273 214 PRO A CA  
3274 C C   . PRO A 229 ? 0.3113 0.2747 0.3666 -0.0169 0.0382  -0.0335 214 PRO A C   
3275 O O   . PRO A 229 ? 0.3091 0.2771 0.3681 -0.0224 0.0403  -0.0329 214 PRO A O   
3276 C CB  . PRO A 229 ? 0.3318 0.3020 0.3795 0.0043  0.0293  -0.0124 214 PRO A CB  
3277 C CG  . PRO A 229 ? 0.2933 0.2845 0.3459 0.0094  0.0186  -0.0086 214 PRO A CG  
3278 C CD  . PRO A 229 ? 0.2619 0.2679 0.3217 0.0016  0.0132  -0.0171 214 PRO A CD  
3286 N N   . LEU A 230 ? 0.3306 0.2766 0.3829 -0.0207 0.0462  -0.0401 215 LEU A N   
3287 C CA  . LEU A 230 ? 0.3530 0.2806 0.4059 -0.0320 0.0592  -0.0463 215 LEU A CA  
3288 C C   . LEU A 230 ? 0.3923 0.3370 0.4607 -0.0454 0.0576  -0.0623 215 LEU A C   
3289 O O   . LEU A 230 ? 0.3637 0.2971 0.4362 -0.0572 0.0696  -0.0682 215 LEU A O   
3290 C CB  . LEU A 230 ? 0.3675 0.2766 0.4102 -0.0302 0.0688  -0.0325 215 LEU A CB  
3291 C CG  . LEU A 230 ? 0.3779 0.2699 0.4066 -0.0155 0.0699  -0.0169 215 LEU A CG  
3292 C CD1 . LEU A 230 ? 0.3946 0.2703 0.4102 -0.0126 0.0765  -0.0034 215 LEU A CD1 
3293 C CD2 . LEU A 230 ? 0.4457 0.3143 0.4694 -0.0139 0.0781  -0.0203 215 LEU A CD2 
3305 N N   . PHE A 231 ? 0.3259 0.2970 0.4033 -0.0436 0.0435  -0.0696 216 PHE A N   
3306 C CA  . PHE A 231 ? 0.3481 0.3399 0.4433 -0.0538 0.0395  -0.0855 216 PHE A CA  
3307 C C   . PHE A 231 ? 0.3379 0.3234 0.4415 -0.0661 0.0463  -0.1031 216 PHE A C   
3308 O O   . PHE A 231 ? 0.3377 0.3376 0.4595 -0.0774 0.0475  -0.1175 216 PHE A O   
3309 C CB  . PHE A 231 ? 0.3476 0.3648 0.4471 -0.0464 0.0217  -0.0894 216 PHE A CB  
3310 C CG  . PHE A 231 ? 0.3846 0.4269 0.5036 -0.0523 0.0152  -0.1016 216 PHE A CG  
3311 C CD1 . PHE A 231 ? 0.3744 0.4233 0.5003 -0.0547 0.0192  -0.0966 216 PHE A CD1 
3312 C CD2 . PHE A 231 ? 0.4141 0.4742 0.5440 -0.0542 0.0042  -0.1187 216 PHE A CD2 
3313 C CE1 . PHE A 231 ? 0.3274 0.4006 0.4734 -0.0593 0.0140  -0.1089 216 PHE A CE1 
3314 C CE2 . PHE A 231 ? 0.3576 0.4431 0.5083 -0.0578 -0.0029 -0.1309 216 PHE A CE2 
3315 C CZ  . PHE A 231 ? 0.2976 0.3899 0.4576 -0.0605 0.0027  -0.1261 216 PHE A CZ  
3325 N N   . ASP A 232 ? 0.3693 0.3349 0.4620 -0.0644 0.0509  -0.1039 217 ASP A N   
3326 C CA  . ASP A 232 ? 0.3762 0.3325 0.4759 -0.0769 0.0586  -0.1214 217 ASP A CA  
3327 C C   . ASP A 232 ? 0.4183 0.3448 0.5153 -0.0865 0.0793  -0.1179 217 ASP A C   
3328 O O   . ASP A 232 ? 0.4671 0.3796 0.5686 -0.0977 0.0890  -0.1314 217 ASP A O   
3329 C CB  . ASP A 232 ? 0.4731 0.4207 0.5607 -0.0707 0.0542  -0.1257 217 ASP A CB  
3330 C CG  . ASP A 232 ? 0.4948 0.4209 0.5636 -0.0578 0.0591  -0.1069 217 ASP A CG  
3331 O OD1 . ASP A 232 ? 0.4355 0.3659 0.5003 -0.0491 0.0564  -0.0907 217 ASP A OD1 
3332 O OD2 . ASP A 232 ? 0.4515 0.3574 0.5107 -0.0561 0.0656  -0.1095 217 ASP A OD2 
3337 N N   . VAL A 233 ? 0.4240 0.3384 0.5114 -0.0820 0.0864  -0.1001 218 VAL A N   
3338 C CA  . VAL A 233 ? 0.4312 0.3126 0.5095 -0.0887 0.1062  -0.0931 218 VAL A CA  
3339 C C   . VAL A 233 ? 0.4599 0.3502 0.5497 -0.1013 0.1141  -0.0970 218 VAL A C   
3340 O O   . VAL A 233 ? 0.4068 0.3227 0.5031 -0.0975 0.1042  -0.0942 218 VAL A O   
3341 C CB  . VAL A 233 ? 0.4384 0.2971 0.4939 -0.0729 0.1084  -0.0698 218 VAL A CB  
3342 C CG1 . VAL A 233 ? 0.4756 0.2953 0.5168 -0.0780 0.1285  -0.0614 218 VAL A CG1 
3343 C CG2 . VAL A 233 ? 0.4469 0.3013 0.4948 -0.0603 0.1011  -0.0674 218 VAL A CG2 
3353 N N   . HIS A 234 ? 0.5030 0.3705 0.5949 -0.1165 0.1334  -0.1037 219 HIS A N   
3354 C CA  . HIS A 234 ? 0.4683 0.3435 0.5728 -0.1311 0.1444  -0.1100 219 HIS A CA  
3355 C C   . HIS A 234 ? 0.4572 0.3326 0.5465 -0.1216 0.1434  -0.0906 219 HIS A C   
3356 O O   . HIS A 234 ? 0.4705 0.3199 0.5338 -0.1094 0.1460  -0.0706 219 HIS A O   
3357 C CB  . HIS A 234 ? 0.5191 0.3595 0.6211 -0.1482 0.1696  -0.1153 219 HIS A CB  
3358 C CG  . HIS A 234 ? 0.5131 0.3638 0.6333 -0.1669 0.1835  -0.1270 219 HIS A CG  
3359 N ND1 . HIS A 234 ? 0.5392 0.3789 0.6455 -0.1677 0.1950  -0.1131 219 HIS A ND1 
3360 C CD2 . HIS A 234 ? 0.5466 0.4196 0.6990 -0.1855 0.1880  -0.1525 219 HIS A CD2 
3361 C CE1 . HIS A 234 ? 0.5876 0.4411 0.7165 -0.1866 0.2079  -0.1292 219 HIS A CE1 
3362 N NE2 . HIS A 234 ? 0.6265 0.5017 0.7857 -0.1978 0.2036  -0.1537 219 HIS A NE2 
3370 N N   . PRO A 235 ? 0.4377 0.3422 0.5427 -0.1263 0.1395  -0.0968 220 PRO A N   
3371 C CA  . PRO A 235 ? 0.4295 0.3362 0.5194 -0.1166 0.1368  -0.0798 220 PRO A CA  
3372 C C   . PRO A 235 ? 0.4660 0.3332 0.5277 -0.1177 0.1557  -0.0632 220 PRO A C   
3373 O O   . PRO A 235 ? 0.4983 0.3556 0.5368 -0.1033 0.1505  -0.0444 220 PRO A O   
3374 C CB  . PRO A 235 ? 0.4098 0.3515 0.5254 -0.1258 0.1343  -0.0944 220 PRO A CB  
3375 C CG  . PRO A 235 ? 0.4526 0.4026 0.5944 -0.1432 0.1424  -0.1173 220 PRO A CG  
3376 C CD  . PRO A 235 ? 0.4416 0.3790 0.5798 -0.1400 0.1371  -0.1206 220 PRO A CD  
3384 N N   . LEU A 236 ? 0.4994 0.3424 0.5614 -0.1344 0.1778  -0.0700 221 LEU A N   
3385 C CA  . LEU A 236 ? 0.5680 0.3672 0.5979 -0.1348 0.1971  -0.0529 221 LEU A CA  
3386 C C   . LEU A 236 ? 0.5945 0.3625 0.5979 -0.1178 0.1929  -0.0353 221 LEU A C   
3387 O O   . LEU A 236 ? 0.5967 0.3450 0.5711 -0.1040 0.1921  -0.0150 221 LEU A O   
3388 C CB  . LEU A 236 ? 0.6033 0.3807 0.6404 -0.1579 0.2235  -0.0652 221 LEU A CB  
3389 C CG  . LEU A 236 ? 0.6600 0.4049 0.6718 -0.1659 0.2474  -0.0537 221 LEU A CG  
3390 C CD1 . LEU A 236 ? 0.7002 0.4701 0.7089 -0.1612 0.2409  -0.0485 221 LEU A CD1 
3391 C CD2 . LEU A 236 ? 0.7365 0.4705 0.7664 -0.1924 0.2730  -0.0719 221 LEU A CD2 
3403 N N   . ARG A 237 ? 0.5557 0.3207 0.5694 -0.1173 0.1889  -0.0439 222 ARG A N   
3404 C CA  . ARG A 237 ? 0.5704 0.3083 0.5627 -0.1004 0.1851  -0.0292 222 ARG A CA  
3405 C C   . ARG A 237 ? 0.5408 0.2996 0.5261 -0.0791 0.1636  -0.0156 222 ARG A C   
3406 O O   . ARG A 237 ? 0.5580 0.2942 0.5195 -0.0630 0.1621  0.0025  222 ARG A O   
3407 C CB  . ARG A 237 ? 0.6479 0.3833 0.6548 -0.1046 0.1843  -0.0439 222 ARG A CB  
3408 C CG  . ARG A 237 ? 0.6310 0.3385 0.6189 -0.0875 0.1822  -0.0311 222 ARG A CG  
3409 C CD  . ARG A 237 ? 0.6514 0.3439 0.6487 -0.0959 0.1895  -0.0465 222 ARG A CD  
3410 N NE  . ARG A 237 ? 0.7435 0.3984 0.7355 -0.1130 0.2141  -0.0515 222 ARG A NE  
3411 C CZ  . ARG A 237 ? 0.7969 0.4600 0.8109 -0.1357 0.2241  -0.0732 222 ARG A CZ  
3412 N NH1 . ARG A 237 ? 0.7133 0.4220 0.7561 -0.1430 0.2102  -0.0925 222 ARG A NH1 
3413 N NH2 . ARG A 237 ? 0.9053 0.5294 0.9125 -0.1512 0.2490  -0.0760 222 ARG A NH2 
3427 N N   . VAL A 238 ? 0.5124 0.3141 0.5186 -0.0783 0.1468  -0.0246 223 VAL A N   
3428 C CA  . VAL A 238 ? 0.4794 0.3011 0.4805 -0.0604 0.1282  -0.0128 223 VAL A CA  
3429 C C   . VAL A 238 ? 0.5317 0.3414 0.5102 -0.0540 0.1315  0.0038  223 VAL A C   
3430 O O   . VAL A 238 ? 0.4921 0.2930 0.4532 -0.0372 0.1240  0.0193  223 VAL A O   
3431 C CB  . VAL A 238 ? 0.4293 0.2948 0.4550 -0.0623 0.1121  -0.0253 223 VAL A CB  
3432 C CG1 . VAL A 238 ? 0.4102 0.2936 0.4306 -0.0464 0.0958  -0.0135 223 VAL A CG1 
3433 C CG2 . VAL A 238 ? 0.4453 0.3209 0.4872 -0.0654 0.1064  -0.0400 223 VAL A CG2 
3443 N N   . LEU A 239 ? 0.5182 0.3284 0.4968 -0.0673 0.1428  -0.0004 224 LEU A N   
3444 C CA  . LEU A 239 ? 0.6087 0.4042 0.5613 -0.0628 0.1482  0.0144  224 LEU A CA  
3445 C C   . LEU A 239 ? 0.5991 0.3493 0.5187 -0.0526 0.1573  0.0321  224 LEU A C   
3446 O O   . LEU A 239 ? 0.5891 0.3324 0.4863 -0.0363 0.1490  0.0482  224 LEU A O   
3447 C CB  . LEU A 239 ? 0.6247 0.4214 0.5822 -0.0817 0.1648  0.0051  224 LEU A CB  
3448 C CG  . LEU A 239 ? 0.6364 0.4770 0.6188 -0.0866 0.1544  -0.0074 224 LEU A CG  
3449 C CD1 . LEU A 239 ? 0.5762 0.4199 0.5709 -0.1069 0.1729  -0.0207 224 LEU A CD1 
3450 C CD2 . LEU A 239 ? 0.5662 0.4182 0.5328 -0.0722 0.1412  0.0054  224 LEU A CD2 
3462 N N   . PHE A 240 ? 0.5930 0.3114 0.5094 -0.0616 0.1741  0.0287  225 PHE A N   
3463 C CA  . PHE A 240 ? 0.6391 0.3107 0.5241 -0.0505 0.1830  0.0454  225 PHE A CA  
3464 C C   . PHE A 240 ? 0.6856 0.3639 0.5673 -0.0271 0.1636  0.0557  225 PHE A C   
3465 O O   . PHE A 240 ? 0.6470 0.3087 0.5024 -0.0098 0.1586  0.0733  225 PHE A O   
3466 C CB  . PHE A 240 ? 0.7416 0.3807 0.6296 -0.0644 0.2029  0.0369  225 PHE A CB  
3467 C CG  . PHE A 240 ? 0.6966 0.3202 0.5843 -0.0879 0.2267  0.0286  225 PHE A CG  
3468 C CD1 . PHE A 240 ? 0.8072 0.4379 0.6846 -0.0933 0.2318  0.0325  225 PHE A CD1 
3469 C CD2 . PHE A 240 ? 0.9386 0.5403 0.8370 -0.1054 0.2453  0.0155  225 PHE A CD2 
3470 C CE1 . PHE A 240 ? 0.8901 0.5072 0.7688 -0.1158 0.2560  0.0239  225 PHE A CE1 
3471 C CE2 . PHE A 240 ? 0.8356 0.4240 0.7369 -0.1287 0.2691  0.0063  225 PHE A CE2 
3472 C CZ  . PHE A 240 ? 0.7631 0.3595 0.6549 -0.1339 0.2750  0.0107  225 PHE A CZ  
3482 N N   . LEU A 241 ? 0.6457 0.3495 0.5540 -0.0259 0.1524  0.0441  226 LEU A N   
3483 C CA  . LEU A 241 ? 0.5781 0.2889 0.4866 -0.0053 0.1368  0.0518  226 LEU A CA  
3484 C C   . LEU A 241 ? 0.7126 0.4509 0.6183 0.0081  0.1190  0.0608  226 LEU A C   
3485 O O   . LEU A 241 ? 0.6578 0.3891 0.5505 0.0273  0.1103  0.0739  226 LEU A O   
3486 C CB  . LEU A 241 ? 0.6395 0.3730 0.5753 -0.0089 0.1300  0.0364  226 LEU A CB  
3487 C CG  . LEU A 241 ? 0.7386 0.4453 0.6777 -0.0191 0.1449  0.0263  226 LEU A CG  
3488 C CD1 . LEU A 241 ? 0.6622 0.3957 0.6254 -0.0218 0.1356  0.0105  226 LEU A CD1 
3489 C CD2 . LEU A 241 ? 0.7312 0.3944 0.6475 -0.0056 0.1535  0.0399  226 LEU A CD2 
3501 N N   . MET A 242 ? 0.5984 0.3690 0.5177 -0.0013 0.1130  0.0529  227 MET A N   
3502 C CA  . MET A 242 ? 0.6137 0.4127 0.5339 0.0096  0.0960  0.0585  227 MET A CA  
3503 C C   . MET A 242 ? 0.6725 0.4511 0.5616 0.0221  0.0955  0.0755  227 MET A C   
3504 O O   . MET A 242 ? 0.7214 0.5170 0.6086 0.0369  0.0798  0.0823  227 MET A O   
3505 C CB  . MET A 242 ? 0.6909 0.5205 0.6272 -0.0036 0.0932  0.0473  227 MET A CB  
3506 C CG  . MET A 242 ? 0.7675 0.6249 0.7335 -0.0116 0.0872  0.0314  227 MET A CG  
3507 S SD  . MET A 242 ? 0.6018 0.4927 0.5821 -0.0214 0.0817  0.0220  227 MET A SD  
3508 C CE  . MET A 242 ? 0.4435 0.3553 0.4208 -0.0041 0.0624  0.0320  227 MET A CE  
3518 N N   . THR A 243 ? 0.6930 0.4358 0.5570 0.0159  0.1126  0.0818  228 THR A N   
3519 C CA  . THR A 243 ? 0.8204 0.5412 0.6490 0.0267  0.1131  0.0980  228 THR A CA  
3520 C C   . THR A 243 ? 0.8570 0.5370 0.6594 0.0431  0.1167  0.1131  228 THR A C   
3521 O O   . THR A 243 ? 1.0296 0.6843 0.7969 0.0537  0.1178  0.1281  228 THR A O   
3522 C CB  . THR A 243 ? 0.7688 0.4747 0.5815 0.0098  0.1310  0.0965  228 THR A CB  
3523 O OG1 . THR A 243 ? 0.9062 0.5878 0.7243 -0.0070 0.1519  0.0889  228 THR A OG1 
3524 C CG2 . THR A 243 ? 0.7544 0.5028 0.5896 -0.0009 0.1238  0.0838  228 THR A CG2 
3532 N N   . LYS A 244 ? 0.8816 0.5532 0.6983 0.0463  0.1183  0.1096  229 LYS A N   
3533 C CA  . LYS A 244 ? 0.8661 0.5047 0.6628 0.0661  0.1177  0.1233  229 LYS A CA  
3534 C C   . LYS A 244 ? 0.8898 0.5553 0.6905 0.0888  0.0941  0.1300  229 LYS A C   
3535 O O   . LYS A 244 ? 0.8609 0.5704 0.6903 0.0878  0.0801  0.1204  229 LYS A O   
3536 C CB  . LYS A 244 ? 0.8001 0.4245 0.6135 0.0629  0.1263  0.1154  229 LYS A CB  
3537 C CG  . LYS A 244 ? 0.8938 0.4937 0.7079 0.0394  0.1492  0.1058  229 LYS A CG  
3538 C CD  . LYS A 244 ? 0.9220 0.4624 0.6992 0.0414  0.1684  0.1193  229 LYS A CD  
3539 C CE  . LYS A 244 ? 1.1486 0.6668 0.9302 0.0151  0.1929  0.1075  229 LYS A CE  
3540 N NZ  . LYS A 244 ? 1.1113 0.6472 0.9278 0.0043  0.1933  0.0882  229 LYS A NZ  
3554 N N   . SER A 245 ? 1.0388 0.6770 0.8104 0.1098  0.0899  0.1464  230 SER A N   
3555 C CA  . SER A 245 ? 0.9429 0.6086 0.7197 0.1320  0.0667  0.1516  230 SER A CA  
3556 C C   . SER A 245 ? 0.8981 0.5896 0.7110 0.1396  0.0577  0.1428  230 SER A C   
3557 O O   . SER A 245 ? 0.9919 0.7220 0.8248 0.1495  0.0395  0.1396  230 SER A O   
3558 C CB  . SER A 245 ? 1.0579 0.6875 0.7952 0.1549  0.0632  0.1705  230 SER A CB  
3559 O OG  . SER A 245 ? 1.0357 0.6240 0.7636 0.1628  0.0748  0.1765  230 SER A OG  
3565 N N   . GLY A 246 ? 0.8953 0.5659 0.7170 0.1342  0.0711  0.1378  231 GLY A N   
3566 C CA  . GLY A 246 ? 0.7729 0.4653 0.6265 0.1394  0.0657  0.1284  231 GLY A CA  
3567 C C   . GLY A 246 ? 0.7234 0.4553 0.6090 0.1216  0.0635  0.1118  231 GLY A C   
3568 O O   . GLY A 246 ? 0.5829 0.3322 0.4928 0.1242  0.0606  0.1034  231 GLY A O   
3572 N N   . TYR A 247 ? 0.6545 0.4004 0.5398 0.1043  0.0650  0.1068  232 TYR A N   
3573 C CA  . TYR A 247 ? 0.6521 0.4303 0.5648 0.0878  0.0638  0.0913  232 TYR A CA  
3574 C C   . TYR A 247 ? 0.5381 0.3546 0.4758 0.0971  0.0483  0.0869  232 TYR A C   
3575 O O   . TYR A 247 ? 0.5832 0.4179 0.5209 0.1090  0.0349  0.0928  232 TYR A O   
3576 C CB  . TYR A 247 ? 0.6518 0.4426 0.5611 0.0720  0.0650  0.0877  232 TYR A CB  
3577 C CG  . TYR A 247 ? 0.5731 0.3941 0.5086 0.0563  0.0633  0.0721  232 TYR A CG  
3578 C CD1 . TYR A 247 ? 0.5975 0.4118 0.5448 0.0457  0.0725  0.0612  232 TYR A CD1 
3579 C CD2 . TYR A 247 ? 0.5283 0.3831 0.4753 0.0528  0.0521  0.0680  232 TYR A CD2 
3580 C CE1 . TYR A 247 ? 0.5994 0.4403 0.5675 0.0334  0.0691  0.0473  232 TYR A CE1 
3581 C CE2 . TYR A 247 ? 0.5245 0.4040 0.4929 0.0404  0.0500  0.0548  232 TYR A CE2 
3582 C CZ  . TYR A 247 ? 0.5556 0.4282 0.5337 0.0315  0.0578  0.0449  232 TYR A CZ  
3583 O OH  . TYR A 247 ? 0.4844 0.3807 0.4809 0.0212  0.0539  0.0322  232 TYR A OH  
3593 N N   . GLN A 248 ? 0.5437 0.3719 0.5021 0.0909  0.0507  0.0757  233 GLN A N   
3594 C CA  . GLN A 248 ? 0.4882 0.3506 0.4704 0.0964  0.0399  0.0702  233 GLN A CA  
3595 C C   . GLN A 248 ? 0.5078 0.3982 0.5027 0.0811  0.0357  0.0607  233 GLN A C   
3596 O O   . GLN A 248 ? 0.4524 0.3378 0.4490 0.0667  0.0433  0.0520  233 GLN A O   
3597 C CB  . GLN A 248 ? 0.5149 0.3700 0.5078 0.1000  0.0462  0.0642  233 GLN A CB  
3598 C CG  . GLN A 248 ? 0.6840 0.5134 0.6681 0.1179  0.0495  0.0728  233 GLN A CG  
3599 C CD  . GLN A 248 ? 0.8196 0.6706 0.8138 0.1371  0.0359  0.0789  233 GLN A CD  
3600 O OE1 . GLN A 248 ? 0.9177 0.7628 0.8978 0.1483  0.0287  0.0896  233 GLN A OE1 
3601 N NE2 . GLN A 248 ? 0.8729 0.7496 0.8913 0.1410  0.0326  0.0715  233 GLN A NE2 
3610 N N   . PRO A 249 ? 0.4664 0.3859 0.4710 0.0839  0.0236  0.0612  234 PRO A N   
3611 C CA  . PRO A 249 ? 0.4306 0.3737 0.4470 0.0708  0.0199  0.0525  234 PRO A CA  
3612 C C   . PRO A 249 ? 0.3831 0.3321 0.4125 0.0650  0.0236  0.0427  234 PRO A C   
3613 O O   . PRO A 249 ? 0.4108 0.3584 0.4469 0.0733  0.0252  0.0425  234 PRO A O   
3614 C CB  . PRO A 249 ? 0.3315 0.3020 0.3576 0.0779  0.0069  0.0548  234 PRO A CB  
3615 C CG  . PRO A 249 ? 0.4828 0.4426 0.4957 0.0918  0.0030  0.0653  234 PRO A CG  
3616 C CD  . PRO A 249 ? 0.4147 0.3465 0.4199 0.0993  0.0122  0.0691  234 PRO A CD  
3624 N N   . PRO A 250 ? 0.3571 0.3130 0.3898 0.0516  0.0247  0.0342  235 PRO A N   
3625 C CA  . PRO A 250 ? 0.3697 0.3291 0.4098 0.0466  0.0271  0.0249  235 PRO A CA  
3626 C C   . PRO A 250 ? 0.4114 0.3918 0.4635 0.0520  0.0210  0.0242  235 PRO A C   
3627 O O   . PRO A 250 ? 0.3320 0.3283 0.3908 0.0574  0.0139  0.0290  235 PRO A O   
3628 C CB  . PRO A 250 ? 0.3996 0.3645 0.4401 0.0329  0.0267  0.0165  235 PRO A CB  
3629 C CG  . PRO A 250 ? 0.4322 0.4059 0.4712 0.0315  0.0219  0.0211  235 PRO A CG  
3630 C CD  . PRO A 250 ? 0.3160 0.2759 0.3447 0.0412  0.0238  0.0321  235 PRO A CD  
3638 N N   . ARG A 251 ? 0.3673 0.3467 0.4215 0.0497  0.0247  0.0173  236 ARG A N   
3639 C CA  . ARG A 251 ? 0.3758 0.3706 0.4388 0.0529  0.0227  0.0157  236 ARG A CA  
3640 C C   . ARG A 251 ? 0.3894 0.3847 0.4473 0.0446  0.0233  0.0071  236 ARG A C   
3641 O O   . ARG A 251 ? 0.3260 0.3103 0.3763 0.0379  0.0254  0.0009  236 ARG A O   
3642 C CB  . ARG A 251 ? 0.4788 0.4683 0.5467 0.0633  0.0288  0.0174  236 ARG A CB  
3643 C CG  . ARG A 251 ? 0.5829 0.5733 0.6563 0.0750  0.0261  0.0258  236 ARG A CG  
3644 C CD  . ARG A 251 ? 0.7096 0.7257 0.7967 0.0779  0.0174  0.0285  236 ARG A CD  
3645 N NE  . ARG A 251 ? 0.6563 0.6759 0.7474 0.0896  0.0118  0.0355  236 ARG A NE  
3646 C CZ  . ARG A 251 ? 0.6226 0.6451 0.7074 0.0898  0.0040  0.0406  236 ARG A CZ  
3647 N NH1 . ARG A 251 ? 0.4597 0.4822 0.5363 0.0784  0.0021  0.0390  236 ARG A NH1 
3648 N NH2 . ARG A 251 ? 0.5923 0.6180 0.6787 0.1025  -0.0024 0.0467  236 ARG A NH2 
3662 N N   . LEU A 252 ? 0.3540 0.3620 0.4158 0.0451  0.0215  0.0064  237 LEU A N   
3663 C CA  . LEU A 252 ? 0.3104 0.3157 0.3628 0.0402  0.0224  -0.0005 237 LEU A CA  
3664 C C   . LEU A 252 ? 0.3402 0.3301 0.3851 0.0422  0.0313  -0.0057 237 LEU A C   
3665 O O   . LEU A 252 ? 0.3811 0.3677 0.4319 0.0494  0.0380  -0.0031 237 LEU A O   
3666 C CB  . LEU A 252 ? 0.2725 0.2896 0.3277 0.0410  0.0213  0.0016  237 LEU A CB  
3667 C CG  . LEU A 252 ? 0.3161 0.3468 0.3777 0.0382  0.0130  0.0050  237 LEU A CG  
3668 C CD1 . LEU A 252 ? 0.2622 0.3029 0.3309 0.0393  0.0150  0.0079  237 LEU A CD1 
3669 C CD2 . LEU A 252 ? 0.2804 0.3092 0.3321 0.0325  0.0063  0.0004  237 LEU A CD2 
3681 N N   . LYS A 253 ? 0.3296 0.3113 0.3624 0.0364  0.0308  -0.0142 238 LYS A N   
3682 C CA  . LYS A 253 ? 0.4053 0.3711 0.4291 0.0367  0.0388  -0.0216 238 LYS A CA  
3683 C C   . LYS A 253 ? 0.4837 0.4488 0.5023 0.0415  0.0457  -0.0222 238 LYS A C   
3684 O O   . LYS A 253 ? 0.4947 0.4518 0.5166 0.0471  0.0551  -0.0224 238 LYS A O   
3685 C CB  . LYS A 253 ? 0.4726 0.4337 0.4859 0.0285  0.0342  -0.0326 238 LYS A CB  
3686 C CG  . LYS A 253 ? 0.5249 0.4706 0.5265 0.0272  0.0409  -0.0433 238 LYS A CG  
3687 C CD  . LYS A 253 ? 0.7267 0.6558 0.7332 0.0259  0.0490  -0.0457 238 LYS A CD  
3688 C CE  . LYS A 253 ? 0.5306 0.4438 0.5256 0.0227  0.0551  -0.0591 238 LYS A CE  
3689 N NZ  . LYS A 253 ? 0.6255 0.5427 0.6154 0.0129  0.0471  -0.0721 238 LYS A NZ  
3703 N N   . GLU A 254 ? 0.4986 0.4704 0.5082 0.0396  0.0423  -0.0225 239 GLU A N   
3704 C CA  . GLU A 254 ? 0.5394 0.5080 0.5394 0.0423  0.0509  -0.0236 239 GLU A CA  
3705 C C   . GLU A 254 ? 0.4734 0.4551 0.4897 0.0462  0.0550  -0.0154 239 GLU A C   
3706 O O   . GLU A 254 ? 0.5895 0.5818 0.6097 0.0440  0.0489  -0.0103 239 GLU A O   
3707 C CB  . GLU A 254 ? 0.5143 0.4797 0.4920 0.0387  0.0458  -0.0275 239 GLU A CB  
3708 C CG  . GLU A 254 ? 0.7090 0.6663 0.6730 0.0348  0.0391  -0.0379 239 GLU A CG  
3709 C CD  . GLU A 254 ? 0.8338 0.7874 0.7728 0.0341  0.0327  -0.0420 239 GLU A CD  
3710 O OE1 . GLU A 254 ? 0.8441 0.7908 0.7671 0.0367  0.0404  -0.0399 239 GLU A OE1 
3711 O OE2 . GLU A 254 ? 0.8139 0.7714 0.7488 0.0314  0.0202  -0.0474 239 GLU A OE2 
3718 N N   . LYS A 255 ? 0.4756 0.4570 0.5025 0.0521  0.0656  -0.0153 240 LYS A N   
3719 C CA  . LYS A 255 ? 0.3982 0.3961 0.4468 0.0561  0.0686  -0.0096 240 LYS A CA  
3720 C C   . LYS A 255 ? 0.4416 0.4444 0.4850 0.0522  0.0746  -0.0089 240 LYS A C   
3721 O O   . LYS A 255 ? 0.4411 0.4570 0.4956 0.0498  0.0708  -0.0042 240 LYS A O   
3722 C CB  . LYS A 255 ? 0.4378 0.4355 0.5016 0.0649  0.0777  -0.0111 240 LYS A CB  
3723 C CG  . LYS A 255 ? 0.5478 0.5336 0.6121 0.0693  0.0745  -0.0111 240 LYS A CG  
3724 C CD  . LYS A 255 ? 0.3989 0.3905 0.4682 0.0678  0.0620  -0.0048 240 LYS A CD  
3725 C CE  . LYS A 255 ? 0.5787 0.5553 0.6475 0.0726  0.0616  -0.0033 240 LYS A CE  
3726 N NZ  . LYS A 255 ? 0.4941 0.4727 0.5625 0.0695  0.0515  0.0023  240 LYS A NZ  
3740 N N   . GLY A 256 ? 0.3967 0.3871 0.4215 0.0512  0.0850  -0.0138 241 GLY A N   
3741 C CA  . GLY A 256 ? 0.4038 0.3947 0.4213 0.0477  0.0947  -0.0127 241 GLY A CA  
3742 C C   . GLY A 256 ? 0.4765 0.4628 0.4754 0.0420  0.0867  -0.0086 241 GLY A C   
3743 O O   . GLY A 256 ? 0.4299 0.4161 0.4250 0.0384  0.0943  -0.0054 241 GLY A O   
3747 N N   . LYS A 257 ? 0.4907 0.4726 0.4787 0.0410  0.0724  -0.0090 242 LYS A N   
3748 C CA  . LYS A 257 ? 0.5078 0.4854 0.4790 0.0377  0.0633  -0.0057 242 LYS A CA  
3749 C C   . LYS A 257 ? 0.4082 0.3998 0.3996 0.0354  0.0586  0.0008  242 LYS A C   
3750 O O   . LYS A 257 ? 0.4177 0.4042 0.3971 0.0329  0.0554  0.0046  242 LYS A O   
3751 C CB  . LYS A 257 ? 0.4768 0.4495 0.4356 0.0377  0.0491  -0.0102 242 LYS A CB  
3752 C CG  . LYS A 257 ? 0.5485 0.5180 0.4915 0.0365  0.0377  -0.0078 242 LYS A CG  
3753 C CD  . LYS A 257 ? 0.5620 0.5277 0.4916 0.0370  0.0249  -0.0154 242 LYS A CD  
3754 C CE  . LYS A 257 ? 0.5344 0.4983 0.4498 0.0384  0.0121  -0.0134 242 LYS A CE  
3755 N NZ  . LYS A 257 ? 0.6555 0.6191 0.5597 0.0396  -0.0012 -0.0230 242 LYS A NZ  
3769 N N   . TRP A 258 ? 0.3246 0.3323 0.3448 0.0369  0.0579  0.0020  243 TRP A N   
3770 C CA  . TRP A 258 ? 0.3313 0.3534 0.3704 0.0349  0.0512  0.0063  243 TRP A CA  
3771 C C   . TRP A 258 ? 0.3658 0.4034 0.4310 0.0354  0.0602  0.0068  243 TRP A C   
3772 O O   . TRP A 258 ? 0.3300 0.3714 0.4059 0.0398  0.0679  0.0040  243 TRP A O   
3773 C CB  . TRP A 258 ? 0.2987 0.3275 0.3467 0.0364  0.0382  0.0064  243 TRP A CB  
3774 C CG  . TRP A 258 ? 0.3076 0.3247 0.3363 0.0358  0.0309  0.0028  243 TRP A CG  
3775 C CD1 . TRP A 258 ? 0.3316 0.3425 0.3569 0.0375  0.0307  -0.0017 243 TRP A CD1 
3776 C CD2 . TRP A 258 ? 0.2841 0.2950 0.2958 0.0335  0.0227  0.0022  243 TRP A CD2 
3777 N NE1 . TRP A 258 ? 0.3676 0.3714 0.3773 0.0351  0.0229  -0.0063 243 TRP A NE1 
3778 C CE2 . TRP A 258 ? 0.2894 0.2941 0.2907 0.0336  0.0170  -0.0040 243 TRP A CE2 
3779 C CE3 . TRP A 258 ? 0.3930 0.4023 0.3979 0.0318  0.0195  0.0059  243 TRP A CE3 
3780 C CZ2 . TRP A 258 ? 0.3081 0.3090 0.2948 0.0330  0.0067  -0.0075 243 TRP A CZ2 
3781 C CZ3 . TRP A 258 ? 0.3175 0.3196 0.3051 0.0324  0.0095  0.0039  243 TRP A CZ3 
3782 C CH2 . TRP A 258 ? 0.3613 0.3612 0.3411 0.0334  0.0025  -0.0031 243 TRP A CH2 
3793 N N   . SER A 259 ? 0.3054 0.3525 0.3823 0.0310  0.0588  0.0093  244 SER A N   
3794 C CA  . SER A 259 ? 0.2681 0.3329 0.3726 0.0298  0.0667  0.0078  244 SER A CA  
3795 C C   . SER A 259 ? 0.2494 0.3341 0.3797 0.0358  0.0577  0.0069  244 SER A C   
3796 O O   . SER A 259 ? 0.3128 0.3964 0.4385 0.0386  0.0453  0.0089  244 SER A O   
3797 C CB  . SER A 259 ? 0.2677 0.3346 0.3761 0.0218  0.0683  0.0095  244 SER A CB  
3798 O OG  . SER A 259 ? 0.2492 0.3262 0.3672 0.0214  0.0539  0.0107  244 SER A OG  
3804 N N   . ALA A 260 ? 0.2484 0.3515 0.4058 0.0380  0.0642  0.0035  245 ALA A N   
3805 C CA  . ALA A 260 ? 0.2330 0.3563 0.4146 0.0455  0.0543  0.0026  245 ALA A CA  
3806 C C   . ALA A 260 ? 0.2694 0.4000 0.4531 0.0427  0.0401  0.0049  245 ALA A C   
3807 O O   . ALA A 260 ? 0.2579 0.3922 0.4425 0.0491  0.0286  0.0071  245 ALA A O   
3808 C CB  . ALA A 260 ? 0.2325 0.3792 0.4469 0.0474  0.0623  -0.0033 245 ALA A CB  
3814 N N   . ALA A 261 ? 0.2430 0.3736 0.4258 0.0332  0.0415  0.0045  246 ALA A N   
3815 C CA  . ALA A 261 ? 0.2049 0.3421 0.3900 0.0303  0.0289  0.0053  246 ALA A CA  
3816 C C   . ALA A 261 ? 0.2024 0.3249 0.3646 0.0328  0.0192  0.0096  246 ALA A C   
3817 O O   . ALA A 261 ? 0.2310 0.3609 0.3964 0.0357  0.0081  0.0104  246 ALA A O   
3818 C CB  . ALA A 261 ? 0.2779 0.4118 0.4628 0.0196  0.0341  0.0041  246 ALA A CB  
3824 N N   . PHE A 262 ? 0.2122 0.3144 0.3512 0.0316  0.0234  0.0115  247 PHE A N   
3825 C CA  . PHE A 262 ? 0.2106 0.3011 0.3315 0.0329  0.0150  0.0134  247 PHE A CA  
3826 C C   . PHE A 262 ? 0.2095 0.3014 0.3331 0.0402  0.0119  0.0142  247 PHE A C   
3827 O O   . PHE A 262 ? 0.2098 0.3022 0.3306 0.0413  0.0035  0.0157  247 PHE A O   
3828 C CB  . PHE A 262 ? 0.2241 0.2951 0.3214 0.0307  0.0194  0.0133  247 PHE A CB  
3829 C CG  . PHE A 262 ? 0.2228 0.2849 0.3048 0.0305  0.0106  0.0129  247 PHE A CG  
3830 C CD1 . PHE A 262 ? 0.3242 0.3938 0.4126 0.0305  0.0014  0.0131  247 PHE A CD1 
3831 C CD2 . PHE A 262 ? 0.2799 0.3268 0.3412 0.0303  0.0118  0.0111  247 PHE A CD2 
3832 C CE1 . PHE A 262 ? 0.2585 0.3218 0.3362 0.0293  -0.0049 0.0111  247 PHE A CE1 
3833 C CE2 . PHE A 262 ? 0.3167 0.3590 0.3682 0.0298  0.0033  0.0085  247 PHE A CE2 
3834 C CZ  . PHE A 262 ? 0.2635 0.3147 0.3250 0.0289  -0.0043 0.0082  247 PHE A CZ  
3844 N N   . HIS A 263 ? 0.2330 0.3236 0.3612 0.0454  0.0196  0.0133  248 HIS A N   
3845 C CA  . HIS A 263 ? 0.2297 0.3182 0.3600 0.0536  0.0175  0.0149  248 HIS A CA  
3846 C C   . HIS A 263 ? 0.2777 0.3818 0.4219 0.0583  0.0080  0.0171  248 HIS A C   
3847 O O   . HIS A 263 ? 0.2164 0.3140 0.3527 0.0623  0.0022  0.0204  248 HIS A O   
3848 C CB  . HIS A 263 ? 0.2464 0.3335 0.3837 0.0598  0.0278  0.0127  248 HIS A CB  
3849 C CG  . HIS A 263 ? 0.2683 0.3362 0.3865 0.0572  0.0363  0.0102  248 HIS A CG  
3850 N ND1 . HIS A 263 ? 0.2902 0.3409 0.3908 0.0567  0.0342  0.0099  248 HIS A ND1 
3851 C CD2 . HIS A 263 ? 0.2564 0.3194 0.3696 0.0547  0.0475  0.0069  248 HIS A CD2 
3852 C CE1 . HIS A 263 ? 0.3546 0.3920 0.4407 0.0544  0.0419  0.0058  248 HIS A CE1 
3853 N NE2 . HIS A 263 ? 0.2695 0.3130 0.3607 0.0536  0.0501  0.0045  248 HIS A NE2 
3862 N N   . ASN A 264 ? 0.2155 0.3395 0.3794 0.0575  0.0066  0.0148  249 ASN A N   
3863 C CA  . ASN A 264 ? 0.2759 0.4169 0.4528 0.0627  -0.0040 0.0154  249 ASN A CA  
3864 C C   . ASN A 264 ? 0.2435 0.3818 0.4083 0.0575  -0.0131 0.0171  249 ASN A C   
3865 O O   . ASN A 264 ? 0.2219 0.3630 0.3835 0.0630  -0.0218 0.0198  249 ASN A O   
3866 C CB  . ASN A 264 ? 0.2398 0.4052 0.4440 0.0616  -0.0031 0.0098  249 ASN A CB  
3867 C CG  . ASN A 264 ? 0.2690 0.4549 0.4875 0.0680  -0.0160 0.0086  249 ASN A CG  
3868 O OD1 . ASN A 264 ? 0.2572 0.4513 0.4770 0.0621  -0.0232 0.0066  249 ASN A OD1 
3869 N ND2 . ASN A 264 ? 0.3285 0.5215 0.5560 0.0812  -0.0197 0.0095  249 ASN A ND2 
3876 N N   . PHE A 265 ? 0.1891 0.3208 0.3458 0.0478  -0.0109 0.0157  250 PHE A N   
3877 C CA  . PHE A 265 ? 0.2647 0.3927 0.4103 0.0433  -0.0181 0.0163  250 PHE A CA  
3878 C C   . PHE A 265 ? 0.2987 0.4123 0.4275 0.0463  -0.0196 0.0198  250 PHE A C   
3879 O O   . PHE A 265 ? 0.2666 0.3813 0.3898 0.0471  -0.0259 0.0213  250 PHE A O   
3880 C CB  . PHE A 265 ? 0.2103 0.3308 0.3492 0.0347  -0.0149 0.0143  250 PHE A CB  
3881 C CG  . PHE A 265 ? 0.2083 0.3265 0.3392 0.0304  -0.0216 0.0134  250 PHE A CG  
3882 C CD1 . PHE A 265 ? 0.2512 0.3571 0.3672 0.0297  -0.0226 0.0139  250 PHE A CD1 
3883 C CD2 . PHE A 265 ? 0.2345 0.3633 0.3744 0.0265  -0.0262 0.0105  250 PHE A CD2 
3884 C CE1 . PHE A 265 ? 0.2210 0.3267 0.3324 0.0261  -0.0277 0.0118  250 PHE A CE1 
3885 C CE2 . PHE A 265 ? 0.2107 0.3371 0.3438 0.0231  -0.0314 0.0087  250 PHE A CE2 
3886 C CZ  . PHE A 265 ? 0.1686 0.2839 0.2878 0.0233  -0.0320 0.0095  250 PHE A CZ  
3896 N N   . ILE A 266 ? 0.2450 0.3440 0.3648 0.0474  -0.0128 0.0205  251 ILE A N   
3897 C CA  . ILE A 266 ? 0.2130 0.2967 0.3187 0.0488  -0.0121 0.0227  251 ILE A CA  
3898 C C   . ILE A 266 ? 0.3220 0.4060 0.4287 0.0582  -0.0148 0.0275  251 ILE A C   
3899 O O   . ILE A 266 ? 0.2995 0.3750 0.3945 0.0588  -0.0171 0.0307  251 ILE A O   
3900 C CB  . ILE A 266 ? 0.2711 0.3396 0.3684 0.0476  -0.0042 0.0205  251 ILE A CB  
3901 C CG1 . ILE A 266 ? 0.2666 0.3326 0.3574 0.0398  -0.0043 0.0161  251 ILE A CG1 
3902 C CG2 . ILE A 266 ? 0.2991 0.3510 0.3853 0.0492  -0.0014 0.0220  251 ILE A CG2 
3903 C CD1 . ILE A 266 ? 0.2557 0.3232 0.3422 0.0344  -0.0105 0.0145  251 ILE A CD1 
3915 N N   . LYS A 267 ? 0.2933 0.3868 0.4134 0.0661  -0.0143 0.0281  252 LYS A N   
3916 C CA  . LYS A 267 ? 0.2323 0.3257 0.3530 0.0780  -0.0183 0.0329  252 LYS A CA  
3917 C C   . LYS A 267 ? 0.2752 0.3775 0.3921 0.0797  -0.0288 0.0352  252 LYS A C   
3918 O O   . LYS A 267 ? 0.3086 0.3987 0.4104 0.0859  -0.0314 0.0411  252 LYS A O   
3919 C CB  . LYS A 267 ? 0.2327 0.3410 0.3743 0.0866  -0.0172 0.0307  252 LYS A CB  
3920 C CG  . LYS A 267 ? 0.4019 0.5114 0.5455 0.1020  -0.0233 0.0354  252 LYS A CG  
3921 C CD  . LYS A 267 ? 0.3536 0.4805 0.5222 0.1114  -0.0219 0.0315  252 LYS A CD  
3922 C CE  . LYS A 267 ? 0.3881 0.5156 0.5580 0.1295  -0.0300 0.0363  252 LYS A CE  
3923 N NZ  . LYS A 267 ? 0.5574 0.7057 0.7561 0.1401  -0.0294 0.0310  252 LYS A NZ  
3937 N N   . VAL A 268 ? 0.2894 0.4111 0.4181 0.0741  -0.0343 0.0306  253 VAL A N   
3938 C CA  . VAL A 268 ? 0.2432 0.3764 0.3701 0.0769  -0.0451 0.0311  253 VAL A CA  
3939 C C   . VAL A 268 ? 0.2205 0.3428 0.3284 0.0691  -0.0456 0.0321  253 VAL A C   
3940 O O   . VAL A 268 ? 0.2678 0.3882 0.3627 0.0733  -0.0517 0.0354  253 VAL A O   
3941 C CB  . VAL A 268 ? 0.2822 0.4422 0.4325 0.0745  -0.0508 0.0240  253 VAL A CB  
3942 C CG1 . VAL A 268 ? 0.2458 0.4199 0.4177 0.0832  -0.0502 0.0220  253 VAL A CG1 
3943 C CG2 . VAL A 268 ? 0.2628 0.4237 0.4183 0.0609  -0.0451 0.0188  253 VAL A CG2 
3953 N N   . THR A 269 ? 0.2100 0.3254 0.3156 0.0585  -0.0396 0.0290  254 THR A N   
3954 C CA  . THR A 269 ? 0.2284 0.3347 0.3190 0.0519  -0.0391 0.0287  254 THR A CA  
3955 C C   . THR A 269 ? 0.3181 0.4035 0.3901 0.0549  -0.0339 0.0346  254 THR A C   
3956 O O   . THR A 269 ? 0.2988 0.3778 0.3560 0.0540  -0.0346 0.0368  254 THR A O   
3957 C CB  . THR A 269 ? 0.2483 0.3529 0.3420 0.0420  -0.0351 0.0234  254 THR A CB  
3958 O OG1 . THR A 269 ? 0.2340 0.3278 0.3273 0.0416  -0.0281 0.0235  254 THR A OG1 
3959 C CG2 . THR A 269 ? 0.2018 0.3220 0.3099 0.0382  -0.0391 0.0184  254 THR A CG2 
3967 N N   . LEU A 270 ? 0.2375 0.3104 0.3089 0.0581  -0.0274 0.0368  255 LEU A N   
3968 C CA  . LEU A 270 ? 0.2586 0.3078 0.3129 0.0598  -0.0204 0.0417  255 LEU A CA  
3969 C C   . LEU A 270 ? 0.2803 0.3227 0.3258 0.0733  -0.0238 0.0500  255 LEU A C   
3970 O O   . LEU A 270 ? 0.3420 0.3674 0.3819 0.0800  -0.0186 0.0543  255 LEU A O   
3971 C CB  . LEU A 270 ? 0.3298 0.3672 0.3868 0.0564  -0.0117 0.0387  255 LEU A CB  
3972 C CG  . LEU A 270 ? 0.3056 0.3480 0.3680 0.0449  -0.0099 0.0306  255 LEU A CG  
3973 C CD1 . LEU A 270 ? 0.3397 0.3685 0.4006 0.0423  -0.0021 0.0270  255 LEU A CD1 
3974 C CD2 . LEU A 270 ? 0.2415 0.2831 0.2971 0.0368  -0.0097 0.0282  255 LEU A CD2 
3986 N N   . THR A 271 ? 0.3238 0.3790 0.3669 0.0780  -0.0335 0.0517  256 THR A N   
3987 C CA  . THR A 271 ? 0.3840 0.4321 0.4135 0.0921  -0.0393 0.0599  256 THR A CA  
3988 C C   . THR A 271 ? 0.3978 0.4201 0.3978 0.0899  -0.0332 0.0664  256 THR A C   
3989 O O   . THR A 271 ? 0.3906 0.4147 0.3835 0.0796  -0.0314 0.0632  256 THR A O   
3990 C CB  . THR A 271 ? 0.3885 0.4627 0.4272 0.0981  -0.0536 0.0574  256 THR A CB  
3991 O OG1 . THR A 271 ? 0.2802 0.3779 0.3483 0.0978  -0.0565 0.0503  256 THR A OG1 
3992 C CG2 . THR A 271 ? 0.3587 0.4268 0.3819 0.1150  -0.0622 0.0656  256 THR A CG2 
4000 N N   . LYS A 272 ? 0.4007 0.3976 0.3831 0.0999  -0.0290 0.0755  257 LYS A N   
4001 C CA  . LYS A 272 ? 0.4205 0.3865 0.3735 0.0962  -0.0187 0.0823  257 LYS A CA  
4002 C C   . LYS A 272 ? 0.4124 0.3786 0.3428 0.0993  -0.0252 0.0867  257 LYS A C   
4003 O O   . LYS A 272 ? 0.5170 0.4744 0.4334 0.0877  -0.0172 0.0854  257 LYS A O   
4004 C CB  . LYS A 272 ? 0.4474 0.3826 0.3857 0.1075  -0.0122 0.0917  257 LYS A CB  
4005 C CG  . LYS A 272 ? 0.5385 0.4504 0.4766 0.0962  0.0044  0.0891  257 LYS A CG  
4006 C CD  . LYS A 272 ? 0.6105 0.4849 0.5280 0.1070  0.0125  0.0994  257 LYS A CD  
4007 C CE  . LYS A 272 ? 0.6349 0.5163 0.5640 0.1262  0.0030  0.1027  257 LYS A CE  
4008 N NZ  . LYS A 272 ? 0.8449 0.6876 0.7555 0.1374  0.0116  0.1120  257 LYS A NZ  
4022 N N   . SER A 273 ? 0.4362 0.4116 0.3618 0.1153  -0.0393 0.0915  258 SER A N   
4023 C CA  . SER A 273 ? 0.4979 0.4731 0.3983 0.1199  -0.0472 0.0954  258 SER A CA  
4024 C C   . SER A 273 ? 0.4331 0.4387 0.3495 0.1086  -0.0533 0.0840  258 SER A C   
4025 O O   . SER A 273 ? 0.4408 0.4756 0.3876 0.1083  -0.0620 0.0756  258 SER A O   
4026 C CB  . SER A 273 ? 0.5423 0.5222 0.4351 0.1418  -0.0633 0.1021  258 SER A CB  
4027 O OG  . SER A 273 ? 0.8530 0.8390 0.7236 0.1462  -0.0740 0.1033  258 SER A OG  
4033 N N   . PRO A 274 ? 0.5545 0.5530 0.4513 0.0989  -0.0477 0.0828  259 PRO A N   
4034 C CA  . PRO A 274 ? 0.4245 0.4505 0.3363 0.0894  -0.0537 0.0714  259 PRO A CA  
4035 C C   . PRO A 274 ? 0.5326 0.5830 0.4483 0.1002  -0.0726 0.0684  259 PRO A C   
4036 O O   . PRO A 274 ? 0.4922 0.5694 0.4309 0.0935  -0.0792 0.0574  259 PRO A O   
4037 C CB  . PRO A 274 ? 0.5089 0.5178 0.3946 0.0791  -0.0422 0.0718  259 PRO A CB  
4038 C CG  . PRO A 274 ? 0.5643 0.5377 0.4275 0.0793  -0.0273 0.0820  259 PRO A CG  
4039 C CD  . PRO A 274 ? 0.5880 0.5525 0.4478 0.0963  -0.0348 0.0915  259 PRO A CD  
4047 N N   . LYS A 275 ? 0.5195 0.5609 0.4130 0.1169  -0.0820 0.0774  260 LYS A N   
4048 C CA  . LYS A 275 ? 0.6565 0.7238 0.5546 0.1282  -0.1021 0.0730  260 LYS A CA  
4049 C C   . LYS A 275 ? 0.6041 0.7021 0.5449 0.1314  -0.1112 0.0650  260 LYS A C   
4050 O O   . LYS A 275 ? 0.6602 0.7875 0.6166 0.1347  -0.1261 0.0561  260 LYS A O   
4051 C CB  . LYS A 275 ? 0.6740 0.7228 0.5363 0.1479  -0.1111 0.0852  260 LYS A CB  
4052 C CG  . LYS A 275 ? 0.8624 0.9207 0.7001 0.1535  -0.1252 0.0825  260 LYS A CG  
4053 C CD  . LYS A 275 ? 0.9319 0.9584 0.7196 0.1704  -0.1283 0.0977  260 LYS A CD  
4054 C CE  . LYS A 275 ? 0.9685 1.0030 0.7269 0.1755  -0.1421 0.0945  260 LYS A CE  
4055 N NZ  . LYS A 275 ? 1.0266 1.0259 0.7294 0.1924  -0.1445 0.1105  260 LYS A NZ  
4069 N N   . LYS A 276 ? 0.5335 0.6256 0.4935 0.1298  -0.1019 0.0669  261 LYS A N   
4070 C CA  . LYS A 276 ? 0.4415 0.5599 0.4407 0.1316  -0.1069 0.0594  261 LYS A CA  
4071 C C   . LYS A 276 ? 0.4498 0.5769 0.4743 0.1139  -0.0963 0.0509  261 LYS A C   
4072 O O   . LYS A 276 ? 0.5278 0.6746 0.5833 0.1130  -0.0975 0.0445  261 LYS A O   
4073 C CB  . LYS A 276 ? 0.4863 0.5921 0.4881 0.1456  -0.1050 0.0674  261 LYS A CB  
4074 C CG  . LYS A 276 ? 0.5435 0.6466 0.5278 0.1676  -0.1194 0.0749  261 LYS A CG  
4075 C CD  . LYS A 276 ? 0.6069 0.7492 0.6250 0.1776  -0.1361 0.0653  261 LYS A CD  
4076 C CE  . LYS A 276 ? 0.6797 0.8218 0.6814 0.2019  -0.1531 0.0718  261 LYS A CE  
4077 N NZ  . LYS A 276 ? 0.7523 0.9325 0.7902 0.2034  -0.1666 0.0588  261 LYS A NZ  
4091 N N   . ARG A 277 ? 0.3557 0.4683 0.3673 0.1006  -0.0856 0.0505  262 ARG A N   
4092 C CA  . ARG A 277 ? 0.3062 0.4239 0.3385 0.0862  -0.0765 0.0435  262 ARG A CA  
4093 C C   . ARG A 277 ? 0.3124 0.4556 0.3635 0.0787  -0.0835 0.0325  262 ARG A C   
4094 O O   . ARG A 277 ? 0.2855 0.4340 0.3246 0.0777  -0.0898 0.0295  262 ARG A O   
4095 C CB  . ARG A 277 ? 0.2928 0.3878 0.3076 0.0758  -0.0634 0.0457  262 ARG A CB  
4096 C CG  . ARG A 277 ? 0.2812 0.3775 0.3142 0.0641  -0.0546 0.0399  262 ARG A CG  
4097 C CD  . ARG A 277 ? 0.2732 0.3500 0.2918 0.0549  -0.0427 0.0406  262 ARG A CD  
4098 N NE  . ARG A 277 ? 0.3064 0.3582 0.3052 0.0601  -0.0355 0.0495  262 ARG A NE  
4099 C CZ  . ARG A 277 ? 0.3664 0.3984 0.3432 0.0556  -0.0265 0.0528  262 ARG A CZ  
4100 N NH1 . ARG A 277 ? 0.3167 0.3528 0.2897 0.0460  -0.0234 0.0472  262 ARG A NH1 
4101 N NH2 . ARG A 277 ? 0.4018 0.4081 0.3603 0.0608  -0.0193 0.0617  262 ARG A NH2 
4115 N N   . PRO A 278 ? 0.2819 0.4394 0.3606 0.0731  -0.0817 0.0261  263 PRO A N   
4116 C CA  . PRO A 278 ? 0.2721 0.4509 0.3689 0.0656  -0.0871 0.0157  263 PRO A CA  
4117 C C   . PRO A 278 ? 0.2727 0.4445 0.3608 0.0541  -0.0823 0.0116  263 PRO A C   
4118 O O   . PRO A 278 ? 0.3010 0.4558 0.3794 0.0492  -0.0728 0.0148  263 PRO A O   
4119 C CB  . PRO A 278 ? 0.2472 0.4355 0.3714 0.0622  -0.0823 0.0120  263 PRO A CB  
4120 C CG  . PRO A 278 ? 0.3118 0.4799 0.4282 0.0635  -0.0720 0.0194  263 PRO A CG  
4121 C CD  . PRO A 278 ? 0.3628 0.5162 0.4561 0.0736  -0.0740 0.0280  263 PRO A CD  
4129 N N   . SER A 279 ? 0.2524 0.4388 0.3457 0.0501  -0.0893 0.0031  264 SER A N   
4130 C CA  . SER A 279 ? 0.2495 0.4313 0.3367 0.0404  -0.0856 -0.0023 264 SER A CA  
4131 C C   . SER A 279 ? 0.2440 0.4247 0.3494 0.0315  -0.0785 -0.0064 264 SER A C   
4132 O O   . SER A 279 ? 0.1872 0.3706 0.3083 0.0317  -0.0758 -0.0052 264 SER A O   
4133 C CB  . SER A 279 ? 0.2844 0.4810 0.3702 0.0396  -0.0955 -0.0110 264 SER A CB  
4134 O OG  . SER A 279 ? 0.2806 0.4972 0.3926 0.0377  -0.1014 -0.0190 264 SER A OG  
4140 N N   . ALA A 280 ? 0.2029 0.3783 0.3047 0.0243  -0.0749 -0.0112 265 ALA A N   
4141 C CA  . ALA A 280 ? 0.2231 0.3950 0.3386 0.0178  -0.0696 -0.0145 265 ALA A CA  
4142 C C   . ALA A 280 ? 0.2544 0.4389 0.3898 0.0143  -0.0728 -0.0210 265 ALA A C   
4143 O O   . ALA A 280 ? 0.2112 0.3932 0.3588 0.0120  -0.0681 -0.0199 265 ALA A O   
4144 C CB  . ALA A 280 ? 0.2135 0.3780 0.3222 0.0128  -0.0662 -0.0191 265 ALA A CB  
4150 N N   . THR A 281 ? 0.2762 0.4737 0.4142 0.0134  -0.0803 -0.0284 266 THR A N   
4151 C CA  . THR A 281 ? 0.2345 0.4455 0.3939 0.0085  -0.0829 -0.0366 266 THR A CA  
4152 C C   . THR A 281 ? 0.2237 0.4448 0.3987 0.0121  -0.0829 -0.0335 266 THR A C   
4153 O O   . THR A 281 ? 0.2121 0.4348 0.4051 0.0066  -0.0771 -0.0361 266 THR A O   
4154 C CB  . THR A 281 ? 0.2127 0.4381 0.3714 0.0075  -0.0925 -0.0465 266 THR A CB  
4155 O OG1 . THR A 281 ? 0.2609 0.4766 0.4078 0.0031  -0.0904 -0.0510 266 THR A OG1 
4156 C CG2 . THR A 281 ? 0.2190 0.4609 0.4037 0.0014  -0.0951 -0.0568 266 THR A CG2 
4164 N N   . LYS A 282 ? 0.2521 0.4789 0.4201 0.0218  -0.0885 -0.0281 267 LYS A N   
4165 C CA  . LYS A 282 ? 0.1938 0.4313 0.3786 0.0267  -0.0884 -0.0261 267 LYS A CA  
4166 C C   . LYS A 282 ? 0.1922 0.4150 0.3799 0.0242  -0.0761 -0.0200 267 LYS A C   
4167 O O   . LYS A 282 ? 0.2178 0.4480 0.4252 0.0218  -0.0711 -0.0223 267 LYS A O   
4168 C CB  . LYS A 282 ? 0.2190 0.4607 0.3926 0.0399  -0.0965 -0.0200 267 LYS A CB  
4169 C CG  . LYS A 282 ? 0.2242 0.4766 0.4164 0.0469  -0.0959 -0.0182 267 LYS A CG  
4170 C CD  . LYS A 282 ? 0.3233 0.5829 0.5075 0.0619  -0.1069 -0.0140 267 LYS A CD  
4171 C CE  . LYS A 282 ? 0.2894 0.5597 0.4951 0.0697  -0.1053 -0.0130 267 LYS A CE  
4172 N NZ  . LYS A 282 ? 0.4597 0.7362 0.6584 0.0869  -0.1171 -0.0086 267 LYS A NZ  
4186 N N   . MET A 283 ? 0.2123 0.4149 0.3805 0.0245  -0.0708 -0.0131 268 MET A N   
4187 C CA  . MET A 283 ? 0.1945 0.3827 0.3618 0.0228  -0.0607 -0.0080 268 MET A CA  
4188 C C   . MET A 283 ? 0.2193 0.4034 0.3965 0.0138  -0.0545 -0.0123 268 MET A C   
4189 O O   . MET A 283 ? 0.1712 0.3485 0.3524 0.0124  -0.0463 -0.0097 268 MET A O   
4190 C CB  . MET A 283 ? 0.1655 0.3356 0.3117 0.0243  -0.0579 -0.0022 268 MET A CB  
4191 C CG  . MET A 283 ? 0.2266 0.3926 0.3607 0.0329  -0.0594 0.0044  268 MET A CG  
4192 S SD  . MET A 283 ? 0.2542 0.4238 0.3996 0.0405  -0.0565 0.0084  268 MET A SD  
4193 C CE  . MET A 283 ? 0.2095 0.3680 0.3588 0.0337  -0.0457 0.0081  268 MET A CE  
4203 N N   . LEU A 284 ? 0.2435 0.4293 0.4225 0.0079  -0.0573 -0.0187 269 LEU A N   
4204 C CA  . LEU A 284 ? 0.1607 0.3386 0.3471 -0.0001 -0.0508 -0.0222 269 LEU A CA  
4205 C C   . LEU A 284 ? 0.1900 0.3795 0.3982 -0.0047 -0.0463 -0.0264 269 LEU A C   
4206 O O   . LEU A 284 ? 0.2373 0.4159 0.4497 -0.0114 -0.0372 -0.0271 269 LEU A O   
4207 C CB  . LEU A 284 ? 0.2654 0.4417 0.4496 -0.0048 -0.0547 -0.0291 269 LEU A CB  
4208 C CG  . LEU A 284 ? 0.2427 0.4037 0.4092 -0.0027 -0.0547 -0.0262 269 LEU A CG  
4209 C CD1 . LEU A 284 ? 0.2633 0.4253 0.4289 -0.0061 -0.0585 -0.0343 269 LEU A CD1 
4210 C CD2 . LEU A 284 ? 0.2387 0.3808 0.3997 -0.0033 -0.0475 -0.0214 269 LEU A CD2 
4222 N N   . SER A 285 ? 0.1714 0.3823 0.3934 -0.0008 -0.0520 -0.0295 270 SER A N   
4223 C CA  . SER A 285 ? 0.2265 0.4529 0.4738 -0.0043 -0.0473 -0.0348 270 SER A CA  
4224 C C   . SER A 285 ? 0.3001 0.5231 0.5485 0.0008  -0.0394 -0.0280 270 SER A C   
4225 O O   . SER A 285 ? 0.2134 0.4510 0.4844 -0.0013 -0.0341 -0.0327 270 SER A O   
4226 C CB  . SER A 285 ? 0.1840 0.4393 0.4492 -0.0012 -0.0592 -0.0436 270 SER A CB  
4227 O OG  . SER A 285 ? 0.4263 0.6857 0.6912 -0.0069 -0.0660 -0.0520 270 SER A OG  
4233 N N   . HIS A 286 ? 0.2713 0.4768 0.4976 0.0069  -0.0379 -0.0187 271 HIS A N   
4234 C CA  . HIS A 286 ? 0.1881 0.3897 0.4142 0.0121  -0.0307 -0.0134 271 HIS A CA  
4235 C C   . HIS A 286 ? 0.2464 0.4347 0.4732 0.0047  -0.0163 -0.0127 271 HIS A C   
4236 O O   . HIS A 286 ? 0.2053 0.3763 0.4198 -0.0015 -0.0126 -0.0114 271 HIS A O   
4237 C CB  . HIS A 286 ? 0.1621 0.3479 0.3644 0.0196  -0.0330 -0.0052 271 HIS A CB  
4238 C CG  . HIS A 286 ? 0.1655 0.3485 0.3678 0.0264  -0.0273 -0.0010 271 HIS A CG  
4239 N ND1 . HIS A 286 ? 0.1702 0.3375 0.3642 0.0241  -0.0163 0.0019  271 HIS A ND1 
4240 C CD2 . HIS A 286 ? 0.1912 0.3838 0.3995 0.0362  -0.0311 0.0004  271 HIS A CD2 
4241 C CE1 . HIS A 286 ? 0.1892 0.3571 0.3853 0.0313  -0.0127 0.0041  271 HIS A CE1 
4242 N NE2 . HIS A 286 ? 0.2052 0.3879 0.4106 0.0391  -0.0216 0.0035  271 HIS A NE2 
4250 N N   . GLN A 287 ? 0.1821 0.3772 0.4219 0.0062  -0.0079 -0.0132 272 GLN A N   
4251 C CA  . GLN A 287 ? 0.1809 0.3629 0.4196 -0.0010 0.0079  -0.0125 272 GLN A CA  
4252 C C   . GLN A 287 ? 0.2854 0.4375 0.4926 -0.0016 0.0112  -0.0049 272 GLN A C   
4253 O O   . GLN A 287 ? 0.2479 0.3837 0.4467 -0.0088 0.0190  -0.0040 272 GLN A O   
4254 C CB  . GLN A 287 ? 0.2318 0.4230 0.4833 0.0035  0.0165  -0.0132 272 GLN A CB  
4255 C CG  . GLN A 287 ? 0.2946 0.4778 0.5507 -0.0053 0.0348  -0.0148 272 GLN A CG  
4256 C CD  . GLN A 287 ? 0.3703 0.5625 0.6389 -0.0006 0.0448  -0.0164 272 GLN A CD  
4257 O OE1 . GLN A 287 ? 0.2527 0.4561 0.5267 0.0105  0.0372  -0.0159 272 GLN A OE1 
4258 N NE2 . GLN A 287 ? 0.4303 0.6160 0.7030 -0.0089 0.0632  -0.0184 272 GLN A NE2 
4267 N N   . LEU A 288 ? 0.1937 0.3378 0.3832 0.0064  0.0050  0.0002  273 LEU A N   
4268 C CA  . LEU A 288 ? 0.2301 0.3496 0.3924 0.0070  0.0072  0.0057  273 LEU A CA  
4269 C C   . LEU A 288 ? 0.2889 0.3966 0.4411 0.0025  0.0035  0.0058  273 LEU A C   
4270 O O   . LEU A 288 ? 0.2739 0.3612 0.4085 0.0007  0.0089  0.0091  273 LEU A O   
4271 C CB  . LEU A 288 ? 0.1955 0.3117 0.3450 0.0147  0.0001  0.0086  273 LEU A CB  
4272 C CG  . LEU A 288 ? 0.2542 0.3489 0.3788 0.0158  0.0019  0.0120  273 LEU A CG  
4273 C CD1 . LEU A 288 ? 0.2568 0.3425 0.3746 0.0167  0.0135  0.0134  273 LEU A CD1 
4274 C CD2 . LEU A 288 ? 0.3083 0.4015 0.4240 0.0204  -0.0064 0.0126  273 LEU A CD2 
4286 N N   . VAL A 289 ? 0.1955 0.3144 0.3561 0.0018  -0.0062 0.0022  274 VAL A N   
4287 C CA  . VAL A 289 ? 0.2343 0.3429 0.3872 -0.0014 -0.0101 0.0012  274 VAL A CA  
4288 C C   . VAL A 289 ? 0.2650 0.3760 0.4323 -0.0099 -0.0054 -0.0038 274 VAL A C   
4289 O O   . VAL A 289 ? 0.2670 0.3669 0.4286 -0.0126 -0.0072 -0.0050 274 VAL A O   
4290 C CB  . VAL A 289 ? 0.2249 0.3417 0.3760 0.0022  -0.0219 -0.0009 274 VAL A CB  
4291 C CG1 . VAL A 289 ? 0.2546 0.3665 0.3918 0.0086  -0.0248 0.0031  274 VAL A CG1 
4292 C CG2 . VAL A 289 ? 0.2143 0.3536 0.3833 0.0018  -0.0275 -0.0058 274 VAL A CG2 
4302 N N   . SER A 290 ? 0.2569 0.3828 0.4449 -0.0142 0.0008  -0.0077 275 SER A N   
4303 C CA  . SER A 290 ? 0.2170 0.3472 0.4228 -0.0242 0.0067  -0.0144 275 SER A CA  
4304 C C   . SER A 290 ? 0.3009 0.4122 0.5020 -0.0310 0.0236  -0.0116 275 SER A C   
4305 O O   . SER A 290 ? 0.2664 0.3741 0.4789 -0.0410 0.0316  -0.0165 275 SER A O   
4306 C CB  . SER A 290 ? 0.2004 0.3624 0.4361 -0.0256 0.0028  -0.0231 275 SER A CB  
4307 O OG  . SER A 290 ? 0.4280 0.6040 0.6648 -0.0208 -0.0123 -0.0263 275 SER A OG  
4313 N N   . GLN A 291 ? 0.3150 0.4126 0.4983 -0.0263 0.0300  -0.0043 276 GLN A N   
4314 C CA  . GLN A 291 ? 0.4170 0.4963 0.5927 -0.0323 0.0475  -0.0012 276 GLN A CA  
4315 C C   . GLN A 291 ? 0.3357 0.3831 0.4887 -0.0359 0.0520  0.0035  276 GLN A C   
4316 O O   . GLN A 291 ? 0.3455 0.3834 0.4841 -0.0304 0.0405  0.0058  276 GLN A O   
4317 C CB  . GLN A 291 ? 0.2921 0.3638 0.4504 -0.0253 0.0521  0.0049  276 GLN A CB  
4318 C CG  . GLN A 291 ? 0.3975 0.4562 0.5290 -0.0155 0.0405  0.0108  276 GLN A CG  
4319 C CD  . GLN A 291 ? 0.3377 0.3889 0.4526 -0.0097 0.0452  0.0148  276 GLN A CD  
4320 O OE1 . GLN A 291 ? 0.4217 0.4628 0.5306 -0.0132 0.0600  0.0163  276 GLN A OE1 
4321 N NE2 . GLN A 291 ? 0.2658 0.3210 0.3729 -0.0016 0.0337  0.0158  276 GLN A NE2 
4330 N N   . PRO A 292 ? 0.3944 0.4244 0.5447 -0.0450 0.0696  0.0046  277 PRO A N   
4331 C CA  . PRO A 292 ? 0.3922 0.3865 0.5172 -0.0472 0.0751  0.0105  277 PRO A CA  
4332 C C   . PRO A 292 ? 0.3451 0.3129 0.4306 -0.0361 0.0715  0.0213  277 PRO A C   
4333 O O   . PRO A 292 ? 0.4480 0.4221 0.5251 -0.0296 0.0696  0.0237  277 PRO A O   
4334 C CB  . PRO A 292 ? 0.4376 0.4206 0.5703 -0.0608 0.0978  0.0090  277 PRO A CB  
4335 C CG  . PRO A 292 ? 0.4335 0.4385 0.5815 -0.0613 0.1054  0.0062  277 PRO A CG  
4336 C CD  . PRO A 292 ? 0.4241 0.4648 0.5938 -0.0534 0.0865  0.0004  277 PRO A CD  
4344 N N   . GLY A 293 ? 0.3790 0.3172 0.4407 -0.0333 0.0699  0.0268  278 GLY A N   
4345 C CA  . GLY A 293 ? 0.3888 0.3003 0.4117 -0.0222 0.0658  0.0363  278 GLY A CA  
4346 C C   . GLY A 293 ? 0.4013 0.3247 0.4195 -0.0100 0.0450  0.0355  278 GLY A C   
4347 O O   . GLY A 293 ? 0.5155 0.4233 0.5051 -0.0002 0.0395  0.0412  278 GLY A O   
4351 N N   . LEU A 294 ? 0.3822 0.3328 0.4270 -0.0105 0.0337  0.0279  279 LEU A N   
4352 C CA  . LEU A 294 ? 0.3325 0.2937 0.3745 -0.0006 0.0162  0.0262  279 LEU A CA  
4353 C C   . LEU A 294 ? 0.3836 0.3291 0.4187 0.0032  0.0093  0.0261  279 LEU A C   
4354 O O   . LEU A 294 ? 0.3476 0.2987 0.4010 -0.0030 0.0101  0.0208  279 LEU A O   
4355 C CB  . LEU A 294 ? 0.3333 0.3286 0.4030 -0.0025 0.0090  0.0188  279 LEU A CB  
4356 C CG  . LEU A 294 ? 0.3164 0.3283 0.3966 -0.0049 0.0153  0.0182  279 LEU A CG  
4357 C CD1 . LEU A 294 ? 0.3018 0.3421 0.4025 -0.0034 0.0057  0.0128  279 LEU A CD1 
4358 C CD2 . LEU A 294 ? 0.2912 0.2897 0.3473 0.0011  0.0178  0.0237  279 LEU A CD2 
4370 N N   . ASN A 295 ? 0.3515 0.2775 0.3606 0.0140  0.0022  0.0312  280 ASN A N   
4371 C CA  . ASN A 295 ? 0.4223 0.3329 0.4243 0.0207  -0.0057 0.0311  280 ASN A CA  
4372 C C   . ASN A 295 ? 0.3851 0.2911 0.3674 0.0349  -0.0195 0.0330  280 ASN A C   
4373 O O   . ASN A 295 ? 0.3693 0.2780 0.3390 0.0383  -0.0209 0.0352  280 ASN A O   
4374 C CB  . ASN A 295 ? 0.3984 0.2742 0.3846 0.0175  0.0064  0.0373  280 ASN A CB  
4375 C CG  . ASN A 295 ? 0.4940 0.3414 0.4462 0.0210  0.0149  0.0477  280 ASN A CG  
4376 O OD1 . ASN A 295 ? 0.4714 0.3067 0.3980 0.0339  0.0050  0.0522  280 ASN A OD1 
4377 N ND2 . ASN A 295 ? 0.5284 0.3655 0.4801 0.0095  0.0334  0.0506  280 ASN A ND2 
4384 N N   . ARG A 296 ? 0.3155 0.2669 0.4606 0.0321  0.0927  0.1120  281 ARG A N   
4385 C CA  . ARG A 296 ? 0.3033 0.2426 0.4515 0.0330  0.0848  0.1159  281 ARG A CA  
4386 C C   . ARG A 296 ? 0.3297 0.2470 0.4409 0.0327  0.0845  0.1171  281 ARG A C   
4387 O O   . ARG A 296 ? 0.3601 0.2808 0.4664 0.0322  0.0737  0.1037  281 ARG A O   
4388 C CB  . ARG A 296 ? 0.2965 0.2469 0.4497 0.0363  0.0650  0.1179  281 ARG A CB  
4389 C CG  . ARG A 296 ? 0.3177 0.2600 0.4404 0.0383  0.0570  0.1258  281 ARG A CG  
4390 C CD  . ARG A 296 ? 0.3504 0.3075 0.4804 0.0390  0.0409  0.1231  281 ARG A CD  
4391 N NE  . ARG A 296 ? 0.2822 0.2295 0.3841 0.0407  0.0332  0.1290  281 ARG A NE  
4392 C CZ  . ARG A 296 ? 0.3122 0.2467 0.3939 0.0455  0.0186  0.1358  281 ARG A CZ  
4393 N NH1 . ARG A 296 ? 0.3614 0.2933 0.4493 0.0503  0.0076  0.1373  281 ARG A NH1 
4394 N NH2 . ARG A 296 ? 0.3659 0.2920 0.4223 0.0460  0.0134  0.1400  281 ARG A NH2 
4408 N N   . GLY A 297 ? 0.3147 0.2177 0.3956 0.0324  0.0925  0.1260  282 GLY A N   
4409 C CA  . GLY A 297 ? 0.3832 0.2741 0.4238 0.0308  0.0910  0.1194  282 GLY A CA  
4410 C C   . GLY A 297 ? 0.3994 0.2918 0.4427 0.0260  0.0990  0.1023  282 GLY A C   
4411 O O   . GLY A 297 ? 0.3874 0.2766 0.4073 0.0253  0.0899  0.0910  282 GLY A O   
4415 N N   . LEU A 298 ? 0.3698 0.2672 0.4423 0.0226  0.1161  0.1000  283 LEU A N   
4416 C CA  . LEU A 298 ? 0.3789 0.2779 0.4570 0.0180  0.1247  0.0836  283 LEU A CA  
4417 C C   . LEU A 298 ? 0.3963 0.3062 0.4868 0.0187  0.1078  0.0695  283 LEU A C   
4418 O O   . LEU A 298 ? 0.4001 0.3080 0.4779 0.0159  0.1065  0.0546  283 LEU A O   
4419 C CB  . LEU A 298 ? 0.3569 0.2609 0.4690 0.0148  0.1449  0.0851  283 LEU A CB  
4420 C CG  . LEU A 298 ? 0.3300 0.2256 0.4311 0.0143  0.1606  0.0955  283 LEU A CG  
4421 C CD1 . LEU A 298 ? 0.3881 0.3028 0.5173 0.0187  0.1576  0.0845  283 LEU A CD1 
4422 C CD2 . LEU A 298 ? 0.5132 0.3925 0.5813 0.0100  0.1740  0.0913  283 LEU A CD2 
4434 N N   . ILE A 299 ? 0.2987 0.2205 0.4144 0.0223  0.0948  0.0738  284 ILE A N   
4435 C CA  . ILE A 299 ? 0.2937 0.2268 0.4241 0.0233  0.0785  0.0614  284 ILE A CA  
4436 C C   . ILE A 299 ? 0.3236 0.2519 0.4209 0.0263  0.0578  0.0592  284 ILE A C   
4437 O O   . ILE A 299 ? 0.3552 0.2877 0.4498 0.0257  0.0463  0.0451  284 ILE A O   
4438 C CB  . ILE A 299 ? 0.3288 0.2772 0.5013 0.0259  0.0741  0.0665  284 ILE A CB  
4439 C CG1 . ILE A 299 ? 0.2658 0.2199 0.4720 0.0227  0.0943  0.0679  284 ILE A CG1 
4440 C CG2 . ILE A 299 ? 0.2520 0.2122 0.4404 0.0271  0.0568  0.0542  284 ILE A CG2 
4441 C CD1 . ILE A 299 ? 0.2884 0.2419 0.5001 0.0175  0.1061  0.0528  284 ILE A CD1 
4453 N N   . LEU A 300 ? 0.3493 0.2694 0.4222 0.0297  0.0524  0.0729  285 LEU A N   
4454 C CA  . LEU A 300 ? 0.3686 0.2824 0.4059 0.0323  0.0346  0.0714  285 LEU A CA  
4455 C C   . LEU A 300 ? 0.4050 0.3103 0.4119 0.0285  0.0379  0.0581  285 LEU A C   
4456 O O   . LEU A 300 ? 0.4263 0.3329 0.4174 0.0292  0.0221  0.0479  285 LEU A O   
4457 C CB  . LEU A 300 ? 0.3855 0.2896 0.3996 0.0359  0.0324  0.0891  285 LEU A CB  
4458 C CG  . LEU A 300 ? 0.3501 0.2622 0.3894 0.0403  0.0249  0.1019  285 LEU A CG  
4459 C CD1 . LEU A 300 ? 0.4235 0.3245 0.4365 0.0436  0.0226  0.1183  285 LEU A CD1 
4460 C CD2 . LEU A 300 ? 0.3619 0.2864 0.4178 0.0434  0.0040  0.0951  285 LEU A CD2 
4472 N N   . ASP A 301 ? 0.4226 0.3196 0.4217 0.0244  0.0586  0.0576  286 ASP A N   
4473 C CA  . ASP A 301 ? 0.4458 0.3355 0.4189 0.0205  0.0636  0.0435  286 ASP A CA  
4474 C C   . ASP A 301 ? 0.4946 0.3950 0.4892 0.0181  0.0578  0.0247  286 ASP A C   
4475 O O   . ASP A 301 ? 0.4684 0.3668 0.4407 0.0171  0.0479  0.0118  286 ASP A O   
4476 C CB  . ASP A 301 ? 0.4737 0.3540 0.4417 0.0164  0.0884  0.0461  286 ASP A CB  
4477 C CG  . ASP A 301 ? 0.7527 0.6181 0.6813 0.0175  0.0932  0.0587  286 ASP A CG  
4478 O OD1 . ASP A 301 ? 0.9259 0.7860 0.8216 0.0202  0.0781  0.0601  286 ASP A OD1 
4479 O OD2 . ASP A 301 ? 0.7289 0.5878 0.6597 0.0158  0.1122  0.0676  286 ASP A OD2 
4484 N N   . LEU A 302 ? 0.4978 0.4098 0.5362 0.0171  0.0639  0.0229  287 LEU A N   
4485 C CA  . LEU A 302 ? 0.3935 0.3164 0.4568 0.0149  0.0591  0.0058  287 LEU A CA  
4486 C C   . LEU A 302 ? 0.3996 0.3297 0.4597 0.0184  0.0340  0.0006  287 LEU A C   
4487 O O   . LEU A 302 ? 0.4156 0.3486 0.4716 0.0167  0.0256  -0.0155 287 LEU A O   
4488 C CB  . LEU A 302 ? 0.4096 0.3440 0.5211 0.0139  0.0704  0.0082  287 LEU A CB  
4489 C CG  . LEU A 302 ? 0.3357 0.2818 0.4802 0.0111  0.0705  -0.0080 287 LEU A CG  
4490 C CD1 . LEU A 302 ? 0.3587 0.2980 0.4915 0.0057  0.0831  -0.0227 287 LEU A CD1 
4491 C CD2 . LEU A 302 ? 0.2926 0.2498 0.4824 0.0112  0.0806  -0.0011 287 LEU A CD2 
4503 N N   . LEU A 303 ? 0.3874 0.3203 0.4496 0.0235  0.0218  0.0141  288 LEU A N   
4504 C CA  . LEU A 303 ? 0.3906 0.3309 0.4526 0.0272  -0.0022 0.0104  288 LEU A CA  
4505 C C   . LEU A 303 ? 0.4342 0.3652 0.4512 0.0278  -0.0150 0.0055  288 LEU A C   
4506 O O   . LEU A 303 ? 0.4451 0.3819 0.4598 0.0287  -0.0325 -0.0053 288 LEU A O   
4507 C CB  . LEU A 303 ? 0.3723 0.3177 0.4490 0.0324  -0.0106 0.0266  288 LEU A CB  
4508 C CG  . LEU A 303 ? 0.3485 0.3054 0.4712 0.0324  -0.0009 0.0316  288 LEU A CG  
4509 C CD1 . LEU A 303 ? 0.3007 0.2638 0.4363 0.0379  -0.0134 0.0447  288 LEU A CD1 
4510 C CD2 . LEU A 303 ? 0.3200 0.2891 0.4753 0.0298  -0.0009 0.0162  288 LEU A CD2 
4522 N N   . ASP A 304 ? 0.4600 0.3770 0.4410 0.0274  -0.0068 0.0134  289 ASP A N   
4523 C CA  . ASP A 304 ? 0.5121 0.4202 0.4491 0.0274  -0.0166 0.0073  289 ASP A CA  
4524 C C   . ASP A 304 ? 0.5327 0.4421 0.4670 0.0226  -0.0138 -0.0135 289 ASP A C   
4525 O O   . ASP A 304 ? 0.5434 0.4550 0.4622 0.0230  -0.0303 -0.0248 289 ASP A O   
4526 C CB  . ASP A 304 ? 0.5271 0.4199 0.4282 0.0274  -0.0052 0.0198  289 ASP A CB  
4527 C CG  . ASP A 304 ? 0.6914 0.5746 0.5464 0.0263  -0.0110 0.0123  289 ASP A CG  
4528 O OD1 . ASP A 304 ? 0.7055 0.5907 0.5437 0.0295  -0.0319 0.0104  289 ASP A OD1 
4529 O OD2 . ASP A 304 ? 0.7548 0.6288 0.5905 0.0225  0.0053  0.0081  289 ASP A OD2 
4534 N N   . LYS A 305 ? 0.5103 0.4186 0.4605 0.0180  0.0070  -0.0191 290 LYS A N   
4535 C CA  . LYS A 305 ? 0.5228 0.4332 0.4760 0.0133  0.0110  -0.0395 290 LYS A CA  
4536 C C   . LYS A 305 ? 0.5399 0.4646 0.5219 0.0140  -0.0054 -0.0515 290 LYS A C   
4537 O O   . LYS A 305 ? 0.5308 0.4569 0.5004 0.0124  -0.0157 -0.0675 290 LYS A O   
4538 C CB  . LYS A 305 ? 0.5061 0.4149 0.4806 0.0087  0.0362  -0.0415 290 LYS A CB  
4539 C CG  . LYS A 305 ? 0.5868 0.4948 0.5599 0.0033  0.0440  -0.0619 290 LYS A CG  
4540 C CD  . LYS A 305 ? 0.5254 0.4319 0.5219 -0.0008 0.0693  -0.0622 290 LYS A CD  
4541 C CE  . LYS A 305 ? 0.6004 0.5078 0.6033 -0.0061 0.0769  -0.0832 290 LYS A CE  
4542 N NZ  . LYS A 305 ? 0.5692 0.4784 0.6055 -0.0097 0.0997  -0.0832 290 LYS A NZ  
4556 N N   . LEU A 306 ? 0.4977 0.4332 0.5178 0.0165  -0.0084 -0.0440 291 LEU A N   
4557 C CA  . LEU A 306 ? 0.4516 0.4014 0.5025 0.0173  -0.0229 -0.0545 291 LEU A CA  
4558 C C   . LEU A 306 ? 0.5392 0.4900 0.5664 0.0205  -0.0478 -0.0584 291 LEU A C   
4559 O O   . LEU A 306 ? 0.5471 0.5051 0.5822 0.0194  -0.0594 -0.0740 291 LEU A O   
4560 C CB  . LEU A 306 ? 0.4312 0.3917 0.5235 0.0200  -0.0214 -0.0432 291 LEU A CB  
4561 C CG  . LEU A 306 ? 0.4889 0.4648 0.6155 0.0217  -0.0367 -0.0506 291 LEU A CG  
4562 C CD1 . LEU A 306 ? 0.3766 0.3595 0.5307 0.0169  -0.0282 -0.0677 291 LEU A CD1 
4563 C CD2 . LEU A 306 ? 0.3914 0.3759 0.5486 0.0256  -0.0375 -0.0357 291 LEU A CD2 
4575 N N   . LYS A 307 ? 0.5472 0.4911 0.5463 0.0247  -0.0565 -0.0442 292 LYS A N   
4576 C CA  . LYS A 307 ? 0.6030 0.5490 0.5836 0.0286  -0.0810 -0.0451 292 LYS A CA  
4577 C C   . LYS A 307 ? 0.6029 0.5394 0.5373 0.0272  -0.0874 -0.0537 292 LYS A C   
4578 O O   . LYS A 307 ? 0.7146 0.6553 0.6385 0.0288  -0.1074 -0.0621 292 LYS A O   
4579 C CB  . LYS A 307 ? 0.6510 0.5954 0.6269 0.0342  -0.0888 -0.0251 292 LYS A CB  
4580 C CG  . LYS A 307 ? 0.7784 0.7352 0.7995 0.0368  -0.0905 -0.0180 292 LYS A CG  
4581 C CD  . LYS A 307 ? 0.8139 0.7848 0.8625 0.0372  -0.1062 -0.0315 292 LYS A CD  
4582 C CE  . LYS A 307 ? 0.8581 0.8410 0.9451 0.0411  -0.1125 -0.0229 292 LYS A CE  
4583 N NZ  . LYS A 307 ? 0.8146 0.8072 0.9451 0.0384  -0.0979 -0.0270 292 LYS A NZ  
4597 N N   . ASN A 308 ? 0.6798 0.6040 0.5865 0.0243  -0.0711 -0.0523 293 ASN A N   
4598 C CA  . ASN A 308 ? 0.6949 0.6090 0.5532 0.0237  -0.0768 -0.0572 293 ASN A CA  
4599 C C   . ASN A 308 ? 0.6805 0.5894 0.5263 0.0179  -0.0624 -0.0732 293 ASN A C   
4600 O O   . ASN A 308 ? 0.8666 0.7678 0.6719 0.0170  -0.0668 -0.0793 293 ASN A O   
4601 C CB  . ASN A 308 ? 0.6950 0.5970 0.5204 0.0267  -0.0734 -0.0379 293 ASN A CB  
4602 C CG  . ASN A 308 ? 0.8270 0.7328 0.6571 0.0328  -0.0906 -0.0228 293 ASN A CG  
4603 O OD1 . ASN A 308 ? 0.7110 0.6217 0.5720 0.0348  -0.0865 -0.0117 293 ASN A OD1 
4604 N ND2 . ASN A 308 ? 0.9830 0.8868 0.7824 0.0359  -0.1101 -0.0224 293 ASN A ND2 
4611 N N   . GLY A 309 ? 0.6656 0.5786 0.5445 0.0139  -0.0455 -0.0804 294 GLY A N   
4612 C CA  . GLY A 309 ? 0.6817 0.5893 0.5510 0.0083  -0.0302 -0.0952 294 GLY A CA  
4613 C C   . GLY A 309 ? 0.7686 0.6640 0.6226 0.0064  -0.0071 -0.0851 294 GLY A C   
4614 O O   . GLY A 309 ? 0.8899 0.7790 0.7309 0.0095  -0.0045 -0.0666 294 GLY A O   
4618 N N   . ASN A 310 ? 1.0908 0.9829 0.9471 0.0011  0.0101  -0.0978 295 ASN A N   
4619 C CA  . ASN A 310 ? 1.1865 1.0684 1.0364 -0.0012 0.0343  -0.0895 295 ASN A CA  
4620 C C   . ASN A 310 ? 1.2093 1.0776 1.0094 0.0006  0.0347  -0.0786 295 ASN A C   
4621 O O   . ASN A 310 ? 1.2487 1.1114 1.0450 0.0029  0.0423  -0.0599 295 ASN A O   
4622 C CB  . ASN A 310 ? 1.2375 1.1182 1.0965 -0.0072 0.0512  -0.1072 295 ASN A CB  
4623 C CG  . ASN A 310 ? 1.2599 1.1352 1.1349 -0.0097 0.0772  -0.0988 295 ASN A CG  
4624 O OD1 . ASN A 310 ? 1.2151 1.0857 1.0864 -0.0072 0.0834  -0.0800 295 ASN A OD1 
4625 N ND2 . ASN A 310 ? 1.2385 1.1149 1.1323 -0.0147 0.0925  -0.1129 295 ASN A ND2 
4632 N N   . SER A 311 ? 1.1123 0.9756 0.8741 -0.0004 0.0266  -0.0899 296 SER A N   
4633 C CA  . SER A 311 ? 1.2439 1.0944 0.9560 0.0011  0.0273  -0.0807 296 SER A CA  
4634 C C   . SER A 311 ? 1.1766 1.0259 0.8804 0.0070  0.0151  -0.0596 296 SER A C   
4635 O O   . SER A 311 ? 1.0925 0.9502 0.8049 0.0105  -0.0058 -0.0587 296 SER A O   
4636 C CB  . SER A 311 ? 1.1594 1.0077 0.8339 -0.0001 0.0150  -0.0968 296 SER A CB  
4637 O OG  . SER A 311 ? 1.1340 0.9852 0.8208 -0.0054 0.0236  -0.1181 296 SER A OG  
4643 N N   . ILE B 23  ? 1.0985 0.9624 0.8353 0.0739  0.0155  -0.1794 8   ILE B N   
4644 C CA  . ILE B 23  ? 1.1266 1.0040 0.8611 0.0458  0.0100  -0.1628 8   ILE B CA  
4645 C C   . ILE B 23  ? 1.1324 0.9676 0.8023 0.0309  0.0056  -0.1661 8   ILE B C   
4646 O O   . ILE B 23  ? 1.2905 1.0944 0.9196 0.0434  0.0140  -0.1814 8   ILE B O   
4647 C CB  . ILE B 23  ? 1.1168 1.0450 0.8869 0.0432  0.0251  -0.1540 8   ILE B CB  
4648 C CG1 . ILE B 23  ? 1.0951 1.0619 0.9236 0.0597  0.0312  -0.1541 8   ILE B CG1 
4649 C CG2 . ILE B 23  ? 0.9762 0.9209 0.7520 0.0166  0.0170  -0.1344 8   ILE B CG2 
4650 C CD1 . ILE B 23  ? 1.0437 1.0597 0.9091 0.0535  0.0442  -0.1435 8   ILE B CD1 
4661 N N   . PHE B 24  ? 1.2745 1.1086 0.9340 0.0043  -0.0077 -0.1514 9   PHE B N   
4662 C CA  . PHE B 24  ? 1.2754 1.0760 0.8764 -0.0155 -0.0140 -0.1510 9   PHE B CA  
4663 C C   . PHE B 24  ? 1.2579 1.0909 0.8636 -0.0319 -0.0078 -0.1377 9   PHE B C   
4664 O O   . PHE B 24  ? 1.2203 1.0943 0.8701 -0.0392 -0.0095 -0.1217 9   PHE B O   
4665 C CB  . PHE B 24  ? 1.3268 1.1019 0.9086 -0.0357 -0.0363 -0.1434 9   PHE B CB  
4666 C CG  . PHE B 24  ? 1.4490 1.1772 1.0059 -0.0243 -0.0441 -0.1574 9   PHE B CG  
4667 C CD1 . PHE B 24  ? 1.4626 1.1761 1.0198 0.0051  -0.0323 -0.1749 9   PHE B CD1 
4668 C CD2 . PHE B 24  ? 1.4075 1.1069 0.9396 -0.0434 -0.0636 -0.1521 9   PHE B CD2 
4669 C CE1 . PHE B 24  ? 1.4901 1.1573 1.0215 0.0165  -0.0402 -0.1871 9   PHE B CE1 
4670 C CE2 . PHE B 24  ? 1.4202 1.0727 0.9257 -0.0345 -0.0714 -0.1643 9   PHE B CE2 
4671 C CZ  . PHE B 24  ? 1.5199 1.1542 1.0239 -0.0039 -0.0599 -0.1819 9   PHE B CZ  
4681 N N   . ASN B 25  ? 1.2064 1.0180 0.7635 -0.0372 -0.0006 -0.1442 10  ASN B N   
4682 C CA  . ASN B 25  ? 1.2119 1.0481 0.7639 -0.0536 0.0049  -0.1322 10  ASN B CA  
4683 C C   . ASN B 25  ? 1.2773 1.0933 0.7878 -0.0828 -0.0127 -0.1217 10  ASN B C   
4684 O O   . ASN B 25  ? 1.3001 1.1092 0.7734 -0.0960 -0.0094 -0.1198 10  ASN B O   
4685 C CB  . ASN B 25  ? 1.2416 1.0732 0.7693 -0.0405 0.0262  -0.1452 10  ASN B CB  
4686 C CG  . ASN B 25  ? 1.2942 1.1684 0.8752 -0.0187 0.0447  -0.1477 10  ASN B CG  
4687 O OD1 . ASN B 25  ? 1.2788 1.1543 0.8857 0.0024  0.0475  -0.1572 10  ASN B OD1 
4688 N ND2 . ASN B 25  ? 1.2172 1.1271 0.8142 -0.0250 0.0568  -0.1383 10  ASN B ND2 
4695 N N   . ARG B 26  ? 1.2735 1.0816 0.7897 -0.0942 -0.0317 -0.1141 11  ARG B N   
4696 C CA  . ARG B 26  ? 1.3450 1.1410 0.8285 -0.1234 -0.0505 -0.1020 11  ARG B CA  
4697 C C   . ARG B 26  ? 1.2640 1.1073 0.7953 -0.1353 -0.0600 -0.0787 11  ARG B C   
4698 O O   . ARG B 26  ? 1.2289 1.1069 0.8145 -0.1213 -0.0530 -0.0733 11  ARG B O   
4699 C CB  . ARG B 26  ? 1.3507 1.0986 0.7973 -0.1295 -0.0657 -0.1109 11  ARG B CB  
4700 C CG  . ARG B 26  ? 1.4757 1.1701 0.8746 -0.1133 -0.0570 -0.1348 11  ARG B CG  
4701 C CD  . ARG B 26  ? 1.5368 1.1840 0.9050 -0.1187 -0.0730 -0.1417 11  ARG B CD  
4702 N NE  . ARG B 26  ? 1.5648 1.2047 0.9061 -0.1529 -0.0937 -0.1277 11  ARG B NE  
4703 C CZ  . ARG B 26  ? 1.5803 1.1753 0.8535 -0.1738 -0.1024 -0.1322 11  ARG B CZ  
4704 N NH1 . ARG B 26  ? 1.6414 1.1884 0.8613 -0.1628 -0.0919 -0.1514 11  ARG B NH1 
4705 N NH2 . ARG B 26  ? 1.6210 1.2197 0.8782 -0.2065 -0.1223 -0.1169 11  ARG B NH2 
4719 N N   . ASP B 27  ? 1.2319 1.0757 0.7409 -0.1615 -0.0765 -0.0647 12  ASP B N   
4720 C CA  . ASP B 27  ? 1.1201 1.0034 0.6699 -0.1718 -0.0884 -0.0429 12  ASP B CA  
4721 C C   . ASP B 27  ? 1.0600 0.9305 0.6227 -0.1692 -0.0997 -0.0454 12  ASP B C   
4722 O O   . ASP B 27  ? 1.0358 0.8669 0.5557 -0.1806 -0.1105 -0.0534 12  ASP B O   
4723 C CB  . ASP B 27  ? 1.1378 1.0315 0.6611 -0.2000 -0.1026 -0.0258 12  ASP B CB  
4724 C CG  . ASP B 27  ? 1.0260 0.9695 0.5959 -0.2059 -0.1106 -0.0013 12  ASP B CG  
4725 O OD1 . ASP B 27  ? 0.9689 0.9246 0.5752 -0.1981 -0.1150 0.0026  12  ASP B OD1 
4726 O OD2 . ASP B 27  ? 1.0849 1.0544 0.6537 -0.2171 -0.1123 0.0142  12  ASP B OD2 
4731 N N   . PRO B 28  ? 1.1044 1.0030 0.7213 -0.1553 -0.0974 -0.0393 13  PRO B N   
4732 C CA  . PRO B 28  ? 0.9625 0.8471 0.5894 -0.1528 -0.1077 -0.0420 13  PRO B CA  
4733 C C   . PRO B 28  ? 1.0240 0.9061 0.6301 -0.1788 -0.1274 -0.0292 13  PRO B C   
4734 O O   . PRO B 28  ? 0.9553 0.8096 0.5461 -0.1827 -0.1372 -0.0353 13  PRO B O   
4735 C CB  . PRO B 28  ? 0.9011 0.8234 0.5902 -0.1361 -0.1015 -0.0337 13  PRO B CB  
4736 C CG  . PRO B 28  ? 0.8663 0.8258 0.5744 -0.1391 -0.0946 -0.0193 13  PRO B CG  
4737 C CD  . PRO B 28  ? 0.8909 0.8330 0.5589 -0.1432 -0.0866 -0.0286 13  PRO B CD  
4745 N N   . ARG B 29  ? 1.0210 0.9328 0.6260 -0.1973 -0.1340 -0.0107 14  ARG B N   
4746 C CA  . ARG B 29  ? 1.0400 0.9569 0.6276 -0.2238 -0.1533 0.0034  14  ARG B CA  
4747 C C   . ARG B 29  ? 1.0658 0.9320 0.5884 -0.2427 -0.1631 -0.0089 14  ARG B C   
4748 O O   . ARG B 29  ? 1.0392 0.9014 0.5434 -0.2659 -0.1801 -0.0003 14  ARG B O   
4749 C CB  . ARG B 29  ? 0.9361 0.8985 0.5367 -0.2375 -0.1579 0.0262  14  ARG B CB  
4750 C CG  . ARG B 29  ? 0.8763 0.8864 0.5376 -0.2230 -0.1534 0.0423  14  ARG B CG  
4751 C CD  . ARG B 29  ? 0.8646 0.9184 0.5381 -0.2336 -0.1580 0.0657  14  ARG B CD  
4752 N NE  . ARG B 29  ? 0.9769 1.0295 0.6356 -0.2310 -0.1474 0.0631  14  ARG B NE  
4753 C CZ  . ARG B 29  ? 1.0554 1.1433 0.7346 -0.2288 -0.1440 0.0801  14  ARG B CZ  
4754 N NH1 . ARG B 29  ? 0.9624 1.0900 0.6796 -0.2257 -0.1491 0.1006  14  ARG B NH1 
4755 N NH2 . ARG B 29  ? 0.9968 1.0787 0.6562 -0.2286 -0.1345 0.0764  14  ARG B NH2 
4769 N N   . ASP B 30  ? 1.0816 0.9082 0.5678 -0.2335 -0.1525 -0.0285 15  ASP B N   
4770 C CA  . ASP B 30  ? 1.1815 0.9488 0.6028 -0.2466 -0.1603 -0.0434 15  ASP B CA  
4771 C C   . ASP B 30  ? 1.1597 0.8980 0.5807 -0.2417 -0.1671 -0.0517 15  ASP B C   
4772 O O   . ASP B 30  ? 1.2827 0.9815 0.6563 -0.2622 -0.1812 -0.0551 15  ASP B O   
4773 C CB  . ASP B 30  ? 1.2089 0.9394 0.5947 -0.2310 -0.1445 -0.0641 15  ASP B CB  
4774 C CG  . ASP B 30  ? 1.2355 0.9916 0.6177 -0.2359 -0.1366 -0.0568 15  ASP B CG  
4775 O OD1 . ASP B 30  ? 1.2507 1.0469 0.6492 -0.2543 -0.1461 -0.0358 15  ASP B OD1 
4776 O OD2 . ASP B 30  ? 1.1951 0.9320 0.5580 -0.2205 -0.1204 -0.0717 15  ASP B OD2 
4781 N N   . HIS B 31  ? 1.0742 0.8299 0.5455 -0.2161 -0.1581 -0.0545 16  HIS B N   
4782 C CA  . HIS B 31  ? 1.0758 0.8022 0.5476 -0.2075 -0.1628 -0.0637 16  HIS B CA  
4783 C C   . HIS B 31  ? 1.0405 0.8032 0.5563 -0.2135 -0.1723 -0.0468 16  HIS B C   
4784 O O   . HIS B 31  ? 1.0354 0.7724 0.5437 -0.2141 -0.1800 -0.0514 16  HIS B O   
4785 C CB  . HIS B 31  ? 1.0642 0.7775 0.5556 -0.1725 -0.1460 -0.0818 16  HIS B CB  
4786 C CG  . HIS B 31  ? 1.1310 0.8040 0.5777 -0.1618 -0.1350 -0.1010 16  HIS B CG  
4787 N ND1 . HIS B 31  ? 1.2730 0.8931 0.6878 -0.1451 -0.1320 -0.1213 16  HIS B ND1 
4788 C CD2 . HIS B 31  ? 1.2198 0.8975 0.6475 -0.1637 -0.1256 -0.1029 16  HIS B CD2 
4789 C CE1 . HIS B 31  ? 1.1999 0.7944 0.5780 -0.1363 -0.1204 -0.1350 16  HIS B CE1 
4790 N NE2 . HIS B 31  ? 1.2542 0.8829 0.6391 -0.1481 -0.1162 -0.1244 16  HIS B NE2 
4798 N N   . TYR B 32  ? 0.9808 0.8003 0.5398 -0.2169 -0.1716 -0.0273 17  TYR B N   
4799 C CA  . TYR B 32  ? 0.9352 0.7912 0.5371 -0.2190 -0.1783 -0.0110 17  TYR B CA  
4800 C C   . TYR B 32  ? 0.9223 0.8244 0.5345 -0.2409 -0.1874 0.0128  17  TYR B C   
4801 O O   . TYR B 32  ? 0.9890 0.9070 0.5938 -0.2460 -0.1842 0.0182  17  TYR B O   
4802 C CB  . TYR B 32  ? 0.8805 0.7630 0.5390 -0.1900 -0.1648 -0.0117 17  TYR B CB  
4803 C CG  . TYR B 32  ? 0.8979 0.7440 0.5544 -0.1663 -0.1560 -0.0333 17  TYR B CG  
4804 C CD1 . TYR B 32  ? 0.9005 0.7334 0.5496 -0.1494 -0.1420 -0.0480 17  TYR B CD1 
4805 C CD2 . TYR B 32  ? 0.8819 0.7092 0.5445 -0.1604 -0.1616 -0.0382 17  TYR B CD2 
4806 C CE1 . TYR B 32  ? 0.9070 0.7119 0.5569 -0.1263 -0.1341 -0.0667 17  TYR B CE1 
4807 C CE2 . TYR B 32  ? 0.8893 0.6853 0.5507 -0.1377 -0.1546 -0.0569 17  TYR B CE2 
4808 C CZ  . TYR B 32  ? 0.9014 0.6878 0.5576 -0.1202 -0.1410 -0.0709 17  TYR B CZ  
4809 O OH  . TYR B 32  ? 0.9092 0.6693 0.5664 -0.0962 -0.1341 -0.0886 17  TYR B OH  
4819 N N   . ASP B 33  ? 1.0062 0.9311 0.6354 -0.2531 -0.1987 0.0276  18  ASP B N   
4820 C CA  . ASP B 33  ? 0.9022 0.8812 0.5537 -0.2684 -0.2065 0.0527  18  ASP B CA  
4821 C C   . ASP B 33  ? 0.8259 0.8479 0.5379 -0.2451 -0.1966 0.0636  18  ASP B C   
4822 O O   . ASP B 33  ? 0.7998 0.8165 0.5345 -0.2316 -0.1940 0.0594  18  ASP B O   
4823 C CB  . ASP B 33  ? 0.9523 0.9353 0.5864 -0.2966 -0.2244 0.0641  18  ASP B CB  
4824 C CG  . ASP B 33  ? 1.1308 1.0704 0.7001 -0.3245 -0.2364 0.0557  18  ASP B CG  
4825 O OD1 . ASP B 33  ? 1.1395 1.0673 0.6812 -0.3288 -0.2339 0.0508  18  ASP B OD1 
4826 O OD2 . ASP B 33  ? 1.2047 1.1196 0.7479 -0.3431 -0.2484 0.0541  18  ASP B OD2 
4831 N N   . LEU B 34  ? 0.8015 0.8622 0.5361 -0.2404 -0.1914 0.0772  19  LEU B N   
4832 C CA  . LEU B 34  ? 0.7892 0.8895 0.5763 -0.2206 -0.1835 0.0902  19  LEU B CA  
4833 C C   . LEU B 34  ? 0.7351 0.8719 0.5410 -0.2316 -0.1944 0.1104  19  LEU B C   
4834 O O   . LEU B 34  ? 0.7519 0.9124 0.5437 -0.2543 -0.2066 0.1254  19  LEU B O   
4835 C CB  . LEU B 34  ? 0.7392 0.8667 0.5404 -0.2131 -0.1753 0.0999  19  LEU B CB  
4836 C CG  . LEU B 34  ? 0.7960 0.8977 0.5888 -0.1988 -0.1610 0.0826  19  LEU B CG  
4837 C CD1 . LEU B 34  ? 0.7437 0.8759 0.5543 -0.1918 -0.1531 0.0957  19  LEU B CD1 
4838 C CD2 . LEU B 34  ? 0.7651 0.8448 0.5787 -0.1761 -0.1503 0.0660  19  LEU B CD2 
4850 N N   . LEU B 35  ? 0.7257 0.8682 0.5630 -0.2159 -0.1902 0.1109  20  LEU B N   
4851 C CA  . LEU B 35  ? 0.7430 0.9219 0.6020 -0.2222 -0.1977 0.1297  20  LEU B CA  
4852 C C   . LEU B 35  ? 0.7078 0.9340 0.6090 -0.2048 -0.1904 0.1489  20  LEU B C   
4853 O O   . LEU B 35  ? 0.7597 1.0293 0.6692 -0.2151 -0.1975 0.1703  20  LEU B O   
4854 C CB  . LEU B 35  ? 0.6798 0.8343 0.5434 -0.2161 -0.1976 0.1193  20  LEU B CB  
4855 C CG  . LEU B 35  ? 0.7276 0.8292 0.5473 -0.2305 -0.2048 0.1001  20  LEU B CG  
4856 C CD1 . LEU B 35  ? 0.8609 0.9450 0.6866 -0.2264 -0.2066 0.0946  20  LEU B CD1 
4857 C CD2 . LEU B 35  ? 0.7599 0.8618 0.5408 -0.2634 -0.2196 0.1068  20  LEU B CD2 
4869 N N   . GLN B 36  ? 0.6907 0.9088 0.6175 -0.1784 -0.1767 0.1421  21  GLN B N   
4870 C CA  . GLN B 36  ? 0.7552 1.0098 0.7170 -0.1606 -0.1691 0.1593  21  GLN B CA  
4871 C C   . GLN B 36  ? 0.7466 0.9797 0.7229 -0.1373 -0.1545 0.1471  21  GLN B C   
4872 O O   . GLN B 36  ? 0.6488 0.8451 0.6174 -0.1317 -0.1500 0.1266  21  GLN B O   
4873 C CB  . GLN B 36  ? 0.7363 1.0190 0.7243 -0.1544 -0.1708 0.1735  21  GLN B CB  
4874 C CG  . GLN B 36  ? 0.8363 1.0889 0.8285 -0.1459 -0.1678 0.1586  21  GLN B CG  
4875 C CD  . GLN B 36  ? 0.8468 1.1281 0.8633 -0.1395 -0.1681 0.1734  21  GLN B CD  
4876 O OE1 . GLN B 36  ? 0.8261 1.1369 0.8690 -0.1226 -0.1613 0.1885  21  GLN B OE1 
4877 N NE2 . GLN B 36  ? 0.8128 1.0840 0.8180 -0.1526 -0.1756 0.1694  21  GLN B NE2 
4886 N N   . ARG B 37  ? 0.7979 1.0554 0.7950 -0.1239 -0.1475 0.1611  22  ARG B N   
4887 C CA  . ARG B 37  ? 0.7663 1.0082 0.7787 -0.1036 -0.1339 0.1536  22  ARG B CA  
4888 C C   . ARG B 37  ? 0.6853 0.9244 0.7234 -0.0855 -0.1286 0.1537  22  ARG B C   
4889 O O   . ARG B 37  ? 0.7434 1.0102 0.7981 -0.0794 -0.1299 0.1712  22  ARG B O   
4890 C CB  . ARG B 37  ? 0.8172 1.0824 0.8351 -0.0990 -0.1298 0.1697  22  ARG B CB  
4891 C CG  . ARG B 37  ? 0.8252 1.0741 0.8529 -0.0830 -0.1163 0.1636  22  ARG B CG  
4892 C CD  . ARG B 37  ? 0.7784 1.0491 0.8047 -0.0822 -0.1145 0.1813  22  ARG B CD  
4893 N NE  . ARG B 37  ? 0.9236 1.1801 0.9578 -0.0688 -0.1020 0.1787  22  ARG B NE  
4894 C CZ  . ARG B 37  ? 0.9627 1.2191 1.0169 -0.0507 -0.0950 0.1868  22  ARG B CZ  
4895 N NH1 . ARG B 37  ? 0.9044 1.1738 0.9745 -0.0410 -0.0978 0.1966  22  ARG B NH1 
4896 N NH2 . ARG B 37  ? 0.8904 1.1320 0.9467 -0.0426 -0.0846 0.1850  22  ARG B NH2 
4910 N N   . LEU B 38  ? 0.6251 0.8317 0.6657 -0.0766 -0.1226 0.1346  23  LEU B N   
4911 C CA  . LEU B 38  ? 0.5345 0.7329 0.5951 -0.0610 -0.1184 0.1324  23  LEU B CA  
4912 C C   . LEU B 38  ? 0.6636 0.8583 0.7428 -0.0424 -0.1069 0.1348  23  LEU B C   
4913 O O   . LEU B 38  ? 0.6459 0.8400 0.7411 -0.0288 -0.1033 0.1394  23  LEU B O   
4914 C CB  . LEU B 38  ? 0.5726 0.7372 0.6248 -0.0621 -0.1201 0.1108  23  LEU B CB  
4915 C CG  . LEU B 38  ? 0.6491 0.8054 0.6774 -0.0804 -0.1315 0.1053  23  LEU B CG  
4916 C CD1 . LEU B 38  ? 0.6046 0.7243 0.6256 -0.0767 -0.1324 0.0848  23  LEU B CD1 
4917 C CD2 . LEU B 38  ? 0.7135 0.8983 0.7462 -0.0884 -0.1391 0.1233  23  LEU B CD2 
4929 N N   . GLY B 39  ? 0.6496 0.8396 0.7243 -0.0425 -0.1009 0.1318  24  GLY B N   
4930 C CA  . GLY B 39  ? 0.6483 0.8308 0.7367 -0.0281 -0.0904 0.1333  24  GLY B CA  
4931 C C   . GLY B 39  ? 0.6362 0.8136 0.7157 -0.0330 -0.0845 0.1282  24  GLY B C   
4932 O O   . GLY B 39  ? 0.6751 0.8400 0.7423 -0.0414 -0.0848 0.1125  24  GLY B O   
4936 N N   . GLY B 40  ? 0.8215 1.0075 0.9050 -0.0272 -0.0786 0.1417  25  GLY B N   
4937 C CA  . GLY B 40  ? 0.8266 1.0082 0.9014 -0.0320 -0.0718 0.1385  25  GLY B CA  
4938 C C   . GLY B 40  ? 0.8047 0.9732 0.8909 -0.0209 -0.0617 0.1400  25  GLY B C   
4939 O O   . GLY B 40  ? 0.8981 1.0560 0.9975 -0.0097 -0.0601 0.1398  25  GLY B O   
4943 N N   . GLY B 41  ? 0.8160 0.9833 0.8947 -0.0253 -0.0549 0.1415  26  GLY B N   
4944 C CA  . GLY B 41  ? 0.8580 1.0114 0.9436 -0.0181 -0.0457 0.1445  26  GLY B CA  
4945 C C   . GLY B 41  ? 0.8313 0.9814 0.9087 -0.0275 -0.0378 0.1376  26  GLY B C   
4946 O O   . GLY B 41  ? 0.7997 0.9580 0.8647 -0.0379 -0.0387 0.1309  26  GLY B O   
4950 N N   . THR B 42  ? 0.9641 1.1006 1.0465 -0.0243 -0.0295 0.1394  27  THR B N   
4951 C CA  . THR B 42  ? 0.9291 1.0642 1.0050 -0.0338 -0.0204 0.1346  27  THR B CA  
4952 C C   . THR B 42  ? 0.8519 0.9905 0.9311 -0.0402 -0.0182 0.1135  27  THR B C   
4953 O O   . THR B 42  ? 0.9081 1.0541 0.9758 -0.0492 -0.0130 0.1092  27  THR B O   
4954 C CB  . THR B 42  ? 0.9048 1.0222 0.9865 -0.0310 -0.0129 0.1386  27  THR B CB  
4955 O OG1 . THR B 42  ? 0.9606 1.0707 1.0352 -0.0224 -0.0145 0.1585  27  THR B OG1 
4956 C CG2 . THR B 42  ? 0.9113 1.0299 0.9866 -0.0428 -0.0029 0.1353  27  THR B CG2 
4964 N N   . TYR B 43  ? 0.7516 0.8840 0.8445 -0.0346 -0.0220 0.1005  28  TYR B N   
4965 C CA  . TYR B 43  ? 0.7555 0.8883 0.8543 -0.0368 -0.0189 0.0804  28  TYR B CA  
4966 C C   . TYR B 43  ? 0.6915 0.8258 0.7819 -0.0369 -0.0267 0.0701  28  TYR B C   
4967 O O   . TYR B 43  ? 0.6981 0.8292 0.7930 -0.0350 -0.0254 0.0531  28  TYR B O   
4968 C CB  . TYR B 43  ? 0.6481 0.7707 0.7676 -0.0309 -0.0173 0.0722  28  TYR B CB  
4969 C CG  . TYR B 43  ? 0.6791 0.7954 0.8033 -0.0333 -0.0101 0.0814  28  TYR B CG  
4970 C CD1 . TYR B 43  ? 0.6580 0.7815 0.7838 -0.0420 -0.0002 0.0774  28  TYR B CD1 
4971 C CD2 . TYR B 43  ? 0.7149 0.8166 0.8396 -0.0271 -0.0129 0.0943  28  TYR B CD2 
4972 C CE1 . TYR B 43  ? 0.6041 0.7191 0.7311 -0.0469 0.0059  0.0863  28  TYR B CE1 
4973 C CE2 . TYR B 43  ? 0.7078 0.7971 0.8314 -0.0300 -0.0067 0.1026  28  TYR B CE2 
4974 C CZ  . TYR B 43  ? 0.7058 0.8012 0.8301 -0.0412 0.0022  0.0987  28  TYR B CZ  
4975 O OH  . TYR B 43  ? 0.5985 0.6792 0.7189 -0.0467 0.0078  0.1073  28  TYR B OH  
4985 N N   . GLY B 44  ? 0.6321 0.7711 0.7094 -0.0393 -0.0348 0.0803  29  GLY B N   
4986 C CA  . GLY B 44  ? 0.7163 0.8538 0.7801 -0.0431 -0.0426 0.0713  29  GLY B CA  
4987 C C   . GLY B 44  ? 0.6665 0.8104 0.7247 -0.0447 -0.0535 0.0847  29  GLY B C   
4988 O O   . GLY B 44  ? 0.7310 0.8800 0.8001 -0.0386 -0.0551 0.0991  29  GLY B O   
4992 N N   . GLU B 45  ? 0.5501 0.6938 0.5891 -0.0533 -0.0610 0.0801  30  GLU B N   
4993 C CA  . GLU B 45  ? 0.5518 0.7044 0.5842 -0.0583 -0.0727 0.0912  30  GLU B CA  
4994 C C   . GLU B 45  ? 0.5484 0.6856 0.5714 -0.0614 -0.0801 0.0765  30  GLU B C   
4995 O O   . GLU B 45  ? 0.5671 0.6893 0.5744 -0.0647 -0.0781 0.0605  30  GLU B O   
4996 C CB  . GLU B 45  ? 0.6331 0.8014 0.6448 -0.0709 -0.0770 0.1041  30  GLU B CB  
4997 C CG  . GLU B 45  ? 0.7212 0.9052 0.7398 -0.0674 -0.0721 0.1225  30  GLU B CG  
4998 C CD  . GLU B 45  ? 0.7203 0.9185 0.7162 -0.0804 -0.0762 0.1335  30  GLU B CD  
4999 O OE1 . GLU B 45  ? 0.7217 0.9321 0.7066 -0.0900 -0.0878 0.1408  30  GLU B OE1 
5000 O OE2 . GLU B 45  ? 0.7628 0.9604 0.7508 -0.0823 -0.0683 0.1351  30  GLU B OE2 
5007 N N   . VAL B 46  ? 0.5373 0.6769 0.5680 -0.0596 -0.0881 0.0824  31  VAL B N   
5008 C CA  . VAL B 46  ? 0.5712 0.6935 0.5933 -0.0621 -0.0956 0.0700  31  VAL B CA  
5009 C C   . VAL B 46  ? 0.5505 0.6848 0.5575 -0.0761 -0.1076 0.0815  31  VAL B C   
5010 O O   . VAL B 46  ? 0.5599 0.7187 0.5786 -0.0758 -0.1103 0.1002  31  VAL B O   
5011 C CB  . VAL B 46  ? 0.5205 0.6334 0.5651 -0.0486 -0.0945 0.0655  31  VAL B CB  
5012 C CG1 . VAL B 46  ? 0.5276 0.6196 0.5606 -0.0512 -0.1024 0.0525  31  VAL B CG1 
5013 C CG2 . VAL B 46  ? 0.5118 0.6171 0.5727 -0.0372 -0.0838 0.0564  31  VAL B CG2 
5023 N N   . PHE B 47  ? 0.5728 0.6896 0.5530 -0.0881 -0.1147 0.0707  32  PHE B N   
5024 C CA  . PHE B 47  ? 0.5879 0.7137 0.5489 -0.1060 -0.1273 0.0804  32  PHE B CA  
5025 C C   . PHE B 47  ? 0.5963 0.6981 0.5454 -0.1102 -0.1352 0.0695  32  PHE B C   
5026 O O   . PHE B 47  ? 0.6053 0.6759 0.5454 -0.1036 -0.1324 0.0505  32  PHE B O   
5027 C CB  . PHE B 47  ? 0.6185 0.7415 0.5472 -0.1223 -0.1305 0.0793  32  PHE B CB  
5028 C CG  . PHE B 47  ? 0.6153 0.7608 0.5506 -0.1207 -0.1239 0.0909  32  PHE B CG  
5029 C CD1 . PHE B 47  ? 0.6122 0.7910 0.5523 -0.1283 -0.1301 0.1132  32  PHE B CD1 
5030 C CD2 . PHE B 47  ? 0.6202 0.7549 0.5565 -0.1115 -0.1117 0.0805  32  PHE B CD2 
5031 C CE1 . PHE B 47  ? 0.6125 0.8094 0.5561 -0.1262 -0.1246 0.1246  32  PHE B CE1 
5032 C CE2 . PHE B 47  ? 0.6325 0.7855 0.5721 -0.1112 -0.1057 0.0917  32  PHE B CE2 
5033 C CZ  . PHE B 47  ? 0.6158 0.7979 0.5579 -0.1183 -0.1124 0.1137  32  PHE B CZ  
5043 N N   . LYS B 48  ? 0.5951 0.7127 0.5440 -0.1210 -0.1450 0.0826  33  LYS B N   
5044 C CA  . LYS B 48  ? 0.6122 0.7070 0.5409 -0.1319 -0.1549 0.0750  33  LYS B CA  
5045 C C   . LYS B 48  ? 0.6781 0.7592 0.5660 -0.1546 -0.1640 0.0718  33  LYS B C   
5046 O O   . LYS B 48  ? 0.6579 0.7657 0.5397 -0.1686 -0.1688 0.0865  33  LYS B O   
5047 C CB  . LYS B 48  ? 0.6544 0.7750 0.6004 -0.1353 -0.1607 0.0914  33  LYS B CB  
5048 C CG  . LYS B 48  ? 0.6169 0.7155 0.5429 -0.1481 -0.1709 0.0857  33  LYS B CG  
5049 C CD  . LYS B 48  ? 0.6096 0.7407 0.5557 -0.1510 -0.1748 0.1039  33  LYS B CD  
5050 C CE  . LYS B 48  ? 0.7529 0.8629 0.6781 -0.1659 -0.1848 0.0996  33  LYS B CE  
5051 N NZ  . LYS B 48  ? 0.7566 0.9028 0.7020 -0.1693 -0.1873 0.1183  33  LYS B NZ  
5065 N N   . ALA B 49  ? 0.6789 0.7167 0.5369 -0.1576 -0.1666 0.0526  34  ALA B N   
5066 C CA  . ALA B 49  ? 0.7283 0.7425 0.5406 -0.1777 -0.1743 0.0464  34  ALA B CA  
5067 C C   . ALA B 49  ? 0.7534 0.7260 0.5344 -0.1871 -0.1835 0.0345  34  ALA B C   
5068 O O   . ALA B 49  ? 0.7545 0.7123 0.5489 -0.1741 -0.1819 0.0273  34  ALA B O   
5069 C CB  . ALA B 49  ? 0.7759 0.7714 0.5740 -0.1686 -0.1641 0.0321  34  ALA B CB  
5075 N N   . ARG B 50  ? 0.8042 0.7553 0.5400 -0.2108 -0.1939 0.0327  35  ARG B N   
5076 C CA  . ARG B 50  ? 0.8816 0.7857 0.5774 -0.2231 -0.2038 0.0214  35  ARG B CA  
5077 C C   . ARG B 50  ? 0.8899 0.7450 0.5359 -0.2261 -0.2030 0.0029  35  ARG B C   
5078 O O   . ARG B 50  ? 0.9075 0.7694 0.5345 -0.2374 -0.2032 0.0060  35  ARG B O   
5079 C CB  . ARG B 50  ? 0.9824 0.9017 0.6632 -0.2537 -0.2195 0.0379  35  ARG B CB  
5080 C CG  . ARG B 50  ? 1.0602 0.9252 0.6920 -0.2705 -0.2308 0.0266  35  ARG B CG  
5081 C CD  . ARG B 50  ? 1.1385 1.0230 0.7610 -0.3018 -0.2460 0.0443  35  ARG B CD  
5082 N NE  . ARG B 50  ? 1.0467 0.9804 0.7199 -0.2937 -0.2434 0.0605  35  ARG B NE  
5083 C CZ  . ARG B 50  ? 1.0524 1.0483 0.7589 -0.2998 -0.2442 0.0827  35  ARG B CZ  
5084 N NH1 . ARG B 50  ? 1.0434 1.0635 0.7398 -0.3158 -0.2489 0.0929  35  ARG B NH1 
5085 N NH2 . ARG B 50  ? 0.9136 0.9474 0.6629 -0.2885 -0.2402 0.0953  35  ARG B NH2 
5099 N N   . ASP B 51  ? 0.9821 0.7867 0.6052 -0.2150 -0.2021 -0.0161 36  ASP B N   
5100 C CA  . ASP B 51  ? 1.0905 0.8421 0.6616 -0.2151 -0.2010 -0.0349 36  ASP B CA  
5101 C C   . ASP B 51  ? 1.1506 0.8756 0.6661 -0.2495 -0.2166 -0.0310 36  ASP B C   
5102 O O   . ASP B 51  ? 1.1638 0.8865 0.6709 -0.2693 -0.2294 -0.0220 36  ASP B O   
5103 C CB  . ASP B 51  ? 1.0577 0.7629 0.6195 -0.1925 -0.1969 -0.0546 36  ASP B CB  
5104 C CG  . ASP B 51  ? 1.2103 0.8689 0.7313 -0.1799 -0.1894 -0.0754 36  ASP B CG  
5105 O OD1 . ASP B 51  ? 1.2568 0.8830 0.7242 -0.1995 -0.1958 -0.0789 36  ASP B OD1 
5106 O OD2 . ASP B 51  ? 1.2672 0.9220 0.8092 -0.1503 -0.1769 -0.0881 36  ASP B OD2 
5111 N N   . LYS B 52  ? 1.2020 0.9068 0.6779 -0.2580 -0.2155 -0.0374 37  LYS B N   
5112 C CA  . LYS B 52  ? 1.3315 1.0114 0.7516 -0.2934 -0.2310 -0.0332 37  LYS B CA  
5113 C C   . LYS B 52  ? 1.3518 0.9605 0.7167 -0.3005 -0.2396 -0.0483 37  LYS B C   
5114 O O   . LYS B 52  ? 1.3864 0.9848 0.7281 -0.3288 -0.2552 -0.0395 37  LYS B O   
5115 C CB  . LYS B 52  ? 1.2749 0.9489 0.6642 -0.2996 -0.2270 -0.0368 37  LYS B CB  
5116 C CG  . LYS B 52  ? 1.2151 0.9561 0.6490 -0.2994 -0.2219 -0.0191 37  LYS B CG  
5117 C CD  . LYS B 52  ? 1.3292 1.0589 0.7248 -0.3089 -0.2195 -0.0227 37  LYS B CD  
5118 C CE  . LYS B 52  ? 1.1523 0.9455 0.5897 -0.3075 -0.2144 -0.0049 37  LYS B CE  
5119 N NZ  . LYS B 52  ? 1.2643 1.0455 0.6610 -0.3187 -0.2130 -0.0077 37  LYS B NZ  
5133 N N   . VAL B 53  ? 1.4022 0.9611 0.7445 -0.2748 -0.2293 -0.0706 38  VAL B N   
5134 C CA  . VAL B 53  ? 1.5054 0.9889 0.7876 -0.2792 -0.2370 -0.0860 38  VAL B CA  
5135 C C   . VAL B 53  ? 1.4955 0.9743 0.7981 -0.2751 -0.2430 -0.0834 38  VAL B C   
5136 O O   . VAL B 53  ? 1.5724 1.0032 0.8285 -0.2947 -0.2562 -0.0857 38  VAL B O   
5137 C CB  . VAL B 53  ? 1.5528 0.9867 0.8055 -0.2493 -0.2232 -0.1102 38  VAL B CB  
5138 C CG1 . VAL B 53  ? 1.5244 0.9901 0.8384 -0.2094 -0.2067 -0.1159 38  VAL B CG1 
5139 C CG2 . VAL B 53  ? 1.6191 0.9686 0.8030 -0.2523 -0.2313 -0.1262 38  VAL B CG2 
5149 N N   . SER B 54  ? 1.4177 0.9430 0.7865 -0.2510 -0.2337 -0.0785 39  SER B N   
5150 C CA  . SER B 54  ? 1.3920 0.9102 0.7798 -0.2427 -0.2376 -0.0780 39  SER B CA  
5151 C C   . SER B 54  ? 1.3125 0.8888 0.7453 -0.2589 -0.2440 -0.0555 39  SER B C   
5152 O O   . SER B 54  ? 1.3870 0.9519 0.8218 -0.2626 -0.2508 -0.0527 39  SER B O   
5153 C CB  . SER B 54  ? 1.3130 0.8329 0.7381 -0.2014 -0.2230 -0.0912 39  SER B CB  
5154 O OG  . SER B 54  ? 1.2816 0.8677 0.7703 -0.1881 -0.2122 -0.0810 39  SER B OG  
5160 N N   . GLY B 55  ? 1.2470 0.8842 0.7145 -0.2672 -0.2414 -0.0392 40  GLY B N   
5161 C CA  . GLY B 55  ? 1.1284 0.8237 0.6390 -0.2793 -0.2460 -0.0172 40  GLY B CA  
5162 C C   . GLY B 55  ? 1.1383 0.8690 0.7101 -0.2507 -0.2352 -0.0144 40  GLY B C   
5163 O O   . GLY B 55  ? 1.0406 0.8173 0.6480 -0.2573 -0.2376 0.0034  40  GLY B O   
5167 N N   . ASP B 56  ? 0.9973 0.7091 0.5816 -0.2195 -0.2235 -0.0308 41  ASP B N   
5168 C CA  . ASP B 56  ? 1.0485 0.7878 0.6861 -0.1938 -0.2145 -0.0294 41  ASP B CA  
5169 C C   . ASP B 56  ? 0.9364 0.7366 0.6231 -0.1861 -0.2050 -0.0159 41  ASP B C   
5170 O O   . ASP B 56  ? 0.9743 0.7861 0.6564 -0.1873 -0.2000 -0.0160 41  ASP B O   
5171 C CB  . ASP B 56  ? 1.0820 0.7837 0.7167 -0.1643 -0.2061 -0.0507 41  ASP B CB  
5172 C CG  . ASP B 56  ? 1.1806 0.8195 0.7691 -0.1669 -0.2152 -0.0637 41  ASP B CG  
5173 O OD1 . ASP B 56  ? 1.1954 0.8273 0.7734 -0.1848 -0.2261 -0.0552 41  ASP B OD1 
5174 O OD2 . ASP B 56  ? 1.1816 0.7780 0.7434 -0.1504 -0.2110 -0.0821 41  ASP B OD2 
5179 N N   . LEU B 57  ? 0.8266 0.6629 0.5573 -0.1778 -0.2024 -0.0043 42  LEU B N   
5180 C CA  . LEU B 57  ? 0.8247 0.7126 0.6016 -0.1663 -0.1926 0.0076  42  LEU B CA  
5181 C C   . LEU B 57  ? 0.8015 0.6830 0.6000 -0.1380 -0.1795 -0.0063 42  LEU B C   
5182 O O   . LEU B 57  ? 0.7865 0.6384 0.5842 -0.1224 -0.1778 -0.0205 42  LEU B O   
5183 C CB  . LEU B 57  ? 0.7258 0.6498 0.5384 -0.1654 -0.1936 0.0241  42  LEU B CB  
5184 C CG  . LEU B 57  ? 0.8129 0.7598 0.6161 -0.1922 -0.2049 0.0423  42  LEU B CG  
5185 C CD1 . LEU B 57  ? 0.8000 0.7865 0.6439 -0.1842 -0.2016 0.0579  42  LEU B CD1 
5186 C CD2 . LEU B 57  ? 0.7610 0.7343 0.5531 -0.2109 -0.2086 0.0539  42  LEU B CD2 
5198 N N   . VAL B 58  ? 0.7527 0.6639 0.5707 -0.1322 -0.1704 -0.0014 43  VAL B N   
5199 C CA  . VAL B 58  ? 0.7035 0.6154 0.5432 -0.1089 -0.1574 -0.0123 43  VAL B CA  
5200 C C   . VAL B 58  ? 0.6650 0.6226 0.5431 -0.1033 -0.1493 0.0026  43  VAL B C   
5201 O O   . VAL B 58  ? 0.6564 0.6437 0.5402 -0.1163 -0.1534 0.0204  43  VAL B O   
5202 C CB  . VAL B 58  ? 0.7539 0.6394 0.5620 -0.1073 -0.1529 -0.0276 43  VAL B CB  
5203 C CG1 . VAL B 58  ? 0.8005 0.6342 0.5706 -0.1061 -0.1590 -0.0447 43  VAL B CG1 
5204 C CG2 . VAL B 58  ? 0.7577 0.6564 0.5433 -0.1280 -0.1560 -0.0177 43  VAL B CG2 
5214 N N   . ALA B 59  ? 0.6445 0.6073 0.5481 -0.0838 -0.1380 -0.0045 44  ALA B N   
5215 C CA  . ALA B 59  ? 0.6650 0.6627 0.5989 -0.0776 -0.1289 0.0069  44  ALA B CA  
5216 C C   . ALA B 59  ? 0.6292 0.6251 0.5541 -0.0745 -0.1196 -0.0016 44  ALA B C   
5217 O O   . ALA B 59  ? 0.6418 0.6157 0.5596 -0.0637 -0.1146 -0.0189 44  ALA B O   
5218 C CB  . ALA B 59  ? 0.5832 0.5891 0.5535 -0.0601 -0.1232 0.0073  44  ALA B CB  
5224 N N   . LEU B 60  ? 0.6281 0.6481 0.5527 -0.0831 -0.1170 0.0110  45  LEU B N   
5225 C CA  . LEU B 60  ? 0.6404 0.6625 0.5567 -0.0815 -0.1072 0.0055  45  LEU B CA  
5226 C C   . LEU B 60  ? 0.6113 0.6623 0.5608 -0.0730 -0.0975 0.0163  45  LEU B C   
5227 O O   . LEU B 60  ? 0.5970 0.6717 0.5582 -0.0780 -0.1005 0.0346  45  LEU B O   
5228 C CB  . LEU B 60  ? 0.6716 0.6924 0.5523 -0.1007 -0.1129 0.0105  45  LEU B CB  
5229 C CG  . LEU B 60  ? 0.7421 0.7253 0.5792 -0.1101 -0.1202 -0.0036 45  LEU B CG  
5230 C CD1 . LEU B 60  ? 0.7621 0.7466 0.5641 -0.1324 -0.1276 0.0046  45  LEU B CD1 
5231 C CD2 . LEU B 60  ? 0.7376 0.6946 0.5640 -0.0949 -0.1098 -0.0249 45  LEU B CD2 
5243 N N   . LYS B 61  ? 0.6049 0.6540 0.5688 -0.0600 -0.0861 0.0056  46  LYS B N   
5244 C CA  . LYS B 61  ? 0.5845 0.6560 0.5744 -0.0541 -0.0762 0.0144  46  LYS B CA  
5245 C C   . LYS B 61  ? 0.6157 0.6929 0.5899 -0.0593 -0.0674 0.0129  46  LYS B C   
5246 O O   . LYS B 61  ? 0.6201 0.6851 0.5834 -0.0546 -0.0606 -0.0029 46  LYS B O   
5247 C CB  . LYS B 61  ? 0.5646 0.6338 0.5831 -0.0388 -0.0696 0.0054  46  LYS B CB  
5248 C CG  . LYS B 61  ? 0.5828 0.6712 0.6257 -0.0352 -0.0606 0.0158  46  LYS B CG  
5249 C CD  . LYS B 61  ? 0.6085 0.6951 0.6768 -0.0234 -0.0544 0.0062  46  LYS B CD  
5250 C CE  . LYS B 61  ? 0.5945 0.6950 0.6831 -0.0225 -0.0475 0.0184  46  LYS B CE  
5251 N NZ  . LYS B 61  ? 0.6290 0.7290 0.7412 -0.0143 -0.0422 0.0097  46  LYS B NZ  
5265 N N   . MET B 62  ? 0.6128 0.7088 0.5853 -0.0678 -0.0672 0.0297  47  MET B N   
5266 C CA  . MET B 62  ? 0.6216 0.7242 0.5783 -0.0739 -0.0590 0.0308  47  MET B CA  
5267 C C   . MET B 62  ? 0.6054 0.7222 0.5876 -0.0663 -0.0468 0.0353  47  MET B C   
5268 O O   . MET B 62  ? 0.5855 0.7137 0.5885 -0.0631 -0.0480 0.0492  47  MET B O   
5269 C CB  . MET B 62  ? 0.6352 0.7493 0.5716 -0.0889 -0.0670 0.0473  47  MET B CB  
5270 C CG  . MET B 62  ? 0.6939 0.8111 0.6076 -0.0968 -0.0597 0.0478  47  MET B CG  
5271 S SD  . MET B 62  ? 0.8258 0.9700 0.7455 -0.1028 -0.0595 0.0732  47  MET B SD  
5272 C CE  . MET B 62  ? 0.7111 0.8623 0.6694 -0.0872 -0.0474 0.0756  47  MET B CE  
5282 N N   . VAL B 63  ? 0.6169 0.7323 0.5957 -0.0635 -0.0349 0.0237  48  VAL B N   
5283 C CA  . VAL B 63  ? 0.6082 0.7375 0.6062 -0.0604 -0.0227 0.0278  48  VAL B CA  
5284 C C   . VAL B 63  ? 0.6335 0.7686 0.6077 -0.0696 -0.0148 0.0303  48  VAL B C   
5285 O O   . VAL B 63  ? 0.6574 0.7829 0.6075 -0.0714 -0.0118 0.0175  48  VAL B O   
5286 C CB  . VAL B 63  ? 0.5977 0.7261 0.6181 -0.0489 -0.0144 0.0124  48  VAL B CB  
5287 C CG1 . VAL B 63  ? 0.5935 0.7368 0.6350 -0.0489 -0.0037 0.0192  48  VAL B CG1 
5288 C CG2 . VAL B 63  ? 0.6486 0.7668 0.6856 -0.0403 -0.0236 0.0076  48  VAL B CG2 
5298 N N   . LYS B 64  ? 0.6898 0.8375 0.6676 -0.0749 -0.0114 0.0466  49  LYS B N   
5299 C CA  . LYS B 64  ? 0.6954 0.8487 0.6505 -0.0842 -0.0035 0.0504  49  LYS B CA  
5300 C C   . LYS B 64  ? 0.6819 0.8409 0.6463 -0.0806 0.0130  0.0394  49  LYS B C   
5301 O O   . LYS B 64  ? 0.6423 0.8079 0.6353 -0.0748 0.0184  0.0394  49  LYS B O   
5302 C CB  . LYS B 64  ? 0.6627 0.8262 0.6166 -0.0905 -0.0064 0.0730  49  LYS B CB  
5303 C CG  . LYS B 64  ? 0.7571 0.9222 0.6899 -0.0987 -0.0205 0.0849  49  LYS B CG  
5304 C CD  . LYS B 64  ? 0.8379 1.0154 0.7748 -0.1005 -0.0242 0.1085  49  LYS B CD  
5305 C CE  . LYS B 64  ? 0.8592 1.0448 0.7765 -0.1095 -0.0386 0.1213  49  LYS B CE  
5306 N NZ  . LYS B 64  ? 0.8623 1.0623 0.7853 -0.1079 -0.0427 0.1455  49  LYS B NZ  
5320 N N   . MET B 65  ? 0.6991 0.8562 0.6381 -0.0846 0.0210  0.0301  50  MET B N   
5321 C CA  . MET B 65  ? 0.7137 0.8805 0.6595 -0.0812 0.0381  0.0195  50  MET B CA  
5322 C C   . MET B 65  ? 0.7316 0.9079 0.6608 -0.0923 0.0479  0.0301  50  MET B C   
5323 O O   . MET B 65  ? 0.8224 0.9946 0.7273 -0.1022 0.0412  0.0427  50  MET B O   
5324 C CB  . MET B 65  ? 0.7496 0.9063 0.6785 -0.0736 0.0428  -0.0015 50  MET B CB  
5325 C CG  . MET B 65  ? 0.7565 0.9056 0.7056 -0.0601 0.0371  -0.0144 50  MET B CG  
5326 S SD  . MET B 65  ? 0.9117 1.0520 0.8459 -0.0464 0.0475  -0.0390 50  MET B SD  
5327 C CE  . MET B 65  ? 0.7215 0.8944 0.6805 -0.0435 0.0690  -0.0407 50  MET B CE  
5337 N N   . GLU B 66  ? 0.7362 0.9269 0.6788 -0.0912 0.0637  0.0254  51  GLU B N   
5338 C CA  . GLU B 66  ? 0.7932 0.9936 0.7201 -0.1017 0.0761  0.0330  51  GLU B CA  
5339 C C   . GLU B 66  ? 0.7695 0.9726 0.6757 -0.0992 0.0900  0.0167  51  GLU B C   
5340 O O   . GLU B 66  ? 0.7671 0.9691 0.6810 -0.0868 0.0929  -0.0006 51  GLU B O   
5341 C CB  . GLU B 66  ? 0.8434 1.0596 0.7995 -0.1047 0.0853  0.0409  51  GLU B CB  
5342 C CG  . GLU B 66  ? 0.8501 1.0603 0.8285 -0.1038 0.0738  0.0543  51  GLU B CG  
5343 C CD  . GLU B 66  ? 0.8444 1.0470 0.8052 -0.1128 0.0676  0.0756  51  GLU B CD  
5344 O OE1 . GLU B 66  ? 0.8447 1.0498 0.7802 -0.1224 0.0743  0.0817  51  GLU B OE1 
5345 O OE2 . GLU B 66  ? 0.8667 1.0610 0.8383 -0.1092 0.0561  0.0866  51  GLU B OE2 
5352 N N   . PRO B 67  ? 0.8472 1.0526 0.7248 -0.1094 0.0992  0.0218  52  PRO B N   
5353 C CA  . PRO B 67  ? 0.8232 1.0393 0.6910 -0.1060 0.1185  0.0080  52  PRO B CA  
5354 C C   . PRO B 67  ? 0.8039 1.0466 0.7117 -0.1016 0.1318  0.0051  52  PRO B C   
5355 O O   . PRO B 67  ? 0.8081 1.0636 0.7258 -0.0903 0.1437  -0.0109 52  PRO B O   
5356 C CB  . PRO B 67  ? 0.8565 1.0704 0.6878 -0.1207 0.1245  0.0187  52  PRO B CB  
5357 C CG  . PRO B 67  ? 0.8567 1.0525 0.6688 -0.1287 0.1048  0.0324  52  PRO B CG  
5358 C CD  . PRO B 67  ? 0.8237 1.0210 0.6726 -0.1232 0.0919  0.0393  52  PRO B CD  
5366 N N   . ASP B 68  ? 0.9075 1.1582 0.8382 -0.1101 0.1290  0.0207  53  ASP B N   
5367 C CA  . ASP B 68  ? 0.8651 1.1390 0.8342 -0.1097 0.1381  0.0203  53  ASP B CA  
5368 C C   . ASP B 68  ? 0.8673 1.1442 0.8684 -0.0949 0.1314  0.0079  53  ASP B C   
5369 O O   . ASP B 68  ? 0.8238 1.1204 0.8588 -0.0944 0.1364  0.0069  53  ASP B O   
5370 C CB  . ASP B 68  ? 0.9662 1.2376 0.9447 -0.1229 0.1338  0.0406  53  ASP B CB  
5371 C CG  . ASP B 68  ? 0.9976 1.2791 0.9598 -0.1382 0.1481  0.0510  53  ASP B CG  
5372 O OD1 . ASP B 68  ? 0.9478 1.2502 0.9087 -0.1388 0.1653  0.0417  53  ASP B OD1 
5373 O OD2 . ASP B 68  ? 1.0854 1.3538 1.0353 -0.1489 0.1426  0.0691  53  ASP B OD2 
5378 N N   . ASP B 69  ? 0.8489 1.1061 0.8389 -0.0843 0.1193  -0.0009 54  ASP B N   
5379 C CA  . ASP B 69  ? 0.7682 1.0258 0.7838 -0.0693 0.1133  -0.0138 54  ASP B CA  
5380 C C   . ASP B 69  ? 0.7287 0.9984 0.7423 -0.0558 0.1263  -0.0328 54  ASP B C   
5381 O O   . ASP B 69  ? 0.7585 1.0319 0.7464 -0.0574 0.1392  -0.0368 54  ASP B O   
5382 C CB  . ASP B 69  ? 0.7461 0.9759 0.7503 -0.0648 0.0941  -0.0136 54  ASP B CB  
5383 C CG  . ASP B 69  ? 0.6761 0.9003 0.7000 -0.0697 0.0814  0.0010  54  ASP B CG  
5384 O OD1 . ASP B 69  ? 0.6574 0.8951 0.7129 -0.0693 0.0842  0.0029  54  ASP B OD1 
5385 O OD2 . ASP B 69  ? 0.6758 0.8829 0.6829 -0.0739 0.0688  0.0107  54  ASP B OD2 
5390 N N   . ASP B 70  ? 0.7109 0.9863 0.7511 -0.0411 0.1230  -0.0442 55  ASP B N   
5391 C CA  . ASP B 70  ? 0.7231 1.0154 0.7705 -0.0246 0.1357  -0.0614 55  ASP B CA  
5392 C C   . ASP B 70  ? 0.7244 0.9908 0.7624 -0.0074 0.1241  -0.0751 55  ASP B C   
5393 O O   . ASP B 70  ? 0.6986 0.9632 0.7626 -0.0010 0.1128  -0.0765 55  ASP B O   
5394 C CB  . ASP B 70  ? 0.7023 1.0332 0.7954 -0.0232 0.1439  -0.0611 55  ASP B CB  
5395 C CG  . ASP B 70  ? 0.7183 1.0771 0.8202 -0.0073 0.1609  -0.0757 55  ASP B CG  
5396 O OD1 . ASP B 70  ? 0.7399 1.1188 0.8317 -0.0127 0.1785  -0.0745 55  ASP B OD1 
5397 O OD2 . ASP B 70  ? 0.7354 1.0963 0.8533 0.0115  0.1570  -0.0880 55  ASP B OD2 
5402 N N   . VAL B 71  ? 0.7584 1.0021 0.7562 -0.0007 0.1271  -0.0854 56  VAL B N   
5403 C CA  . VAL B 71  ? 0.8132 1.0250 0.7942 0.0133  0.1153  -0.0977 56  VAL B CA  
5404 C C   . VAL B 71  ? 0.7782 1.0035 0.7810 0.0366  0.1219  -0.1134 56  VAL B C   
5405 O O   . VAL B 71  ? 0.7727 0.9743 0.7717 0.0493  0.1104  -0.1222 56  VAL B O   
5406 C CB  . VAL B 71  ? 0.8143 0.9914 0.7392 0.0108  0.1148  -0.1034 56  VAL B CB  
5407 C CG1 . VAL B 71  ? 0.8468 1.0312 0.7522 0.0234  0.1351  -0.1168 56  VAL B CG1 
5408 C CG2 . VAL B 71  ? 0.8954 1.0330 0.7996 0.0171  0.0973  -0.1108 56  VAL B CG2 
5418 N N   . SER B 72  ? 0.7684 1.0329 0.7946 0.0427  0.1400  -0.1162 57  SER B N   
5419 C CA  . SER B 72  ? 0.7675 1.0516 0.8191 0.0663  0.1461  -0.1296 57  SER B CA  
5420 C C   . SER B 72  ? 0.7810 1.0707 0.8716 0.0688  0.1305  -0.1267 57  SER B C   
5421 O O   . SER B 72  ? 0.7559 1.0301 0.8479 0.0872  0.1225  -0.1376 57  SER B O   
5422 C CB  . SER B 72  ? 0.7952 1.1288 0.8699 0.0692  0.1684  -0.1302 57  SER B CB  
5423 O OG  . SER B 72  ? 0.8154 1.1414 0.8513 0.0754  0.1845  -0.1381 57  SER B OG  
5429 N N   . THR B 73  ? 0.9686 1.2765 1.0877 0.0505  0.1257  -0.1119 58  THR B N   
5430 C CA  . THR B 73  ? 0.9512 1.2648 1.1063 0.0517  0.1120  -0.1088 58  THR B CA  
5431 C C   . THR B 73  ? 0.8746 1.1444 1.0108 0.0561  0.0926  -0.1115 58  THR B C   
5432 O O   . THR B 73  ? 0.8758 1.1401 1.0258 0.0713  0.0841  -0.1198 58  THR B O   
5433 C CB  . THR B 73  ? 0.8901 1.2218 1.0693 0.0295  0.1103  -0.0920 58  THR B CB  
5434 O OG1 . THR B 73  ? 0.9513 1.2548 1.1020 0.0134  0.1038  -0.0805 58  THR B OG1 
5435 C CG2 . THR B 73  ? 0.8138 1.1899 1.0122 0.0226  0.1292  -0.0887 58  THR B CG2 
5443 N N   . LEU B 74  ? 0.8599 1.0996 0.9646 0.0425  0.0851  -0.1037 59  LEU B N   
5444 C CA  . LEU B 74  ? 1.0216 1.2230 1.1085 0.0439  0.0670  -0.1046 59  LEU B CA  
5445 C C   . LEU B 74  ? 1.0018 1.1767 1.0611 0.0623  0.0657  -0.1213 59  LEU B C   
5446 O O   . LEU B 74  ? 0.8995 1.0485 0.9543 0.0691  0.0516  -0.1256 59  LEU B O   
5447 C CB  . LEU B 74  ? 1.0514 1.2327 1.1113 0.0249  0.0600  -0.0915 59  LEU B CB  
5448 C CG  . LEU B 74  ? 1.0878 1.2547 1.1042 0.0198  0.0672  -0.0939 59  LEU B CG  
5449 C CD1 . LEU B 74  ? 1.0788 1.2046 1.0565 0.0240  0.0557  -0.1023 59  LEU B CD1 
5450 C CD2 . LEU B 74  ? 1.0508 1.2236 1.0592 -0.0009 0.0674  -0.0766 59  LEU B CD2 
5462 N N   . GLN B 75  ? 0.8660 1.0440 0.9037 0.0709  0.0806  -0.1308 60  GLN B N   
5463 C CA  . GLN B 75  ? 0.8400 0.9889 0.8478 0.0909  0.0809  -0.1476 60  GLN B CA  
5464 C C   . GLN B 75  ? 0.8695 1.0280 0.9080 0.1121  0.0770  -0.1565 60  GLN B C   
5465 O O   . GLN B 75  ? 0.8287 0.9521 0.8479 0.1243  0.0663  -0.1655 60  GLN B O   
5466 C CB  . GLN B 75  ? 0.8037 0.9591 0.7865 0.0988  0.1005  -0.1562 60  GLN B CB  
5467 C CG  . GLN B 75  ? 0.8649 0.9710 0.7903 0.1067  0.0989  -0.1686 60  GLN B CG  
5468 C CD  . GLN B 75  ? 0.9895 1.0945 0.8795 0.1028  0.1155  -0.1713 60  GLN B CD  
5469 O OE1 . GLN B 75  ? 0.8926 1.0331 0.7989 0.1120  0.1347  -0.1744 60  GLN B OE1 
5470 N NE2 . GLN B 75  ? 1.0323 1.0979 0.8732 0.0878  0.1080  -0.1695 60  GLN B NE2 
5479 N N   . LYS B 76  ? 1.0073 1.2127 1.0926 0.1154  0.0848  -0.1533 61  LYS B N   
5480 C CA  . LYS B 76  ? 1.0264 1.2465 1.1438 0.1349  0.0804  -0.1605 61  LYS B CA  
5481 C C   . LYS B 76  ? 0.9937 1.1934 1.1227 0.1283  0.0596  -0.1548 61  LYS B C   
5482 O O   . LYS B 76  ? 0.9946 1.1735 1.1207 0.1445  0.0496  -0.1633 61  LYS B O   
5483 C CB  . LYS B 76  ? 0.9611 1.2406 1.1261 0.1362  0.0933  -0.1570 61  LYS B CB  
5484 C CG  . LYS B 76  ? 0.9956 1.3031 1.1536 0.1367  0.1156  -0.1587 61  LYS B CG  
5485 C CD  . LYS B 76  ? 1.0101 1.3124 1.1478 0.1654  0.1272  -0.1752 61  LYS B CD  
5486 C CE  . LYS B 76  ? 1.0503 1.3926 1.2307 0.1879  0.1302  -0.1812 61  LYS B CE  
5487 N NZ  . LYS B 76  ? 1.1564 1.5000 1.3190 0.2187  0.1449  -0.1964 61  LYS B NZ  
5501 N N   . GLU B 77  ? 0.9971 1.2009 1.1373 0.1056  0.0534  -0.1401 62  GLU B N   
5502 C CA  . GLU B 77  ? 1.0039 1.1884 1.1531 0.0994  0.0351  -0.1340 62  GLU B CA  
5503 C C   . GLU B 77  ? 1.0069 1.1419 1.1158 0.1019  0.0228  -0.1389 62  GLU B C   
5504 O O   . GLU B 77  ? 0.9457 1.0612 1.0583 0.1061  0.0085  -0.1400 62  GLU B O   
5505 C CB  . GLU B 77  ? 0.9688 1.1640 1.1315 0.0761  0.0327  -0.1171 62  GLU B CB  
5506 C CG  . GLU B 77  ? 1.0430 1.2829 1.2417 0.0693  0.0441  -0.1109 62  GLU B CG  
5507 C CD  . GLU B 77  ? 1.0224 1.2762 1.2582 0.0677  0.0348  -0.1068 62  GLU B CD  
5508 O OE1 . GLU B 77  ? 0.9025 1.1399 1.1389 0.0553  0.0244  -0.0964 62  GLU B OE1 
5509 O OE2 . GLU B 77  ? 0.9819 1.2634 1.2453 0.0793  0.0380  -0.1137 62  GLU B OE2 
5516 N N   . ILE B 78  ? 0.9624 1.0759 1.0307 0.0979  0.0277  -0.1416 63  ILE B N   
5517 C CA  . ILE B 78  ? 0.9194 0.9849 0.9453 0.0976  0.0160  -0.1463 63  ILE B CA  
5518 C C   . ILE B 78  ? 0.9726 1.0168 0.9917 0.1209  0.0114  -0.1611 63  ILE B C   
5519 O O   . ILE B 78  ? 0.9580 0.9698 0.9639 0.1213  -0.0036 -0.1623 63  ILE B O   
5520 C CB  . ILE B 78  ? 0.9315 0.9790 0.9129 0.0893  0.0232  -0.1478 63  ILE B CB  
5521 C CG1 . ILE B 78  ? 0.8852 0.9418 0.8652 0.0643  0.0208  -0.1310 63  ILE B CG1 
5522 C CG2 . ILE B 78  ? 0.9124 0.9082 0.8453 0.0938  0.0136  -0.1578 63  ILE B CG2 
5523 C CD1 . ILE B 78  ? 0.9006 0.9292 0.8637 0.0504  0.0029  -0.1227 63  ILE B CD1 
5535 N N   . LEU B 79  ? 1.1522 1.2147 1.1796 0.1414  0.0247  -0.1721 64  LEU B N   
5536 C CA  . LEU B 79  ? 1.1575 1.1971 1.1730 0.1670  0.0216  -0.1866 64  LEU B CA  
5537 C C   . LEU B 79  ? 1.1061 1.1470 1.1512 0.1727  0.0069  -0.1848 64  LEU B C   
5538 O O   . LEU B 79  ? 1.1059 1.1095 1.1296 0.1855  -0.0036 -0.1929 64  LEU B O   
5539 C CB  . LEU B 79  ? 1.0725 1.1417 1.0990 0.1897  0.0400  -0.1968 64  LEU B CB  
5540 C CG  . LEU B 79  ? 1.2869 1.3284 1.2634 0.1982  0.0521  -0.2075 64  LEU B CG  
5541 C CD1 . LEU B 79  ? 1.1899 1.2389 1.1509 0.1740  0.0602  -0.1986 64  LEU B CD1 
5542 C CD2 . LEU B 79  ? 1.2098 1.2762 1.1970 0.2286  0.0690  -0.2196 64  LEU B CD2 
5554 N N   . ILE B 80  ? 1.0287 1.1082 1.1194 0.1626  0.0055  -0.1742 65  ILE B N   
5555 C CA  . ILE B 80  ? 1.0108 1.0919 1.1287 0.1675  -0.0083 -0.1726 65  ILE B CA  
5556 C C   . ILE B 80  ? 1.0542 1.0893 1.1447 0.1571  -0.0252 -0.1692 65  ILE B C   
5557 O O   . ILE B 80  ? 1.0264 1.0332 1.1059 0.1698  -0.0363 -0.1760 65  ILE B O   
5558 C CB  . ILE B 80  ? 1.0202 1.1473 1.1865 0.1553  -0.0065 -0.1613 65  ILE B CB  
5559 C CG1 . ILE B 80  ? 0.9071 1.0828 1.1000 0.1631  0.0109  -0.1640 65  ILE B CG1 
5560 C CG2 . ILE B 80  ? 1.0021 1.1286 1.1935 0.1601  -0.0212 -0.1603 65  ILE B CG2 
5561 C CD1 . ILE B 80  ? 0.9439 1.1646 1.1833 0.1506  0.0124  -0.1537 65  ILE B CD1 
5573 N N   . LEU B 81  ? 0.9684 0.9965 1.0469 0.1339  -0.0275 -0.1579 66  LEU B N   
5574 C CA  . LEU B 81  ? 0.9437 0.9346 0.9982 0.1222  -0.0426 -0.1528 66  LEU B CA  
5575 C C   . LEU B 81  ? 0.9879 0.9317 0.9940 0.1300  -0.0473 -0.1638 66  LEU B C   
5576 O O   . LEU B 81  ? 1.0113 0.9216 1.0005 0.1302  -0.0609 -0.1652 66  LEU B O   
5577 C CB  . LEU B 81  ? 0.9730 0.9704 1.0231 0.0979  -0.0424 -0.1382 66  LEU B CB  
5578 C CG  . LEU B 81  ? 0.8267 0.8667 0.9120 0.0888  -0.0327 -0.1278 66  LEU B CG  
5579 C CD1 . LEU B 81  ? 0.8464 0.8855 0.9192 0.0676  -0.0337 -0.1137 66  LEU B CD1 
5580 C CD2 . LEU B 81  ? 0.8534 0.9126 0.9788 0.0919  -0.0378 -0.1241 66  LEU B CD2 
5592 N N   . LYS B 82  ? 1.0878 1.0258 1.0680 0.1357  -0.0359 -0.1718 67  LYS B N   
5593 C CA  . LYS B 82  ? 1.1271 1.0153 1.0553 0.1434  -0.0392 -0.1832 67  LYS B CA  
5594 C C   . LYS B 82  ? 1.2574 1.1247 1.1838 0.1685  -0.0448 -0.1952 67  LYS B C   
5595 O O   . LYS B 82  ? 1.3029 1.1193 1.1847 0.1732  -0.0526 -0.2031 67  LYS B O   
5596 C CB  . LYS B 82  ? 1.1484 1.0376 1.0514 0.1476  -0.0235 -0.1902 67  LYS B CB  
5597 C CG  . LYS B 82  ? 1.1266 0.9594 0.9662 0.1483  -0.0265 -0.2001 67  LYS B CG  
5598 C CD  . LYS B 82  ? 1.2480 1.0852 1.0641 0.1511  -0.0096 -0.2060 67  LYS B CD  
5599 C CE  . LYS B 82  ? 1.3506 1.1268 1.0978 0.1518  -0.0121 -0.2169 67  LYS B CE  
5600 N NZ  . LYS B 82  ? 1.3992 1.1781 1.1217 0.1580  0.0059  -0.2243 67  LYS B NZ  
5614 N N   . THR B 83  ? 1.3874 1.2913 1.3596 0.1840  -0.0420 -0.1961 68  THR B N   
5615 C CA  . THR B 83  ? 1.3531 1.2452 1.3283 0.2113  -0.0459 -0.2071 68  THR B CA  
5616 C C   . THR B 83  ? 1.3005 1.1885 1.2972 0.2101  -0.0621 -0.2022 68  THR B C   
5617 O O   . THR B 83  ? 1.3182 1.1703 1.2947 0.2251  -0.0719 -0.2097 68  THR B O   
5618 C CB  . THR B 83  ? 1.4028 1.3437 1.4144 0.2325  -0.0308 -0.2124 68  THR B CB  
5619 O OG1 . THR B 83  ? 1.3907 1.3303 1.3765 0.2381  -0.0147 -0.2191 68  THR B OG1 
5620 C CG2 . THR B 83  ? 1.3698 1.3060 1.3908 0.2624  -0.0359 -0.2220 68  THR B CG2 
5628 N N   . CYS B 84  ? 1.2420 1.1622 1.2757 0.1928  -0.0652 -0.1897 69  CYS B N   
5629 C CA  . CYS B 84  ? 1.1438 1.0717 1.2069 0.1947  -0.0773 -0.1856 69  CYS B CA  
5630 C C   . CYS B 84  ? 1.1466 1.0532 1.1995 0.1716  -0.0892 -0.1746 69  CYS B C   
5631 O O   . CYS B 84  ? 1.1068 1.0250 1.1605 0.1513  -0.0851 -0.1647 69  CYS B O   
5632 C CB  . CYS B 84  ? 1.0866 1.0720 1.2032 0.1961  -0.0701 -0.1809 69  CYS B CB  
5633 S SG  . CYS B 84  ? 1.1504 1.1731 1.2836 0.2210  -0.0529 -0.1916 69  CYS B SG  
5639 N N   . ARG B 85  ? 1.0374 0.9143 1.0808 0.1757  -0.1035 -0.1759 70  ARG B N   
5640 C CA  . ARG B 85  ? 0.9395 0.7924 0.9685 0.1564  -0.1149 -0.1666 70  ARG B CA  
5641 C C   . ARG B 85  ? 0.8014 0.6636 0.8594 0.1576  -0.1247 -0.1618 70  ARG B C   
5642 O O   . ARG B 85  ? 0.8141 0.6928 0.8970 0.1744  -0.1259 -0.1672 70  ARG B O   
5643 C CB  . ARG B 85  ? 0.9031 0.7006 0.8805 0.1561  -0.1240 -0.1723 70  ARG B CB  
5644 C CG  . ARG B 85  ? 1.0483 0.8258 0.9876 0.1555  -0.1163 -0.1788 70  ARG B CG  
5645 C CD  . ARG B 85  ? 1.0538 0.8226 0.9839 0.1835  -0.1101 -0.1938 70  ARG B CD  
5646 N NE  . ARG B 85  ? 1.1641 0.8927 1.0419 0.1839  -0.1067 -0.2019 70  ARG B NE  
5647 C CZ  . ARG B 85  ? 1.1940 0.9333 1.0603 0.1750  -0.0952 -0.2014 70  ARG B CZ  
5648 N NH1 . ARG B 85  ? 1.1586 0.9477 1.0619 0.1649  -0.0856 -0.1927 70  ARG B NH1 
5649 N NH2 . ARG B 85  ? 1.2853 0.9812 1.0984 0.1755  -0.0937 -0.2098 70  ARG B NH2 
5663 N N   . HIS B 86  ? 0.7063 0.5584 0.7600 0.1395  -0.1319 -0.1512 71  HIS B N   
5664 C CA  . HIS B 86  ? 0.6713 0.5183 0.7389 0.1387  -0.1428 -0.1468 71  HIS B CA  
5665 C C   . HIS B 86  ? 0.6206 0.4492 0.6693 0.1188  -0.1484 -0.1359 71  HIS B C   
5666 O O   . HIS B 86  ? 0.6106 0.4521 0.6572 0.1039  -0.1419 -0.1276 71  HIS B O   
5667 C CB  . HIS B 86  ? 0.5945 0.4821 0.7071 0.1393  -0.1391 -0.1421 71  HIS B CB  
5668 C CG  . HIS B 86  ? 0.5798 0.4598 0.7043 0.1412  -0.1507 -0.1398 71  HIS B CG  
5669 N ND1 . HIS B 86  ? 0.5756 0.4472 0.6982 0.1266  -0.1553 -0.1293 71  HIS B ND1 
5670 C CD2 . HIS B 86  ? 0.5840 0.4642 0.7218 0.1563  -0.1584 -0.1463 71  HIS B CD2 
5671 C CE1 . HIS B 86  ? 0.5604 0.4244 0.6922 0.1319  -0.1650 -0.1301 71  HIS B CE1 
5672 N NE2 . HIS B 86  ? 0.5719 0.4411 0.7132 0.1493  -0.1679 -0.1402 71  HIS B NE2 
5680 N N   . ALA B 87  ? 0.6286 0.4291 0.6641 0.1189  -0.1604 -0.1354 72  ALA B N   
5681 C CA  . ALA B 87  ? 0.6284 0.4118 0.6437 0.1007  -0.1656 -0.1253 72  ALA B CA  
5682 C C   . ALA B 87  ? 0.5930 0.4079 0.6333 0.0874  -0.1596 -0.1116 72  ALA B C   
5683 O O   . ALA B 87  ? 0.5909 0.4081 0.6191 0.0719  -0.1577 -0.1021 72  ALA B O   
5684 C CB  . ALA B 87  ? 0.6655 0.4174 0.6666 0.1037  -0.1785 -0.1266 72  ALA B CB  
5690 N N   . ASN B 88  ? 0.5679 0.4065 0.6417 0.0932  -0.1571 -0.1101 73  ASN B N   
5691 C CA  . ASN B 88  ? 0.5395 0.4020 0.6340 0.0828  -0.1516 -0.0975 73  ASN B CA  
5692 C C   . ASN B 88  ? 0.5281 0.4200 0.6358 0.0778  -0.1394 -0.0937 73  ASN B C   
5693 O O   . ASN B 88  ? 0.5075 0.4191 0.6335 0.0715  -0.1340 -0.0839 73  ASN B O   
5694 C CB  . ASN B 88  ? 0.5626 0.4323 0.6821 0.0891  -0.1548 -0.0975 73  ASN B CB  
5695 C CG  . ASN B 88  ? 0.5332 0.3742 0.6391 0.0918  -0.1665 -0.0987 73  ASN B CG  
5696 O OD1 . ASN B 88  ? 0.5431 0.3736 0.6513 0.1035  -0.1739 -0.1077 73  ASN B OD1 
5697 N ND2 . ASN B 88  ? 0.5312 0.3615 0.6233 0.0812  -0.1682 -0.0888 73  ASN B ND2 
5704 N N   . ILE B 89  ? 0.5738 0.4667 0.6701 0.0809  -0.1347 -0.1010 74  ILE B N   
5705 C CA  . ILE B 89  ? 0.5383 0.4563 0.6415 0.0751  -0.1231 -0.0973 74  ILE B CA  
5706 C C   . ILE B 89  ? 0.5559 0.4608 0.6277 0.0637  -0.1233 -0.0937 74  ILE B C   
5707 O O   . ILE B 89  ? 0.5834 0.4601 0.6264 0.0658  -0.1292 -0.1014 74  ILE B O   
5708 C CB  . ILE B 89  ? 0.5791 0.5128 0.6949 0.0877  -0.1158 -0.1085 74  ILE B CB  
5709 C CG1 . ILE B 89  ? 0.5387 0.4893 0.6871 0.0970  -0.1172 -0.1113 74  ILE B CG1 
5710 C CG2 . ILE B 89  ? 0.5411 0.4993 0.6608 0.0802  -0.1032 -0.1042 74  ILE B CG2 
5711 C CD1 . ILE B 89  ? 0.5113 0.4853 0.6848 0.0868  -0.1125 -0.1000 74  ILE B CD1 
5723 N N   . VAL B 90  ? 0.5432 0.4669 0.6186 0.0511  -0.1175 -0.0815 75  VAL B N   
5724 C CA  . VAL B 90  ? 0.5780 0.4945 0.6253 0.0381  -0.1184 -0.0764 75  VAL B CA  
5725 C C   . VAL B 90  ? 0.5894 0.4922 0.6133 0.0428  -0.1156 -0.0892 75  VAL B C   
5726 O O   . VAL B 90  ? 0.6276 0.5460 0.6643 0.0515  -0.1062 -0.0958 75  VAL B O   
5727 C CB  . VAL B 90  ? 0.5465 0.4908 0.6050 0.0270  -0.1113 -0.0617 75  VAL B CB  
5728 C CG1 . VAL B 90  ? 0.6003 0.5403 0.6300 0.0124  -0.1136 -0.0555 75  VAL B CG1 
5729 C CG2 . VAL B 90  ? 0.6146 0.5687 0.6928 0.0253  -0.1132 -0.0492 75  VAL B CG2 
5739 N N   . ALA B 91  ? 0.6188 0.4915 0.6066 0.0365  -0.1232 -0.0925 76  ALA B N   
5740 C CA  . ALA B 91  ? 0.6556 0.5051 0.6139 0.0429  -0.1215 -0.1063 76  ALA B CA  
5741 C C   . ALA B 91  ? 0.6633 0.5285 0.6130 0.0355  -0.1117 -0.1043 76  ALA B C   
5742 O O   . ALA B 91  ? 0.6545 0.5340 0.6015 0.0187  -0.1119 -0.0914 76  ALA B O   
5743 C CB  . ALA B 91  ? 0.6907 0.4980 0.6070 0.0353  -0.1332 -0.1096 76  ALA B CB  
5749 N N   . TYR B 92  ? 0.7490 0.6124 0.6938 0.0489  -0.1031 -0.1169 77  TYR B N   
5750 C CA  . TYR B 92  ? 0.7039 0.5770 0.6345 0.0436  -0.0930 -0.1175 77  TYR B CA  
5751 C C   . TYR B 92  ? 0.7801 0.6119 0.6579 0.0385  -0.0976 -0.1258 77  TYR B C   
5752 O O   . TYR B 92  ? 0.8223 0.6212 0.6791 0.0520  -0.1009 -0.1390 77  TYR B O   
5753 C CB  . TYR B 92  ? 0.7065 0.6031 0.6608 0.0610  -0.0793 -0.1263 77  TYR B CB  
5754 C CG  . TYR B 92  ? 0.8054 0.7082 0.7410 0.0584  -0.0676 -0.1294 77  TYR B CG  
5755 C CD1 . TYR B 92  ? 0.8564 0.7890 0.8044 0.0447  -0.0606 -0.1173 77  TYR B CD1 
5756 C CD2 . TYR B 92  ? 0.8231 0.6998 0.7261 0.0705  -0.0630 -0.1444 77  TYR B CD2 
5757 C CE1 . TYR B 92  ? 0.8120 0.7493 0.7408 0.0416  -0.0498 -0.1199 77  TYR B CE1 
5758 C CE2 . TYR B 92  ? 0.8850 0.7657 0.7679 0.0684  -0.0514 -0.1477 77  TYR B CE2 
5759 C CZ  . TYR B 92  ? 0.8393 0.7511 0.7356 0.0532  -0.0450 -0.1353 77  TYR B CZ  
5760 O OH  . TYR B 92  ? 0.8553 0.7703 0.7297 0.0504  -0.0334 -0.1383 77  TYR B OH  
5770 N N   . HIS B 93  ? 0.7581 0.5900 0.6125 0.0189  -0.0984 -0.1177 78  HIS B N   
5771 C CA  . HIS B 93  ? 0.8084 0.5994 0.6084 0.0089  -0.1042 -0.1238 78  HIS B CA  
5772 C C   . HIS B 93  ? 0.8370 0.6269 0.6124 0.0078  -0.0935 -0.1294 78  HIS B C   
5773 O O   . HIS B 93  ? 0.8876 0.6364 0.6148 0.0070  -0.0955 -0.1402 78  HIS B O   
5774 C CB  . HIS B 93  ? 0.8081 0.5947 0.5921 -0.0171 -0.1174 -0.1094 78  HIS B CB  
5775 C CG  . HIS B 93  ? 0.7986 0.5767 0.5939 -0.0180 -0.1286 -0.1051 78  HIS B CG  
5776 N ND1 . HIS B 93  ? 0.8913 0.6449 0.6875 0.0001  -0.1311 -0.1170 78  HIS B ND1 
5777 C CD2 . HIS B 93  ? 0.8151 0.6072 0.6209 -0.0343 -0.1376 -0.0898 78  HIS B CD2 
5778 C CE1 . HIS B 93  ? 0.8919 0.6422 0.6967 -0.0062 -0.1413 -0.1096 78  HIS B CE1 
5779 N NE2 . HIS B 93  ? 0.9298 0.7040 0.7410 -0.0267 -0.1448 -0.0931 78  HIS B NE2 
5787 N N   . GLY B 94  ? 0.8659 0.6961 0.6693 0.0071  -0.0824 -0.1225 79  GLY B N   
5788 C CA  . GLY B 94  ? 0.8656 0.6964 0.6453 0.0049  -0.0716 -0.1268 79  GLY B CA  
5789 C C   . GLY B 94  ? 0.8042 0.6798 0.6132 -0.0046 -0.0639 -0.1126 79  GLY B C   
5790 O O   . GLY B 94  ? 0.7646 0.6665 0.6061 -0.0119 -0.0685 -0.0982 79  GLY B O   
5794 N N   . SER B 95  ? 0.8248 0.7062 0.6188 -0.0037 -0.0516 -0.1168 80  SER B N   
5795 C CA  . SER B 95  ? 0.8090 0.7292 0.6253 -0.0119 -0.0428 -0.1044 80  SER B CA  
5796 C C   . SER B 95  ? 0.8402 0.7490 0.6138 -0.0240 -0.0384 -0.1052 80  SER B C   
5797 O O   . SER B 95  ? 0.8944 0.7693 0.6268 -0.0189 -0.0359 -0.1196 80  SER B O   
5798 C CB  . SER B 95  ? 0.7915 0.7436 0.6493 0.0056  -0.0278 -0.1084 80  SER B CB  
5799 O OG  . SER B 95  ? 0.8372 0.7743 0.6826 0.0253  -0.0186 -0.1266 80  SER B OG  
5805 N N   . TYR B 96  ? 0.8250 0.7602 0.6061 -0.0398 -0.0378 -0.0893 81  TYR B N   
5806 C CA  . TYR B 96  ? 0.8636 0.7910 0.6047 -0.0545 -0.0356 -0.0870 81  TYR B CA  
5807 C C   . TYR B 96  ? 0.8531 0.8181 0.6173 -0.0572 -0.0236 -0.0762 81  TYR B C   
5808 O O   . TYR B 96  ? 0.8006 0.7947 0.6008 -0.0614 -0.0264 -0.0607 81  TYR B O   
5809 C CB  . TYR B 96  ? 0.8728 0.7875 0.5866 -0.0780 -0.0536 -0.0752 81  TYR B CB  
5810 C CG  . TYR B 96  ? 0.8973 0.7724 0.5835 -0.0800 -0.0667 -0.0840 81  TYR B CG  
5811 C CD1 . TYR B 96  ? 0.8673 0.7441 0.5823 -0.0734 -0.0745 -0.0823 81  TYR B CD1 
5812 C CD2 . TYR B 96  ? 0.9807 0.8136 0.6084 -0.0897 -0.0715 -0.0938 81  TYR B CD2 
5813 C CE1 . TYR B 96  ? 0.8919 0.7312 0.5799 -0.0763 -0.0866 -0.0896 81  TYR B CE1 
5814 C CE2 . TYR B 96  ? 0.9814 0.7739 0.5801 -0.0932 -0.0840 -0.1014 81  TYR B CE2 
5815 C CZ  . TYR B 96  ? 0.9950 0.7917 0.6248 -0.0865 -0.0914 -0.0990 81  TYR B CZ  
5816 O OH  . TYR B 96  ? 1.0474 0.8027 0.6472 -0.0909 -0.1039 -0.1059 81  TYR B OH  
5826 N N   . LEU B 97  ? 0.8710 0.8329 0.6118 -0.0546 -0.0100 -0.0842 82  LEU B N   
5827 C CA  . LEU B 97  ? 0.8621 0.8547 0.6146 -0.0601 0.0017  -0.0742 82  LEU B CA  
5828 C C   . LEU B 97  ? 0.9169 0.8962 0.6226 -0.0798 -0.0029 -0.0681 82  LEU B C   
5829 O O   . LEU B 97  ? 0.9588 0.9062 0.6181 -0.0803 -0.0009 -0.0812 82  LEU B O   
5830 C CB  . LEU B 97  ? 0.8683 0.8732 0.6323 -0.0427 0.0223  -0.0868 82  LEU B CB  
5831 C CG  . LEU B 97  ? 0.8720 0.9069 0.6450 -0.0494 0.0360  -0.0772 82  LEU B CG  
5832 C CD1 . LEU B 97  ? 0.8442 0.9099 0.6599 -0.0564 0.0317  -0.0582 82  LEU B CD1 
5833 C CD2 . LEU B 97  ? 0.8923 0.9408 0.6748 -0.0326 0.0569  -0.0905 82  LEU B CD2 
5845 N N   . TRP B 98  ? 0.8810 0.8831 0.5968 -0.0953 -0.0093 -0.0481 83  TRP B N   
5846 C CA  . TRP B 98  ? 0.9137 0.9069 0.5876 -0.1159 -0.0172 -0.0394 83  TRP B CA  
5847 C C   . TRP B 98  ? 0.9137 0.9413 0.6101 -0.1261 -0.0185 -0.0170 83  TRP B C   
5848 O O   . TRP B 98  ? 0.8520 0.9003 0.5867 -0.1241 -0.0250 -0.0044 83  TRP B O   
5849 C CB  . TRP B 98  ? 0.9848 0.9529 0.6320 -0.1288 -0.0371 -0.0385 83  TRP B CB  
5850 C CG  . TRP B 98  ? 1.0346 0.9859 0.6297 -0.1507 -0.0459 -0.0342 83  TRP B CG  
5851 C CD1 . TRP B 98  ? 1.0235 0.9872 0.6112 -0.1718 -0.0626 -0.0156 83  TRP B CD1 
5852 C CD2 . TRP B 98  ? 1.1459 1.0652 0.6874 -0.1537 -0.0387 -0.0485 83  TRP B CD2 
5853 N NE1 . TRP B 98  ? 1.1443 1.0863 0.6774 -0.1897 -0.0676 -0.0171 83  TRP B NE1 
5854 C CE2 . TRP B 98  ? 1.1869 1.0987 0.6888 -0.1790 -0.0529 -0.0377 83  TRP B CE2 
5855 C CE3 . TRP B 98  ? 1.1472 1.0445 0.6699 -0.1366 -0.0213 -0.0691 83  TRP B CE3 
5856 C CZ2 . TRP B 98  ? 1.2702 1.1488 0.7112 -0.1892 -0.0507 -0.0475 83  TRP B CZ2 
5857 C CZ3 . TRP B 98  ? 1.2549 1.1195 0.7177 -0.1444 -0.0177 -0.0791 83  TRP B CZ3 
5858 C CH2 . TRP B 98  ? 1.2898 1.1431 0.7107 -0.1712 -0.0325 -0.0686 83  TRP B CH2 
5869 N N   . LEU B 99  ? 1.1850 1.0786 0.3342 -0.1196 -0.0610 -0.0947 84  LEU B N   
5870 C CA  . LEU B 99  ? 1.1802 1.0904 0.3339 -0.1346 -0.0754 -0.0650 84  LEU B CA  
5871 C C   . LEU B 99  ? 1.1868 1.1234 0.3729 -0.1288 -0.0622 -0.0467 84  LEU B C   
5872 O O   . LEU B 99  ? 1.1474 1.0951 0.3599 -0.1370 -0.0775 -0.0209 84  LEU B O   
5873 C CB  . LEU B 99  ? 1.2303 1.1309 0.4000 -0.1490 -0.1080 -0.0491 84  LEU B CB  
5874 C CG  . LEU B 99  ? 1.3541 1.2364 0.4899 -0.1643 -0.1285 -0.0527 84  LEU B CG  
5875 C CD1 . LEU B 99  ? 1.3039 1.1631 0.4022 -0.1578 -0.1167 -0.0853 84  LEU B CD1 
5876 C CD2 . LEU B 99  ? 1.2761 1.1513 0.4389 -0.1759 -0.1588 -0.0387 84  LEU B CD2 
5888 N N   . GLN B 100 ? 1.2114 1.1588 0.3976 -0.1143 -0.0337 -0.0601 85  GLN B N   
5889 C CA  . GLN B 100 ? 1.1237 1.0960 0.3414 -0.1088 -0.0191 -0.0452 85  GLN B CA  
5890 C C   . GLN B 100 ? 1.1121 1.0855 0.3726 -0.1068 -0.0305 -0.0336 85  GLN B C   
5891 O O   . GLN B 100 ? 1.0855 1.0770 0.3742 -0.1084 -0.0300 -0.0126 85  GLN B O   
5892 C CB  . GLN B 100 ? 1.2213 1.2104 0.4321 -0.1212 -0.0216 -0.0206 85  GLN B CB  
5893 C CG  . GLN B 100 ? 1.1543 1.1497 0.3279 -0.1207 -0.0014 -0.0303 85  GLN B CG  
5894 C CD  . GLN B 100 ? 1.2697 1.2726 0.4262 -0.1375 -0.0111 -0.0069 85  GLN B CD  
5895 O OE1 . GLN B 100 ? 1.2319 1.2344 0.4054 -0.1486 -0.0342 0.0162  85  GLN B OE1 
5896 N NE2 . GLN B 100 ? 1.2180 1.2275 0.3412 -0.1389 0.0066  -0.0128 85  GLN B NE2 
5905 N N   . LYS B 101 ? 1.0251 0.9777 0.2903 -0.1035 -0.0407 -0.0472 86  LYS B N   
5906 C CA  . LYS B 101 ? 0.9758 0.9267 0.2783 -0.1008 -0.0498 -0.0391 86  LYS B CA  
5907 C C   . LYS B 101 ? 0.9628 0.9020 0.2803 -0.0823 -0.0341 -0.0636 86  LYS B C   
5908 O O   . LYS B 101 ? 0.9897 0.9051 0.2761 -0.0805 -0.0335 -0.0868 86  LYS B O   
5909 C CB  . LYS B 101 ? 1.0072 0.9447 0.3163 -0.1133 -0.0803 -0.0275 86  LYS B CB  
5910 C CG  . LYS B 101 ? 1.0087 0.9622 0.3305 -0.1258 -0.0979 0.0025  86  LYS B CG  
5911 C CD  . LYS B 101 ? 1.0419 0.9861 0.3761 -0.1369 -0.1278 0.0134  86  LYS B CD  
5912 C CE  . LYS B 101 ? 1.2120 1.1455 0.5124 -0.1499 -0.1421 0.0105  86  LYS B CE  
5913 N NZ  . LYS B 101 ? 1.3526 1.3005 0.6415 -0.1577 -0.1438 0.0288  86  LYS B NZ  
5927 N N   . LEU B 102 ? 0.9007 0.8548 0.2662 -0.0683 -0.0224 -0.0581 87  LEU B N   
5928 C CA  . LEU B 102 ? 0.8838 0.8285 0.2719 -0.0499 -0.0100 -0.0771 87  LEU B CA  
5929 C C   . LEU B 102 ? 0.8471 0.7797 0.2731 -0.0485 -0.0268 -0.0699 87  LEU B C   
5930 O O   . LEU B 102 ? 0.8538 0.8005 0.3146 -0.0510 -0.0340 -0.0486 87  LEU B O   
5931 C CB  . LEU B 102 ? 0.8932 0.8623 0.3087 -0.0364 0.0131  -0.0760 87  LEU B CB  
5932 C CG  . LEU B 102 ? 0.8827 0.8434 0.3208 -0.0167 0.0255  -0.0953 87  LEU B CG  
5933 C CD1 . LEU B 102 ? 0.9304 0.8742 0.3292 -0.0100 0.0364  -0.1233 87  LEU B CD1 
5934 C CD2 . LEU B 102 ? 0.8346 0.8221 0.3094 -0.0056 0.0428  -0.0886 87  LEU B CD2 
5946 N N   . TRP B 103 ? 0.8822 0.7879 0.3002 -0.0447 -0.0326 -0.0878 88  TRP B N   
5947 C CA  . TRP B 103 ? 0.8357 0.7287 0.2871 -0.0435 -0.0462 -0.0833 88  TRP B CA  
5948 C C   . TRP B 103 ? 0.8375 0.7219 0.3108 -0.0250 -0.0323 -0.0980 88  TRP B C   
5949 O O   . TRP B 103 ? 0.8851 0.7557 0.3353 -0.0155 -0.0211 -0.1200 88  TRP B O   
5950 C CB  . TRP B 103 ? 0.8933 0.7597 0.3193 -0.0568 -0.0672 -0.0898 88  TRP B CB  
5951 C CG  . TRP B 103 ? 0.8944 0.7678 0.2980 -0.0759 -0.0843 -0.0752 88  TRP B CG  
5952 C CD1 . TRP B 103 ? 0.9434 0.8183 0.3006 -0.0847 -0.0826 -0.0790 88  TRP B CD1 
5953 C CD2 . TRP B 103 ? 0.8779 0.7580 0.3044 -0.0891 -0.1067 -0.0540 88  TRP B CD2 
5954 N NE1 . TRP B 103 ? 1.0000 0.8806 0.3486 -0.1031 -0.1046 -0.0603 88  TRP B NE1 
5955 C CE2 . TRP B 103 ? 0.9124 0.7974 0.3058 -0.1054 -0.1198 -0.0447 88  TRP B CE2 
5956 C CE3 . TRP B 103 ? 0.9117 0.7957 0.3842 -0.0887 -0.1163 -0.0415 88  TRP B CE3 
5957 C CZ2 . TRP B 103 ? 0.9868 0.8813 0.3955 -0.1200 -0.1436 -0.0228 88  TRP B CZ2 
5958 C CZ3 . TRP B 103 ? 0.9791 0.8743 0.4675 -0.1026 -0.1374 -0.0210 88  TRP B CZ3 
5959 C CH2 . TRP B 103 ? 0.8683 0.7689 0.3268 -0.1176 -0.1516 -0.0115 88  TRP B CH2 
5970 N N   . ILE B 104 ? 0.7715 0.6635 0.2884 -0.0194 -0.0332 -0.0859 89  ILE B N   
5971 C CA  . ILE B 104 ? 0.8173 0.6990 0.3574 -0.0041 -0.0250 -0.0962 89  ILE B CA  
5972 C C   . ILE B 104 ? 0.7893 0.6514 0.3458 -0.0097 -0.0415 -0.0921 89  ILE B C   
5973 O O   . ILE B 104 ? 0.7175 0.5911 0.2977 -0.0179 -0.0506 -0.0734 89  ILE B O   
5974 C CB  . ILE B 104 ? 0.7800 0.6863 0.3544 0.0061  -0.0113 -0.0858 89  ILE B CB  
5975 C CG1 . ILE B 104 ? 0.7224 0.6510 0.2823 0.0094  0.0054  -0.0883 89  ILE B CG1 
5976 C CG2 . ILE B 104 ? 0.6983 0.5925 0.2952 0.0207  -0.0059 -0.0952 89  ILE B CG2 
5977 C CD1 . ILE B 104 ? 0.7240 0.6781 0.2940 0.0002  0.0051  -0.0663 89  ILE B CD1 
5989 N N   . CYS B 105 ? 0.8312 0.6637 0.3753 -0.0052 -0.0447 -0.1095 90  CYS B N   
5990 C CA  . CYS B 105 ? 0.7666 0.5782 0.3240 -0.0115 -0.0597 -0.1065 90  CYS B CA  
5991 C C   . CYS B 105 ? 0.8476 0.6575 0.4375 0.0012  -0.0525 -0.1047 90  CYS B C   
5992 O O   . CYS B 105 ? 0.8391 0.6422 0.4278 0.0167  -0.0409 -0.1181 90  CYS B O   
5993 C CB  . CYS B 105 ? 0.8582 0.6335 0.3812 -0.0160 -0.0698 -0.1254 90  CYS B CB  
5994 S SG  . CYS B 105 ? 0.9508 0.6992 0.4867 -0.0284 -0.0904 -0.1204 90  CYS B SG  
6000 N N   . MET B 106 ? 0.7057 0.5222 0.3244 -0.0052 -0.0592 -0.0881 91  MET B N   
6001 C CA  . MET B 106 ? 0.6725 0.4906 0.3203 0.0044  -0.0526 -0.0831 91  MET B CA  
6002 C C   . MET B 106 ? 0.6865 0.4884 0.3476 -0.0047 -0.0645 -0.0761 91  MET B C   
6003 O O   . MET B 106 ? 0.6812 0.4788 0.3373 -0.0194 -0.0775 -0.0710 91  MET B O   
6004 C CB  . MET B 106 ? 0.7176 0.5669 0.3898 0.0069  -0.0433 -0.0674 91  MET B CB  
6005 C CG  . MET B 106 ? 0.8130 0.6827 0.4749 0.0122  -0.0320 -0.0695 91  MET B CG  
6006 S SD  . MET B 106 ? 0.6815 0.5819 0.3700 0.0095  -0.0270 -0.0479 91  MET B SD  
6007 C CE  . MET B 106 ? 0.6384 0.5436 0.3236 -0.0072 -0.0425 -0.0346 91  MET B CE  
6017 N N   . GLU B 107 ? 0.7273 0.5219 0.4062 0.0034  -0.0600 -0.0748 92  GLU B N   
6018 C CA  . GLU B 107 ? 0.7405 0.5247 0.4353 -0.0050 -0.0676 -0.0651 92  GLU B CA  
6019 C C   . GLU B 107 ? 0.7260 0.5357 0.4409 -0.0161 -0.0692 -0.0469 92  GLU B C   
6020 O O   . GLU B 107 ? 0.6732 0.5076 0.4009 -0.0116 -0.0603 -0.0388 92  GLU B O   
6021 C CB  . GLU B 107 ? 0.7533 0.5310 0.4622 0.0064  -0.0604 -0.0646 92  GLU B CB  
6022 C CG  . GLU B 107 ? 0.7056 0.4777 0.4311 -0.0017 -0.0641 -0.0523 92  GLU B CG  
6023 C CD  . GLU B 107 ? 0.8445 0.6104 0.5796 0.0092  -0.0578 -0.0516 92  GLU B CD  
6024 O OE1 . GLU B 107 ? 0.6624 0.4313 0.3955 0.0233  -0.0512 -0.0599 92  GLU B OE1 
6025 O OE2 . GLU B 107 ? 0.8425 0.6018 0.5870 0.0030  -0.0595 -0.0420 92  GLU B OE2 
6032 N N   . PHE B 108 ? 0.6263 0.4297 0.3459 -0.0305 -0.0806 -0.0403 93  PHE B N   
6033 C CA  . PHE B 108 ? 0.6045 0.4334 0.3475 -0.0404 -0.0824 -0.0231 93  PHE B CA  
6034 C C   . PHE B 108 ? 0.6891 0.5228 0.4564 -0.0393 -0.0748 -0.0131 93  PHE B C   
6035 O O   . PHE B 108 ? 0.6243 0.4370 0.3894 -0.0424 -0.0775 -0.0151 93  PHE B O   
6036 C CB  . PHE B 108 ? 0.6269 0.4522 0.3662 -0.0577 -0.0988 -0.0196 93  PHE B CB  
6037 C CG  . PHE B 108 ? 0.6728 0.5271 0.4426 -0.0671 -0.1012 -0.0012 93  PHE B CG  
6038 C CD1 . PHE B 108 ? 0.6527 0.5338 0.4324 -0.0650 -0.0997 0.0075  93  PHE B CD1 
6039 C CD2 . PHE B 108 ? 0.6467 0.5019 0.4365 -0.0778 -0.1046 0.0080  93  PHE B CD2 
6040 C CE1 . PHE B 108 ? 0.6923 0.6004 0.5039 -0.0712 -0.1019 0.0243  93  PHE B CE1 
6041 C CE2 . PHE B 108 ? 0.5967 0.4817 0.4184 -0.0848 -0.1050 0.0244  93  PHE B CE2 
6042 C CZ  . PHE B 108 ? 0.6689 0.5803 0.5029 -0.0804 -0.1038 0.0322  93  PHE B CZ  
6052 N N   . CYS B 109 ? 0.6108 0.4698 0.3987 -0.0353 -0.0656 -0.0023 94  CYS B N   
6053 C CA  . CYS B 109 ? 0.6594 0.5245 0.4677 -0.0336 -0.0561 0.0065  94  CYS B CA  
6054 C C   . CYS B 109 ? 0.5765 0.4651 0.4102 -0.0426 -0.0573 0.0207  94  CYS B C   
6055 O O   . CYS B 109 ? 0.5571 0.4674 0.4031 -0.0395 -0.0551 0.0274  94  CYS B O   
6056 C CB  . CYS B 109 ? 0.5586 0.4306 0.3690 -0.0201 -0.0435 0.0056  94  CYS B CB  
6057 S SG  . CYS B 109 ? 0.6734 0.5232 0.4619 -0.0085 -0.0416 -0.0096 94  CYS B SG  
6063 N N   . GLY B 110 ? 0.5275 0.4123 0.3705 -0.0539 -0.0611 0.0259  95  GLY B N   
6064 C CA  . GLY B 110 ? 0.6002 0.5091 0.4692 -0.0643 -0.0649 0.0387  95  GLY B CA  
6065 C C   . GLY B 110 ? 0.5590 0.4931 0.4565 -0.0578 -0.0511 0.0492  95  GLY B C   
6066 O O   . GLY B 110 ? 0.6333 0.5928 0.5563 -0.0617 -0.0537 0.0598  95  GLY B O   
6070 N N   . ALA B 111 ? 0.5038 0.4306 0.3978 -0.0480 -0.0371 0.0464  96  ALA B N   
6071 C CA  . ALA B 111 ? 0.5508 0.4963 0.4678 -0.0415 -0.0229 0.0541  96  ALA B CA  
6072 C C   . ALA B 111 ? 0.5355 0.4901 0.4550 -0.0292 -0.0191 0.0542  96  ALA B C   
6073 O O   . ALA B 111 ? 0.4598 0.4271 0.3978 -0.0224 -0.0081 0.0598  96  ALA B O   
6074 C CB  . ALA B 111 ? 0.5409 0.4719 0.4502 -0.0394 -0.0101 0.0517  96  ALA B CB  
6080 N N   . GLY B 112 ? 0.5368 0.4845 0.4375 -0.0265 -0.0273 0.0482  97  GLY B N   
6081 C CA  . GLY B 112 ? 0.4859 0.4415 0.3872 -0.0171 -0.0242 0.0497  97  GLY B CA  
6082 C C   . GLY B 112 ? 0.4783 0.4219 0.3691 -0.0075 -0.0128 0.0441  97  GLY B C   
6083 O O   . GLY B 112 ? 0.4896 0.4155 0.3629 -0.0070 -0.0116 0.0357  97  GLY B O   
6087 N N   . SER B 113 ? 0.4995 0.4515 0.4013 -0.0002 -0.0057 0.0493  98  SER B N   
6088 C CA  . SER B 113 ? 0.4319 0.3729 0.3250 0.0073  0.0038  0.0452  98  SER B CA  
6089 C C   . SER B 113 ? 0.4369 0.3753 0.3415 0.0095  0.0157  0.0474  98  SER B C   
6090 O O   . SER B 113 ? 0.4226 0.3727 0.3470 0.0075  0.0186  0.0534  98  SER B O   
6091 C CB  . SER B 113 ? 0.5351 0.4824 0.4286 0.0125  0.0033  0.0490  98  SER B CB  
6092 O OG  . SER B 113 ? 0.4419 0.4015 0.3581 0.0153  0.0051  0.0588  98  SER B OG  
6098 N N   . LEU B 114 ? 0.4227 0.3462 0.3142 0.0135  0.0228  0.0424  99  LEU B N   
6099 C CA  . LEU B 114 ? 0.4255 0.3432 0.3214 0.0157  0.0351  0.0430  99  LEU B CA  
6100 C C   . LEU B 114 ? 0.4261 0.3546 0.3423 0.0223  0.0412  0.0490  99  LEU B C   
6101 O O   . LEU B 114 ? 0.4851 0.4163 0.4136 0.0244  0.0521  0.0506  99  LEU B O   
6102 C CB  . LEU B 114 ? 0.4298 0.3280 0.3047 0.0174  0.0385  0.0367  99  LEU B CB  
6103 C CG  . LEU B 114 ? 0.4525 0.3365 0.3105 0.0118  0.0357  0.0320  99  LEU B CG  
6104 C CD1 . LEU B 114 ? 0.5506 0.4181 0.3901 0.0139  0.0352  0.0272  99  LEU B CD1 
6105 C CD2 . LEU B 114 ? 0.4471 0.3297 0.3084 0.0066  0.0440  0.0345  99  LEU B CD2 
6117 N N   . GLN B 115 ? 0.4183 0.3524 0.3381 0.0259  0.0349  0.0526  100 GLN B N   
6118 C CA  . GLN B 115 ? 0.4334 0.3759 0.3743 0.0327  0.0380  0.0598  100 GLN B CA  
6119 C C   . GLN B 115 ? 0.4626 0.4264 0.4308 0.0317  0.0361  0.0673  100 GLN B C   
6120 O O   . GLN B 115 ? 0.4300 0.4009 0.4207 0.0382  0.0448  0.0712  100 GLN B O   
6121 C CB  . GLN B 115 ? 0.4392 0.3824 0.3760 0.0344  0.0295  0.0641  100 GLN B CB  
6122 C CG  . GLN B 115 ? 0.5108 0.4571 0.4675 0.0420  0.0310  0.0724  100 GLN B CG  
6123 C CD  . GLN B 115 ? 0.4481 0.3944 0.3982 0.0411  0.0211  0.0787  100 GLN B CD  
6124 O OE1 . GLN B 115 ? 0.6029 0.5358 0.5364 0.0405  0.0225  0.0758  100 GLN B OE1 
6125 N NE2 . GLN B 115 ? 0.5552 0.5174 0.5176 0.0394  0.0104  0.0883  100 GLN B NE2 
6134 N N   . ASP B 116 ? 0.4151 0.3893 0.3826 0.0236  0.0245  0.0692  101 ASP B N   
6135 C CA  . ASP B 116 ? 0.4189 0.4143 0.4130 0.0200  0.0209  0.0770  101 ASP B CA  
6136 C C   . ASP B 116 ? 0.4174 0.4156 0.4227 0.0189  0.0343  0.0753  101 ASP B C   
6137 O O   . ASP B 116 ? 0.4932 0.5120 0.5293 0.0202  0.0381  0.0826  101 ASP B O   
6138 C CB  . ASP B 116 ? 0.4932 0.4935 0.4779 0.0090  0.0055  0.0772  101 ASP B CB  
6139 C CG  . ASP B 116 ? 0.4782 0.4780 0.4497 0.0088  -0.0066 0.0790  101 ASP B CG  
6140 O OD1 . ASP B 116 ? 0.5250 0.5289 0.5058 0.0156  -0.0067 0.0855  101 ASP B OD1 
6141 O OD2 . ASP B 116 ? 0.5081 0.5022 0.4585 0.0014  -0.0159 0.0737  101 ASP B OD2 
6146 N N   . ILE B 117 ? 0.5170 0.4961 0.4982 0.0160  0.0415  0.0667  102 ILE B N   
6147 C CA  . ILE B 117 ? 0.5167 0.4971 0.5026 0.0120  0.0537  0.0657  102 ILE B CA  
6148 C C   . ILE B 117 ? 0.4849 0.4628 0.4786 0.0221  0.0717  0.0640  102 ILE B C   
6149 O O   . ILE B 117 ? 0.4856 0.4809 0.5045 0.0241  0.0830  0.0681  102 ILE B O   
6150 C CB  . ILE B 117 ? 0.4800 0.4390 0.4349 0.0035  0.0518  0.0586  102 ILE B CB  
6151 C CG1 . ILE B 117 ? 0.5110 0.4709 0.4599 -0.0058 0.0350  0.0591  102 ILE B CG1 
6152 C CG2 . ILE B 117 ? 0.4455 0.4027 0.3999 -0.0017 0.0656  0.0586  102 ILE B CG2 
6153 C CD1 . ILE B 117 ? 0.5362 0.4718 0.4551 -0.0109 0.0301  0.0516  102 ILE B CD1 
6165 N N   . TYR B 118 ? 0.4567 0.4133 0.4296 0.0285  0.0750  0.0577  103 TYR B N   
6166 C CA  . TYR B 118 ? 0.5200 0.4676 0.4931 0.0369  0.0922  0.0537  103 TYR B CA  
6167 C C   . TYR B 118 ? 0.5701 0.5330 0.5761 0.0488  0.0967  0.0592  103 TYR B C   
6168 O O   . TYR B 118 ? 0.5571 0.5193 0.5727 0.0567  0.1136  0.0563  103 TYR B O   
6169 C CB  . TYR B 118 ? 0.5295 0.4480 0.4701 0.0384  0.0927  0.0456  103 TYR B CB  
6170 C CG  . TYR B 118 ? 0.5186 0.4301 0.4562 0.0436  0.0827  0.0467  103 TYR B CG  
6171 C CD1 . TYR B 118 ? 0.4976 0.4142 0.4561 0.0535  0.0843  0.0512  103 TYR B CD1 
6172 C CD2 . TYR B 118 ? 0.4677 0.3670 0.3819 0.0386  0.0722  0.0436  103 TYR B CD2 
6173 C CE1 . TYR B 118 ? 0.5424 0.4510 0.4961 0.0561  0.0749  0.0538  103 TYR B CE1 
6174 C CE2 . TYR B 118 ? 0.4415 0.3366 0.3530 0.0415  0.0645  0.0456  103 TYR B CE2 
6175 C CZ  . TYR B 118 ? 0.4445 0.3433 0.3742 0.0493  0.0656  0.0511  103 TYR B CZ  
6176 O OH  . TYR B 118 ? 0.4710 0.3645 0.3965 0.0502  0.0575  0.0547  103 TYR B OH  
6186 N N   . GLN B 119 ? 0.4713 0.4473 0.4943 0.0507  0.0822  0.0672  104 GLN B N   
6187 C CA  . GLN B 119 ? 0.5514 0.5436 0.6098 0.0620  0.0842  0.0748  104 GLN B CA  
6188 C C   . GLN B 119 ? 0.6036 0.6236 0.6963 0.0628  0.0937  0.0797  104 GLN B C   
6189 O O   . GLN B 119 ? 0.5548 0.5885 0.6805 0.0750  0.1009  0.0842  104 GLN B O   
6190 C CB  . GLN B 119 ? 0.5538 0.5552 0.6210 0.0612  0.0643  0.0844  104 GLN B CB  
6191 C CG  . GLN B 119 ? 0.5381 0.5169 0.5826 0.0641  0.0582  0.0826  104 GLN B CG  
6192 C CD  . GLN B 119 ? 0.5316 0.5199 0.5797 0.0608  0.0392  0.0926  104 GLN B CD  
6193 O OE1 . GLN B 119 ? 0.6067 0.6151 0.6664 0.0541  0.0286  0.0990  104 GLN B OE1 
6194 N NE2 . GLN B 119 ? 0.4667 0.4397 0.5025 0.0639  0.0344  0.0945  104 GLN B NE2 
6203 N N   . VAL B 120 ? 0.6038 0.6326 0.6913 0.0501  0.0939  0.0794  105 VAL B N   
6204 C CA  . VAL B 120 ? 0.6059 0.6627 0.7250 0.0477  0.1043  0.0845  105 VAL B CA  
6205 C C   . VAL B 120 ? 0.5448 0.5912 0.6468 0.0456  0.1259  0.0759  105 VAL B C   
6206 O O   . VAL B 120 ? 0.4801 0.5423 0.6061 0.0526  0.1447  0.0761  105 VAL B O   
6207 C CB  . VAL B 120 ? 0.5786 0.6542 0.7061 0.0322  0.0875  0.0924  105 VAL B CB  
6208 C CG1 . VAL B 120 ? 0.6114 0.7206 0.7774 0.0283  0.0968  0.1001  105 VAL B CG1 
6209 C CG2 . VAL B 120 ? 0.5306 0.6126 0.6660 0.0324  0.0650  0.0999  105 VAL B CG2 
6219 N N   . THR B 121 ? 0.5252 0.5451 0.5854 0.0361  0.1237  0.0686  106 THR B N   
6220 C CA  . THR B 121 ? 0.5176 0.5264 0.5565 0.0303  0.1410  0.0624  106 THR B CA  
6221 C C   . THR B 121 ? 0.5853 0.5721 0.6063 0.0416  0.1583  0.0524  106 THR B C   
6222 O O   . THR B 121 ? 0.5394 0.5227 0.5496 0.0395  0.1773  0.0476  106 THR B O   
6223 C CB  . THR B 121 ? 0.5775 0.5644 0.5786 0.0159  0.1295  0.0596  106 THR B CB  
6224 O OG1 . THR B 121 ? 0.5651 0.5262 0.5395 0.0203  0.1190  0.0535  106 THR B OG1 
6225 C CG2 . THR B 121 ? 0.5557 0.5587 0.5697 0.0039  0.1124  0.0676  106 THR B CG2 
6233 N N   . GLY B 122 ? 0.5475 0.5184 0.5633 0.0522  0.1520  0.0491  107 GLY B N   
6234 C CA  . GLY B 122 ? 0.5087 0.4500 0.4976 0.0595  0.1637  0.0384  107 GLY B CA  
6235 C C   . GLY B 122 ? 0.5637 0.4753 0.5079 0.0495  0.1540  0.0327  107 GLY B C   
6236 O O   . GLY B 122 ? 0.4976 0.4109 0.4328 0.0390  0.1388  0.0364  107 GLY B O   
6240 N N   . SER B 123 ? 0.5746 0.4577 0.4905 0.0530  0.1626  0.0231  108 SER B N   
6241 C CA  . SER B 123 ? 0.5688 0.4242 0.4458 0.0449  0.1514  0.0185  108 SER B CA  
6242 C C   . SER B 123 ? 0.5932 0.4456 0.4480 0.0307  0.1492  0.0193  108 SER B C   
6243 O O   . SER B 123 ? 0.5754 0.4385 0.4338 0.0261  0.1620  0.0206  108 SER B O   
6244 C CB  . SER B 123 ? 0.5652 0.3899 0.4157 0.0498  0.1609  0.0083  108 SER B CB  
6245 O OG  . SER B 123 ? 0.5920 0.4092 0.4258 0.0479  0.1809  0.0018  108 SER B OG  
6251 N N   . LEU B 124 ? 0.5494 0.3871 0.3821 0.0237  0.1327  0.0191  109 LEU B N   
6252 C CA  . LEU B 124 ? 0.5705 0.4010 0.3817 0.0112  0.1270  0.0206  109 LEU B CA  
6253 C C   . LEU B 124 ? 0.5701 0.3739 0.3434 0.0054  0.1354  0.0145  109 LEU B C   
6254 O O   . LEU B 124 ? 0.5848 0.3703 0.3424 0.0101  0.1397  0.0078  109 LEU B O   
6255 C CB  . LEU B 124 ? 0.5801 0.4069 0.3862 0.0081  0.1059  0.0226  109 LEU B CB  
6256 C CG  . LEU B 124 ? 0.5097 0.3587 0.3411 0.0075  0.0954  0.0287  109 LEU B CG  
6257 C CD1 . LEU B 124 ? 0.4876 0.3569 0.3500 0.0170  0.0973  0.0317  109 LEU B CD1 
6258 C CD2 . LEU B 124 ? 0.5353 0.3765 0.3555 0.0050  0.0776  0.0281  109 LEU B CD2 
6270 N N   . SER B 125 ? 0.6116 0.4112 0.3679 -0.0062 0.1363  0.0174  110 SER B N   
6271 C CA  . SER B 125 ? 0.6152 0.3878 0.3303 -0.0146 0.1403  0.0136  110 SER B CA  
6272 C C   . SER B 125 ? 0.6206 0.3723 0.3139 -0.0177 0.1199  0.0129  110 SER B C   
6273 O O   . SER B 125 ? 0.6488 0.4088 0.3579 -0.0154 0.1036  0.0162  110 SER B O   
6274 C CB  . SER B 125 ? 0.6314 0.4057 0.3349 -0.0276 0.1455  0.0194  110 SER B CB  
6275 O OG  . SER B 125 ? 0.6187 0.3908 0.3219 -0.0343 0.1250  0.0259  110 SER B OG  
6281 N N   . GLU B 126 ? 0.6443 0.3694 0.3004 -0.0236 0.1208  0.0086  111 GLU B N   
6282 C CA  . GLU B 126 ? 0.6455 0.3530 0.2836 -0.0270 0.1007  0.0089  111 GLU B CA  
6283 C C   . GLU B 126 ? 0.7206 0.4309 0.3613 -0.0329 0.0839  0.0166  111 GLU B C   
6284 O O   . GLU B 126 ? 0.6179 0.3300 0.2678 -0.0296 0.0669  0.0179  111 GLU B O   
6285 C CB  . GLU B 126 ? 0.6850 0.3626 0.2801 -0.0348 0.1029  0.0041  111 GLU B CB  
6286 C CG  . GLU B 126 ? 0.7258 0.3874 0.3051 -0.0391 0.0806  0.0057  111 GLU B CG  
6287 C CD  . GLU B 126 ? 0.8924 0.5233 0.4286 -0.0475 0.0809  0.0005  111 GLU B CD  
6288 O OE1 . GLU B 126 ? 0.8796 0.5007 0.4028 -0.0453 0.0985  -0.0080 111 GLU B OE1 
6289 O OE2 . GLU B 126 ? 0.7766 0.3924 0.2915 -0.0562 0.0628  0.0047  111 GLU B OE2 
6296 N N   . LEU B 127 ? 0.6981 0.4084 0.3311 -0.0416 0.0888  0.0217  112 LEU B N   
6297 C CA  . LEU B 127 ? 0.6443 0.3520 0.2782 -0.0472 0.0719  0.0288  112 LEU B CA  
6298 C C   . LEU B 127 ? 0.6089 0.3384 0.2791 -0.0386 0.0641  0.0297  112 LEU B C   
6299 O O   . LEU B 127 ? 0.5986 0.3251 0.2734 -0.0359 0.0470  0.0307  112 LEU B O   
6300 C CB  . LEU B 127 ? 0.6682 0.3710 0.2871 -0.0600 0.0791  0.0354  112 LEU B CB  
6301 C CG  . LEU B 127 ? 0.7617 0.4366 0.3364 -0.0728 0.0775  0.0383  112 LEU B CG  
6302 C CD1 . LEU B 127 ? 0.9305 0.6023 0.4960 -0.0864 0.0789  0.0479  112 LEU B CD1 
6303 C CD2 . LEU B 127 ? 0.7788 0.4331 0.3367 -0.0728 0.0549  0.0393  112 LEU B CD2 
6315 N N   . GLN B 128 ? 0.5927 0.3446 0.2888 -0.0341 0.0766  0.0291  113 GLN B N   
6316 C CA  . GLN B 128 ? 0.5632 0.3350 0.2902 -0.0272 0.0689  0.0299  113 GLN B CA  
6317 C C   . GLN B 128 ? 0.5736 0.3465 0.3070 -0.0176 0.0591  0.0256  113 GLN B C   
6318 O O   . GLN B 128 ? 0.5351 0.3137 0.2796 -0.0142 0.0463  0.0258  113 GLN B O   
6319 C CB  . GLN B 128 ? 0.5519 0.3481 0.3057 -0.0240 0.0833  0.0310  113 GLN B CB  
6320 C CG  . GLN B 128 ? 0.5818 0.3849 0.3378 -0.0345 0.0922  0.0369  113 GLN B CG  
6321 C CD  . GLN B 128 ? 0.5596 0.3883 0.3427 -0.0305 0.1097  0.0380  113 GLN B CD  
6322 O OE1 . GLN B 128 ? 0.6199 0.4535 0.4117 -0.0200 0.1186  0.0333  113 GLN B OE1 
6323 N NE2 . GLN B 128 ? 0.5611 0.4060 0.3596 -0.0390 0.1139  0.0447  113 GLN B NE2 
6332 N N   . ILE B 129 ? 0.5506 0.3177 0.2765 -0.0137 0.0654  0.0216  114 ILE B N   
6333 C CA  . ILE B 129 ? 0.5420 0.3101 0.2732 -0.0071 0.0561  0.0190  114 ILE B CA  
6334 C C   . ILE B 129 ? 0.5673 0.3224 0.2839 -0.0102 0.0401  0.0198  114 ILE B C   
6335 O O   . ILE B 129 ? 0.5806 0.3446 0.3100 -0.0051 0.0295  0.0194  114 ILE B O   
6336 C CB  . ILE B 129 ? 0.5470 0.3072 0.2711 -0.0041 0.0656  0.0148  114 ILE B CB  
6337 C CG1 . ILE B 129 ? 0.5753 0.3505 0.3204 0.0021  0.0806  0.0145  114 ILE B CG1 
6338 C CG2 . ILE B 129 ? 0.5372 0.2969 0.2645 -0.0006 0.0547  0.0138  114 ILE B CG2 
6339 C CD1 . ILE B 129 ? 0.5979 0.3618 0.3369 0.0069  0.0912  0.0094  114 ILE B CD1 
6351 N N   . SER B 130 ? 0.5693 0.3041 0.2595 -0.0185 0.0382  0.0212  115 SER B N   
6352 C CA  . SER B 130 ? 0.5930 0.3153 0.2717 -0.0212 0.0211  0.0236  115 SER B CA  
6353 C C   . SER B 130 ? 0.5736 0.3047 0.2697 -0.0172 0.0107  0.0255  115 SER B C   
6354 O O   . SER B 130 ? 0.5864 0.3206 0.2912 -0.0117 -0.0019 0.0249  115 SER B O   
6355 C CB  . SER B 130 ? 0.6570 0.3550 0.3024 -0.0324 0.0201  0.0268  115 SER B CB  
6356 O OG  . SER B 130 ? 0.6877 0.3734 0.3117 -0.0362 0.0287  0.0232  115 SER B OG  
6362 N N   . TYR B 131 ? 0.5845 0.3198 0.2863 -0.0201 0.0161  0.0274  116 TYR B N   
6363 C CA  . TYR B 131 ? 0.5947 0.3337 0.3096 -0.0173 0.0059  0.0280  116 TYR B CA  
6364 C C   . TYR B 131 ? 0.5290 0.2889 0.2677 -0.0070 0.0050  0.0233  116 TYR B C   
6365 O O   . TYR B 131 ? 0.5251 0.2863 0.2712 -0.0009 -0.0056 0.0208  116 TYR B O   
6366 C CB  . TYR B 131 ? 0.5637 0.3020 0.2785 -0.0254 0.0115  0.0319  116 TYR B CB  
6367 C CG  . TYR B 131 ? 0.5572 0.2991 0.2859 -0.0235 0.0025  0.0311  116 TYR B CG  
6368 C CD1 . TYR B 131 ? 0.6264 0.3497 0.3474 -0.0234 -0.0127 0.0318  116 TYR B CD1 
6369 C CD2 . TYR B 131 ? 0.5557 0.3174 0.3042 -0.0220 0.0080  0.0298  116 TYR B CD2 
6370 C CE1 . TYR B 131 ? 0.6029 0.3249 0.3335 -0.0215 -0.0207 0.0294  116 TYR B CE1 
6371 C CE2 . TYR B 131 ? 0.6041 0.3659 0.3608 -0.0217 -0.0012 0.0282  116 TYR B CE2 
6372 C CZ  . TYR B 131 ? 0.5675 0.3082 0.3141 -0.0214 -0.0149 0.0272  116 TYR B CZ  
6373 O OH  . TYR B 131 ? 0.6418 0.3785 0.3939 -0.0208 -0.0239 0.0237  116 TYR B OH  
6383 N N   . VAL B 132 ? 0.5361 0.3120 0.2864 -0.0046 0.0162  0.0221  117 VAL B N   
6384 C CA  . VAL B 132 ? 0.5232 0.3181 0.2926 0.0035  0.0150  0.0192  117 VAL B CA  
6385 C C   . VAL B 132 ? 0.5236 0.3194 0.2931 0.0089  0.0077  0.0169  117 VAL B C   
6386 O O   . VAL B 132 ? 0.4955 0.3014 0.2754 0.0149  0.0016  0.0141  117 VAL B O   
6387 C CB  . VAL B 132 ? 0.5476 0.3570 0.3291 0.0048  0.0268  0.0203  117 VAL B CB  
6388 C CG1 . VAL B 132 ? 0.4892 0.3157 0.2858 0.0117  0.0245  0.0190  117 VAL B CG1 
6389 C CG2 . VAL B 132 ? 0.4834 0.2996 0.2732 0.0003  0.0325  0.0233  117 VAL B CG2 
6399 N N   . CYS B 133 ? 0.5202 0.3059 0.2776 0.0061  0.0083  0.0179  118 CYS B N   
6400 C CA  . CYS B 133 ? 0.5497 0.3390 0.3101 0.0094  0.0006  0.0172  118 CYS B CA  
6401 C C   . CYS B 133 ? 0.5633 0.3485 0.3248 0.0125  -0.0124 0.0170  118 CYS B C   
6402 O O   . CYS B 133 ? 0.4912 0.2901 0.2667 0.0189  -0.0176 0.0153  118 CYS B O   
6403 C CB  . CYS B 133 ? 0.6161 0.3920 0.3605 0.0037  0.0019  0.0184  118 CYS B CB  
6404 S SG  . CYS B 133 ? 0.6060 0.3865 0.3540 0.0040  0.0156  0.0173  118 CYS B SG  
6410 N N   . ARG B 134 ? 0.5529 0.3194 0.3005 0.0081  -0.0175 0.0191  119 ARG B N   
6411 C CA  . ARG B 134 ? 0.5280 0.2873 0.2780 0.0124  -0.0311 0.0194  119 ARG B CA  
6412 C C   . ARG B 134 ? 0.5324 0.3050 0.3003 0.0217  -0.0318 0.0138  119 ARG B C   
6413 O O   . ARG B 134 ? 0.5417 0.3238 0.3230 0.0307  -0.0380 0.0108  119 ARG B O   
6414 C CB  . ARG B 134 ? 0.5801 0.3143 0.3102 0.0045  -0.0366 0.0241  119 ARG B CB  
6415 C CG  . ARG B 134 ? 0.5809 0.3026 0.3124 0.0092  -0.0531 0.0258  119 ARG B CG  
6416 C CD  . ARG B 134 ? 0.6389 0.3335 0.3500 0.0003  -0.0594 0.0319  119 ARG B CD  
6417 N NE  . ARG B 134 ? 0.6692 0.3619 0.3836 -0.0011 -0.0548 0.0298  119 ARG B NE  
6418 C CZ  . ARG B 134 ? 0.6525 0.3245 0.3514 -0.0108 -0.0580 0.0355  119 ARG B CZ  
6419 N NH1 . ARG B 134 ? 0.7226 0.3729 0.3995 -0.0198 -0.0654 0.0437  119 ARG B NH1 
6420 N NH2 . ARG B 134 ? 0.7385 0.4112 0.4429 -0.0132 -0.0544 0.0336  119 ARG B NH2 
6434 N N   . GLU B 135 ? 0.5260 0.3003 0.2943 0.0195  -0.0250 0.0122  120 GLU B N   
6435 C CA  . GLU B 135 ? 0.5547 0.3373 0.3341 0.0264  -0.0263 0.0062  120 GLU B CA  
6436 C C   . GLU B 135 ? 0.4874 0.2946 0.2812 0.0337  -0.0215 0.0022  120 GLU B C   
6437 O O   . GLU B 135 ? 0.4875 0.3021 0.2896 0.0424  -0.0244 -0.0039 120 GLU B O   
6438 C CB  . GLU B 135 ? 0.5567 0.3372 0.3332 0.0195  -0.0215 0.0070  120 GLU B CB  
6439 C CG  . GLU B 135 ? 0.5662 0.3239 0.3286 0.0101  -0.0253 0.0121  120 GLU B CG  
6440 C CD  . GLU B 135 ? 0.6244 0.3615 0.3818 0.0137  -0.0389 0.0104  120 GLU B CD  
6441 O OE1 . GLU B 135 ? 0.5676 0.3027 0.3299 0.0184  -0.0433 0.0043  120 GLU B OE1 
6442 O OE2 . GLU B 135 ? 0.6200 0.3414 0.3675 0.0121  -0.0460 0.0151  120 GLU B OE2 
6449 N N   . VAL B 136 ? 0.4974 0.3165 0.2934 0.0303  -0.0135 0.0054  121 VAL B N   
6450 C CA  . VAL B 136 ? 0.5039 0.3452 0.3119 0.0350  -0.0094 0.0038  121 VAL B CA  
6451 C C   . VAL B 136 ? 0.5059 0.3540 0.3217 0.0406  -0.0150 0.0029  121 VAL B C   
6452 O O   . VAL B 136 ? 0.4566 0.3228 0.2839 0.0474  -0.0136 -0.0010 121 VAL B O   
6453 C CB  . VAL B 136 ? 0.4508 0.2988 0.2591 0.0298  -0.0013 0.0086  121 VAL B CB  
6454 C CG1 . VAL B 136 ? 0.4399 0.3081 0.2588 0.0324  0.0010  0.0093  121 VAL B CG1 
6455 C CG2 . VAL B 136 ? 0.4988 0.3484 0.3076 0.0268  0.0042  0.0096  121 VAL B CG2 
6465 N N   . LEU B 137 ? 0.5259 0.3612 0.3358 0.0373  -0.0214 0.0068  122 LEU B N   
6466 C CA  . LEU B 137 ? 0.4986 0.3422 0.3196 0.0420  -0.0290 0.0075  122 LEU B CA  
6467 C C   . LEU B 137 ? 0.4827 0.3275 0.3138 0.0531  -0.0349 0.0019  122 LEU B C   
6468 O O   . LEU B 137 ? 0.5478 0.4122 0.3968 0.0613  -0.0357 -0.0005 122 LEU B O   
6469 C CB  . LEU B 137 ? 0.5250 0.3512 0.3341 0.0347  -0.0374 0.0136  122 LEU B CB  
6470 C CG  . LEU B 137 ? 0.5336 0.3596 0.3348 0.0254  -0.0330 0.0176  122 LEU B CG  
6471 C CD1 . LEU B 137 ? 0.5184 0.3199 0.2985 0.0166  -0.0404 0.0219  122 LEU B CD1 
6472 C CD2 . LEU B 137 ? 0.4866 0.3361 0.3059 0.0269  -0.0340 0.0191  122 LEU B CD2 
6484 N N   . GLN B 138 ? 0.4942 0.3181 0.3149 0.0536  -0.0387 -0.0003 123 GLN B N   
6485 C CA  . GLN B 138 ? 0.5124 0.3317 0.3407 0.0650  -0.0446 -0.0070 123 GLN B CA  
6486 C C   . GLN B 138 ? 0.5047 0.3451 0.3430 0.0731  -0.0354 -0.0159 123 GLN B C   
6487 O O   . GLN B 138 ? 0.5214 0.3747 0.3748 0.0849  -0.0356 -0.0217 123 GLN B O   
6488 C CB  . GLN B 138 ? 0.5264 0.3160 0.3387 0.0611  -0.0506 -0.0069 123 GLN B CB  
6489 C CG  . GLN B 138 ? 0.5419 0.3090 0.3418 0.0536  -0.0609 0.0022  123 GLN B CG  
6490 C CD  . GLN B 138 ? 0.5777 0.3176 0.3587 0.0446  -0.0640 0.0052  123 GLN B CD  
6491 O OE1 . GLN B 138 ? 0.6055 0.3429 0.3841 0.0434  -0.0596 0.0006  123 GLN B OE1 
6492 N NE2 . GLN B 138 ? 0.6530 0.3727 0.4192 0.0365  -0.0722 0.0138  123 GLN B NE2 
6501 N N   . GLY B 139 ? 0.4866 0.3319 0.3168 0.0667  -0.0268 -0.0167 124 GLY B N   
6502 C CA  . GLY B 139 ? 0.4814 0.3462 0.3162 0.0718  -0.0186 -0.0238 124 GLY B CA  
6503 C C   . GLY B 139 ? 0.5462 0.4397 0.3961 0.0750  -0.0127 -0.0221 124 GLY B C   
6504 O O   . GLY B 139 ? 0.5806 0.4913 0.4390 0.0838  -0.0075 -0.0293 124 GLY B O   
6508 N N   . LEU B 140 ? 0.4771 0.3758 0.3297 0.0672  -0.0129 -0.0129 125 LEU B N   
6509 C CA  . LEU B 140 ? 0.5267 0.4519 0.3942 0.0675  -0.0088 -0.0096 125 LEU B CA  
6510 C C   . LEU B 140 ? 0.4590 0.3953 0.3454 0.0778  -0.0136 -0.0122 125 LEU B C   
6511 O O   . LEU B 140 ? 0.5333 0.4959 0.4348 0.0844  -0.0069 -0.0157 125 LEU B O   
6512 C CB  . LEU B 140 ? 0.4511 0.3734 0.3151 0.0560  -0.0101 0.0002  125 LEU B CB  
6513 C CG  . LEU B 140 ? 0.4481 0.3684 0.3014 0.0477  -0.0032 0.0038  125 LEU B CG  
6514 C CD1 . LEU B 140 ? 0.4583 0.3721 0.3083 0.0384  -0.0047 0.0116  125 LEU B CD1 
6515 C CD2 . LEU B 140 ? 0.5215 0.4645 0.3797 0.0490  0.0050  0.0025  125 LEU B CD2 
6527 N N   . ALA B 141 ? 0.4733 0.3908 0.3597 0.0793  -0.0252 -0.0097 126 ALA B N   
6528 C CA  . ALA B 141 ? 0.5157 0.4431 0.4235 0.0904  -0.0322 -0.0110 126 ALA B CA  
6529 C C   . ALA B 141 ? 0.5466 0.4849 0.4646 0.1056  -0.0253 -0.0230 126 ALA B C   
6530 O O   . ALA B 141 ? 0.5125 0.4772 0.4546 0.1156  -0.0220 -0.0255 126 ALA B O   
6531 C CB  . ALA B 141 ? 0.4903 0.3889 0.3912 0.0900  -0.0474 -0.0068 126 ALA B CB  
6537 N N   . TYR B 142 ? 0.5289 0.4478 0.4285 0.1071  -0.0223 -0.0309 127 TYR B N   
6538 C CA  . TYR B 142 ? 0.6091 0.5325 0.5118 0.1207  -0.0156 -0.0444 127 TYR B CA  
6539 C C   . TYR B 142 ? 0.6122 0.5687 0.5196 0.1208  -0.0003 -0.0478 127 TYR B C   
6540 O O   . TYR B 142 ? 0.5229 0.5017 0.4472 0.1333  0.0072  -0.0552 127 TYR B O   
6541 C CB  . TYR B 142 ? 0.5648 0.4563 0.4434 0.1187  -0.0184 -0.0510 127 TYR B CB  
6542 C CG  . TYR B 142 ? 0.7032 0.5964 0.5766 0.1295  -0.0103 -0.0663 127 TYR B CG  
6543 C CD1 . TYR B 142 ? 0.6783 0.5620 0.5613 0.1466  -0.0131 -0.0771 127 TYR B CD1 
6544 C CD2 . TYR B 142 ? 0.7402 0.6430 0.5980 0.1227  -0.0003 -0.0701 127 TYR B CD2 
6545 C CE1 . TYR B 142 ? 0.7491 0.6313 0.6238 0.1570  -0.0045 -0.0933 127 TYR B CE1 
6546 C CE2 . TYR B 142 ? 0.7862 0.6884 0.6340 0.1313  0.0070  -0.0850 127 TYR B CE2 
6547 C CZ  . TYR B 142 ? 0.7797 0.6710 0.6349 0.1486  0.0057  -0.0974 127 TYR B CZ  
6548 O OH  . TYR B 142 ? 0.8304 0.7181 0.6723 0.1575  0.0140  -0.1143 127 TYR B OH  
6558 N N   . LEU B 143 ? 0.6566 0.6172 0.5497 0.1071  0.0049  -0.0420 128 LEU B N   
6559 C CA  . LEU B 143 ? 0.5146 0.5041 0.4085 0.1047  0.0181  -0.0430 128 LEU B CA  
6560 C C   . LEU B 143 ? 0.5415 0.5646 0.4617 0.1073  0.0226  -0.0380 128 LEU B C   
6561 O O   . LEU B 143 ? 0.5523 0.6023 0.4814 0.1139  0.0345  -0.0439 128 LEU B O   
6562 C CB  . LEU B 143 ? 0.4806 0.4667 0.3581 0.0892  0.0195  -0.0342 128 LEU B CB  
6563 C CG  . LEU B 143 ? 0.5201 0.4842 0.3745 0.0857  0.0180  -0.0390 128 LEU B CG  
6564 C CD1 . LEU B 143 ? 0.4810 0.4419 0.3269 0.0720  0.0171  -0.0280 128 LEU B CD1 
6565 C CD2 . LEU B 143 ? 0.5205 0.4939 0.3641 0.0910  0.0267  -0.0504 128 LEU B CD2 
6577 N N   . HIS B 144 ? 0.4559 0.4785 0.3879 0.1011  0.0134  -0.0270 129 HIS B N   
6578 C CA  . HIS B 144 ? 0.4721 0.5271 0.4312 0.1012  0.0150  -0.0205 129 HIS B CA  
6579 C C   . HIS B 144 ? 0.4794 0.5508 0.4642 0.1191  0.0163  -0.0286 129 HIS B C   
6580 O O   . HIS B 144 ? 0.4676 0.5759 0.4759 0.1232  0.0256  -0.0283 129 HIS B O   
6581 C CB  . HIS B 144 ? 0.4692 0.5140 0.4313 0.0897  0.0020  -0.0079 129 HIS B CB  
6582 C CG  . HIS B 144 ? 0.4537 0.4840 0.3939 0.0740  0.0025  -0.0007 129 HIS B CG  
6583 N ND1 . HIS B 144 ? 0.5299 0.5431 0.4636 0.0630  -0.0075 0.0082  129 HIS B ND1 
6584 C CD2 . HIS B 144 ? 0.4392 0.4688 0.3628 0.0682  0.0114  -0.0012 129 HIS B CD2 
6585 C CE1 . HIS B 144 ? 0.4747 0.4774 0.3907 0.0527  -0.0034 0.0119  129 HIS B CE1 
6586 N NE2 . HIS B 144 ? 0.4885 0.5016 0.3996 0.0556  0.0071  0.0072  129 HIS B NE2 
6595 N N   . SER B 145 ? 0.4740 0.5186 0.4561 0.1303  0.0072  -0.0354 130 SER B N   
6596 C CA  . SER B 145 ? 0.4947 0.5512 0.5020 0.1502  0.0081  -0.0443 130 SER B CA  
6597 C C   . SER B 145 ? 0.5386 0.6146 0.5449 0.1608  0.0269  -0.0584 130 SER B C   
6598 O O   . SER B 145 ? 0.5696 0.6748 0.6041 0.1753  0.0351  -0.0640 130 SER B O   
6599 C CB  . SER B 145 ? 0.5059 0.5233 0.5056 0.1591  -0.0063 -0.0486 130 SER B CB  
6600 O OG  . SER B 145 ? 0.5967 0.5858 0.5667 0.1595  -0.0025 -0.0591 130 SER B OG  
6606 N N   . GLN B 146 ? 0.5811 0.6424 0.5555 0.1538  0.0342  -0.0642 131 GLN B N   
6607 C CA  . GLN B 146 ? 0.5603 0.6391 0.5258 0.1598  0.0522  -0.0766 131 GLN B CA  
6608 C C   . GLN B 146 ? 0.5137 0.6329 0.4866 0.1489  0.0653  -0.0681 131 GLN B C   
6609 O O   . GLN B 146 ? 0.5668 0.7005 0.5256 0.1490  0.0807  -0.0757 131 GLN B O   
6610 C CB  . GLN B 146 ? 0.6349 0.6817 0.5617 0.1541  0.0520  -0.0845 131 GLN B CB  
6611 C CG  . GLN B 146 ? 0.7153 0.7188 0.6305 0.1602  0.0381  -0.0908 131 GLN B CG  
6612 C CD  . GLN B 146 ? 0.8289 0.8264 0.7568 0.1823  0.0399  -0.1062 131 GLN B CD  
6613 O OE1 . GLN B 146 ? 0.8449 0.8307 0.7922 0.1916  0.0281  -0.1037 131 GLN B OE1 
6614 N NE2 . GLN B 146 ? 0.8697 0.8729 0.7852 0.1911  0.0543  -0.1223 131 GLN B NE2 
6623 N N   . LYS B 147 ? 0.5455 0.6811 0.5377 0.1383  0.0589  -0.0524 132 LYS B N   
6624 C CA  . LYS B 147 ? 0.5423 0.7129 0.5417 0.1252  0.0689  -0.0418 132 LYS B CA  
6625 C C   . LYS B 147 ? 0.5237 0.6827 0.4885 0.1103  0.0734  -0.0389 132 LYS B C   
6626 O O   . LYS B 147 ? 0.4942 0.6781 0.4533 0.1044  0.0871  -0.0376 132 LYS B O   
6627 C CB  . LYS B 147 ? 0.6193 0.8335 0.6433 0.1364  0.0864  -0.0484 132 LYS B CB  
6628 C CG  . LYS B 147 ? 0.6168 0.8514 0.6839 0.1505  0.0814  -0.0478 132 LYS B CG  
6629 C CD  . LYS B 147 ? 0.7093 0.9565 0.7982 0.1359  0.0682  -0.0288 132 LYS B CD  
6630 C CE  . LYS B 147 ? 0.7377 1.0021 0.8692 0.1490  0.0587  -0.0266 132 LYS B CE  
6631 N NZ  . LYS B 147 ? 0.7421 0.9655 0.8669 0.1614  0.0426  -0.0330 132 LYS B NZ  
6645 N N   . LYS B 148 ? 0.5214 0.6433 0.4641 0.1039  0.0615  -0.0368 133 LYS B N   
6646 C CA  . LYS B 148 ? 0.6012 0.7102 0.5154 0.0905  0.0624  -0.0323 133 LYS B CA  
6647 C C   . LYS B 148 ? 0.5023 0.5976 0.4159 0.0766  0.0514  -0.0176 133 LYS B C   
6648 O O   . LYS B 148 ? 0.6180 0.7012 0.5430 0.0775  0.0407  -0.0140 133 LYS B O   
6649 C CB  . LYS B 148 ? 0.5804 0.6587 0.4688 0.0952  0.0595  -0.0437 133 LYS B CB  
6650 C CG  . LYS B 148 ? 0.6601 0.7483 0.5310 0.0997  0.0723  -0.0555 133 LYS B CG  
6651 C CD  . LYS B 148 ? 0.6316 0.6870 0.4787 0.1047  0.0669  -0.0682 133 LYS B CD  
6652 C CE  . LYS B 148 ? 0.7876 0.8477 0.6305 0.1203  0.0777  -0.0870 133 LYS B CE  
6653 N NZ  . LYS B 148 ? 0.8103 0.8366 0.6246 0.1225  0.0723  -0.0999 133 LYS B NZ  
6667 N N   . ILE B 149 ? 0.5486 0.6438 0.4466 0.0637  0.0537  -0.0094 134 ILE B N   
6668 C CA  . ILE B 149 ? 0.5324 0.6119 0.4268 0.0514  0.0450  0.0031  134 ILE B CA  
6669 C C   . ILE B 149 ? 0.5448 0.6031 0.4157 0.0468  0.0431  0.0033  134 ILE B C   
6670 O O   . ILE B 149 ? 0.5569 0.6242 0.4145 0.0447  0.0495  0.0018  134 ILE B O   
6671 C CB  . ILE B 149 ? 0.5119 0.6137 0.4164 0.0394  0.0482  0.0160  134 ILE B CB  
6672 C CG1 . ILE B 149 ? 0.5874 0.7171 0.5194 0.0435  0.0506  0.0162  134 ILE B CG1 
6673 C CG2 . ILE B 149 ? 0.5803 0.6603 0.4803 0.0282  0.0387  0.0270  134 ILE B CG2 
6674 C CD1 . ILE B 149 ? 0.4913 0.6427 0.4360 0.0293  0.0516  0.0303  134 ILE B CD1 
6686 N N   . HIS B 150 ? 0.4724 0.5039 0.3383 0.0449  0.0342  0.0055  135 HIS B N   
6687 C CA  . HIS B 150 ? 0.5562 0.5707 0.4055 0.0410  0.0318  0.0066  135 HIS B CA  
6688 C C   . HIS B 150 ? 0.4283 0.4491 0.2737 0.0304  0.0332  0.0187  135 HIS B C   
6689 O O   . HIS B 150 ? 0.4707 0.4938 0.3037 0.0273  0.0345  0.0202  135 HIS B O   
6690 C CB  . HIS B 150 ? 0.5066 0.4943 0.3541 0.0416  0.0241  0.0062  135 HIS B CB  
6691 C CG  . HIS B 150 ? 0.5012 0.4750 0.3370 0.0387  0.0217  0.0070  135 HIS B CG  
6692 N ND1 . HIS B 150 ? 0.4802 0.4530 0.3141 0.0315  0.0215  0.0166  135 HIS B ND1 
6693 C CD2 . HIS B 150 ? 0.4964 0.4572 0.3240 0.0416  0.0185  0.0000  135 HIS B CD2 
6694 C CE1 . HIS B 150 ? 0.4839 0.4471 0.3116 0.0307  0.0185  0.0159  135 HIS B CE1 
6695 N NE2 . HIS B 150 ? 0.5521 0.5080 0.3751 0.0357  0.0165  0.0060  135 HIS B NE2 
6703 N N   . ARG B 151 ? 0.5044 0.5253 0.3589 0.0242  0.0313  0.0278  136 ARG B N   
6704 C CA  . ARG B 151 ? 0.5051 0.5301 0.3585 0.0139  0.0316  0.0403  136 ARG B CA  
6705 C C   . ARG B 151 ? 0.5092 0.5126 0.3553 0.0111  0.0268  0.0459  136 ARG B C   
6706 O O   . ARG B 151 ? 0.5553 0.5554 0.4016 0.0038  0.0252  0.0567  136 ARG B O   
6707 C CB  . ARG B 151 ? 0.4835 0.5325 0.3312 0.0097  0.0384  0.0437  136 ARG B CB  
6708 C CG  . ARG B 151 ? 0.5495 0.6253 0.4078 0.0124  0.0460  0.0391  136 ARG B CG  
6709 C CD  . ARG B 151 ? 0.6417 0.7411 0.4896 0.0083  0.0554  0.0408  136 ARG B CD  
6710 N NE  . ARG B 151 ? 0.6717 0.7924 0.5245 0.0178  0.0652  0.0285  136 ARG B NE  
6711 C CZ  . ARG B 151 ? 0.6277 0.7768 0.4982 0.0176  0.0731  0.0296  136 ARG B CZ  
6712 N NH1 . ARG B 151 ? 0.7371 0.8972 0.6204 0.0061  0.0714  0.0433  136 ARG B NH1 
6713 N NH2 . ARG B 151 ? 0.7267 0.8937 0.6034 0.0294  0.0827  0.0166  136 ARG B NH2 
6727 N N   . ASP B 152 ? 0.4544 0.4436 0.2959 0.0166  0.0244  0.0398  137 ASP B N   
6728 C CA  . ASP B 152 ? 0.4371 0.4119 0.2763 0.0149  0.0211  0.0455  137 ASP B CA  
6729 C C   . ASP B 152 ? 0.4175 0.3739 0.2581 0.0197  0.0193  0.0396  137 ASP B C   
6730 O O   . ASP B 152 ? 0.4177 0.3691 0.2569 0.0211  0.0176  0.0389  137 ASP B O   
6731 C CB  . ASP B 152 ? 0.4381 0.4220 0.2690 0.0134  0.0200  0.0477  137 ASP B CB  
6732 C CG  . ASP B 152 ? 0.5545 0.5313 0.3878 0.0098  0.0157  0.0591  137 ASP B CG  
6733 O OD1 . ASP B 152 ? 0.6061 0.5710 0.4468 0.0090  0.0153  0.0648  137 ASP B OD1 
6734 O OD2 . ASP B 152 ? 0.5513 0.5336 0.3788 0.0080  0.0121  0.0623  137 ASP B OD2 
6739 N N   . ILE B 153 ? 0.4155 0.3622 0.2585 0.0207  0.0191  0.0365  138 ILE B N   
6740 C CA  . ILE B 153 ? 0.4154 0.3439 0.2565 0.0234  0.0181  0.0319  138 ILE B CA  
6741 C C   . ILE B 153 ? 0.5433 0.4581 0.3857 0.0217  0.0198  0.0374  138 ILE B C   
6742 O O   . ILE B 153 ? 0.4443 0.3529 0.2873 0.0186  0.0202  0.0424  138 ILE B O   
6743 C CB  . ILE B 153 ? 0.4248 0.3464 0.2651 0.0241  0.0160  0.0277  138 ILE B CB  
6744 C CG1 . ILE B 153 ? 0.4159 0.3506 0.2588 0.0290  0.0147  0.0212  138 ILE B CG1 
6745 C CG2 . ILE B 153 ? 0.4559 0.3563 0.2898 0.0245  0.0154  0.0249  138 ILE B CG2 
6746 C CD1 . ILE B 153 ? 0.5194 0.4473 0.3572 0.0337  0.0133  0.0141  138 ILE B CD1 
6758 N N   . LYS B 154 ? 0.5007 0.4106 0.3446 0.0239  0.0208  0.0364  139 LYS B N   
6759 C CA  . LYS B 154 ? 0.4437 0.3440 0.2930 0.0247  0.0242  0.0406  139 LYS B CA  
6760 C C   . LYS B 154 ? 0.4179 0.3199 0.2716 0.0263  0.0249  0.0388  139 LYS B C   
6761 O O   . LYS B 154 ? 0.4468 0.3564 0.2979 0.0256  0.0211  0.0354  139 LYS B O   
6762 C CB  . LYS B 154 ? 0.4404 0.3466 0.2968 0.0241  0.0230  0.0497  139 LYS B CB  
6763 C CG  . LYS B 154 ? 0.5675 0.4901 0.4282 0.0237  0.0187  0.0537  139 LYS B CG  
6764 C CD  . LYS B 154 ? 0.5160 0.4481 0.3751 0.0200  0.0152  0.0619  139 LYS B CD  
6765 C CE  . LYS B 154 ? 0.5606 0.4824 0.4271 0.0205  0.0151  0.0708  139 LYS B CE  
6766 N NZ  . LYS B 154 ? 0.6821 0.6130 0.5462 0.0153  0.0100  0.0814  139 LYS B NZ  
6780 N N   . GLY B 155 ? 0.4458 0.3406 0.3066 0.0281  0.0302  0.0408  140 GLY B N   
6781 C CA  . GLY B 155 ? 0.4734 0.3721 0.3414 0.0281  0.0320  0.0402  140 GLY B CA  
6782 C C   . GLY B 155 ? 0.5051 0.4205 0.3812 0.0265  0.0250  0.0439  140 GLY B C   
6783 O O   . GLY B 155 ? 0.4160 0.3344 0.2922 0.0236  0.0223  0.0415  140 GLY B O   
6787 N N   . ALA B 156 ? 0.4640 0.3887 0.3448 0.0271  0.0208  0.0503  141 ALA B N   
6788 C CA  . ALA B 156 ? 0.4166 0.3561 0.3016 0.0243  0.0126  0.0547  141 ALA B CA  
6789 C C   . ALA B 156 ? 0.4422 0.3841 0.3108 0.0208  0.0077  0.0475  141 ALA B C   
6790 O O   . ALA B 156 ? 0.4289 0.3785 0.2960 0.0171  0.0007  0.0480  141 ALA B O   
6791 C CB  . ALA B 156 ? 0.4189 0.3650 0.3092 0.0249  0.0088  0.0647  141 ALA B CB  
6797 N N   . ASN B 157 ? 0.4391 0.3739 0.2957 0.0221  0.0106  0.0405  142 ASN B N   
6798 C CA  . ASN B 157 ? 0.4274 0.3641 0.2705 0.0215  0.0075  0.0324  142 ASN B CA  
6799 C C   . ASN B 157 ? 0.5032 0.4269 0.3412 0.0230  0.0081  0.0238  142 ASN B C   
6800 O O   . ASN B 157 ? 0.5075 0.4296 0.3361 0.0250  0.0063  0.0159  142 ASN B O   
6801 C CB  . ASN B 157 ? 0.4219 0.3659 0.2588 0.0224  0.0097  0.0323  142 ASN B CB  
6802 C CG  . ASN B 157 ? 0.4978 0.4529 0.3361 0.0192  0.0078  0.0422  142 ASN B CG  
6803 O OD1 . ASN B 157 ? 0.4944 0.4549 0.3334 0.0164  0.0024  0.0466  142 ASN B OD1 
6804 N ND2 . ASN B 157 ? 0.4242 0.3822 0.2630 0.0183  0.0108  0.0470  142 ASN B ND2 
6811 N N   . ILE B 158 ? 0.4403 0.3544 0.2841 0.0222  0.0108  0.0253  143 ILE B N   
6812 C CA  . ILE B 158 ? 0.4886 0.3887 0.3260 0.0214  0.0098  0.0196  143 ILE B CA  
6813 C C   . ILE B 158 ? 0.4658 0.3665 0.3075 0.0162  0.0062  0.0211  143 ILE B C   
6814 O O   . ILE B 158 ? 0.4499 0.3559 0.3040 0.0139  0.0097  0.0276  143 ILE B O   
6815 C CB  . ILE B 158 ? 0.4752 0.3632 0.3115 0.0218  0.0155  0.0207  143 ILE B CB  
6816 C CG1 . ILE B 158 ? 0.4573 0.3453 0.2903 0.0249  0.0167  0.0201  143 ILE B CG1 
6817 C CG2 . ILE B 158 ? 0.4995 0.3721 0.3269 0.0195  0.0129  0.0167  143 ILE B CG2 
6818 C CD1 . ILE B 158 ? 0.5144 0.3888 0.3429 0.0238  0.0210  0.0212  143 ILE B CD1 
6830 N N   . LEU B 159 ? 0.4798 0.3754 0.3124 0.0144  -0.0008 0.0150  144 LEU B N   
6831 C CA  . LEU B 159 ? 0.4820 0.3780 0.3171 0.0073  -0.0070 0.0164  144 LEU B CA  
6832 C C   . LEU B 159 ? 0.5225 0.4023 0.3546 0.0027  -0.0079 0.0152  144 LEU B C   
6833 O O   . LEU B 159 ? 0.4639 0.3283 0.2858 0.0059  -0.0077 0.0104  144 LEU B O   
6834 C CB  . LEU B 159 ? 0.4901 0.3863 0.3129 0.0065  -0.0152 0.0098  144 LEU B CB  
6835 C CG  . LEU B 159 ? 0.5147 0.4254 0.3343 0.0101  -0.0139 0.0104  144 LEU B CG  
6836 C CD1 . LEU B 159 ? 0.5873 0.4975 0.3907 0.0074  -0.0214 0.0035  144 LEU B CD1 
6837 C CD2 . LEU B 159 ? 0.5501 0.4764 0.3859 0.0084  -0.0118 0.0224  144 LEU B CD2 
6849 N N   . ILE B 160 ? 0.4621 0.3463 0.3040 -0.0057 -0.0099 0.0210  145 ILE B N   
6850 C CA  . ILE B 160 ? 0.4724 0.3441 0.3130 -0.0132 -0.0100 0.0228  145 ILE B CA  
6851 C C   . ILE B 160 ? 0.5381 0.4082 0.3789 -0.0232 -0.0209 0.0231  145 ILE B C   
6852 O O   . ILE B 160 ? 0.5523 0.4402 0.4059 -0.0272 -0.0244 0.0280  145 ILE B O   
6853 C CB  . ILE B 160 ? 0.5119 0.3941 0.3677 -0.0154 0.0015  0.0312  145 ILE B CB  
6854 C CG1 . ILE B 160 ? 0.4542 0.3368 0.3087 -0.0062 0.0115  0.0306  145 ILE B CG1 
6855 C CG2 . ILE B 160 ? 0.5531 0.4218 0.4034 -0.0246 0.0029  0.0337  145 ILE B CG2 
6856 C CD1 . ILE B 160 ? 0.5127 0.3744 0.3482 -0.0039 0.0122  0.0256  145 ILE B CD1 
6868 N N   . ASN B 161 ? 0.5458 0.3931 0.3724 -0.0280 -0.0279 0.0186  146 ASN B N   
6869 C CA  . ASN B 161 ? 0.5238 0.3644 0.3483 -0.0399 -0.0396 0.0189  146 ASN B CA  
6870 C C   . ASN B 161 ? 0.5876 0.4291 0.4228 -0.0525 -0.0372 0.0288  146 ASN B C   
6871 O O   . ASN B 161 ? 0.6058 0.4496 0.4453 -0.0513 -0.0259 0.0336  146 ASN B O   
6872 C CB  . ASN B 161 ? 0.5472 0.3590 0.3488 -0.0378 -0.0500 0.0072  146 ASN B CB  
6873 C CG  . ASN B 161 ? 0.5594 0.3458 0.3506 -0.0369 -0.0500 0.0061  146 ASN B CG  
6874 O OD1 . ASN B 161 ? 0.6150 0.4029 0.4123 -0.0422 -0.0436 0.0148  146 ASN B OD1 
6875 N ND2 . ASN B 161 ? 0.6416 0.4037 0.4161 -0.0301 -0.0575 -0.0046 146 ASN B ND2 
6882 N N   . ASP B 162 ? 0.5602 0.4005 0.3987 -0.0661 -0.0478 0.0319  147 ASP B N   
6883 C CA  . ASP B 162 ? 0.6094 0.4564 0.4618 -0.0804 -0.0451 0.0430  147 ASP B CA  
6884 C C   . ASP B 162 ? 0.6434 0.4638 0.4796 -0.0843 -0.0431 0.0434  147 ASP B C   
6885 O O   . ASP B 162 ? 0.6709 0.4982 0.5162 -0.0950 -0.0359 0.0533  147 ASP B O   
6886 C CB  . ASP B 162 ? 0.6632 0.5137 0.5224 -0.0962 -0.0595 0.0468  147 ASP B CB  
6887 C CG  . ASP B 162 ? 0.7155 0.5960 0.5941 -0.0949 -0.0624 0.0503  147 ASP B CG  
6888 O OD1 . ASP B 162 ? 0.7426 0.6471 0.6389 -0.0849 -0.0501 0.0546  147 ASP B OD1 
6889 O OD2 . ASP B 162 ? 1.0045 0.8825 0.8790 -0.1042 -0.0780 0.0488  147 ASP B OD2 
6894 N N   . ALA B 163 ? 0.6194 0.4110 0.4325 -0.0760 -0.0489 0.0337  148 ALA B N   
6895 C CA  . ALA B 163 ? 0.5977 0.3632 0.3951 -0.0780 -0.0486 0.0352  148 ALA B CA  
6896 C C   . ALA B 163 ? 0.6184 0.3913 0.4154 -0.0688 -0.0343 0.0372  148 ALA B C   
6897 O O   . ALA B 163 ? 0.5925 0.3445 0.3744 -0.0704 -0.0343 0.0394  148 ALA B O   
6898 C CB  . ALA B 163 ? 0.6163 0.3477 0.3923 -0.0712 -0.0620 0.0243  148 ALA B CB  
6904 N N   . GLY B 164 ? 0.5524 0.3518 0.3636 -0.0598 -0.0236 0.0367  149 GLY B N   
6905 C CA  . GLY B 164 ? 0.5403 0.3437 0.3489 -0.0513 -0.0112 0.0371  149 GLY B CA  
6906 C C   . GLY B 164 ? 0.5743 0.3631 0.3690 -0.0382 -0.0151 0.0287  149 GLY B C   
6907 O O   . GLY B 164 ? 0.5346 0.3203 0.3226 -0.0337 -0.0081 0.0295  149 GLY B O   
6911 N N   . GLU B 165 ? 0.5419 0.3225 0.3320 -0.0321 -0.0259 0.0205  150 GLU B N   
6912 C CA  . GLU B 165 ? 0.5575 0.3290 0.3392 -0.0189 -0.0289 0.0125  150 GLU B CA  
6913 C C   . GLU B 165 ? 0.5164 0.3117 0.3083 -0.0092 -0.0217 0.0095  150 GLU B C   
6914 O O   . GLU B 165 ? 0.5120 0.3270 0.3155 -0.0117 -0.0182 0.0121  150 GLU B O   
6915 C CB  . GLU B 165 ? 0.6161 0.3670 0.3882 -0.0157 -0.0419 0.0038  150 GLU B CB  
6916 C CG  . GLU B 165 ? 0.6597 0.3807 0.4198 -0.0247 -0.0515 0.0071  150 GLU B CG  
6917 C CD  . GLU B 165 ? 0.7510 0.4485 0.5018 -0.0223 -0.0647 -0.0023 150 GLU B CD  
6918 O OE1 . GLU B 165 ? 0.7146 0.4185 0.4670 -0.0259 -0.0676 -0.0067 150 GLU B OE1 
6919 O OE2 . GLU B 165 ? 0.8928 0.5639 0.6339 -0.0167 -0.0730 -0.0054 150 GLU B OE2 
6926 N N   . VAL B 166 ? 0.5271 0.4489 0.5183 -0.0573 0.0787  0.0254  151 VAL B N   
6927 C CA  . VAL B 166 ? 0.5342 0.4533 0.5149 -0.0605 0.0740  0.0303  151 VAL B CA  
6928 C C   . VAL B 166 ? 0.5345 0.4617 0.5251 -0.0630 0.0813  0.0309  151 VAL B C   
6929 O O   . VAL B 166 ? 0.5308 0.4630 0.5393 -0.0639 0.0874  0.0346  151 VAL B O   
6930 C CB  . VAL B 166 ? 0.5375 0.4494 0.5155 -0.0638 0.0654  0.0400  151 VAL B CB  
6931 C CG1 . VAL B 166 ? 0.5455 0.4535 0.5097 -0.0669 0.0613  0.0441  151 VAL B CG1 
6932 C CG2 . VAL B 166 ? 0.5698 0.4711 0.5388 -0.0623 0.0596  0.0394  151 VAL B CG2 
6942 N N   . ARG B 167 ? 0.5389 0.4673 0.5187 -0.0643 0.0811  0.0284  152 ARG B N   
6943 C CA  . ARG B 167 ? 0.5397 0.4739 0.5270 -0.0670 0.0881  0.0277  152 ARG B CA  
6944 C C   . ARG B 167 ? 0.5439 0.4767 0.5215 -0.0686 0.0822  0.0313  152 ARG B C   
6945 O O   . ARG B 167 ? 0.5468 0.4765 0.5088 -0.0676 0.0763  0.0307  152 ARG B O   
6946 C CB  . ARG B 167 ? 0.5399 0.4797 0.5251 -0.0683 0.0972  0.0179  152 ARG B CB  
6947 C CG  . ARG B 167 ? 0.5364 0.4776 0.5292 -0.0670 0.1050  0.0128  152 ARG B CG  
6948 C CD  . ARG B 167 ? 0.5439 0.4866 0.5563 -0.0683 0.1163  0.0154  152 ARG B CD  
6949 N NE  . ARG B 167 ? 0.5318 0.4762 0.5510 -0.0671 0.1264  0.0094  152 ARG B NE  
6950 C CZ  . ARG B 167 ? 0.5334 0.4776 0.5626 -0.0629 0.1254  0.0119  152 ARG B CZ  
6951 N NH1 . ARG B 167 ? 0.5222 0.4645 0.5553 -0.0608 0.1147  0.0207  152 ARG B NH1 
6952 N NH2 . ARG B 167 ? 0.5629 0.5089 0.5974 -0.0615 0.1359  0.0052  152 ARG B NH2 
6966 N N   . LEU B 168 ? 0.5442 0.4789 0.5314 -0.0707 0.0849  0.0358  153 LEU B N   
6967 C CA  . LEU B 168 ? 0.5469 0.4816 0.5268 -0.0719 0.0810  0.0375  153 LEU B CA  
6968 C C   . LEU B 168 ? 0.5792 0.5189 0.5638 -0.0740 0.0895  0.0313  153 LEU B C   
6969 O O   . LEU B 168 ? 0.5877 0.5285 0.5852 -0.0756 0.0994  0.0299  153 LEU B O   
6970 C CB  . LEU B 168 ? 0.5480 0.4800 0.5337 -0.0733 0.0765  0.0483  153 LEU B CB  
6971 C CG  . LEU B 168 ? 0.5859 0.5126 0.5657 -0.0745 0.0680  0.0561  153 LEU B CG  
6972 C CD1 . LEU B 168 ? 0.5516 0.4789 0.5383 -0.0778 0.0647  0.0679  153 LEU B CD1 
6973 C CD2 . LEU B 168 ? 0.5553 0.4755 0.5136 -0.0739 0.0617  0.0533  153 LEU B CD2 
6985 N N   . ALA B 169 ? 0.5552 0.4975 0.5292 -0.0746 0.0867  0.0281  154 ALA B N   
6986 C CA  . ALA B 169 ? 0.6800 0.6270 0.6567 -0.0781 0.0937  0.0223  154 ALA B CA  
6987 C C   . ALA B 169 ? 0.6911 0.6353 0.6744 -0.0783 0.0925  0.0274  154 ALA B C   
6988 O O   . ALA B 169 ? 0.7344 0.6767 0.7111 -0.0759 0.0837  0.0322  154 ALA B O   
6989 C CB  . ALA B 169 ? 0.7931 0.7476 0.7564 -0.0792 0.0915  0.0167  154 ALA B CB  
6995 N N   . ASP B 170 ? 0.7488 0.6913 0.7443 -0.0813 0.1022  0.0266  155 ASP B N   
6996 C CA  . ASP B 170 ? 0.7896 0.7285 0.7921 -0.0815 0.1024  0.0312  155 ASP B CA  
6997 C C   . ASP B 170 ? 0.7258 0.6684 0.7215 -0.0847 0.1037  0.0230  155 ASP B C   
6998 O O   . ASP B 170 ? 0.7634 0.7067 0.7612 -0.0904 0.1140  0.0162  155 ASP B O   
6999 C CB  . ASP B 170 ? 0.7484 0.6818 0.7688 -0.0830 0.1140  0.0368  155 ASP B CB  
7000 C CG  . ASP B 170 ? 0.7790 0.7073 0.8078 -0.0826 0.1146  0.0437  155 ASP B CG  
7001 O OD1 . ASP B 170 ? 0.8643 0.7917 0.8965 -0.0795 0.1068  0.0547  155 ASP B OD1 
7002 O OD2 . ASP B 170 ? 0.8552 0.7800 0.8864 -0.0862 0.1229  0.0384  155 ASP B OD2 
7007 N N   . PHE B 171 ? 0.6951 0.6402 0.6824 -0.0819 0.0941  0.0238  156 PHE B N   
7008 C CA  . PHE B 171 ? 0.7946 0.7462 0.7758 -0.0844 0.0939  0.0166  156 PHE B CA  
7009 C C   . PHE B 171 ? 0.7704 0.7175 0.7577 -0.0839 0.0931  0.0182  156 PHE B C   
7010 O O   . PHE B 171 ? 0.8371 0.7901 0.8199 -0.0850 0.0910  0.0131  156 PHE B O   
7011 C CB  . PHE B 171 ? 0.7110 0.6705 0.6784 -0.0811 0.0852  0.0159  156 PHE B CB  
7012 C CG  . PHE B 171 ? 0.8652 0.8320 0.8255 -0.0831 0.0874  0.0123  156 PHE B CG  
7013 C CD1 . PHE B 171 ? 0.8352 0.8055 0.7985 -0.0896 0.0964  0.0066  156 PHE B CD1 
7014 C CD2 . PHE B 171 ? 0.8344 0.8037 0.7839 -0.0788 0.0814  0.0153  156 PHE B CD2 
7015 C CE1 . PHE B 171 ? 0.8266 0.8044 0.7824 -0.0916 0.0977  0.0042  156 PHE B CE1 
7016 C CE2 . PHE B 171 ? 0.7437 0.7193 0.6871 -0.0800 0.0833  0.0136  156 PHE B CE2 
7017 C CZ  . PHE B 171 ? 0.8028 0.7835 0.7495 -0.0862 0.0907  0.0082  156 PHE B CZ  
7027 N N   . GLY B 172 ? 0.6381 0.5759 0.6364 -0.0823 0.0951  0.0261  157 GLY B N   
7028 C CA  . GLY B 172 ? 0.6151 0.5477 0.6185 -0.0805 0.0928  0.0295  157 GLY B CA  
7029 C C   . GLY B 172 ? 0.7104 0.6433 0.7151 -0.0853 0.0988  0.0207  157 GLY B C   
7030 O O   . GLY B 172 ? 0.6629 0.5955 0.6667 -0.0831 0.0936  0.0198  157 GLY B O   
7034 N N   . ILE B 173 ? 0.6819 0.6153 0.6880 -0.0927 0.1101  0.0139  158 ILE B N   
7035 C CA  . ILE B 173 ? 0.7510 0.6839 0.7572 -0.1002 0.1172  0.0057  158 ILE B CA  
7036 C C   . ILE B 173 ? 0.7697 0.7170 0.7655 -0.1005 0.1083  -0.0009 158 ILE B C   
7037 O O   . ILE B 173 ? 0.7458 0.6935 0.7427 -0.1010 0.1060  -0.0039 158 ILE B O   
7038 C CB  . ILE B 173 ? 0.8413 0.7714 0.8482 -0.1103 0.1325  0.0001  158 ILE B CB  
7039 C CG1 . ILE B 173 ? 0.9437 0.8588 0.9638 -0.1096 0.1442  0.0077  158 ILE B CG1 
7040 C CG2 . ILE B 173 ? 0.8935 0.8247 0.8965 -0.1212 0.1395  -0.0092 158 ILE B CG2 
7041 C CD1 . ILE B 173 ? 0.9663 0.8731 0.9880 -0.1205 0.1636  0.0022  158 ILE B CD1 
7053 N N   . SER B 174 ? 0.7702 0.7296 0.7567 -0.0997 0.1039  -0.0023 159 SER B N   
7054 C CA  . SER B 174 ? 0.7835 0.7589 0.7616 -0.1006 0.0983  -0.0066 159 SER B CA  
7055 C C   . SER B 174 ? 0.7414 0.7181 0.7190 -0.0925 0.0885  -0.0043 159 SER B C   
7056 O O   . SER B 174 ? 0.6342 0.6227 0.6095 -0.0938 0.0860  -0.0083 159 SER B O   
7057 C CB  . SER B 174 ? 0.7553 0.7412 0.7245 -0.0994 0.0957  -0.0053 159 SER B CB  
7058 O OG  . SER B 174 ? 0.9427 0.9459 0.9056 -0.1007 0.0923  -0.0071 159 SER B OG  
7064 N N   . ALA B 175 ? 0.6211 0.5869 0.6006 -0.0848 0.0832  0.0026  160 ALA B N   
7065 C CA  . ALA B 175 ? 0.6319 0.5988 0.6075 -0.0773 0.0740  0.0050  160 ALA B CA  
7066 C C   . ALA B 175 ? 0.6126 0.5757 0.5949 -0.0772 0.0735  0.0020  160 ALA B C   
7067 O O   . ALA B 175 ? 0.5135 0.4791 0.4923 -0.0711 0.0662  0.0023  160 ALA B O   
7068 C CB  . ALA B 175 ? 0.6191 0.5761 0.5921 -0.0713 0.0684  0.0142  160 ALA B CB  
7074 N N   . GLN B 176 ? 0.5155 0.4715 0.5068 -0.0841 0.0819  -0.0012 161 GLN B N   
7075 C CA  . GLN B 176 ? 0.5385 0.4880 0.5365 -0.0843 0.0821  -0.0038 161 GLN B CA  
7076 C C   . GLN B 176 ? 0.5103 0.4672 0.5093 -0.0942 0.0883  -0.0135 161 GLN B C   
7077 O O   . GLN B 176 ? 0.5128 0.4612 0.5182 -0.0971 0.0913  -0.0166 161 GLN B O   
7078 C CB  . GLN B 176 ? 0.6400 0.5703 0.6484 -0.0837 0.0875  0.0034  161 GLN B CB  
7079 C CG  . GLN B 176 ? 0.6688 0.5939 0.6768 -0.0749 0.0794  0.0148  161 GLN B CG  
7080 C CD  . GLN B 176 ? 0.8051 0.7141 0.8256 -0.0738 0.0844  0.0247  161 GLN B CD  
7081 O OE1 . GLN B 176 ? 0.9221 0.8218 0.9517 -0.0798 0.0971  0.0249  161 GLN B OE1 
7082 N NE2 . GLN B 176 ? 0.7600 0.6653 0.7804 -0.0668 0.0755  0.0342  161 GLN B NE2 
7091 N N   . ILE B 177 ? 0.5101 0.4831 0.5025 -0.1000 0.0900  -0.0176 162 ILE B N   
7092 C CA  . ILE B 177 ? 0.5566 0.5411 0.5485 -0.1115 0.0951  -0.0255 162 ILE B CA  
7093 C C   . ILE B 177 ? 0.5012 0.5100 0.4861 -0.1109 0.0900  -0.0258 162 ILE B C   
7094 O O   . ILE B 177 ? 0.4999 0.5130 0.4796 -0.1027 0.0850  -0.0204 162 ILE B O   
7095 C CB  . ILE B 177 ? 0.5472 0.5244 0.5389 -0.1252 0.1086  -0.0288 162 ILE B CB  
7096 C CG1 . ILE B 177 ? 0.5270 0.5104 0.5123 -0.1257 0.1106  -0.0259 162 ILE B CG1 
7097 C CG2 . ILE B 177 ? 0.5786 0.5308 0.5786 -0.1253 0.1167  -0.0265 162 ILE B CG2 
7098 C CD1 . ILE B 177 ? 0.6223 0.6002 0.6053 -0.1393 0.1245  -0.0297 162 ILE B CD1 
7110 N N   . GLY B 178 ? 0.5053 0.5299 0.4905 -0.1206 0.0922  -0.0310 163 GLY B N   
7111 C CA  . GLY B 178 ? 0.5050 0.5551 0.4854 -0.1228 0.0901  -0.0292 163 GLY B CA  
7112 C C   . GLY B 178 ? 0.4959 0.5553 0.4754 -0.1087 0.0815  -0.0244 163 GLY B C   
7113 O O   . GLY B 178 ? 0.4731 0.5253 0.4560 -0.0998 0.0761  -0.0253 163 GLY B O   
7117 N N   . ALA B 179 ? 0.4789 0.5535 0.4528 -0.1067 0.0811  -0.0187 164 ALA B N   
7118 C CA  . ALA B 179 ? 0.4879 0.5724 0.4598 -0.0950 0.0763  -0.0135 164 ALA B CA  
7119 C C   . ALA B 179 ? 0.5155 0.5790 0.4834 -0.0827 0.0715  -0.0111 164 ALA B C   
7120 O O   . ALA B 179 ? 0.4655 0.5295 0.4327 -0.0736 0.0674  -0.0104 164 ALA B O   
7121 C CB  . ALA B 179 ? 0.5653 0.6670 0.5320 -0.0960 0.0791  -0.0061 164 ALA B CB  
7127 N N   . GLU B 180 ? 0.5047 0.5505 0.4695 -0.0829 0.0723  -0.0095 165 GLU B N   
7128 C CA  . GLU B 180 ? 0.5508 0.5787 0.5113 -0.0735 0.0676  -0.0055 165 GLU B CA  
7129 C C   . GLU B 180 ? 0.5437 0.5623 0.5089 -0.0691 0.0632  -0.0082 165 GLU B C   
7130 O O   . GLU B 180 ? 0.4793 0.4939 0.4392 -0.0606 0.0582  -0.0054 165 GLU B O   
7131 C CB  . GLU B 180 ? 0.5477 0.5607 0.5076 -0.0761 0.0698  -0.0031 165 GLU B CB  
7132 C CG  . GLU B 180 ? 0.6045 0.6072 0.5560 -0.0691 0.0661  0.0038  165 GLU B CG  
7133 C CD  . GLU B 180 ? 0.6947 0.6895 0.6459 -0.0723 0.0691  0.0063  165 GLU B CD  
7134 O OE1 . GLU B 180 ? 0.6607 0.6630 0.6139 -0.0789 0.0744  0.0033  165 GLU B OE1 
7135 O OE2 . GLU B 180 ? 0.7801 0.7621 0.7288 -0.0689 0.0661  0.0115  165 GLU B OE2 
7142 N N   . LEU B 181 ? 0.4818 0.4959 0.4560 -0.0754 0.0657  -0.0133 166 LEU B N   
7143 C CA  . LEU B 181 ? 0.4762 0.4812 0.4557 -0.0712 0.0616  -0.0156 166 LEU B CA  
7144 C C   . LEU B 181 ? 0.4630 0.4831 0.4420 -0.0660 0.0575  -0.0188 166 LEU B C   
7145 O O   . LEU B 181 ? 0.4581 0.4720 0.4349 -0.0571 0.0517  -0.0178 166 LEU B O   
7146 C CB  . LEU B 181 ? 0.5017 0.4978 0.4905 -0.0802 0.0674  -0.0204 166 LEU B CB  
7147 C CG  . LEU B 181 ? 0.4752 0.4605 0.4707 -0.0761 0.0638  -0.0226 166 LEU B CG  
7148 C CD1 . LEU B 181 ? 0.4804 0.4506 0.4739 -0.0662 0.0578  -0.0149 166 LEU B CD1 
7149 C CD2 . LEU B 181 ? 0.5009 0.4742 0.5048 -0.0864 0.0722  -0.0268 166 LEU B CD2 
7161 N N   . ALA B 182 ? 0.4570 0.4980 0.4380 -0.0716 0.0608  -0.0218 167 ALA B N   
7162 C CA  . ALA B 182 ? 0.4714 0.5299 0.4547 -0.0669 0.0583  -0.0240 167 ALA B CA  
7163 C C   . ALA B 182 ? 0.4410 0.5001 0.4151 -0.0550 0.0556  -0.0186 167 ALA B C   
7164 O O   . ALA B 182 ? 0.4327 0.4908 0.4063 -0.0468 0.0517  -0.0203 167 ALA B O   
7165 C CB  . ALA B 182 ? 0.4621 0.5463 0.4496 -0.0762 0.0631  -0.0248 167 ALA B CB  
7171 N N   . ARG B 183 ? 0.4494 0.5088 0.4151 -0.0546 0.0585  -0.0121 168 ARG B N   
7172 C CA  . ARG B 183 ? 0.4507 0.5075 0.4054 -0.0452 0.0583  -0.0067 168 ARG B CA  
7173 C C   . ARG B 183 ? 0.4590 0.4942 0.4070 -0.0393 0.0526  -0.0063 168 ARG B C   
7174 O O   . ARG B 183 ? 0.4521 0.4857 0.3926 -0.0316 0.0513  -0.0054 168 ARG B O   
7175 C CB  . ARG B 183 ? 0.4717 0.5286 0.4184 -0.0468 0.0628  0.0003  168 ARG B CB  
7176 C CG  . ARG B 183 ? 0.5154 0.5939 0.4675 -0.0535 0.0684  0.0024  168 ARG B CG  
7177 C CD  . ARG B 183 ? 0.4462 0.5476 0.4017 -0.0497 0.0725  0.0054  168 ARG B CD  
7178 N NE  . ARG B 183 ? 0.5613 0.6729 0.5271 -0.0500 0.0698  -0.0015 168 ARG B NE  
7179 C CZ  . ARG B 183 ? 0.5165 0.6414 0.4929 -0.0598 0.0696  -0.0060 168 ARG B CZ  
7180 N NH1 . ARG B 183 ? 0.5740 0.7041 0.5512 -0.0706 0.0723  -0.0047 168 ARG B NH1 
7181 N NH2 . ARG B 183 ? 0.4844 0.6169 0.4697 -0.0594 0.0669  -0.0124 168 ARG B NH2 
7195 N N   . ARG B 184 ? 0.4633 0.4823 0.4138 -0.0431 0.0499  -0.0059 169 ARG B N   
7196 C CA  . ARG B 184 ? 0.4674 0.4682 0.4132 -0.0388 0.0442  -0.0032 169 ARG B CA  
7197 C C   . ARG B 184 ? 0.4644 0.4664 0.4140 -0.0333 0.0398  -0.0081 169 ARG B C   
7198 O O   . ARG B 184 ? 0.4825 0.4788 0.4224 -0.0267 0.0362  -0.0061 169 ARG B O   
7199 C CB  . ARG B 184 ? 0.5101 0.4968 0.4625 -0.0441 0.0439  -0.0005 169 ARG B CB  
7200 C CG  . ARG B 184 ? 0.5331 0.5034 0.4835 -0.0407 0.0381  0.0049  169 ARG B CG  
7201 C CD  . ARG B 184 ? 0.7504 0.7092 0.7004 -0.0445 0.0388  0.0131  169 ARG B CD  
7202 N NE  . ARG B 184 ? 0.7611 0.7173 0.7244 -0.0506 0.0445  0.0119  169 ARG B NE  
7203 C CZ  . ARG B 184 ? 0.8653 0.8102 0.8394 -0.0519 0.0455  0.0154  169 ARG B CZ  
7204 N NH1 . ARG B 184 ? 0.7923 0.7286 0.7664 -0.0473 0.0397  0.0210  169 ARG B NH1 
7205 N NH2 . ARG B 184 ? 0.6733 0.6148 0.6578 -0.0582 0.0536  0.0141  169 ARG B NH2 
7219 N N   . LEU B 185 ? 0.4473 0.4563 0.4099 -0.0366 0.0405  -0.0147 170 LEU B N   
7220 C CA  . LEU B 185 ? 0.4374 0.4479 0.4047 -0.0311 0.0361  -0.0202 170 LEU B CA  
7221 C C   . LEU B 185 ? 0.4894 0.5149 0.4504 -0.0237 0.0367  -0.0216 170 LEU B C   
7222 O O   . LEU B 185 ? 0.4664 0.4877 0.4230 -0.0158 0.0325  -0.0232 170 LEU B O   
7223 C CB  . LEU B 185 ? 0.4705 0.4867 0.4523 -0.0380 0.0381  -0.0273 170 LEU B CB  
7224 C CG  . LEU B 185 ? 0.4520 0.4504 0.4406 -0.0452 0.0401  -0.0263 170 LEU B CG  
7225 C CD1 . LEU B 185 ? 0.4670 0.4716 0.4665 -0.0550 0.0448  -0.0338 170 LEU B CD1 
7226 C CD2 . LEU B 185 ? 0.4396 0.4178 0.4288 -0.0390 0.0345  -0.0225 170 LEU B CD2 
7238 N N   . GLU B 186 ? 0.5112 0.5537 0.4711 -0.0259 0.0431  -0.0199 171 GLU B N   
7239 C CA  . GLU B 186 ? 0.4684 0.5265 0.4244 -0.0189 0.0467  -0.0196 171 GLU B CA  
7240 C C   . GLU B 186 ? 0.4247 0.4695 0.3628 -0.0122 0.0474  -0.0144 171 GLU B C   
7241 O O   . GLU B 186 ? 0.4896 0.5356 0.4220 -0.0044 0.0475  -0.0162 171 GLU B O   
7242 C CB  . GLU B 186 ? 0.4663 0.5463 0.4270 -0.0237 0.0545  -0.0163 171 GLU B CB  
7243 C CG  . GLU B 186 ? 0.5121 0.6096 0.4707 -0.0165 0.0612  -0.0130 171 GLU B CG  
7244 C CD  . GLU B 186 ? 0.6195 0.7413 0.5854 -0.0216 0.0690  -0.0072 171 GLU B CD  
7245 O OE1 . GLU B 186 ? 0.5242 0.6482 0.4942 -0.0313 0.0685  -0.0064 171 GLU B OE1 
7246 O OE2 . GLU B 186 ? 0.4789 0.6181 0.4462 -0.0161 0.0765  -0.0025 171 GLU B OE2 
7253 N N   . PHE B 187 ? 0.4403 0.4719 0.3683 -0.0159 0.0484  -0.0081 172 PHE B N   
7254 C CA  . PHE B 187 ? 0.5484 0.5674 0.4572 -0.0125 0.0507  -0.0024 172 PHE B CA  
7255 C C   . PHE B 187 ? 0.5908 0.5907 0.4909 -0.0112 0.0428  -0.0017 172 PHE B C   
7256 O O   . PHE B 187 ? 0.4920 0.4858 0.3776 -0.0067 0.0435  -0.0009 172 PHE B O   
7257 C CB  . PHE B 187 ? 0.4657 0.4793 0.3672 -0.0179 0.0553  0.0044  172 PHE B CB  
7258 C CG  . PHE B 187 ? 0.4616 0.4939 0.3696 -0.0190 0.0635  0.0063  172 PHE B CG  
7259 C CD1 . PHE B 187 ? 0.4948 0.5455 0.4070 -0.0139 0.0698  0.0057  172 PHE B CD1 
7260 C CD2 . PHE B 187 ? 0.4690 0.5017 0.3796 -0.0253 0.0652  0.0098  172 PHE B CD2 
7261 C CE1 . PHE B 187 ? 0.4850 0.5552 0.4044 -0.0155 0.0776  0.0102  172 PHE B CE1 
7262 C CE2 . PHE B 187 ? 0.4654 0.5162 0.3815 -0.0268 0.0724  0.0132  172 PHE B CE2 
7263 C CZ  . PHE B 187 ? 0.4629 0.5329 0.3836 -0.0222 0.0786  0.0142  172 PHE B CZ  
7273 N N   . ILE B 188 ? 0.4893 0.4799 0.3978 -0.0156 0.0364  -0.0010 173 ILE B N   
7274 C CA  . ILE B 188 ? 0.5043 0.4788 0.4068 -0.0147 0.0288  0.0024  173 ILE B CA  
7275 C C   . ILE B 188 ? 0.5146 0.4914 0.4252 -0.0088 0.0236  -0.0039 173 ILE B C   
7276 O O   . ILE B 188 ? 0.5973 0.5649 0.4981 -0.0050 0.0185  -0.0020 173 ILE B O   
7277 C CB  . ILE B 188 ? 0.6256 0.5894 0.5352 -0.0214 0.0259  0.0083  173 ILE B CB  
7278 C CG1 . ILE B 188 ? 0.6401 0.6033 0.5437 -0.0268 0.0310  0.0131  173 ILE B CG1 
7279 C CG2 . ILE B 188 ? 0.5886 0.5378 0.4920 -0.0213 0.0187  0.0157  173 ILE B CG2 
7280 C CD1 . ILE B 188 ? 0.5963 0.5478 0.5023 -0.0326 0.0284  0.0210  173 ILE B CD1 
7292 N N   . GLY B 189 ? 0.4602 0.4486 0.3877 -0.0086 0.0246  -0.0112 174 GLY B N   
7293 C CA  . GLY B 189 ? 0.4237 0.4145 0.3599 -0.0032 0.0199  -0.0181 174 GLY B CA  
7294 C C   . GLY B 189 ? 0.4296 0.4137 0.3823 -0.0073 0.0171  -0.0201 174 GLY B C   
7295 O O   . GLY B 189 ? 0.4325 0.4051 0.3879 -0.0131 0.0175  -0.0140 174 GLY B O   
7299 N N   . THR B 190 ? 0.4405 0.4312 0.4049 -0.0049 0.0154  -0.0284 175 THR B N   
7300 C CA  . THR B 190 ? 0.4247 0.4044 0.4028 -0.0086 0.0135  -0.0302 175 THR B CA  
7301 C C   . THR B 190 ? 0.4102 0.3697 0.3845 -0.0038 0.0067  -0.0234 175 THR B C   
7302 O O   . THR B 190 ? 0.4418 0.3992 0.4030 0.0028  0.0021  -0.0202 175 THR B O   
7303 C CB  . THR B 190 ? 0.4500 0.4410 0.4403 -0.0079 0.0132  -0.0409 175 THR B CB  
7304 O OG1 . THR B 190 ? 0.5282 0.5271 0.5130 0.0027  0.0090  -0.0448 175 THR B OG1 
7305 C CG2 . THR B 190 ? 0.5194 0.5305 0.5161 -0.0164 0.0204  -0.0450 175 THR B CG2 
7313 N N   . PRO B 191 ? 0.4152 0.3596 0.4004 -0.0078 0.0072  -0.0197 176 PRO B N   
7314 C CA  . PRO B 191 ? 0.4388 0.3652 0.4221 -0.0038 0.0014  -0.0098 176 PRO B CA  
7315 C C   . PRO B 191 ? 0.4074 0.3279 0.3943 0.0044  -0.0055 -0.0139 176 PRO B C   
7316 O O   . PRO B 191 ? 0.4101 0.3186 0.3923 0.0090  -0.0117 -0.0049 176 PRO B O   
7317 C CB  . PRO B 191 ? 0.4311 0.3441 0.4268 -0.0115 0.0078  -0.0029 176 PRO B CB  
7318 C CG  . PRO B 191 ? 0.4480 0.3680 0.4538 -0.0182 0.0151  -0.0140 176 PRO B CG  
7319 C CD  . PRO B 191 ? 0.4202 0.3623 0.4180 -0.0177 0.0150  -0.0220 176 PRO B CD  
7327 N N   . TYR B 192 ? 0.3937 0.3228 0.3890 0.0057  -0.0049 -0.0264 177 TYR B N   
7328 C CA  . TYR B 192 ? 0.3827 0.3015 0.3865 0.0114  -0.0101 -0.0304 177 TYR B CA  
7329 C C   . TYR B 192 ? 0.3760 0.2923 0.3682 0.0227  -0.0197 -0.0281 177 TYR B C   
7330 O O   . TYR B 192 ? 0.3732 0.2742 0.3693 0.0277  -0.0253 -0.0241 177 TYR B O   
7331 C CB  . TYR B 192 ? 0.3687 0.3003 0.3832 0.0092  -0.0076 -0.0447 177 TYR B CB  
7332 C CG  . TYR B 192 ? 0.3771 0.3111 0.4003 -0.0042 0.0024  -0.0467 177 TYR B CG  
7333 C CD1 . TYR B 192 ? 0.3860 0.3001 0.4193 -0.0113 0.0077  -0.0439 177 TYR B CD1 
7334 C CD2 . TYR B 192 ? 0.3774 0.3326 0.3977 -0.0100 0.0075  -0.0504 177 TYR B CD2 
7335 C CE1 . TYR B 192 ? 0.4199 0.3349 0.4586 -0.0247 0.0182  -0.0461 177 TYR B CE1 
7336 C CE2 . TYR B 192 ? 0.4088 0.3666 0.4350 -0.0231 0.0164  -0.0519 177 TYR B CE2 
7337 C CZ  . TYR B 192 ? 0.4618 0.3993 0.4964 -0.0308 0.0218  -0.0504 177 TYR B CZ  
7338 O OH  . TYR B 192 ? 0.4918 0.4305 0.5300 -0.0449 0.0321  -0.0523 177 TYR B OH  
7348 N N   . TRP B 193 ? 0.3750 0.3045 0.3519 0.0263  -0.0208 -0.0295 178 TRP B N   
7349 C CA  . TRP B 193 ? 0.4081 0.3352 0.3702 0.0354  -0.0282 -0.0275 178 TRP B CA  
7350 C C   . TRP B 193 ? 0.4104 0.3288 0.3562 0.0324  -0.0301 -0.0131 178 TRP B C   
7351 O O   . TRP B 193 ? 0.3881 0.3039 0.3179 0.0375  -0.0356 -0.0100 178 TRP B O   
7352 C CB  . TRP B 193 ? 0.3594 0.3054 0.3133 0.0411  -0.0261 -0.0383 178 TRP B CB  
7353 C CG  . TRP B 193 ? 0.3390 0.2966 0.3081 0.0457  -0.0261 -0.0520 178 TRP B CG  
7354 C CD1 . TRP B 193 ? 0.3227 0.2796 0.2937 0.0557  -0.0326 -0.0594 178 TRP B CD1 
7355 C CD2 . TRP B 193 ? 0.3528 0.3257 0.3367 0.0395  -0.0196 -0.0595 178 TRP B CD2 
7356 N NE1 . TRP B 193 ? 0.3059 0.2771 0.2932 0.0562  -0.0305 -0.0712 178 TRP B NE1 
7357 C CE2 . TRP B 193 ? 0.3121 0.2939 0.3071 0.0456  -0.0225 -0.0710 178 TRP B CE2 
7358 C CE3 . TRP B 193 ? 0.3570 0.3378 0.3455 0.0288  -0.0117 -0.0573 178 TRP B CE3 
7359 C CZ2 . TRP B 193 ? 0.3014 0.3007 0.3119 0.0400  -0.0179 -0.0793 178 TRP B CZ2 
7360 C CZ3 . TRP B 193 ? 0.3322 0.3298 0.3347 0.0234  -0.0071 -0.0655 178 TRP B CZ3 
7361 C CH2 . TRP B 193 ? 0.3336 0.3408 0.3471 0.0282  -0.0101 -0.0759 178 TRP B CH2 
7372 N N   . MET B 194 ? 0.4025 0.3173 0.3512 0.0234  -0.0253 -0.0041 179 MET B N   
7373 C CA  . MET B 194 ? 0.4185 0.3275 0.3526 0.0189  -0.0267 0.0099  179 MET B CA  
7374 C C   . MET B 194 ? 0.4223 0.3164 0.3586 0.0202  -0.0337 0.0236  179 MET B C   
7375 O O   . MET B 194 ? 0.4192 0.3036 0.3736 0.0208  -0.0333 0.0262  179 MET B O   
7376 C CB  . MET B 194 ? 0.4313 0.3420 0.3698 0.0094  -0.0193 0.0153  179 MET B CB  
7377 C CG  . MET B 194 ? 0.4782 0.4033 0.4130 0.0069  -0.0122 0.0059  179 MET B CG  
7378 S SD  . MET B 194 ? 0.4579 0.3824 0.3941 -0.0036 -0.0054 0.0145  179 MET B SD  
7379 C CE  . MET B 194 ? 0.4445 0.3863 0.3739 -0.0043 0.0019  0.0040  179 MET B CE  
7389 N N   . ALA B 195 ? 0.4304 0.3223 0.3478 0.0193  -0.0390 0.0337  180 ALA B N   
7390 C CA  . ALA B 195 ? 0.4374 0.3181 0.3562 0.0177  -0.0448 0.0516  180 ALA B CA  
7391 C C   . ALA B 195 ? 0.5042 0.3819 0.4348 0.0088  -0.0392 0.0649  180 ALA B C   
7392 O O   . ALA B 195 ? 0.4569 0.3415 0.3850 0.0028  -0.0329 0.0617  180 ALA B O   
7393 C CB  . ALA B 195 ? 0.4463 0.3276 0.3393 0.0162  -0.0513 0.0596  180 ALA B CB  
7399 N N   . PRO B 196 ? 0.4547 0.3223 0.3986 0.0082  -0.0407 0.0809  181 PRO B N   
7400 C CA  . PRO B 196 ? 0.4791 0.3447 0.4368 0.0004  -0.0334 0.0940  181 PRO B CA  
7401 C C   . PRO B 196 ? 0.4773 0.3512 0.4202 -0.0085 -0.0332 0.1024  181 PRO B C   
7402 O O   . PRO B 196 ? 0.4836 0.3606 0.4341 -0.0142 -0.0255 0.1027  181 PRO B O   
7403 C CB  . PRO B 196 ? 0.4866 0.3408 0.4581 0.0023  -0.0355 0.1132  181 PRO B CB  
7404 C CG  . PRO B 196 ? 0.4523 0.2997 0.4238 0.0122  -0.0418 0.1041  181 PRO B CG  
7405 C CD  . PRO B 196 ? 0.4468 0.3044 0.3953 0.0150  -0.0478 0.0886  181 PRO B CD  
7413 N N   . GLU B 197 ? 0.4822 0.3592 0.4030 -0.0106 -0.0410 0.1090  182 GLU B N   
7414 C CA  . GLU B 197 ? 0.4959 0.3792 0.4007 -0.0209 -0.0403 0.1165  182 GLU B CA  
7415 C C   . GLU B 197 ? 0.4964 0.3857 0.3922 -0.0219 -0.0341 0.0990  182 GLU B C   
7416 O O   . GLU B 197 ? 0.5062 0.3989 0.3994 -0.0296 -0.0298 0.1027  182 GLU B O   
7417 C CB  . GLU B 197 ? 0.5029 0.3870 0.3830 -0.0252 -0.0489 0.1272  182 GLU B CB  
7418 C CG  . GLU B 197 ? 0.4983 0.3828 0.3548 -0.0201 -0.0518 0.1113  182 GLU B CG  
7419 C CD  . GLU B 197 ? 0.5412 0.4207 0.4022 -0.0092 -0.0583 0.1075  182 GLU B CD  
7420 O OE1 . GLU B 197 ? 0.5071 0.3813 0.3920 -0.0040 -0.0589 0.1127  182 GLU B OE1 
7421 O OE2 . GLU B 197 ? 0.4821 0.3620 0.3221 -0.0059 -0.0619 0.0995  182 GLU B OE2 
7428 N N   . VAL B 198 ? 0.4854 0.3765 0.3778 -0.0140 -0.0333 0.0808  183 VAL B N   
7429 C CA  . VAL B 198 ? 0.4848 0.3831 0.3717 -0.0143 -0.0264 0.0662  183 VAL B CA  
7430 C C   . VAL B 198 ? 0.5022 0.4025 0.4110 -0.0157 -0.0191 0.0623  183 VAL B C   
7431 O O   . VAL B 198 ? 0.5068 0.4115 0.4129 -0.0209 -0.0134 0.0605  183 VAL B O   
7432 C CB  . VAL B 198 ? 0.4882 0.3906 0.3676 -0.0054 -0.0267 0.0499  183 VAL B CB  
7433 C CG1 . VAL B 198 ? 0.4705 0.3824 0.3483 -0.0053 -0.0182 0.0370  183 VAL B CG1 
7434 C CG2 . VAL B 198 ? 0.5571 0.4570 0.4110 -0.0051 -0.0318 0.0529  183 VAL B CG2 
7444 N N   . ALA B 199 ? 0.4998 0.3954 0.4293 -0.0118 -0.0184 0.0614  184 ALA B N   
7445 C CA  . ALA B 199 ? 0.4744 0.3703 0.4228 -0.0147 -0.0100 0.0573  184 ALA B CA  
7446 C C   . ALA B 199 ? 0.4871 0.3818 0.4396 -0.0226 -0.0058 0.0704  184 ALA B C   
7447 O O   . ALA B 199 ? 0.5584 0.4572 0.5161 -0.0266 0.0014  0.0654  184 ALA B O   
7448 C CB  . ALA B 199 ? 0.4666 0.3537 0.4343 -0.0108 -0.0087 0.0561  184 ALA B CB  
7454 N N   . ALA B 200 ? 0.5181 0.4084 0.4687 -0.0252 -0.0103 0.0880  185 ALA B N   
7455 C CA  . ALA B 200 ? 0.5140 0.4050 0.4707 -0.0327 -0.0064 0.1019  185 ALA B CA  
7456 C C   . ALA B 200 ? 0.6089 0.5071 0.5499 -0.0383 -0.0052 0.0974  185 ALA B C   
7457 O O   . ALA B 200 ? 0.5969 0.4972 0.5456 -0.0430 0.0009  0.0997  185 ALA B O   
7458 C CB  . ALA B 200 ? 0.5101 0.3986 0.4668 -0.0354 -0.0122 0.1236  185 ALA B CB  
7464 N N   . VAL B 201 ? 0.5870 0.4877 0.5053 -0.0377 -0.0100 0.0912  186 VAL B N   
7465 C CA  . VAL B 201 ? 0.6488 0.5536 0.5512 -0.0426 -0.0072 0.0865  186 VAL B CA  
7466 C C   . VAL B 201 ? 0.6539 0.5635 0.5645 -0.0398 0.0003  0.0716  186 VAL B C   
7467 O O   . VAL B 201 ? 0.6460 0.5578 0.5578 -0.0443 0.0051  0.0715  186 VAL B O   
7468 C CB  . VAL B 201 ? 0.6040 0.5080 0.4794 -0.0429 -0.0112 0.0837  186 VAL B CB  
7469 C CG1 . VAL B 201 ? 0.6755 0.5807 0.5344 -0.0479 -0.0059 0.0788  186 VAL B CG1 
7470 C CG2 . VAL B 201 ? 0.6254 0.5257 0.4902 -0.0484 -0.0188 0.1000  186 VAL B CG2 
7480 N N   . ALA B 202 ? 0.6136 0.5257 0.5301 -0.0328 0.0010  0.0594  187 ALA B N   
7481 C CA  . ALA B 202 ? 0.5624 0.4818 0.4863 -0.0315 0.0077  0.0463  187 ALA B CA  
7482 C C   . ALA B 202 ? 0.6238 0.5421 0.5661 -0.0357 0.0139  0.0481  187 ALA B C   
7483 O O   . ALA B 202 ? 0.6533 0.5780 0.5981 -0.0377 0.0198  0.0404  187 ALA B O   
7484 C CB  . ALA B 202 ? 0.6417 0.5651 0.5706 -0.0245 0.0068  0.0347  187 ALA B CB  
7490 N N   . LEU B 203 ? 0.6873 0.5978 0.6422 -0.0371 0.0138  0.0589  188 LEU B N   
7491 C CA  . LEU B 203 ? 0.7818 0.6897 0.7548 -0.0408 0.0222  0.0604  188 LEU B CA  
7492 C C   . LEU B 203 ? 0.7911 0.7010 0.7626 -0.0465 0.0254  0.0674  188 LEU B C   
7493 O O   . LEU B 203 ? 0.7595 0.6729 0.7359 -0.0494 0.0325  0.0610  188 LEU B O   
7494 C CB  . LEU B 203 ? 0.7108 0.6084 0.6994 -0.0396 0.0234  0.0707  188 LEU B CB  
7495 C CG  . LEU B 203 ? 0.8062 0.6973 0.8142 -0.0428 0.0351  0.0705  188 LEU B CG  
7496 C CD1 . LEU B 203 ? 0.6920 0.5859 0.7016 -0.0436 0.0402  0.0530  188 LEU B CD1 
7497 C CD2 . LEU B 203 ? 0.8305 0.7095 0.8527 -0.0406 0.0369  0.0833  188 LEU B CD2 
7509 N N   . LYS B 204 ? 0.8391 0.7476 0.8034 -0.0489 0.0202  0.0807  189 LYS B N   
7510 C CA  . LYS B 204 ? 0.9034 0.8140 0.8667 -0.0547 0.0222  0.0884  189 LYS B CA  
7511 C C   . LYS B 204 ? 0.9282 0.8424 0.8704 -0.0568 0.0193  0.0832  189 LYS B C   
7512 O O   . LYS B 204 ? 0.9913 0.9063 0.9306 -0.0620 0.0204  0.0885  189 LYS B O   
7513 C CB  . LYS B 204 ? 0.8976 0.8062 0.8661 -0.0583 0.0189  0.1081  189 LYS B CB  
7516 N N   . GLY B 205 ? 0.8240 0.7396 0.7520 -0.0530 0.0166  0.0733  190 GLY B N   
7517 C CA  . GLY B 205 ? 0.8211 0.7371 0.7275 -0.0551 0.0156  0.0708  190 GLY B CA  
7518 C C   . GLY B 205 ? 0.7171 0.6282 0.6060 -0.0597 0.0094  0.0815  190 GLY B C   
7519 O O   . GLY B 205 ? 0.7585 0.6671 0.6261 -0.0619 0.0097  0.0789  190 GLY B O   
7523 N N   . GLY B 206 ? 0.7538 0.6631 0.6506 -0.0623 0.0048  0.0947  191 GLY B N   
7524 C CA  . GLY B 206 ? 0.6326 0.5390 0.5124 -0.0679 -0.0019 0.1060  191 GLY B CA  
7525 C C   . GLY B 206 ? 0.9404 0.8460 0.8099 -0.0791 -0.0029 0.1177  191 GLY B C   
7526 O O   . GLY B 206 ? 0.9028 0.8050 0.7496 -0.0862 -0.0069 0.1236  191 GLY B O   
7530 N N   . TYR B 207 ? 0.8921 0.8006 0.7766 -0.0817 0.0009  0.1210  192 TYR B N   
7531 C CA  . TYR B 207 ? 0.8258 0.7342 0.7020 -0.0924 0.0002  0.1309  192 TYR B CA  
7532 C C   . TYR B 207 ? 0.8107 0.7251 0.7131 -0.0934 0.0032  0.1400  192 TYR B C   
7533 O O   . TYR B 207 ? 0.6740 0.5907 0.5985 -0.0866 0.0067  0.1395  192 TYR B O   
7534 C CB  . TYR B 207 ? 0.7111 0.6141 0.5690 -0.0939 0.0044  0.1192  192 TYR B CB  
7535 C CG  . TYR B 207 ? 0.7231 0.6281 0.5935 -0.0849 0.0109  0.1047  192 TYR B CG  
7536 C CD1 . TYR B 207 ? 0.7468 0.6549 0.6334 -0.0852 0.0150  0.1045  192 TYR B CD1 
7537 C CD2 . TYR B 207 ? 0.7350 0.6402 0.6010 -0.0769 0.0133  0.0918  192 TYR B CD2 
7538 C CE1 . TYR B 207 ? 0.6645 0.5752 0.5603 -0.0785 0.0209  0.0918  192 TYR B CE1 
7539 C CE2 . TYR B 207 ? 0.7791 0.6885 0.6559 -0.0706 0.0190  0.0802  192 TYR B CE2 
7540 C CZ  . TYR B 207 ? 0.7272 0.6390 0.6178 -0.0719 0.0226  0.0803  192 TYR B CZ  
7541 O OH  . TYR B 207 ? 0.7114 0.6282 0.6107 -0.0672 0.0283  0.0694  192 TYR B OH  
7551 N N   . ASN B 208 ? 0.6353 0.5514 0.5348 -0.1024 0.0030  0.1481  193 ASN B N   
7552 C CA  . ASN B 208 ? 0.6523 0.5758 0.5754 -0.1050 0.0057  0.1601  193 ASN B CA  
7553 C C   . ASN B 208 ? 0.7880 0.7107 0.7141 -0.1050 0.0110  0.1511  193 ASN B C   
7554 O O   . ASN B 208 ? 0.7847 0.7009 0.6940 -0.1036 0.0122  0.1375  193 ASN B O   
7555 C CB  . ASN B 208 ? 0.8421 0.7716 0.7615 -0.1171 -0.0003 0.1813  193 ASN B CB  
7556 C CG  . ASN B 208 ? 0.8583 0.7834 0.7509 -0.1286 -0.0038 0.1810  193 ASN B CG  
7557 O OD1 . ASN B 208 ? 0.9032 0.8182 0.7736 -0.1273 -0.0028 0.1666  193 ASN B OD1 
7558 N ND2 . ASN B 208 ? 0.9423 0.8746 0.8371 -0.1407 -0.0067 0.1978  193 ASN B ND2 
7565 N N   . GLU B 209 ? 0.4740 0.5965 0.5946 0.0855  0.0815  0.0161  194 GLU B N   
7566 C CA  . GLU B 209 ? 0.4809 0.5776 0.5657 0.0896  0.0697  0.0134  194 GLU B CA  
7567 C C   . GLU B 209 ? 0.4528 0.5437 0.5277 0.0791  0.0487  0.0150  194 GLU B C   
7568 O O   . GLU B 209 ? 0.4069 0.4757 0.4496 0.0787  0.0418  0.0130  194 GLU B O   
7569 C CB  . GLU B 209 ? 0.3975 0.4931 0.4906 0.1054  0.0675  0.0118  194 GLU B CB  
7570 C CG  . GLU B 209 ? 0.4524 0.5662 0.5798 0.1085  0.0497  0.0154  194 GLU B CG  
7571 C CD  . GLU B 209 ? 0.6747 0.8223 0.8547 0.1119  0.0574  0.0185  194 GLU B CD  
7572 O OE1 . GLU B 209 ? 0.7382 0.8960 0.9280 0.1095  0.0783  0.0180  194 GLU B OE1 
7573 O OE2 . GLU B 209 ? 0.6742 0.8381 0.8868 0.1169  0.0421  0.0221  194 GLU B OE2 
7580 N N   . LEU B 210 ? 0.4120 0.5207 0.5128 0.0700  0.0388  0.0184  195 LEU B N   
7581 C CA  . LEU B 210 ? 0.4162 0.5141 0.5010 0.0588  0.0205  0.0192  195 LEU B CA  
7582 C C   . LEU B 210 ? 0.4194 0.4976 0.4711 0.0499  0.0263  0.0171  195 LEU B C   
7583 O O   . LEU B 210 ? 0.4608 0.5244 0.4921 0.0426  0.0150  0.0164  195 LEU B O   
7584 C CB  . LEU B 210 ? 0.3763 0.4952 0.4937 0.0493  0.0083  0.0232  195 LEU B CB  
7585 C CG  . LEU B 210 ? 0.4223 0.5627 0.5779 0.0591  -0.0007 0.0264  195 LEU B CG  
7586 C CD1 . LEU B 210 ? 0.3856 0.5498 0.5787 0.0487  -0.0146 0.0312  195 LEU B CD1 
7587 C CD2 . LEU B 210 ? 0.4326 0.5545 0.5670 0.0669  -0.0164 0.0260  195 LEU B CD2 
7599 N N   A CYS B 211 ? 0.4017 0.4771 0.4461 0.0510  0.0438  0.0162  196 CYS B N   
7600 N N   B CYS B 211 ? 0.4044 0.4802 0.4493 0.0508  0.0438  0.0162  196 CYS B N   
7601 C CA  A CYS B 211 ? 0.4319 0.4874 0.4460 0.0448  0.0476  0.0148  196 CYS B CA  
7602 C CA  B CYS B 211 ? 0.4318 0.4874 0.4460 0.0450  0.0479  0.0148  196 CYS B CA  
7603 C C   A CYS B 211 ? 0.4272 0.4626 0.4128 0.0500  0.0421  0.0122  196 CYS B C   
7604 C C   B CYS B 211 ? 0.4287 0.4646 0.4151 0.0498  0.0413  0.0123  196 CYS B C   
7605 O O   A CYS B 211 ? 0.3827 0.4036 0.3483 0.0446  0.0397  0.0113  196 CYS B O   
7606 O O   B CYS B 211 ? 0.3829 0.4046 0.3501 0.0439  0.0376  0.0114  196 CYS B O   
7607 C CB  A CYS B 211 ? 0.4258 0.4796 0.4353 0.0453  0.0657  0.0154  196 CYS B CB  
7608 C CB  B CYS B 211 ? 0.4254 0.4785 0.4337 0.0467  0.0661  0.0152  196 CYS B CB  
7609 S SG  A CYS B 211 ? 0.4782 0.5557 0.5222 0.0374  0.0761  0.0191  196 CYS B SG  
7610 S SG  B CYS B 211 ? 0.5135 0.5567 0.5065 0.0615  0.0756  0.0124  196 CYS B SG  
7621 N N   . ASP B 212 ? 0.3801 0.4144 0.3652 0.0605  0.0409  0.0110  197 ASP B N   
7622 C CA  . ASP B 212 ? 0.4206 0.4367 0.3814 0.0636  0.0346  0.0090  197 ASP B CA  
7623 C C   . ASP B 212 ? 0.3767 0.3877 0.3324 0.0573  0.0204  0.0095  197 ASP B C   
7624 O O   . ASP B 212 ? 0.3776 0.3734 0.3126 0.0550  0.0176  0.0083  197 ASP B O   
7625 C CB  . ASP B 212 ? 0.4233 0.4360 0.3831 0.0754  0.0359  0.0076  197 ASP B CB  
7626 C CG  . ASP B 212 ? 0.4701 0.4784 0.4225 0.0816  0.0509  0.0059  197 ASP B CG  
7627 O OD1 . ASP B 212 ? 0.4032 0.4048 0.3420 0.0768  0.0579  0.0061  197 ASP B OD1 
7628 O OD2 . ASP B 212 ? 0.4008 0.4091 0.3580 0.0918  0.0557  0.0043  197 ASP B OD2 
7634 N N   . ILE B 213 ? 0.4056 0.4286 0.3799 0.0540  0.0114  0.0116  198 ILE B N   
7635 C CA  . ILE B 213 ? 0.3850 0.3986 0.3485 0.0469  -0.0029 0.0122  198 ILE B CA  
7636 C C   . ILE B 213 ? 0.4111 0.4145 0.3592 0.0357  -0.0007 0.0108  198 ILE B C   
7637 O O   . ILE B 213 ? 0.4097 0.3960 0.3352 0.0312  -0.0047 0.0094  198 ILE B O   
7638 C CB  . ILE B 213 ? 0.3904 0.4187 0.3782 0.0462  -0.0161 0.0155  198 ILE B CB  
7639 C CG1 . ILE B 213 ? 0.4718 0.5079 0.4756 0.0597  -0.0179 0.0168  198 ILE B CG1 
7640 C CG2 . ILE B 213 ? 0.4195 0.4336 0.3899 0.0370  -0.0322 0.0164  198 ILE B CG2 
7641 C CD1 . ILE B 213 ? 0.4868 0.5020 0.4650 0.0658  -0.0208 0.0155  198 ILE B CD1 
7653 N N   . TRP B 214 ? 0.3838 0.3958 0.3430 0.0311  0.0069  0.0112  199 TRP B N   
7654 C CA  . TRP B 214 ? 0.4109 0.4099 0.3541 0.0224  0.0109  0.0096  199 TRP B CA  
7655 C C   . TRP B 214 ? 0.4147 0.3994 0.3381 0.0270  0.0188  0.0076  199 TRP B C   
7656 O O   . TRP B 214 ? 0.3905 0.3601 0.2962 0.0233  0.0178  0.0056  199 TRP B O   
7657 C CB  . TRP B 214 ? 0.3981 0.4070 0.3563 0.0172  0.0185  0.0111  199 TRP B CB  
7658 C CG  . TRP B 214 ? 0.4558 0.4484 0.3972 0.0092  0.0228  0.0096  199 TRP B CG  
7659 C CD1 . TRP B 214 ? 0.3991 0.3791 0.3256 0.0127  0.0322  0.0086  199 TRP B CD1 
7660 C CD2 . TRP B 214 ? 0.4074 0.3924 0.3451 -0.0030 0.0170  0.0089  199 TRP B CD2 
7661 N NE1 . TRP B 214 ? 0.4363 0.4018 0.3517 0.0049  0.0338  0.0074  199 TRP B NE1 
7662 C CE2 . TRP B 214 ? 0.4141 0.3806 0.3338 -0.0053 0.0252  0.0071  199 TRP B CE2 
7663 C CE3 . TRP B 214 ? 0.4285 0.4191 0.3761 -0.0125 0.0042  0.0098  199 TRP B CE3 
7664 C CZ2 . TRP B 214 ? 0.4340 0.3849 0.3425 -0.0163 0.0230  0.0053  199 TRP B CZ2 
7665 C CZ3 . TRP B 214 ? 0.4739 0.4489 0.4090 -0.0252 0.0004  0.0081  199 TRP B CZ3 
7666 C CH2 . TRP B 214 ? 0.4446 0.3988 0.3591 -0.0268 0.0108  0.0055  199 TRP B CH2 
7677 N N   . SER B 215 ? 0.3775 0.3665 0.3039 0.0350  0.0266  0.0081  200 SER B N   
7678 C CA  . SER B 215 ? 0.3760 0.3532 0.2871 0.0386  0.0314  0.0071  200 SER B CA  
7679 C C   . SER B 215 ? 0.3804 0.3481 0.2797 0.0392  0.0256  0.0056  200 SER B C   
7680 O O   . SER B 215 ? 0.4032 0.3616 0.2930 0.0384  0.0286  0.0047  200 SER B O   
7681 C CB  . SER B 215 ? 0.3744 0.3542 0.2862 0.0463  0.0375  0.0078  200 SER B CB  
7682 O OG  . SER B 215 ? 0.4424 0.4273 0.3604 0.0450  0.0458  0.0095  200 SER B OG  
7688 N N   . LEU B 216 ? 0.3805 0.3503 0.2816 0.0406  0.0177  0.0059  201 LEU B N   
7689 C CA  . LEU B 216 ? 0.3988 0.3566 0.2855 0.0399  0.0129  0.0052  201 LEU B CA  
7690 C C   . LEU B 216 ? 0.3966 0.3430 0.2702 0.0311  0.0119  0.0040  201 LEU B C   
7691 O O   . LEU B 216 ? 0.4320 0.3672 0.2928 0.0292  0.0156  0.0028  201 LEU B O   
7692 C CB  . LEU B 216 ? 0.3915 0.3506 0.2808 0.0442  0.0038  0.0066  201 LEU B CB  
7693 C CG  . LEU B 216 ? 0.4111 0.3546 0.2824 0.0420  -0.0018 0.0069  201 LEU B CG  
7694 C CD1 . LEU B 216 ? 0.4483 0.3851 0.3118 0.0435  0.0047  0.0058  201 LEU B CD1 
7695 C CD2 . LEU B 216 ? 0.4583 0.4011 0.3324 0.0472  -0.0123 0.0091  201 LEU B CD2 
7707 N N   . GLY B 217 ? 0.4029 0.3509 0.2791 0.0251  0.0076  0.0041  202 GLY B N   
7708 C CA  . GLY B 217 ? 0.4183 0.3506 0.2768 0.0162  0.0078  0.0019  202 GLY B CA  
7709 C C   . GLY B 217 ? 0.4294 0.3547 0.2832 0.0163  0.0205  -0.0005 202 GLY B C   
7710 O O   . GLY B 217 ? 0.5092 0.4199 0.3473 0.0135  0.0258  -0.0028 202 GLY B O   
7714 N N   . ILE B 218 ? 0.4048 0.3398 0.2724 0.0198  0.0261  0.0004  203 ILE B N   
7715 C CA  . ILE B 218 ? 0.4227 0.3513 0.2887 0.0217  0.0360  -0.0006 203 ILE B CA  
7716 C C   . ILE B 218 ? 0.3993 0.3271 0.2646 0.0268  0.0394  -0.0006 203 ILE B C   
7717 O O   . ILE B 218 ? 0.4053 0.3247 0.2668 0.0265  0.0467  -0.0023 203 ILE B O   
7718 C CB  . ILE B 218 ? 0.4222 0.3589 0.3000 0.0245  0.0394  0.0016  203 ILE B CB  
7719 C CG1 . ILE B 218 ? 0.4066 0.3457 0.2883 0.0175  0.0368  0.0020  203 ILE B CG1 
7720 C CG2 . ILE B 218 ? 0.3989 0.3272 0.2753 0.0273  0.0472  0.0015  203 ILE B CG2 
7721 C CD1 . ILE B 218 ? 0.4195 0.3416 0.2886 0.0096  0.0386  -0.0008 203 ILE B CD1 
7733 N N   . THR B 219 ? 0.3903 0.3266 0.2610 0.0314  0.0348  0.0013  204 THR B N   
7734 C CA  . THR B 219 ? 0.3872 0.3228 0.2584 0.0345  0.0360  0.0018  204 THR B CA  
7735 C C   . THR B 219 ? 0.3986 0.3238 0.2583 0.0295  0.0383  0.0002  204 THR B C   
7736 O O   . THR B 219 ? 0.3997 0.3232 0.2624 0.0296  0.0445  0.0000  204 THR B O   
7737 C CB  . THR B 219 ? 0.3816 0.3231 0.2554 0.0392  0.0297  0.0034  204 THR B CB  
7738 O OG1 . THR B 219 ? 0.3761 0.3244 0.2566 0.0434  0.0305  0.0045  204 THR B OG1 
7739 C CG2 . THR B 219 ? 0.3957 0.3348 0.2691 0.0405  0.0291  0.0040  204 THR B CG2 
7747 N N   . ALA B 220 ? 0.4101 0.3277 0.2567 0.0246  0.0333  -0.0005 205 ALA B N   
7748 C CA  . ALA B 220 ? 0.4283 0.3304 0.2564 0.0186  0.0362  -0.0019 205 ALA B CA  
7749 C C   . ALA B 220 ? 0.4917 0.3846 0.3150 0.0158  0.0489  -0.0051 205 ALA B C   
7750 O O   . ALA B 220 ? 0.4477 0.3334 0.2661 0.0140  0.0585  -0.0062 205 ALA B O   
7751 C CB  . ALA B 220 ? 0.4626 0.3551 0.2743 0.0134  0.0256  -0.0015 205 ALA B CB  
7757 N N   . ILE B 221 ? 0.4914 0.3834 0.3168 0.0154  0.0503  -0.0067 206 ILE B N   
7758 C CA  . ILE B 221 ? 0.4561 0.3377 0.2784 0.0150  0.0632  -0.0100 206 ILE B CA  
7759 C C   . ILE B 221 ? 0.4361 0.3294 0.2806 0.0225  0.0710  -0.0085 206 ILE B C   
7760 O O   . ILE B 221 ? 0.4697 0.3576 0.3160 0.0231  0.0832  -0.0104 206 ILE B O   
7761 C CB  . ILE B 221 ? 0.5201 0.3965 0.3399 0.0128  0.0616  -0.0115 206 ILE B CB  
7762 C CG1 . ILE B 221 ? 0.4701 0.3375 0.2720 0.0041  0.0503  -0.0122 206 ILE B CG1 
7763 C CG2 . ILE B 221 ? 0.4995 0.3605 0.3135 0.0134  0.0755  -0.0155 206 ILE B CG2 
7764 C CD1 . ILE B 221 ? 0.5489 0.4113 0.3494 -0.0007 0.0472  -0.0134 206 ILE B CD1 
7776 N N   . GLU B 222 ? 0.4736 0.3825 0.3353 0.0280  0.0639  -0.0049 207 GLU B N   
7777 C CA  . GLU B 222 ? 0.4275 0.3471 0.3098 0.0343  0.0666  -0.0025 207 GLU B CA  
7778 C C   . GLU B 222 ? 0.4500 0.3718 0.3371 0.0329  0.0712  -0.0023 207 GLU B C   
7779 O O   . GLU B 222 ? 0.4089 0.3348 0.3122 0.0356  0.0798  -0.0021 207 GLU B O   
7780 C CB  . GLU B 222 ? 0.3910 0.3217 0.2812 0.0384  0.0561  0.0011  207 GLU B CB  
7781 C CG  . GLU B 222 ? 0.3836 0.3232 0.2909 0.0436  0.0539  0.0043  207 GLU B CG  
7782 C CD  . GLU B 222 ? 0.3991 0.3436 0.3048 0.0459  0.0436  0.0070  207 GLU B CD  
7783 O OE1 . GLU B 222 ? 0.3760 0.3194 0.2711 0.0448  0.0404  0.0062  207 GLU B OE1 
7784 O OE2 . GLU B 222 ? 0.4167 0.3656 0.3320 0.0488  0.0386  0.0098  207 GLU B OE2 
7791 N N   . LEU B 223 ? 0.4701 0.3898 0.3455 0.0286  0.0655  -0.0018 208 LEU B N   
7792 C CA  . LEU B 223 ? 0.4140 0.3343 0.2924 0.0254  0.0697  -0.0009 208 LEU B CA  
7793 C C   . LEU B 223 ? 0.4381 0.3457 0.3061 0.0206  0.0850  -0.0041 208 LEU B C   
7794 O O   . LEU B 223 ? 0.4952 0.4066 0.3751 0.0190  0.0949  -0.0035 208 LEU B O   
7795 C CB  . LEU B 223 ? 0.4329 0.3493 0.2975 0.0221  0.0593  0.0007  208 LEU B CB  
7796 C CG  . LEU B 223 ? 0.4013 0.3265 0.2724 0.0273  0.0465  0.0028  208 LEU B CG  
7797 C CD1 . LEU B 223 ? 0.4510 0.3690 0.3075 0.0255  0.0377  0.0038  208 LEU B CD1 
7798 C CD2 . LEU B 223 ? 0.3918 0.3279 0.2826 0.0303  0.0448  0.0051  208 LEU B CD2 
7810 N N   . ALA B 224 ? 0.4496 0.3413 0.2951 0.0175  0.0876  -0.0075 209 ALA B N   
7811 C CA  . ALA B 224 ? 0.5032 0.3767 0.3310 0.0126  0.1033  -0.0114 209 ALA B CA  
7812 C C   . ALA B 224 ? 0.4934 0.3687 0.3384 0.0184  0.1184  -0.0140 209 ALA B C   
7813 O O   . ALA B 224 ? 0.5446 0.4104 0.3857 0.0167  0.1362  -0.0169 209 ALA B O   
7814 C CB  . ALA B 224 ? 0.5665 0.4181 0.3595 0.0061  0.0979  -0.0142 209 ALA B CB  
7820 N N   . GLU B 225 ? 0.5405 0.4263 0.4039 0.0256  0.1128  -0.0129 210 GLU B N   
7821 C CA  . GLU B 225 ? 0.5130 0.3955 0.3889 0.0320  0.1254  -0.0153 210 GLU B CA  
7822 C C   . GLU B 225 ? 0.4489 0.3526 0.3618 0.0414  0.1216  -0.0108 210 GLU B C   
7823 O O   . GLU B 225 ? 0.4933 0.3954 0.4213 0.0485  0.1310  -0.0118 210 GLU B O   
7824 C CB  . GLU B 225 ? 0.5619 0.4264 0.4161 0.0304  0.1229  -0.0187 210 GLU B CB  
7825 C CG  . GLU B 225 ? 0.5936 0.4356 0.4094 0.0199  0.1216  -0.0226 210 GLU B CG  
7826 C CD  . GLU B 225 ? 0.6342 0.4574 0.4296 0.0164  0.1185  -0.0262 210 GLU B CD  
7827 O OE1 . GLU B 225 ? 0.5997 0.4289 0.4104 0.0216  0.1153  -0.0247 210 GLU B OE1 
7828 O OE2 . GLU B 225 ? 0.7669 0.5669 0.5287 0.0074  0.1183  -0.0300 210 GLU B OE2 
7835 N N   . LEU B 226 ? 0.4891 0.4095 0.4148 0.0419  0.1073  -0.0058 211 LEU B N   
7836 C CA  . LEU B 226 ? 0.4366 0.3748 0.3922 0.0490  0.0992  -0.0007 211 LEU B CA  
7837 C C   . LEU B 226 ? 0.4560 0.3913 0.4097 0.0541  0.0903  0.0011  211 LEU B C   
7838 O O   . LEU B 226 ? 0.4511 0.3967 0.4233 0.0596  0.0813  0.0060  211 LEU B O   
7839 C CB  . LEU B 226 ? 0.4161 0.3644 0.4037 0.0546  0.1109  0.0002  211 LEU B CB  
7840 C CG  . LEU B 226 ? 0.4984 0.4521 0.4937 0.0489  0.1226  -0.0008 211 LEU B CG  
7841 C CD1 . LEU B 226 ? 0.6331 0.6043 0.6712 0.0553  0.1316  0.0017  211 LEU B CD1 
7842 C CD2 . LEU B 226 ? 0.5117 0.4716 0.5001 0.0414  0.1098  0.0021  211 LEU B CD2 
7854 N N   . GLN B 227 ? 0.5041 0.4244 0.4348 0.0513  0.0917  -0.0020 212 GLN B N   
7855 C CA  . GLN B 227 ? 0.4150 0.3313 0.3417 0.0540  0.0843  0.0002  212 GLN B CA  
7856 C C   . GLN B 227 ? 0.4183 0.3257 0.3206 0.0464  0.0806  -0.0023 212 GLN B C   
7857 O O   . GLN B 227 ? 0.4506 0.3472 0.3365 0.0404  0.0861  -0.0067 212 GLN B O   
7858 C CB  . GLN B 227 ? 0.5287 0.4342 0.4625 0.0602  0.0927  -0.0005 212 GLN B CB  
7859 C CG  . GLN B 227 ? 0.6135 0.5300 0.5782 0.0698  0.0939  0.0033  212 GLN B CG  
7860 C CD  . GLN B 227 ? 0.6243 0.5501 0.5991 0.0737  0.0780  0.0104  212 GLN B CD  
7861 O OE1 . GLN B 227 ? 0.6660 0.5888 0.6232 0.0698  0.0691  0.0119  212 GLN B OE1 
7862 N NE2 . GLN B 227 ? 0.6254 0.5620 0.6287 0.0813  0.0744  0.0149  212 GLN B NE2 
7871 N N   . PRO B 228 ? 0.4621 0.3730 0.3615 0.0461  0.0715  0.0007  213 PRO B N   
7872 C CA  . PRO B 228 ? 0.4851 0.3895 0.3685 0.0391  0.0689  -0.0010 213 PRO B CA  
7873 C C   . PRO B 228 ? 0.5116 0.3981 0.3855 0.0366  0.0759  -0.0041 213 PRO B C   
7874 O O   . PRO B 228 ? 0.4542 0.3337 0.3354 0.0426  0.0824  -0.0038 213 PRO B O   
7875 C CB  . PRO B 228 ? 0.4063 0.3193 0.2936 0.0407  0.0614  0.0035  213 PRO B CB  
7876 C CG  . PRO B 228 ? 0.4235 0.3372 0.3217 0.0482  0.0611  0.0072  213 PRO B CG  
7877 C CD  . PRO B 228 ? 0.4703 0.3888 0.3802 0.0516  0.0641  0.0061  213 PRO B CD  
7885 N N   . PRO B 229 ? 0.4449 0.3225 0.3032 0.0279  0.0739  -0.0069 214 PRO B N   
7886 C CA  . PRO B 229 ? 0.5426 0.3992 0.3884 0.0240  0.0793  -0.0100 214 PRO B CA  
7887 C C   . PRO B 229 ? 0.4956 0.3500 0.3488 0.0273  0.0791  -0.0060 214 PRO B C   
7888 O O   . PRO B 229 ? 0.4594 0.3274 0.3216 0.0286  0.0731  -0.0010 214 PRO B O   
7889 C CB  . PRO B 229 ? 0.6125 0.4644 0.4430 0.0122  0.0718  -0.0122 214 PRO B CB  
7890 C CG  . PRO B 229 ? 0.4638 0.3290 0.2955 0.0118  0.0659  -0.0116 214 PRO B CG  
7891 C CD  . PRO B 229 ? 0.4409 0.3249 0.2920 0.0211  0.0657  -0.0074 214 PRO B CD  
7899 N N   . LEU B 230 ? 0.4930 0.3266 0.3395 0.0288  0.0865  -0.0083 215 LEU B N   
7900 C CA  . LEU B 230 ? 0.5384 0.3626 0.3871 0.0314  0.0867  -0.0043 215 LEU B CA  
7901 C C   . LEU B 230 ? 0.4836 0.3193 0.3501 0.0427  0.0844  0.0019  215 LEU B C   
7902 O O   . LEU B 230 ? 0.4894 0.3191 0.3557 0.0444  0.0816  0.0071  215 LEU B O   
7903 C CB  . LEU B 230 ? 0.5334 0.3593 0.3760 0.0208  0.0801  -0.0018 215 LEU B CB  
7904 C CG  . LEU B 230 ? 0.5662 0.3786 0.3923 0.0077  0.0787  -0.0069 215 LEU B CG  
7905 C CD1 . LEU B 230 ? 0.5089 0.3329 0.3391 -0.0028 0.0712  -0.0034 215 LEU B CD1 
7906 C CD2 . LEU B 230 ? 0.6186 0.3994 0.4289 0.0064  0.0858  -0.0106 215 LEU B CD2 
7918 N N   . PHE B 231 ? 0.5052 0.3551 0.3856 0.0496  0.0850  0.0019  216 PHE B N   
7919 C CA  . PHE B 231 ? 0.4942 0.3562 0.3918 0.0587  0.0792  0.0081  216 PHE B CA  
7920 C C   . PHE B 231 ? 0.4753 0.3235 0.3800 0.0675  0.0808  0.0115  216 PHE B C   
7921 O O   . PHE B 231 ? 0.4739 0.3255 0.3857 0.0730  0.0723  0.0184  216 PHE B O   
7922 C CB  . PHE B 231 ? 0.4631 0.3415 0.3768 0.0629  0.0800  0.0069  216 PHE B CB  
7923 C CG  . PHE B 231 ? 0.5801 0.4532 0.5078 0.0703  0.0907  0.0044  216 PHE B CG  
7924 C CD1 . PHE B 231 ? 0.6131 0.4745 0.5298 0.0667  0.1033  -0.0029 216 PHE B CD1 
7925 C CD2 . PHE B 231 ? 0.5584 0.4368 0.5100 0.0812  0.0883  0.0094  216 PHE B CD2 
7926 C CE1 . PHE B 231 ? 0.6639 0.5190 0.5931 0.0743  0.1169  -0.0060 216 PHE B CE1 
7927 C CE2 . PHE B 231 ? 0.5500 0.4259 0.5204 0.0895  0.1000  0.0071  216 PHE B CE2 
7928 C CZ  . PHE B 231 ? 0.6065 0.4707 0.5657 0.0864  0.1160  -0.0010 216 PHE B CZ  
7938 N N   . ASP B 232 ? 0.4942 0.3246 0.3959 0.0698  0.0912  0.0070  217 ASP B N   
7939 C CA  . ASP B 232 ? 0.5129 0.3277 0.4227 0.0799  0.0935  0.0100  217 ASP B CA  
7940 C C   . ASP B 232 ? 0.5820 0.3736 0.4716 0.0750  0.0914  0.0124  217 ASP B C   
7941 O O   . ASP B 232 ? 0.5565 0.3293 0.4481 0.0830  0.0930  0.0151  217 ASP B O   
7942 C CB  . ASP B 232 ? 0.5283 0.3327 0.4454 0.0865  0.1085  0.0034  217 ASP B CB  
7943 C CG  . ASP B 232 ? 0.5434 0.3299 0.4337 0.0759  0.1184  -0.0057 217 ASP B CG  
7944 O OD1 . ASP B 232 ? 0.5326 0.3261 0.4079 0.0639  0.1129  -0.0072 217 ASP B OD1 
7945 O OD2 . ASP B 232 ? 0.6555 0.4196 0.5391 0.0798  0.1313  -0.0114 217 ASP B OD2 
7950 N N   . VAL B 233 ? 0.5281 0.3208 0.4004 0.0622  0.0880  0.0120  218 VAL B N   
7951 C CA  . VAL B 233 ? 0.5473 0.3198 0.4012 0.0541  0.0873  0.0140  218 VAL B CA  
7952 C C   . VAL B 233 ? 0.5417 0.3212 0.3941 0.0530  0.0787  0.0227  218 VAL B C   
7953 O O   . VAL B 233 ? 0.5205 0.3219 0.3790 0.0526  0.0735  0.0246  218 VAL B O   
7954 C CB  . VAL B 233 ? 0.5499 0.3194 0.3885 0.0393  0.0898  0.0078  218 VAL B CB  
7955 C CG1 . VAL B 233 ? 0.6297 0.3812 0.4532 0.0287  0.0887  0.0106  218 VAL B CG1 
7956 C CG2 . VAL B 233 ? 0.5885 0.3433 0.4199 0.0396  0.0986  -0.0011 218 VAL B CG2 
7966 N N   . HIS B 234 ? 0.5827 0.3398 0.4234 0.0523  0.0779  0.0280  219 HIS B N   
7967 C CA  . HIS B 234 ? 0.5690 0.3257 0.4017 0.0507  0.0715  0.0367  219 HIS B CA  
7968 C C   . HIS B 234 ? 0.5611 0.3377 0.3904 0.0394  0.0720  0.0358  219 HIS B C   
7969 O O   . HIS B 234 ? 0.5691 0.3475 0.3954 0.0283  0.0766  0.0312  219 HIS B O   
7970 C CB  . HIS B 234 ? 0.6022 0.3274 0.4172 0.0473  0.0730  0.0417  219 HIS B CB  
7971 C CG  . HIS B 234 ? 0.6610 0.3785 0.4627 0.0468  0.0672  0.0517  219 HIS B CG  
7972 N ND1 . HIS B 234 ? 0.6521 0.3803 0.4442 0.0362  0.0690  0.0540  219 HIS B ND1 
7973 C CD2 . HIS B 234 ? 0.6879 0.3852 0.4819 0.0555  0.0600  0.0602  219 HIS B CD2 
7974 C CE1 . HIS B 234 ? 0.6300 0.3432 0.4053 0.0376  0.0647  0.0630  219 HIS B CE1 
7975 N NE2 . HIS B 234 ? 0.6554 0.3490 0.4305 0.0490  0.0576  0.0673  219 HIS B NE2 
7983 N N   . PRO B 235 ? 0.5772 0.3675 0.4068 0.0421  0.0668  0.0401  220 PRO B N   
7984 C CA  . PRO B 235 ? 0.5232 0.3342 0.3537 0.0342  0.0689  0.0381  220 PRO B CA  
7985 C C   . PRO B 235 ? 0.5364 0.3418 0.3571 0.0214  0.0753  0.0401  220 PRO B C   
7986 O O   . PRO B 235 ? 0.5225 0.3450 0.3513 0.0133  0.0785  0.0363  220 PRO B O   
7987 C CB  . PRO B 235 ? 0.5185 0.3369 0.3461 0.0410  0.0624  0.0425  220 PRO B CB  
7988 C CG  . PRO B 235 ? 0.5411 0.3381 0.3601 0.0483  0.0562  0.0495  220 PRO B CG  
7989 C CD  . PRO B 235 ? 0.5948 0.3809 0.4236 0.0525  0.0580  0.0469  220 PRO B CD  
7997 N N   . LEU B 236 ? 0.5627 0.3449 0.3675 0.0189  0.0770  0.0466  221 LEU B N   
7998 C CA  . LEU B 236 ? 0.5774 0.3538 0.3747 0.0049  0.0847  0.0489  221 LEU B CA  
7999 C C   . LEU B 236 ? 0.5778 0.3525 0.3826 -0.0046 0.0869  0.0430  221 LEU B C   
8000 O O   . LEU B 236 ? 0.5711 0.3607 0.3848 -0.0163 0.0903  0.0410  221 LEU B O   
8001 C CB  . LEU B 236 ? 0.6549 0.4010 0.4296 0.0038  0.0859  0.0577  221 LEU B CB  
8002 C CG  . LEU B 236 ? 0.6319 0.3710 0.3955 -0.0111 0.0958  0.0625  221 LEU B CG  
8003 C CD1 . LEU B 236 ? 0.7143 0.4783 0.4834 -0.0144 0.1025  0.0625  221 LEU B CD1 
8004 C CD2 . LEU B 236 ? 0.6709 0.3744 0.4068 -0.0110 0.0957  0.0720  221 LEU B CD2 
8016 N N   . ARG B 237 ? 0.5886 0.3442 0.3899 0.0005  0.0845  0.0401  222 ARG B N   
8017 C CA  . ARG B 237 ? 0.5941 0.3430 0.3965 -0.0080 0.0858  0.0332  222 ARG B CA  
8018 C C   . ARG B 237 ? 0.6092 0.3863 0.4262 -0.0116 0.0835  0.0269  222 ARG B C   
8019 O O   . ARG B 237 ? 0.5865 0.3672 0.4060 -0.0248 0.0829  0.0238  222 ARG B O   
8020 C CB  . ARG B 237 ? 0.6622 0.3872 0.4587 0.0020  0.0857  0.0298  222 ARG B CB  
8021 C CG  . ARG B 237 ? 0.6282 0.3339 0.4158 -0.0070 0.0882  0.0227  222 ARG B CG  
8022 C CD  . ARG B 237 ? 0.6639 0.3377 0.4418 0.0035  0.0915  0.0207  222 ARG B CD  
8023 N NE  . ARG B 237 ? 0.6872 0.3298 0.4496 -0.0001 0.0926  0.0266  222 ARG B NE  
8024 C CZ  . ARG B 237 ? 0.7701 0.3941 0.5292 0.0128  0.0918  0.0328  222 ARG B CZ  
8025 N NH1 . ARG B 237 ? 0.7264 0.3624 0.5004 0.0303  0.0893  0.0341  222 ARG B NH1 
8026 N NH2 . ARG B 237 ? 0.7863 0.3783 0.5276 0.0074  0.0925  0.0384  222 ARG B NH2 
8040 N N   . VAL B 238 ? 0.5575 0.3539 0.3842 -0.0007 0.0808  0.0255  223 VAL B N   
8041 C CA  . VAL B 238 ? 0.5551 0.3753 0.3934 -0.0034 0.0778  0.0203  223 VAL B CA  
8042 C C   . VAL B 238 ? 0.5144 0.3535 0.3622 -0.0140 0.0783  0.0227  223 VAL B C   
8043 O O   . VAL B 238 ? 0.5108 0.3600 0.3664 -0.0234 0.0749  0.0193  223 VAL B O   
8044 C CB  . VAL B 238 ? 0.4999 0.3354 0.3460 0.0095  0.0751  0.0195  223 VAL B CB  
8045 C CG1 . VAL B 238 ? 0.4788 0.3385 0.3355 0.0067  0.0717  0.0162  223 VAL B CG1 
8046 C CG2 . VAL B 238 ? 0.5055 0.3278 0.3496 0.0181  0.0761  0.0158  223 VAL B CG2 
8056 N N   . LEU B 239 ? 0.5161 0.3591 0.3632 -0.0129 0.0826  0.0289  224 LEU B N   
8057 C CA  . LEU B 239 ? 0.5538 0.4150 0.4126 -0.0222 0.0869  0.0315  224 LEU B CA  
8058 C C   . LEU B 239 ? 0.6000 0.4544 0.4619 -0.0384 0.0881  0.0318  224 LEU B C   
8059 O O   . LEU B 239 ? 0.5709 0.4459 0.4516 -0.0478 0.0867  0.0308  224 LEU B O   
8060 C CB  . LEU B 239 ? 0.6342 0.4926 0.4841 -0.0188 0.0943  0.0380  224 LEU B CB  
8061 C CG  . LEU B 239 ? 0.5417 0.4091 0.3888 -0.0057 0.0926  0.0380  224 LEU B CG  
8062 C CD1 . LEU B 239 ? 0.5456 0.3956 0.3716 -0.0028 0.0974  0.0447  224 LEU B CD1 
8063 C CD2 . LEU B 239 ? 0.4882 0.3837 0.3536 -0.0057 0.0945  0.0353  224 LEU B CD2 
8075 N N   . PHE B 240 ? 0.5831 0.4081 0.4277 -0.0421 0.0897  0.0335  225 PHE B N   
8076 C CA  . PHE B 240 ? 0.5755 0.3892 0.4198 -0.0590 0.0899  0.0336  225 PHE B CA  
8077 C C   . PHE B 240 ? 0.5710 0.3896 0.4218 -0.0655 0.0807  0.0263  225 PHE B C   
8078 O O   . PHE B 240 ? 0.5814 0.4120 0.4463 -0.0803 0.0771  0.0262  225 PHE B O   
8079 C CB  . PHE B 240 ? 0.6141 0.3895 0.4347 -0.0597 0.0926  0.0362  225 PHE B CB  
8080 C CG  . PHE B 240 ? 0.7122 0.4768 0.5213 -0.0572 0.1003  0.0450  225 PHE B CG  
8081 C CD1 . PHE B 240 ? 0.6129 0.3991 0.4316 -0.0603 0.1075  0.0497  225 PHE B CD1 
8082 C CD2 . PHE B 240 ? 0.7433 0.4732 0.5299 -0.0515 0.1005  0.0486  225 PHE B CD2 
8083 C CE1 . PHE B 240 ? 0.6328 0.4038 0.4340 -0.0590 0.1151  0.0576  225 PHE B CE1 
8084 C CE2 . PHE B 240 ? 0.7723 0.4877 0.5433 -0.0499 0.1056  0.0574  225 PHE B CE2 
8085 C CZ  . PHE B 240 ? 0.6603 0.3951 0.4361 -0.0544 0.1131  0.0618  225 PHE B CZ  
8095 N N   . LEU B 241 ? 0.5663 0.3758 0.4071 -0.0552 0.0764  0.0205  226 LEU B N   
8096 C CA  . LEU B 241 ? 0.5841 0.3918 0.4229 -0.0617 0.0680  0.0135  226 LEU B CA  
8097 C C   . LEU B 241 ? 0.6065 0.4480 0.4678 -0.0653 0.0610  0.0133  226 LEU B C   
8098 O O   . LEU B 241 ? 0.5549 0.3995 0.4210 -0.0784 0.0519  0.0111  226 LEU B O   
8099 C CB  . LEU B 241 ? 0.6424 0.4341 0.4657 -0.0490 0.0685  0.0077  226 LEU B CB  
8100 C CG  . LEU B 241 ? 0.6842 0.4391 0.4864 -0.0454 0.0743  0.0059  226 LEU B CG  
8101 C CD1 . LEU B 241 ? 0.7737 0.5222 0.5705 -0.0296 0.0779  0.0014  226 LEU B CD1 
8102 C CD2 . LEU B 241 ? 0.7254 0.4535 0.5106 -0.0610 0.0711  0.0013  226 LEU B CD2 
8114 N N   . MET B 242 ? 0.5301 0.3955 0.4047 -0.0537 0.0637  0.0157  227 MET B N   
8115 C CA  . MET B 242 ? 0.6504 0.5468 0.5478 -0.0548 0.0578  0.0159  227 MET B CA  
8116 C C   . MET B 242 ? 0.6133 0.5275 0.5339 -0.0687 0.0575  0.0200  227 MET B C   
8117 O O   . MET B 242 ? 0.7147 0.6523 0.6572 -0.0727 0.0491  0.0199  227 MET B O   
8118 C CB  . MET B 242 ? 0.6066 0.5210 0.5118 -0.0400 0.0628  0.0179  227 MET B CB  
8119 C CG  . MET B 242 ? 0.7375 0.6434 0.6289 -0.0273 0.0610  0.0143  227 MET B CG  
8120 S SD  . MET B 242 ? 0.7713 0.6964 0.6708 -0.0128 0.0646  0.0166  227 MET B SD  
8121 C CE  . MET B 242 ? 0.7481 0.6628 0.6346 -0.0026 0.0605  0.0121  227 MET B CE  
8131 N N   . THR B 243 ? 0.6728 0.5769 0.5908 -0.0758 0.0666  0.0244  228 THR B N   
8132 C CA  . THR B 243 ? 0.7395 0.6613 0.6822 -0.0903 0.0694  0.0291  228 THR B CA  
8133 C C   . THR B 243 ? 0.8224 0.7351 0.7670 -0.1088 0.0578  0.0272  228 THR B C   
8134 O O   . THR B 243 ? 0.8841 0.8206 0.8586 -0.1214 0.0535  0.0300  228 THR B O   
8135 C CB  . THR B 243 ? 0.7324 0.6427 0.6668 -0.0922 0.0848  0.0351  228 THR B CB  
8136 O OG1 . THR B 243 ? 0.6491 0.5604 0.5735 -0.0754 0.0930  0.0364  228 THR B OG1 
8137 C CG2 . THR B 243 ? 0.8809 0.8139 0.8446 -0.1064 0.0921  0.0406  228 THR B CG2 
8145 N N   . LYS B 244 ? 0.8222 0.7001 0.7361 -0.1110 0.0527  0.0224  229 LYS B N   
8146 C CA  . LYS B 244 ? 0.7184 0.5794 0.6256 -0.1295 0.0413  0.0197  229 LYS B CA  
8147 C C   . LYS B 244 ? 0.7568 0.6435 0.6873 -0.1371 0.0249  0.0186  229 LYS B C   
8148 O O   . LYS B 244 ? 0.7230 0.6291 0.6623 -0.1250 0.0207  0.0173  229 LYS B O   
8149 C CB  . LYS B 244 ? 0.7967 0.6154 0.6640 -0.1261 0.0393  0.0128  229 LYS B CB  
8150 C CG  . LYS B 244 ? 0.8600 0.6421 0.7047 -0.1328 0.0470  0.0137  229 LYS B CG  
8151 C CD  . LYS B 244 ? 0.8229 0.6045 0.6672 -0.1208 0.0619  0.0198  229 LYS B CD  
8152 C CE  . LYS B 244 ? 1.0462 0.7853 0.8633 -0.1244 0.0679  0.0206  229 LYS B CE  
8153 N NZ  . LYS B 244 ? 1.0140 0.7498 0.8287 -0.1154 0.0800  0.0282  229 LYS B NZ  
8167 N N   . SER B 245 ? 0.7361 0.6216 0.6765 -0.1579 0.0141  0.0195  230 SER B N   
8168 C CA  . SER B 245 ? 0.7074 0.6171 0.6723 -0.1668 -0.0051 0.0196  230 SER B CA  
8169 C C   . SER B 245 ? 0.6473 0.5362 0.5816 -0.1619 -0.0191 0.0125  230 SER B C   
8170 O O   . SER B 245 ? 0.7247 0.6357 0.6742 -0.1567 -0.0307 0.0129  230 SER B O   
8171 C CB  . SER B 245 ? 0.6287 0.5379 0.6089 -0.1922 -0.0159 0.0223  230 SER B CB  
8172 O OG  . SER B 245 ? 0.9249 0.8395 0.9203 -0.1987 0.0007  0.0281  230 SER B OG  
8178 N N   . GLY B 246 ? 0.6956 0.5402 0.5856 -0.1634 -0.0173 0.0062  231 GLY B N   
8179 C CA  . GLY B 246 ? 0.7272 0.5466 0.5826 -0.1603 -0.0272 -0.0011 231 GLY B CA  
8180 C C   . GLY B 246 ? 0.7423 0.5561 0.5807 -0.1381 -0.0137 -0.0042 231 GLY B C   
8181 O O   . GLY B 246 ? 0.7696 0.5506 0.5709 -0.1347 -0.0125 -0.0111 231 GLY B O   
8185 N N   . TYR B 247 ? 0.7314 0.5759 0.5964 -0.1236 -0.0030 0.0006  232 TYR B N   
8186 C CA  . TYR B 247 ? 0.6960 0.5388 0.5492 -0.1039 0.0072  -0.0016 232 TYR B CA  
8187 C C   . TYR B 247 ? 0.6224 0.4617 0.4613 -0.1017 -0.0042 -0.0057 232 TYR B C   
8188 O O   . TYR B 247 ? 0.6808 0.5402 0.5370 -0.1076 -0.0193 -0.0033 232 TYR B O   
8189 C CB  . TYR B 247 ? 0.6004 0.4767 0.4835 -0.0913 0.0168  0.0042  232 TYR B CB  
8190 C CG  . TYR B 247 ? 0.6259 0.5030 0.5002 -0.0727 0.0245  0.0025  232 TYR B CG  
8191 C CD1 . TYR B 247 ? 0.6488 0.5001 0.4994 -0.0645 0.0346  -0.0006 232 TYR B CD1 
8192 C CD2 . TYR B 247 ? 0.6495 0.5531 0.5412 -0.0633 0.0213  0.0043  232 TYR B CD2 
8193 C CE1 . TYR B 247 ? 0.6126 0.4671 0.4598 -0.0491 0.0407  -0.0017 232 TYR B CE1 
8194 C CE2 . TYR B 247 ? 0.6264 0.5295 0.5100 -0.0482 0.0275  0.0028  232 TYR B CE2 
8195 C CZ  . TYR B 247 ? 0.6314 0.5111 0.4939 -0.0419 0.0369  0.0001  232 TYR B CZ  
8196 O OH  . TYR B 247 ? 0.7487 0.6299 0.6074 -0.0284 0.0423  -0.0008 232 TYR B OH  
8206 N N   . GLN B 248 ? 0.7432 0.5562 0.5511 -0.0932 0.0032  -0.0115 233 GLN B N   
8207 C CA  . GLN B 248 ? 0.7517 0.5564 0.5400 -0.0908 -0.0041 -0.0153 233 GLN B CA  
8208 C C   . GLN B 248 ? 0.7528 0.5768 0.5525 -0.0730 0.0050  -0.0136 233 GLN B C   
8209 O O   . GLN B 248 ? 0.7678 0.5855 0.5641 -0.0619 0.0202  -0.0146 233 GLN B O   
8210 C CB  . GLN B 248 ? 0.7580 0.5179 0.5019 -0.0948 0.0005  -0.0234 233 GLN B CB  
8211 C CG  . GLN B 248 ? 0.9810 0.7140 0.7060 -0.1135 -0.0091 -0.0262 233 GLN B CG  
8212 C CD  . GLN B 248 ? 1.0778 0.8082 0.7930 -0.1282 -0.0321 -0.0264 233 GLN B CD  
8213 O OE1 . GLN B 248 ? 1.0917 0.8494 0.8378 -0.1372 -0.0473 -0.0205 233 GLN B OE1 
8214 N NE2 . GLN B 248 ? 1.1203 0.8170 0.7926 -0.1309 -0.0348 -0.0328 233 GLN B NE2 
8223 N N   . PRO B 249 ? 0.6703 0.5167 0.4843 -0.0698 -0.0049 -0.0107 234 PRO B N   
8224 C CA  . PRO B 249 ? 0.6601 0.5214 0.4823 -0.0541 0.0031  -0.0094 234 PRO B CA  
8225 C C   . PRO B 249 ? 0.5999 0.4357 0.3927 -0.0484 0.0132  -0.0147 234 PRO B C   
8226 O O   . PRO B 249 ? 0.6355 0.4424 0.3971 -0.0565 0.0107  -0.0197 234 PRO B O   
8227 C CB  . PRO B 249 ? 0.5368 0.4178 0.3725 -0.0545 -0.0123 -0.0061 234 PRO B CB  
8228 C CG  . PRO B 249 ? 0.6213 0.5125 0.4741 -0.0675 -0.0260 -0.0032 234 PRO B CG  
8229 C CD  . PRO B 249 ? 0.6156 0.4766 0.4433 -0.0800 -0.0247 -0.0076 234 PRO B CD  
8237 N N   . PRO B 250 ? 0.6914 0.5362 0.4926 -0.0350 0.0251  -0.0139 235 PRO B N   
8238 C CA  . PRO B 250 ? 0.6669 0.4919 0.4472 -0.0293 0.0365  -0.0184 235 PRO B CA  
8239 C C   . PRO B 250 ? 0.6809 0.4950 0.4393 -0.0331 0.0302  -0.0206 235 PRO B C   
8240 O O   . PRO B 250 ? 0.5651 0.3885 0.3261 -0.0382 0.0151  -0.0179 235 PRO B O   
8241 C CB  . PRO B 250 ? 0.7132 0.5577 0.5151 -0.0154 0.0455  -0.0152 235 PRO B CB  
8242 C CG  . PRO B 250 ? 0.6676 0.5329 0.4934 -0.0144 0.0421  -0.0101 235 PRO B CG  
8243 C CD  . PRO B 250 ? 0.5868 0.4592 0.4165 -0.0251 0.0288  -0.0088 235 PRO B CD  
8251 N N   . ARG B 251 ? 0.6374 0.4301 0.3739 -0.0304 0.0429  -0.0253 236 ARG B N   
8252 C CA  . ARG B 251 ? 0.6169 0.3943 0.3273 -0.0338 0.0416  -0.0275 236 ARG B CA  
8253 C C   . ARG B 251 ? 0.7130 0.4870 0.4229 -0.0244 0.0608  -0.0296 236 ARG B C   
8254 O O   . ARG B 251 ? 0.6362 0.4139 0.3616 -0.0164 0.0738  -0.0305 236 ARG B O   
8255 C CB  . ARG B 251 ? 0.7568 0.4984 0.4267 -0.0471 0.0367  -0.0327 236 ARG B CB  
8256 C CG  . ARG B 251 ? 0.7911 0.5358 0.4621 -0.0588 0.0144  -0.0301 236 ARG B CG  
8257 C CD  . ARG B 251 ? 0.9865 0.6912 0.6112 -0.0734 0.0067  -0.0353 236 ARG B CD  
8258 N NE  . ARG B 251 ? 1.0698 0.7438 0.6715 -0.0755 0.0222  -0.0426 236 ARG B NE  
8259 C CZ  . ARG B 251 ? 1.1842 0.8147 0.7375 -0.0860 0.0233  -0.0495 236 ARG B CZ  
8260 N NH1 . ARG B 251 ? 1.1784 0.7893 0.6981 -0.0966 0.0084  -0.0496 236 ARG B NH1 
8261 N NH2 . ARG B 251 ? 1.1771 0.7799 0.7127 -0.0856 0.0396  -0.0565 236 ARG B NH2 
8275 N N   . LEU B 252 ? 0.7627 0.5298 0.4563 -0.0257 0.0619  -0.0297 237 LEU B N   
8276 C CA  . LEU B 252 ? 0.7227 0.4854 0.4153 -0.0193 0.0813  -0.0319 237 LEU B CA  
8277 C C   . LEU B 252 ? 0.6291 0.3621 0.2991 -0.0207 0.0988  -0.0392 237 LEU B C   
8278 O O   . LEU B 252 ? 0.6892 0.3930 0.3248 -0.0306 0.0948  -0.0436 237 LEU B O   
8279 C CB  . LEU B 252 ? 0.6075 0.3632 0.2811 -0.0234 0.0794  -0.0304 237 LEU B CB  
8280 C CG  . LEU B 252 ? 0.5753 0.3587 0.2730 -0.0192 0.0661  -0.0236 237 LEU B CG  
8281 C CD1 . LEU B 252 ? 0.6747 0.4435 0.3453 -0.0259 0.0583  -0.0217 237 LEU B CD1 
8282 C CD2 . LEU B 252 ? 0.5776 0.3843 0.3083 -0.0087 0.0773  -0.0215 237 LEU B CD2 
8294 N N   . LYS B 253 ? 0.6538 0.3933 0.3438 -0.0104 0.1175  -0.0405 238 LYS B N   
8295 C CA  . LYS B 253 ? 0.7127 0.4258 0.3878 -0.0083 0.1368  -0.0475 238 LYS B CA  
8296 C C   . LYS B 253 ? 0.8555 0.5352 0.4883 -0.0154 0.1505  -0.0536 238 LYS B C   
8297 O O   . LYS B 253 ? 0.8869 0.5304 0.4812 -0.0226 0.1543  -0.0602 238 LYS B O   
8298 C CB  . LYS B 253 ? 0.7255 0.4588 0.4403 0.0062  0.1515  -0.0459 238 LYS B CB  
8299 C CG  . LYS B 253 ? 0.7602 0.4701 0.4692 0.0124  0.1718  -0.0524 238 LYS B CG  
8300 C CD  . LYS B 253 ? 1.0220 0.7324 0.7443 0.0165  0.1644  -0.0511 238 LYS B CD  
8301 C CE  . LYS B 253 ? 1.0589 0.7438 0.7768 0.0246  0.1844  -0.0574 238 LYS B CE  
8302 N NZ  . LYS B 253 ? 1.1088 0.7910 0.8376 0.0283  0.1764  -0.0552 238 LYS B NZ  
8316 N N   . GLU B 254 ? 0.7464 0.4346 0.3825 -0.0144 0.1588  -0.0515 239 GLU B N   
8317 C CA  . GLU B 254 ? 0.7413 0.3972 0.3361 -0.0214 0.1750  -0.0566 239 GLU B CA  
8318 C C   . GLU B 254 ? 0.8776 0.5162 0.4329 -0.0350 0.1553  -0.0545 239 GLU B C   
8319 O O   . GLU B 254 ? 0.9680 0.6267 0.5357 -0.0358 0.1429  -0.0478 239 GLU B O   
8320 C CB  . GLU B 254 ? 0.9103 0.5834 0.5293 -0.0151 0.1949  -0.0546 239 GLU B CB  
8321 C CG  . GLU B 254 ? 0.9332 0.6213 0.5917 -0.0015 0.2158  -0.0566 239 GLU B CG  
8322 C CD  . GLU B 254 ? 0.9380 0.6340 0.6122 0.0016  0.2401  -0.0564 239 GLU B CD  
8323 O OE1 . GLU B 254 ? 0.9337 0.5980 0.5698 -0.0047 0.2601  -0.0621 239 GLU B OE1 
8324 O OE2 . GLU B 254 ? 0.9960 0.7291 0.7195 0.0093  0.2390  -0.0505 239 GLU B OE2 
8331 N N   . LYS B 255 ? 0.9390 0.5376 0.4449 -0.0456 0.1518  -0.0601 240 LYS B N   
8332 C CA  . LYS B 255 ? 0.9498 0.5302 0.4178 -0.0588 0.1290  -0.0574 240 LYS B CA  
8333 C C   . LYS B 255 ? 0.9550 0.5223 0.3974 -0.0633 0.1373  -0.0553 240 LYS B C   
8334 O O   . LYS B 255 ? 0.9407 0.5226 0.3893 -0.0655 0.1193  -0.0480 240 LYS B O   
8335 C CB  . LYS B 255 ? 1.0404 0.5766 0.4576 -0.0706 0.1228  -0.0641 240 LYS B CB  
8336 C CG  . LYS B 255 ? 1.1555 0.6915 0.5623 -0.0815 0.0878  -0.0595 240 LYS B CG  
8337 C CD  . LYS B 255 ? 1.2760 0.7711 0.6396 -0.0935 0.0806  -0.0664 240 LYS B CD  
8338 C CE  . LYS B 255 ? 1.3603 0.8691 0.7360 -0.1021 0.0458  -0.0611 240 LYS B CE  
8339 N NZ  . LYS B 255 ? 1.3874 0.8946 0.7462 -0.1102 0.0207  -0.0542 240 LYS B NZ  
8353 N N   . GLY B 256 ? 0.9056 0.4439 0.3191 -0.0644 0.1661  -0.0617 241 GLY B N   
8354 C CA  . GLY B 256 ? 0.9538 0.4695 0.3311 -0.0719 0.1769  -0.0606 241 GLY B CA  
8355 C C   . GLY B 256 ? 0.9446 0.4958 0.3624 -0.0657 0.1826  -0.0534 241 GLY B C   
8356 O O   . GLY B 256 ? 0.9449 0.4798 0.3343 -0.0734 0.1852  -0.0501 241 GLY B O   
8360 N N   . LYS B 257 ? 0.8384 0.4347 0.3191 -0.0530 0.1837  -0.0506 242 LYS B N   
8361 C CA  . LYS B 257 ? 0.8214 0.4509 0.3416 -0.0480 0.1876  -0.0441 242 LYS B CA  
8362 C C   . LYS B 257 ? 0.8998 0.5417 0.4216 -0.0516 0.1587  -0.0359 242 LYS B C   
8363 O O   . LYS B 257 ? 0.8481 0.5046 0.3855 -0.0514 0.1605  -0.0305 242 LYS B O   
8364 C CB  . LYS B 257 ? 0.8128 0.4831 0.3959 -0.0339 0.1942  -0.0434 242 LYS B CB  
8365 C CG  . LYS B 257 ? 0.8956 0.5987 0.5208 -0.0295 0.1998  -0.0375 242 LYS B CG  
8366 C CD  . LYS B 257 ? 0.7859 0.5258 0.4699 -0.0161 0.2042  -0.0366 242 LYS B CD  
8367 C CE  . LYS B 257 ? 0.8009 0.5717 0.5253 -0.0138 0.2070  -0.0305 242 LYS B CE  
8368 N NZ  . LYS B 257 ? 0.7489 0.5521 0.5285 -0.0017 0.2123  -0.0293 242 LYS B NZ  
8382 N N   . TRP B 258 ? 0.8278 0.4640 0.3357 -0.0548 0.1325  -0.0347 243 TRP B N   
8383 C CA  . TRP B 258 ? 0.7508 0.4052 0.2721 -0.0544 0.1050  -0.0271 243 TRP B CA  
8384 C C   . TRP B 258 ? 0.8093 0.4306 0.2809 -0.0657 0.0844  -0.0253 243 TRP B C   
8385 O O   . TRP B 258 ? 0.8336 0.4227 0.2657 -0.0736 0.0845  -0.0304 243 TRP B O   
8386 C CB  . TRP B 258 ? 0.7484 0.4379 0.3152 -0.0452 0.0904  -0.0256 243 TRP B CB  
8387 C CG  . TRP B 258 ? 0.6685 0.3849 0.2786 -0.0346 0.1078  -0.0274 243 TRP B CG  
8388 C CD1 . TRP B 258 ? 0.6639 0.3823 0.2863 -0.0299 0.1169  -0.0323 243 TRP B CD1 
8389 C CD2 . TRP B 258 ? 0.6573 0.4004 0.3033 -0.0277 0.1161  -0.0239 243 TRP B CD2 
8390 N NE1 . TRP B 258 ? 0.6324 0.3777 0.2969 -0.0196 0.1295  -0.0314 243 TRP B NE1 
8391 C CE2 . TRP B 258 ? 0.6596 0.4212 0.3399 -0.0186 0.1286  -0.0263 243 TRP B CE2 
8392 C CE3 . TRP B 258 ? 0.6932 0.4445 0.3449 -0.0289 0.1130  -0.0186 243 TRP B CE3 
8393 C CZ2 . TRP B 258 ? 0.5863 0.3756 0.3071 -0.0111 0.1362  -0.0234 243 TRP B CZ2 
8394 C CZ3 . TRP B 258 ? 0.6009 0.3790 0.2921 -0.0224 0.1216  -0.0163 243 TRP B CZ3 
8395 C CH2 . TRP B 258 ? 0.6461 0.4438 0.3720 -0.0137 0.1322  -0.0186 243 TRP B CH2 
8406 N N   . SER B 259 ? 0.7889 0.4166 0.2619 -0.0664 0.0653  -0.0178 244 SER B N   
8407 C CA  . SER B 259 ? 0.8290 0.4274 0.2592 -0.0760 0.0417  -0.0142 244 SER B CA  
8408 C C   . SER B 259 ? 0.8128 0.4225 0.2566 -0.0755 0.0161  -0.0136 244 SER B C   
8409 O O   . SER B 259 ? 0.7763 0.4207 0.2666 -0.0669 0.0152  -0.0144 244 SER B O   
8410 C CB  . SER B 259 ? 0.8211 0.4232 0.2527 -0.0749 0.0286  -0.0057 244 SER B CB  
8411 O OG  . SER B 259 ? 0.8141 0.4522 0.2913 -0.0652 0.0081  -0.0012 244 SER B OG  
8417 N N   . ALA B 260 ? 0.8559 0.4357 0.2587 -0.0858 -0.0059 -0.0114 245 ALA B N   
8418 C CA  . ALA B 260 ? 0.8910 0.4816 0.3081 -0.0876 -0.0324 -0.0100 245 ALA B CA  
8419 C C   . ALA B 260 ? 0.8474 0.4820 0.3200 -0.0764 -0.0493 -0.0031 245 ALA B C   
8420 O O   . ALA B 260 ? 0.7706 0.4335 0.2813 -0.0724 -0.0579 -0.0033 245 ALA B O   
8421 C CB  . ALA B 260 ? 0.9101 0.4586 0.2715 -0.1017 -0.0557 -0.0079 245 ALA B CB  
8427 N N   . ALA B 261 ? 0.7914 0.4303 0.2681 -0.0714 -0.0526 0.0029  246 ALA B N   
8428 C CA  . ALA B 261 ? 0.7906 0.4675 0.3171 -0.0594 -0.0655 0.0086  246 ALA B CA  
8429 C C   . ALA B 261 ? 0.6945 0.4091 0.2701 -0.0491 -0.0488 0.0049  246 ALA B C   
8430 O O   . ALA B 261 ? 0.6637 0.4086 0.2791 -0.0423 -0.0593 0.0068  246 ALA B O   
8431 C CB  . ALA B 261 ? 0.7531 0.4226 0.2710 -0.0558 -0.0671 0.0144  246 ALA B CB  
8437 N N   . PHE B 262 ? 0.6875 0.4002 0.2610 -0.0480 -0.0227 0.0001  247 PHE B N   
8438 C CA  . PHE B 262 ? 0.6425 0.3874 0.2592 -0.0385 -0.0085 -0.0027 247 PHE B CA  
8439 C C   . PHE B 262 ? 0.6831 0.4366 0.3126 -0.0400 -0.0120 -0.0060 247 PHE B C   
8440 O O   . PHE B 262 ? 0.6382 0.4215 0.3062 -0.0329 -0.0169 -0.0045 247 PHE B O   
8441 C CB  . PHE B 262 ? 0.6795 0.4186 0.2913 -0.0378 0.0181  -0.0066 247 PHE B CB  
8442 C CG  . PHE B 262 ? 0.6210 0.3924 0.2769 -0.0273 0.0298  -0.0073 247 PHE B CG  
8443 C CD1 . PHE B 262 ? 0.6392 0.4392 0.3303 -0.0192 0.0184  -0.0046 247 PHE B CD1 
8444 C CD2 . PHE B 262 ? 0.6147 0.3867 0.2764 -0.0256 0.0524  -0.0106 247 PHE B CD2 
8445 C CE1 . PHE B 262 ? 0.5435 0.3677 0.2679 -0.0107 0.0279  -0.0051 247 PHE B CE1 
8446 C CE2 . PHE B 262 ? 0.5654 0.3649 0.2658 -0.0166 0.0599  -0.0104 247 PHE B CE2 
8447 C CZ  . PHE B 262 ? 0.5567 0.3804 0.2854 -0.0095 0.0469  -0.0077 247 PHE B CZ  
8457 N N   . HIS B 263 ? 0.6807 0.4050 0.2750 -0.0502 -0.0094 -0.0107 248 HIS B N   
8458 C CA  . HIS B 263 ? 0.6940 0.4208 0.2954 -0.0540 -0.0138 -0.0139 248 HIS B CA  
8459 C C   . HIS B 263 ? 0.6735 0.4203 0.2988 -0.0547 -0.0396 -0.0086 248 HIS B C   
8460 O O   . HIS B 263 ? 0.6336 0.4040 0.2918 -0.0521 -0.0411 -0.0087 248 HIS B O   
8461 C CB  . HIS B 263 ? 0.7239 0.4083 0.2746 -0.0665 -0.0104 -0.0198 248 HIS B CB  
8462 C CG  . HIS B 263 ? 0.7730 0.4401 0.3072 -0.0648 0.0190  -0.0265 248 HIS B CG  
8463 N ND1 . HIS B 263 ? 0.7617 0.4437 0.3231 -0.0575 0.0359  -0.0304 248 HIS B ND1 
8464 C CD2 . HIS B 263 ? 0.7741 0.4093 0.2679 -0.0693 0.0350  -0.0298 248 HIS B CD2 
8465 C CE1 . HIS B 263 ? 0.7544 0.4172 0.2974 -0.0563 0.0606  -0.0358 248 HIS B CE1 
8466 N NE2 . HIS B 263 ? 0.7970 0.4319 0.2994 -0.0636 0.0620  -0.0358 248 HIS B NE2 
8474 N N   . ASN B 264 ? 0.6848 0.4222 0.2951 -0.0583 -0.0601 -0.0035 249 ASN B N   
8475 C CA  . ASN B 264 ? 0.6688 0.4283 0.3081 -0.0577 -0.0850 0.0023  249 ASN B CA  
8476 C C   . ASN B 264 ? 0.6380 0.4377 0.3284 -0.0432 -0.0812 0.0058  249 ASN B C   
8477 O O   . ASN B 264 ? 0.6257 0.4528 0.3533 -0.0406 -0.0908 0.0084  249 ASN B O   
8478 C CB  . ASN B 264 ? 0.7073 0.4450 0.3182 -0.0636 -0.1091 0.0078  249 ASN B CB  
8479 C CG  . ASN B 264 ? 0.7875 0.5506 0.4345 -0.0616 -0.1361 0.0146  249 ASN B CG  
8480 O OD1 . ASN B 264 ? 0.7329 0.5216 0.4142 -0.0496 -0.1404 0.0196  249 ASN B OD1 
8481 N ND2 . ASN B 264 ? 0.7717 0.5273 0.4124 -0.0736 -0.1542 0.0147  249 ASN B ND2 
8488 N N   . PHE B 265 ? 0.6326 0.4354 0.3249 -0.0345 -0.0667 0.0058  250 PHE B N   
8489 C CA  . PHE B 265 ? 0.5969 0.4326 0.3313 -0.0215 -0.0612 0.0079  250 PHE B CA  
8490 C C   . PHE B 265 ? 0.6125 0.4684 0.3735 -0.0192 -0.0488 0.0046  250 PHE B C   
8491 O O   . PHE B 265 ? 0.5561 0.4387 0.3522 -0.0137 -0.0528 0.0069  250 PHE B O   
8492 C CB  . PHE B 265 ? 0.6440 0.4744 0.3705 -0.0153 -0.0481 0.0079  250 PHE B CB  
8493 C CG  . PHE B 265 ? 0.5427 0.4000 0.3043 -0.0027 -0.0445 0.0097  250 PHE B CG  
8494 C CD1 . PHE B 265 ? 0.5539 0.4176 0.3267 0.0042  -0.0580 0.0145  250 PHE B CD1 
8495 C CD2 . PHE B 265 ? 0.5212 0.3939 0.3018 0.0024  -0.0281 0.0067  250 PHE B CD2 
8496 C CE1 . PHE B 265 ? 0.5138 0.3973 0.3139 0.0158  -0.0532 0.0152  250 PHE B CE1 
8497 C CE2 . PHE B 265 ? 0.5134 0.4055 0.3194 0.0129  -0.0252 0.0081  250 PHE B CE2 
8498 C CZ  . PHE B 265 ? 0.4712 0.3679 0.2857 0.0195  -0.0369 0.0118  250 PHE B CZ  
8508 N N   . ILE B 266 ? 0.6597 0.5013 0.4036 -0.0234 -0.0330 -0.0006 251 ILE B N   
8509 C CA  . ILE B 266 ? 0.5236 0.3788 0.2879 -0.0216 -0.0217 -0.0033 251 ILE B CA  
8510 C C   . ILE B 266 ? 0.5273 0.3909 0.3049 -0.0284 -0.0348 -0.0020 251 ILE B C   
8511 O O   . ILE B 266 ? 0.5533 0.4420 0.3637 -0.0241 -0.0336 -0.0001 251 ILE B O   
8512 C CB  . ILE B 266 ? 0.6215 0.4549 0.3624 -0.0249 -0.0041 -0.0089 251 ILE B CB  
8513 C CG1 . ILE B 266 ? 0.5862 0.4173 0.3229 -0.0184 0.0098  -0.0094 251 ILE B CG1 
8514 C CG2 . ILE B 266 ? 0.5328 0.3754 0.2916 -0.0233 0.0053  -0.0110 251 ILE B CG2 
8515 C CD1 . ILE B 266 ? 0.5041 0.3619 0.2739 -0.0073 0.0153  -0.0069 251 ILE B CD1 
8527 N N   . LYS B 267 ? 0.5611 0.4025 0.3121 -0.0402 -0.0476 -0.0030 252 LYS B N   
8528 C CA  . LYS B 267 ? 0.5693 0.4169 0.3324 -0.0495 -0.0621 -0.0018 252 LYS B CA  
8529 C C   . LYS B 267 ? 0.5830 0.4650 0.3890 -0.0438 -0.0751 0.0046  252 LYS B C   
8530 O O   . LYS B 267 ? 0.6005 0.5036 0.4369 -0.0461 -0.0763 0.0060  252 LYS B O   
8531 C CB  . LYS B 267 ? 0.6502 0.4649 0.3730 -0.0635 -0.0779 -0.0032 252 LYS B CB  
8532 C CG  . LYS B 267 ? 0.7054 0.5228 0.4374 -0.0762 -0.0966 -0.0018 252 LYS B CG  
8533 C CD  . LYS B 267 ? 0.8310 0.6051 0.5103 -0.0915 -0.1082 -0.0054 252 LYS B CD  
8534 C CE  . LYS B 267 ? 0.9604 0.7350 0.6470 -0.1064 -0.1323 -0.0034 252 LYS B CE  
8535 N NZ  . LYS B 267 ? 0.9838 0.7749 0.6899 -0.1072 -0.1606 0.0047  252 LYS B NZ  
8549 N N   . VAL B 268 ? 0.5431 0.4303 0.3526 -0.0364 -0.0836 0.0085  253 VAL B N   
8550 C CA  . VAL B 268 ? 0.5396 0.4570 0.3898 -0.0296 -0.0962 0.0144  253 VAL B CA  
8551 C C   . VAL B 268 ? 0.5132 0.4587 0.3980 -0.0173 -0.0787 0.0144  253 VAL B C   
8552 O O   . VAL B 268 ? 0.4904 0.4634 0.4135 -0.0149 -0.0806 0.0172  253 VAL B O   
8553 C CB  . VAL B 268 ? 0.6608 0.5687 0.4991 -0.0252 -0.1118 0.0186  253 VAL B CB  
8554 C CG1 . VAL B 268 ? 0.6912 0.6301 0.5733 -0.0127 -0.1184 0.0239  253 VAL B CG1 
8555 C CG2 . VAL B 268 ? 0.6470 0.5310 0.4570 -0.0388 -0.1350 0.0204  253 VAL B CG2 
8565 N N   . THR B 269 ? 0.5324 0.4707 0.4042 -0.0099 -0.0613 0.0114  254 THR B N   
8566 C CA  . THR B 269 ? 0.4489 0.4084 0.3464 0.0008  -0.0463 0.0114  254 THR B CA  
8567 C C   . THR B 269 ? 0.5526 0.5206 0.4625 -0.0039 -0.0358 0.0098  254 THR B C   
8568 O O   . THR B 269 ? 0.4582 0.4479 0.3959 0.0015  -0.0286 0.0115  254 THR B O   
8569 C CB  . THR B 269 ? 0.4510 0.3993 0.3309 0.0080  -0.0336 0.0091  254 THR B CB  
8570 O OG1 . THR B 269 ? 0.5016 0.4275 0.3527 0.0009  -0.0264 0.0053  254 THR B OG1 
8571 C CG2 . THR B 269 ? 0.5039 0.4462 0.3764 0.0138  -0.0425 0.0115  254 THR B CG2 
8579 N N   . LEU B 270 ? 0.4826 0.4311 0.3698 -0.0141 -0.0338 0.0066  255 LEU B N   
8580 C CA  . LEU B 270 ? 0.4816 0.4321 0.3756 -0.0195 -0.0244 0.0053  255 LEU B CA  
8581 C C   . LEU B 270 ? 0.4651 0.4229 0.3735 -0.0314 -0.0373 0.0072  255 LEU B C   
8582 O O   . LEU B 270 ? 0.4823 0.4243 0.3765 -0.0426 -0.0376 0.0048  255 LEU B O   
8583 C CB  . LEU B 270 ? 0.5154 0.4391 0.3785 -0.0227 -0.0140 0.0004  255 LEU B CB  
8584 C CG  . LEU B 270 ? 0.4722 0.3914 0.3265 -0.0121 -0.0016 -0.0010 255 LEU B CG  
8585 C CD1 . LEU B 270 ? 0.5350 0.4323 0.3681 -0.0141 0.0105  -0.0054 255 LEU B CD1 
8586 C CD2 . LEU B 270 ? 0.4508 0.3914 0.3294 -0.0019 0.0060  0.0017  255 LEU B CD2 
8598 N N   . THR B 271 ? 0.4904 0.4720 0.4287 -0.0291 -0.0486 0.0118  256 THR B N   
8599 C CA  . THR B 271 ? 0.4898 0.4861 0.4531 -0.0401 -0.0615 0.0149  256 THR B CA  
8600 C C   . THR B 271 ? 0.4693 0.4849 0.4600 -0.0411 -0.0467 0.0162  256 THR B C   
8601 O O   . THR B 271 ? 0.4499 0.4837 0.4604 -0.0295 -0.0333 0.0177  256 THR B O   
8602 C CB  . THR B 271 ? 0.4840 0.5015 0.4754 -0.0355 -0.0786 0.0200  256 THR B CB  
8603 O OG1 . THR B 271 ? 0.5149 0.5092 0.4753 -0.0378 -0.0952 0.0197  256 THR B OG1 
8604 C CG2 . THR B 271 ? 0.5278 0.5692 0.5575 -0.0459 -0.0907 0.0243  256 THR B CG2 
8612 N N   . LYS B 272 ? 0.5408 0.5491 0.5294 -0.0558 -0.0489 0.0157  257 LYS B N   
8613 C CA  . LYS B 272 ? 0.5088 0.5286 0.5161 -0.0589 -0.0335 0.0171  257 LYS B CA  
8614 C C   . LYS B 272 ? 0.4412 0.4991 0.4968 -0.0544 -0.0304 0.0224  257 LYS B C   
8615 O O   . LYS B 272 ? 0.5114 0.5804 0.5779 -0.0455 -0.0118 0.0233  257 LYS B O   
8616 C CB  . LYS B 272 ? 0.5887 0.5924 0.5859 -0.0774 -0.0396 0.0160  257 LYS B CB  
8617 C CG  . LYS B 272 ? 0.7456 0.7132 0.7008 -0.0791 -0.0294 0.0107  257 LYS B CG  
8618 C CD  . LYS B 272 ? 0.7879 0.7345 0.7296 -0.0978 -0.0360 0.0090  257 LYS B CD  
8619 C CE  . LYS B 272 ? 0.7181 0.6856 0.6936 -0.1074 -0.0315 0.0139  257 LYS B CE  
8620 N NZ  . LYS B 272 ? 0.8415 0.7828 0.7990 -0.1256 -0.0355 0.0119  257 LYS B NZ  
8634 N N   . SER B 273 ? 0.5014 0.5787 0.5863 -0.0604 -0.0483 0.0260  258 SER B N   
8635 C CA  . SER B 273 ? 0.4330 0.5494 0.5707 -0.0564 -0.0443 0.0312  258 SER B CA  
8636 C C   . SER B 273 ? 0.5533 0.6818 0.7006 -0.0362 -0.0389 0.0315  258 SER B C   
8637 O O   . SER B 273 ? 0.5571 0.6762 0.6906 -0.0305 -0.0541 0.0309  258 SER B O   
8638 C CB  . SER B 273 ? 0.5629 0.6984 0.7344 -0.0690 -0.0677 0.0357  258 SER B CB  
8639 O OG  . SER B 273 ? 0.5568 0.7338 0.7861 -0.0633 -0.0627 0.0409  258 SER B OG  
8645 N N   . PRO B 274 ? 0.5397 0.6852 0.7066 -0.0258 -0.0175 0.0322  259 PRO B N   
8646 C CA  . PRO B 274 ? 0.4528 0.6078 0.6290 -0.0068 -0.0130 0.0321  259 PRO B CA  
8647 C C   . PRO B 274 ? 0.5054 0.6859 0.7227 -0.0028 -0.0305 0.0364  259 PRO B C   
8648 O O   . PRO B 274 ? 0.5645 0.7423 0.7785 0.0109  -0.0369 0.0361  259 PRO B O   
8649 C CB  . PRO B 274 ? 0.5758 0.7424 0.7646 0.0002  0.0144  0.0320  259 PRO B CB  
8650 C CG  . PRO B 274 ? 0.4627 0.6186 0.6376 -0.0140 0.0241  0.0320  259 PRO B CG  
8651 C CD  . PRO B 274 ? 0.4350 0.5890 0.6140 -0.0311 0.0037  0.0334  259 PRO B CD  
8659 N N   . LYS B 275 ? 0.5058 0.7107 0.7630 -0.0146 -0.0396 0.0408  260 LYS B N   
8660 C CA  . LYS B 275 ? 0.5427 0.7747 0.8452 -0.0113 -0.0593 0.0461  260 LYS B CA  
8661 C C   . LYS B 275 ? 0.5055 0.7165 0.7819 -0.0147 -0.0898 0.0467  260 LYS B C   
8662 O O   . LYS B 275 ? 0.5882 0.8168 0.8968 -0.0106 -0.1103 0.0517  260 LYS B O   
8663 C CB  . LYS B 275 ? 0.6261 0.8903 0.9802 -0.0257 -0.0627 0.0512  260 LYS B CB  
8664 C CG  . LYS B 275 ? 0.6502 0.9434 1.0439 -0.0203 -0.0326 0.0524  260 LYS B CG  
8665 C CD  . LYS B 275 ? 0.6146 0.9449 1.0683 -0.0348 -0.0367 0.0586  260 LYS B CD  
8666 C CE  . LYS B 275 ? 0.5973 0.9586 1.1044 -0.0306 -0.0628 0.0646  260 LYS B CE  
8667 N NZ  . LYS B 275 ? 0.5757 0.9764 1.1469 -0.0463 -0.0685 0.0712  260 LYS B NZ  
8681 N N   . LYS B 276 ? 0.4784 0.6514 0.6976 -0.0221 -0.0931 0.0421  261 LYS B N   
8682 C CA  . LYS B 276 ? 0.5323 0.6787 0.7167 -0.0256 -0.1179 0.0421  261 LYS B CA  
8683 C C   . LYS B 276 ? 0.5439 0.6590 0.6786 -0.0154 -0.1086 0.0372  261 LYS B C   
8684 O O   . LYS B 276 ? 0.5409 0.6307 0.6419 -0.0174 -0.1254 0.0370  261 LYS B O   
8685 C CB  . LYS B 276 ? 0.5937 0.7203 0.7540 -0.0476 -0.1332 0.0411  261 LYS B CB  
8686 C CG  . LYS B 276 ? 0.5564 0.7119 0.7653 -0.0608 -0.1498 0.0468  261 LYS B CG  
8687 C CD  . LYS B 276 ? 0.7218 0.8531 0.9020 -0.0840 -0.1624 0.0447  261 LYS B CD  
8688 C CE  . LYS B 276 ? 0.6585 0.8136 0.8819 -0.0989 -0.1894 0.0513  261 LYS B CE  
8689 N NZ  . LYS B 276 ? 0.8198 0.9756 1.0485 -0.0944 -0.2203 0.0563  261 LYS B NZ  
8703 N N   . ARG B 277 ? 0.4635 0.5786 0.5920 -0.0057 -0.0827 0.0336  262 ARG B N   
8704 C CA  . ARG B 277 ? 0.5354 0.6243 0.6227 0.0034  -0.0744 0.0296  262 ARG B CA  
8705 C C   . ARG B 277 ? 0.4544 0.5491 0.5531 0.0192  -0.0806 0.0319  262 ARG B C   
8706 O O   . ARG B 277 ? 0.4105 0.5314 0.5487 0.0299  -0.0739 0.0341  262 ARG B O   
8707 C CB  . ARG B 277 ? 0.5162 0.6023 0.5936 0.0076  -0.0481 0.0257  262 ARG B CB  
8708 C CG  . ARG B 277 ? 0.5345 0.5922 0.5685 0.0120  -0.0411 0.0214  262 ARG B CG  
8709 C CD  . ARG B 277 ? 0.4765 0.5308 0.5014 0.0152  -0.0189 0.0186  262 ARG B CD  
8710 N NE  . ARG B 277 ? 0.4224 0.4785 0.4512 0.0035  -0.0129 0.0186  262 ARG B NE  
8711 C CZ  . ARG B 277 ? 0.3909 0.4604 0.4374 0.0040  0.0023  0.0197  262 ARG B CZ  
8712 N NH1 . ARG B 277 ? 0.4057 0.4868 0.4647 0.0159  0.0150  0.0201  262 ARG B NH1 
8713 N NH2 . ARG B 277 ? 0.4149 0.4827 0.4629 -0.0084 0.0056  0.0203  262 ARG B NH2 
8727 N N   . PRO B 278 ? 0.4727 0.5418 0.5370 0.0209  -0.0922 0.0315  263 PRO B N   
8728 C CA  . PRO B 278 ? 0.4375 0.5084 0.5110 0.0352  -0.1006 0.0345  263 PRO B CA  
8729 C C   . PRO B 278 ? 0.4291 0.5026 0.5049 0.0505  -0.0795 0.0315  263 PRO B C   
8730 O O   . PRO B 278 ? 0.4507 0.5128 0.5032 0.0496  -0.0620 0.0269  263 PRO B O   
8731 C CB  . PRO B 278 ? 0.4600 0.4964 0.4867 0.0297  -0.1156 0.0346  263 PRO B CB  
8732 C CG  . PRO B 278 ? 0.5372 0.5587 0.5391 0.0121  -0.1198 0.0325  263 PRO B CG  
8733 C CD  . PRO B 278 ? 0.4900 0.5261 0.5063 0.0091  -0.0991 0.0289  263 PRO B CD  
8741 N N   . SER B 279 ? 0.5053 0.5920 0.6086 0.0650  -0.0828 0.0343  264 SER B N   
8742 C CA  . SER B 279 ? 0.4616 0.5458 0.5637 0.0803  -0.0653 0.0312  264 SER B CA  
8743 C C   . SER B 279 ? 0.5672 0.6181 0.6222 0.0810  -0.0661 0.0286  264 SER B C   
8744 O O   . SER B 279 ? 0.5747 0.6055 0.6012 0.0718  -0.0803 0.0300  264 SER B O   
8745 C CB  . SER B 279 ? 0.4211 0.5231 0.5622 0.0963  -0.0703 0.0347  264 SER B CB  
8746 O OG  . SER B 279 ? 0.4586 0.5443 0.5876 0.0989  -0.0935 0.0389  264 SER B OG  
8752 N N   . ALA B 280 ? 0.4629 0.5064 0.5088 0.0914  -0.0503 0.0250  265 ALA B N   
8753 C CA  . ALA B 280 ? 0.4994 0.5134 0.5055 0.0917  -0.0509 0.0229  265 ALA B CA  
8754 C C   . ALA B 280 ? 0.5297 0.5290 0.5284 0.0962  -0.0701 0.0272  265 ALA B C   
8755 O O   . ALA B 280 ? 0.4933 0.4680 0.4577 0.0887  -0.0781 0.0279  265 ALA B O   
8756 C CB  . ALA B 280 ? 0.4692 0.4776 0.4684 0.1014  -0.0330 0.0185  265 ALA B CB  
8762 N N   . THR B 281 ? 0.5963 0.6095 0.6273 0.1087  -0.0771 0.0305  266 THR B N   
8763 C CA  . THR B 281 ? 0.5926 0.5903 0.6176 0.1145  -0.0973 0.0356  266 THR B CA  
8764 C C   . THR B 281 ? 0.5391 0.5292 0.5507 0.1007  -0.1192 0.0405  266 THR B C   
8765 O O   . THR B 281 ? 0.6665 0.6279 0.6436 0.0967  -0.1321 0.0432  266 THR B O   
8766 C CB  . THR B 281 ? 0.5730 0.5905 0.6423 0.1321  -0.1004 0.0384  266 THR B CB  
8767 O OG1 . THR B 281 ? 0.4833 0.4981 0.5542 0.1453  -0.0796 0.0331  266 THR B OG1 
8768 C CG2 . THR B 281 ? 0.6091 0.6105 0.6745 0.1381  -0.1250 0.0452  266 THR B CG2 
8776 N N   . LYS B 282 ? 0.5218 0.5345 0.5571 0.0922  -0.1235 0.0417  267 LYS B N   
8777 C CA  . LYS B 282 ? 0.5957 0.5978 0.6143 0.0777  -0.1451 0.0457  267 LYS B CA  
8778 C C   . LYS B 282 ? 0.5938 0.5647 0.5587 0.0639  -0.1398 0.0421  267 LYS B C   
8779 O O   . LYS B 282 ? 0.6845 0.6304 0.6170 0.0547  -0.1565 0.0452  267 LYS B O   
8780 C CB  . LYS B 282 ? 0.6897 0.7212 0.7438 0.0696  -0.1489 0.0469  267 LYS B CB  
8781 C CG  . LYS B 282 ? 0.7820 0.8010 0.8179 0.0531  -0.1731 0.0506  267 LYS B CG  
8782 C CD  . LYS B 282 ? 0.8863 0.8873 0.9112 0.0569  -0.2007 0.0578  267 LYS B CD  
8783 C CE  . LYS B 282 ? 0.8700 0.8631 0.8852 0.0411  -0.2287 0.0626  267 LYS B CE  
8784 N NZ  . LYS B 282 ? 0.9528 0.9858 1.0282 0.0411  -0.2401 0.0666  267 LYS B NZ  
8798 N N   . MET B 283 ? 0.5475 0.5185 0.5021 0.0624  -0.1166 0.0359  268 MET B N   
8799 C CA  . MET B 283 ? 0.5091 0.4546 0.4202 0.0504  -0.1094 0.0324  268 MET B CA  
8800 C C   . MET B 283 ? 0.6315 0.5484 0.5094 0.0528  -0.1112 0.0335  268 MET B C   
8801 O O   . MET B 283 ? 0.6062 0.4979 0.4463 0.0418  -0.1116 0.0329  268 MET B O   
8802 C CB  . MET B 283 ? 0.6145 0.5702 0.5291 0.0491  -0.0863 0.0265  268 MET B CB  
8803 C CG  . MET B 283 ? 0.5627 0.5381 0.4982 0.0418  -0.0832 0.0253  268 MET B CG  
8804 S SD  . MET B 283 ? 0.5691 0.5260 0.4771 0.0237  -0.0975 0.0258  268 MET B SD  
8805 C CE  . MET B 283 ? 0.5369 0.4610 0.3961 0.0182  -0.0851 0.0217  268 MET B CE  
8815 N N   . LEU B 284 ? 0.5658 0.4840 0.4559 0.0665  -0.1109 0.0348  269 LEU B N   
8816 C CA  . LEU B 284 ? 0.5707 0.4595 0.4294 0.0678  -0.1147 0.0367  269 LEU B CA  
8817 C C   . LEU B 284 ? 0.5997 0.4659 0.4354 0.0621  -0.1374 0.0432  269 LEU B C   
8818 O O   . LEU B 284 ? 0.6347 0.4709 0.4356 0.0588  -0.1402 0.0453  269 LEU B O   
8819 C CB  . LEU B 284 ? 0.5920 0.4840 0.4681 0.0842  -0.1107 0.0364  269 LEU B CB  
8820 C CG  . LEU B 284 ? 0.5396 0.4397 0.4199 0.0873  -0.0885 0.0299  269 LEU B CG  
8821 C CD1 . LEU B 284 ? 0.5072 0.4146 0.4098 0.1042  -0.0836 0.0286  269 LEU B CD1 
8822 C CD2 . LEU B 284 ? 0.5246 0.4003 0.3688 0.0782  -0.0811 0.0279  269 LEU B CD2 
8834 N N   . SER B 285 ? 0.5875 0.4660 0.4407 0.0597  -0.1543 0.0468  270 SER B N   
8835 C CA  . SER B 285 ? 0.6091 0.4632 0.4349 0.0515  -0.1783 0.0532  270 SER B CA  
8836 C C   . SER B 285 ? 0.6254 0.4569 0.4080 0.0329  -0.1748 0.0505  270 SER B C   
8837 O O   . SER B 285 ? 0.6929 0.4944 0.4384 0.0239  -0.1915 0.0550  270 SER B O   
8838 C CB  . SER B 285 ? 0.6502 0.5270 0.5139 0.0552  -0.2005 0.0585  270 SER B CB  
8839 O OG  . SER B 285 ? 0.8436 0.7463 0.7544 0.0737  -0.1993 0.0600  270 SER B OG  
8845 N N   . HIS B 286 ? 0.6011 0.4435 0.3854 0.0273  -0.1533 0.0434  271 HIS B N   
8846 C CA  . HIS B 286 ? 0.6171 0.4405 0.3662 0.0112  -0.1486 0.0401  271 HIS B CA  
8847 C C   . HIS B 286 ? 0.6453 0.4314 0.3442 0.0037  -0.1416 0.0400  271 HIS B C   
8848 O O   . HIS B 286 ? 0.6359 0.4188 0.3329 0.0093  -0.1288 0.0393  271 HIS B O   
8849 C CB  . HIS B 286 ? 0.6222 0.4664 0.3891 0.0095  -0.1266 0.0329  271 HIS B CB  
8850 C CG  . HIS B 286 ? 0.6258 0.4544 0.3652 -0.0053 -0.1234 0.0291  271 HIS B CG  
8851 N ND1 . HIS B 286 ? 0.6581 0.4586 0.3562 -0.0138 -0.1095 0.0256  271 HIS B ND1 
8852 C CD2 . HIS B 286 ? 0.6431 0.4791 0.3905 -0.0131 -0.1312 0.0280  271 HIS B CD2 
8853 C CE1 . HIS B 286 ? 0.7334 0.5225 0.4130 -0.0251 -0.1082 0.0219  271 HIS B CE1 
8854 N NE2 . HIS B 286 ? 0.6765 0.4855 0.3839 -0.0255 -0.1222 0.0233  271 HIS B NE2 
8862 N N   . GLN B 287 ? 0.7261 0.4827 0.3829 -0.0102 -0.1489 0.0405  272 GLN B N   
8863 C CA  . GLN B 287 ? 0.7332 0.4511 0.3383 -0.0191 -0.1413 0.0410  272 GLN B CA  
8864 C C   . GLN B 287 ? 0.7637 0.4871 0.3716 -0.0179 -0.1119 0.0354  272 GLN B C   
8865 O O   . GLN B 287 ? 0.7585 0.4642 0.3470 -0.0184 -0.1051 0.0375  272 GLN B O   
8866 C CB  . GLN B 287 ? 0.8406 0.5276 0.4000 -0.0352 -0.1466 0.0396  272 GLN B CB  
8867 C CG  . GLN B 287 ? 0.9121 0.5573 0.4143 -0.0463 -0.1332 0.0389  272 GLN B CG  
8868 C CD  . GLN B 287 ? 1.0839 0.6943 0.5360 -0.0621 -0.1371 0.0364  272 GLN B CD  
8869 O OE1 . GLN B 287 ? 1.0600 0.6779 0.5208 -0.0655 -0.1515 0.0351  272 GLN B OE1 
8870 N NE2 . GLN B 287 ? 1.0333 0.6039 0.4313 -0.0726 -0.1235 0.0356  272 GLN B NE2 
8879 N N   . LEU B 288 ? 0.7210 0.4692 0.3547 -0.0164 -0.0954 0.0290  273 LEU B N   
8880 C CA  . LEU B 288 ? 0.6809 0.4336 0.3174 -0.0163 -0.0696 0.0242  273 LEU B CA  
8881 C C   . LEU B 288 ? 0.6342 0.3977 0.2903 -0.0065 -0.0665 0.0264  273 LEU B C   
8882 O O   . LEU B 288 ? 0.6859 0.4377 0.3282 -0.0099 -0.0531 0.0260  273 LEU B O   
8883 C CB  . LEU B 288 ? 0.6157 0.3932 0.2793 -0.0146 -0.0562 0.0182  273 LEU B CB  
8884 C CG  . LEU B 288 ? 0.5991 0.3799 0.2655 -0.0151 -0.0314 0.0137  273 LEU B CG  
8885 C CD1 . LEU B 288 ? 0.6342 0.3849 0.2602 -0.0270 -0.0188 0.0111  273 LEU B CD1 
8886 C CD2 . LEU B 288 ? 0.6680 0.4767 0.3684 -0.0094 -0.0217 0.0096  273 LEU B CD2 
8898 N N   . VAL B 289 ? 0.6067 0.3921 0.2958 0.0052  -0.0776 0.0284  274 VAL B N   
8899 C CA  . VAL B 289 ? 0.6273 0.4201 0.3329 0.0151  -0.0743 0.0294  274 VAL B CA  
8900 C C   . VAL B 289 ? 0.6715 0.4437 0.3622 0.0188  -0.0912 0.0358  274 VAL B C   
8901 O O   . VAL B 289 ? 0.6683 0.4411 0.3686 0.0271  -0.0902 0.0367  274 VAL B O   
8902 C CB  . VAL B 289 ? 0.5582 0.3840 0.3063 0.0269  -0.0715 0.0267  274 VAL B CB  
8903 C CG1 . VAL B 289 ? 0.5665 0.4081 0.3260 0.0237  -0.0537 0.0211  274 VAL B CG1 
8904 C CG2 . VAL B 289 ? 0.5512 0.3910 0.3197 0.0318  -0.0878 0.0293  274 VAL B CG2 
8914 N N   . SER B 290 ? 0.7517 0.5024 0.4163 0.0126  -0.1076 0.0405  275 SER B N   
8915 C CA  . SER B 290 ? 0.7830 0.5104 0.4304 0.0161  -0.1264 0.0478  275 SER B CA  
8916 C C   . SER B 290 ? 0.8685 0.5565 0.4668 0.0042  -0.1223 0.0508  275 SER B C   
8917 O O   . SER B 290 ? 0.8803 0.5459 0.4626 0.0073  -0.1339 0.0569  275 SER B O   
8918 C CB  . SER B 290 ? 0.7515 0.4774 0.4002 0.0166  -0.1517 0.0528  275 SER B CB  
8919 O OG  . SER B 290 ? 0.8732 0.6367 0.5700 0.0262  -0.1547 0.0507  275 SER B OG  
8925 N N   . GLN B 291 ? 0.9128 0.5909 0.4872 -0.0088 -0.1050 0.0468  276 GLN B N   
8926 C CA  . GLN B 291 ? 0.9037 0.5432 0.4292 -0.0218 -0.0988 0.0498  276 GLN B CA  
8927 C C   . GLN B 291 ? 0.8064 0.4386 0.3325 -0.0199 -0.0907 0.0519  276 GLN B C   
8928 O O   . GLN B 291 ? 0.8047 0.4631 0.3669 -0.0113 -0.0824 0.0484  276 GLN B O   
8929 C CB  . GLN B 291 ? 0.8635 0.4984 0.3709 -0.0343 -0.0764 0.0438  276 GLN B CB  
8930 C CG  . GLN B 291 ? 0.7246 0.3927 0.2697 -0.0306 -0.0539 0.0366  276 GLN B CG  
8931 C CD  . GLN B 291 ? 0.8186 0.4828 0.3496 -0.0403 -0.0333 0.0307  276 GLN B CD  
8932 O OE1 . GLN B 291 ? 0.7978 0.4308 0.2875 -0.0521 -0.0236 0.0313  276 GLN B OE1 
8933 N NE2 . GLN B 291 ? 0.6947 0.3883 0.2586 -0.0351 -0.0255 0.0249  276 GLN B NE2 
8942 N N   . PRO B 292 ? 0.8250 0.4187 0.3087 -0.0286 -0.0937 0.0579  277 PRO B N   
8943 C CA  . PRO B 292 ? 0.8146 0.3978 0.2952 -0.0305 -0.0838 0.0597  277 PRO B CA  
8944 C C   . PRO B 292 ? 0.8836 0.4808 0.3740 -0.0394 -0.0553 0.0538  277 PRO B C   
8945 O O   . PRO B 292 ? 0.9697 0.5805 0.4651 -0.0436 -0.0421 0.0485  277 PRO B O   
8946 C CB  . PRO B 292 ? 0.9326 0.4673 0.3593 -0.0404 -0.0937 0.0682  277 PRO B CB  
8947 C CG  . PRO B 292 ? 0.9476 0.4659 0.3414 -0.0494 -0.0977 0.0684  277 PRO B CG  
8948 C CD  . PRO B 292 ? 0.9150 0.4695 0.3480 -0.0386 -0.1073 0.0637  277 PRO B CD  
8956 N N   . GLY B 293 ? 0.8711 0.4646 0.3662 -0.0421 -0.0465 0.0550  278 GLY B N   
8957 C CA  . GLY B 293 ? 0.8629 0.4695 0.3707 -0.0512 -0.0215 0.0510  278 GLY B CA  
8958 C C   . GLY B 293 ? 0.7650 0.4136 0.3222 -0.0424 -0.0141 0.0443  278 GLY B C   
8959 O O   . GLY B 293 ? 0.8604 0.5225 0.4344 -0.0488 0.0038  0.0418  278 GLY B O   
8963 N N   . LEU B 294 ? 0.8211 0.4909 0.4030 -0.0284 -0.0271 0.0418  279 LEU B N   
8964 C CA  . LEU B 294 ? 0.6970 0.4025 0.3207 -0.0202 -0.0208 0.0361  279 LEU B CA  
8965 C C   . LEU B 294 ? 0.7245 0.4308 0.3613 -0.0154 -0.0254 0.0368  279 LEU B C   
8966 O O   . LEU B 294 ? 0.8062 0.5028 0.4400 -0.0060 -0.0407 0.0390  279 LEU B O   
8967 C CB  . LEU B 294 ? 0.6829 0.4085 0.3252 -0.0087 -0.0306 0.0334  279 LEU B CB  
8968 C CG  . LEU B 294 ? 0.6937 0.4173 0.3225 -0.0141 -0.0282 0.0320  279 LEU B CG  
8969 C CD1 . LEU B 294 ? 0.6590 0.4043 0.3107 -0.0039 -0.0388 0.0299  279 LEU B CD1 
8970 C CD2 . LEU B 294 ? 0.6802 0.4115 0.3123 -0.0225 -0.0060 0.0278  279 LEU B CD2 
8982 N N   . ASN B 295 ? 0.7027 0.4195 0.3547 -0.0217 -0.0127 0.0349  280 ASN B N   
8983 C CA  . ASN B 295 ? 0.6829 0.3975 0.3443 -0.0196 -0.0175 0.0350  280 ASN B CA  
8984 C C   . ASN B 295 ? 0.6061 0.3458 0.2967 -0.0235 -0.0062 0.0314  280 ASN B C   
8985 O O   . ASN B 295 ? 0.5983 0.3550 0.3017 -0.0281 0.0068  0.0296  280 ASN B O   
8986 C CB  . ASN B 295 ? 0.6709 0.3517 0.3032 -0.0297 -0.0201 0.0407  280 ASN B CB  
8987 C CG  . ASN B 295 ? 0.6875 0.3617 0.3090 -0.0470 -0.0032 0.0429  280 ASN B CG  
8988 O OD1 . ASN B 295 ? 0.6999 0.3914 0.3439 -0.0543 0.0089  0.0412  280 ASN B OD1 
8989 N ND2 . ASN B 295 ? 0.7612 0.4099 0.3484 -0.0536 -0.0021 0.0470  280 ASN B ND2 
8996 N N   . ARG B 296 ? 0.6100 0.3493 0.3100 -0.0216 -0.0121 0.0305  281 ARG B N   
8997 C CA  . ARG B 296 ? 0.5806 0.3427 0.3086 -0.0246 -0.0065 0.0277  281 ARG B CA  
8998 C C   . ARG B 296 ? 0.5868 0.3537 0.3232 -0.0403 0.0072  0.0301  281 ARG B C   
8999 O O   . ARG B 296 ? 0.5665 0.3576 0.3319 -0.0425 0.0132  0.0285  281 ARG B O   
9000 C CB  . ARG B 296 ? 0.5853 0.3386 0.3138 -0.0213 -0.0176 0.0264  281 ARG B CB  
9001 C CG  . ARG B 296 ? 0.6439 0.3679 0.3521 -0.0322 -0.0216 0.0302  281 ARG B CG  
9002 C CD  . ARG B 296 ? 0.6291 0.3376 0.3306 -0.0267 -0.0340 0.0278  281 ARG B CD  
9003 N NE  . ARG B 296 ? 0.7329 0.4099 0.4131 -0.0375 -0.0387 0.0314  281 ARG B NE  
9004 C CZ  . ARG B 296 ? 0.6733 0.3485 0.3607 -0.0529 -0.0378 0.0328  281 ARG B CZ  
9005 N NH1 . ARG B 296 ? 0.6500 0.3544 0.3674 -0.0587 -0.0333 0.0313  281 ARG B NH1 
9006 N NH2 . ARG B 296 ? 0.7288 0.3719 0.3939 -0.0632 -0.0424 0.0363  281 ARG B NH2 
9020 N N   . GLY B 297 ? 0.6167 0.3608 0.3293 -0.0512 0.0126  0.0344  282 GLY B N   
9021 C CA  . GLY B 297 ? 0.6246 0.3746 0.3466 -0.0661 0.0299  0.0366  282 GLY B CA  
9022 C C   . GLY B 297 ? 0.6040 0.3789 0.3459 -0.0637 0.0447  0.0335  282 GLY B C   
9023 O O   . GLY B 297 ? 0.5974 0.3907 0.3655 -0.0713 0.0588  0.0337  282 GLY B O   
9027 N N   . LEU B 298 ? 0.6412 0.4170 0.3729 -0.0529 0.0415  0.0308  283 LEU B N   
9028 C CA  . LEU B 298 ? 0.5787 0.3741 0.3260 -0.0499 0.0546  0.0272  283 LEU B CA  
9029 C C   . LEU B 298 ? 0.5584 0.3856 0.3474 -0.0446 0.0552  0.0247  283 LEU B C   
9030 O O   . LEU B 298 ? 0.5691 0.4140 0.3811 -0.0467 0.0700  0.0235  283 LEU B O   
9031 C CB  . LEU B 298 ? 0.5769 0.3660 0.3057 -0.0404 0.0473  0.0250  283 LEU B CB  
9032 C CG  . LEU B 298 ? 0.6134 0.3702 0.2995 -0.0460 0.0454  0.0279  283 LEU B CG  
9033 C CD1 . LEU B 298 ? 0.6554 0.4097 0.3296 -0.0368 0.0338  0.0262  283 LEU B CD1 
9034 C CD2 . LEU B 298 ? 0.6779 0.4235 0.3492 -0.0585 0.0666  0.0284  283 LEU B CD2 
9046 N N   . ILE B 299 ? 0.5547 0.3873 0.3524 -0.0372 0.0392  0.0240  284 ILE B N   
9047 C CA  . ILE B 299 ? 0.5057 0.3638 0.3370 -0.0327 0.0366  0.0224  284 ILE B CA  
9048 C C   . ILE B 299 ? 0.5661 0.4311 0.4185 -0.0438 0.0376  0.0253  284 ILE B C   
9049 O O   . ILE B 299 ? 0.4945 0.3833 0.3804 -0.0438 0.0403  0.0253  284 ILE B O   
9050 C CB  . ILE B 299 ? 0.5994 0.4573 0.4268 -0.0210 0.0206  0.0201  284 ILE B CB  
9051 C CG1 . ILE B 299 ? 0.6053 0.4616 0.4198 -0.0111 0.0203  0.0177  284 ILE B CG1 
9052 C CG2 . ILE B 299 ? 0.4740 0.3527 0.3293 -0.0174 0.0163  0.0191  284 ILE B CG2 
9053 C CD1 . ILE B 299 ? 0.5817 0.4535 0.4096 -0.0096 0.0323  0.0159  284 ILE B CD1 
9065 N N   . LEU B 300 ? 0.5343 0.3790 0.3695 -0.0537 0.0343  0.0283  285 LEU B N   
9066 C CA  . LEU B 300 ? 0.5420 0.3941 0.3994 -0.0674 0.0374  0.0317  285 LEU B CA  
9067 C C   . LEU B 300 ? 0.5391 0.4107 0.4223 -0.0737 0.0588  0.0328  285 LEU B C   
9068 O O   . LEU B 300 ? 0.5834 0.4786 0.5055 -0.0792 0.0620  0.0346  285 LEU B O   
9069 C CB  . LEU B 300 ? 0.5755 0.3981 0.4057 -0.0787 0.0333  0.0352  285 LEU B CB  
9070 C CG  . LEU B 300 ? 0.5840 0.3840 0.3914 -0.0744 0.0132  0.0343  285 LEU B CG  
9071 C CD1 . LEU B 300 ? 0.7039 0.4743 0.4880 -0.0883 0.0120  0.0387  285 LEU B CD1 
9072 C CD2 . LEU B 300 ? 0.5906 0.4048 0.4202 -0.0719 -0.0001 0.0323  285 LEU B CD2 
9084 N N   . ASP B 301 ? 0.5497 0.4106 0.4116 -0.0728 0.0735  0.0318  286 ASP B N   
9085 C CA  . ASP B 301 ? 0.5820 0.4573 0.4634 -0.0768 0.0972  0.0315  286 ASP B CA  
9086 C C   . ASP B 301 ? 0.6020 0.5081 0.5216 -0.0657 0.0984  0.0287  286 ASP B C   
9087 O O   . ASP B 301 ? 0.5529 0.4816 0.5101 -0.0686 0.1128  0.0296  286 ASP B O   
9088 C CB  . ASP B 301 ? 0.6512 0.5014 0.4916 -0.0772 0.1095  0.0300  286 ASP B CB  
9089 C CG  . ASP B 301 ? 0.6899 0.5428 0.5373 -0.0853 0.1379  0.0300  286 ASP B CG  
9090 O OD1 . ASP B 301 ? 0.8144 0.6713 0.6778 -0.0983 0.1494  0.0338  286 ASP B OD1 
9091 O OD2 . ASP B 301 ? 0.7191 0.5679 0.5541 -0.0794 0.1495  0.0260  286 ASP B OD2 
9096 N N   . LEU B 302 ? 0.5027 0.4099 0.4149 -0.0527 0.0839  0.0256  287 LEU B N   
9097 C CA  . LEU B 302 ? 0.5405 0.4726 0.4845 -0.0422 0.0831  0.0237  287 LEU B CA  
9098 C C   . LEU B 302 ? 0.4824 0.4360 0.4645 -0.0444 0.0716  0.0268  287 LEU B C   
9099 O O   . LEU B 302 ? 0.4535 0.4316 0.4747 -0.0416 0.0775  0.0277  287 LEU B O   
9100 C CB  . LEU B 302 ? 0.4657 0.3909 0.3888 -0.0297 0.0711  0.0203  287 LEU B CB  
9101 C CG  . LEU B 302 ? 0.4983 0.4413 0.4425 -0.0184 0.0716  0.0181  287 LEU B CG  
9102 C CD1 . LEU B 302 ? 0.5182 0.4650 0.4698 -0.0172 0.0930  0.0158  287 LEU B CD1 
9103 C CD2 . LEU B 302 ? 0.5153 0.4492 0.4367 -0.0091 0.0590  0.0156  287 LEU B CD2 
9115 N N   . LEU B 303 ? 0.5121 0.4551 0.4832 -0.0497 0.0544  0.0286  288 LEU B N   
9116 C CA  . LEU B 303 ? 0.5116 0.4703 0.5132 -0.0537 0.0400  0.0315  288 LEU B CA  
9117 C C   . LEU B 303 ? 0.5385 0.5148 0.5772 -0.0670 0.0509  0.0358  288 LEU B C   
9118 O O   . LEU B 303 ? 0.4747 0.4755 0.5551 -0.0684 0.0438  0.0387  288 LEU B O   
9119 C CB  . LEU B 303 ? 0.4778 0.4146 0.4519 -0.0567 0.0199  0.0314  288 LEU B CB  
9120 C CG  . LEU B 303 ? 0.5166 0.4372 0.4581 -0.0437 0.0091  0.0273  288 LEU B CG  
9121 C CD1 . LEU B 303 ? 0.4896 0.3882 0.4078 -0.0469 -0.0085 0.0269  288 LEU B CD1 
9122 C CD2 . LEU B 303 ? 0.4524 0.3907 0.4107 -0.0319 0.0050  0.0259  288 LEU B CD2 
9134 N N   . ASP B 304 ? 0.5748 0.5385 0.5993 -0.0775 0.0674  0.0369  289 ASP B N   
9135 C CA  . ASP B 304 ? 0.5663 0.5480 0.6280 -0.0905 0.0828  0.0411  289 ASP B CA  
9136 C C   . ASP B 304 ? 0.5461 0.5571 0.6494 -0.0827 0.1003  0.0404  289 ASP B C   
9137 O O   . ASP B 304 ? 0.7004 0.7407 0.8559 -0.0873 0.1029  0.0442  289 ASP B O   
9138 C CB  . ASP B 304 ? 0.5799 0.5371 0.6104 -0.1030 0.0999  0.0424  289 ASP B CB  
9139 C CG  . ASP B 304 ? 0.6924 0.6682 0.7606 -0.1167 0.1218  0.0464  289 ASP B CG  
9140 O OD1 . ASP B 304 ? 0.6532 0.6470 0.7584 -0.1271 0.1125  0.0508  289 ASP B OD1 
9141 O OD2 . ASP B 304 ? 0.6925 0.6644 0.7533 -0.1175 0.1486  0.0451  289 ASP B OD2 
9146 N N   . LYS B 305 ? 0.5768 0.5800 0.6593 -0.0707 0.1119  0.0357  290 LYS B N   
9147 C CA  . LYS B 305 ? 0.5974 0.6236 0.7152 -0.0610 0.1278  0.0342  290 LYS B CA  
9148 C C   . LYS B 305 ? 0.5648 0.6157 0.7205 -0.0513 0.1082  0.0360  290 LYS B C   
9149 O O   . LYS B 305 ? 0.6199 0.6986 0.8252 -0.0472 0.1164  0.0379  290 LYS B O   
9150 C CB  . LYS B 305 ? 0.6287 0.6354 0.7090 -0.0511 0.1404  0.0284  290 LYS B CB  
9151 C CG  . LYS B 305 ? 0.6145 0.6388 0.7249 -0.0398 0.1571  0.0258  290 LYS B CG  
9152 C CD  . LYS B 305 ? 0.6416 0.6421 0.7098 -0.0317 0.1667  0.0197  290 LYS B CD  
9153 C CE  . LYS B 305 ? 0.5680 0.5816 0.6639 -0.0203 0.1839  0.0167  290 LYS B CE  
9154 N NZ  . LYS B 305 ? 0.6583 0.6459 0.7113 -0.0142 0.1926  0.0103  290 LYS B NZ  
9168 N N   . LEU B 306 ? 0.5540 0.5937 0.6864 -0.0471 0.0828  0.0355  291 LEU B N   
9169 C CA  . LEU B 306 ? 0.4926 0.5497 0.6526 -0.0395 0.0620  0.0377  291 LEU B CA  
9170 C C   . LEU B 306 ? 0.6102 0.6916 0.8189 -0.0498 0.0530  0.0439  291 LEU B C   
9171 O O   . LEU B 306 ? 0.6039 0.7118 0.8592 -0.0441 0.0488  0.0471  291 LEU B O   
9172 C CB  . LEU B 306 ? 0.5249 0.5601 0.6438 -0.0355 0.0393  0.0358  291 LEU B CB  
9173 C CG  . LEU B 306 ? 0.5547 0.5975 0.6860 -0.0296 0.0149  0.0380  291 LEU B CG  
9174 C CD1 . LEU B 306 ? 0.5735 0.6274 0.7191 -0.0150 0.0188  0.0373  291 LEU B CD1 
9175 C CD2 . LEU B 306 ? 0.4786 0.4945 0.5636 -0.0292 -0.0026 0.0354  291 LEU B CD2 
9187 N N   . LYS B 307 ? 0.5519 0.6243 0.7522 -0.0654 0.0492  0.0460  292 LYS B N   
9188 C CA  . LYS B 307 ? 0.6108 0.7036 0.8541 -0.0779 0.0358  0.0520  292 LYS B CA  
9189 C C   . LYS B 307 ? 0.7046 0.8290 1.0053 -0.0838 0.0581  0.0558  292 LYS B C   
9190 O O   . LYS B 307 ? 0.7079 0.8614 1.0628 -0.0887 0.0470  0.0615  292 LYS B O   
9191 C CB  . LYS B 307 ? 0.7291 0.7975 0.9406 -0.0936 0.0241  0.0527  292 LYS B CB  
9192 C CG  . LYS B 307 ? 0.7201 0.7792 0.9217 -0.0961 -0.0091 0.0539  292 LYS B CG  
9193 C CD  . LYS B 307 ? 0.8480 0.9381 1.1081 -0.1045 -0.0243 0.0604  292 LYS B CD  
9194 C CE  . LYS B 307 ? 0.8101 0.8853 1.0531 -0.1082 -0.0591 0.0612  292 LYS B CE  
9195 N NZ  . LYS B 307 ? 0.8663 0.9708 1.1665 -0.1185 -0.0779 0.0685  292 LYS B NZ  
9209 N N   . ASN B 308 ? 0.7090 0.8279 0.9993 -0.0839 0.0893  0.0530  293 ASN B N   
9210 C CA  . ASN B 308 ? 0.7252 0.8696 1.0642 -0.0912 0.1161  0.0560  293 ASN B CA  
9211 C C   . ASN B 308 ? 0.8000 0.9494 1.1444 -0.0761 0.1434  0.0515  293 ASN B C   
9212 O O   . ASN B 308 ? 0.7430 0.8644 1.0380 -0.0739 0.1609  0.0462  293 ASN B O   
9213 C CB  . ASN B 308 ? 0.7393 0.8653 1.0543 -0.1101 0.1312  0.0572  293 ASN B CB  
9214 C CG  . ASN B 308 ? 0.6707 0.7766 0.9578 -0.1228 0.1034  0.0595  293 ASN B CG  
9215 O OD1 . ASN B 308 ? 0.6704 0.7400 0.8983 -0.1256 0.1012  0.0567  293 ASN B OD1 
9216 N ND2 . ASN B 308 ? 0.6956 0.8236 1.0251 -0.1302 0.0809  0.0646  293 ASN B ND2 
9223 N N   . GLY B 309 ? 0.9585 1.1411 1.3616 -0.0658 0.1455  0.0538  294 GLY B N   
9224 C CA  . GLY B 309 ? 0.8897 1.0771 1.3030 -0.0505 0.1715  0.0495  294 GLY B CA  
9225 C C   . GLY B 309 ? 0.8662 1.0230 1.2214 -0.0374 0.1661  0.0429  294 GLY B C   
9226 O O   . GLY B 309 ? 0.9921 1.1183 1.2930 -0.0403 0.1801  0.0378  294 GLY B O   
# 
