data_9F7Y
# 
_entry.id   9F7Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9F7Y         pdb_00009f7y 10.2210/pdb9f7y/pdb 
WWPDB D_1292138384 ?            ?                   
# 
_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       2025-05-14 
_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                        9F7Y 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              acamara@ual.es 
_pdbx_contact_author.name_first         ana 
_pdbx_contact_author.name_last          camara-artigas 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2197-726X 
# 
_audit_author.name               'Camara-Artigas, A.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-2197-726X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'SARS-CoV-2 papain-like protease (PLpro) C112S-K191D-Q222D-K229R-Q230R-C271S mutant' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Camara-Artigas, A.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0003-2197-726X 
# 
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 'Replicase polyprotein 1ab' 36926.727 1   3.4.19.12,3.4.22.- ? ? ? 
2 non-polymer syn 'ZINC ION'                  65.409    1   ?                  ? ? ? 
3 non-polymer syn 'MALONIC ACID'              104.061   2   ?                  ? ? ? 
4 non-polymer syn 'SODIUM ION'                22.990    3   ?                  ? ? ? 
5 non-polymer syn 'CHLORIDE ION'              35.453    2   ?                  ? ? ? 
6 water       nat water                       18.015    327 ?                  ? ? ? 
# 
_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       
;MEVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSF
LGRYMSALNHTKKWKYPQVNGLTSIKWADNNSYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTV
GELGDVRETMSYLFQHANLDSCKRVLNVVCDTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVDIPCTCGRRATKYLVQQES
PFVMMSAPPAQYELKHGTFTCASEYTGNYQSGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTH
HHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MEVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSF
LGRYMSALNHTKKWKYPQVNGLTSIKWADNNSYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTV
GELGDVRETMSYLFQHANLDSCKRVLNVVCDTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVDIPCTCGRRATKYLVQQES
PFVMMSAPPAQYELKHGTFTCASEYTGNYQSGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTH
HHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'     ZN  
3 'MALONIC ACID' MLA 
4 'SODIUM ION'   NA  
5 'CHLORIDE ION' CL  
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   GLU n 
1 3   VAL n 
1 4   ARG n 
1 5   THR n 
1 6   ILE n 
1 7   LYS n 
1 8   VAL n 
1 9   PHE n 
1 10  THR n 
1 11  THR n 
1 12  VAL n 
1 13  ASP n 
1 14  ASN n 
1 15  ILE n 
1 16  ASN n 
1 17  LEU n 
1 18  HIS n 
1 19  THR n 
1 20  GLN n 
1 21  VAL n 
1 22  VAL n 
1 23  ASP n 
1 24  MET n 
1 25  SER n 
1 26  MET n 
1 27  THR n 
1 28  TYR n 
1 29  GLY n 
1 30  GLN n 
1 31  GLN n 
1 32  PHE n 
1 33  GLY n 
1 34  PRO n 
1 35  THR n 
1 36  TYR n 
1 37  LEU n 
1 38  ASP n 
1 39  GLY n 
1 40  ALA n 
1 41  ASP n 
1 42  VAL n 
1 43  THR n 
1 44  LYS n 
1 45  ILE n 
1 46  LYS n 
1 47  PRO n 
1 48  HIS n 
1 49  ASN n 
1 50  SER n 
1 51  HIS n 
1 52  GLU n 
1 53  GLY n 
1 54  LYS n 
1 55  THR n 
1 56  PHE n 
1 57  TYR n 
1 58  VAL n 
1 59  LEU n 
1 60  PRO n 
1 61  ASN n 
1 62  ASP n 
1 63  ASP n 
1 64  THR n 
1 65  LEU n 
1 66  ARG n 
1 67  VAL n 
1 68  GLU n 
1 69  ALA n 
1 70  PHE n 
1 71  GLU n 
1 72  TYR n 
1 73  TYR n 
1 74  HIS n 
1 75  THR n 
1 76  THR n 
1 77  ASP n 
1 78  PRO n 
1 79  SER n 
1 80  PHE n 
1 81  LEU n 
1 82  GLY n 
1 83  ARG n 
1 84  TYR n 
1 85  MET n 
1 86  SER n 
1 87  ALA n 
1 88  LEU n 
1 89  ASN n 
1 90  HIS n 
1 91  THR n 
1 92  LYS n 
1 93  LYS n 
1 94  TRP n 
1 95  LYS n 
1 96  TYR n 
1 97  PRO n 
1 98  GLN n 
1 99  VAL n 
1 100 ASN n 
1 101 GLY n 
1 102 LEU n 
1 103 THR n 
1 104 SER n 
1 105 ILE n 
1 106 LYS n 
1 107 TRP n 
1 108 ALA n 
1 109 ASP n 
1 110 ASN n 
1 111 ASN n 
1 112 SER n 
1 113 TYR n 
1 114 LEU n 
1 115 ALA n 
1 116 THR n 
1 117 ALA n 
1 118 LEU n 
1 119 LEU n 
1 120 THR n 
1 121 LEU n 
1 122 GLN n 
1 123 GLN n 
1 124 ILE n 
1 125 GLU n 
1 126 LEU n 
1 127 LYS n 
1 128 PHE n 
1 129 ASN n 
1 130 PRO n 
1 131 PRO n 
1 132 ALA n 
1 133 LEU n 
1 134 GLN n 
1 135 ASP n 
1 136 ALA n 
1 137 TYR n 
1 138 TYR n 
1 139 ARG n 
1 140 ALA n 
1 141 ARG n 
1 142 ALA n 
1 143 GLY n 
1 144 GLU n 
1 145 ALA n 
1 146 ALA n 
1 147 ASN n 
1 148 PHE n 
1 149 CYS n 
1 150 ALA n 
1 151 LEU n 
1 152 ILE n 
1 153 LEU n 
1 154 ALA n 
1 155 TYR n 
1 156 CYS n 
1 157 ASN n 
1 158 LYS n 
1 159 THR n 
1 160 VAL n 
1 161 GLY n 
1 162 GLU n 
1 163 LEU n 
1 164 GLY n 
1 165 ASP n 
1 166 VAL n 
1 167 ARG n 
1 168 GLU n 
1 169 THR n 
1 170 MET n 
1 171 SER n 
1 172 TYR n 
1 173 LEU n 
1 174 PHE n 
1 175 GLN n 
1 176 HIS n 
1 177 ALA n 
1 178 ASN n 
1 179 LEU n 
1 180 ASP n 
1 181 SER n 
1 182 CYS n 
1 183 LYS n 
1 184 ARG n 
1 185 VAL n 
1 186 LEU n 
1 187 ASN n 
1 188 VAL n 
1 189 VAL n 
1 190 CYS n 
1 191 ASP n 
1 192 THR n 
1 193 CYS n 
1 194 GLY n 
1 195 GLN n 
1 196 GLN n 
1 197 GLN n 
1 198 THR n 
1 199 THR n 
1 200 LEU n 
1 201 LYS n 
1 202 GLY n 
1 203 VAL n 
1 204 GLU n 
1 205 ALA n 
1 206 VAL n 
1 207 MET n 
1 208 TYR n 
1 209 MET n 
1 210 GLY n 
1 211 THR n 
1 212 LEU n 
1 213 SER n 
1 214 TYR n 
1 215 GLU n 
1 216 GLN n 
1 217 PHE n 
1 218 LYS n 
1 219 LYS n 
1 220 GLY n 
1 221 VAL n 
1 222 ASP n 
1 223 ILE n 
1 224 PRO n 
1 225 CYS n 
1 226 THR n 
1 227 CYS n 
1 228 GLY n 
1 229 ARG n 
1 230 ARG n 
1 231 ALA n 
1 232 THR n 
1 233 LYS n 
1 234 TYR n 
1 235 LEU n 
1 236 VAL n 
1 237 GLN n 
1 238 GLN n 
1 239 GLU n 
1 240 SER n 
1 241 PRO n 
1 242 PHE n 
1 243 VAL n 
1 244 MET n 
1 245 MET n 
1 246 SER n 
1 247 ALA n 
1 248 PRO n 
1 249 PRO n 
1 250 ALA n 
1 251 GLN n 
1 252 TYR n 
1 253 GLU n 
1 254 LEU n 
1 255 LYS n 
1 256 HIS n 
1 257 GLY n 
1 258 THR n 
1 259 PHE n 
1 260 THR n 
1 261 CYS n 
1 262 ALA n 
1 263 SER n 
1 264 GLU n 
1 265 TYR n 
1 266 THR n 
1 267 GLY n 
1 268 ASN n 
1 269 TYR n 
1 270 GLN n 
1 271 SER n 
1 272 GLY n 
1 273 HIS n 
1 274 TYR n 
1 275 LYS n 
1 276 HIS n 
1 277 ILE n 
1 278 THR n 
1 279 SER n 
1 280 LYS n 
1 281 GLU n 
1 282 THR n 
1 283 LEU n 
1 284 TYR n 
1 285 CYS n 
1 286 ILE n 
1 287 ASP n 
1 288 GLY n 
1 289 ALA n 
1 290 LEU n 
1 291 LEU n 
1 292 THR n 
1 293 LYS n 
1 294 SER n 
1 295 SER n 
1 296 GLU n 
1 297 TYR n 
1 298 LYS n 
1 299 GLY n 
1 300 PRO n 
1 301 ILE n 
1 302 THR n 
1 303 ASP n 
1 304 VAL n 
1 305 PHE n 
1 306 TYR n 
1 307 LYS n 
1 308 GLU n 
1 309 ASN n 
1 310 SER n 
1 311 TYR n 
1 312 THR n 
1 313 THR n 
1 314 THR n 
1 315 ILE n 
1 316 LYS n 
1 317 PRO n 
1 318 VAL n 
1 319 THR n 
1 320 HIS n 
1 321 HIS n 
1 322 HIS n 
1 323 HIS n 
1 324 HIS n 
1 325 HIS 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                   325 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CL  non-polymer         . 'CHLORIDE ION'  ?                                                                    'Cl -1'          
35.453  
CYS 'L-peptide linking' y CYSTEINE        ?                                                                    'C3 H7 N O2 S'   
121.158 
GLN 'L-peptide linking' y GLUTAMINE       ?                                                                    'C5 H10 N2 O3'   
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                                                                    'C5 H9 N O4'     
147.129 
GLY 'peptide linking'   y GLYCINE         ?                                                                    'C2 H5 N O2'     
75.067  
HIS 'L-peptide linking' y HISTIDINE       ?                                                                    'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER           ?                                                                    'H2 O'           
18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                                                                    'C6 H13 N O2'    
131.173 
LEU 'L-peptide linking' y LEUCINE         ?                                                                    'C6 H13 N O2'    
131.173 
LYS 'L-peptide linking' y LYSINE          ?                                                                    'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking' y METHIONINE      ?                                                                    'C5 H11 N O2 S'  
149.211 
MLA non-polymer         . 'MALONIC ACID'  'DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID; METHANEDICARBOXYLIC ACID' 'C3 H4 O4'       
104.061 
NA  non-polymer         . 'SODIUM ION'    ?                                                                    'Na 1'           
22.990  
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 
ZN  non-polymer         . 'ZINC ION'      ?                                                                    'Zn 2'           
65.409  
# 
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   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   2   GLU GLU A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  ILE 15  15  15  ILE ILE A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  HIS 18  18  18  HIS HIS A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  GLN 20  20  20  GLN GLN A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  MET 24  24  24  MET MET A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  MET 26  26  26  MET MET A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  TYR 28  28  28  TYR TYR A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  VAL 67  67  67  VAL VAL A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  TYR 73  73  73  TYR TYR A . n 
A 1 74  HIS 74  74  74  HIS HIS A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  TYR 84  84  84  TYR TYR A . n 
A 1 85  MET 85  85  85  MET MET A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 ASN 100 100 100 ASN ASN A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 TRP 107 107 107 TRP TRP A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 GLN 122 122 122 GLN GLN A . n 
A 1 123 GLN 123 123 123 GLN GLN A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 ASN 129 129 129 ASN ASN A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 GLN 134 134 134 GLN GLN A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 TYR 138 138 138 TYR TYR A . n 
A 1 139 ARG 139 139 139 ARG ARG A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 CYS 149 149 149 CYS CYS A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 ASN 157 157 157 ASN ASN A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 THR 159 159 159 THR THR A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 ASP 165 165 165 ASP ASP A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 MET 170 170 170 MET MET A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 HIS 176 176 176 HIS HIS A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 CYS 182 182 182 CYS CYS A . n 
A 1 183 LYS 183 183 183 LYS LYS A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 ASN 187 187 187 ASN ASN A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 CYS 190 190 190 CYS CYS A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 CYS 193 193 193 CYS CYS A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 GLN 195 195 195 GLN GLN A . n 
A 1 196 GLN 196 196 196 GLN GLN A . n 
A 1 197 GLN 197 197 197 GLN GLN A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 MET 207 207 207 MET MET A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 MET 209 209 209 MET MET A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 LYS 219 219 219 LYS LYS A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 ILE 223 223 223 ILE ILE A . n 
A 1 224 PRO 224 224 224 PRO PRO A . n 
A 1 225 CYS 225 225 225 CYS CYS A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 CYS 227 227 227 CYS CYS A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 ARG 230 230 230 ARG ARG A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 LYS 233 233 233 LYS LYS A . n 
A 1 234 TYR 234 234 234 TYR TYR A . n 
A 1 235 LEU 235 235 235 LEU LEU A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 GLN 237 237 237 GLN GLN A . n 
A 1 238 GLN 238 238 238 GLN GLN A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 MET 244 244 244 MET MET A . n 
A 1 245 MET 245 245 245 MET MET A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 GLN 251 251 251 GLN GLN A . n 
A 1 252 TYR 252 252 252 TYR TYR A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 LYS 255 255 255 LYS LYS A . n 
A 1 256 HIS 256 256 256 HIS HIS A . n 
A 1 257 GLY 257 257 257 GLY GLY A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 THR 260 260 260 THR THR A . n 
A 1 261 CYS 261 261 261 CYS CYS A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 TYR 265 265 265 TYR TYR A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 ASN 268 268 268 ASN ASN A . n 
A 1 269 TYR 269 269 269 TYR TYR A . n 
A 1 270 GLN 270 270 270 GLN GLN A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 HIS 273 273 273 HIS HIS A . n 
A 1 274 TYR 274 274 274 TYR TYR A . n 
A 1 275 LYS 275 275 275 LYS LYS A . n 
A 1 276 HIS 276 276 276 HIS HIS A . n 
A 1 277 ILE 277 277 277 ILE ILE A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 THR 282 282 282 THR THR A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 TYR 284 284 284 TYR TYR A . n 
A 1 285 CYS 285 285 285 CYS CYS A . n 
A 1 286 ILE 286 286 286 ILE ILE A . n 
A 1 287 ASP 287 287 287 ASP ASP A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 LEU 291 291 291 LEU LEU A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 LYS 293 293 293 LYS LYS A . n 
A 1 294 SER 294 294 294 SER SER A . n 
A 1 295 SER 295 295 295 SER SER A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 TYR 297 297 297 TYR TYR A . n 
A 1 298 LYS 298 298 298 LYS LYS A . n 
A 1 299 GLY 299 299 299 GLY GLY A . n 
A 1 300 PRO 300 300 300 PRO PRO A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 THR 302 302 302 THR THR A . n 
A 1 303 ASP 303 303 303 ASP ASP A . n 
A 1 304 VAL 304 304 304 VAL VAL A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 TYR 306 306 306 TYR TYR A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 ASN 309 309 309 ASN ASN A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 THR 312 312 312 THR THR A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 THR 314 314 314 THR THR A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 LYS 316 316 316 LYS LYS A . n 
A 1 317 PRO 317 317 317 PRO PRO A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 THR 319 319 319 THR THR A . n 
A 1 320 HIS 320 320 320 HIS HIS A . n 
A 1 321 HIS 321 321 321 HIS HIS A . n 
A 1 322 HIS 322 322 322 HIS HIS A . n 
A 1 323 HIS 323 323 323 HIS HIS A . n 
A 1 324 HIS 324 324 324 HIS HIS A . n 
A 1 325 HIS 325 325 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   401 401 ZN  ZN  A . 
C 3 MLA 1   402 406 MLA MLA A . 
D 3 MLA 1   403 407 MLA MLA A . 
E 4 NA  1   404 1   NA  NA  A . 
F 4 NA  1   405 2   NA  NA  A . 
G 4 NA  1   406 3   NA  NA  A . 
H 5 CL  1   407 1   CL  CL  A . 
I 5 CL  1   408 2   CL  CL  A . 
J 6 HOH 1   501 116 HOH HOH A . 
J 6 HOH 2   502 281 HOH HOH A . 
J 6 HOH 3   503 208 HOH HOH A . 
J 6 HOH 4   504 317 HOH HOH A . 
J 6 HOH 5   505 123 HOH HOH A . 
J 6 HOH 6   506 50  HOH HOH A . 
J 6 HOH 7   507 261 HOH HOH A . 
J 6 HOH 8   508 144 HOH HOH A . 
J 6 HOH 9   509 72  HOH HOH A . 
J 6 HOH 10  510 71  HOH HOH A . 
J 6 HOH 11  511 149 HOH HOH A . 
J 6 HOH 12  512 87  HOH HOH A . 
J 6 HOH 13  513 263 HOH HOH A . 
J 6 HOH 14  514 246 HOH HOH A . 
J 6 HOH 15  515 67  HOH HOH A . 
J 6 HOH 16  516 160 HOH HOH A . 
J 6 HOH 17  517 148 HOH HOH A . 
J 6 HOH 18  518 267 HOH HOH A . 
J 6 HOH 19  519 143 HOH HOH A . 
J 6 HOH 20  520 112 HOH HOH A . 
J 6 HOH 21  521 21  HOH HOH A . 
J 6 HOH 22  522 158 HOH HOH A . 
J 6 HOH 23  523 275 HOH HOH A . 
J 6 HOH 24  524 9   HOH HOH A . 
J 6 HOH 25  525 222 HOH HOH A . 
J 6 HOH 26  526 130 HOH HOH A . 
J 6 HOH 27  527 94  HOH HOH A . 
J 6 HOH 28  528 90  HOH HOH A . 
J 6 HOH 29  529 288 HOH HOH A . 
J 6 HOH 30  530 233 HOH HOH A . 
J 6 HOH 31  531 60  HOH HOH A . 
J 6 HOH 32  532 178 HOH HOH A . 
J 6 HOH 33  533 17  HOH HOH A . 
J 6 HOH 34  534 6   HOH HOH A . 
J 6 HOH 35  535 84  HOH HOH A . 
J 6 HOH 36  536 113 HOH HOH A . 
J 6 HOH 37  537 129 HOH HOH A . 
J 6 HOH 38  538 157 HOH HOH A . 
J 6 HOH 39  539 139 HOH HOH A . 
J 6 HOH 40  540 55  HOH HOH A . 
J 6 HOH 41  541 173 HOH HOH A . 
J 6 HOH 42  542 308 HOH HOH A . 
J 6 HOH 43  543 214 HOH HOH A . 
J 6 HOH 44  544 196 HOH HOH A . 
J 6 HOH 45  545 54  HOH HOH A . 
J 6 HOH 46  546 52  HOH HOH A . 
J 6 HOH 47  547 63  HOH HOH A . 
J 6 HOH 48  548 211 HOH HOH A . 
J 6 HOH 49  549 38  HOH HOH A . 
J 6 HOH 50  550 108 HOH HOH A . 
J 6 HOH 51  551 231 HOH HOH A . 
J 6 HOH 52  552 131 HOH HOH A . 
J 6 HOH 53  553 244 HOH HOH A . 
J 6 HOH 54  554 124 HOH HOH A . 
J 6 HOH 55  555 65  HOH HOH A . 
J 6 HOH 56  556 155 HOH HOH A . 
J 6 HOH 57  557 312 HOH HOH A . 
J 6 HOH 58  558 299 HOH HOH A . 
J 6 HOH 59  559 48  HOH HOH A . 
J 6 HOH 60  560 19  HOH HOH A . 
J 6 HOH 61  561 57  HOH HOH A . 
J 6 HOH 62  562 179 HOH HOH A . 
J 6 HOH 63  563 118 HOH HOH A . 
J 6 HOH 64  564 32  HOH HOH A . 
J 6 HOH 65  565 274 HOH HOH A . 
J 6 HOH 66  566 2   HOH HOH A . 
J 6 HOH 67  567 42  HOH HOH A . 
J 6 HOH 68  568 203 HOH HOH A . 
J 6 HOH 69  569 74  HOH HOH A . 
J 6 HOH 70  570 322 HOH HOH A . 
J 6 HOH 71  571 8   HOH HOH A . 
J 6 HOH 72  572 153 HOH HOH A . 
J 6 HOH 73  573 78  HOH HOH A . 
J 6 HOH 74  574 92  HOH HOH A . 
J 6 HOH 75  575 174 HOH HOH A . 
J 6 HOH 76  576 73  HOH HOH A . 
J 6 HOH 77  577 3   HOH HOH A . 
J 6 HOH 78  578 318 HOH HOH A . 
J 6 HOH 79  579 150 HOH HOH A . 
J 6 HOH 80  580 234 HOH HOH A . 
J 6 HOH 81  581 82  HOH HOH A . 
J 6 HOH 82  582 176 HOH HOH A . 
J 6 HOH 83  583 58  HOH HOH A . 
J 6 HOH 84  584 257 HOH HOH A . 
J 6 HOH 85  585 135 HOH HOH A . 
J 6 HOH 86  586 215 HOH HOH A . 
J 6 HOH 87  587 107 HOH HOH A . 
J 6 HOH 88  588 22  HOH HOH A . 
J 6 HOH 89  589 36  HOH HOH A . 
J 6 HOH 90  590 313 HOH HOH A . 
J 6 HOH 91  591 44  HOH HOH A . 
J 6 HOH 92  592 80  HOH HOH A . 
J 6 HOH 93  593 200 HOH HOH A . 
J 6 HOH 94  594 25  HOH HOH A . 
J 6 HOH 95  595 159 HOH HOH A . 
J 6 HOH 96  596 43  HOH HOH A . 
J 6 HOH 97  597 61  HOH HOH A . 
J 6 HOH 98  598 106 HOH HOH A . 
J 6 HOH 99  599 56  HOH HOH A . 
J 6 HOH 100 600 20  HOH HOH A . 
J 6 HOH 101 601 309 HOH HOH A . 
J 6 HOH 102 602 170 HOH HOH A . 
J 6 HOH 103 603 245 HOH HOH A . 
J 6 HOH 104 604 53  HOH HOH A . 
J 6 HOH 105 605 226 HOH HOH A . 
J 6 HOH 106 606 232 HOH HOH A . 
J 6 HOH 107 607 7   HOH HOH A . 
J 6 HOH 108 608 62  HOH HOH A . 
J 6 HOH 109 609 68  HOH HOH A . 
J 6 HOH 110 610 260 HOH HOH A . 
J 6 HOH 111 611 104 HOH HOH A . 
J 6 HOH 112 612 75  HOH HOH A . 
J 6 HOH 113 613 332 HOH HOH A . 
J 6 HOH 114 614 284 HOH HOH A . 
J 6 HOH 115 615 86  HOH HOH A . 
J 6 HOH 116 616 168 HOH HOH A . 
J 6 HOH 117 617 265 HOH HOH A . 
J 6 HOH 118 618 236 HOH HOH A . 
J 6 HOH 119 619 220 HOH HOH A . 
J 6 HOH 120 620 134 HOH HOH A . 
J 6 HOH 121 621 16  HOH HOH A . 
J 6 HOH 122 622 5   HOH HOH A . 
J 6 HOH 123 623 34  HOH HOH A . 
J 6 HOH 124 624 26  HOH HOH A . 
J 6 HOH 125 625 79  HOH HOH A . 
J 6 HOH 126 626 259 HOH HOH A . 
J 6 HOH 127 627 147 HOH HOH A . 
J 6 HOH 128 628 152 HOH HOH A . 
J 6 HOH 129 629 10  HOH HOH A . 
J 6 HOH 130 630 1   HOH HOH A . 
J 6 HOH 131 631 167 HOH HOH A . 
J 6 HOH 132 632 228 HOH HOH A . 
J 6 HOH 133 633 126 HOH HOH A . 
J 6 HOH 134 634 15  HOH HOH A . 
J 6 HOH 135 635 186 HOH HOH A . 
J 6 HOH 136 636 30  HOH HOH A . 
J 6 HOH 137 637 307 HOH HOH A . 
J 6 HOH 138 638 164 HOH HOH A . 
J 6 HOH 139 639 295 HOH HOH A . 
J 6 HOH 140 640 227 HOH HOH A . 
J 6 HOH 141 641 66  HOH HOH A . 
J 6 HOH 142 642 45  HOH HOH A . 
J 6 HOH 143 643 138 HOH HOH A . 
J 6 HOH 144 644 11  HOH HOH A . 
J 6 HOH 145 645 40  HOH HOH A . 
J 6 HOH 146 646 85  HOH HOH A . 
J 6 HOH 147 647 18  HOH HOH A . 
J 6 HOH 148 648 145 HOH HOH A . 
J 6 HOH 149 649 292 HOH HOH A . 
J 6 HOH 150 650 297 HOH HOH A . 
J 6 HOH 151 651 127 HOH HOH A . 
J 6 HOH 152 652 195 HOH HOH A . 
J 6 HOH 153 653 323 HOH HOH A . 
J 6 HOH 154 654 13  HOH HOH A . 
J 6 HOH 155 655 119 HOH HOH A . 
J 6 HOH 156 656 98  HOH HOH A . 
J 6 HOH 157 657 101 HOH HOH A . 
J 6 HOH 158 658 329 HOH HOH A . 
J 6 HOH 159 659 287 HOH HOH A . 
J 6 HOH 160 660 142 HOH HOH A . 
J 6 HOH 161 661 262 HOH HOH A . 
J 6 HOH 162 662 128 HOH HOH A . 
J 6 HOH 163 663 125 HOH HOH A . 
J 6 HOH 164 664 109 HOH HOH A . 
J 6 HOH 165 665 27  HOH HOH A . 
J 6 HOH 166 666 238 HOH HOH A . 
J 6 HOH 167 667 33  HOH HOH A . 
J 6 HOH 168 668 37  HOH HOH A . 
J 6 HOH 169 669 96  HOH HOH A . 
J 6 HOH 170 670 12  HOH HOH A . 
J 6 HOH 171 671 205 HOH HOH A . 
J 6 HOH 172 672 103 HOH HOH A . 
J 6 HOH 173 673 24  HOH HOH A . 
J 6 HOH 174 674 47  HOH HOH A . 
J 6 HOH 175 675 225 HOH HOH A . 
J 6 HOH 176 676 115 HOH HOH A . 
J 6 HOH 177 677 29  HOH HOH A . 
J 6 HOH 178 678 315 HOH HOH A . 
J 6 HOH 179 679 95  HOH HOH A . 
J 6 HOH 180 680 161 HOH HOH A . 
J 6 HOH 181 681 23  HOH HOH A . 
J 6 HOH 182 682 303 HOH HOH A . 
J 6 HOH 183 683 39  HOH HOH A . 
J 6 HOH 184 684 14  HOH HOH A . 
J 6 HOH 185 685 111 HOH HOH A . 
J 6 HOH 186 686 76  HOH HOH A . 
J 6 HOH 187 687 121 HOH HOH A . 
J 6 HOH 188 688 99  HOH HOH A . 
J 6 HOH 189 689 105 HOH HOH A . 
J 6 HOH 190 690 324 HOH HOH A . 
J 6 HOH 191 691 283 HOH HOH A . 
J 6 HOH 192 692 46  HOH HOH A . 
J 6 HOH 193 693 230 HOH HOH A . 
J 6 HOH 194 694 70  HOH HOH A . 
J 6 HOH 195 695 252 HOH HOH A . 
J 6 HOH 196 696 310 HOH HOH A . 
J 6 HOH 197 697 282 HOH HOH A . 
J 6 HOH 198 698 254 HOH HOH A . 
J 6 HOH 199 699 240 HOH HOH A . 
J 6 HOH 200 700 49  HOH HOH A . 
J 6 HOH 201 701 102 HOH HOH A . 
J 6 HOH 202 702 175 HOH HOH A . 
J 6 HOH 203 703 184 HOH HOH A . 
J 6 HOH 204 704 35  HOH HOH A . 
J 6 HOH 205 705 209 HOH HOH A . 
J 6 HOH 206 706 249 HOH HOH A . 
J 6 HOH 207 707 258 HOH HOH A . 
J 6 HOH 208 708 212 HOH HOH A . 
J 6 HOH 209 709 91  HOH HOH A . 
J 6 HOH 210 710 325 HOH HOH A . 
J 6 HOH 211 711 28  HOH HOH A . 
J 6 HOH 212 712 316 HOH HOH A . 
J 6 HOH 213 713 314 HOH HOH A . 
J 6 HOH 214 714 83  HOH HOH A . 
J 6 HOH 215 715 217 HOH HOH A . 
J 6 HOH 216 716 151 HOH HOH A . 
J 6 HOH 217 717 64  HOH HOH A . 
J 6 HOH 218 718 110 HOH HOH A . 
J 6 HOH 219 719 4   HOH HOH A . 
J 6 HOH 220 720 273 HOH HOH A . 
J 6 HOH 221 721 136 HOH HOH A . 
J 6 HOH 222 722 270 HOH HOH A . 
J 6 HOH 223 723 190 HOH HOH A . 
J 6 HOH 224 724 166 HOH HOH A . 
J 6 HOH 225 725 204 HOH HOH A . 
J 6 HOH 226 726 302 HOH HOH A . 
J 6 HOH 227 727 89  HOH HOH A . 
J 6 HOH 228 728 321 HOH HOH A . 
J 6 HOH 229 729 229 HOH HOH A . 
J 6 HOH 230 730 31  HOH HOH A . 
J 6 HOH 231 731 280 HOH HOH A . 
J 6 HOH 232 732 286 HOH HOH A . 
J 6 HOH 233 733 285 HOH HOH A . 
J 6 HOH 234 734 59  HOH HOH A . 
J 6 HOH 235 735 224 HOH HOH A . 
J 6 HOH 236 736 298 HOH HOH A . 
J 6 HOH 237 737 250 HOH HOH A . 
J 6 HOH 238 738 185 HOH HOH A . 
J 6 HOH 239 739 194 HOH HOH A . 
J 6 HOH 240 740 253 HOH HOH A . 
J 6 HOH 241 741 268 HOH HOH A . 
J 6 HOH 242 742 311 HOH HOH A . 
J 6 HOH 243 743 140 HOH HOH A . 
J 6 HOH 244 744 221 HOH HOH A . 
J 6 HOH 245 745 206 HOH HOH A . 
J 6 HOH 246 746 319 HOH HOH A . 
J 6 HOH 247 747 333 HOH HOH A . 
J 6 HOH 248 748 193 HOH HOH A . 
J 6 HOH 249 749 165 HOH HOH A . 
J 6 HOH 250 750 293 HOH HOH A . 
J 6 HOH 251 751 296 HOH HOH A . 
J 6 HOH 252 752 266 HOH HOH A . 
J 6 HOH 253 753 331 HOH HOH A . 
J 6 HOH 254 754 272 HOH HOH A . 
J 6 HOH 255 755 255 HOH HOH A . 
J 6 HOH 256 756 243 HOH HOH A . 
J 6 HOH 257 757 279 HOH HOH A . 
J 6 HOH 258 758 269 HOH HOH A . 
J 6 HOH 259 759 328 HOH HOH A . 
J 6 HOH 260 760 327 HOH HOH A . 
J 6 HOH 261 761 41  HOH HOH A . 
J 6 HOH 262 762 330 HOH HOH A . 
J 6 HOH 263 763 248 HOH HOH A . 
J 6 HOH 264 764 81  HOH HOH A . 
J 6 HOH 265 765 320 HOH HOH A . 
J 6 HOH 266 766 182 HOH HOH A . 
J 6 HOH 267 767 223 HOH HOH A . 
J 6 HOH 268 768 239 HOH HOH A . 
J 6 HOH 269 769 237 HOH HOH A . 
J 6 HOH 270 770 77  HOH HOH A . 
J 6 HOH 271 771 189 HOH HOH A . 
J 6 HOH 272 772 304 HOH HOH A . 
J 6 HOH 273 773 216 HOH HOH A . 
J 6 HOH 274 774 256 HOH HOH A . 
J 6 HOH 275 775 93  HOH HOH A . 
J 6 HOH 276 776 271 HOH HOH A . 
J 6 HOH 277 777 247 HOH HOH A . 
J 6 HOH 278 778 88  HOH HOH A . 
J 6 HOH 279 779 188 HOH HOH A . 
J 6 HOH 280 780 294 HOH HOH A . 
J 6 HOH 281 781 133 HOH HOH A . 
J 6 HOH 282 782 326 HOH HOH A . 
J 6 HOH 283 783 235 HOH HOH A . 
J 6 HOH 284 784 141 HOH HOH A . 
J 6 HOH 285 785 202 HOH HOH A . 
J 6 HOH 286 786 117 HOH HOH A . 
J 6 HOH 287 787 169 HOH HOH A . 
J 6 HOH 288 788 100 HOH HOH A . 
J 6 HOH 289 789 201 HOH HOH A . 
J 6 HOH 290 790 132 HOH HOH A . 
J 6 HOH 291 791 51  HOH HOH A . 
J 6 HOH 292 792 291 HOH HOH A . 
J 6 HOH 293 793 218 HOH HOH A . 
J 6 HOH 294 794 122 HOH HOH A . 
J 6 HOH 295 795 276 HOH HOH A . 
J 6 HOH 296 796 199 HOH HOH A . 
J 6 HOH 297 797 207 HOH HOH A . 
J 6 HOH 298 798 305 HOH HOH A . 
J 6 HOH 299 799 241 HOH HOH A . 
J 6 HOH 300 800 191 HOH HOH A . 
J 6 HOH 301 801 114 HOH HOH A . 
J 6 HOH 302 802 306 HOH HOH A . 
J 6 HOH 303 803 171 HOH HOH A . 
J 6 HOH 304 804 146 HOH HOH A . 
J 6 HOH 305 805 213 HOH HOH A . 
J 6 HOH 306 806 301 HOH HOH A . 
J 6 HOH 307 807 172 HOH HOH A . 
J 6 HOH 308 808 192 HOH HOH A . 
J 6 HOH 309 809 219 HOH HOH A . 
J 6 HOH 310 810 181 HOH HOH A . 
J 6 HOH 311 811 197 HOH HOH A . 
J 6 HOH 312 812 300 HOH HOH A . 
J 6 HOH 313 813 163 HOH HOH A . 
J 6 HOH 314 814 290 HOH HOH A . 
J 6 HOH 315 815 162 HOH HOH A . 
J 6 HOH 316 816 154 HOH HOH A . 
J 6 HOH 317 817 69  HOH HOH A . 
J 6 HOH 318 818 277 HOH HOH A . 
J 6 HOH 319 819 97  HOH HOH A . 
J 6 HOH 320 820 137 HOH HOH A . 
J 6 HOH 321 821 120 HOH HOH A . 
J 6 HOH 322 822 180 HOH HOH A . 
J 6 HOH 323 823 198 HOH HOH A . 
J 6 HOH 324 824 156 HOH HOH A . 
J 6 HOH 325 825 251 HOH HOH A . 
J 6 HOH 326 826 187 HOH HOH A . 
J 6 HOH 327 827 210 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 4   ? CG  ? A ARG 4   CG  
2  1 Y 1 A ARG 4   ? CD  ? A ARG 4   CD  
3  1 Y 1 A ARG 4   ? NE  ? A ARG 4   NE  
4  1 Y 1 A ARG 4   ? CZ  ? A ARG 4   CZ  
5  1 Y 1 A ARG 4   ? NH1 ? A ARG 4   NH1 
6  1 Y 1 A ARG 4   ? NH2 ? A ARG 4   NH2 
7  1 Y 1 A LYS 316 ? CG  ? A LYS 316 CG  
8  1 Y 1 A LYS 316 ? CD  ? A LYS 316 CD  
9  1 Y 1 A LYS 316 ? CE  ? A LYS 316 CE  
10 1 Y 1 A LYS 316 ? NZ  ? A LYS 316 NZ  
11 1 Y 1 A VAL 318 ? CG1 ? A VAL 318 CG1 
12 1 Y 1 A VAL 318 ? CG2 ? A VAL 318 CG2 
13 1 Y 1 A THR 319 ? OG1 ? A THR 319 OG1 
14 1 Y 1 A THR 319 ? CG2 ? A THR 319 CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F7Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     81.465 
_cell.length_a_esd                 ? 
_cell.length_b                     81.465 
_cell.length_b_esd                 ? 
_cell.length_c                     134.931 
_cell.length_c_esd                 ? 
_cell.volume                       775504.807 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9F7Y 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            
;P 32 2"
;
_symmetry.space_group_name_H-M             'P 32 2 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                   9F7Y 
_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             3.50 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.86 
_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              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.4 M sodium malonate, 0.1 M sodium succinate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            288 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 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         2023-04-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.282703 
_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                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.282703 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          32.42 
_reflns.entry_id                                       9F7Y 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               19.69 
_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                                     48714 
_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                                12.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.97 
_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                                0.066 
_reflns.pdbx_Rpim_I_all                                0.019 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       586914 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.063 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           32373 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2862 
_reflns_shell.percent_possible_obs                          100.0 
_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                               11.3 
_reflns_shell.pdbx_chi_squared                              0.94 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.4 
_reflns_shell.pdbx_Rrim_I_all                               0.975 
_reflns_shell.pdbx_Rpim_I_all                               0.286 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.824 
_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                                  0.931 
_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                               39.83 
_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                                 9F7Y 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             19.69 
_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                     48660 
_refine.ls_number_reflns_R_free                  2437 
_refine.ls_number_reflns_R_work                  46223 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1658 
_refine.ls_R_factor_R_free                       0.1830 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1648 
_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                          1.07 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 18.7095 
_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                            0.1910 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        19.69 
_refine_hist.number_atoms_solvent             327 
_refine_hist.number_atoms_total               2907 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2560 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0067  ? 2673 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8606  ? 3636 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0527  ? 398  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0060  ? 471  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.1823 ? 964  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.84  . . 151 2678 99.93  . . . . 0.2708 . . . . . . . . . . . 0.3008 
'X-RAY DIFFRACTION' 1.84 1.88  . . 144 2674 99.93  . . . . 0.2444 . . . . . . . . . . . 0.2770 
'X-RAY DIFFRACTION' 1.88 1.92  . . 134 2681 100.00 . . . . 0.2189 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 1.92 1.97  . . 166 2662 100.00 . . . . 0.2021 . . . . . . . . . . . 0.2299 
'X-RAY DIFFRACTION' 1.97 2.02  . . 113 2718 100.00 . . . . 0.1914 . . . . . . . . . . . 0.2258 
'X-RAY DIFFRACTION' 2.02 2.08  . . 125 2702 99.89  . . . . 0.1870 . . . . . . . . . . . 0.1740 
'X-RAY DIFFRACTION' 2.08 2.15  . . 147 2697 100.00 . . . . 0.1842 . . . . . . . . . . . 0.2014 
'X-RAY DIFFRACTION' 2.15 2.22  . . 147 2675 100.00 . . . . 0.1698 . . . . . . . . . . . 0.1972 
'X-RAY DIFFRACTION' 2.22 2.31  . . 134 2721 100.00 . . . . 0.1689 . . . . . . . . . . . 0.1897 
'X-RAY DIFFRACTION' 2.31 2.42  . . 141 2695 100.00 . . . . 0.1677 . . . . . . . . . . . 0.2028 
'X-RAY DIFFRACTION' 2.42 2.55  . . 128 2743 100.00 . . . . 0.1703 . . . . . . . . . . . 0.1827 
'X-RAY DIFFRACTION' 2.55 2.70  . . 146 2700 99.96  . . . . 0.1816 . . . . . . . . . . . 0.2027 
'X-RAY DIFFRACTION' 2.71 2.91  . . 132 2747 100.00 . . . . 0.1750 . . . . . . . . . . . 0.1886 
'X-RAY DIFFRACTION' 2.91 3.21  . . 156 2728 100.00 . . . . 0.1780 . . . . . . . . . . . 0.2060 
'X-RAY DIFFRACTION' 3.21 3.67  . . 144 2750 100.00 . . . . 0.1488 . . . . . . . . . . . 0.1867 
'X-RAY DIFFRACTION' 3.67 4.61  . . 168 2754 100.00 . . . . 0.1283 . . . . . . . . . . . 0.1431 
'X-RAY DIFFRACTION' 4.61 19.69 . . 161 2898 99.93  . . . . 0.1616 . . . . . . . . . . . 0.1646 
# 
_struct.entry_id                     9F7Y 
_struct.title                        'SARS-CoV-2 papain-like protease (PLpro) C112S-K191D-Q222D-K229R-Q230R-C271S mutant' 
_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        9F7Y 
_struct_keywords.text            'Protease, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
J N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFL
GRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVG
ELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESP
FVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVT
;
_struct_ref.pdbx_align_begin           1564 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9F7Y 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 319 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  1564 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1881 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       319 
# 
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 9F7Y MET A 1   ? UNP P0DTD1 ?   ?    'initiating methionine' 1   1  
1 9F7Y SER A 112 ? UNP P0DTD1 CYS 1674 'engineered mutation'   112 2  
1 9F7Y ASP A 191 ? UNP P0DTD1 LYS 1753 'engineered mutation'   191 3  
1 9F7Y ASP A 222 ? UNP P0DTD1 GLN 1784 'engineered mutation'   222 4  
1 9F7Y ARG A 229 ? UNP P0DTD1 LYS 1791 'engineered mutation'   229 5  
1 9F7Y ARG A 230 ? UNP P0DTD1 GLN 1792 'engineered mutation'   230 6  
1 9F7Y SER A 271 ? UNP P0DTD1 CYS 1833 'engineered mutation'   271 7  
1 9F7Y HIS A 320 ? UNP P0DTD1 ?   ?    'expression tag'        320 8  
1 9F7Y HIS A 321 ? UNP P0DTD1 ?   ?    'expression tag'        321 9  
1 9F7Y HIS A 322 ? UNP P0DTD1 ?   ?    'expression tag'        322 10 
1 9F7Y HIS A 323 ? UNP P0DTD1 ?   ?    'expression tag'        323 11 
1 9F7Y HIS A 324 ? UNP P0DTD1 ?   ?    'expression tag'        324 12 
1 9F7Y HIS A 325 ? UNP P0DTD1 ?   ?    'expression tag'        325 13 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 1210  ? 
1 MORE         -58   ? 
1 'SSA (A^2)'  15360 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_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 THR A 27  ? GLY A 33  ? THR A 27  GLY A 33  1 ? 7  
HELX_P HELX_P2  AA2 HIS A 48  ? GLU A 52  ? HIS A 48  GLU A 52  5 ? 5  
HELX_P HELX_P3  AA3 ASP A 62  ? HIS A 74  ? ASP A 62  HIS A 74  1 ? 13 
HELX_P HELX_P4  AA4 SER A 79  ? LYS A 92  ? SER A 79  LYS A 92  1 ? 14 
HELX_P HELX_P5  AA5 ASN A 111 ? GLN A 122 ? ASN A 111 GLN A 122 1 ? 12 
HELX_P HELX_P6  AA6 PRO A 130 ? ALA A 142 ? PRO A 130 ALA A 142 1 ? 13 
HELX_P HELX_P7  AA7 ALA A 145 ? ASN A 157 ? ALA A 145 ASN A 157 1 ? 13 
HELX_P HELX_P8  AA8 ASP A 165 ? HIS A 176 ? ASP A 165 HIS A 176 1 ? 12 
HELX_P HELX_P9  AA9 GLY A 202 ? VAL A 206 ? GLY A 202 VAL A 206 1 ? 5  
HELX_P HELX_P10 AB1 SER A 213 ? GLY A 220 ? SER A 213 GLY A 220 1 ? 8  
HELX_P HELX_P11 AB2 LYS A 316 ? HIS A 323 ? LYS A 316 HIS A 323 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A LEU 121 O  ? ? ? 1_555 E NA  . NA ? ? A LEU 121 A NA  404 1_555 ? ? ? ? ? ? ? 2.381 ? ? 
metalc2  metalc ? ? A ILE 124 O  ? ? ? 1_555 E NA  . NA ? ? A ILE 124 A NA  404 1_555 ? ? ? ? ? ? ? 2.257 ? ? 
metalc3  metalc ? ? A ARG 141 O  ? ? ? 1_555 G NA  . NA ? ? A ARG 141 A NA  406 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc4  metalc ? ? A ALA 177 O  ? ? ? 1_555 F NA  . NA ? ? A ALA 177 A NA  405 1_555 ? ? ? ? ? ? ? 2.482 ? ? 
metalc5  metalc ? ? A CYS 190 SG ? ? ? 1_555 B ZN  . ZN ? ? A CYS 190 A ZN  401 1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc6  metalc ? ? A CYS 193 SG ? ? ? 1_555 B ZN  . ZN ? ? A CYS 193 A ZN  401 1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc7  metalc ? ? A CYS 225 SG ? ? ? 1_555 B ZN  . ZN ? ? A CYS 225 A ZN  401 1_555 ? ? ? ? ? ? ? 2.365 ? ? 
metalc8  metalc ? ? A CYS 227 SG ? ? ? 1_555 B ZN  . ZN ? ? A CYS 227 A ZN  401 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc9  metalc ? ? E NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  404 A HOH 566 1_555 ? ? ? ? ? ? ? 2.439 ? ? 
metalc10 metalc ? ? E NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  404 A HOH 693 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
metalc11 metalc ? ? E NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  404 A HOH 709 1_555 ? ? ? ? ? ? ? 2.480 ? ? 
metalc12 metalc ? ? E NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  404 A HOH 731 1_555 ? ? ? ? ? ? ? 2.600 ? ? 
metalc13 metalc ? ? F NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  405 A HOH 504 6_555 ? ? ? ? ? ? ? 2.429 ? ? 
metalc14 metalc ? ? F NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  405 A HOH 534 1_555 ? ? ? ? ? ? ? 2.529 ? ? 
metalc15 metalc ? ? F NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  405 A HOH 551 1_555 ? ? ? ? ? ? ? 2.285 ? ? 
metalc16 metalc ? ? F NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  405 A HOH 621 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc17 metalc ? ? F NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  405 A HOH 632 1_555 ? ? ? ? ? ? ? 2.642 ? ? 
metalc18 metalc ? ? G NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  406 A HOH 501 1_555 ? ? ? ? ? ? ? 2.554 ? ? 
metalc19 metalc ? ? G NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  406 A HOH 555 1_555 ? ? ? ? ? ? ? 2.412 ? ? 
metalc20 metalc ? ? G NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  406 A HOH 609 1_555 ? ? ? ? ? ? ? 2.529 ? ? 
metalc21 metalc ? ? G NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  406 A HOH 735 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc22 metalc ? ? G NA  .   NA ? ? ? 1_555 J HOH . O  ? ? A NA  406 A HOH 736 1_555 ? ? ? ? ? ? ? 2.908 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O  ? A LEU 121 ? A LEU 121 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? A ILE 124 ? A ILE 124 ? 1_555 88.0  ? 
2  O  ? A LEU 121 ? A LEU 121 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 566 ? 1_555 97.4  ? 
3  O  ? A ILE 124 ? A ILE 124 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 566 ? 1_555 160.1 ? 
4  O  ? A LEU 121 ? A LEU 121 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 693 ? 1_555 86.9  ? 
5  O  ? A ILE 124 ? A ILE 124 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 693 ? 1_555 106.8 ? 
6  O  ? J HOH .   ? A HOH 566 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 693 ? 1_555 92.7  ? 
7  O  ? A LEU 121 ? A LEU 121 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 709 ? 1_555 98.0  ? 
8  O  ? A ILE 124 ? A ILE 124 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 709 ? 1_555 81.1  ? 
9  O  ? J HOH .   ? A HOH 566 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 709 ? 1_555 79.2  ? 
10 O  ? J HOH .   ? A HOH 693 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 709 ? 1_555 171.0 ? 
11 O  ? A LEU 121 ? A LEU 121 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 731 ? 1_555 166.3 ? 
12 O  ? A ILE 124 ? A ILE 124 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 731 ? 1_555 85.1  ? 
13 O  ? J HOH .   ? A HOH 566 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 731 ? 1_555 93.1  ? 
14 O  ? J HOH .   ? A HOH 693 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 731 ? 1_555 83.8  ? 
15 O  ? J HOH .   ? A HOH 709 ? 1_555 NA ? E NA . ? A NA 404 ? 1_555 O  ? J HOH .   ? A HOH 731 ? 1_555 92.7  ? 
16 O  ? A ARG 141 ? A ARG 141 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 501 ? 1_555 153.6 ? 
17 O  ? A ARG 141 ? A ARG 141 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 555 ? 1_555 80.1  ? 
18 O  ? J HOH .   ? A HOH 501 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 555 ? 1_555 73.5  ? 
19 O  ? A ARG 141 ? A ARG 141 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 609 ? 1_555 103.5 ? 
20 O  ? J HOH .   ? A HOH 501 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 609 ? 1_555 73.8  ? 
21 O  ? J HOH .   ? A HOH 555 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 609 ? 1_555 85.1  ? 
22 O  ? A ARG 141 ? A ARG 141 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 735 ? 1_555 105.8 ? 
23 O  ? J HOH .   ? A HOH 501 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 735 ? 1_555 100.7 ? 
24 O  ? J HOH .   ? A HOH 555 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 735 ? 1_555 173.4 ? 
25 O  ? J HOH .   ? A HOH 609 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 735 ? 1_555 96.4  ? 
26 O  ? A ARG 141 ? A ARG 141 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 736 ? 1_555 71.1  ? 
27 O  ? J HOH .   ? A HOH 501 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 736 ? 1_555 102.7 ? 
28 O  ? J HOH .   ? A HOH 555 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 736 ? 1_555 76.3  ? 
29 O  ? J HOH .   ? A HOH 609 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 736 ? 1_555 161.2 ? 
30 O  ? J HOH .   ? A HOH 735 ? 1_555 NA ? G NA . ? A NA 406 ? 1_555 O  ? J HOH .   ? A HOH 736 ? 1_555 102.4 ? 
31 O  ? A ALA 177 ? A ALA 177 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 504 ? 6_555 173.0 ? 
32 O  ? A ALA 177 ? A ALA 177 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 534 ? 1_555 89.2  ? 
33 O  ? J HOH .   ? A HOH 504 ? 6_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 534 ? 1_555 89.7  ? 
34 O  ? A ALA 177 ? A ALA 177 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 551 ? 1_555 91.3  ? 
35 O  ? J HOH .   ? A HOH 504 ? 6_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 551 ? 1_555 91.0  ? 
36 O  ? J HOH .   ? A HOH 534 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 551 ? 1_555 169.9 ? 
37 O  ? A ALA 177 ? A ALA 177 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 621 ? 1_555 81.0  ? 
38 O  ? J HOH .   ? A HOH 504 ? 6_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 621 ? 1_555 92.1  ? 
39 O  ? J HOH .   ? A HOH 534 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 621 ? 1_555 77.9  ? 
40 O  ? J HOH .   ? A HOH 551 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 621 ? 1_555 112.2 ? 
41 O  ? A ALA 177 ? A ALA 177 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 632 ? 1_555 86.9  ? 
42 O  ? J HOH .   ? A HOH 504 ? 6_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 632 ? 1_555 99.8  ? 
43 O  ? J HOH .   ? A HOH 534 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 632 ? 1_555 82.4  ? 
44 O  ? J HOH .   ? A HOH 551 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 632 ? 1_555 87.5  ? 
45 O  ? J HOH .   ? A HOH 621 ? 1_555 NA ? F NA . ? A NA 405 ? 1_555 O  ? J HOH .   ? A HOH 632 ? 1_555 156.9 ? 
46 SG ? A CYS 190 ? A CYS 190 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 SG ? A CYS 193 ? A CYS 193 ? 1_555 113.0 ? 
47 SG ? A CYS 190 ? A CYS 190 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 SG ? A CYS 225 ? A CYS 225 ? 1_555 114.0 ? 
48 SG ? A CYS 193 ? A CYS 193 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 SG ? A CYS 225 ? A CYS 225 ? 1_555 104.2 ? 
49 SG ? A CYS 190 ? A CYS 190 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 SG ? A CYS 227 ? A CYS 227 ? 1_555 106.4 ? 
50 SG ? A CYS 193 ? A CYS 193 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 SG ? A CYS 227 ? A CYS 227 ? 1_555 110.2 ? 
51 SG ? A CYS 225 ? A CYS 225 ? 1_555 ZN ? B ZN . ? A ZN 401 ? 1_555 SG ? A CYS 227 ? A CYS 227 ? 1_555 109.1 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? 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 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? 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 HIS A 18  ? ASP A 23  ? HIS A 18  ASP A 23  
AA1 2 THR A 5   ? THR A 11  ? THR A 5   THR A 11  
AA1 3 THR A 55  ? VAL A 58  ? THR A 55  VAL A 58  
AA1 4 THR A 35  ? LEU A 37  ? THR A 35  LEU A 37  
AA1 5 ALA A 40  ? ASP A 41  ? ALA A 40  ASP A 41  
AA2 1 GLN A 98  ? VAL A 99  ? GLN A 98  VAL A 99  
AA2 2 LEU A 102 ? THR A 103 ? LEU A 102 THR A 103 
AA3 1 GLY A 194 ? LYS A 201 ? GLY A 194 LYS A 201 
AA3 2 LYS A 183 ? CYS A 190 ? LYS A 183 CYS A 190 
AA3 3 ARG A 230 ? GLU A 239 ? ARG A 230 GLU A 239 
AA3 4 VAL A 221 ? PRO A 224 ? VAL A 221 PRO A 224 
AA4 1 GLY A 194 ? LYS A 201 ? GLY A 194 LYS A 201 
AA4 2 LYS A 183 ? CYS A 190 ? LYS A 183 CYS A 190 
AA4 3 ARG A 230 ? GLU A 239 ? ARG A 230 GLU A 239 
AA4 4 SER A 310 ? THR A 312 ? SER A 310 THR A 312 
AA5 1 MET A 207 ? MET A 209 ? MET A 207 MET A 209 
AA5 2 PHE A 242 ? LEU A 254 ? PHE A 242 LEU A 254 
AA5 3 TYR A 297 ? LYS A 307 ? TYR A 297 LYS A 307 
AA5 4 CYS A 261 ? GLY A 267 ? CYS A 261 GLY A 267 
AA5 5 GLY A 272 ? SER A 279 ? GLY A 272 SER A 279 
AA5 6 LEU A 283 ? ASP A 287 ? LEU A 283 ASP A 287 
AA5 7 LEU A 290 ? SER A 294 ? LEU A 290 SER A 294 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLN A 20  ? O GLN A 20  N VAL A 8   ? N VAL A 8   
AA1 2 3 N PHE A 9   ? N PHE A 9   O PHE A 56  ? O PHE A 56  
AA1 3 4 O TYR A 57  ? O TYR A 57  N TYR A 36  ? N TYR A 36  
AA1 4 5 N LEU A 37  ? N LEU A 37  O ALA A 40  ? O ALA A 40  
AA2 1 2 N VAL A 99  ? N VAL A 99  O LEU A 102 ? O LEU A 102 
AA3 1 2 O THR A 198 ? O THR A 198 N LEU A 186 ? N LEU A 186 
AA3 2 3 N VAL A 185 ? N VAL A 185 O VAL A 236 ? O VAL A 236 
AA3 3 4 O LYS A 233 ? O LYS A 233 N VAL A 221 ? N VAL A 221 
AA4 1 2 O THR A 198 ? O THR A 198 N LEU A 186 ? N LEU A 186 
AA4 2 3 N VAL A 185 ? N VAL A 185 O VAL A 236 ? O VAL A 236 
AA4 3 4 N GLN A 238 ? N GLN A 238 O TYR A 311 ? O TYR A 311 
AA5 1 2 N TYR A 208 ? N TYR A 208 O SER A 246 ? O SER A 246 
AA5 2 3 N MET A 245 ? N MET A 245 O VAL A 304 ? O VAL A 304 
AA5 3 4 O PHE A 305 ? O PHE A 305 N CYS A 261 ? N CYS A 261 
AA5 4 5 N GLU A 264 ? N GLU A 264 O LYS A 275 ? O LYS A 275 
AA5 5 6 N HIS A 276 ? N HIS A 276 O ILE A 286 ? O ILE A 286 
AA5 6 7 N CYS A 285 ? N CYS A 285 O THR A 292 ? O THR A 292 
# 
_pdbx_entry_details.entry_id                   9F7Y 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 ILE A 15  ? ? -120.64 -58.66  
2 1 PRO A 60  ? ? -69.20  93.40   
3 1 SER A 104 ? ? -109.90 -169.55 
4 1 LYS A 280 ? ? -122.53 -127.31 
5 1 ASN A 309 ? A -138.41 -71.33  
6 1 ASN A 309 ? B -143.69 -70.20  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+2/3   
3 -x+y,-x,z+1/3  
4 x-y,-y,-z+1/3  
5 -x,-x+y,-z+2/3 
6 y,x,-z         
# 
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 -43.4939883139 35.503532709  61.4952587308 0.246659725244 ? -0.045303641633 ? 0.107809222475   ? 
0.215717446793 ? -0.0262869856078 ? 0.283113662208 ? 0.185394786154 ? 0.140252708785  ? -0.3200231911    ? 0.344014776383  ? 
0.0837880417249  ? 0.114453166146  ? 0.154322047001  ? -0.0324532640402 ? 0.148486933036   ? -0.0269533536548 ? -0.0348916617321 ? 
0.0543411479705   ? 0.150728887357   ? 0.0578964102132  ? -4.2810605247e-08  ? 
2 'X-RAY DIFFRACTION' ? refined -30.8554409823 27.7196606616 41.7856340502 0.198691120428 ? 0.016668540944  ? 0.00444369369616 ? 
0.205068687444 ? 0.0117117953486  ? 0.189347954081 ? 0.280490181086 ? 0.0474913336454 ? -0.0240979940307 ? -0.347607822957 ? 
-0.0306981446529 ? 0.514665037206  ? 0.118191613201  ? 0.0456409628464  ? 0.0329339094806  ? 0.0478612907189  ? -0.0478654987837 ? 
-0.00416649725158 ? 0.0245232060873  ? -0.0105407323104 ? 1.75240235636e-09  ? 
3 'X-RAY DIFFRACTION' ? refined -9.83271983708 22.735060369  27.3312230429 0.145015071587 ? 0.0389896024563 ? -0.0384573121285 ? 
0.226042665361 ? -0.0323856132554 ? 0.219161106563 ? 0.685372061885 ? 0.0551820532241 ? -0.0565562176173 ? 0.282278272742  ? 
-0.543141506577  ? -0.33185323907  ? -0.031094879385 ? 0.136682595697   ? -0.0672363559288 ? 0.138375165555   ? -0.048152281091  ? 
-0.121047576555   ? -0.0455117633642 ? -0.104934293454  ? 8.69095645769e-09  ? 
4 'X-RAY DIFFRACTION' ? refined -20.1230639274 20.2438427784 21.4278814767 0.154997383416 ? 0.0206644600075 ? -0.0258179250957 ? 
0.309871803523 ? -0.0544362939781 ? 0.197767026846 ? 0.199051525739 ? 0.330792601213  ? -0.0668892623407 ? 0.0372667173725 ? 
-0.253282927953  ? -0.262288216143 ? -0.14234447065  ? 0.155962613129   ? -0.0927007619651 ? 0.0402099938298  ? 0.172664778222   ? 
-0.0793895867806  ? -0.0885970754145 ? -0.0553301738746 ? -6.06413343707e-09 ? 
# 
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 A 1   A 2   ? A 61  A 62  ? ? 
;chain 'A' and (resid 2 through 62 )
;
2 'X-RAY DIFFRACTION' 2 A 62  A 63  ? A 175 A 176 ? ? 
;chain 'A' and (resid 63 through 176 )
;
3 'X-RAY DIFFRACTION' 3 A 176 A 177 ? A 270 A 271 ? ? 
;chain 'A' and (resid 177 through 271 )
;
4 'X-RAY DIFFRACTION' 4 A 271 A 272 ? A 323 A 324 ? ? 
;chain 'A' and (resid 272 through 324 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       827 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.96 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 1   ? A MET 1   
2 1 Y 1 A HIS 325 ? A HIS 325 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
MLA C1   C  N N 251 
MLA O1A  O  N N 252 
MLA O1B  O  N N 253 
MLA C2   C  N N 254 
MLA C3   C  N N 255 
MLA O3A  O  N N 256 
MLA O3B  O  N N 257 
MLA H1A  H  N N 258 
MLA HC21 H  N N 259 
MLA HC22 H  N N 260 
MLA H3B  H  N N 261 
NA  NA   NA N N 262 
PHE N    N  N N 263 
PHE CA   C  N S 264 
PHE C    C  N N 265 
PHE O    O  N N 266 
PHE CB   C  N N 267 
PHE CG   C  Y N 268 
PHE CD1  C  Y N 269 
PHE CD2  C  Y N 270 
PHE CE1  C  Y N 271 
PHE CE2  C  Y N 272 
PHE CZ   C  Y N 273 
PHE OXT  O  N N 274 
PHE H    H  N N 275 
PHE H2   H  N N 276 
PHE HA   H  N N 277 
PHE HB2  H  N N 278 
PHE HB3  H  N N 279 
PHE HD1  H  N N 280 
PHE HD2  H  N N 281 
PHE HE1  H  N N 282 
PHE HE2  H  N N 283 
PHE HZ   H  N N 284 
PHE HXT  H  N N 285 
PRO N    N  N N 286 
PRO CA   C  N S 287 
PRO C    C  N N 288 
PRO O    O  N N 289 
PRO CB   C  N N 290 
PRO CG   C  N N 291 
PRO CD   C  N N 292 
PRO OXT  O  N N 293 
PRO H    H  N N 294 
PRO HA   H  N N 295 
PRO HB2  H  N N 296 
PRO HB3  H  N N 297 
PRO HG2  H  N N 298 
PRO HG3  H  N N 299 
PRO HD2  H  N N 300 
PRO HD3  H  N N 301 
PRO HXT  H  N N 302 
SER N    N  N N 303 
SER CA   C  N S 304 
SER C    C  N N 305 
SER O    O  N N 306 
SER CB   C  N N 307 
SER OG   O  N N 308 
SER OXT  O  N N 309 
SER H    H  N N 310 
SER H2   H  N N 311 
SER HA   H  N N 312 
SER HB2  H  N N 313 
SER HB3  H  N N 314 
SER HG   H  N N 315 
SER HXT  H  N N 316 
THR N    N  N N 317 
THR CA   C  N S 318 
THR C    C  N N 319 
THR O    O  N N 320 
THR CB   C  N R 321 
THR OG1  O  N N 322 
THR CG2  C  N N 323 
THR OXT  O  N N 324 
THR H    H  N N 325 
THR H2   H  N N 326 
THR HA   H  N N 327 
THR HB   H  N N 328 
THR HG1  H  N N 329 
THR HG21 H  N N 330 
THR HG22 H  N N 331 
THR HG23 H  N N 332 
THR HXT  H  N N 333 
TRP N    N  N N 334 
TRP CA   C  N S 335 
TRP C    C  N N 336 
TRP O    O  N N 337 
TRP CB   C  N N 338 
TRP CG   C  Y N 339 
TRP CD1  C  Y N 340 
TRP CD2  C  Y N 341 
TRP NE1  N  Y N 342 
TRP CE2  C  Y N 343 
TRP CE3  C  Y N 344 
TRP CZ2  C  Y N 345 
TRP CZ3  C  Y N 346 
TRP CH2  C  Y N 347 
TRP OXT  O  N N 348 
TRP H    H  N N 349 
TRP H2   H  N N 350 
TRP HA   H  N N 351 
TRP HB2  H  N N 352 
TRP HB3  H  N N 353 
TRP HD1  H  N N 354 
TRP HE1  H  N N 355 
TRP HE3  H  N N 356 
TRP HZ2  H  N N 357 
TRP HZ3  H  N N 358 
TRP HH2  H  N N 359 
TRP HXT  H  N N 360 
TYR N    N  N N 361 
TYR CA   C  N S 362 
TYR C    C  N N 363 
TYR O    O  N N 364 
TYR CB   C  N N 365 
TYR CG   C  Y N 366 
TYR CD1  C  Y N 367 
TYR CD2  C  Y N 368 
TYR CE1  C  Y N 369 
TYR CE2  C  Y N 370 
TYR CZ   C  Y N 371 
TYR OH   O  N N 372 
TYR OXT  O  N N 373 
TYR H    H  N N 374 
TYR H2   H  N N 375 
TYR HA   H  N N 376 
TYR HB2  H  N N 377 
TYR HB3  H  N N 378 
TYR HD1  H  N N 379 
TYR HD2  H  N N 380 
TYR HE1  H  N N 381 
TYR HE2  H  N N 382 
TYR HH   H  N N 383 
TYR HXT  H  N N 384 
VAL N    N  N N 385 
VAL CA   C  N S 386 
VAL C    C  N N 387 
VAL O    O  N N 388 
VAL CB   C  N N 389 
VAL CG1  C  N N 390 
VAL CG2  C  N N 391 
VAL OXT  O  N N 392 
VAL H    H  N N 393 
VAL H2   H  N N 394 
VAL HA   H  N N 395 
VAL HB   H  N N 396 
VAL HG11 H  N N 397 
VAL HG12 H  N N 398 
VAL HG13 H  N N 399 
VAL HG21 H  N N 400 
VAL HG22 H  N N 401 
VAL HG23 H  N N 402 
VAL HXT  H  N N 403 
ZN  ZN   ZN N N 404 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
MLA C1  O1A  sing N N 237 
MLA C1  O1B  doub N N 238 
MLA C1  C2   sing N N 239 
MLA O1A H1A  sing N N 240 
MLA C2  C3   sing N N 241 
MLA C2  HC21 sing N N 242 
MLA C2  HC22 sing N N 243 
MLA C3  O3A  doub N N 244 
MLA C3  O3B  sing N N 245 
MLA O3B H3B  sing N N 246 
PHE N   CA   sing N N 247 
PHE N   H    sing N N 248 
PHE N   H2   sing N N 249 
PHE CA  C    sing N N 250 
PHE CA  CB   sing N N 251 
PHE CA  HA   sing N N 252 
PHE C   O    doub N N 253 
PHE C   OXT  sing N N 254 
PHE CB  CG   sing N N 255 
PHE CB  HB2  sing N N 256 
PHE CB  HB3  sing N N 257 
PHE CG  CD1  doub Y N 258 
PHE CG  CD2  sing Y N 259 
PHE CD1 CE1  sing Y N 260 
PHE CD1 HD1  sing N N 261 
PHE CD2 CE2  doub Y N 262 
PHE CD2 HD2  sing N N 263 
PHE CE1 CZ   doub Y N 264 
PHE CE1 HE1  sing N N 265 
PHE CE2 CZ   sing Y N 266 
PHE CE2 HE2  sing N N 267 
PHE CZ  HZ   sing N N 268 
PHE OXT HXT  sing N N 269 
PRO N   CA   sing N N 270 
PRO N   CD   sing N N 271 
PRO N   H    sing N N 272 
PRO CA  C    sing N N 273 
PRO CA  CB   sing N N 274 
PRO CA  HA   sing N N 275 
PRO C   O    doub N N 276 
PRO C   OXT  sing N N 277 
PRO CB  CG   sing N N 278 
PRO CB  HB2  sing N N 279 
PRO CB  HB3  sing N N 280 
PRO CG  CD   sing N N 281 
PRO CG  HG2  sing N N 282 
PRO CG  HG3  sing N N 283 
PRO CD  HD2  sing N N 284 
PRO CD  HD3  sing N N 285 
PRO OXT HXT  sing N N 286 
SER N   CA   sing N N 287 
SER N   H    sing N N 288 
SER N   H2   sing N N 289 
SER CA  C    sing N N 290 
SER CA  CB   sing N N 291 
SER CA  HA   sing N N 292 
SER C   O    doub N N 293 
SER C   OXT  sing N N 294 
SER CB  OG   sing N N 295 
SER CB  HB2  sing N N 296 
SER CB  HB3  sing N N 297 
SER OG  HG   sing N N 298 
SER OXT HXT  sing N N 299 
THR N   CA   sing N N 300 
THR N   H    sing N N 301 
THR N   H2   sing N N 302 
THR CA  C    sing N N 303 
THR CA  CB   sing N N 304 
THR CA  HA   sing N N 305 
THR C   O    doub N N 306 
THR C   OXT  sing N N 307 
THR CB  OG1  sing N N 308 
THR CB  CG2  sing N N 309 
THR CB  HB   sing N N 310 
THR OG1 HG1  sing N N 311 
THR CG2 HG21 sing N N 312 
THR CG2 HG22 sing N N 313 
THR CG2 HG23 sing N N 314 
THR OXT HXT  sing N N 315 
TRP N   CA   sing N N 316 
TRP N   H    sing N N 317 
TRP N   H2   sing N N 318 
TRP CA  C    sing N N 319 
TRP CA  CB   sing N N 320 
TRP CA  HA   sing N N 321 
TRP C   O    doub N N 322 
TRP C   OXT  sing N N 323 
TRP CB  CG   sing N N 324 
TRP CB  HB2  sing N N 325 
TRP CB  HB3  sing N N 326 
TRP CG  CD1  doub Y N 327 
TRP CG  CD2  sing Y N 328 
TRP CD1 NE1  sing Y N 329 
TRP CD1 HD1  sing N N 330 
TRP CD2 CE2  doub Y N 331 
TRP CD2 CE3  sing Y N 332 
TRP NE1 CE2  sing Y N 333 
TRP NE1 HE1  sing N N 334 
TRP CE2 CZ2  sing Y N 335 
TRP CE3 CZ3  doub Y N 336 
TRP CE3 HE3  sing N N 337 
TRP CZ2 CH2  doub Y N 338 
TRP CZ2 HZ2  sing N N 339 
TRP CZ3 CH2  sing Y N 340 
TRP CZ3 HZ3  sing N N 341 
TRP CH2 HH2  sing N N 342 
TRP OXT HXT  sing N N 343 
TYR N   CA   sing N N 344 
TYR N   H    sing N N 345 
TYR N   H2   sing N N 346 
TYR CA  C    sing N N 347 
TYR CA  CB   sing N N 348 
TYR CA  HA   sing N N 349 
TYR C   O    doub N N 350 
TYR C   OXT  sing N N 351 
TYR CB  CG   sing N N 352 
TYR CB  HB2  sing N N 353 
TYR CB  HB3  sing N N 354 
TYR CG  CD1  doub Y N 355 
TYR CG  CD2  sing Y N 356 
TYR CD1 CE1  sing Y N 357 
TYR CD1 HD1  sing N N 358 
TYR CD2 CE2  doub Y N 359 
TYR CD2 HD2  sing N N 360 
TYR CE1 CZ   doub Y N 361 
TYR CE1 HE1  sing N N 362 
TYR CE2 CZ   sing Y N 363 
TYR CE2 HE2  sing N N 364 
TYR CZ  OH   sing N N 365 
TYR OH  HH   sing N N 366 
TYR OXT HXT  sing N N 367 
VAL N   CA   sing N N 368 
VAL N   H    sing N N 369 
VAL N   H2   sing N N 370 
VAL CA  C    sing N N 371 
VAL CA  CB   sing N N 372 
VAL CA  HA   sing N N 373 
VAL C   O    doub N N 374 
VAL C   OXT  sing N N 375 
VAL CB  CG1  sing N N 376 
VAL CB  CG2  sing N N 377 
VAL CB  HB   sing N N 378 
VAL CG1 HG11 sing N N 379 
VAL CG1 HG12 sing N N 380 
VAL CG1 HG13 sing N N 381 
VAL CG2 HG21 sing N N 382 
VAL CG2 HG22 sing N N 383 
VAL CG2 HG23 sing N N 384 
VAL OXT HXT  sing N N 385 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                Spain 
_pdbx_audit_support.grant_number           P20_00149 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7d6h 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 32 2 1' 
_space_group.name_Hall        
;P 32 2"
;
_space_group.IT_number        154 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9F7Y 
_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]   0.012275 
_atom_sites.fract_transf_matrix[1][2]   0.007087 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014174 
_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]   0.007411 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345  0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? 9.38062  1.54875 ? ? 3.38349  72.32734 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . GLU A 1 2   ? -55.52600 45.58500 75.39300 1.000 70.58778  ? 2   GLU A N    1 
ATOM   2    C  CA   . GLU A 1 2   ? -55.53800 44.13000 75.30400 1.000 83.60546  ? 2   GLU A CA   1 
ATOM   3    C  C    . GLU A 1 2   ? -54.51900 43.63500 74.28000 1.000 72.76304  ? 2   GLU A C    1 
ATOM   4    O  O    . GLU A 1 2   ? -54.44200 44.18000 73.17800 1.000 70.01114  ? 2   GLU A O    1 
ATOM   5    C  CB   . GLU A 1 2   ? -56.92900 43.62500 74.92500 1.000 80.17907  ? 2   GLU A CB   1 
ATOM   6    C  CG   . GLU A 1 2   ? -57.10100 42.12500 75.12400 1.000 88.42981  ? 2   GLU A CG   1 
ATOM   7    C  CD   . GLU A 1 2   ? -58.54400 41.72800 75.37700 1.000 80.36983  ? 2   GLU A CD   1 
ATOM   8    O  OE1  . GLU A 1 2   ? -59.36500 41.89800 74.45300 1.000 71.39598  ? 2   GLU A OE1  1 
ATOM   9    O  OE2  . GLU A 1 2   ? -58.85700 41.25600 76.49500 1.000 78.10351  ? 2   GLU A OE2  1 
ATOM   10   H  HA   . GLU A 1 2   ? -55.30400 43.76400 76.17200 1.000 91.81558  ? 2   GLU A HA   1 
ATOM   11   H  HB2  . GLU A 1 2   ? -57.58700 44.07700 75.47600 1.000 87.92558  ? 2   GLU A HB2  1 
ATOM   12   H  HB3  . GLU A 1 2   ? -57.08900 43.82200 73.98900 1.000 87.92558  ? 2   GLU A HB3  1 
ATOM   13   H  HG2  . GLU A 1 2   ? -56.79900 41.66300 74.32700 1.000 98.30558  ? 2   GLU A HG2  1 
ATOM   14   H  HG3  . GLU A 1 2   ? -56.57500 41.84500 75.89000 1.000 98.30558  ? 2   GLU A HG3  1 
ATOM   15   N  N    . VAL A 1 3   ? -53.75700 42.59900 74.63200 1.000 57.93269  ? 3   VAL A N    1 
ATOM   16   C  CA   . VAL A 1 3   ? -52.71800 42.05600 73.75400 1.000 75.50697  ? 3   VAL A CA   1 
ATOM   17   C  C    . VAL A 1 3   ? -53.29200 40.87300 72.98400 1.000 67.80717  ? 3   VAL A C    1 
ATOM   18   O  O    . VAL A 1 3   ? -53.73400 39.88400 73.58000 1.000 65.35853  ? 3   VAL A O    1 
ATOM   19   C  CB   . VAL A 1 3   ? -51.46700 41.63400 74.54300 1.000 66.11529  ? 3   VAL A CB   1 
ATOM   20   C  CG1  . VAL A 1 3   ? -50.55700 40.77900 73.67100 1.000 60.03012  ? 3   VAL A CG1  1 
ATOM   21   C  CG2  . VAL A 1 3   ? -50.72300 42.85500 75.05100 1.000 83.56831  ? 3   VAL A CG2  1 
ATOM   22   H  H    . VAL A 1 3   ? -53.82400 42.18800 75.38400 1.000 62.02558  ? 3   VAL A H    1 
ATOM   23   H  HA   . VAL A 1 3   ? -52.46600 42.74200 73.11600 1.000 83.76558  ? 3   VAL A HA   1 
ATOM   24   H  HB   . VAL A 1 3   ? -51.74000 41.10700 75.31000 1.000 72.23558  ? 3   VAL A HB   1 
ATOM   25   H  HG11 . VAL A 1 3   ? -49.66500 40.77700 74.05200 1.000 65.61558  ? 3   VAL A HG11 1 
ATOM   26   H  HG12 . VAL A 1 3   ? -50.90700 39.87500 73.64100 1.000 65.61558  ? 3   VAL A HG12 1 
ATOM   27   H  HG13 . VAL A 1 3   ? -50.53400 41.15400 72.77700 1.000 65.61558  ? 3   VAL A HG13 1 
ATOM   28   H  HG21 . VAL A 1 3   ? -49.94900 42.56400 75.55900 1.000 92.45558  ? 3   VAL A HG21 1 
ATOM   29   H  HG22 . VAL A 1 3   ? -50.43900 43.39000 74.29400 1.000 92.45558  ? 3   VAL A HG22 1 
ATOM   30   H  HG23 . VAL A 1 3   ? -51.31600 43.37300 75.61900 1.000 92.45558  ? 3   VAL A HG23 1 
ATOM   31   N  N    . ARG A 1 4   ? -53.27400 40.96800 71.66000 1.000 58.11684  ? 4   ARG A N    1 
ATOM   32   C  CA   . ARG A 1 4   ? -53.74300 39.90800 70.78500 1.000 46.85034  ? 4   ARG A CA   1 
ATOM   33   C  C    . ARG A 1 4   ? -52.53700 39.22100 70.15400 1.000 45.67269  ? 4   ARG A C    1 
ATOM   34   O  O    . ARG A 1 4   ? -51.55800 39.88100 69.79100 1.000 43.74912  ? 4   ARG A O    1 
ATOM   35   C  CB   . ARG A 1 4   ? -54.67200 40.47300 69.71000 1.000 53.47528  ? 4   ARG A CB   1 
ATOM   36   H  H    . ARG A 1 4   ? -52.98600 41.65800 71.23600 1.000 64.17558  ? 4   ARG A H    1 
ATOM   37   H  HA   . ARG A 1 4   ? -54.24200 39.24300 71.28500 1.000 51.31558  ? 4   ARG A HA   1 
ATOM   38   N  N    . THR A 1 5   ? -52.59500 37.89500 70.04900 1.000 44.99541  ? 5   THR A N    1 
ATOM   39   C  CA   . THR A 1 5   ? -51.48600 37.13500 69.49200 1.000 42.77217  ? 5   THR A CA   1 
ATOM   40   C  C    . THR A 1 5   ? -52.00100 36.05200 68.55900 1.000 40.07300  ? 5   THR A C    1 
ATOM   41   O  O    . THR A 1 5   ? -53.16600 35.65100 68.61700 1.000 42.49214  ? 5   THR A O    1 
ATOM   42   C  CB   . THR A 1 5   ? -50.63700 36.47400 70.58600 1.000 55.48222  ? 5   THR A CB   1 
ATOM   43   O  OG1  . THR A 1 5   ? -51.40500 35.45400 71.23600 1.000 50.13941  ? 5   THR A OG1  1 
ATOM   44   C  CG2  . THR A 1 5   ? -50.19000 37.50300 71.60600 1.000 57.49497  ? 5   THR A CG2  1 
ATOM   45   H  H    . THR A 1 5   ? -53.26700 37.41600 70.29400 1.000 50.02558  ? 5   THR A H    1 
ATOM   46   H  HA   . THR A 1 5   ? -50.93500 37.74800 68.98100 1.000 47.81558  ? 5   THR A HA   1 
ATOM   47   H  HB   . THR A 1 5   ? -49.84600 36.07700 70.18900 1.000 62.77558  ? 5   THR A HB   1 
ATOM   48   H  HG1  . THR A 1 5   ? -50.94100 35.07900 71.82800 1.000 56.32558  ? 5   THR A HG1  1 
ATOM   49   H  HG21 . THR A 1 5   ? -49.59600 37.09100 72.25300 1.000 64.47558  ? 5   THR A HG21 1 
ATOM   50   H  HG22 . THR A 1 5   ? -49.72000 38.22700 71.16300 1.000 64.47558  ? 5   THR A HG22 1 
ATOM   51   H  HG23 . THR A 1 5   ? -50.95900 37.86600 72.07100 1.000 64.47558  ? 5   THR A HG23 1 
ATOM   52   N  N    . ILE A 1 6   ? -51.10500 35.59900 67.67800 1.000 40.38421  ? 6   ILE A N    1 
ATOM   53   C  CA   . ILE A 1 6   ? -51.30600 34.39600 66.89200 1.000 43.25253  ? 6   ILE A CA   1 
ATOM   54   C  C    . ILE A 1 6   ? -50.03400 33.56300 66.96800 1.000 39.39646  ? 6   ILE A C    1 
ATOM   55   O  O    . ILE A 1 6   ? -48.95000 34.05200 67.30100 1.000 40.85970  ? 6   ILE A O    1 
ATOM   56   C  CB   . ILE A 1 6   ? -51.66200 34.67700 65.41300 1.000 46.54705  ? 6   ILE A CB   1 
ATOM   57   C  CG1  . ILE A 1 6   ? -50.56200 35.48900 64.73600 1.000 38.26544  ? 6   ILE A CG1  1 
ATOM   58   C  CG2  . ILE A 1 6   ? -53.00200 35.38100 65.30000 1.000 54.53181  ? 6   ILE A CG2  1 
ATOM   59   C  CD1  . ILE A 1 6   ? -50.72500 35.59300 63.22900 1.000 43.08641  ? 6   ILE A CD1  1 
ATOM   60   H  H    . ILE A 1 6   ? -50.35400 35.98800 67.51900 1.000 45.97558  ? 6   ILE A H    1 
ATOM   61   H  HA   . ILE A 1 6   ? -52.04200 33.89600 67.27700 1.000 49.92558  ? 6   ILE A HA   1 
ATOM   62   H  HB   . ILE A 1 6   ? -51.73100 33.82400 64.95700 1.000 54.21558  ? 6   ILE A HB   1 
ATOM   63   H  HG12 . ILE A 1 6   ? -50.56900 36.38900 65.09800 1.000 44.34558  ? 6   ILE A HG12 1 
ATOM   64   H  HG13 . ILE A 1 6   ? -49.70700 35.06700 64.91400 1.000 44.34558  ? 6   ILE A HG13 1 
ATOM   65   H  HG21 . ILE A 1 6   ? -53.23600 35.46700 64.36300 1.000 63.54558  ? 6   ILE A HG21 1 
ATOM   66   H  HG22 . ILE A 1 6   ? -53.67500 34.85500 65.76200 1.000 63.54558  ? 6   ILE A HG22 1 
ATOM   67   H  HG23 . ILE A 1 6   ? -52.93300 36.25900 65.70600 1.000 63.54558  ? 6   ILE A HG23 1 
ATOM   68   H  HD11 . ILE A 1 6   ? -49.92500 35.99100 62.85200 1.000 50.43558  ? 6   ILE A HD11 1 
ATOM   69   H  HD12 . ILE A 1 6   ? -50.85600 34.70400 62.86400 1.000 50.43558  ? 6   ILE A HD12 1 
ATOM   70   H  HD13 . ILE A 1 6   ? -51.49500 36.14900 63.03300 1.000 50.43558  ? 6   ILE A HD13 1 
ATOM   71   N  N    . LYS A 1 7   ? -50.18700 32.28700 66.64800 1.000 37.97676  ? 7   LYS A N    1 
ATOM   72   C  CA   . LYS A 1 7   ? -49.06800 31.36500 66.53600 1.000 35.13013  ? 7   LYS A CA   1 
ATOM   73   C  C    . LYS A 1 7   ? -48.61700 31.31200 65.08600 1.000 32.01557  ? 7   LYS A C    1 
ATOM   74   O  O    . LYS A 1 7   ? -49.43600 31.09600 64.19000 1.000 33.96239  ? 7   LYS A O    1 
ATOM   75   C  CB   . LYS A 1 7   ? -49.48200 29.96600 66.99600 1.000 36.57023  ? 7   LYS A CB   1 
ATOM   76   C  CG   . LYS A 1 7   ? -48.36200 28.93700 66.99300 1.000 37.98743  ? 7   LYS A CG   1 
ATOM   77   C  CD   . LYS A 1 7   ? -48.89000 27.51300 67.17300 1.000 41.13043  ? 7   LYS A CD   1 
ATOM   78   C  CE   . LYS A 1 7   ? -49.84100 27.08200 66.05200 1.000 40.77909  ? 7   LYS A CE   1 
ATOM   79   N  NZ   . LYS A 1 7   ? -50.31300 25.67100 66.27300 1.000 40.18195  ? 7   LYS A NZ   1 
ATOM   80   H  H    . LYS A 1 7   ? -50.94900 31.92100 66.48800 1.000 44.06558  ? 7   LYS A H    1 
ATOM   81   H  HA   . LYS A 1 7   ? -48.33200 31.66800 67.09100 1.000 40.79558  ? 7   LYS A HA   1 
ATOM   82   H  HB2  . LYS A 1 7   ? -49.82000 30.02700 67.90300 1.000 42.53558  ? 7   LYS A HB2  1 
ATOM   83   H  HB3  . LYS A 1 7   ? -50.17900 29.64000 66.40400 1.000 42.53558  ? 7   LYS A HB3  1 
ATOM   84   H  HG2  . LYS A 1 7   ? -47.89100 28.98100 66.14600 1.000 44.25558  ? 7   LYS A HG2  1 
ATOM   85   H  HG3  . LYS A 1 7   ? -47.75100 29.12800 67.72200 1.000 44.25558  ? 7   LYS A HG3  1 
ATOM   86   H  HD2  . LYS A 1 7   ? -48.14100 26.89700 67.18300 1.000 48.08558  ? 7   LYS A HD2  1 
ATOM   87   H  HD3  . LYS A 1 7   ? -49.37400 27.45900 68.01200 1.000 48.08558  ? 7   LYS A HD3  1 
ATOM   88   H  HE2  . LYS A 1 7   ? -50.61400 27.66800 66.03900 1.000 48.15558  ? 7   LYS A HE2  1 
ATOM   89   H  HE3  . LYS A 1 7   ? -49.37900 27.12400 65.20000 1.000 48.15558  ? 7   LYS A HE3  1 
ATOM   90   H  HZ1  . LYS A 1 7   ? -50.86900 25.43100 65.62100 1.000 47.43558  ? 7   LYS A HZ1  1 
ATOM   91   H  HZ2  . LYS A 1 7   ? -49.61800 25.11600 66.27900 1.000 47.43558  ? 7   LYS A HZ2  1 
ATOM   92   H  HZ3  . LYS A 1 7   ? -50.73800 25.61100 67.05200 1.000 47.43558  ? 7   LYS A HZ3  1 
ATOM   93   N  N    . VAL A 1 8   ? -47.31900 31.49100 64.85500 1.000 33.52133  ? 8   VAL A N    1 
ATOM   94   C  CA   . VAL A 1 8   ? -46.72400 31.27000 63.54000 1.000 32.71827  ? 8   VAL A CA   1 
ATOM   95   C  C    . VAL A 1 8   ? -45.46400 30.43800 63.74700 1.000 28.41447  ? 8   VAL A C    1 
ATOM   96   O  O    . VAL A 1 8   ? -45.02000 30.21800 64.87800 1.000 31.51118  ? 8   VAL A O    1 
ATOM   97   C  CB   . VAL A 1 8   ? -46.39500 32.58600 62.79300 1.000 31.98399  ? 8   VAL A CB   1 
ATOM   98   C  CG1  . VAL A 1 8   ? -47.61500 33.48500 62.71500 1.000 36.64564  ? 8   VAL A CG1  1 
ATOM   99   C  CG2  . VAL A 1 8   ? -45.25000 33.30400 63.45900 1.000 36.63365  ? 8   VAL A CG2  1 
ATOM   100  H  H    . VAL A 1 8   ? -46.75500 31.74400 65.45300 1.000 39.31558  ? 8   VAL A H    1 
ATOM   101  H  HA   . VAL A 1 8   ? -47.34600 30.77600 62.98400 1.000 38.73558  ? 8   VAL A HA   1 
ATOM   102  H  HB   . VAL A 1 8   ? -46.12900 32.36400 61.88700 1.000 37.87558  ? 8   VAL A HB   1 
ATOM   103  H  HG11 . VAL A 1 8   ? -47.39300 34.27400 62.19700 1.000 43.37558  ? 8   VAL A HG11 1 
ATOM   104  H  HG12 . VAL A 1 8   ? -48.33800 33.00000 62.28700 1.000 43.37558  ? 8   VAL A HG12 1 
ATOM   105  H  HG13 . VAL A 1 8   ? -47.87600 33.74200 63.61400 1.000 43.37558  ? 8   VAL A HG13 1 
ATOM   106  H  HG21 . VAL A 1 8   ? -45.22800 34.22200 63.14400 1.000 43.07558  ? 8   VAL A HG21 1 
ATOM   107  H  HG22 . VAL A 1 8   ? -45.38200 33.28700 64.41900 1.000 43.07558  ? 8   VAL A HG22 1 
ATOM   108  H  HG23 . VAL A 1 8   ? -44.42100 32.85600 63.23000 1.000 43.07558  ? 8   VAL A HG23 1 
ATOM   109  N  N    . PHE A 1 9   ? -44.89800 29.96100 62.64400 1.000 26.58181  ? 9   PHE A N    1 
ATOM   110  C  CA   . PHE A 1 9   ? -43.64000 29.23300 62.67800 1.000 28.53380  ? 9   PHE A CA   1 
ATOM   111  C  C    . PHE A 1 9   ? -42.59400 29.99200 61.88100 1.000 32.12745  ? 9   PHE A C    1 
ATOM   112  O  O    . PHE A 1 9   ? -42.87700 30.49600 60.78700 1.000 32.11234  ? 9   PHE A O    1 
ATOM   113  C  CB   . PHE A 1 9   ? -43.79700 27.81500 62.12400 1.000 25.99626  ? 9   PHE A CB   1 
ATOM   114  C  CG   . PHE A 1 9   ? -44.79800 27.01100 62.87000 1.000 28.05244  ? 9   PHE A CG   1 
ATOM   115  C  CD1  . PHE A 1 9   ? -44.50300 26.52700 64.13300 1.000 28.24001  ? 9   PHE A CD1  1 
ATOM   116  C  CD2  . PHE A 1 9   ? -46.04700 26.77300 62.33600 1.000 31.06777  ? 9   PHE A CD2  1 
ATOM   117  C  CE1  . PHE A 1 9   ? -45.44600 25.79200 64.85000 1.000 30.96313  ? 9   PHE A CE1  1 
ATOM   118  C  CE2  . PHE A 1 9   ? -46.99000 26.03700 63.03000 1.000 35.74138  ? 9   PHE A CE2  1 
ATOM   119  C  CZ   . PHE A 1 9   ? -46.69200 25.54900 64.30100 1.000 33.33015  ? 9   PHE A CZ   1 
ATOM   120  H  H    . PHE A 1 9   ? -45.23000 30.04800 61.85600 1.000 31.61558  ? 9   PHE A H    1 
ATOM   121  H  HA   . PHE A 1 9   ? -43.33400 29.16000 63.59600 1.000 33.83558  ? 9   PHE A HA   1 
ATOM   122  H  HB2  . PHE A 1 9   ? -44.08400 27.86900 61.19900 1.000 31.04558  ? 9   PHE A HB2  1 
ATOM   123  H  HB3  . PHE A 1 9   ? -42.94300 27.35900 62.18000 1.000 31.04558  ? 9   PHE A HB3  1 
ATOM   124  H  HD1  . PHE A 1 9   ? -43.66800 26.69500 64.50700 1.000 33.21558  ? 9   PHE A HD1  1 
ATOM   125  H  HD2  . PHE A 1 9   ? -46.25800 27.11200 61.49700 1.000 37.38558  ? 9   PHE A HD2  1 
ATOM   126  H  HE1  . PHE A 1 9   ? -45.23800 25.46500 65.69600 1.000 36.37558  ? 9   PHE A HE1  1 
ATOM   127  H  HE2  . PHE A 1 9   ? -47.82200 25.86900 62.64900 1.000 42.90558  ? 9   PHE A HE2  1 
ATOM   128  H  HZ   . PHE A 1 9   ? -47.32600 25.06300 64.77600 1.000 39.58558  ? 9   PHE A HZ   1 
ATOM   129  N  N    . THR A 1 10  ? -41.38900 30.07200 62.43500 1.000 27.13520  ? 10  THR A N    1 
ATOM   130  C  CA   . THR A 1 10  ? -40.24800 30.58900 61.69100 1.000 27.72472  ? 10  THR A CA   1 
ATOM   131  C  C    . THR A 1 10  ? -39.33400 29.43900 61.30000 1.000 28.34394  ? 10  THR A C    1 
ATOM   132  O  O    . THR A 1 10  ? -39.38100 28.34600 61.87300 1.000 27.84103  ? 10  THR A O    1 
ATOM   133  C  CB   . THR A 1 10  ? -39.47000 31.63000 62.49600 1.000 30.71871  ? 10  THR A CB   1 
ATOM   134  O  OG1  . THR A 1 10  ? -39.11100 31.07700 63.77100 1.000 30.00938  ? 10  THR A OG1  1 
ATOM   135  C  CG2  . THR A 1 10  ? -40.32200 32.88600 62.69300 1.000 31.73983  ? 10  THR A CG2  1 
ATOM   136  H  H    . THR A 1 10  ? -41.20900 29.83300 63.24200 1.000 31.78558  ? 10  THR A H    1 
ATOM   137  H  HA   . THR A 1 10  ? -40.56200 31.02800 60.88500 1.000 32.46558  ? 10  THR A HA   1 
ATOM   138  H  HB   . THR A 1 10  ? -38.66200 31.88300 62.02300 1.000 35.51558  ? 10  THR A HB   1 
ATOM   139  H  HG1  . THR A 1 10  ? -38.68300 31.64300 64.22000 1.000 34.10558  ? 10  THR A HG1  1 
ATOM   140  H  HG21 . THR A 1 10  ? -39.83900 33.53500 63.22800 1.000 36.74558  ? 10  THR A HG21 1 
ATOM   141  H  HG22 . THR A 1 10  ? -40.53400 33.28100 61.83300 1.000 36.74558  ? 10  THR A HG22 1 
ATOM   142  H  HG23 . THR A 1 10  ? -41.14900 32.65800 63.14600 1.000 36.74558  ? 10  THR A HG23 1 
ATOM   143  N  N    . THR A 1 11  ? -38.51200 29.69700 60.28900 1.000 27.33044  ? 11  THR A N    1 
ATOM   144  C  CA   . THR A 1 11  ? -37.66700 28.66600 59.71500 1.000 27.12610  ? 11  THR A CA   1 
ATOM   145  C  C    . THR A 1 11  ? -36.55000 29.34800 58.94400 1.000 28.27084  ? 11  THR A C    1 
ATOM   146  O  O    . THR A 1 11  ? -36.65100 30.52400 58.58600 1.000 25.43485  ? 11  THR A O    1 
ATOM   147  C  CB   . THR A 1 11  ? -38.46300 27.74900 58.78600 1.000 26.10560  ? 11  THR A CB   1 
ATOM   148  O  OG1  . THR A 1 11  ? -37.66100 26.62000 58.44100 1.000 27.61211  ? 11  THR A OG1  1 
ATOM   149  C  CG2  . THR A 1 11  ? -38.85600 28.50400 57.52300 1.000 24.92444  ? 11  THR A CG2  1 
ATOM   150  H  H    . THR A 1 11  ? -38.42700 30.46800 59.91700 1.000 32.09558  ? 11  THR A H    1 
ATOM   151  H  HA   . THR A 1 11  ? -37.28000 28.12800 60.42300 1.000 31.84558  ? 11  THR A HA   1 
ATOM   152  H  HB   . THR A 1 11  ? -39.27200 27.44500 59.22600 1.000 31.12558  ? 11  THR A HB   1 
ATOM   153  H  HG1  . THR A 1 11  ? -37.42300 26.21300 59.13700 1.000 32.81558  ? 11  THR A HG1  1 
ATOM   154  H  HG21 . THR A 1 11  ? -39.54800 28.01900 57.04800 1.000 30.11558  ? 11  THR A HG21 1 
ATOM   155  H  HG22 . THR A 1 11  ? -39.19100 29.38500 57.75400 1.000 30.11558  ? 11  THR A HG22 1 
ATOM   156  H  HG23 . THR A 1 11  ? -38.08500 28.60300 56.94200 1.000 30.11558  ? 11  THR A HG23 1 
ATOM   157  N  N    . VAL A 1 12  ? -35.46900 28.60700 58.72600 1.000 26.21283  ? 12  VAL A N    1 
ATOM   158  C  CA   . VAL A 1 12  ? -34.49000 28.97000 57.70800 1.000 29.22769  ? 12  VAL A CA   1 
ATOM   159  C  C    . VAL A 1 12  ? -34.42000 27.95200 56.58500 1.000 29.74077  ? 12  VAL A C    1 
ATOM   160  O  O    . VAL A 1 12  ? -33.84200 28.25700 55.53200 1.000 29.04766  ? 12  VAL A O    1 
ATOM   161  C  CB   . VAL A 1 12  ? -33.08400 29.18500 58.31300 1.000 27.72945  ? 12  VAL A CB   1 
ATOM   162  C  CG1  . VAL A 1 12  ? -33.09900 30.39700 59.22400 1.000 30.67649  ? 12  VAL A CG1  1 
ATOM   163  C  CG2  . VAL A 1 12  ? -32.59500 27.93800 59.04600 1.000 33.11246  ? 12  VAL A CG2  1 
ATOM   164  H  H    . VAL A 1 12  ? -35.28000 27.88700 59.15600 1.000 30.41558  ? 12  VAL A H    1 
ATOM   165  H  HA   . VAL A 1 12  ? -34.76000 29.81600 57.31800 1.000 34.03558  ? 12  VAL A HA   1 
ATOM   166  H  HB   . VAL A 1 12  ? -32.45200 29.34900 57.59600 1.000 31.53558  ? 12  VAL A HB   1 
ATOM   167  H  HG11 . VAL A 1 12  ? -32.21800 30.50900 59.61500 1.000 34.72558  ? 12  VAL A HG11 1 
ATOM   168  H  HG12 . VAL A 1 12  ? -33.33100 31.18100 58.70200 1.000 34.72558  ? 12  VAL A HG12 1 
ATOM   169  H  HG13 . VAL A 1 12  ? -33.75600 30.25800 59.92300 1.000 34.72558  ? 12  VAL A HG13 1 
ATOM   170  H  HG21 . VAL A 1 12  ? -31.71100 28.11000 59.40700 1.000 37.50558  ? 12  VAL A HG21 1 
ATOM   171  H  HG22 . VAL A 1 12  ? -33.21200 27.73200 59.76600 1.000 37.50558  ? 12  VAL A HG22 1 
ATOM   172  H  HG23 . VAL A 1 12  ? -32.55900 27.19700 58.42100 1.000 37.50558  ? 12  VAL A HG23 1 
ATOM   173  N  N    . ASP A 1 13  ? -34.99000 26.75500 56.75700 1.000 31.71418  ? 13  ASP A N    1 
ATOM   174  C  CA   . ASP A 1 13  ? -34.88600 25.71800 55.73600 1.000 30.62723  ? 13  ASP A CA   1 
ATOM   175  C  C    . ASP A 1 13  ? -36.22400 25.14700 55.29200 1.000 33.01014  ? 13  ASP A C    1 
ATOM   176  O  O    . ASP A 1 13  ? -36.24100 24.27200 54.41100 1.000 31.80725  ? 13  ASP A O    1 
ATOM   177  C  CB   . ASP A 1 13  ? -33.97700 24.57100 56.21900 1.000 29.89840  ? 13  ASP A CB   1 
ATOM   178  C  CG   . ASP A 1 13  ? -34.47800 23.89200 57.50200 1.000 30.81756  ? 13  ASP A CG   1 
ATOM   179  O  OD1  . ASP A 1 13  ? -35.65900 24.03000 57.86000 1.000 31.77928  ? 13  ASP A OD1  1 
ATOM   180  O  OD2  . ASP A 1 13  ? -33.67000 23.20100 58.15100 1.000 34.02344  ? 13  ASP A OD2  1 
ATOM   181  H  H    . ASP A 1 13  ? -35.43800 26.52400 57.45400 1.000 37.44558  ? 13  ASP A H    1 
ATOM   182  H  HA   . ASP A 1 13  ? -34.47300 26.11300 54.95300 1.000 36.33558  ? 13  ASP A HA   1 
ATOM   183  H  HB2  . ASP A 1 13  ? -33.92900 23.89600 55.52400 1.000 34.94558  ? 13  ASP A HB2  1 
ATOM   184  H  HB3  . ASP A 1 13  ? -33.09200 24.92700 56.39700 1.000 34.94558  ? 13  ASP A HB3  1 
ATOM   185  N  N    . ASN A 1 14  ? -37.33800 25.64900 55.82800 1.000 26.67130  ? 14  ASN A N    1 
ATOM   186  C  CA   . ASN A 1 14  ? -38.68900 25.19900 55.49800 1.000 26.83744  ? 14  ASN A CA   1 
ATOM   187  C  C    . ASN A 1 14  ? -38.94200 23.74100 55.87400 1.000 28.83799  ? 14  ASN A C    1 
ATOM   188  O  O    . ASN A 1 14  ? -39.90100 23.12600 55.38500 1.000 29.33472  ? 14  ASN A O    1 
ATOM   189  C  CB   . ASN A 1 14  ? -39.00100 25.40100 54.01500 1.000 31.04092  ? 14  ASN A CB   1 
ATOM   190  C  CG   . ASN A 1 14  ? -40.46300 25.66300 53.77400 1.000 38.18304  ? 14  ASN A CG   1 
ATOM   191  O  OD1  . ASN A 1 14  ? -41.13700 26.27900 54.59700 1.000 33.37557  ? 14  ASN A OD1  1 
ATOM   192  N  ND2  . ASN A 1 14  ? -40.97500 25.16800 52.65800 1.000 40.15883  ? 14  ASN A ND2  1 
ATOM   193  H  H    . ASN A 1 14  ? -37.33400 26.28100 56.41100 1.000 32.24558  ? 14  ASN A H    1 
ATOM   194  H  HA   . ASN A 1 14  ? -39.30200 25.74100 56.01800 1.000 32.80558  ? 14  ASN A HA   1 
ATOM   195  H  HB2  . ASN A 1 14  ? -38.49900 26.16300 53.68500 1.000 38.15558  ? 14  ASN A HB2  1 
ATOM   196  H  HB3  . ASN A 1 14  ? -38.75200 24.60200 53.52500 1.000 38.15558  ? 14  ASN A HB3  1 
ATOM   197  H  HD21 . ASN A 1 14  ? -41.80600 25.29000 52.47500 1.000 49.49558  ? 14  ASN A HD21 1 
ATOM   198  H  HD22 . ASN A 1 14  ? -40.47600 24.72300 52.11700 1.000 49.49558  ? 14  ASN A HD22 1 
ATOM   199  N  N    . ILE A 1 15  ? -38.09800 23.17900 56.73100 1.000 27.46016  ? 15  ILE A N    1 
ATOM   200  C  CA   . ILE A 1 15  ? -38.26100 21.82000 57.22900 1.000 26.06936  ? 15  ILE A CA   1 
ATOM   201  C  C    . ILE A 1 15  ? -38.38000 21.89000 58.74700 1.000 32.51541  ? 15  ILE A C    1 
ATOM   202  O  O    . ILE A 1 15  ? -39.39200 21.48900 59.33300 1.000 29.58613  ? 15  ILE A O    1 
ATOM   203  C  CB   . ILE A 1 15  ? -37.07800 20.94400 56.79600 1.000 30.45062  ? 15  ILE A CB   1 
ATOM   204  C  CG1  . ILE A 1 15  ? -37.04200 20.84200 55.26600 1.000 28.03785  ? 15  ILE A CG1  1 
ATOM   205  C  CG2  . ILE A 1 15  ? -37.18800 19.58300 57.42200 1.000 34.23713  ? 15  ILE A CG2  1 
ATOM   206  C  CD1  . ILE A 1 15  ? -35.72900 20.30000 54.72100 1.000 32.74154  ? 15  ILE A CD1  1 
ATOM   207  H  H    . ILE A 1 15  ? -37.40400 23.57500 57.04800 1.000 33.03558  ? 15  ILE A H    1 
ATOM   208  H  HA   . ILE A 1 15  ? -39.07100 21.42300 56.87300 1.000 31.15558  ? 15  ILE A HA   1 
ATOM   209  H  HB   . ILE A 1 15  ? -36.25100 21.35100 57.09900 1.000 36.08558  ? 15  ILE A HB   1 
ATOM   210  H  HG12 . ILE A 1 15  ? -37.75100 20.24800 54.97600 1.000 33.53558  ? 15  ILE A HG12 1 
ATOM   211  H  HG13 . ILE A 1 15  ? -37.17600 21.72700 54.89100 1.000 33.53558  ? 15  ILE A HG13 1 
ATOM   212  H  HG21 . ILE A 1 15  ? -36.56400 18.98300 56.98500 1.000 40.28558  ? 15  ILE A HG21 1 
ATOM   213  H  HG22 . ILE A 1 15  ? -36.97600 19.65100 58.36600 1.000 40.28558  ? 15  ILE A HG22 1 
ATOM   214  H  HG23 . ILE A 1 15  ? -38.09500 19.25600 57.30900 1.000 40.28558  ? 15  ILE A HG23 1 
ATOM   215  H  HD11 . ILE A 1 15  ? -35.72100 20.40400 53.75700 1.000 38.84558  ? 15  ILE A HD11 1 
ATOM   216  H  HD12 . ILE A 1 15  ? -34.99500 20.79800 55.11300 1.000 38.84558  ? 15  ILE A HD12 1 
ATOM   217  H  HD13 . ILE A 1 15  ? -35.65400 19.36200 54.95400 1.000 38.84558  ? 15  ILE A HD13 1 
ATOM   218  N  N    . ASN A 1 16  ? -37.36100 22.44100 59.38300 1.000 29.61447  ? 16  ASN A N    1 
ATOM   219  C  CA   . ASN A 1 16  ? -37.32800 22.58400 60.83300 1.000 26.78525  ? 16  ASN A CA   1 
ATOM   220  C  C    . ASN A 1 16  ? -38.03800 23.86900 61.21100 1.000 27.64247  ? 16  ASN A C    1 
ATOM   221  O  O    . ASN A 1 16  ? -37.65300 24.95900 60.76900 1.000 30.31229  ? 16  ASN A O    1 
ATOM   222  C  CB   . ASN A 1 16  ? -35.88000 22.55400 61.31200 1.000 34.39732  ? 16  ASN A CB   1 
ATOM   223  C  CG   . ASN A 1 16  ? -35.20000 21.24300 60.96500 1.000 50.73508  ? 16  ASN A CG   1 
ATOM   224  O  OD1  . ASN A 1 16  ? -35.39200 20.25500 61.65400 1.000 55.02337  ? 16  ASN A OD1  1 
ATOM   225  N  ND2  . ASN A 1 16  ? -34.42100 21.22300 59.87100 1.000 46.28878  ? 16  ASN A ND2  1 
ATOM   226  H  H    . ASN A 1 16  ? -36.66000 22.74800 58.99100 1.000 34.55558  ? 16  ASN A H    1 
ATOM   227  H  HA   . ASN A 1 16  ? -37.79800 21.85700 61.27000 1.000 30.64558  ? 16  ASN A HA   1 
ATOM   228  H  HB2  . ASN A 1 16  ? -35.38800 23.27400 60.88700 1.000 39.04558  ? 16  ASN A HB2  1 
ATOM   229  H  HB3  . ASN A 1 16  ? -35.86000 22.66200 62.27600 1.000 39.04558  ? 16  ASN A HB3  1 
ATOM   230  H  HD21 . ASN A 1 16  ? -34.32400 21.93500 59.39900 1.000 53.12558  ? 16  ASN A HD21 1 
ATOM   231  H  HD22 . ASN A 1 16  ? -34.01900 20.49800 59.64200 1.000 53.12558  ? 16  ASN A HD22 1 
ATOM   232  N  N    . LEU A 1 17  ? -39.08500 23.73800 62.01800 1.000 28.10429  ? 17  LEU A N    1 
ATOM   233  C  CA   . LEU A 1 17  ? -39.96100 24.84000 62.36400 1.000 26.90453  ? 17  LEU A CA   1 
ATOM   234  C  C    . LEU A 1 17  ? -39.72000 25.26100 63.80500 1.000 32.03340  ? 17  LEU A C    1 
ATOM   235  O  O    . LEU A 1 17  ? -39.32800 24.45300 64.65100 1.000 32.83068  ? 17  LEU A O    1 
ATOM   236  C  CB   . LEU A 1 17  ? -41.42400 24.44600 62.18700 1.000 27.48730  ? 17  LEU A CB   1 
ATOM   237  C  CG   . LEU A 1 17  ? -41.77800 23.90100 60.79700 1.000 30.41667  ? 17  LEU A CG   1 
ATOM   238  C  CD1  . LEU A 1 17  ? -43.25100 23.63700 60.68400 1.000 34.82428  ? 17  LEU A CD1  1 
ATOM   239  C  CD2  . LEU A 1 17  ? -41.34400 24.89600 59.74500 1.000 30.19344  ? 17  LEU A CD2  1 
ATOM   240  H  H    . LEU A 1 17  ? -39.31300 22.99400 62.38600 1.000 32.44558  ? 17  LEU A H    1 
ATOM   241  H  HA   . LEU A 1 17  ? -39.77300 25.59700 61.78700 1.000 31.21558  ? 17  LEU A HA   1 
ATOM   242  H  HB2  . LEU A 1 17  ? -41.63700 23.75700 62.83500 1.000 32.33558  ? 17  LEU A HB2  1 
ATOM   243  H  HB3  . LEU A 1 17  ? -41.97300 25.23000 62.34200 1.000 32.33558  ? 17  LEU A HB3  1 
ATOM   244  H  HG   . LEU A 1 17  ? -41.31700 23.05900 60.65300 1.000 36.36558  ? 17  LEU A HG   1 
ATOM   245  H  HD11 . LEU A 1 17  ? -43.44200 23.28500 59.80100 1.000 41.95558  ? 17  LEU A HD11 1 
ATOM   246  H  HD12 . LEU A 1 17  ? -43.50900 22.99200 61.36100 1.000 41.95558  ? 17  LEU A HD12 1 
ATOM   247  H  HD13 . LEU A 1 17  ? -43.73200 24.46800 60.82000 1.000 41.95558  ? 17  LEU A HD13 1 
ATOM   248  H  HD21 . LEU A 1 17  ? -41.74400 24.65300 58.89600 1.000 36.36558  ? 17  LEU A HD21 1 
ATOM   249  H  HD22 . LEU A 1 17  ? -41.63900 25.78200 60.00800 1.000 36.36558  ? 17  LEU A HD22 1 
ATOM   250  H  HD23 . LEU A 1 17  ? -40.37700 24.87800 59.67200 1.000 36.36558  ? 17  LEU A HD23 1 
ATOM   251  N  N    . HIS A 1 18  ? -39.98400 26.52800 64.07500 1.000 30.10079  ? 18  HIS A N    1 
ATOM   252  C  CA   . HIS A 1 18  ? -39.76300 27.11300 65.39400 1.000 31.19171  ? 18  HIS A CA   1 
ATOM   253  C  C    . HIS A 1 18  ? -41.01500 27.87600 65.77300 1.000 32.11611  ? 18  HIS A C    1 
ATOM   254  O  O    . HIS A 1 18  ? -41.38400 28.84200 65.10100 1.000 30.09376  ? 18  HIS A O    1 
ATOM   255  C  CB   . HIS A 1 18  ? -38.52800 28.01400 65.36500 1.000 32.33020  ? 18  HIS A CB   1 
ATOM   256  C  CG   . HIS A 1 18  ? -37.28000 27.28100 65.00100 1.000 32.92738  ? 18  HIS A CG   1 
ATOM   257  N  ND1  . HIS A 1 18  ? -36.51800 26.60300 65.92700 1.000 41.30040  ? 18  HIS A ND1  1 
ATOM   258  C  CD2  . HIS A 1 18  ? -36.69200 27.06600 63.79900 1.000 33.14308  ? 18  HIS A CD2  1 
ATOM   259  C  CE1  . HIS A 1 18  ? -35.49500 26.03000 65.31800 1.000 40.05510  ? 18  HIS A CE1  1 
ATOM   260  N  NE2  . HIS A 1 18  ? -35.57500 26.30100 64.02600 1.000 38.84692  ? 18  HIS A NE2  1 
ATOM   261  H  H    . HIS A 1 18  ? -40.29900 27.08500 63.50000 1.000 34.41558  ? 18  HIS A H    1 
ATOM   262  H  HA   . HIS A 1 18  ? -39.61800 26.43000 66.06600 1.000 35.07558  ? 18  HIS A HA   1 
ATOM   263  H  HB2  . HIS A 1 18  ? -38.66500 28.71600 64.70900 1.000 36.05558  ? 18  HIS A HB2  1 
ATOM   264  H  HB3  . HIS A 1 18  ? -38.40100 28.40200 66.24500 1.000 36.05558  ? 18  HIS A HB3  1 
ATOM   265  H  HD1  . HIS A 1 18  ? -36.68200 26.56000 66.77000 1.000 45.71558  ? 18  HIS A HD1  1 
ATOM   266  H  HD2  . HIS A 1 18  ? -36.98900 27.37900 62.97500 1.000 37.09558  ? 18  HIS A HD2  1 
ATOM   267  H  HE1  . HIS A 1 18  ? -34.83200 25.52300 65.72800 1.000 44.06558  ? 18  HIS A HE1  1 
ATOM   268  H  HE2  . HIS A 1 18  ? -35.01700 26.03900 63.42500 1.000 43.33558  ? 18  HIS A HE2  1 
ATOM   269  N  N    . THR A 1 19  ? -41.68200 27.42900 66.83500 1.000 29.79040  ? 19  THR A N    1 
ATOM   270  C  CA   . THR A 1 19  ? -42.93900 28.03800 67.22600 1.000 29.28534  ? 19  THR A CA   1 
ATOM   271  C  C    . THR A 1 19  ? -42.69400 29.44500 67.74200 1.000 35.67260  ? 19  THR A C    1 
ATOM   272  O  O    . THR A 1 19  ? -41.77300 29.68000 68.53100 1.000 35.33295  ? 19  THR A O    1 
ATOM   273  C  CB   . THR A 1 19  ? -43.62200 27.22000 68.32700 1.000 30.04929  ? 19  THR A CB   1 
ATOM   274  O  OG1  . THR A 1 19  ? -43.69700 25.84100 67.96000 1.000 32.33226  ? 19  THR A OG1  1 
ATOM   275  C  CG2  . THR A 1 19  ? -45.01900 27.73400 68.55500 1.000 34.93594  ? 19  THR A CG2  1 
ATOM   276  H  H    . THR A 1 19  ? -41.42700 26.78000 67.33800 1.000 33.28558  ? 19  THR A H    1 
ATOM   277  H  HA   . THR A 1 19  ? -43.52800 28.06900 66.45500 1.000 32.83558  ? 19  THR A HA   1 
ATOM   278  H  HB   . THR A 1 19  ? -43.10600 27.30100 69.14400 1.000 33.38558  ? 19  THR A HB   1 
ATOM   279  H  HG1  . THR A 1 19  ? -42.92400 25.52500 67.87100 1.000 36.31558  ? 19  THR A HG1  1 
ATOM   280  H  HG21 . THR A 1 19  ? -45.49700 27.13800 69.15200 1.000 39.46558  ? 19  THR A HG21 1 
ATOM   281  H  HG22 . THR A 1 19  ? -44.98600 28.61800 68.95100 1.000 39.46558  ? 19  THR A HG22 1 
ATOM   282  H  HG23 . THR A 1 19  ? -45.49600 27.78400 67.71200 1.000 39.46558  ? 19  THR A HG23 1 
ATOM   283  N  N    . GLN A 1 20  ? -43.54900 30.37500 67.32200 1.000 31.17211  ? 20  GLN A N    1 
ATOM   284  C  CA   . GLN A 1 20  ? -43.48200 31.75600 67.77600 1.000 32.82586  ? 20  GLN A CA   1 
ATOM   285  C  C    . GLN A 1 20  ? -44.87800 32.23800 68.12300 1.000 37.93034  ? 20  GLN A C    1 
ATOM   286  O  O    . GLN A 1 20  ? -45.85000 31.89600 67.44800 1.000 37.88125  ? 20  GLN A O    1 
ATOM   287  C  CB   . GLN A 1 20  ? -42.91300 32.69300 66.70700 1.000 33.79319  ? 20  GLN A CB   1 
ATOM   288  C  CG   . GLN A 1 20  ? -41.54500 32.31400 66.16200 1.000 32.60369  ? 20  GLN A CG   1 
ATOM   289  C  CD   . GLN A 1 20  ? -40.46100 32.28700 67.20400 1.000 39.41326  ? 20  GLN A CD   1 
ATOM   290  O  OE1  . GLN A 1 20  ? -40.57400 32.91000 68.26500 1.000 39.62913  ? 20  GLN A OE1  1 
ATOM   291  N  NE2  . GLN A 1 20  ? -39.39000 31.56100 66.90800 1.000 44.20858  ? 20  GLN A NE2  1 
ATOM   292  H  H    . GLN A 1 20  ? -44.18700 30.22600 66.76500 1.000 35.08558  ? 20  GLN A H    1 
ATOM   293  H  HA   . GLN A 1 20  ? -42.91400 31.79100 68.56200 1.000 36.73558  ? 20  GLN A HA   1 
ATOM   294  H  HB2  . GLN A 1 20  ? -43.52800 32.70900 65.95700 1.000 38.16558  ? 20  GLN A HB2  1 
ATOM   295  H  HB3  . GLN A 1 20  ? -42.83500 33.58100 67.09000 1.000 38.16558  ? 20  GLN A HB3  1 
ATOM   296  H  HG2  . GLN A 1 20  ? -41.60000 31.42800 65.77100 1.000 36.71558  ? 20  GLN A HG2  1 
ATOM   297  H  HG3  . GLN A 1 20  ? -41.28900 32.96000 65.48600 1.000 36.71558  ? 20  GLN A HG3  1 
ATOM   298  H  HE21 . GLN A 1 20  ? -39.34800 31.14200 66.15700 1.000 49.72558  ? 20  GLN A HE21 1 
ATOM   299  H  HE22 . GLN A 1 20  ? -38.73800 31.50900 67.46600 1.000 49.72558  ? 20  GLN A HE22 1 
ATOM   300  N  N    . VAL A 1 21  ? -44.97200 33.04000 69.16400 1.000 36.03160  ? 21  VAL A N    1 
ATOM   301  C  CA   . VAL A 1 21  ? -46.20800 33.72600 69.51200 1.000 35.85862  ? 21  VAL A CA   1 
ATOM   302  C  C    . VAL A 1 21  ? -45.94600 35.19600 69.24800 1.000 44.05445  ? 21  VAL A C    1 
ATOM   303  O  O    . VAL A 1 21  ? -45.09300 35.80600 69.90100 1.000 46.29267  ? 21  VAL A O    1 
ATOM   304  C  CB   . VAL A 1 21  ? -46.61500 33.46900 70.96900 1.000 47.37273  ? 21  VAL A CB   1 
ATOM   305  C  CG1  . VAL A 1 21  ? -47.84400 34.28600 71.33400 1.000 50.66702  ? 21  VAL A CG1  1 
ATOM   306  C  CG2  . VAL A 1 21  ? -46.87500 31.98200 71.18200 1.000 54.73508  ? 21  VAL A CG2  1 
ATOM   307  H  H    . VAL A 1 21  ? -44.32000 33.21000 69.69900 1.000 40.07558  ? 21  VAL A H    1 
ATOM   308  H  HA   . VAL A 1 21  ? -46.93900 33.42400 68.95100 1.000 39.81558  ? 21  VAL A HA   1 
ATOM   309  H  HB   . VAL A 1 21  ? -45.89200 33.74200 71.55600 1.000 53.01558  ? 21  VAL A HB   1 
ATOM   310  H  HG11 . VAL A 1 21  ? -48.19100 33.97300 72.18300 1.000 56.85558  ? 21  VAL A HG11 1 
ATOM   311  H  HG12 . VAL A 1 21  ? -47.59200 35.22100 71.40400 1.000 56.85558  ? 21  VAL A HG12 1 
ATOM   312  H  HG13 . VAL A 1 21  ? -48.51400 34.17500 70.64100 1.000 56.85558  ? 21  VAL A HG13 1 
ATOM   313  H  HG21 . VAL A 1 21  ? -47.15600 31.83800 72.09900 1.000 61.97558  ? 21  VAL A HG21 1 
ATOM   314  H  HG22 . VAL A 1 21  ? -47.57200 31.69300 70.57300 1.000 61.97558  ? 21  VAL A HG22 1 
ATOM   315  H  HG23 . VAL A 1 21  ? -46.05700 31.49000 71.00600 1.000 61.97558  ? 21  VAL A HG23 1 
ATOM   316  N  N    . VAL A 1 22  ? -46.63200 35.75900 68.26600 1.000 38.66175  ? 22  VAL A N    1 
ATOM   317  C  CA   . VAL A 1 22  ? -46.36400 37.11600 67.81800 1.000 39.13289  ? 22  VAL A CA   1 
ATOM   318  C  C    . VAL A 1 22  ? -47.49000 38.02900 68.27300 1.000 45.38451  ? 22  VAL A C    1 
ATOM   319  O  O    . VAL A 1 22  ? -48.66500 37.64000 68.30500 1.000 46.57221  ? 22  VAL A O    1 
ATOM   320  C  CB   . VAL A 1 22  ? -46.17000 37.22000 66.29200 1.000 42.99915  ? 22  VAL A CB   1 
ATOM   321  C  CG1  . VAL A 1 22  ? -44.93500 36.45100 65.87900 1.000 45.97922  ? 22  VAL A CG1  1 
ATOM   322  C  CG2  . VAL A 1 22  ? -47.39200 36.73000 65.54300 1.000 41.77990  ? 22  VAL A CG2  1 
ATOM   323  H  H    . VAL A 1 22  ? -47.26800 35.36900 67.83700 1.000 43.45558  ? 22  VAL A H    1 
ATOM   324  H  HA   . VAL A 1 22  ? -45.54000 37.40400 68.24100 1.000 43.90558  ? 22  VAL A HA   1 
ATOM   325  H  HB   . VAL A 1 22  ? -46.04900 38.15200 66.05500 1.000 49.09558  ? 22  VAL A HB   1 
ATOM   326  H  HG11 . VAL A 1 22  ? -44.81400 36.54000 64.92000 1.000 52.86558  ? 22  VAL A HG11 1 
ATOM   327  H  HG12 . VAL A 1 22  ? -44.16600 36.81500 66.34500 1.000 52.86558  ? 22  VAL A HG12 1 
ATOM   328  H  HG13 . VAL A 1 22  ? -45.05100 35.51700 66.11200 1.000 52.86558  ? 22  VAL A HG13 1 
ATOM   329  H  HG21 . VAL A 1 22  ? -47.21400 36.76700 64.59100 1.000 48.07558  ? 22  VAL A HG21 1 
ATOM   330  H  HG22 . VAL A 1 22  ? -47.58000 35.81600 65.80900 1.000 48.07558  ? 22  VAL A HG22 1 
ATOM   331  H  HG23 . VAL A 1 22  ? -48.14600 37.29900 65.76200 1.000 48.07558  ? 22  VAL A HG23 1 
ATOM   332  N  N    . ASP A 1 23  ? -47.11000 39.24700 68.61900 1.000 42.72768  ? 23  ASP A N    1 
ATOM   333  C  CA   . ASP A 1 23  ? -48.02600 40.30600 69.01600 1.000 44.05373  ? 23  ASP A CA   1 
ATOM   334  C  C    . ASP A 1 23  ? -48.55100 40.98900 67.76200 1.000 45.41608  ? 23  ASP A C    1 
ATOM   335  O  O    . ASP A 1 23  ? -47.76500 41.47500 66.94200 1.000 48.76607  ? 23  ASP A O    1 
ATOM   336  C  CB   . ASP A 1 23  ? -47.26200 41.28100 69.90500 1.000 52.10629  ? 23  ASP A CB   1 
ATOM   337  C  CG   . ASP A 1 23  ? -48.11600 42.41800 70.42200 1.000 60.57842  ? 23  ASP A CG   1 
ATOM   338  O  OD1  . ASP A 1 23  ? -49.12600 42.78800 69.78200 1.000 48.93391  ? 23  ASP A OD1  1 
ATOM   339  O  OD2  . ASP A 1 23  ? -47.71700 42.97600 71.46000 1.000 56.37431  ? 23  ASP A OD2  1 
ATOM   340  H  H    . ASP A 1 23  ? -46.28800 39.50000 68.63400 1.000 47.42558  ? 23  ASP A H    1 
ATOM   341  H  HA   . ASP A 1 23  ? -48.78700 39.95900 69.50700 1.000 48.61558  ? 23  ASP A HA   1 
ATOM   342  H  HB2  . ASP A 1 23  ? -46.91300 40.80000 70.67100 1.000 57.55558  ? 23  ASP A HB2  1 
ATOM   343  H  HB3  . ASP A 1 23  ? -46.53300 41.66600 69.39400 1.000 57.55558  ? 23  ASP A HB3  1 
ATOM   344  N  N    . MET A 1 24  ? -49.87000 41.01700 67.60000 1.000 42.74402  ? 24  MET A N    1 
ATOM   345  C  CA   . MET A 1 24  ? -50.44500 41.51900 66.35700 1.000 43.11896  ? 24  MET A CA   1 
ATOM   346  C  C    . MET A 1 24  ? -50.39400 43.03500 66.24100 1.000 49.36979  ? 24  MET A C    1 
ATOM   347  O  O    . MET A 1 24  ? -50.76900 43.56400 65.18500 1.000 46.71673  ? 24  MET A O    1 
ATOM   348  C  CB   . MET A 1 24  ? -51.88600 41.03100 66.20500 1.000 50.06732  ? 24  MET A CB   1 
ATOM   349  C  CG   . MET A 1 24  ? -51.99400 39.50800 66.14500 1.000 55.61947  ? 24  MET A CG   1 
ATOM   350  S  SD   . MET A 1 24  ? -53.69800 38.93900 66.08200 1.000 62.84678  ? 24  MET A SD   1 
ATOM   351  C  CE   . MET A 1 24  ? -53.95400 39.02400 64.31200 1.000 57.46538  ? 24  MET A CE   1 
ATOM   352  H  H    . MET A 1 24  ? -50.44400 40.75600 68.18500 1.000 47.37558  ? 24  MET A H    1 
ATOM   353  H  HA   . MET A 1 24  ? -49.93600 41.14600 65.62000 1.000 48.01558  ? 24  MET A HA   1 
ATOM   354  H  HB2  . MET A 1 24  ? -52.40500 41.33800 66.96500 1.000 56.43558  ? 24  MET A HB2  1 
ATOM   355  H  HB3  . MET A 1 24  ? -52.25600 41.39000 65.38400 1.000 56.43558  ? 24  MET A HB3  1 
ATOM   356  H  HG2  . MET A 1 24  ? -51.54100 39.18900 65.34900 1.000 63.60558  ? 24  MET A HG2  1 
ATOM   357  H  HG3  . MET A 1 24  ? -51.58000 39.12900 66.93600 1.000 63.60558  ? 24  MET A HG3  1 
ATOM   358  H  HE1  . MET A 1 24  ? -54.88900 38.85500 64.12000 1.000 66.08558  ? 24  MET A HE1  1 
ATOM   359  H  HE2  . MET A 1 24  ? -53.70700 39.90900 64.00000 1.000 66.08558  ? 24  MET A HE2  1 
ATOM   360  H  HE3  . MET A 1 24  ? -53.40100 38.35400 63.88100 1.000 66.08558  ? 24  MET A HE3  1 
ATOM   361  N  N    . SER A 1 25  ? -49.91800 43.73300 67.27500 1.000 47.64053  ? 25  SER A N    1 
ATOM   362  C  CA   . SER A 1 25  ? -49.74300 45.17800 67.23200 1.000 50.26102  ? 25  SER A CA   1 
ATOM   363  C  C    . SER A 1 25  ? -48.33700 45.60100 66.81900 1.000 54.61880  ? 25  SER A C    1 
ATOM   364  O  O    . SER A 1 25  ? -48.08300 46.80500 66.70700 1.000 50.75251  ? 25  SER A O    1 
ATOM   365  C  CB   . SER A 1 25  ? -50.05900 45.78600 68.60200 1.000 47.17870  ? 25  SER A CB   1 
ATOM   366  O  OG   . SER A 1 25  ? -49.05300 45.43600 69.53700 1.000 52.22535  ? 25  SER A OG   1 
ATOM   367  H  H    . SER A 1 25  ? -49.68600 43.38200 68.02500 1.000 52.39558  ? 25  SER A H    1 
ATOM   368  H  HA   . SER A 1 25  ? -50.36800 45.53800 66.58400 1.000 54.99558  ? 25  SER A HA   1 
ATOM   369  H  HB2  . SER A 1 25  ? -50.09500 46.75200 68.52000 1.000 50.56558  ? 25  SER A HB2  1 
ATOM   370  H  HB3  . SER A 1 25  ? -50.91300 45.44700 68.91100 1.000 50.56558  ? 25  SER A HB3  1 
ATOM   371  H  HG   . SER A 1 25  ? -49.03800 44.60200 69.64300 1.000 56.45558  ? 25  SER A HG   1 
ATOM   372  N  N    . MET A 1 26  ? -47.43500 44.63100 66.64300 1.000 50.37248  ? 26  MET A N    1 
ATOM   373  C  CA   . MET A 1 26  ? -46.02800 44.89800 66.25600 1.000 44.88287  ? 26  MET A CA   1 
ATOM   374  C  C    . MET A 1 26  ? -45.77700 44.26000 64.88800 1.000 45.72706  ? 26  MET A C    1 
ATOM   375  O  O    . MET A 1 26  ? -46.41800 43.25400 64.58900 1.000 39.75912  ? 26  MET A O    1 
ATOM   376  C  CB   . MET A 1 26  ? -45.06700 44.29800 67.27500 1.000 46.90579  ? 26  MET A CB   1 
ATOM   377  C  CG   . MET A 1 26  ? -45.08000 44.98400 68.61800 1.000 64.63076  ? 26  MET A CG   1 
ATOM   378  S  SD   . MET A 1 26  ? -44.08700 44.10200 69.83600 1.000 63.61959  ? 26  MET A SD   1 
ATOM   379  C  CE   . MET A 1 26  ? -42.47000 44.32400 69.08300 1.000 75.57553  ? 26  MET A CE   1 
ATOM   380  H  H    . MET A 1 26  ? -47.63300 43.75800 66.75600 1.000 55.60558  ? 26  MET A H    1 
ATOM   381  H  HA   . MET A 1 26  ? -45.88000 45.87100 66.19000 1.000 49.02558  ? 26  MET A HA   1 
ATOM   382  H  HB2  . MET A 1 26  ? -45.29900 43.35300 67.40200 1.000 51.25558  ? 26  MET A HB2  1 
ATOM   383  H  HB3  . MET A 1 26  ? -44.16000 44.33500 66.90400 1.000 51.25558  ? 26  MET A HB3  1 
ATOM   384  H  HG2  . MET A 1 26  ? -44.73100 45.89200 68.51900 1.000 71.71558  ? 26  MET A HG2  1 
ATOM   385  H  HG3  . MET A 1 26  ? -46.00100 45.04600 68.94300 1.000 71.71558  ? 26  MET A HG3  1 
ATOM   386  H  HE1  . MET A 1 26  ? -41.77600 44.14900 69.74400 1.000 84.50558  ? 26  MET A HE1  1 
ATOM   387  H  HE2  . MET A 1 26  ? -42.37100 43.70700 68.33500 1.000 84.50558  ? 26  MET A HE2  1 
ATOM   388  H  HE3  . MET A 1 26  ? -42.38900 45.23900 68.75500 1.000 84.50558  ? 26  MET A HE3  1 
ATOM   389  N  N    . THR A 1 27  ? -44.88900 44.83900 64.08800 1.000 41.83792  ? 27  THR A N    1 
ATOM   390  C  CA   . THR A 1 27  ? -44.57500 44.30200 62.76000 1.000 44.13051  ? 27  THR A CA   1 
ATOM   391  C  C    . THR A 1 27  ? -43.73000 43.06700 62.95400 1.000 41.84515  ? 27  THR A C    1 
ATOM   392  O  O    . THR A 1 27  ? -43.12300 42.91800 64.01500 1.000 37.09854  ? 27  THR A O    1 
ATOM   393  C  CB   . THR A 1 27  ? -43.87900 45.32300 61.85700 1.000 44.67864  ? 27  THR A CB   1 
ATOM   394  O  OG1  . THR A 1 27  ? -42.60900 45.59900 62.42200 1.000 42.24827  ? 27  THR A OG1  1 
ATOM   395  C  CG2  . THR A 1 27  ? -44.68500 46.59700 61.69500 1.000 45.79510  ? 27  THR A CG2  1 
ATOM   396  H  H    . THR A 1 27  ? -44.40900 45.57100 64.29700 1.000 46.04558  ? 27  THR A H    1 
ATOM   397  H  HA   . THR A 1 27  ? -45.41600 44.04100 62.33300 1.000 49.36558  ? 27  THR A HA   1 
ATOM   398  H  HB   . THR A 1 27  ? -43.76000 44.92100 60.96300 1.000 49.85558  ? 27  THR A HB   1 
ATOM   399  H  HG1  . THR A 1 27  ? -41.98200 45.28200 61.91700 1.000 46.63558  ? 27  THR A HG1  1 
ATOM   400  H  HG21 . THR A 1 27  ? -44.31600 47.12200 60.96500 1.000 50.71558  ? 27  THR A HG21 1 
ATOM   401  H  HG22 . THR A 1 27  ? -45.60900 46.37000 61.49500 1.000 50.71558  ? 27  THR A HG22 1 
ATOM   402  H  HG23 . THR A 1 27  ? -44.64900 47.11200 62.51700 1.000 50.71558  ? 27  THR A HG23 1 
ATOM   403  N  N    . TYR A 1 28  ? -43.69200 42.19400 61.95900 1.000 37.21958  ? 28  TYR A N    1 
ATOM   404  C  CA   . TYR A 1 28  ? -42.80200 41.04600 62.02600 1.000 35.43409  ? 28  TYR A CA   1 
ATOM   405  C  C    . TYR A 1 28  ? -41.36800 41.49500 62.26100 1.000 33.08579  ? 28  TYR A C    1 
ATOM   406  O  O    . TYR A 1 28  ? -40.63700 40.87100 63.03700 1.000 37.20918  ? 28  TYR A O    1 
ATOM   407  C  CB   . TYR A 1 28  ? -42.91100 40.21100 60.75300 1.000 36.05299  ? 28  TYR A CB   1 
ATOM   408  C  CG   . TYR A 1 28  ? -44.18900 39.40500 60.71300 1.000 34.78249  ? 28  TYR A CG   1 
ATOM   409  C  CD1  . TYR A 1 28  ? -44.37600 38.33400 61.57600 1.000 36.48284  ? 28  TYR A CD1  1 
ATOM   410  C  CD2  . TYR A 1 28  ? -45.21700 39.72800 59.84000 1.000 33.62843  ? 28  TYR A CD2  1 
ATOM   411  C  CE1  . TYR A 1 28  ? -45.53800 37.59200 61.56000 1.000 37.65920  ? 28  TYR A CE1  1 
ATOM   412  C  CE2  . TYR A 1 28  ? -46.39200 38.98800 59.82000 1.000 33.47917  ? 28  TYR A CE2  1 
ATOM   413  C  CZ   . TYR A 1 28  ? -46.54600 37.92300 60.68500 1.000 34.19355  ? 28  TYR A CZ   1 
ATOM   414  O  OH   . TYR A 1 28  ? -47.69600 37.17100 60.68000 1.000 35.31799  ? 28  TYR A OH   1 
ATOM   415  H  H    . TYR A 1 28  ? -44.14900 42.27300 61.23400 1.000 41.98558  ? 28  TYR A H    1 
ATOM   416  H  HA   . TYR A 1 28  ? -43.07000 40.47900 62.76600 1.000 40.11558  ? 28  TYR A HA   1 
ATOM   417  H  HB2  . TYR A 1 28  ? -42.90000 40.80100 59.98300 1.000 41.43558  ? 28  TYR A HB2  1 
ATOM   418  H  HB3  . TYR A 1 28  ? -42.16200 39.59600 60.71000 1.000 41.43558  ? 28  TYR A HB3  1 
ATOM   419  H  HD1  . TYR A 1 28  ? -43.70300 38.11200 62.17800 1.000 42.33558  ? 28  TYR A HD1  1 
ATOM   420  H  HD2  . TYR A 1 28  ? -45.11800 40.44900 59.26100 1.000 38.90558  ? 28  TYR A HD2  1 
ATOM   421  H  HE1  . TYR A 1 28  ? -45.64000 36.87100 62.13800 1.000 43.97558  ? 28  TYR A HE1  1 
ATOM   422  H  HE2  . TYR A 1 28  ? -47.07300 39.20800 59.22600 1.000 38.91558  ? 28  TYR A HE2  1 
ATOM   423  H  HH   . TYR A 1 28  ? -48.35700 37.65800 60.50400 1.000 41.41558  ? 28  TYR A HH   1 
ATOM   424  N  N    . GLY A 1 29  ? -40.95600 42.59300 61.61800 1.000 39.97646  ? 29  GLY A N    1 
ATOM   425  C  CA   . GLY A 1 29  ? -39.58300 43.05500 61.76100 1.000 40.15077  ? 29  GLY A CA   1 
ATOM   426  C  C    . GLY A 1 29  ? -39.22800 43.43200 63.18800 1.000 44.72852  ? 29  GLY A C    1 
ATOM   427  O  O    . GLY A 1 29  ? -38.11500 43.16500 63.65300 1.000 41.95506  ? 29  GLY A O    1 
ATOM   428  H  H    . GLY A 1 29  ? -41.44700 43.07700 61.10300 1.000 45.03558  ? 29  GLY A H    1 
ATOM   429  H  HA2  . GLY A 1 29  ? -38.98000 42.35200 61.47500 1.000 44.87558  ? 29  GLY A HA2  1 
ATOM   430  H  HA3  . GLY A 1 29  ? -39.44900 43.83400 61.20000 1.000 44.87558  ? 29  GLY A HA3  1 
ATOM   431  N  N    . GLN A 1 30  ? -40.15900 44.06700 63.90100 1.000 44.73775  ? 30  GLN A N    1 
ATOM   432  C  CA   . GLN A 1 30  ? -39.90900 44.39200 65.29800 1.000 43.63682  ? 30  GLN A CA   1 
ATOM   433  C  C    . GLN A 1 30  ? -39.67900 43.15200 66.14800 1.000 44.99103  ? 30  GLN A C    1 
ATOM   434  O  O    . GLN A 1 30  ? -39.05400 43.24400 67.20700 1.000 51.52585  ? 30  GLN A O    1 
ATOM   435  C  CB   . GLN A 1 30  ? -41.08600 45.15100 65.90300 1.000 46.31650  ? 30  GLN A CB   1 
ATOM   436  C  CG   . GLN A 1 30  ? -41.40200 46.50500 65.29300 1.000 58.96332  ? 30  GLN A CG   1 
ATOM   437  C  CD   . GLN A 1 30  ? -42.67700 47.07500 65.88300 1.000 52.75195  ? 30  GLN A CD   1 
ATOM   438  O  OE1  . GLN A 1 30  ? -43.70600 47.17600 65.21000 1.000 55.62410  ? 30  GLN A OE1  1 
ATOM   439  N  NE2  . GLN A 1 30  ? -42.60900 47.47300 67.14600 1.000 85.33886  ? 30  GLN A NE2  1 
ATOM   440  H  H    . GLN A 1 30  ? -40.92700 44.31500 63.60300 1.000 49.41558  ? 30  GLN A H    1 
ATOM   441  H  HA   . GLN A 1 30  ? -39.12200 44.95800 65.32300 1.000 47.39558  ? 30  GLN A HA   1 
ATOM   442  H  HB2  . GLN A 1 30  ? -41.88000 44.60200 65.80700 1.000 50.31558  ? 30  GLN A HB2  1 
ATOM   443  H  HB3  . GLN A 1 30  ? -40.89800 45.29900 66.84300 1.000 50.31558  ? 30  GLN A HB3  1 
ATOM   444  H  HG2  . GLN A 1 30  ? -40.67500 47.12000 65.47600 1.000 65.27558  ? 30  GLN A HG2  1 
ATOM   445  H  HG3  . GLN A 1 30  ? -41.52100 46.40800 64.33500 1.000 65.27558  ? 30  GLN A HG3  1 
ATOM   446  H  HE21 . GLN A 1 30  ? -41.87100 47.39900 67.58100 1.000 95.95558  ? 30  GLN A HE21 1 
ATOM   447  H  HE22 . GLN A 1 30  ? -43.30300 47.80400 67.53000 1.000 95.95558  ? 30  GLN A HE22 1 
ATOM   448  N  N    . GLN A 1 31  ? -40.19600 42.00100 65.72100 1.000 42.97935  ? 31  GLN A N    1 
ATOM   449  C  CA   . GLN A 1 31  ? -40.20200 40.78500 66.52700 1.000 41.05126  ? 31  GLN A CA   1 
ATOM   450  C  C    . GLN A 1 31  ? -39.20000 39.74300 66.07100 1.000 47.93801  ? 31  GLN A C    1 
ATOM   451  O  O    . GLN A 1 31  ? -38.61600 39.05800 66.91300 1.000 40.57155  ? 31  GLN A O    1 
ATOM   452  C  CB   . GLN A 1 31  ? -41.61000 40.17400 66.51600 1.000 40.17716  ? 31  GLN A CB   1 
ATOM   453  C  CG   . GLN A 1 31  ? -42.66500 41.17600 66.98300 1.000 43.19382  ? 31  GLN A CG   1 
ATOM   454  C  CD   . GLN A 1 31  ? -44.05900 40.60200 67.03800 1.000 43.61390  ? 31  GLN A CD   1 
ATOM   455  O  OE1  . GLN A 1 31  ? -44.40300 39.84900 67.95000 1.000 46.02592  ? 31  GLN A OE1  1 
ATOM   456  N  NE2  . GLN A 1 31  ? -44.88000 40.96700 66.06300 1.000 41.86933  ? 31  GLN A NE2  1 
ATOM   457  H  H    . GLN A 1 31  ? -40.55700 41.89900 64.94800 1.000 47.22558  ? 31  GLN A H    1 
ATOM   458  H  HA   . GLN A 1 31  ? -39.97600 41.01300 67.44200 1.000 44.87558  ? 31  GLN A HA   1 
ATOM   459  H  HB2  . GLN A 1 31  ? -41.83200 39.89700 65.61300 1.000 44.27558  ? 31  GLN A HB2  1 
ATOM   460  H  HB3  . GLN A 1 31  ? -41.63100 39.40900 67.11300 1.000 44.27558  ? 31  GLN A HB3  1 
ATOM   461  H  HG2  . GLN A 1 31  ? -42.43500 41.48000 67.87500 1.000 47.61558  ? 31  GLN A HG2  1 
ATOM   462  H  HG3  . GLN A 1 31  ? -42.67800 41.92600 66.36900 1.000 47.61558  ? 31  GLN A HG3  1 
ATOM   463  H  HE21 . GLN A 1 31  ? -44.60500 41.50200 65.44800 1.000 46.74558  ? 31  GLN A HE21 1 
ATOM   464  H  HE22 . GLN A 1 31  ? -45.68600 40.67000 66.04500 1.000 46.74558  ? 31  GLN A HE22 1 
ATOM   465  N  N    . PHE A 1 32  ? -38.98100 39.61900 64.75500 1.000 39.38455  ? 32  PHE A N    1 
ATOM   466  C  CA   . PHE A 1 32  ? -38.09400 38.61700 64.18500 1.000 35.92281  ? 32  PHE A CA   1 
ATOM   467  C  C    . PHE A 1 32  ? -36.88600 39.18300 63.45200 1.000 37.91255  ? 32  PHE A C    1 
ATOM   468  O  O    . PHE A 1 32  ? -35.96200 38.42000 63.14000 1.000 41.17125  ? 32  PHE A O    1 
ATOM   469  C  CB   . PHE A 1 32  ? -38.84200 37.75200 63.15600 1.000 36.38960  ? 32  PHE A CB   1 
ATOM   470  C  CG   . PHE A 1 32  ? -40.00100 36.98600 63.70400 1.000 35.72785  ? 32  PHE A CG   1 
ATOM   471  C  CD1  . PHE A 1 32  ? -40.07200 36.64300 65.04300 1.000 40.18366  ? 32  PHE A CD1  1 
ATOM   472  C  CD2  . PHE A 1 32  ? -41.01300 36.57400 62.85200 1.000 36.97730  ? 32  PHE A CD2  1 
ATOM   473  C  CE1  . PHE A 1 32  ? -41.13800 35.92600 65.52400 1.000 41.33360  ? 32  PHE A CE1  1 
ATOM   474  C  CE2  . PHE A 1 32  ? -42.07800 35.84700 63.32400 1.000 42.95592  ? 32  PHE A CE2  1 
ATOM   475  C  CZ   . PHE A 1 32  ? -42.14500 35.52600 64.66800 1.000 42.13001  ? 32  PHE A CZ   1 
ATOM   476  H  H    . PHE A 1 32  ? -39.34900 40.12100 64.16200 1.000 43.64558  ? 32  PHE A H    1 
ATOM   477  H  HA   . PHE A 1 32  ? -37.78800 38.06600 64.92200 1.000 39.73558  ? 32  PHE A HA   1 
ATOM   478  H  HB2  . PHE A 1 32  ? -39.18000 38.33100 62.45500 1.000 41.07558  ? 32  PHE A HB2  1 
ATOM   479  H  HB3  . PHE A 1 32  ? -38.21800 37.10900 62.78300 1.000 41.07558  ? 32  PHE A HB3  1 
ATOM   480  H  HD1  . PHE A 1 32  ? -39.39200 36.90200 65.62200 1.000 45.34558  ? 32  PHE A HD1  1 
ATOM   481  H  HD2  . PHE A 1 32  ? -40.97100 36.79200 61.94900 1.000 42.56558  ? 32  PHE A HD2  1 
ATOM   482  H  HE1  . PHE A 1 32  ? -41.18200 35.70800 66.42700 1.000 46.89558  ? 32  PHE A HE1  1 
ATOM   483  H  HE2  . PHE A 1 32  ? -42.75100 35.57200 62.74400 1.000 49.89558  ? 32  PHE A HE2  1 
ATOM   484  H  HZ   . PHE A 1 32  ? -42.86800 35.04200 64.99500 1.000 48.47558  ? 32  PHE A HZ   1 
ATOM   485  N  N    . GLY A 1 33  ? -36.87900 40.47200 63.12600 1.000 38.39116  ? 33  GLY A N    1 
ATOM   486  C  CA   . GLY A 1 33  ? -35.99000 40.98600 62.10700 1.000 40.31710  ? 33  GLY A CA   1 
ATOM   487  C  C    . GLY A 1 33  ? -36.59100 40.74700 60.73700 1.000 36.10215  ? 33  GLY A C    1 
ATOM   488  O  O    . GLY A 1 33  ? -37.78700 40.46100 60.60500 1.000 35.58732  ? 33  GLY A O    1 
ATOM   489  H  H    . GLY A 1 33  ? -37.38400 41.06800 63.48500 1.000 42.40558  ? 33  GLY A H    1 
ATOM   490  H  HA2  . GLY A 1 33  ? -35.85700 41.93800 62.23400 1.000 44.75558  ? 33  GLY A HA2  1 
ATOM   491  H  HA3  . GLY A 1 33  ? -35.13200 40.53700 62.16000 1.000 44.75558  ? 33  GLY A HA3  1 
ATOM   492  N  N    . PRO A 1 34  ? -35.77900 40.85300 59.68800 1.000 33.40563  ? 34  PRO A N    1 
ATOM   493  C  CA   . PRO A 1 34  ? -36.29600 40.60900 58.33500 1.000 32.21257  ? 34  PRO A CA   1 
ATOM   494  C  C    . PRO A 1 34  ? -37.05200 39.28900 58.25100 1.000 33.42819  ? 34  PRO A C    1 
ATOM   495  O  O    . PRO A 1 34  ? -36.54500 38.23300 58.64300 1.000 34.05719  ? 34  PRO A O    1 
ATOM   496  C  CB   . PRO A 1 34  ? -35.02700 40.59400 57.47400 1.000 38.51933  ? 34  PRO A CB   1 
ATOM   497  C  CG   . PRO A 1 34  ? -34.04600 41.44700 58.23800 1.000 37.02665  ? 34  PRO A CG   1 
ATOM   498  C  CD   . PRO A 1 34  ? -34.33100 41.12300 59.69000 1.000 38.35585  ? 34  PRO A CD   1 
ATOM   499  H  HA   . PRO A 1 34  ? -36.87700 41.33300 58.05500 1.000 36.43558  ? 34  PRO A HA   1 
ATOM   500  H  HB2  . PRO A 1 34  ? -34.70000 39.68500 57.37800 1.000 43.94558  ? 34  PRO A HB2  1 
ATOM   501  H  HB3  . PRO A 1 34  ? -35.21300 40.97300 56.60000 1.000 43.94558  ? 34  PRO A HB3  1 
ATOM   502  H  HG2  . PRO A 1 34  ? -33.13700 41.20800 57.99800 1.000 41.49558  ? 34  PRO A HG2  1 
ATOM   503  H  HG3  . PRO A 1 34  ? -34.20300 42.38600 58.05200 1.000 41.49558  ? 34  PRO A HG3  1 
ATOM   504  H  HD2  . PRO A 1 34  ? -33.83300 40.34000 59.97500 1.000 42.77558  ? 34  PRO A HD2  1 
ATOM   505  H  HD3  . PRO A 1 34  ? -34.11900 41.87700 60.26200 1.000 42.77558  ? 34  PRO A HD3  1 
ATOM   506  N  N    . THR A 1 35  ? -38.26900 39.35100 57.71200 1.000 30.35978  ? 35  THR A N    1 
ATOM   507  C  CA   . THR A 1 35  ? -39.18500 38.20900 57.70100 1.000 30.83754  ? 35  THR A CA   1 
ATOM   508  C  C    . THR A 1 35  ? -39.84700 38.10600 56.33700 1.000 31.26955  ? 35  THR A C    1 
ATOM   509  O  O    . THR A 1 35  ? -40.23300 39.12400 55.75600 1.000 31.33494  ? 35  THR A O    1 
ATOM   510  C  CB   . THR A 1 35  ? -40.27100 38.35200 58.77800 1.000 32.88576  ? 35  THR A CB   1 
ATOM   511  O  OG1  . THR A 1 35  ? -39.67100 38.56600 60.05600 1.000 37.13893  ? 35  THR A OG1  1 
ATOM   512  C  CG2  . THR A 1 35  ? -41.13000 37.09300 58.86400 1.000 30.69682  ? 35  THR A CG2  1 
ATOM   513  H  H    . THR A 1 35  ? -38.59400 40.05600 57.34100 1.000 35.03558  ? 35  THR A H    1 
ATOM   514  H  HA   . THR A 1 35  ? -38.68400 37.39500 57.86700 1.000 35.99558  ? 35  THR A HA   1 
ATOM   515  H  HB   . THR A 1 35  ? -40.83600 39.10600 58.54400 1.000 38.32558  ? 35  THR A HB   1 
ATOM   516  H  HG1  . THR A 1 35  ? -39.21000 39.26800 60.04300 1.000 42.98558  ? 35  THR A HG1  1 
ATOM   517  H  HG21 . THR A 1 35  ? -41.72600 37.14800 59.62700 1.000 36.06558  ? 35  THR A HG21 1 
ATOM   518  H  HG22 . THR A 1 35  ? -41.66000 36.99700 58.05700 1.000 36.06558  ? 35  THR A HG22 1 
ATOM   519  H  HG23 . THR A 1 35  ? -40.56400 36.31100 58.96200 1.000 36.06558  ? 35  THR A HG23 1 
ATOM   520  N  N    . TYR A 1 36  ? -40.00300 36.87500 55.84000 1.000 29.01341  ? 36  TYR A N    1 
ATOM   521  C  CA   . TYR A 1 36  ? -40.55100 36.63900 54.51100 1.000 26.47447  ? 36  TYR A CA   1 
ATOM   522  C  C    . TYR A 1 36  ? -41.57100 35.51500 54.55100 1.000 33.37412  ? 36  TYR A C    1 
ATOM   523  O  O    . TYR A 1 36  ? -41.41500 34.53200 55.28800 1.000 30.72902  ? 36  TYR A O    1 
ATOM   524  C  CB   . TYR A 1 36  ? -39.45500 36.26400 53.49400 1.000 26.69995  ? 36  TYR A CB   1 
ATOM   525  C  CG   . TYR A 1 36  ? -38.31700 37.25200 53.45200 1.000 29.86702  ? 36  TYR A CG   1 
ATOM   526  C  CD1  . TYR A 1 36  ? -37.29500 37.19200 54.38700 1.000 30.11791  ? 36  TYR A CD1  1 
ATOM   527  C  CD2  . TYR A 1 36  ? -38.25600 38.23000 52.46400 1.000 31.42084  ? 36  TYR A CD2  1 
ATOM   528  C  CE1  . TYR A 1 36  ? -36.25200 38.10300 54.35800 1.000 35.43348  ? 36  TYR A CE1  1 
ATOM   529  C  CE2  . TYR A 1 36  ? -37.20600 39.13900 52.41900 1.000 33.02078  ? 36  TYR A CE2  1 
ATOM   530  C  CZ   . TYR A 1 36  ? -36.21500 39.07100 53.36700 1.000 38.51447  ? 36  TYR A CZ   1 
ATOM   531  O  OH   . TYR A 1 36  ? -35.17900 39.97000 53.31500 1.000 39.28049  ? 36  TYR A OH   1 
ATOM   532  H  H    . TYR A 1 36  ? -39.79400 36.15600 56.26200 1.000 34.52558  ? 36  TYR A H    1 
ATOM   533  H  HA   . TYR A 1 36  ? -40.99300 37.45200 54.22100 1.000 31.72558  ? 36  TYR A HA   1 
ATOM   534  H  HB2  . TYR A 1 36  ? -39.08900 35.39800 53.73300 1.000 32.08558  ? 36  TYR A HB2  1 
ATOM   535  H  HB3  . TYR A 1 36  ? -39.84900 36.22500 52.60900 1.000 32.08558  ? 36  TYR A HB3  1 
ATOM   536  H  HD1  . TYR A 1 36  ? -37.31000 36.53200 55.04200 1.000 35.66558  ? 36  TYR A HD1  1 
ATOM   537  H  HD2  . TYR A 1 36  ? -38.92800 38.27600 51.82300 1.000 37.30558  ? 36  TYR A HD2  1 
ATOM   538  H  HE1  . TYR A 1 36  ? -35.58100 38.06600 55.00100 1.000 41.70558  ? 36  TYR A HE1  1 
ATOM   539  H  HE2  . TYR A 1 36  ? -37.17400 39.78800 51.75300 1.000 38.91558  ? 36  TYR A HE2  1 
ATOM   540  H  HH   . TYR A 1 36  ? -35.27800 40.48400 52.65900 1.000 45.86558  ? 36  TYR A HH   1 
ATOM   541  N  N    . LEU A 1 37  ? -42.60300 35.66600 53.73000 1.000 28.77229  ? 37  LEU A N    1 
ATOM   542  C  CA   . LEU A 1 37  ? -43.67900 34.69300 53.58900 1.000 25.69206  ? 37  LEU A CA   1 
ATOM   543  C  C    . LEU A 1 37  ? -43.65600 34.21900 52.14100 1.000 35.86700  ? 37  LEU A C    1 
ATOM   544  O  O    . LEU A 1 37  ? -44.10300 34.93800 51.24000 1.000 32.68028  ? 37  LEU A O    1 
ATOM   545  C  CB   . LEU A 1 37  ? -45.02500 35.30900 53.96100 1.000 32.31916  ? 37  LEU A CB   1 
ATOM   546  C  CG   . LEU A 1 37  ? -46.22700 34.36800 53.85600 1.000 31.76923  ? 37  LEU A CG   1 
ATOM   547  C  CD1  . LEU A 1 37  ? -46.01000 33.11900 54.69100 1.000 34.03047  ? 37  LEU A CD1  1 
ATOM   548  C  CD2  . LEU A 1 37  ? -47.49600 35.09100 54.28700 1.000 35.48538  ? 37  LEU A CD2  1 
ATOM   549  H  H    . LEU A 1 37  ? -42.70600 36.35300 53.22400 1.000 34.78558  ? 37  LEU A H    1 
ATOM   550  H  HA   . LEU A 1 37  ? -43.52600 33.93500 54.17500 1.000 31.26558  ? 37  LEU A HA   1 
ATOM   551  H  HB2  . LEU A 1 37  ? -44.97700 35.61600 54.88000 1.000 39.01558  ? 37  LEU A HB2  1 
ATOM   552  H  HB3  . LEU A 1 37  ? -45.19200 36.05900 53.36900 1.000 39.01558  ? 37  LEU A HB3  1 
ATOM   553  H  HG   . LEU A 1 37  ? -46.33200 34.08900 52.93300 1.000 38.45558  ? 37  LEU A HG   1 
ATOM   554  H  HD11 . LEU A 1 37  ? -46.84300 32.62400 54.74100 1.000 41.41558  ? 37  LEU A HD11 1 
ATOM   555  H  HD12 . LEU A 1 37  ? -45.32600 32.57400 54.27300 1.000 41.41558  ? 37  LEU A HD12 1 
ATOM   556  H  HD13 . LEU A 1 37  ? -45.72700 33.37900 55.58200 1.000 41.41558  ? 37  LEU A HD13 1 
ATOM   557  H  HD21 . LEU A 1 37  ? -48.24700 34.48100 54.21400 1.000 42.60558  ? 37  LEU A HD21 1 
ATOM   558  H  HD22 . LEU A 1 37  ? -47.39600 35.38300 55.20700 1.000 42.60558  ? 37  LEU A HD22 1 
ATOM   559  H  HD23 . LEU A 1 37  ? -47.63400 35.85800 53.70900 1.000 42.60558  ? 37  LEU A HD23 1 
ATOM   560  N  N    . ASP A 1 38  ? -43.10100 33.02800 51.92000 1.000 34.10090  ? 38  ASP A N    1 
ATOM   561  C  CA   . ASP A 1 38  ? -42.92800 32.46600 50.58200 1.000 40.19760  ? 38  ASP A CA   1 
ATOM   562  C  C    . ASP A 1 38  ? -42.33500 33.48900 49.61800 1.000 34.14861  ? 38  ASP A C    1 
ATOM   563  O  O    . ASP A 1 38  ? -42.80900 33.66000 48.49500 1.000 35.95118  ? 38  ASP A O    1 
ATOM   564  C  CB   . ASP A 1 38  ? -44.25000 31.92800 50.02900 1.000 42.09897  ? 38  ASP A CB   1 
ATOM   565  C  CG   . ASP A 1 38  ? -44.04600 30.99300 48.82800 1.000 76.56003  ? 38  ASP A CG   1 
ATOM   566  O  OD1  . ASP A 1 38  ? -42.97300 30.34900 48.73900 1.000 46.02317  ? 38  ASP A OD1  1 
ATOM   567  O  OD2  . ASP A 1 38  ? -44.96800 30.87800 47.98700 1.000 54.06565  ? 38  ASP A OD2  1 
ATOM   568  H  H    . ASP A 1 38  ? -42.81000 32.51400 52.54500 1.000 41.68558  ? 38  ASP A H    1 
ATOM   569  H  HA   . ASP A 1 38  ? -42.30300 31.72800 50.65800 1.000 49.05558  ? 38  ASP A HA   1 
ATOM   570  H  HB2  . ASP A 1 38  ? -44.70600 31.43000 50.72500 1.000 51.28558  ? 38  ASP A HB2  1 
ATOM   571  H  HB3  . ASP A 1 38  ? -44.80000 32.67400 49.74100 1.000 51.28558  ? 38  ASP A HB3  1 
ATOM   572  N  N    . GLY A 1 39  ? -41.27200 34.16000 50.06200 1.000 30.25118  ? 39  GLY A N    1 
ATOM   573  C  CA   . GLY A 1 39  ? -40.53400 35.11500 49.25700 1.000 31.31429  ? 39  GLY A CA   1 
ATOM   574  C  C    . GLY A 1 39  ? -40.96100 36.55800 49.44100 1.000 31.66390  ? 39  GLY A C    1 
ATOM   575  O  O    . GLY A 1 39  ? -40.14900 37.47400 49.21700 1.000 33.53469  ? 39  GLY A O    1 
ATOM   576  H  H    . GLY A 1 39  ? -40.95300 34.07200 50.85500 1.000 36.85558  ? 39  GLY A H    1 
ATOM   577  H  HA2  . GLY A 1 39  ? -39.59300 35.05200 49.48300 1.000 37.91558  ? 39  GLY A HA2  1 
ATOM   578  H  HA3  . GLY A 1 39  ? -40.64900 34.88800 48.32100 1.000 37.91558  ? 39  GLY A HA3  1 
ATOM   579  N  N    . ALA A 1 40  ? -42.19700 36.78600 49.86200 1.000 31.40331  ? 40  ALA A N    1 
ATOM   580  C  CA   . ALA A 1 40  ? -42.69100 38.14000 50.04400 1.000 34.56474  ? 40  ALA A CA   1 
ATOM   581  C  C    . ALA A 1 40  ? -42.14700 38.73300 51.33900 1.000 35.73872  ? 40  ALA A C    1 
ATOM   582  O  O    . ALA A 1 40  ? -42.17200 38.08800 52.38900 1.000 34.34020  ? 40  ALA A O    1 
ATOM   583  C  CB   . ALA A 1 40  ? -44.21800 38.14200 50.05000 1.000 39.80816  ? 40  ALA A CB   1 
ATOM   584  H  H    . ALA A 1 40  ? -42.77000 36.17300 50.04900 1.000 37.62558  ? 40  ALA A H    1 
ATOM   585  H  HA   . ALA A 1 40  ? -42.38800 38.69900 49.31100 1.000 41.04558  ? 40  ALA A HA   1 
ATOM   586  H  HB1  . ALA A 1 40  ? -44.53200 39.05100 50.17600 1.000 47.16558  ? 40  ALA A HB1  1 
ATOM   587  H  HB2  . ALA A 1 40  ? -44.53800 37.79600 49.20300 1.000 47.16558  ? 40  ALA A HB2  1 
ATOM   588  H  HB3  . ALA A 1 40  ? -44.53100 37.58000 50.77600 1.000 47.16558  ? 40  ALA A HB3  1 
ATOM   589  N  N    . ASP A 1 41  ? -41.65400 39.96300 51.25500 1.000 32.98917  ? 41  ASP A N    1 
ATOM   590  C  CA   . ASP A 1 41  ? -41.07400 40.66000 52.39700 1.000 31.18926  ? 41  ASP A CA   1 
ATOM   591  C  C    . ASP A 1 41  ? -42.20100 41.19800 53.26800 1.000 34.18839  ? 41  ASP A C    1 
ATOM   592  O  O    . ASP A 1 41  ? -42.89900 42.13200 52.86400 1.000 38.23682  ? 41  ASP A O    1 
ATOM   593  C  CB   . ASP A 1 41  ? -40.18200 41.79600 51.90600 1.000 36.35780  ? 41  ASP A CB   1 
ATOM   594  C  CG   . ASP A 1 41  ? -39.31000 42.37600 53.00300 1.000 49.30599  ? 41  ASP A CG   1 
ATOM   595  O  OD1  . ASP A 1 41  ? -39.68300 42.25500 54.18700 1.000 37.38092  ? 41  ASP A OD1  1 
ATOM   596  O  OD2  . ASP A 1 41  ? -38.28900 43.02000 52.67500 1.000 44.04509  ? 41  ASP A OD2  1 
ATOM   597  H  H    . ASP A 1 41  ? -41.64300 40.42700 50.53100 1.000 38.78558  ? 41  ASP A H    1 
ATOM   598  H  HA   . ASP A 1 41  ? -40.54100 40.04300 52.92400 1.000 36.44558  ? 41  ASP A HA   1 
ATOM   599  H  HB2  . ASP A 1 41  ? -39.60000 41.46100 51.20600 1.000 42.31558  ? 41  ASP A HB2  1 
ATOM   600  H  HB3  . ASP A 1 41  ? -40.74100 42.50900 51.56000 1.000 42.31558  ? 41  ASP A HB3  1 
ATOM   601  N  N    . VAL A 1 42  ? -42.36300 40.64300 54.47000 1.000 32.66985  ? 42  VAL A N    1 
ATOM   602  C  CA   . VAL A 1 42  ? -43.39500 41.08600 55.40600 1.000 34.43235  ? 42  VAL A CA   1 
ATOM   603  C  C    . VAL A 1 42  ? -42.79200 41.79900 56.61700 1.000 36.51951  ? 42  VAL A C    1 
ATOM   604  O  O    . VAL A 1 42  ? -43.46700 41.97200 57.62900 1.000 37.52283  ? 42  VAL A O    1 
ATOM   605  C  CB   . VAL A 1 42  ? -44.29400 39.92100 55.86100 1.000 36.01179  ? 42  VAL A CB   1 
ATOM   606  C  CG1  . VAL A 1 42  ? -45.13100 39.39000 54.70400 1.000 39.48387  ? 42  VAL A CG1  1 
ATOM   607  C  CG2  . VAL A 1 42  ? -43.48200 38.80800 56.51400 1.000 32.82969  ? 42  VAL A CG2  1 
ATOM   608  H  H    . VAL A 1 42  ? -41.88000 39.99800 54.77000 1.000 38.14558  ? 42  VAL A H    1 
ATOM   609  H  HA   . VAL A 1 42  ? -43.94800 41.72600 54.93200 1.000 40.02558  ? 42  VAL A HA   1 
ATOM   610  H  HB   . VAL A 1 42  ? -44.90500 40.26000 56.53300 1.000 42.22558  ? 42  VAL A HB   1 
ATOM   611  H  HG11 . VAL A 1 42  ? -45.68100 38.65700 55.02300 1.000 46.53558  ? 42  VAL A HG11 1 
ATOM   612  H  HG12 . VAL A 1 42  ? -45.69500 40.10400 54.36800 1.000 46.53558  ? 42  VAL A HG12 1 
ATOM   613  H  HG13 . VAL A 1 42  ? -44.53900 39.07800 54.00200 1.000 46.53558  ? 42  VAL A HG13 1 
ATOM   614  H  HG21 . VAL A 1 42  ? -44.08400 38.10200 56.79700 1.000 38.69558  ? 42  VAL A HG21 1 
ATOM   615  H  HG22 . VAL A 1 42  ? -42.84600 38.46100 55.86900 1.000 38.69558  ? 42  VAL A HG22 1 
ATOM   616  H  HG23 . VAL A 1 42  ? -43.01100 39.16900 57.28100 1.000 38.69558  ? 42  VAL A HG23 1 
ATOM   617  N  N    . THR A 1 43  ? -41.52500 42.21000 56.53200 1.000 34.60211  ? 43  THR A N    1 
ATOM   618  C  CA   . THR A 1 43  ? -40.85700 42.82100 57.67700 1.000 35.63893  ? 43  THR A CA   1 
ATOM   619  C  C    . THR A 1 43  ? -41.64900 43.99600 58.23100 1.000 40.73354  ? 43  THR A C    1 
ATOM   620  O  O    . THR A 1 43  ? -41.67900 44.21900 59.44400 1.000 41.31625  ? 43  THR A O    1 
ATOM   621  C  CB   . THR A 1 43  ? -39.46200 43.29500 57.27400 1.000 36.70739  ? 43  THR A CB   1 
ATOM   622  O  OG1  . THR A 1 43  ? -38.69900 42.19300 56.77700 1.000 34.06149  ? 43  THR A OG1  1 
ATOM   623  C  CG2  . THR A 1 43  ? -38.72800 43.92100 58.45500 1.000 39.60225  ? 43  THR A CG2  1 
ATOM   624  H  H    . THR A 1 43  ? -41.03500 42.14600 55.82800 1.000 39.78558  ? 43  THR A H    1 
ATOM   625  H  HA   . THR A 1 43  ? -40.77400 42.15000 58.37300 1.000 40.64558  ? 43  THR A HA   1 
ATOM   626  H  HB   . THR A 1 43  ? -39.55000 43.96900 56.58300 1.000 41.74558  ? 43  THR A HB   1 
ATOM   627  H  HG1  . THR A 1 43  ? -39.07400 41.86600 56.10100 1.000 38.94558  ? 43  THR A HG1  1 
ATOM   628  H  HG21 . THR A 1 43  ? -37.82600 44.16400 58.19300 1.000 44.70558  ? 43  THR A HG21 1 
ATOM   629  H  HG22 . THR A 1 43  ? -39.19500 44.71800 58.75100 1.000 44.70558  ? 43  THR A HG22 1 
ATOM   630  H  HG23 . THR A 1 43  ? -38.68400 43.29100 59.19000 1.000 44.70558  ? 43  THR A HG23 1 
ATOM   631  N  N    . LYS A 1 44  ? -42.26900 44.77700 57.35100 1.000 38.38445  ? 44  LYS A N    1 
ATOM   632  C  CA   . LYS A 1 44  ? -42.95300 46.00900 57.73300 1.000 43.91658  ? 44  LYS A CA   1 
ATOM   633  C  C    . LYS A 1 44  ? -44.45500 45.82200 57.88900 1.000 47.85897  ? 44  LYS A C    1 
ATOM   634  O  O    . LYS A 1 44  ? -45.19300 46.80700 57.98000 1.000 46.90556  ? 44  LYS A O    1 
ATOM   635  C  CB   . LYS A 1 44  ? -42.65800 47.08800 56.69500 1.000 44.68019  ? 44  LYS A CB   1 
ATOM   636  C  CG   . LYS A 1 44  ? -41.18900 47.46600 56.65100 1.000 44.48718  ? 44  LYS A CG   1 
ATOM   637  C  CD   . LYS A 1 44  ? -40.96200 48.81100 55.96900 1.000 73.94892  ? 44  LYS A CD   1 
ATOM   638  C  CE   . LYS A 1 44  ? -39.58300 48.87900 55.32100 1.000 75.80603  ? 44  LYS A CE   1 
ATOM   639  N  NZ   . LYS A 1 44  ? -39.20800 50.26600 54.91700 1.000 84.54396  ? 44  LYS A NZ   1 
ATOM   640  H  H    . LYS A 1 44  ? -42.30900 44.61100 56.50800 1.000 43.33558  ? 44  LYS A H    1 
ATOM   641  H  HA   . LYS A 1 44  ? -42.61300 46.30900 58.59000 1.000 49.42558  ? 44  LYS A HA   1 
ATOM   642  H  HB2  . LYS A 1 44  ? -42.91200 46.76200 55.81700 1.000 50.01558  ? 44  LYS A HB2  1 
ATOM   643  H  HB3  . LYS A 1 44  ? -43.16800 47.88500 56.91300 1.000 50.01558  ? 44  LYS A HB3  1 
ATOM   644  H  HG2  . LYS A 1 44  ? -40.84800 47.52500 57.55700 1.000 49.65558  ? 44  LYS A HG2  1 
ATOM   645  H  HG3  . LYS A 1 44  ? -40.70100 46.79000 56.15600 1.000 49.65558  ? 44  LYS A HG3  1 
ATOM   646  H  HD2  . LYS A 1 44  ? -41.63100 48.93800 55.27800 1.000 84.49558  ? 44  LYS A HD2  1 
ATOM   647  H  HD3  . LYS A 1 44  ? -41.02500 49.52000 56.62700 1.000 84.49558  ? 44  LYS A HD3  1 
ATOM   648  H  HE2  . LYS A 1 44  ? -38.91900 48.56000 55.95200 1.000 86.76558  ? 44  LYS A HE2  1 
ATOM   649  H  HE3  . LYS A 1 44  ? -39.57800 48.32300 54.52600 1.000 86.76558  ? 44  LYS A HE3  1 
ATOM   650  H  HZ1  . LYS A 1 44  ? -38.39900 50.26700 54.54400 1.000 96.63558  ? 44  LYS A HZ1  1 
ATOM   651  H  HZ2  . LYS A 1 44  ? -39.79700 50.58200 54.32900 1.000 96.63558  ? 44  LYS A HZ2  1 
ATOM   652  H  HZ3  . LYS A 1 44  ? -39.19700 50.79900 55.63000 1.000 96.63558  ? 44  LYS A HZ3  1 
ATOM   653  N  N    . ILE A 1 45  ? -44.91700 44.58100 57.94000 1.000 39.57010  ? 45  ILE A N    1 
ATOM   654  C  CA   . ILE A 1 45  ? -46.33300 44.23800 58.00200 1.000 41.55060  ? 45  ILE A CA   1 
ATOM   655  C  C    . ILE A 1 45  ? -46.62200 43.70300 59.39600 1.000 40.07069  ? 45  ILE A C    1 
ATOM   656  O  O    . ILE A 1 45  ? -45.77600 43.03400 59.99700 1.000 42.96799  ? 45  ILE A O    1 
ATOM   657  C  CB   . ILE A 1 45  ? -46.66600 43.20700 56.90200 1.000 58.57683  ? 45  ILE A CB   1 
ATOM   658  C  CG1  . ILE A 1 45  ? -47.19300 43.90700 55.64400 1.000 56.72250  ? 45  ILE A CG1  1 
ATOM   659  C  CG2  . ILE A 1 45  ? -47.67300 42.17800 57.35800 1.000 50.35512  ? 45  ILE A CG2  1 
ATOM   660  C  CD1  . ILE A 1 45  ? -46.35100 45.07100 55.19400 1.000 74.70586  ? 45  ILE A CD1  1 
ATOM   661  H  H    . ILE A 1 45  ? -44.40700 43.88800 57.93900 1.000 44.65558  ? 45  ILE A H    1 
ATOM   662  H  HA   . ILE A 1 45  ? -46.89200 45.01900 57.86900 1.000 47.03558  ? 45  ILE A HA   1 
ATOM   663  H  HB   . ILE A 1 45  ? -45.83600 42.74700 56.70100 1.000 67.90558  ? 45  ILE A HB   1 
ATOM   664  H  HG12 . ILE A 1 45  ? -47.21900 43.26400 54.91800 1.000 65.35558  ? 45  ILE A HG12 1 
ATOM   665  H  HG13 . ILE A 1 45  ? -48.08500 44.24000 55.82500 1.000 65.35558  ? 45  ILE A HG13 1 
ATOM   666  H  HG21 . ILE A 1 45  ? -47.88800 41.59500 56.61300 1.000 58.26558  ? 45  ILE A HG21 1 
ATOM   667  H  HG22 . ILE A 1 45  ? -47.28900 41.66100 58.08300 1.000 58.26558  ? 45  ILE A HG22 1 
ATOM   668  H  HG23 . ILE A 1 45  ? -48.47300 42.63400 57.66300 1.000 58.26558  ? 45  ILE A HG23 1 
ATOM   669  H  HD11 . ILE A 1 45  ? -46.73800 45.44700 54.38700 1.000 86.60558  ? 45  ILE A HD11 1 
ATOM   670  H  HD12 . ILE A 1 45  ? -46.33500 45.74000 55.89600 1.000 86.60558  ? 45  ILE A HD12 1 
ATOM   671  H  HD13 . ILE A 1 45  ? -45.45100 44.75900 55.01400 1.000 86.60558  ? 45  ILE A HD13 1 
ATOM   672  N  N    . LYS A 1 46  ? -47.84300 44.02200 59.93500 1.000 42.56276  ? 46  LYS A N    1 
ATOM   673  C  CA   . LYS A 1 46  ? -48.22300 43.39800 61.19400 1.000 38.16839  ? 46  LYS A CA   1 
ATOM   674  C  C    . LYS A 1 46  ? -49.01600 42.13100 60.92300 1.000 39.27351  ? 46  LYS A C    1 
ATOM   675  O  O    . LYS A 1 46  ? -49.66900 42.01600 59.88300 1.000 45.16105  ? 46  LYS A O    1 
ATOM   676  C  CB   . LYS A 1 46  ? -49.06800 44.35000 62.04300 1.000 42.68658  ? 46  LYS A CB   1 
ATOM   677  C  CG   . LYS A 1 46  ? -48.44300 45.72600 62.23000 1.000 45.57857  ? 46  LYS A CG   1 
ATOM   678  C  CD   . LYS A 1 46  ? -48.97500 46.41300 63.46600 1.000 53.87254  ? 46  LYS A CD   1 
ATOM   679  C  CE   . LYS A 1 46  ? -48.13300 47.62400 63.82500 1.000 58.92406  ? 46  LYS A CE   1 
ATOM   680  N  NZ   . LYS A 1 46  ? -48.99200 48.71600 64.38500 1.000 67.34176  ? 46  LYS A NZ   1 
ATOM   681  H  H    . LYS A 1 46  ? -48.41700 44.56500 59.59400 1.000 47.97558  ? 46  LYS A H    1 
ATOM   682  H  HA   . LYS A 1 46  ? -47.42700 43.17500 61.70200 1.000 42.72558  ? 46  LYS A HA   1 
ATOM   683  H  HB2  . LYS A 1 46  ? -49.92900 44.47200 61.61200 1.000 47.55558  ? 46  LYS A HB2  1 
ATOM   684  H  HB3  . LYS A 1 46  ? -49.19000 43.95900 62.92200 1.000 47.55558  ? 46  LYS A HB3  1 
ATOM   685  H  HG2  . LYS A 1 46  ? -47.48200 45.63300 62.32200 1.000 50.48558  ? 46  LYS A HG2  1 
ATOM   686  H  HG3  . LYS A 1 46  ? -48.65000 46.28000 61.46100 1.000 50.48558  ? 46  LYS A HG3  1 
ATOM   687  H  HD2  . LYS A 1 46  ? -49.88400 46.70900 63.30500 1.000 59.84558  ? 46  LYS A HD2  1 
ATOM   688  H  HD3  . LYS A 1 46  ? -48.95500 45.79400 64.21300 1.000 59.84558  ? 46  LYS A HD3  1 
ATOM   689  H  HE2  . LYS A 1 46  ? -47.47500 47.37500 64.49300 1.000 65.36558  ? 46  LYS A HE2  1 
ATOM   690  H  HE3  . LYS A 1 46  ? -47.68800 47.95700 63.03000 1.000 65.36558  ? 46  LYS A HE3  1 
ATOM   691  H  HZ1  . LYS A 1 46  ? -48.48900 49.41900 64.59800 1.000 74.74558  ? 46  LYS A HZ1  1 
ATOM   692  H  HZ2  . LYS A 1 46  ? -49.59800 48.96600 63.78300 1.000 74.74558  ? 46  LYS A HZ2  1 
ATOM   693  H  HZ3  . LYS A 1 46  ? -49.41100 48.42900 65.11600 1.000 74.74558  ? 46  LYS A HZ3  1 
ATOM   694  N  N    . PRO A 1 47  ? -48.97900 41.17300 61.84800 1.000 40.67979  ? 47  PRO A N    1 
ATOM   695  C  CA   . PRO A 1 47  ? -49.63200 39.88200 61.59900 1.000 39.99814  ? 47  PRO A CA   1 
ATOM   696  C  C    . PRO A 1 47  ? -51.11700 39.99200 61.26000 1.000 52.01722  ? 47  PRO A C    1 
ATOM   697  O  O    . PRO A 1 47  ? -51.85700 40.78700 61.84000 1.000 50.63344  ? 47  PRO A O    1 
ATOM   698  C  CB   . PRO A 1 47  ? -49.42100 39.12400 62.91500 1.000 42.11244  ? 47  PRO A CB   1 
ATOM   699  C  CG   . PRO A 1 47  ? -48.19200 39.73600 63.51600 1.000 40.66620  ? 47  PRO A CG   1 
ATOM   700  C  CD   . PRO A 1 47  ? -48.13100 41.15900 63.05200 1.000 43.75914  ? 47  PRO A CD   1 
ATOM   701  H  HA   . PRO A 1 47  ? -49.18400 39.43900 60.86200 1.000 45.94558  ? 47  PRO A HA   1 
ATOM   702  H  HB2  . PRO A 1 47  ? -50.18900 39.24600 63.49500 1.000 48.49558  ? 47  PRO A HB2  1 
ATOM   703  H  HB3  . PRO A 1 47  ? -49.28700 38.18000 62.73600 1.000 48.49558  ? 47  PRO A HB3  1 
ATOM   704  H  HG2  . PRO A 1 47  ? -48.25400 39.69900 64.48300 1.000 46.51558  ? 47  PRO A HG2  1 
ATOM   705  H  HG3  . PRO A 1 47  ? -47.41000 39.24800 63.21500 1.000 46.51558  ? 47  PRO A HG3  1 
ATOM   706  H  HD2  . PRO A 1 47  ? -48.48500 41.75600 63.72900 1.000 49.88558  ? 47  PRO A HD2  1 
ATOM   707  H  HD3  . PRO A 1 47  ? -47.21900 41.40900 62.83300 1.000 49.88558  ? 47  PRO A HD3  1 
ATOM   708  N  N    . HIS A 1 48  ? -51.54300 39.16300 60.30700 1.000 47.56510  ? 48  HIS A N    1 
ATOM   709  C  CA   . HIS A 1 48  ? -52.93900 39.00100 59.93200 1.000 45.92847  ? 48  HIS A CA   1 
ATOM   710  C  C    . HIS A 1 48  ? -53.49100 37.71600 60.54200 1.000 42.54399  ? 48  HIS A C    1 
ATOM   711  O  O    . HIS A 1 48  ? -52.76200 36.74100 60.73300 1.000 42.75012  ? 48  HIS A O    1 
ATOM   712  C  CB   . HIS A 1 48  ? -53.09900 38.93100 58.40800 1.000 47.00416  ? 48  HIS A CB   1 
ATOM   713  C  CG   . HIS A 1 48  ? -52.67700 40.17100 57.69100 1.000 58.25734  ? 48  HIS A CG   1 
ATOM   714  N  ND1  . HIS A 1 48  ? -52.12200 41.25600 58.33500 1.000 73.12601  ? 48  HIS A ND1  1 
ATOM   715  C  CD2  . HIS A 1 48  ? -52.71900 40.49500 56.37700 1.000 73.55565  ? 48  HIS A CD2  1 
ATOM   716  C  CE1  . HIS A 1 48  ? -51.85000 42.19900 57.45100 1.000 72.99206  ? 48  HIS A CE1  1 
ATOM   717  N  NE2  . HIS A 1 48  ? -52.19900 41.76100 56.25500 1.000 70.59009  ? 48  HIS A NE2  1 
ATOM   718  H  H    . HIS A 1 48  ? -51.01600 38.66400 59.84600 1.000 55.13558  ? 48  HIS A H    1 
ATOM   719  H  HA   . HIS A 1 48  ? -53.44700 39.76000 60.26000 1.000 52.95558  ? 48  HIS A HA   1 
ATOM   720  H  HB2  . HIS A 1 48  ? -52.55900 38.19800 58.07300 1.000 54.28558  ? 48  HIS A HB2  1 
ATOM   721  H  HB3  . HIS A 1 48  ? -54.03400 38.77500 58.20100 1.000 54.28558  ? 48  HIS A HB3  1 
ATOM   722  H  HD2  . HIS A 1 48  ? -53.04000 39.96100 55.68700 1.000 85.64558  ? 48  HIS A HD2  1 
ATOM   723  H  HE1  . HIS A 1 48  ? -51.47700 43.03000 57.63900 1.000 84.59558  ? 48  HIS A HE1  1 
ATOM   724  H  HE2  . HIS A 1 48  ? -52.11500 42.19800 55.51900 1.000 81.73558  ? 48  HIS A HE2  1 
ATOM   725  N  N    . ASN A 1 49  ? -54.79600 37.71500 60.82300 1.000 46.55861  ? 49  ASN A N    1 
ATOM   726  C  CA   . ASN A 1 49  ? -55.44500 36.49300 61.28700 1.000 47.46666  ? 49  ASN A CA   1 
ATOM   727  C  C    . ASN A 1 49  ? -55.11000 35.31300 60.38700 1.000 43.84958  ? 49  ASN A C    1 
ATOM   728  O  O    . ASN A 1 49  ? -54.84200 34.20700 60.87200 1.000 41.65034  ? 49  ASN A O    1 
ATOM   729  C  CB   . ASN A 1 49  ? -56.96300 36.68200 61.33700 1.000 52.58846  ? 49  ASN A CB   1 
ATOM   730  C  CG   . ASN A 1 49  ? -57.40700 37.50400 62.51600 1.000 65.35134  ? 49  ASN A CG   1 
ATOM   731  O  OD1  . ASN A 1 49  ? -56.78300 37.47400 63.57900 1.000 79.64670  ? 49  ASN A OD1  1 
ATOM   732  N  ND2  . ASN A 1 49  ? -58.49600 38.24700 62.34100 1.000 77.15695  ? 49  ASN A ND2  1 
ATOM   733  H  H    . ASN A 1 49  ? -55.31700 38.39600 60.75400 1.000 53.63558  ? 49  ASN A H    1 
ATOM   734  H  HA   . ASN A 1 49  ? -55.12800 36.30300 62.18400 1.000 54.90558  ? 49  ASN A HA   1 
ATOM   735  H  HB2  . ASN A 1 49  ? -57.25200 37.13400 60.52900 1.000 60.56558  ? 49  ASN A HB2  1 
ATOM   736  H  HB3  . ASN A 1 49  ? -57.38800 35.81200 61.40000 1.000 60.56558  ? 49  ASN A HB3  1 
ATOM   737  H  HD21 . ASN A 1 49  ? -58.90500 38.23900 61.58500 1.000 88.99558  ? 49  ASN A HD21 1 
ATOM   738  H  HD22 . ASN A 1 49  ? -58.79100 38.73500 62.98500 1.000 88.99558  ? 49  ASN A HD22 1 
ATOM   739  N  N    . SER A 1 50  ? -55.14700 35.52600 59.07000 1.000 43.12893  ? 50  SER A N    1 
ATOM   740  C  CA   . SER A 1 50  ? -54.88400 34.46200 58.11100 1.000 53.15301  ? 50  SER A CA   1 
ATOM   741  C  C    . SER A 1 50  ? -53.46500 33.91400 58.20700 1.000 42.65655  ? 50  SER A C    1 
ATOM   742  O  O    . SER A 1 50  ? -53.19200 32.85100 57.64700 1.000 38.82982  ? 50  SER A O    1 
ATOM   743  C  CB   . SER A 1 50  ? -55.13800 34.97800 56.69400 1.000 56.04010  ? 50  SER A CB   1 
ATOM   744  O  OG   . SER A 1 50  ? -54.13300 35.90900 56.30900 1.000 50.79857  ? 50  SER A OG   1 
ATOM   745  H  H    . SER A 1 50  ? -55.32400 36.28500 58.70700 1.000 50.12558  ? 50  SER A H    1 
ATOM   746  H  HA   . SER A 1 50  ? -55.49500 33.72900 58.28600 1.000 62.51558  ? 50  SER A HA   1 
ATOM   747  H  HB2  . SER A 1 50  ? -55.12700 34.22900 56.07800 1.000 65.70558  ? 50  SER A HB2  1 
ATOM   748  H  HB3  . SER A 1 50  ? -56.00200 35.41700 56.66700 1.000 65.70558  ? 50  SER A HB3  1 
ATOM   749  H  HG   . SER A 1 50  ? -54.27800 36.18100 55.52800 1.000 59.42558  ? 50  SER A HG   1 
ATOM   750  N  N    . HIS A 1 51  ? -52.56000 34.60400 58.89500 1.000 39.62941  ? 51  HIS A N    1 
ATOM   751  C  CA   . HIS A 1 51  ? -51.19400 34.11700 59.03500 1.000 39.05699  ? 51  HIS A CA   1 
ATOM   752  C  C    . HIS A 1 51  ? -51.05500 33.00400 60.06500 1.000 39.05590  ? 51  HIS A C    1 
ATOM   753  O  O    . HIS A 1 51  ? -49.99700 32.36700 60.11700 1.000 34.67618  ? 51  HIS A O    1 
ATOM   754  C  CB   . HIS A 1 51  ? -50.27100 35.27100 59.41600 1.000 33.87381  ? 51  HIS A CB   1 
ATOM   755  C  CG   . HIS A 1 51  ? -50.05100 36.25500 58.31400 1.000 33.74570  ? 51  HIS A CG   1 
ATOM   756  N  ND1  . HIS A 1 51  ? -49.46900 37.48700 58.52400 1.000 36.00286  ? 51  HIS A ND1  1 
ATOM   757  C  CD2  . HIS A 1 51  ? -50.31500 36.18300 56.98900 1.000 38.00885  ? 51  HIS A CD2  1 
ATOM   758  C  CE1  . HIS A 1 51  ? -49.39300 38.13800 57.37600 1.000 42.70482  ? 51  HIS A CE1  1 
ATOM   759  N  NE2  . HIS A 1 51  ? -49.89200 37.36500 56.42600 1.000 37.35857  ? 51  HIS A NE2  1 
ATOM   760  H  H    . HIS A 1 51  ? -52.71200 35.35400 59.28900 1.000 46.79558  ? 51  HIS A H    1 
ATOM   761  H  HA   . HIS A 1 51  ? -50.90700 33.76200 58.17900 1.000 46.45558  ? 51  HIS A HA   1 
ATOM   762  H  HB2  . HIS A 1 51  ? -50.66000 35.74800 60.16500 1.000 40.07558  ? 51  HIS A HB2  1 
ATOM   763  H  HB3  . HIS A 1 51  ? -49.40600 34.90900 59.66600 1.000 40.07558  ? 51  HIS A HB3  1 
ATOM   764  H  HD2  . HIS A 1 51  ? -50.70900 35.46900 56.54200 1.000 44.93558  ? 51  HIS A HD2  1 
ATOM   765  H  HE1  . HIS A 1 51  ? -49.04800 38.99300 57.25600 1.000 50.16558  ? 51  HIS A HE1  1 
ATOM   766  H  HE2  . HIS A 1 51  ? -49.94400 37.56800 55.59200 1.000 43.90558  ? 51  HIS A HE2  1 
ATOM   767  N  N    . GLU A 1 52  ? -52.08900 32.74100 60.87100 1.000 41.54719  ? 52  GLU A N    1 
ATOM   768  C  CA   . GLU A 1 52  ? -51.94800 31.75900 61.93900 1.000 34.45517  ? 52  GLU A CA   1 
ATOM   769  C  C    . GLU A 1 52  ? -51.54900 30.40300 61.37400 1.000 35.42089  ? 52  GLU A C    1 
ATOM   770  O  O    . GLU A 1 52  ? -52.15800 29.90200 60.42100 1.000 35.65483  ? 52  GLU A O    1 
ATOM   771  C  CB   . GLU A 1 52  ? -53.24500 31.62500 62.74300 1.000 40.06923  ? 52  GLU A CB   1 
ATOM   772  C  CG   . GLU A 1 52  ? -53.07800 30.73400 63.97800 1.000 44.34184  ? 52  GLU A CG   1 
ATOM   773  C  CD   . GLU A 1 52  ? -53.80300 31.26700 65.20700 1.000 79.65551  ? 52  GLU A CD   1 
ATOM   774  O  OE1  . GLU A 1 52  ? -54.97700 31.69000 65.06700 1.000 57.65125  ? 52  GLU A OE1  1 
ATOM   775  O  OE2  . GLU A 1 52  ? -53.20300 31.24700 66.31200 1.000 57.09315  ? 52  GLU A OE2  1 
ATOM   776  H  H    . GLU A 1 52  ? -52.86300 33.11100 60.81800 1.000 49.43558  ? 52  GLU A H    1 
ATOM   777  H  HA   . GLU A 1 52  ? -51.25300 32.06500 62.54200 1.000 40.97558  ? 52  GLU A HA   1 
ATOM   778  H  HB2  . GLU A 1 52  ? -53.52600 32.50400 63.04100 1.000 47.44558  ? 52  GLU A HB2  1 
ATOM   779  H  HB3  . GLU A 1 52  ? -53.92900 31.23200 62.17800 1.000 47.44558  ? 52  GLU A HB3  1 
ATOM   780  H  HG2  . GLU A 1 52  ? -53.43500 29.85400 63.78100 1.000 52.51558  ? 52  GLU A HG2  1 
ATOM   781  H  HG3  . GLU A 1 52  ? -52.13500 30.66900 64.19400 1.000 52.51558  ? 52  GLU A HG3  1 
ATOM   782  N  N    . GLY A 1 53  ? -50.51200 29.81600 61.96900 1.000 36.36965  ? 53  GLY A N    1 
ATOM   783  C  CA   . GLY A 1 53  ? -50.03900 28.50500 61.60000 1.000 34.47707  ? 53  GLY A CA   1 
ATOM   784  C  C    . GLY A 1 53  ? -49.14500 28.47900 60.38900 1.000 31.94327  ? 53  GLY A C    1 
ATOM   785  O  O    . GLY A 1 53  ? -48.69600 27.39800 59.99500 1.000 30.94608  ? 53  GLY A O    1 
ATOM   786  H  H    . GLY A 1 53  ? -50.05900 30.17400 62.60600 1.000 43.67558  ? 53  GLY A H    1 
ATOM   787  H  HA2  . GLY A 1 53  ? -49.54100 28.13200 62.34500 1.000 41.64558  ? 53  GLY A HA2  1 
ATOM   788  H  HA3  . GLY A 1 53  ? -50.80400 27.93800 61.41700 1.000 41.64558  ? 53  GLY A HA3  1 
ATOM   789  N  N    . LYS A 1 54  ? -48.87900 29.62700 59.78400 1.000 30.59279  ? 54  LYS A N    1 
ATOM   790  C  CA   . LYS A 1 54  ? -48.07900 29.68000 58.57500 1.000 31.35544  ? 54  LYS A CA   1 
ATOM   791  C  C    . LYS A 1 54  ? -46.60000 29.76900 58.92500 1.000 29.89402  ? 54  LYS A C    1 
ATOM   792  O  O    . LYS A 1 54  ? -46.22000 30.13400 60.04100 1.000 29.84849  ? 54  LYS A O    1 
ATOM   793  C  CB   . LYS A 1 54  ? -48.49900 30.86600 57.70900 1.000 34.40604  ? 54  LYS A CB   1 
ATOM   794  C  CG   . LYS A 1 54  ? -49.78300 30.59200 56.92500 1.000 37.95741  ? 54  LYS A CG   1 
ATOM   795  C  CD   . LYS A 1 54  ? -50.02300 31.64700 55.85500 1.000 42.18234  ? 54  LYS A CD   1 
ATOM   796  C  CE   . LYS A 1 54  ? -51.45600 31.59700 55.34800 1.000 50.07985  ? 54  LYS A CE   1 
ATOM   797  N  NZ   . LYS A 1 54  ? -51.54400 31.97300 53.91000 1.000 65.90438  ? 54  LYS A NZ   1 
ATOM   798  H  H    . LYS A 1 54  ? -49.15400 30.39500 60.05800 1.000 37.22558  ? 54  LYS A H    1 
ATOM   799  H  HA   . LYS A 1 54  ? -48.21500 28.87200 58.05500 1.000 38.32558  ? 54  LYS A HA   1 
ATOM   800  H  HB2  . LYS A 1 54  ? -48.65200 31.63600 58.27900 1.000 41.89558  ? 54  LYS A HB2  1 
ATOM   801  H  HB3  . LYS A 1 54  ? -47.79300 31.06000 57.07300 1.000 41.89558  ? 54  LYS A HB3  1 
ATOM   802  H  HG2  . LYS A 1 54  ? -49.71500 29.72800 56.49100 1.000 46.10558  ? 54  LYS A HG2  1 
ATOM   803  H  HG3  . LYS A 1 54  ? -50.53800 30.59900 57.53400 1.000 46.10558  ? 54  LYS A HG3  1 
ATOM   804  H  HD2  . LYS A 1 54  ? -49.86000 32.52700 56.22700 1.000 50.99558  ? 54  LYS A HD2  1 
ATOM   805  H  HD3  . LYS A 1 54  ? -49.42800 31.48700 55.10500 1.000 50.99558  ? 54  LYS A HD3  1 
ATOM   806  H  HE2  . LYS A 1 54  ? -51.80000 30.69600 55.44800 1.000 60.21558  ? 54  LYS A HE2  1 
ATOM   807  H  HE3  . LYS A 1 54  ? -51.99800 32.21900 55.85900 1.000 60.21558  ? 54  LYS A HE3  1 
ATOM   808  H  HZ1  . LYS A 1 54  ? -52.39000 31.93400 53.63700 1.000 79.01558  ? 54  LYS A HZ1  1 
ATOM   809  H  HZ2  . LYS A 1 54  ? -51.24000 32.80200 53.79300 1.000 79.01558  ? 54  LYS A HZ2  1 
ATOM   810  H  HZ3  . LYS A 1 54  ? -51.05500 31.41500 53.41900 1.000 79.01558  ? 54  LYS A HZ3  1 
ATOM   811  N  N    . THR A 1 55  ? -45.77000 29.40700 57.95200 1.000 29.22744  ? 55  THR A N    1 
ATOM   812  C  CA   . THR A 1 55  ? -44.32500 29.38600 58.10700 1.000 27.99851  ? 55  THR A CA   1 
ATOM   813  C  C    . THR A 1 55  ? -43.71600 30.61600 57.45500 1.000 29.55467  ? 55  THR A C    1 
ATOM   814  O  O    . THR A 1 55  ? -43.99200 30.91500 56.28400 1.000 27.98210  ? 55  THR A O    1 
ATOM   815  C  CB   . THR A 1 55  ? -43.73500 28.11900 57.47500 1.000 30.08153  ? 55  THR A CB   1 
ATOM   816  O  OG1  . THR A 1 55  ? -44.18400 26.98400 58.21600 1.000 32.00022  ? 55  THR A OG1  1 
ATOM   817  C  CG2  . THR A 1 55  ? -42.20200 28.16400 57.49600 1.000 30.56872  ? 55  THR A CG2  1 
ATOM   818  H  H    . THR A 1 55  ? -46.03100 29.16400 57.17000 1.000 35.91558  ? 55  THR A H    1 
ATOM   819  H  HA   . THR A 1 55  ? -44.10400 29.39900 59.05200 1.000 34.36558  ? 55  THR A HA   1 
ATOM   820  H  HB   . THR A 1 55  ? -44.01900 28.04900 56.55100 1.000 37.01558  ? 55  THR A HB   1 
ATOM   821  H  HG1  . THR A 1 55  ? -43.85500 26.28200 57.89400 1.000 39.27558  ? 55  THR A HG1  1 
ATOM   822  H  HG21 . THR A 1 55  ? -41.84200 27.27600 57.34700 1.000 37.44558  ? 55  THR A HG21 1 
ATOM   823  H  HG22 . THR A 1 55  ? -41.87800 28.75600 56.79900 1.000 37.44558  ? 55  THR A HG22 1 
ATOM   824  H  HG23 . THR A 1 55  ? -41.89100 28.49000 58.35500 1.000 37.44558  ? 55  THR A HG23 1 
ATOM   825  N  N    . PHE A 1 56  ? -42.86000 31.29700 58.20000 1.000 24.68137  ? 56  PHE A N    1 
ATOM   826  C  CA   . PHE A 1 56  ? -42.13700 32.47000 57.72400 1.000 28.90639  ? 56  PHE A CA   1 
ATOM   827  C  C    . PHE A 1 56  ? -40.64400 32.19000 57.74000 1.000 27.23897  ? 56  PHE A C    1 
ATOM   828  O  O    . PHE A 1 56  ? -40.12900 31.59000 58.68900 1.000 28.31726  ? 56  PHE A O    1 
ATOM   829  C  CB   . PHE A 1 56  ? -42.45300 33.67700 58.62100 1.000 29.17949  ? 56  PHE A CB   1 
ATOM   830  C  CG   . PHE A 1 56  ? -43.88400 34.09300 58.56600 1.000 29.56984  ? 56  PHE A CG   1 
ATOM   831  C  CD1  . PHE A 1 56  ? -44.85000 33.40300 59.29300 1.000 31.57184  ? 56  PHE A CD1  1 
ATOM   832  C  CD2  . PHE A 1 56  ? -44.27500 35.16300 57.77900 1.000 32.13506  ? 56  PHE A CD2  1 
ATOM   833  C  CE1  . PHE A 1 56  ? -46.17600 33.78600 59.24000 1.000 32.59388  ? 56  PHE A CE1  1 
ATOM   834  C  CE2  . PHE A 1 56  ? -45.59700 35.54100 57.72100 1.000 30.52356  ? 56  PHE A CE2  1 
ATOM   835  C  CZ   . PHE A 1 56  ? -46.54700 34.85300 58.44800 1.000 32.93910  ? 56  PHE A CZ   1 
ATOM   836  H  H    . PHE A 1 56  ? -42.67400 31.09300 59.01500 1.000 30.07558  ? 56  PHE A H    1 
ATOM   837  H  HA   . PHE A 1 56  ? -42.39200 32.67700 56.81200 1.000 35.02558  ? 56  PHE A HA   1 
ATOM   838  H  HB2  . PHE A 1 56  ? -42.24400 33.44700 59.54100 1.000 35.04558  ? 56  PHE A HB2  1 
ATOM   839  H  HB3  . PHE A 1 56  ? -41.91200 34.42900 58.33600 1.000 35.04558  ? 56  PHE A HB3  1 
ATOM   840  H  HD1  . PHE A 1 56  ? -44.60000 32.67700 59.81900 1.000 37.97558  ? 56  PHE A HD1  1 
ATOM   841  H  HD2  . PHE A 1 56  ? -43.63900 35.62900 57.28500 1.000 38.56558  ? 56  PHE A HD2  1 
ATOM   842  H  HE1  . PHE A 1 56  ? -46.81500 33.32700 59.73600 1.000 39.16558  ? 56  PHE A HE1  1 
ATOM   843  H  HE2  . PHE A 1 56  ? -45.85100 36.26200 57.19200 1.000 36.54558  ? 56  PHE A HE2  1 
ATOM   844  H  HZ   . PHE A 1 56  ? -47.44000 35.10900 58.40400 1.000 39.47558  ? 56  PHE A HZ   1 
ATOM   845  N  N    . TYR A 1 57  ? -39.93500 32.63500 56.70000 1.000 29.31891  ? 57  TYR A N    1 
ATOM   846  C  CA   . TYR A 1 57  ? -38.48200 32.59400 56.74100 1.000 24.76417  ? 57  TYR A CA   1 
ATOM   847  C  C    . TYR A 1 57  ? -37.95700 33.79200 57.51600 1.000 27.08994  ? 57  TYR A C    1 
ATOM   848  O  O    . TYR A 1 57  ? -38.48800 34.90100 57.40000 1.000 30.35687  ? 57  TYR A O    1 
ATOM   849  C  CB   . TYR A 1 57  ? -37.86800 32.64100 55.34400 1.000 26.27447  ? 57  TYR A CB   1 
ATOM   850  C  CG   . TYR A 1 57  ? -37.83800 31.35200 54.59500 1.000 27.78032  ? 57  TYR A CG   1 
ATOM   851  C  CD1  . TYR A 1 57  ? -38.99600 30.81100 54.05800 1.000 26.98277  ? 57  TYR A CD1  1 
ATOM   852  C  CD2  . TYR A 1 57  ? -36.64100 30.68600 54.38200 1.000 30.91518  ? 57  TYR A CD2  1 
ATOM   853  C  CE1  . TYR A 1 57  ? -38.96200 29.64100 53.33300 1.000 30.98765  ? 57  TYR A CE1  1 
ATOM   854  C  CE2  . TYR A 1 57  ? -36.59700 29.50800 53.65200 1.000 27.29592  ? 57  TYR A CE2  1 
ATOM   855  C  CZ   . TYR A 1 57  ? -37.76200 28.99300 53.13700 1.000 26.90009  ? 57  TYR A CZ   1 
ATOM   856  O  OH   . TYR A 1 57  ? -37.73600 27.83500 52.39400 1.000 30.03487  ? 57  TYR A OH   1 
ATOM   857  H  H    . TYR A 1 57  ? -40.27000 32.95800 55.97600 1.000 35.43558  ? 57  TYR A H    1 
ATOM   858  H  HA   . TYR A 1 57  ? -38.21600 31.76300 57.16500 1.000 29.74558  ? 57  TYR A HA   1 
ATOM   859  H  HB2  . TYR A 1 57  ? -38.38000 33.26900 54.81000 1.000 31.71558  ? 57  TYR A HB2  1 
ATOM   860  H  HB3  . TYR A 1 57  ? -36.95100 32.94500 55.42600 1.000 31.71558  ? 57  TYR A HB3  1 
ATOM   861  H  HD1  . TYR A 1 57  ? -39.80800 31.24500 54.18900 1.000 33.10558  ? 57  TYR A HD1  1 
ATOM   862  H  HD2  . TYR A 1 57  ? -35.85500 31.03500 54.73400 1.000 37.38558  ? 57  TYR A HD2  1 
ATOM   863  H  HE1  . TYR A 1 57  ? -39.74600 29.28900 52.97800 1.000 38.08558  ? 57  TYR A HE1  1 
ATOM   864  H  HE2  . TYR A 1 57  ? -35.78800 29.07100 53.51300 1.000 33.21558  ? 57  TYR A HE2  1 
ATOM   865  H  HH   . TYR A 1 57  ? -38.50200 27.67000 52.09200 1.000 36.93558  ? 57  TYR A HH   1 
ATOM   866  N  N    . VAL A 1 58  ? -36.88500 33.57300 58.27300 1.000 30.36565  ? 58  VAL A N    1 
ATOM   867  C  CA   . VAL A 1 58  ? -36.18000 34.63600 58.96900 1.000 28.09430  ? 58  VAL A CA   1 
ATOM   868  C  C    . VAL A 1 58  ? -34.69300 34.48500 58.68200 1.000 29.47145  ? 58  VAL A C    1 
ATOM   869  O  O    . VAL A 1 58  ? -34.25300 33.51800 58.07400 1.000 31.21807  ? 58  VAL A O    1 
ATOM   870  C  CB   . VAL A 1 58  ? -36.44100 34.61500 60.48600 1.000 31.65128  ? 58  VAL A CB   1 
ATOM   871  C  CG1  . VAL A 1 58  ? -37.89900 34.92400 60.77400 1.000 32.40453  ? 58  VAL A CG1  1 
ATOM   872  C  CG2  . VAL A 1 58  ? -36.07300 33.26400 61.04900 1.000 32.94298  ? 58  VAL A CG2  1 
ATOM   873  H  H    . VAL A 1 58  ? -36.54100 32.79400 58.39900 1.000 35.64558  ? 58  VAL A H    1 
ATOM   874  H  HA   . VAL A 1 58  ? -36.47400 35.49400 58.62500 1.000 32.40558  ? 58  VAL A HA   1 
ATOM   875  H  HB   . VAL A 1 58  ? -35.89500 35.29200 60.91500 1.000 36.25558  ? 58  VAL A HB   1 
ATOM   876  H  HG11 . VAL A 1 58  ? -38.03900 34.92400 61.73400 1.000 37.40558  ? 58  VAL A HG11 1 
ATOM   877  H  HG12 . VAL A 1 58  ? -38.11600 35.79600 60.40900 1.000 37.40558  ? 58  VAL A HG12 1 
ATOM   878  H  HG13 . VAL A 1 58  ? -38.45400 34.24400 60.36000 1.000 37.40558  ? 58  VAL A HG13 1 
ATOM   879  H  HG21 . VAL A 1 58  ? -36.29500 33.24500 61.99300 1.000 37.63558  ? 58  VAL A HG21 1 
ATOM   880  H  HG22 . VAL A 1 58  ? -36.57300 32.57900 60.57800 1.000 37.63558  ? 58  VAL A HG22 1 
ATOM   881  H  HG23 . VAL A 1 58  ? -35.12100 33.12000 60.93000 1.000 37.63558  ? 58  VAL A HG23 1 
ATOM   882  N  N    . LEU A 1 59  ? -33.92200 35.45500 59.13600 1.000 31.87833  ? 59  LEU A N    1 
ATOM   883  C  CA   . LEU A 1 59  ? -32.47800 35.32300 59.00400 1.000 35.37579  ? 59  LEU A CA   1 
ATOM   884  C  C    . LEU A 1 59  ? -31.92100 34.50800 60.16900 1.000 36.84208  ? 59  LEU A C    1 
ATOM   885  O  O    . LEU A 1 59  ? -32.52900 34.44700 61.24000 1.000 40.29158  ? 59  LEU A O    1 
ATOM   886  C  CB   . LEU A 1 59  ? -31.81100 36.70500 58.96900 1.000 35.97177  ? 59  LEU A CB   1 
ATOM   887  C  CG   . LEU A 1 59  ? -32.29600 37.64400 57.86700 1.000 34.44030  ? 59  LEU A CG   1 
ATOM   888  C  CD1  . LEU A 1 59  ? -31.45300 38.92600 57.81900 1.000 37.19333  ? 59  LEU A CD1  1 
ATOM   889  C  CD2  . LEU A 1 59  ? -32.27700 36.94700 56.49300 1.000 35.84192  ? 59  LEU A CD2  1 
ATOM   890  H  H    . LEU A 1 59  ? -34.19700 36.17700 59.51300 1.000 36.11558  ? 59  LEU A H    1 
ATOM   891  H  HA   . LEU A 1 59  ? -32.26100 34.86900 58.17400 1.000 39.88558  ? 59  LEU A HA   1 
ATOM   892  H  HB2  . LEU A 1 59  ? -31.97800 37.14400 59.81700 1.000 40.18558  ? 59  LEU A HB2  1 
ATOM   893  H  HB3  . LEU A 1 59  ? -30.85800 36.57900 58.84200 1.000 40.18558  ? 59  LEU A HB3  1 
ATOM   894  H  HG   . LEU A 1 59  ? -33.21200 37.89100 58.06800 1.000 38.76558  ? 59  LEU A HG   1 
ATOM   895  H  HD11 . LEU A 1 59  ? -31.77800 39.49100 57.10100 1.000 41.56558  ? 59  LEU A HD11 1 
ATOM   896  H  HD12 . LEU A 1 59  ? -31.53600 39.38900 58.66800 1.000 41.56558  ? 59  LEU A HD12 1 
ATOM   897  H  HD13 . LEU A 1 59  ? -30.52600 38.68900 57.66000 1.000 41.56558  ? 59  LEU A HD13 1 
ATOM   898  H  HD21 . LEU A 1 59  ? -32.44000 37.60800 55.80200 1.000 40.96558  ? 59  LEU A HD21 1 
ATOM   899  H  HD22 . LEU A 1 59  ? -31.40900 36.53500 56.35900 1.000 40.96558  ? 59  LEU A HD22 1 
ATOM   900  H  HD23 . LEU A 1 59  ? -32.97200 36.27000 56.47300 1.000 40.96558  ? 59  LEU A HD23 1 
ATOM   901  N  N    . PRO A 1 60  ? -30.76500 33.85000 59.98500 1.000 37.64809  ? 60  PRO A N    1 
ATOM   902  C  CA   . PRO A 1 60  ? -30.19400 33.07400 61.09600 1.000 36.81434  ? 60  PRO A CA   1 
ATOM   903  C  C    . PRO A 1 60  ? -29.69400 33.98000 62.20700 1.000 44.23408  ? 60  PRO A C    1 
ATOM   904  O  O    . PRO A 1 60  ? -28.54700 34.43800 62.19100 1.000 47.58068  ? 60  PRO A O    1 
ATOM   905  C  CB   . PRO A 1 60  ? -29.06500 32.26800 60.43600 1.000 42.54868  ? 60  PRO A CB   1 
ATOM   906  C  CG   . PRO A 1 60  ? -29.21600 32.45000 58.96800 1.000 42.87730  ? 60  PRO A CG   1 
ATOM   907  C  CD   . PRO A 1 60  ? -29.96400 33.73000 58.75700 1.000 37.71509  ? 60  PRO A CD   1 
ATOM   908  H  HA   . PRO A 1 60  ? -30.84000 32.44500 61.45500 1.000 39.93558  ? 60  PRO A HA   1 
ATOM   909  H  HB2  . PRO A 1 60  ? -28.20800 32.60800 60.73500 1.000 46.60558  ? 60  PRO A HB2  1 
ATOM   910  H  HB3  . PRO A 1 60  ? -29.15300 31.33200 60.67500 1.000 46.60558  ? 60  PRO A HB3  1 
ATOM   911  H  HG2  . PRO A 1 60  ? -28.33900 32.49900 58.55800 1.000 47.73558  ? 60  PRO A HG2  1 
ATOM   912  H  HG3  . PRO A 1 60  ? -29.71300 31.70200 58.60100 1.000 47.73558  ? 60  PRO A HG3  1 
ATOM   913  H  HD2  . PRO A 1 60  ? -29.35300 34.47800 58.66700 1.000 41.91558  ? 60  PRO A HD2  1 
ATOM   914  H  HD3  . PRO A 1 60  ? -30.53600 33.67300 57.97500 1.000 41.91558  ? 60  PRO A HD3  1 
ATOM   915  N  N    . ASN A 1 61  ? -30.55100 34.23500 63.20300 1.000 51.54663  ? 61  ASN A N    1 
ATOM   916  C  CA   . ASN A 1 61  ? -30.22400 35.20300 64.28900 1.000 58.92407  ? 61  ASN A CA   1 
ATOM   917  C  C    . ASN A 1 61  ? -29.63500 34.45900 65.48900 1.000 62.25151  ? 61  ASN A C    1 
ATOM   918  O  O    . ASN A 1 61  ? -28.59600 34.92500 66.00400 1.000 68.74771  ? 61  ASN A O    1 
ATOM   919  C  CB   . ASN A 1 61  ? -31.43800 36.04800 64.66900 1.000 69.92923  ? 61  ASN A CB   1 
ATOM   920  C  CG   . ASN A 1 61  ? -32.64900 35.22800 65.04500 1.000 70.16611  ? 61  ASN A CG   1 
ATOM   921  O  OD1  . ASN A 1 61  ? -32.85400 34.92600 66.22500 1.000 79.17703  ? 61  ASN A OD1  1 
ATOM   922  N  ND2  . ASN A 1 61  ? -33.46300 34.86800 64.06300 1.000 55.94771  ? 61  ASN A ND2  1 
ATOM   923  H  H    . ASN A 1 61  ? -31.33000 33.78700 63.28000 1.000 56.66558  ? 61  ASN A H    1 
ATOM   924  H  HA   . ASN A 1 61  ? -29.54200 35.82400 63.95500 1.000 64.68558  ? 61  ASN A HA   1 
ATOM   925  H  HB2  . ASN A 1 61  ? -31.19900 36.62300 65.42300 1.000 78.20558  ? 61  ASN A HB2  1 
ATOM   926  H  HB3  . ASN A 1 61  ? -31.67000 36.62400 63.91400 1.000 78.20558  ? 61  ASN A HB3  1 
ATOM   927  H  HD21 . ASN A 1 61  ? -33.28800 35.11900 63.23000 1.000 62.78558  ? 61  ASN A HD21 1 
ATOM   928  H  HD22 . ASN A 1 61  ? -34.16900 34.36300 64.23600 1.000 62.78558  ? 61  ASN A HD22 1 
ATOM   929  N  N    . ASP A 1 62  ? -30.14900 33.28400 65.83300 1.000 48.97416  ? 62  ASP A N    1 
ATOM   930  C  CA   . ASP A 1 62  ? -29.66400 32.52700 67.01300 1.000 48.68588  ? 62  ASP A CA   1 
ATOM   931  C  C    . ASP A 1 62  ? -28.71700 31.42500 66.54200 1.000 54.06050  ? 62  ASP A C    1 
ATOM   932  O  O    . ASP A 1 62  ? -28.57800 31.27200 65.34100 1.000 44.74192  ? 62  ASP A O    1 
ATOM   933  C  CB   . ASP A 1 62  ? -30.83200 31.93500 67.80500 1.000 35.85144  ? 62  ASP A CB   1 
ATOM   934  C  CG   . ASP A 1 62  ? -31.70400 31.02500 66.96300 1.000 34.97598  ? 62  ASP A CG   1 
ATOM   935  O  OD1  . ASP A 1 62  ? -31.15400 30.13600 66.28100 1.000 34.87825  ? 62  ASP A OD1  1 
ATOM   936  O  OD2  . ASP A 1 62  ? -32.94900 31.12500 66.92100 1.000 34.40944  ? 62  ASP A OD2  1 
ATOM   937  H  H    . ASP A 1 62  ? -30.78300 32.88100 65.41300 1.000 43.12558  ? 62  ASP A H    1 
ATOM   938  H  HA   . ASP A 1 62  ? -29.18900 33.13100 67.60600 1.000 41.98558  ? 62  ASP A HA   1 
ATOM   939  H  HB2  . ASP A 1 62  ? -30.48600 31.43600 68.56200 1.000 29.28558  ? 62  ASP A HB2  1 
ATOM   940  H  HB3  . ASP A 1 62  ? -31.37300 32.65600 68.16400 1.000 29.28558  ? 62  ASP A HB3  1 
ATOM   941  N  N    . ASP A 1 63  ? -28.08800 30.71400 67.46700 1.000 47.70198  ? 63  ASP A N    1 
ATOM   942  C  CA   . ASP A 1 63  ? -27.11100 29.65300 67.14400 1.000 43.77256  ? 63  ASP A CA   1 
ATOM   943  C  C    . ASP A 1 63  ? -27.83900 28.45500 66.54400 1.000 47.13941  ? 63  ASP A C    1 
ATOM   944  O  O    . ASP A 1 63  ? -27.28000 27.71200 65.72000 1.000 38.77397  ? 63  ASP A O    1 
ATOM   945  C  CB   . ASP A 1 63  ? -26.36800 29.19100 68.38000 1.000 48.46533  ? 63  ASP A CB   1 
ATOM   946  C  CG   . ASP A 1 63  ? -25.44100 30.20500 69.03200 1.000 70.87626  ? 63  ASP A CG   1 
ATOM   947  O  OD1  . ASP A 1 63  ? -25.18100 31.24800 68.41000 1.000 53.13213  ? 63  ASP A OD1  1 
ATOM   948  O  OD2  . ASP A 1 63  ? -24.98800 29.93300 70.15800 1.000 61.70085  ? 63  ASP A OD2  1 
ATOM   949  H  H    . ASP A 1 63  ? -28.25500 30.83300 68.34300 1.000 51.87558  ? 63  ASP A H    1 
ATOM   950  H  HA   . ASP A 1 63  ? -26.47300 30.00200 66.48100 1.000 47.64558  ? 63  ASP A HA   1 
ATOM   951  H  HB2  . ASP A 1 63  ? -27.03200 28.91400 69.04400 1.000 52.78558  ? 63  ASP A HB2  1 
ATOM   952  H  HB3  . ASP A 1 63  ? -25.83500 28.40600 68.14100 1.000 52.78558  ? 63  ASP A HB3  1 
ATOM   953  N  N    . THR A 1 64  ? -29.06700 28.18200 66.96500 1.000 40.73598  ? 64  THR A N    1 
ATOM   954  C  CA   . THR A 1 64  ? -29.81000 27.10900 66.42600 1.000 41.06363  ? 64  THR A CA   1 
ATOM   955  C  C    . THR A 1 64  ? -30.05200 27.27600 64.97000 1.000 38.47975  ? 64  THR A C    1 
ATOM   956  O  O    . THR A 1 64  ? -29.81700 26.35700 64.21100 1.000 34.49693  ? 64  THR A O    1 
ATOM   957  C  CB   . THR A 1 64  ? -31.13500 26.85000 67.20100 1.000 40.49216  ? 64  THR A CB   1 
ATOM   958  O  OG1  . THR A 1 64  ? -30.74500 26.24500 68.42700 1.000 41.61082  ? 64  THR A OG1  1 
ATOM   959  C  CG2  . THR A 1 64  ? -32.11000 25.95500 66.46000 1.000 42.84494  ? 64  THR A CG2  1 
ATOM   960  H  H    . THR A 1 64  ? -29.53100 28.66800 67.56800 1.000 44.68558  ? 64  THR A H    1 
ATOM   961  H  HA   . THR A 1 64  ? -29.21800 26.26000 66.52700 1.000 45.58558  ? 64  THR A HA   1 
ATOM   962  H  HB   . THR A 1 64  ? -31.55300 27.72500 67.37800 1.000 44.66558  ? 64  THR A HB   1 
ATOM   963  H  HG1  . THR A 1 64  ? -30.47900 25.44000 68.26700 1.000 45.78558  ? 64  THR A HG1  1 
ATOM   964  H  HG21 . THR A 1 64  ? -32.77800 25.62300 67.08100 1.000 47.92558  ? 64  THR A HG21 1 
ATOM   965  H  HG22 . THR A 1 64  ? -32.54900 26.46200 65.75500 1.000 47.92558  ? 64  THR A HG22 1 
ATOM   966  H  HG23 . THR A 1 64  ? -31.63100 25.20500 66.06900 1.000 47.92558  ? 64  THR A HG23 1 
ATOM   967  N  N    . LEU A 1 65  ? -30.46900 28.47600 64.58300 1.000 32.79477  ? 65  LEU A N    1 
ATOM   968  C  CA   . LEU A 1 65  ? -30.75300 28.80500 63.19300 1.000 30.97002  ? 65  LEU A CA   1 
ATOM   969  C  C    . LEU A 1 65  ? -29.48300 28.85300 62.35500 1.000 32.70573  ? 65  LEU A C    1 
ATOM   970  O  O    . LEU A 1 65  ? -29.49600 28.45300 61.18300 1.000 30.08143  ? 65  LEU A O    1 
ATOM   971  C  CB   . LEU A 1 65  ? -31.49000 30.13500 63.10700 1.000 38.20552  ? 65  LEU A CB   1 
ATOM   972  C  CG   . LEU A 1 65  ? -32.90700 30.17000 63.67600 1.000 40.25530  ? 65  LEU A CG   1 
ATOM   973  C  CD1  . LEU A 1 65  ? -33.49100 31.56400 63.54400 1.000 41.79859  ? 65  LEU A CD1  1 
ATOM   974  C  CD2  . LEU A 1 65  ? -33.80500 29.14100 62.99300 1.000 37.27830  ? 65  LEU A CD2  1 
ATOM   975  H  H    . LEU A 1 65  ? -30.61900 29.11700 65.13700 1.000 36.08558  ? 65  LEU A H    1 
ATOM   976  H  HA   . LEU A 1 65  ? -31.32700 28.11400 62.82800 1.000 34.33558  ? 65  LEU A HA   1 
ATOM   977  H  HB2  . LEU A 1 65  ? -30.97200 30.79700 63.59200 1.000 42.59558  ? 65  LEU A HB2  1 
ATOM   978  H  HB3  . LEU A 1 65  ? -31.55300 30.38400 62.17200 1.000 42.59558  ? 65  LEU A HB3  1 
ATOM   979  H  HG   . LEU A 1 65  ? -32.87000 29.94100 64.61800 1.000 44.78558  ? 65  LEU A HG   1 
ATOM   980  H  HD11 . LEU A 1 65  ? -34.39000 31.56500 63.90800 1.000 46.03558  ? 65  LEU A HD11 1 
ATOM   981  H  HD12 . LEU A 1 65  ? -32.93400 32.18700 64.03600 1.000 46.03558  ? 65  LEU A HD12 1 
ATOM   982  H  HD13 . LEU A 1 65  ? -33.51300 31.80900 62.60600 1.000 46.03558  ? 65  LEU A HD13 1 
ATOM   983  H  HD21 . LEU A 1 65  ? -34.72500 29.29800 63.25900 1.000 41.78558  ? 65  LEU A HD21 1 
ATOM   984  H  HD22 . LEU A 1 65  ? -33.71900 29.23600 62.03100 1.000 41.78558  ? 65  LEU A HD22 1 
ATOM   985  H  HD23 . LEU A 1 65  ? -33.53000 28.25200 63.26400 1.000 41.78558  ? 65  LEU A HD23 1 
ATOM   986  N  N    . ARG A 1 66  ? -28.39300 29.33500 62.93800 1.000 30.90719  ? 66  ARG A N    1 
ATOM   987  C  CA   . ARG A 1 66  ? -27.11400 29.42300 62.20600 1.000 31.39620  ? 66  ARG A CA   1 
ATOM   988  C  C    . ARG A 1 66  ? -26.67300 28.01500 61.78600 1.000 31.62819  ? 66  ARG A C    1 
ATOM   989  O  O    . ARG A 1 66  ? -26.21100 27.87500 60.67700 1.000 31.23771  ? 66  ARG A O    1 
ATOM   990  C  CB   . ARG A 1 66  ? -26.06900 30.10500 63.08300 1.000 39.52995  ? 66  ARG A CB   1 
ATOM   991  C  CG   . ARG A 1 66  ? -26.20100 31.61700 63.11100 1.000 48.85630  ? 66  ARG A CG   1 
ATOM   992  C  CD   . ARG A 1 66  ? -25.41700 32.18200 64.27100 1.000 69.46593  ? 66  ARG A CD   1 
ATOM   993  N  NE   . ARG A 1 66  ? -25.83500 33.55400 64.57100 1.000 78.97731  ? 66  ARG A NE   1 
ATOM   994  C  CZ   . ARG A 1 66  ? -25.84100 34.10900 65.77200 1.000 94.77752  ? 66  ARG A CZ   1 
ATOM   995  N  NH1  . ARG A 1 66  ? -25.50200 33.41300 66.84000 1.000 79.11838  ? 66  ARG A NH1  1 
ATOM   996  N  NH2  . ARG A 1 66  ? -26.23800 35.35800 65.91400 1.000 69.14109  ? 66  ARG A NH2  1 
ATOM   997  H  H    . ARG A 1 66  ? -28.38400 29.62600 63.79300 1.000 34.10558  ? 66  ARG A H    1 
ATOM   998  H  HA   . ARG A 1 66  ? -27.25700 29.97100 61.39400 1.000 34.83558  ? 66  ARG A HA   1 
ATOM   999  H  HB2  . ARG A 1 66  ? -26.15400 29.76200 63.99800 1.000 43.95558  ? 66  ARG A HB2  1 
ATOM   1000 H  HB3  . ARG A 1 66  ? -25.17600 29.87000 62.75400 1.000 43.95558  ? 66  ARG A HB3  1 
ATOM   1001 H  HG2  . ARG A 1 66  ? -25.86200 31.99400 62.27200 1.000 54.57558  ? 66  ARG A HG2  1 
ATOM   1002 H  HG3  . ARG A 1 66  ? -27.14600 31.86400 63.20500 1.000 54.57558  ? 66  ARG A HG3  1 
ATOM   1003 H  HD2  . ARG A 1 66  ? -25.55900 31.61700 65.05700 1.000 78.48558  ? 66  ARG A HD2  1 
ATOM   1004 H  HD3  . ARG A 1 66  ? -24.46400 32.17300 64.05500 1.000 78.48558  ? 66  ARG A HD3  1 
ATOM   1005 H  HE   . ARG A 1 66  ? -26.11300 34.04300 63.90800 1.000 89.13558  ? 66  ARG A HE   1 
ATOM   1006 H  HH11 . ARG A 1 66  ? -24.72000 33.00600 66.87600 1.000 76.05558  ? 66  ARG A HH11 1 
ATOM   1007 H  HH12 . ARG A 1 66  ? -26.07100 33.34800 67.51300 1.000 76.05558  ? 66  ARG A HH12 1 
ATOM   1008 H  HH21 . ARG A 1 66  ? -26.73800 35.58000 66.60800 1.000 89.78558  ? 66  ARG A HH21 1 
ATOM   1009 H  HH22 . ARG A 1 66  ? -26.00200 35.96100 65.31300 1.000 89.78558  ? 66  ARG A HH22 1 
ATOM   1010 N  N    . VAL A 1 67  ? -26.79200 27.02400 62.65800 1.000 31.89067  ? 67  VAL A N    1 
ATOM   1011 C  CA   . VAL A 1 67  ? -26.41900 25.64900 62.33300 1.000 30.11148  ? 67  VAL A CA   1 
ATOM   1012 C  C    . VAL A 1 67  ? -27.37200 25.06300 61.29400 1.000 28.11348  ? 67  VAL A C    1 
ATOM   1013 O  O    . VAL A 1 67  ? -26.94000 24.42000 60.32800 1.000 29.37103  ? 67  VAL A O    1 
ATOM   1014 C  CB   . VAL A 1 67  ? -26.39100 24.78700 63.60500 1.000 40.47848  ? 67  VAL A CB   1 
ATOM   1015 C  CG1  . VAL A 1 67  ? -26.20700 23.32600 63.24000 1.000 36.17224  ? 67  VAL A CG1  1 
ATOM   1016 C  CG2  . VAL A 1 67  ? -25.28600 25.26300 64.53300 1.000 44.78851  ? 67  VAL A CG2  1 
ATOM   1017 H  H    . VAL A 1 67  ? -27.07500 27.13500 63.46300 1.000 35.75558  ? 67  VAL A H    1 
ATOM   1018 H  HA   . VAL A 1 67  ? -25.52800 25.66000 61.95000 1.000 33.79558  ? 67  VAL A HA   1 
ATOM   1019 H  HB   . VAL A 1 67  ? -27.23500 24.87400 64.07600 1.000 45.81558  ? 67  VAL A HB   1 
ATOM   1020 H  HG11 . VAL A 1 67  ? -25.91500 22.83900 64.02600 1.000 40.65558  ? 67  VAL A HG11 1 
ATOM   1021 H  HG12 . VAL A 1 67  ? -27.05200 22.97000 62.92500 1.000 40.65558  ? 67  VAL A HG12 1 
ATOM   1022 H  HG13 . VAL A 1 67  ? -25.53800 23.25700 62.54100 1.000 40.65558  ? 67  VAL A HG13 1 
ATOM   1023 H  HG21 . VAL A 1 67  ? -25.28000 24.70800 65.32800 1.000 50.48558  ? 67  VAL A HG21 1 
ATOM   1024 H  HG22 . VAL A 1 67  ? -24.43500 25.19200 64.07300 1.000 50.48558  ? 67  VAL A HG22 1 
ATOM   1025 H  HG23 . VAL A 1 67  ? -25.45400 26.18700 64.77700 1.000 50.48558  ? 67  VAL A HG23 1 
ATOM   1026 N  N    . GLU A 1 68  ? -28.68200 25.25100 61.48200 1.000 31.21328  ? 68  GLU A N    1 
ATOM   1027 C  CA   . GLU A 1 68  ? -29.63900 24.72700 60.50700 1.000 30.66571  ? 68  GLU A CA   1 
ATOM   1028 C  C    . GLU A 1 68  ? -29.40000 25.32700 59.12600 1.000 29.62052  ? 68  GLU A C    1 
ATOM   1029 O  O    . GLU A 1 68  ? -29.46600 24.62200 58.11500 1.000 25.95875  ? 68  GLU A O    1 
ATOM   1030 C  CB   . GLU A 1 68  ? -31.07500 24.99600 60.95700 1.000 27.01506  ? 68  GLU A CB   1 
ATOM   1031 C  CG   . GLU A 1 68  ? -31.45700 24.20100 62.19100 1.000 32.93783  ? 68  GLU A CG   1 
ATOM   1032 C  CD   . GLU A 1 68  ? -32.82300 24.54300 62.74800 1.000 39.65845  ? 68  GLU A CD   1 
ATOM   1033 O  OE1  . GLU A 1 68  ? -33.42600 25.53600 62.29600 1.000 34.65473  ? 68  GLU A OE1  1 
ATOM   1034 O  OE2  . GLU A 1 68  ? -33.27700 23.82300 63.67000 1.000 36.74952  ? 68  GLU A OE2  1 
ATOM   1035 H  H    . GLU A 1 68  ? -29.03300 25.66800 62.14800 1.000 35.63558  ? 68  GLU A H    1 
ATOM   1036 H  HA   . GLU A 1 68  ? -29.52100 23.76600 60.45300 1.000 35.34558  ? 68  GLU A HA   1 
ATOM   1037 H  HB2  . GLU A 1 68  ? -31.17000 25.93900 61.16500 1.000 30.89558  ? 68  GLU A HB2  1 
ATOM   1038 H  HB3  . GLU A 1 68  ? -31.68200 24.75200 60.24100 1.000 30.89558  ? 68  GLU A HB3  1 
ATOM   1039 H  HG2  . GLU A 1 68  ? -31.46000 23.25700 61.96400 1.000 37.62558  ? 68  GLU A HG2  1 
ATOM   1040 H  HG3  . GLU A 1 68  ? -30.80400 24.37300 62.88700 1.000 37.62558  ? 68  GLU A HG3  1 
ATOM   1041 N  N    . ALA A 1 69  ? -29.12100 26.63000 59.06100 1.000 27.74279  ? 69  ALA A N    1 
ATOM   1042 C  CA   . ALA A 1 69  ? -28.89200 27.26900 57.77400 1.000 25.52742  ? 69  ALA A CA   1 
ATOM   1043 C  C    . ALA A 1 69  ? -27.61800 26.74900 57.11200 1.000 26.42864  ? 69  ALA A C    1 
ATOM   1044 O  O    . ALA A 1 69  ? -27.60600 26.46700 55.90500 1.000 25.92128  ? 69  ALA A O    1 
ATOM   1045 C  CB   . ALA A 1 69  ? -28.84100 28.79100 57.94400 1.000 27.96360  ? 69  ALA A CB   1 
ATOM   1046 H  H    . ALA A 1 69  ? -29.06000 27.15500 59.73900 1.000 32.14558  ? 69  ALA A H    1 
ATOM   1047 H  HA   . ALA A 1 69  ? -29.63500 27.06300 57.18600 1.000 29.75558  ? 69  ALA A HA   1 
ATOM   1048 H  HB1  . ALA A 1 69  ? -28.68900 29.20000 57.07800 1.000 32.35558  ? 69  ALA A HB1  1 
ATOM   1049 H  HB2  . ALA A 1 69  ? -29.68500 29.09600 58.31100 1.000 32.35558  ? 69  ALA A HB2  1 
ATOM   1050 H  HB3  . ALA A 1 69  ? -28.11600 29.01600 58.54900 1.000 32.35558  ? 69  ALA A HB3  1 
ATOM   1051 N  N    . PHE A 1 70  ? -26.54100 26.59500 57.87900 1.000 25.37204  ? 70  PHE A N    1 
ATOM   1052 C  CA   . PHE A 1 70  ? -25.33100 26.07700 57.26900 1.000 26.71429  ? 70  PHE A CA   1 
ATOM   1053 C  C    . PHE A 1 70  ? -25.52300 24.64200 56.80800 1.000 29.17647  ? 70  PHE A C    1 
ATOM   1054 O  O    . PHE A 1 70  ? -25.07900 24.27200 55.72300 1.000 27.05411  ? 70  PHE A O    1 
ATOM   1055 C  CB   . PHE A 1 70  ? -24.13400 26.13000 58.21000 1.000 29.69127  ? 70  PHE A CB   1 
ATOM   1056 C  CG   . PHE A 1 70  ? -22.88200 25.64200 57.55300 1.000 28.28585  ? 70  PHE A CG   1 
ATOM   1057 C  CD1  . PHE A 1 70  ? -22.26600 26.41400 56.57700 1.000 28.98663  ? 70  PHE A CD1  1 
ATOM   1058 C  CD2  . PHE A 1 70  ? -22.36700 24.38700 57.83600 1.000 32.93737  ? 70  PHE A CD2  1 
ATOM   1059 C  CE1  . PHE A 1 70  ? -21.14000 25.95800 55.92200 1.000 32.59646  ? 70  PHE A CE1  1 
ATOM   1060 C  CE2  . PHE A 1 70  ? -21.22300 23.92500 57.17700 1.000 36.59461  ? 70  PHE A CE2  1 
ATOM   1061 C  CZ   . PHE A 1 70  ? -20.60300 24.71600 56.23800 1.000 31.73961  ? 70  PHE A CZ   1 
ATOM   1062 H  H    . PHE A 1 70  ? -26.49100 26.77600 58.71800 1.000 29.41558  ? 70  PHE A H    1 
ATOM   1063 H  HA   . PHE A 1 70  ? -25.13600 26.65100 56.51200 1.000 31.06558  ? 70  PHE A HA   1 
ATOM   1064 H  HB2  . PHE A 1 70  ? -23.99100 27.04700 58.49200 1.000 34.18558  ? 70  PHE A HB2  1 
ATOM   1065 H  HB3  . PHE A 1 70  ? -24.31000 25.57000 58.98200 1.000 34.18558  ? 70  PHE A HB3  1 
ATOM   1066 H  HD1  . PHE A 1 70  ? -22.61600 27.24900 56.36200 1.000 33.41558  ? 70  PHE A HD1  1 
ATOM   1067 H  HD2  . PHE A 1 70  ? -22.78400 23.84800 58.46900 1.000 37.76558  ? 70  PHE A HD2  1 
ATOM   1068 H  HE1  . PHE A 1 70  ? -20.74000 26.48300 55.26700 1.000 37.65558  ? 70  PHE A HE1  1 
ATOM   1069 H  HE2  . PHE A 1 70  ? -20.88100 23.08300 57.37400 1.000 41.98558  ? 70  PHE A HE2  1 
ATOM   1070 H  HZ   . PHE A 1 70  ? -19.82800 24.42100 55.81800 1.000 36.33558  ? 70  PHE A HZ   1 
ATOM   1071 N  N    . GLU A 1 71  ? -26.17100 23.81700 57.62400 1.000 26.19166  ? 71  GLU A N    1 
ATOM   1072 C  CA   . GLU A 1 71  ? -26.34900 22.42500 57.21600 1.000 26.83382  ? 71  GLU A CA   1 
ATOM   1073 C  C    . GLU A 1 71  ? -27.18900 22.31100 55.94800 1.000 25.78603  ? 71  GLU A C    1 
ATOM   1074 O  O    . GLU A 1 71  ? -26.96900 21.40200 55.14500 1.000 29.00828  ? 71  GLU A O    1 
ATOM   1075 C  CB   . GLU A 1 71  ? -26.98100 21.62300 58.34700 1.000 29.79076  ? 71  GLU A CB   1 
ATOM   1076 C  CG   . GLU A 1 71  ? -26.00400 21.31300 59.49600 1.000 38.64313  ? 71  GLU A CG   1 
ATOM   1077 C  CD   . GLU A 1 71  ? -24.72900 20.59400 59.03500 1.000 61.71813  ? 71  GLU A CD   1 
ATOM   1078 O  OE1  . GLU A 1 71  ? -24.83000 19.55100 58.34100 1.000 73.26655  ? 71  GLU A OE1  1 
ATOM   1079 O  OE2  . GLU A 1 71  ? -23.62600 21.08500 59.36900 1.000 46.05984  ? 71  GLU A OE2  1 
ATOM   1080 H  H    . GLU A 1 71  ? -26.50500 24.02700 58.38800 1.000 30.32558  ? 71  GLU A H    1 
ATOM   1081 H  HA   . GLU A 1 71  ? -25.47700 22.04300 57.03000 1.000 30.97558  ? 71  GLU A HA   1 
ATOM   1082 H  HB2  . GLU A 1 71  ? -27.72200 22.12900 58.71400 1.000 34.15558  ? 71  GLU A HB2  1 
ATOM   1083 H  HB3  . GLU A 1 71  ? -27.30000 20.77800 57.99100 1.000 34.15558  ? 71  GLU A HB3  1 
ATOM   1084 H  HG2  . GLU A 1 71  ? -25.74000 22.14700 59.91600 1.000 44.26558  ? 71  GLU A HG2  1 
ATOM   1085 H  HG3  . GLU A 1 71  ? -26.45000 20.74300 60.14100 1.000 44.26558  ? 71  GLU A HG3  1 
ATOM   1086 N  N    . TYR A 1 72  ? -28.15000 23.21700 55.74900 1.000 25.67864  ? 72  TYR A N    1 
ATOM   1087 C  CA   . TYR A 1 72  ? -29.03000 23.11700 54.58500 1.000 24.89128  ? 72  TYR A CA   1 
ATOM   1088 C  C    . TYR A 1 72  ? -28.39800 23.75200 53.35000 1.000 23.30798  ? 72  TYR A C    1 
ATOM   1089 O  O    . TYR A 1 72  ? -28.49200 23.20000 52.24800 1.000 24.14303  ? 72  TYR A O    1 
ATOM   1090 C  CB   . TYR A 1 72  ? -30.39700 23.76200 54.88500 1.000 25.48473  ? 72  TYR A CB   1 
ATOM   1091 C  CG   . TYR A 1 72  ? -31.49300 23.28600 53.94200 1.000 23.01919  ? 72  TYR A CG   1 
ATOM   1092 C  CD1  . TYR A 1 72  ? -31.84900 21.94700 53.88100 1.000 26.79877  ? 72  TYR A CD1  1 
ATOM   1093 C  CD2  . TYR A 1 72  ? -32.13800 24.17000 53.09400 1.000 24.89852  ? 72  TYR A CD2  1 
ATOM   1094 C  CE1  . TYR A 1 72  ? -32.81100 21.49400 52.98300 1.000 27.82444  ? 72  TYR A CE1  1 
ATOM   1095 C  CE2  . TYR A 1 72  ? -33.11000 23.73600 52.19900 1.000 24.40106  ? 72  TYR A CE2  1 
ATOM   1096 C  CZ   . TYR A 1 72  ? -33.43900 22.38800 52.14800 1.000 25.04781  ? 72  TYR A CZ   1 
ATOM   1097 O  OH   . TYR A 1 72  ? -34.40000 21.95000 51.25400 1.000 26.39730  ? 72  TYR A OH   1 
ATOM   1098 H  H    . TYR A 1 72  ? -28.31000 23.88700 56.26300 1.000 30.26558  ? 72  TYR A H    1 
ATOM   1099 H  HA   . TYR A 1 72  ? -29.18400 22.17800 54.39500 1.000 29.60558  ? 72  TYR A HA   1 
ATOM   1100 H  HB2  . TYR A 1 72  ? -30.66100 23.53600 55.79000 1.000 30.42558  ? 72  TYR A HB2  1 
ATOM   1101 H  HB3  . TYR A 1 72  ? -30.31900 24.72400 54.79300 1.000 30.42558  ? 72  TYR A HB3  1 
ATOM   1102 H  HD1  . TYR A 1 72  ? -31.43700 21.33900 54.45200 1.000 31.86558  ? 72  TYR A HD1  1 
ATOM   1103 H  HD2  . TYR A 1 72  ? -31.91600 25.07200 53.12300 1.000 30.09558  ? 72  TYR A HD2  1 
ATOM   1104 H  HE1  . TYR A 1 72  ? -33.02700 20.59100 52.94700 1.000 33.09558  ? 72  TYR A HE1  1 
ATOM   1105 H  HE2  . TYR A 1 72  ? -33.53700 24.34400 51.64000 1.000 29.54558  ? 72  TYR A HE2  1 
ATOM   1106 H  HH   . TYR A 1 72  ? -34.45700 21.11200 51.28100 1.000 31.65558  ? 72  TYR A HH   1 
ATOM   1107 N  N    . TYR A 1 73  ? -27.76300 24.91400 53.50200 1.000 25.98038  ? 73  TYR A N    1 
ATOM   1108 C  CA   . TYR A 1 73  ? -27.29200 25.67500 52.34800 1.000 25.18059  ? 73  TYR A CA   1 
ATOM   1109 C  C    . TYR A 1 73  ? -25.78400 25.65300 52.13000 1.000 22.23637  ? 73  TYR A C    1 
ATOM   1110 O  O    . TYR A 1 73  ? -25.33600 26.01700 51.03400 1.000 23.50557  ? 73  TYR A O    1 
ATOM   1111 C  CB   . TYR A 1 73  ? -27.71500 27.15400 52.45600 1.000 23.51938  ? 73  TYR A CB   1 
ATOM   1112 C  CG   . TYR A 1 73  ? -29.20100 27.36300 52.58500 1.000 24.24086  ? 73  TYR A CG   1 
ATOM   1113 C  CD1  . TYR A 1 73  ? -30.04100 27.25000 51.48700 1.000 25.69578  ? 73  TYR A CD1  1 
ATOM   1114 C  CD2  . TYR A 1 73  ? -29.75900 27.70200 53.79900 1.000 26.20755  ? 73  TYR A CD2  1 
ATOM   1115 C  CE1  . TYR A 1 73  ? -31.40300 27.44700 51.60600 1.000 25.05080  ? 73  TYR A CE1  1 
ATOM   1116 C  CE2  . TYR A 1 73  ? -31.11300 27.90000 53.92600 1.000 25.69335  ? 73  TYR A CE2  1 
ATOM   1117 C  CZ   . TYR A 1 73  ? -31.92800 27.77200 52.84800 1.000 25.81077  ? 73  TYR A CZ   1 
ATOM   1118 O  OH   . TYR A 1 73  ? -33.28200 27.97800 53.01000 1.000 26.25534  ? 73  TYR A OH   1 
ATOM   1119 H  H    . TYR A 1 73  ? -27.59500 25.28100 54.26100 1.000 31.22558  ? 73  TYR A H    1 
ATOM   1120 H  HA   . TYR A 1 73  ? -27.71100 25.28300 51.56600 1.000 30.47558  ? 73  TYR A HA   1 
ATOM   1121 H  HB2  . TYR A 1 73  ? -27.29500 27.54100 53.24100 1.000 28.47558  ? 73  TYR A HB2  1 
ATOM   1122 H  HB3  . TYR A 1 73  ? -27.42000 27.62100 51.65800 1.000 28.47558  ? 73  TYR A HB3  1 
ATOM   1123 H  HD1  . TYR A 1 73  ? -29.68100 27.03900 50.65600 1.000 31.32558  ? 73  TYR A HD1  1 
ATOM   1124 H  HD2  . TYR A 1 73  ? -29.21000 27.79900 54.54400 1.000 31.47558  ? 73  TYR A HD2  1 
ATOM   1125 H  HE1  . TYR A 1 73  ? -31.95900 27.36400 50.86500 1.000 30.50558  ? 73  TYR A HE1  1 
ATOM   1126 H  HE2  . TYR A 1 73  ? -31.47300 28.12100 54.75400 1.000 30.80558  ? 73  TYR A HE2  1 
ATOM   1127 H  HH   . TYR A 1 73  ? -33.45000 28.16600 53.81200 1.000 31.55558  ? 73  TYR A HH   1 
ATOM   1128 N  N    . HIS A 1 74  ? -24.99900 25.29100 53.14200 1.000 22.53056  ? 74  HIS A N    1 
ATOM   1129 C  CA   . HIS A 1 74  ? -23.54200 25.28100 53.05900 1.000 24.21584  ? 74  HIS A CA   1 
ATOM   1130 C  C    . HIS A 1 74  ? -22.98800 26.68400 52.81000 1.000 31.66183  ? 74  HIS A C    1 
ATOM   1131 O  O    . HIS A 1 74  ? -22.01900 26.86500 52.06900 1.000 27.90181  ? 74  HIS A O    1 
ATOM   1132 C  CB   . HIS A 1 74  ? -23.05100 24.31100 51.98000 1.000 27.36683  ? 74  HIS A CB   1 
ATOM   1133 C  CG   . HIS A 1 74  ? -23.27500 22.86000 52.30400 1.000 29.24955  ? 74  HIS A CG   1 
ATOM   1134 N  ND1  . HIS A 1 74  ? -22.79300 21.83800 51.50500 1.000 30.00167  ? 74  HIS A ND1  1 
ATOM   1135 C  CD2  . HIS A 1 74  ? -23.91500 22.26000 53.33500 1.000 31.35826  ? 74  HIS A CD2  1 
ATOM   1136 C  CE1  . HIS A 1 74  ? -23.13000 20.67100 52.03500 1.000 30.50107  ? 74  HIS A CE1  1 
ATOM   1137 N  NE2  . HIS A 1 74  ? -23.81400 20.89900 53.14300 1.000 30.94490  ? 74  HIS A NE2  1 
ATOM   1138 H  H    . HIS A 1 74  ? -25.29600 25.03900 53.90900 1.000 26.86558  ? 74  HIS A H    1 
ATOM   1139 H  HA   . HIS A 1 74  ? -23.19700 24.97800 53.91400 1.000 28.67558  ? 74  HIS A HA   1 
ATOM   1140 H  HB2  . HIS A 1 74  ? -23.52000 24.50400 51.15400 1.000 32.44558  ? 74  HIS A HB2  1 
ATOM   1141 H  HB3  . HIS A 1 74  ? -22.09700 24.44100 51.85800 1.000 32.44558  ? 74  HIS A HB3  1 
ATOM   1142 H  HD1  . HIS A 1 74  ? -22.34500 21.94400 50.77900 1.000 35.00558  ? 74  HIS A HD1  1 
ATOM   1143 H  HD2  . HIS A 1 74  ? -24.34400 22.68700 54.04200 1.000 36.71558  ? 74  HIS A HD2  1 
ATOM   1144 H  HE1  . HIS A 1 74  ? -22.92000 19.83400 51.68700 1.000 35.17558  ? 74  HIS A HE1  1 
ATOM   1145 N  N    . THR A 1 75  ? -23.62000 27.68900 53.41300 1.000 25.88474  ? 75  THR A N    1 
ATOM   1146 C  CA   . THR A 1 75  ? -23.10500 29.05200 53.37700 1.000 27.16375  ? 75  THR A CA   1 
ATOM   1147 C  C    . THR A 1 75  ? -23.36700 29.69700 54.72500 1.000 28.71535  ? 75  THR A C    1 
ATOM   1148 O  O    . THR A 1 75  ? -24.31100 29.33400 55.42900 1.000 30.13473  ? 75  THR A O    1 
ATOM   1149 C  CB   . THR A 1 75  ? -23.74000 29.90000 52.25800 1.000 30.67766  ? 75  THR A CB   1 
ATOM   1150 O  OG1  . THR A 1 75  ? -23.24800 31.24900 52.32700 1.000 31.24406  ? 75  THR A OG1  1 
ATOM   1151 C  CG2  . THR A 1 75  ? -25.22700 29.92700 52.40300 1.000 34.56592  ? 75  THR A CG2  1 
ATOM   1152 H  H    . THR A 1 75  ? -24.35500 27.60300 53.85100 1.000 30.62558  ? 75  THR A H    1 
ATOM   1153 H  HA   . THR A 1 75  ? -22.15000 29.03100 53.21200 1.000 31.90558  ? 75  THR A HA   1 
ATOM   1154 H  HB   . THR A 1 75  ? -23.51200 29.51300 51.39900 1.000 36.28558  ? 75  THR A HB   1 
ATOM   1155 H  HG1  . THR A 1 75  ? -23.60400 31.71600 51.72600 1.000 36.51558  ? 75  THR A HG1  1 
ATOM   1156 H  HG21 . THR A 1 75  ? -25.62700 30.38200 51.64600 1.000 41.09558  ? 75  THR A HG21 1 
ATOM   1157 H  HG22 . THR A 1 75  ? -25.57300 29.02100 52.44400 1.000 41.09558  ? 75  THR A HG22 1 
ATOM   1158 H  HG23 . THR A 1 75  ? -25.47300 30.39400 53.21700 1.000 41.09558  ? 75  THR A HG23 1 
ATOM   1159 N  N    . THR A 1 76  ? -22.49900 30.63700 55.09600 1.000 26.26790  ? 76  THR A N    1 
ATOM   1160 C  CA   . THR A 1 76  ? -22.73100 31.49000 56.25900 1.000 30.81122  ? 76  THR A CA   1 
ATOM   1161 C  C    . THR A 1 76  ? -22.72100 32.96400 55.86000 1.000 27.99313  ? 76  THR A C    1 
ATOM   1162 O  O    . THR A 1 76  ? -22.46400 33.83700 56.70200 1.000 34.53908  ? 76  THR A O    1 
ATOM   1163 C  CB   . THR A 1 76  ? -21.70300 31.24800 57.36900 1.000 30.56402  ? 76  THR A CB   1 
ATOM   1164 O  OG1  . THR A 1 76  ? -20.37000 31.37100 56.85200 1.000 29.92241  ? 76  THR A OG1  1 
ATOM   1165 C  CG2  . THR A 1 76  ? -21.88300 29.86600 57.98000 1.000 35.40558  ? 76  THR A CG2  1 
ATOM   1166 H  H    . THR A 1 76  ? -21.76100 30.80000 54.68500 1.000 29.94558  ? 76  THR A H    1 
ATOM   1167 H  HA   . THR A 1 76  ? -23.59800 31.26100 56.62900 1.000 34.83558  ? 76  THR A HA   1 
ATOM   1168 H  HB   . THR A 1 76  ? -21.83300 31.91100 58.06500 1.000 34.10558  ? 76  THR A HB   1 
ATOM   1169 H  HG1  . THR A 1 76  ? -19.81800 31.39600 57.48500 1.000 33.17558  ? 76  THR A HG1  1 
ATOM   1170 H  HG21 . THR A 1 76  ? -21.23900 29.73200 58.69300 1.000 40.17558  ? 76  THR A HG21 1 
ATOM   1171 H  HG22 . THR A 1 76  ? -22.77800 29.77700 58.34300 1.000 40.17558  ? 76  THR A HG22 1 
ATOM   1172 H  HG23 . THR A 1 76  ? -21.74900 29.18400 57.30200 1.000 40.17558  ? 76  THR A HG23 1 
ATOM   1173 N  N    . ASP A 1 77  ? -22.98200 33.24900 54.59200 1.000 28.85612  ? 77  ASP A N    1 
ATOM   1174 C  CA   . ASP A 1 77  ? -23.07200 34.63900 54.15600 1.000 29.54435  ? 77  ASP A CA   1 
ATOM   1175 C  C    . ASP A 1 77  ? -24.30000 35.26400 54.79700 1.000 31.91748  ? 77  ASP A C    1 
ATOM   1176 O  O    . ASP A 1 77  ? -25.41000 34.73400 54.62800 1.000 28.97686  ? 77  ASP A O    1 
ATOM   1177 C  CB   . ASP A 1 77  ? -23.15800 34.73500 52.64700 1.000 30.61388  ? 77  ASP A CB   1 
ATOM   1178 C  CG   . ASP A 1 77  ? -23.29400 36.18800 52.18100 1.000 37.77328  ? 77  ASP A CG   1 
ATOM   1179 O  OD1  . ASP A 1 77  ? -22.79500 37.07800 52.89800 1.000 48.37876  ? 77  ASP A OD1  1 
ATOM   1180 O  OD2  . ASP A 1 77  ? -23.87400 36.42900 51.12000 1.000 47.29519  ? 77  ASP A OD2  1 
ATOM   1181 H  H    . ASP A 1 77  ? -23.10900 32.66700 53.97200 1.000 32.26558  ? 77  ASP A H    1 
ATOM   1182 H  HA   . ASP A 1 77  ? -22.27500 35.12100 54.42800 1.000 32.50558  ? 77  ASP A HA   1 
ATOM   1183 H  HB2  . ASP A 1 77  ? -22.35100 34.36300 52.25600 1.000 34.14558  ? 77  ASP A HB2  1 
ATOM   1184 H  HB3  . ASP A 1 77  ? -23.93400 34.24200 52.33900 1.000 34.14558  ? 77  ASP A HB3  1 
ATOM   1185 N  N    . PRO A 1 78  ? -24.15800 36.35000 55.56100 1.000 35.81603  ? 78  PRO A N    1 
ATOM   1186 C  CA   . PRO A 1 78  ? -25.30000 36.85200 56.33400 1.000 38.27315  ? 78  PRO A CA   1 
ATOM   1187 C  C    . PRO A 1 78  ? -26.51200 37.21800 55.49400 1.000 35.62942  ? 78  PRO A C    1 
ATOM   1188 O  O    . PRO A 1 78  ? -27.64400 37.09300 55.97700 1.000 40.28895  ? 78  PRO A O    1 
ATOM   1189 C  CB   . PRO A 1 78  ? -24.72400 38.09400 57.03800 1.000 46.35468  ? 78  PRO A CB   1 
ATOM   1190 C  CG   . PRO A 1 78  ? -23.27400 37.83500 57.12700 1.000 46.71730  ? 78  PRO A CG   1 
ATOM   1191 C  CD   . PRO A 1 78  ? -22.92200 37.10200 55.86300 1.000 42.34441  ? 78  PRO A CD   1 
ATOM   1192 H  HA   . PRO A 1 78  ? -25.55800 36.18400 56.99000 1.000 41.10558  ? 78  PRO A HA   1 
ATOM   1193 H  HB2  . PRO A 1 78  ? -24.90500 38.88700 56.51100 1.000 49.54558  ? 78  PRO A HB2  1 
ATOM   1194 H  HB3  . PRO A 1 78  ? -25.11600 38.18600 57.92100 1.000 49.54558  ? 78  PRO A HB3  1 
ATOM   1195 H  HG2  . PRO A 1 78  ? -22.79200 38.67500 57.18500 1.000 50.02558  ? 78  PRO A HG2  1 
ATOM   1196 H  HG3  . PRO A 1 78  ? -23.08400 37.29000 57.90700 1.000 50.02558  ? 78  PRO A HG3  1 
ATOM   1197 H  HD2  . PRO A 1 78  ? -22.71200 37.72400 55.14900 1.000 45.73558  ? 78  PRO A HD2  1 
ATOM   1198 H  HD3  . PRO A 1 78  ? -22.17600 36.49900 56.00900 1.000 45.73558  ? 78  PRO A HD3  1 
ATOM   1199 N  N    . SER A 1 79  ? -26.31700 37.65800 54.26200 1.000 37.05957  ? 79  SER A N    1 
ATOM   1200 C  CA   . SER A 1 79  ? -27.43400 38.11500 53.44800 1.000 35.76991  ? 79  SER A CA   1 
ATOM   1201 C  C    . SER A 1 79  ? -28.03800 37.02200 52.57700 1.000 42.22017  ? 79  SER A C    1 
ATOM   1202 O  O    . SER A 1 79  ? -28.98900 37.30700 51.84700 1.000 36.82804  ? 79  SER A O    1 
ATOM   1203 C  CB   . SER A 1 79  ? -26.99200 39.26700 52.56200 1.000 41.14918  ? 79  SER A CB   1 
ATOM   1204 O  OG   . SER A 1 79  ? -25.98300 38.83900 51.68200 1.000 41.53351  ? 79  SER A OG   1 
ATOM   1205 H  H    . SER A 1 79  ? -25.55000 37.70300 53.87600 1.000 39.72558  ? 79  SER A H    1 
ATOM   1206 H  HA   . SER A 1 79  ? -28.12900 38.43300 54.04500 1.000 38.05558  ? 79  SER A HA   1 
ATOM   1207 H  HB2  . SER A 1 79  ? -27.75100 39.58200 52.04700 1.000 43.78558  ? 79  SER A HB2  1 
ATOM   1208 H  HB3  . SER A 1 79  ? -26.64800 39.98300 53.11800 1.000 43.78558  ? 79  SER A HB3  1 
ATOM   1209 H  HG   . SER A 1 79  ? -25.73700 39.47700 51.19500 1.000 44.83558  ? 79  SER A HG   1 
ATOM   1210 N  N    . PHE A 1 80  ? -27.52800 35.78800 52.65500 1.000 29.81058  ? 80  PHE A N    1 
ATOM   1211 C  CA   . PHE A 1 80  ? -27.94700 34.74600 51.72100 1.000 27.72648  ? 80  PHE A CA   1 
ATOM   1212 C  C    . PHE A 1 80  ? -29.45500 34.54400 51.73800 1.000 28.18501  ? 80  PHE A C    1 
ATOM   1213 O  O    . PHE A 1 80  ? -30.08800 34.50400 50.68300 1.000 29.39390  ? 80  PHE A O    1 
ATOM   1214 C  CB   . PHE A 1 80  ? -27.25500 33.42300 52.02600 1.000 29.68214  ? 80  PHE A CB   1 
ATOM   1215 C  CG   . PHE A 1 80  ? -27.62300 32.32000 51.06400 1.000 26.26214  ? 80  PHE A CG   1 
ATOM   1216 C  CD1  . PHE A 1 80  ? -26.91800 32.14600 49.88700 1.000 29.07885  ? 80  PHE A CD1  1 
ATOM   1217 C  CD2  . PHE A 1 80  ? -28.68500 31.47100 51.32500 1.000 25.72593  ? 80  PHE A CD2  1 
ATOM   1218 C  CE1  . PHE A 1 80  ? -27.24900 31.13400 49.01600 1.000 25.84653  ? 80  PHE A CE1  1 
ATOM   1219 C  CE2  . PHE A 1 80  ? -29.02400 30.47400 50.44400 1.000 27.04707  ? 80  PHE A CE2  1 
ATOM   1220 C  CZ   . PHE A 1 80  ? -28.30100 30.31100 49.28200 1.000 26.10894  ? 80  PHE A CZ   1 
ATOM   1221 H  H    . PHE A 1 80  ? -26.94500 35.53300 53.23400 1.000 32.83558  ? 80  PHE A H    1 
ATOM   1222 H  HA   . PHE A 1 80  ? -27.67900 35.03400 50.83400 1.000 31.21558  ? 80  PHE A HA   1 
ATOM   1223 H  HB2  . PHE A 1 80  ? -26.29500 33.55200 51.97700 1.000 34.17558  ? 80  PHE A HB2  1 
ATOM   1224 H  HB3  . PHE A 1 80  ? -27.50600 33.13600 52.91800 1.000 34.17558  ? 80  PHE A HB3  1 
ATOM   1225 H  HD1  . PHE A 1 80  ? -26.21400 32.71900 49.68200 1.000 34.43558  ? 80  PHE A HD1  1 
ATOM   1226 H  HD2  . PHE A 1 80  ? -29.17500 31.57700 52.10900 1.000 30.44558  ? 80  PHE A HD2  1 
ATOM   1227 H  HE1  . PHE A 1 80  ? -26.75100 31.01000 48.24000 1.000 31.06558  ? 80  PHE A HE1  1 
ATOM   1228 H  HE2  . PHE A 1 80  ? -29.74000 29.91000 50.63100 1.000 32.51558  ? 80  PHE A HE2  1 
ATOM   1229 H  HZ   . PHE A 1 80  ? -28.53200 29.64000 48.68100 1.000 31.61558  ? 80  PHE A HZ   1 
ATOM   1230 N  N    . LEU A 1 81  ? -30.05000 34.37300 52.92900 1.000 25.68473  ? 81  LEU A N    1 
ATOM   1231 C  CA   . LEU A 1 81  ? -31.48000 34.07300 52.97600 1.000 27.64371  ? 81  LEU A CA   1 
ATOM   1232 C  C    . LEU A 1 81  ? -32.31100 35.22200 52.40500 1.000 31.26556  ? 81  LEU A C    1 
ATOM   1233 O  O    . LEU A 1 81  ? -33.30300 34.98900 51.70500 1.000 30.53872  ? 81  LEU A O    1 
ATOM   1234 C  CB   . LEU A 1 81  ? -31.91700 33.76200 54.41300 1.000 30.59394  ? 81  LEU A CB   1 
ATOM   1235 C  CG   . LEU A 1 81  ? -31.84100 32.31600 54.92000 1.000 51.20302  ? 81  LEU A CG   1 
ATOM   1236 C  CD1  . LEU A 1 81  ? -32.49300 31.35700 53.94700 1.000 50.92675  ? 81  LEU A CD1  1 
ATOM   1237 C  CD2  . LEU A 1 81  ? -30.40800 31.87900 55.17000 1.000 63.01959  ? 81  LEU A CD2  1 
ATOM   1238 H  H    . LEU A 1 81  ? -29.66000 34.42400 53.69300 1.000 28.66558  ? 81  LEU A H    1 
ATOM   1239 H  HA   . LEU A 1 81  ? -31.64300 33.28400 52.43700 1.000 31.10558  ? 81  LEU A HA   1 
ATOM   1240 H  HB2  . LEU A 1 81  ? -31.36000 34.29000 55.00600 1.000 34.44558  ? 81  LEU A HB2  1 
ATOM   1241 H  HB3  . LEU A 1 81  ? -32.84400 34.03400 54.49900 1.000 34.44558  ? 81  LEU A HB3  1 
ATOM   1242 H  HG   . LEU A 1 81  ? -32.32100 32.28300 55.76300 1.000 59.79558  ? 81  LEU A HG   1 
ATOM   1243 H  HD11 . LEU A 1 81  ? -32.66400 30.51600 54.39900 1.000 60.06558  ? 81  LEU A HD11 1 
ATOM   1244 H  HD12 . LEU A 1 81  ? -33.32700 31.74100 53.63600 1.000 60.06558  ? 81  LEU A HD12 1 
ATOM   1245 H  HD13 . LEU A 1 81  ? -31.89500 31.21300 53.19700 1.000 60.06558  ? 81  LEU A HD13 1 
ATOM   1246 H  HD21 . LEU A 1 81  ? -30.40400 30.94600 55.43300 1.000 74.16558  ? 81  LEU A HD21 1 
ATOM   1247 H  HD22 . LEU A 1 81  ? -29.89600 31.99500 54.35400 1.000 74.16558  ? 81  LEU A HD22 1 
ATOM   1248 H  HD23 . LEU A 1 81  ? -30.03100 32.42500 55.87800 1.000 74.16558  ? 81  LEU A HD23 1 
ATOM   1249 N  N    . GLY A 1 82  ? -31.92200 36.46900 52.67800 1.000 33.79329  ? 82  GLY A N    1 
ATOM   1250 C  CA   . GLY A 1 82  ? -32.62300 37.59500 52.07300 1.000 36.49990  ? 82  GLY A CA   1 
ATOM   1251 C  C    . GLY A 1 82  ? -32.53800 37.59900 50.55500 1.000 36.61588  ? 82  GLY A C    1 
ATOM   1252 O  O    . GLY A 1 82  ? -33.50600 37.93400 49.86400 1.000 32.15139  ? 82  GLY A O    1 
ATOM   1253 H  H    . GLY A 1 82  ? -31.27100 36.68300 53.19800 1.000 36.96558  ? 82  GLY A H    1 
ATOM   1254 H  HA2  . GLY A 1 82  ? -33.55900 37.56000 52.32500 1.000 39.41558  ? 82  GLY A HA2  1 
ATOM   1255 H  HA3  . GLY A 1 82  ? -32.23900 38.42300 52.40100 1.000 39.41558  ? 82  GLY A HA3  1 
ATOM   1256 N  N    . ARG A 1 83  ? -31.37800 37.23400 50.01400 1.000 30.07553  ? 83  ARG A N    1 
ATOM   1257 C  CA   . ARG A 1 83  ? -31.22300 37.21500 48.56600 1.000 30.12083  ? 83  ARG A CA   1 
ATOM   1258 C  C    . ARG A 1 83  ? -32.01200 36.07400 47.94100 1.000 31.91456  ? 83  ARG A C    1 
ATOM   1259 O  O    . ARG A 1 83  ? -32.63000 36.25100 46.88200 1.000 28.29173  ? 83  ARG A O    1 
ATOM   1260 C  CB   . ARG A 1 83  ? -29.72900 37.14800 48.20900 1.000 34.77218  ? 83  ARG A CB   1 
ATOM   1261 C  CG   . ARG A 1 83  ? -29.03100 38.44200 48.67200 1.000 39.38123  ? 83  ARG A CG   1 
ATOM   1262 C  CD   . ARG A 1 83  ? -27.54600 38.61300 48.30600 1.000 46.12882  ? 83  ARG A CD   1 
ATOM   1263 N  NE   . ARG A 1 83  ? -26.65300 37.67700 48.98000 1.000 50.59712  ? 83  ARG A NE   1 
ATOM   1264 C  CZ   . ARG A 1 83  ? -26.29900 36.51100 48.46500 1.000 39.67372  ? 83  ARG A CZ   1 
ATOM   1265 N  NH1  . ARG A 1 83  ? -26.77600 36.10600 47.30400 1.000 32.18894  ? 83  ARG A NH1  1 
ATOM   1266 N  NH2  . ARG A 1 83  ? -25.43600 35.74100 49.12200 1.000 37.32838  ? 83  ARG A NH2  1 
ATOM   1267 H  H    . ARG A 1 83  ? -30.67800 36.99900 50.45500 1.000 32.59558  ? 83  ARG A H    1 
ATOM   1268 H  HA   . ARG A 1 83  ? -31.57500 38.03700 48.19000 1.000 32.96558  ? 83  ARG A HA   1 
ATOM   1269 H  HB2  . ARG A 1 83  ? -29.31800 36.39200 48.65600 1.000 38.77558  ? 83  ARG A HB2  1 
ATOM   1270 H  HB3  . ARG A 1 83  ? -29.62600 37.06200 47.24800 1.000 38.77558  ? 83  ARG A HB3  1 
ATOM   1271 H  HG2  . ARG A 1 83  ? -29.50300 39.19400 48.28000 1.000 43.25558  ? 83  ARG A HG2  1 
ATOM   1272 H  HG3  . ARG A 1 83  ? -29.08700 38.48200 49.63900 1.000 43.25558  ? 83  ARG A HG3  1 
ATOM   1273 H  HD2  . ARG A 1 83  ? -27.44400 38.47900 47.35100 1.000 51.33558  ? 83  ARG A HD2  1 
ATOM   1274 H  HD3  . ARG A 1 83  ? -27.26700 39.51000 48.54700 1.000 51.33558  ? 83  ARG A HD3  1 
ATOM   1275 H  HE   . ARG A 1 83  ? -26.34200 37.89400 49.75200 1.000 57.29558  ? 83  ARG A HE   1 
ATOM   1276 H  HH11 . ARG A 1 83  ? -27.32700 36.60200 46.86900 1.000 36.60558  ? 83  ARG A HH11 1 
ATOM   1277 H  HH12 . ARG A 1 83  ? -26.53600 35.34500 46.98200 1.000 36.60558  ? 83  ARG A HH12 1 
ATOM   1278 H  HH21 . ARG A 1 83  ? -25.11300 36.00200 49.87500 1.000 42.61558  ? 83  ARG A HH21 1 
ATOM   1279 H  HH22 . ARG A 1 83  ? -25.20100 34.98200 48.79300 1.000 42.61558  ? 83  ARG A HH22 1 
ATOM   1280 N  N    . TYR A 1 84  ? -32.02100 34.90800 48.59100 1.000 27.96812  ? 84  TYR A N    1 
ATOM   1281 C  CA   . TYR A 1 84  ? -32.82300 33.78400 48.11900 1.000 24.64662  ? 84  TYR A CA   1 
ATOM   1282 C  C    . TYR A 1 84  ? -34.30900 34.13400 48.11900 1.000 27.63646  ? 84  TYR A C    1 
ATOM   1283 O  O    . TYR A 1 84  ? -35.02000 33.91300 47.12600 1.000 25.89449  ? 84  TYR A O    1 
ATOM   1284 C  CB   . TYR A 1 84  ? -32.50800 32.57800 49.01200 1.000 24.86986  ? 84  TYR A CB   1 
ATOM   1285 C  CG   . TYR A 1 84  ? -33.40300 31.38700 48.85700 1.000 26.10137  ? 84  TYR A CG   1 
ATOM   1286 C  CD1  . TYR A 1 84  ? -33.82300 30.96400 47.60700 1.000 27.44624  ? 84  TYR A CD1  1 
ATOM   1287 C  CD2  . TYR A 1 84  ? -33.80800 30.65300 49.96900 1.000 29.05456  ? 84  TYR A CD2  1 
ATOM   1288 C  CE1  . TYR A 1 84  ? -34.64000 29.85000 47.46800 1.000 26.60068  ? 84  TYR A CE1  1 
ATOM   1289 C  CE2  . TYR A 1 84  ? -34.61700 29.54300 49.83400 1.000 31.50668  ? 84  TYR A CE2  1 
ATOM   1290 C  CZ   . TYR A 1 84  ? -35.03900 29.15600 48.58800 1.000 36.71356  ? 84  TYR A CZ   1 
ATOM   1291 O  OH   . TYR A 1 84  ? -35.84400 28.05600 48.45500 1.000 36.69116  ? 84  TYR A OH   1 
ATOM   1292 H  H    . TYR A 1 84  ? -31.57200 34.74400 49.30600 1.000 31.84558  ? 84  TYR A H    1 
ATOM   1293 H  HA   . TYR A 1 84  ? -32.59700 33.55600 47.20300 1.000 28.48558  ? 84  TYR A HA   1 
ATOM   1294 H  HB2  . TYR A 1 84  ? -31.60500 32.28400 48.81500 1.000 29.22558  ? 84  TYR A HB2  1 
ATOM   1295 H  HB3  . TYR A 1 84  ? -32.57000 32.86300 49.93700 1.000 29.22558  ? 84  TYR A HB3  1 
ATOM   1296 H  HD1  . TYR A 1 84  ? -33.55300 31.43200 46.85000 1.000 33.00558  ? 84  TYR A HD1  1 
ATOM   1297 H  HD2  . TYR A 1 84  ? -33.52900 30.91500 50.81600 1.000 34.71558  ? 84  TYR A HD2  1 
ATOM   1298 H  HE1  . TYR A 1 84  ? -34.91600 29.57400 46.62300 1.000 32.23558  ? 84  TYR A HE1  1 
ATOM   1299 H  HE2  . TYR A 1 84  ? -34.87500 29.05900 50.58500 1.000 37.91558  ? 84  TYR A HE2  1 
ATOM   1300 H  HH   . TYR A 1 84  ? -36.00000 27.91000 47.64200 1.000 44.44558  ? 84  TYR A HH   1 
ATOM   1301 N  N    . MET A 1 85  ? -34.79200 34.69700 49.22200 1.000 26.06552  ? 85  MET A N    1 
ATOM   1302 C  CA   . MET A 1 85  ? -36.19800 35.08200 49.32100 1.000 27.88031  ? 85  MET A CA   1 
ATOM   1303 C  C    . MET A 1 85  ? -36.56000 36.13800 48.27100 1.000 29.65244  ? 85  MET A C    1 
ATOM   1304 O  O    . MET A 1 85  ? -37.60200 36.05300 47.60400 1.000 28.41092  ? 85  MET A O    1 
ATOM   1305 C  CB   . MET A 1 85  ? -36.42200 35.60200 50.73700 1.000 32.25589  ? 85  MET A CB   1 
ATOM   1306 C  CG   . MET A 1 85  ? -36.88200 34.57500 51.77300 1.000 31.73004  ? 85  MET A CG   1 
ATOM   1307 S  SD   . MET A 1 85  ? -38.06800 33.29000 51.40300 1.000 34.14853  ? 85  MET A SD   1 
ATOM   1308 C  CE   . MET A 1 85  ? -37.12300 31.91100 50.82400 1.000 32.27312  ? 85  MET A CE   1 
ATOM   1309 H  H    . MET A 1 85  ? -34.33000 34.86800 49.92700 1.000 29.23558  ? 85  MET A H    1 
ATOM   1310 H  HA   . MET A 1 85  ? -36.77400 34.31700 49.16500 1.000 30.91558  ? 85  MET A HA   1 
ATOM   1311 H  HB2  . MET A 1 85  ? -35.58500 35.97400 51.05700 1.000 35.51558  ? 85  MET A HB2  1 
ATOM   1312 H  HB3  . MET A 1 85  ? -37.10100 36.29400 50.70100 1.000 35.51558  ? 85  MET A HB3  1 
ATOM   1313 H  HG2  . MET A 1 85  ? -36.08500 34.10900 52.07300 1.000 35.25558  ? 85  MET A HG2  1 
ATOM   1314 H  HG3  . MET A 1 85  ? -37.26800 35.07700 52.50700 1.000 35.25558  ? 85  MET A HG3  1 
ATOM   1315 H  HE1  . MET A 1 85  ? -37.72800 31.19300 50.58000 1.000 37.47558  ? 85  MET A HE1  1 
ATOM   1316 H  HE2  . MET A 1 85  ? -36.60500 32.18500 50.05100 1.000 37.47558  ? 85  MET A HE2  1 
ATOM   1317 H  HE3  . MET A 1 85  ? -36.52800 31.61600 51.53200 1.000 37.47558  ? 85  MET A HE3  1 
ATOM   1318 N  N    . SER A 1 86  ? -35.72000 37.16600 48.12800 1.000 30.06216  ? 86  SER A N    1 
ATOM   1319 C  CA   . SER A 1 86  ? -35.98700 38.19800 47.13300 1.000 34.77439  ? 86  SER A CA   1 
ATOM   1320 C  C    . SER A 1 86  ? -36.08700 37.60000 45.73800 1.000 30.46148  ? 86  SER A C    1 
ATOM   1321 O  O    . SER A 1 86  ? -36.97600 37.96000 44.96500 1.000 31.83108  ? 86  SER A O    1 
ATOM   1322 C  CB   . SER A 1 86  ? -34.89800 39.27400 47.16000 1.000 39.73805  ? 86  SER A CB   1 
ATOM   1323 O  OG   . SER A 1 86  ? -34.98700 40.04700 48.34400 1.000 56.43880  ? 86  SER A OG   1 
ATOM   1324 H  H    . SER A 1 86  ? -35.00300 37.28500 48.58700 1.000 32.35558  ? 86  SER A H    1 
ATOM   1325 H  HA   . SER A 1 86  ? -36.83200 38.62100 47.35500 1.000 37.29558  ? 86  SER A HA   1 
ATOM   1326 H  HB2  . SER A 1 86  ? -34.02900 38.84400 47.12700 1.000 42.54558  ? 86  SER A HB2  1 
ATOM   1327 H  HB3  . SER A 1 86  ? -35.01000 39.85600 46.39300 1.000 42.54558  ? 86  SER A HB3  1 
ATOM   1328 H  HG   . SER A 1 86  ? -34.39600 40.64400 48.34200 1.000 61.62558  ? 86  SER A HG   1 
ATOM   1329 N  N    . ALA A 1 87  ? -35.19100 36.67000 45.40600 1.000 29.48113  ? 87  ALA A N    1 
ATOM   1330 C  CA   . ALA A 1 87  ? -35.25000 36.04500 44.08900 1.000 26.88788  ? 87  ALA A CA   1 
ATOM   1331 C  C    . ALA A 1 87  ? -36.49800 35.17300 43.95900 1.000 28.24066  ? 87  ALA A C    1 
ATOM   1332 O  O    . ALA A 1 87  ? -37.16200 35.17200 42.91700 1.000 27.89352  ? 87  ALA A O    1 
ATOM   1333 C  CB   . ALA A 1 87  ? -33.98400 35.21800 43.85300 1.000 25.00947  ? 87  ALA A CB   1 
ATOM   1334 H  H    . ALA A 1 87  ? -34.55500 36.39200 45.91300 1.000 32.53558  ? 87  ALA A H    1 
ATOM   1335 H  HA   . ALA A 1 87  ? -35.29000 36.73300 43.40600 1.000 29.97558  ? 87  ALA A HA   1 
ATOM   1336 H  HB1  . ALA A 1 87  ? -34.03800 34.80000 42.97900 1.000 28.47558  ? 87  ALA A HB1  1 
ATOM   1337 H  HB2  . ALA A 1 87  ? -33.21200 35.80500 43.89200 1.000 28.47558  ? 87  ALA A HB2  1 
ATOM   1338 H  HB3  . ALA A 1 87  ? -33.91800 34.53800 44.54100 1.000 28.47558  ? 87  ALA A HB3  1 
ATOM   1339 N  N    . LEU A 1 88  ? -36.83200 34.42700 45.01500 1.000 25.61932  ? 88  LEU A N    1 
ATOM   1340 C  CA   . LEU A 1 88  ? -37.96700 33.51400 44.95000 1.000 27.56698  ? 88  LEU A CA   1 
ATOM   1341 C  C    . LEU A 1 88  ? -39.26400 34.25700 44.69800 1.000 27.79449  ? 88  LEU A C    1 
ATOM   1342 O  O    . LEU A 1 88  ? -40.15900 33.74200 44.01600 1.000 29.76809  ? 88  LEU A O    1 
ATOM   1343 C  CB   . LEU A 1 88  ? -38.07400 32.71800 46.25200 1.000 25.71067  ? 88  LEU A CB   1 
ATOM   1344 C  CG   . LEU A 1 88  ? -39.20100 31.68900 46.34300 1.000 26.92520  ? 88  LEU A CG   1 
ATOM   1345 C  CD1  . LEU A 1 88  ? -39.05100 30.63400 45.28800 1.000 27.91968  ? 88  LEU A CD1  1 
ATOM   1346 C  CD2  . LEU A 1 88  ? -39.20800 31.05500 47.73800 1.000 29.75230  ? 88  LEU A CD2  1 
ATOM   1347 H  H    . LEU A 1 88  ? -36.42200 34.43200 45.77100 1.000 29.03558  ? 88  LEU A H    1 
ATOM   1348 H  HA   . LEU A 1 88  ? -37.82300 32.89100 44.22100 1.000 31.62558  ? 88  LEU A HA   1 
ATOM   1349 H  HB2  . LEU A 1 88  ? -37.24000 32.23800 46.37700 1.000 29.63558  ? 88  LEU A HB2  1 
ATOM   1350 H  HB3  . LEU A 1 88  ? -38.20600 33.34800 46.97700 1.000 29.63558  ? 88  LEU A HB3  1 
ATOM   1351 H  HG   . LEU A 1 88  ? -40.05100 32.13100 46.19600 1.000 31.27558  ? 88  LEU A HG   1 
ATOM   1352 H  HD11 . LEU A 1 88  ? -39.74100 29.96400 45.41200 1.000 32.96558  ? 88  LEU A HD11 1 
ATOM   1353 H  HD12 . LEU A 1 88  ? -39.14200 31.04600 44.41500 1.000 32.96558  ? 88  LEU A HD12 1 
ATOM   1354 H  HD13 . LEU A 1 88  ? -38.17500 30.22600 45.37200 1.000 32.96558  ? 88  LEU A HD13 1 
ATOM   1355 H  HD21 . LEU A 1 88  ? -39.92200 30.40000 47.78300 1.000 34.77558  ? 88  LEU A HD21 1 
ATOM   1356 H  HD22 . LEU A 1 88  ? -38.35300 30.62400 47.89300 1.000 34.77558  ? 88  LEU A HD22 1 
ATOM   1357 H  HD23 . LEU A 1 88  ? -39.35500 31.74900 48.39900 1.000 34.77558  ? 88  LEU A HD23 1 
ATOM   1358 N  N    . ASN A 1 89  ? -39.39100 35.46700 45.24000 1.000 27.99044  ? 89  ASN A N    1 
ATOM   1359 C  CA   . ASN A 1 89  ? -40.61700 36.22200 45.00800 1.000 31.48276  ? 89  ASN A CA   1 
ATOM   1360 C  C    . ASN A 1 89  ? -40.85000 36.44600 43.52400 1.000 33.22040  ? 89  ASN A C    1 
ATOM   1361 O  O    . ASN A 1 89  ? -42.00100 36.59900 43.09900 1.000 35.65490  ? 89  ASN A O    1 
ATOM   1362 C  CB   . ASN A 1 89  ? -40.57200 37.55800 45.74000 1.000 34.43047  ? 89  ASN A CB   1 
ATOM   1363 C  CG   . ASN A 1 89  ? -41.95200 38.05000 46.11200 1.000 40.41805  ? 89  ASN A CG   1 
ATOM   1364 O  OD1  . ASN A 1 89  ? -42.79500 37.27700 46.56500 1.000 38.87698  ? 89  ASN A OD1  1 
ATOM   1365 N  ND2  . ASN A 1 89  ? -42.20300 39.33200 45.89100 1.000 45.66411  ? 89  ASN A ND2  1 
ATOM   1366 H  H    . ASN A 1 89  ? -38.80300 35.85900 45.72900 1.000 30.59558  ? 89  ASN A H    1 
ATOM   1367 H  HA   . ASN A 1 89  ? -41.36400 35.71700 45.36700 1.000 33.92558  ? 89  ASN A HA   1 
ATOM   1368 H  HB2  . ASN A 1 89  ? -40.05600 37.45800 46.55500 1.000 36.38558  ? 89  ASN A HB2  1 
ATOM   1369 H  HB3  . ASN A 1 89  ? -40.15900 38.22200 45.16500 1.000 36.38558  ? 89  ASN A HB3  1 
ATOM   1370 H  HD21 . ASN A 1 89  ? -42.97400 39.65900 46.08700 1.000 47.73558  ? 89  ASN A HD21 1 
ATOM   1371 H  HD22 . ASN A 1 89  ? -41.59400 39.83700 45.55300 1.000 47.73558  ? 89  ASN A HD22 1 
ATOM   1372 N  N    . HIS A 1 90  ? -39.77800 36.47100 42.72700 1.000 29.41106  ? 90  HIS A N    1 
ATOM   1373 C  CA   . HIS A 1 90  ? -39.88900 36.58300 41.27900 1.000 30.24135  ? 90  HIS A CA   1 
ATOM   1374 C  C    . HIS A 1 90  ? -39.97800 35.22200 40.60300 1.000 27.46219  ? 90  HIS A C    1 
ATOM   1375 O  O    . HIS A 1 90  ? -40.82300 35.01400 39.72800 1.000 30.37643  ? 90  HIS A O    1 
ATOM   1376 C  CB   . HIS A 1 90  ? -38.68600 37.33300 40.69300 1.000 31.81047  ? 90  HIS A CB   1 
ATOM   1377 C  CG   . HIS A 1 90  ? -38.58400 38.74800 41.14500 1.000 35.06447  ? 90  HIS A CG   1 
ATOM   1378 N  ND1  . HIS A 1 90  ? -39.20600 39.78600 40.48400 1.000 39.54016  ? 90  HIS A ND1  1 
ATOM   1379 C  CD2  . HIS A 1 90  ? -37.92300 39.30400 42.18800 1.000 41.34305  ? 90  HIS A CD2  1 
ATOM   1380 C  CE1  . HIS A 1 90  ? -38.94200 40.92000 41.10900 1.000 56.88665  ? 90  HIS A CE1  1 
ATOM   1381 N  NE2  . HIS A 1 90  ? -38.16700 40.65600 42.14700 1.000 44.90475  ? 90  HIS A NE2  1 
ATOM   1382 H  H    . HIS A 1 90  ? -38.96600 36.42500 43.00800 1.000 31.71558  ? 90  HIS A H    1 
ATOM   1383 H  HA   . HIS A 1 90  ? -40.69500 37.08900 41.09200 1.000 32.67558  ? 90  HIS A HA   1 
ATOM   1384 H  HB2  . HIS A 1 90  ? -37.87300 36.87700 40.96000 1.000 34.40558  ? 90  HIS A HB2  1 
ATOM   1385 H  HB3  . HIS A 1 90  ? -38.76200 37.33600 39.72500 1.000 34.40558  ? 90  HIS A HB3  1 
ATOM   1386 H  HD2  . HIS A 1 90  ? -37.40100 38.85500 42.81300 1.000 44.36558  ? 90  HIS A HD2  1 
ATOM   1387 H  HE1  . HIS A 1 90  ? -39.25000 41.76200 40.86000 1.000 61.28558  ? 90  HIS A HE1  1 
ATOM   1388 H  HE2  . HIS A 1 90  ? -37.86500 41.23600 42.70600 1.000 47.31558  ? 90  HIS A HE2  1 
ATOM   1389 N  N    . THR A 1 91  ? -39.08800 34.29700 40.96000 1.000 27.74181  ? 91  THR A N    1 
ATOM   1390 C  CA   . THR A 1 91  ? -39.04500 33.05000 40.21700 1.000 28.30841  ? 91  THR A CA   1 
ATOM   1391 C  C    . THR A 1 91  ? -40.29100 32.21100 40.44700 1.000 27.62117  ? 91  THR A C    1 
ATOM   1392 O  O    . THR A 1 91  ? -40.61000 31.36600 39.60600 1.000 27.03259  ? 91  THR A O    1 
ATOM   1393 C  CB   . THR A 1 91  ? -37.81200 32.21500 40.57200 1.000 24.37431  ? 91  THR A CB   1 
ATOM   1394 O  OG1  . THR A 1 91  ? -37.90900 31.76600 41.93800 1.000 27.23150  ? 91  THR A OG1  1 
ATOM   1395 C  CG2  . THR A 1 91  ? -36.52600 33.01000 40.37500 1.000 23.87684  ? 91  THR A CG2  1 
ATOM   1396 H  H    . THR A 1 91  ? -38.52200 34.36800 41.60300 1.000 31.33558  ? 91  THR A H    1 
ATOM   1397 H  HA   . THR A 1 91  ? -38.97700 33.27600 39.27600 1.000 32.66558  ? 91  THR A HA   1 
ATOM   1398 H  HB   . THR A 1 91  ? -37.76900 31.44500 39.98400 1.000 28.59558  ? 91  THR A HB   1 
ATOM   1399 H  HG1  . THR A 1 91  ? -37.24000 31.29900 42.13500 1.000 32.14558  ? 91  THR A HG1  1 
ATOM   1400 H  HG21 . THR A 1 91  ? -35.75700 32.45000 40.56200 1.000 27.95558  ? 91  THR A HG21 1 
ATOM   1401 H  HG22 . THR A 1 91  ? -36.46900 33.32700 39.46000 1.000 27.95558  ? 91  THR A HG22 1 
ATOM   1402 H  HG23 . THR A 1 91  ? -36.51300 33.77300 40.97400 1.000 27.95558  ? 91  THR A HG23 1 
ATOM   1403 N  N    . LYS A 1 92  ? -40.99700 32.40500 41.56700 1.000 27.19375  ? 92  LYS A N    1 
ATOM   1404 C  CA   . LYS A 1 92  ? -42.24200 31.66700 41.74800 1.000 28.39947  ? 92  LYS A CA   1 
ATOM   1405 C  C    . LYS A 1 92  ? -43.30900 32.08600 40.74700 1.000 31.69917  ? 92  LYS A C    1 
ATOM   1406 O  O    . LYS A 1 92  ? -44.29400 31.35800 40.58000 1.000 32.21932  ? 92  LYS A O    1 
ATOM   1407 C  CB   . LYS A 1 92  ? -42.75400 31.82100 43.18600 1.000 33.61610  ? 92  LYS A CB   1 
ATOM   1408 C  CG   . LYS A 1 92  ? -43.30600 33.19600 43.51100 1.000 40.42124  ? 92  LYS A CG   1 
ATOM   1409 C  CD   . LYS A 1 92  ? -43.62600 33.33700 45.01500 1.000 43.89117  ? 92  LYS A CD   1 
ATOM   1410 C  CE   . LYS A 1 92  ? -44.38600 34.63100 45.28300 1.000 45.35268  ? 92  LYS A CE   1 
ATOM   1411 N  NZ   . LYS A 1 92  ? -44.71400 34.79600 46.74100 1.000 44.38731  ? 92  LYS A NZ   1 
ATOM   1412 H  H    . LYS A 1 92  ? -40.78200 32.93800 42.20700 1.000 31.03558  ? 92  LYS A H    1 
ATOM   1413 H  HA   . LYS A 1 92  ? -42.07000 30.72100 41.61600 1.000 32.39558  ? 92  LYS A HA   1 
ATOM   1414 H  HB2  . LYS A 1 92  ? -43.46500 31.17700 43.33200 1.000 38.39558  ? 92  LYS A HB2  1 
ATOM   1415 H  HB3  . LYS A 1 92  ? -42.02000 31.64800 43.79600 1.000 38.39558  ? 92  LYS A HB3  1 
ATOM   1416 H  HG2  . LYS A 1 92  ? -42.64900 33.87000 43.27500 1.000 45.71558  ? 92  LYS A HG2  1 
ATOM   1417 H  HG3  . LYS A 1 92  ? -44.12400 33.34000 43.01100 1.000 45.71558  ? 92  LYS A HG3  1 
ATOM   1418 H  HD2  . LYS A 1 92  ? -44.17600 32.59200 45.30200 1.000 49.60558  ? 92  LYS A HD2  1 
ATOM   1419 H  HD3  . LYS A 1 92  ? -42.80000 33.35400 45.52300 1.000 49.60558  ? 92  LYS A HD3  1 
ATOM   1420 H  HE2  . LYS A 1 92  ? -43.84100 35.38500 45.00700 1.000 50.30558  ? 92  LYS A HE2  1 
ATOM   1421 H  HE3  . LYS A 1 92  ? -45.21700 34.62300 44.78300 1.000 50.30558  ? 92  LYS A HE3  1 
ATOM   1422 H  HZ1  . LYS A 1 92  ? -45.21100 34.11300 47.02100 1.000 48.76558  ? 92  LYS A HZ1  1 
ATOM   1423 H  HZ2  . LYS A 1 92  ? -43.96500 34.82400 47.22100 1.000 48.76558  ? 92  LYS A HZ2  1 
ATOM   1424 H  HZ3  . LYS A 1 92  ? -45.16600 35.55200 46.86800 1.000 48.76558  ? 92  LYS A HZ3  1 
ATOM   1425 N  N    . LYS A 1 93  ? -43.12300 33.21100 40.05300 1.000 31.55054  ? 93  LYS A N    1 
ATOM   1426 C  CA   . LYS A 1 93  ? -44.04600 33.66000 39.01900 1.000 37.19367  ? 93  LYS A CA   1 
ATOM   1427 C  C    . LYS A 1 93  ? -43.57300 33.33100 37.61000 1.000 34.13950  ? 93  LYS A C    1 
ATOM   1428 O  O    . LYS A 1 93  ? -44.31800 33.55600 36.64600 1.000 35.28732  ? 93  LYS A O    1 
ATOM   1429 C  CB   . LYS A 1 93  ? -44.26900 35.17200 39.12800 1.000 38.35619  ? 93  LYS A CB   1 
ATOM   1430 C  CG   . LYS A 1 93  ? -44.72400 35.61100 40.50500 1.000 41.13295  ? 93  LYS A CG   1 
ATOM   1431 C  CD   . LYS A 1 93  ? -44.74500 37.12900 40.65200 1.000 57.65163  ? 93  LYS A CD   1 
ATOM   1432 C  CE   . LYS A 1 93  ? -45.00600 37.52800 42.10600 1.000 81.51335  ? 93  LYS A CE   1 
ATOM   1433 N  NZ   . LYS A 1 93  ? -44.53700 38.91200 42.40900 1.000 95.35773  ? 93  LYS A NZ   1 
ATOM   1434 H  H    . LYS A 1 93  ? -42.45500 33.73900 40.16700 1.000 35.18558  ? 93  LYS A H    1 
ATOM   1435 H  HA   . LYS A 1 93  ? -44.90000 33.22100 39.15900 1.000 41.36558  ? 93  LYS A HA   1 
ATOM   1436 H  HB2  . LYS A 1 93  ? -43.43500 35.62700 38.93000 1.000 41.81558  ? 93  LYS A HB2  1 
ATOM   1437 H  HB3  . LYS A 1 93  ? -44.95000 35.43600 38.49000 1.000 41.81558  ? 93  LYS A HB3  1 
ATOM   1438 H  HG2  . LYS A 1 93  ? -45.62200 35.28000 40.66300 1.000 44.68558  ? 93  LYS A HG2  1 
ATOM   1439 H  HG3  . LYS A 1 93  ? -44.11600 35.25200 41.17000 1.000 44.68558  ? 93  LYS A HG3  1 
ATOM   1440 H  HD2  . LYS A 1 93  ? -43.88800 37.49300 40.38200 1.000 63.41558  ? 93  LYS A HD2  1 
ATOM   1441 H  HD3  . LYS A 1 93  ? -45.45100 37.49900 40.09900 1.000 63.41558  ? 93  LYS A HD3  1 
ATOM   1442 H  HE2  . LYS A 1 93  ? -45.96000 37.48900 42.28000 1.000 91.55558  ? 93  LYS A HE2  1 
ATOM   1443 H  HE3  . LYS A 1 93  ? -44.53700 36.91600 42.69300 1.000 91.55558  ? 93  LYS A HE3  1 
ATOM   1444 H  HZ1  . LYS A 1 93  ? -44.69700 39.10800 43.26300 1.000 107.17558 ? 93  LYS A HZ1  1 
ATOM   1445 H  HZ2  . LYS A 1 93  ? -43.66200 38.97700 42.25700 1.000 107.17558 ? 93  LYS A HZ2  1 
ATOM   1446 H  HZ3  . LYS A 1 93  ? -44.96400 39.49800 41.89300 1.000 107.17558 ? 93  LYS A HZ3  1 
ATOM   1447 N  N    . TRP A 1 94  ? -42.35600 32.83800 37.46200 1.000 28.85411  ? 94  TRP A N    1 
ATOM   1448 C  CA   . TRP A 1 94  ? -41.89600 32.38100 36.16100 1.000 27.92186  ? 94  TRP A CA   1 
ATOM   1449 C  C    . TRP A 1 94  ? -42.65100 31.10400 35.78800 1.000 32.88741  ? 94  TRP A C    1 
ATOM   1450 O  O    . TRP A 1 94  ? -43.21000 30.40800 36.64300 1.000 30.89152  ? 94  TRP A O    1 
ATOM   1451 C  CB   . TRP A 1 94  ? -40.39400 32.10200 36.19600 1.000 25.54353  ? 94  TRP A CB   1 
ATOM   1452 C  CG   . TRP A 1 94  ? -39.50300 33.30100 36.31800 1.000 26.66855  ? 94  TRP A CG   1 
ATOM   1453 C  CD1  . TRP A 1 94  ? -39.88200 34.62500 36.39000 1.000 29.73844  ? 94  TRP A CD1  1 
ATOM   1454 C  CD2  . TRP A 1 94  ? -38.07600 33.28600 36.48000 1.000 26.77084  ? 94  TRP A CD2  1 
ATOM   1455 N  NE1  . TRP A 1 94  ? -38.77100 35.42200 36.53900 1.000 29.81185  ? 94  TRP A NE1  1 
ATOM   1456 C  CE2  . TRP A 1 94  ? -37.65100 34.62800 36.58200 1.000 27.22914  ? 94  TRP A CE2  1 
ATOM   1457 C  CE3  . TRP A 1 94  ? -37.11100 32.26900 36.51400 1.000 26.89794  ? 94  TRP A CE3  1 
ATOM   1458 C  CZ2  . TRP A 1 94  ? -36.31800 34.97300 36.72900 1.000 25.40418  ? 94  TRP A CZ2  1 
ATOM   1459 C  CZ3  . TRP A 1 94  ? -35.78700 32.61900 36.64300 1.000 25.81450  ? 94  TRP A CZ3  1 
ATOM   1460 C  CH2  . TRP A 1 94  ? -35.39800 33.96100 36.75100 1.000 24.20484  ? 94  TRP A CH2  1 
ATOM   1461 H  H    . TRP A 1 94  ? -41.77900 32.75600 38.09400 1.000 32.31558  ? 94  TRP A H    1 
ATOM   1462 H  HA   . TRP A 1 94  ? -42.05600 33.06000 35.48700 1.000 31.45558  ? 94  TRP A HA   1 
ATOM   1463 H  HB2  . TRP A 1 94  ? -40.20900 31.53000 36.95800 1.000 29.19558  ? 94  TRP A HB2  1 
ATOM   1464 H  HB3  . TRP A 1 94  ? -40.15100 31.64800 35.37400 1.000 29.19558  ? 94  TRP A HB3  1 
ATOM   1465 H  HD1  . TRP A 1 94  ? -40.75800 34.93300 36.34500 1.000 33.25558  ? 94  TRP A HD1  1 
ATOM   1466 H  HE1  . TRP A 1 94  ? -38.77700 36.28000 36.59700 1.000 33.24558  ? 94  TRP A HE1  1 
ATOM   1467 H  HE3  . TRP A 1 94  ? -37.36200 31.37600 36.45200 1.000 31.63558  ? 94  TRP A HE3  1 
ATOM   1468 H  HZ2  . TRP A 1 94  ? -36.05700 35.86200 36.81100 1.000 28.83558  ? 94  TRP A HZ2  1 
ATOM   1469 H  HZ3  . TRP A 1 94  ? -35.13800 31.95300 36.65800 1.000 30.50558  ? 94  TRP A HZ3  1 
ATOM   1470 H  HH2  . TRP A 1 94  ? -34.49600 34.16800 36.83900 1.000 28.09558  ? 94  TRP A HH2  1 
ATOM   1471 N  N    . LYS A 1 95  ? -42.62800 30.77800 34.49700 1.000 28.97332  ? 95  LYS A N    1 
ATOM   1472 C  CA   . LYS A 1 95  ? -43.18900 29.53600 33.99100 1.000 31.84990  ? 95  LYS A CA   1 
ATOM   1473 C  C    . LYS A 1 95  ? -42.06200 28.59500 33.57600 1.000 30.29305  ? 95  LYS A C    1 
ATOM   1474 O  O    . LYS A 1 95  ? -41.03200 29.02900 33.05300 1.000 29.41036  ? 95  LYS A O    1 
ATOM   1475 C  CB   . LYS A 1 95  ? -44.09200 29.78800 32.78000 1.000 32.74412  ? 95  LYS A CB   1 
ATOM   1476 C  CG   . LYS A 1 95  ? -45.32300 30.63400 33.06200 1.000 40.58207  ? 95  LYS A CG   1 
ATOM   1477 C  CD   . LYS A 1 95  ? -46.10900 30.13500 34.26100 1.000 42.42908  ? 95  LYS A CD   1 
ATOM   1478 C  CE   . LYS A 1 95  ? -47.47400 30.81400 34.39100 1.000 52.40990  ? 95  LYS A CE   1 
ATOM   1479 N  NZ   . LYS A 1 95  ? -47.68200 31.92300 33.42000 1.000 85.88995  ? 95  LYS A NZ   1 
ATOM   1480 H  H    . LYS A 1 95  ? -42.28400 31.27400 33.88400 1.000 32.83558  ? 95  LYS A H    1 
ATOM   1481 H  HA   . LYS A 1 95  ? -43.71700 29.11700 34.68800 1.000 36.30558  ? 95  LYS A HA   1 
ATOM   1482 H  HB2  . LYS A 1 95  ? -43.57300 30.24600 32.10000 1.000 36.81558  ? 95  LYS A HB2  1 
ATOM   1483 H  HB3  . LYS A 1 95  ? -44.39800 28.93100 32.44200 1.000 36.81558  ? 95  LYS A HB3  1 
ATOM   1484 H  HG2  . LYS A 1 95  ? -45.04600 31.54600 33.24300 1.000 45.57558  ? 95  LYS A HG2  1 
ATOM   1485 H  HG3  . LYS A 1 95  ? -45.90800 30.61200 32.28900 1.000 45.57558  ? 95  LYS A HG3  1 
ATOM   1486 H  HD2  . LYS A 1 95  ? -46.25600 29.18000 34.16800 1.000 47.77558  ? 95  LYS A HD2  1 
ATOM   1487 H  HD3  . LYS A 1 95  ? -45.60500 30.31600 35.06900 1.000 47.77558  ? 95  LYS A HD3  1 
ATOM   1488 H  HE2  . LYS A 1 95  ? -48.16800 30.15300 34.24000 1.000 58.96558  ? 95  LYS A HE2  1 
ATOM   1489 H  HE3  . LYS A 1 95  ? -47.55600 31.18300 35.28500 1.000 58.96558  ? 95  LYS A HE3  1 
ATOM   1490 H  HZ1  . LYS A 1 95  ? -47.02200 32.51600 33.49000 1.000 98.53558  ? 95  LYS A HZ1  1 
ATOM   1491 H  HZ2  . LYS A 1 95  ? -47.69600 31.60200 32.59000 1.000 98.53558  ? 95  LYS A HZ2  1 
ATOM   1492 H  HZ3  . LYS A 1 95  ? -48.45500 32.33100 33.58600 1.000 98.53558  ? 95  LYS A HZ3  1 
ATOM   1493 N  N    . TYR A 1 96  ? -42.28700 27.29700 33.77800 1.000 28.95699  ? 96  TYR A N    1 
ATOM   1494 C  CA   . TYR A 1 96  ? -41.27100 26.26000 33.56500 1.000 25.83029  ? 96  TYR A CA   1 
ATOM   1495 C  C    . TYR A 1 96  ? -41.83900 25.20900 32.62000 1.000 28.49658  ? 96  TYR A C    1 
ATOM   1496 O  O    . TYR A 1 96  ? -42.22900 24.11400 33.03900 1.000 32.39101  ? 96  TYR A O    1 
ATOM   1497 C  CB   . TYR A 1 96  ? -40.83200 25.65700 34.90100 1.000 27.62886  ? 96  TYR A CB   1 
ATOM   1498 C  CG   . TYR A 1 96  ? -40.29900 26.72900 35.81800 1.000 25.35167  ? 96  TYR A CG   1 
ATOM   1499 C  CD1  . TYR A 1 96  ? -38.99800 27.21800 35.65900 1.000 25.32708  ? 96  TYR A CD1  1 
ATOM   1500 C  CD2  . TYR A 1 96  ? -41.09400 27.29400 36.80000 1.000 27.42658  ? 96  TYR A CD2  1 
ATOM   1501 C  CE1  . TYR A 1 96  ? -38.50300 28.21600 36.47600 1.000 27.02263  ? 96  TYR A CE1  1 
ATOM   1502 C  CE2  . TYR A 1 96  ? -40.59600 28.29600 37.62900 1.000 26.59442  ? 96  TYR A CE2  1 
ATOM   1503 C  CZ   . TYR A 1 96  ? -39.30800 28.75200 37.45300 1.000 27.37827  ? 96  TYR A CZ   1 
ATOM   1504 O  OH   . TYR A 1 96  ? -38.79500 29.75200 38.24600 1.000 26.63927  ? 96  TYR A OH   1 
ATOM   1505 H  H    . TYR A 1 96  ? -43.04100 26.98200 34.04600 1.000 33.35558  ? 96  TYR A H    1 
ATOM   1506 H  HA   . TYR A 1 96  ? -40.49300 26.64400 33.13300 1.000 29.86558  ? 96  TYR A HA   1 
ATOM   1507 H  HB2  . TYR A 1 96  ? -41.59100 25.23300 35.33000 1.000 32.31558  ? 96  TYR A HB2  1 
ATOM   1508 H  HB3  . TYR A 1 96  ? -40.13100 25.00500 34.74700 1.000 32.31558  ? 96  TYR A HB3  1 
ATOM   1509 H  HD1  . TYR A 1 96  ? -38.45700 26.86500 34.99100 1.000 30.17558  ? 96  TYR A HD1  1 
ATOM   1510 H  HD2  . TYR A 1 96  ? -41.97000 27.00100 36.90800 1.000 32.27558  ? 96  TYR A HD2  1 
ATOM   1511 H  HE1  . TYR A 1 96  ? -37.63200 28.52200 36.36600 1.000 32.36558  ? 96  TYR A HE1  1 
ATOM   1512 H  HE2  . TYR A 1 96  ? -41.13100 28.65700 38.29800 1.000 31.41558  ? 96  TYR A HE2  1 
ATOM   1513 H  HH   . TYR A 1 96  ? -39.37200 30.00100 38.80400 1.000 31.74558  ? 96  TYR A HH   1 
ATOM   1514 N  N    . PRO A 1 97  ? -41.89400 25.50600 31.33100 1.000 29.83921  ? 97  PRO A N    1 
ATOM   1515 C  CA   . PRO A 1 97  ? -42.46800 24.54000 30.39400 1.000 30.58424  ? 97  PRO A CA   1 
ATOM   1516 C  C    . PRO A 1 97  ? -41.53600 23.36000 30.17900 1.000 31.85002  ? 97  PRO A C    1 
ATOM   1517 O  O    . PRO A 1 97  ? -40.31100 23.47300 30.26500 1.000 31.14863  ? 97  PRO A O    1 
ATOM   1518 C  CB   . PRO A 1 97  ? -42.64100 25.35800 29.10700 1.000 33.60436  ? 97  PRO A CB   1 
ATOM   1519 C  CG   . PRO A 1 97  ? -41.51200 26.33700 29.16000 1.000 29.74383  ? 97  PRO A CG   1 
ATOM   1520 C  CD   . PRO A 1 97  ? -41.43800 26.72800 30.64800 1.000 31.05951  ? 97  PRO A CD   1 
ATOM   1521 H  HA   . PRO A 1 97  ? -43.33300 24.22400 30.69900 1.000 34.36558  ? 97  PRO A HA   1 
ATOM   1522 H  HB2  . PRO A 1 97  ? -42.57100 24.78100 28.33000 1.000 37.75558  ? 97  PRO A HB2  1 
ATOM   1523 H  HB3  . PRO A 1 97  ? -43.50000 25.80900 29.10900 1.000 37.75558  ? 97  PRO A HB3  1 
ATOM   1524 H  HG2  . PRO A 1 97  ? -40.68900 25.91700 28.86600 1.000 33.59558  ? 97  PRO A HG2  1 
ATOM   1525 H  HG3  . PRO A 1 97  ? -41.70900 27.10700 28.60400 1.000 33.59558  ? 97  PRO A HG3  1 
ATOM   1526 H  HD2  . PRO A 1 97  ? -40.52900 26.94900 30.90300 1.000 35.55558  ? 97  PRO A HD2  1 
ATOM   1527 H  HD3  . PRO A 1 97  ? -42.02700 27.47400 30.84000 1.000 35.55558  ? 97  PRO A HD3  1 
ATOM   1528 N  N    . GLN A 1 98  ? -42.14600 22.21300 29.90200 1.000 30.10095  ? 98  GLN A N    1 
ATOM   1529 C  CA   . GLN A 1 98  ? -41.40600 21.03100 29.48400 1.000 30.64644  ? 98  GLN A CA   1 
ATOM   1530 C  C    . GLN A 1 98  ? -41.12200 21.15700 27.99600 1.000 29.11147  ? 98  GLN A C    1 
ATOM   1531 O  O    . GLN A 1 98  ? -42.06200 21.20700 27.19700 1.000 33.28069  ? 98  GLN A O    1 
ATOM   1532 C  CB   . GLN A 1 98  ? -42.22000 19.77000 29.76100 1.000 30.04443  ? 98  GLN A CB   1 
ATOM   1533 C  CG   . GLN A 1 98  ? -42.42700 19.50600 31.24300 1.000 33.40596  ? 98  GLN A CG   1 
ATOM   1534 C  CD   . GLN A 1 98  ? -41.11900 19.23000 31.94700 1.000 36.48797  ? 98  GLN A CD   1 
ATOM   1535 O  OE1  . GLN A 1 98  ? -40.36800 18.33900 31.54200 1.000 36.81950  ? 98  GLN A OE1  1 
ATOM   1536 N  NE2  . GLN A 1 98  ? -40.83600 19.99200 33.00100 1.000 32.95756  ? 98  GLN A NE2  1 
ATOM   1537 H  H    . GLN A 1 98  ? -42.99700 22.09300 29.94800 1.000 33.14558  ? 98  GLN A H    1 
ATOM   1538 H  HA   . GLN A 1 98  ? -40.57200 20.96500 29.97500 1.000 33.42558  ? 98  GLN A HA   1 
ATOM   1539 H  HB2  . GLN A 1 98  ? -43.09400 19.86400 29.35000 1.000 31.96558  ? 98  GLN A HB2  1 
ATOM   1540 H  HB3  . GLN A 1 98  ? -41.75600 19.00700 29.38400 1.000 31.96558  ? 98  GLN A HB3  1 
ATOM   1541 H  HG2  . GLN A 1 98  ? -42.83600 20.28400 31.65400 1.000 36.20558  ? 98  GLN A HG2  1 
ATOM   1542 H  HG3  . GLN A 1 98  ? -43.00200 18.73200 31.35400 1.000 36.20558  ? 98  GLN A HG3  1 
ATOM   1543 H  HE21 . GLN A 1 98  ? -41.38700 20.60400 33.24900 1.000 36.74558  ? 98  GLN A HE21 1 
ATOM   1544 H  HE22 . GLN A 1 98  ? -40.10300 19.87200 33.43400 1.000 36.74558  ? 98  GLN A HE22 1 
ATOM   1545 N  N    . VAL A 1 99  ? -39.84800 21.21900 27.61900 1.000 30.24648  ? 99  VAL A N    1 
ATOM   1546 C  CA   . VAL A 1 99  ? -39.45900 21.34200 26.22000 1.000 29.71464  ? 99  VAL A CA   1 
ATOM   1547 C  C    . VAL A 1 99  ? -38.57600 20.15600 25.86100 1.000 31.46487  ? 99  VAL A C    1 
ATOM   1548 O  O    . VAL A 1 99  ? -37.51600 19.96100 26.46300 1.000 32.65039  ? 99  VAL A O    1 
ATOM   1549 C  CB   . VAL A 1 99  ? -38.72900 22.66300 25.93700 1.000 27.83270  ? 99  VAL A CB   1 
ATOM   1550 C  CG1  . VAL A 1 99  ? -38.39900 22.74600 24.43600 1.000 30.64688  ? 99  VAL A CG1  1 
ATOM   1551 C  CG2  . VAL A 1 99  ? -39.57200 23.84400 26.39300 1.000 27.38124  ? 99  VAL A CG2  1 
ATOM   1552 H  H    . VAL A 1 99  ? -39.18400 21.19100 28.16500 1.000 32.88558  ? 99  VAL A H    1 
ATOM   1553 H  HA   . VAL A 1 99  ? -40.25800 21.30600 25.67000 1.000 31.95558  ? 99  VAL A HA   1 
ATOM   1554 H  HB   . VAL A 1 99  ? -37.89700 22.70000 26.43500 1.000 30.32558  ? 99  VAL A HB   1 
ATOM   1555 H  HG11 . VAL A 1 99  ? -38.10400 23.64600 24.22700 1.000 33.31558  ? 99  VAL A HG11 1 
ATOM   1556 H  HG12 . VAL A 1 99  ? -37.69500 22.11100 24.23200 1.000 33.31558  ? 99  VAL A HG12 1 
ATOM   1557 H  HG13 . VAL A 1 99  ? -39.19500 22.53200 23.92500 1.000 33.31558  ? 99  VAL A HG13 1 
ATOM   1558 H  HG21 . VAL A 1 99  ? -39.11900 24.66700 26.15400 1.000 30.10558  ? 99  VAL A HG21 1 
ATOM   1559 H  HG22 . VAL A 1 99  ? -40.43700 23.80300 25.95500 1.000 30.10558  ? 99  VAL A HG22 1 
ATOM   1560 H  HG23 . VAL A 1 99  ? -39.68700 23.79700 27.35500 1.000 30.10558  ? 99  VAL A HG23 1 
ATOM   1561 N  N    . ASN A 1 100 ? -39.00600 19.38100 24.87000 1.000 31.76980  ? 100 ASN A N    1 
ATOM   1562 C  CA   . ASN A 1 100 ? -38.32000 18.16600 24.47000 1.000 33.37875  ? 100 ASN A CA   1 
ATOM   1563 C  C    . ASN A 1 100 ? -37.95300 17.29700 25.67100 1.000 37.53087  ? 100 ASN A C    1 
ATOM   1564 O  O    . ASN A 1 100 ? -36.86400 16.72200 25.73400 1.000 34.87839  ? 100 ASN A O    1 
ATOM   1565 C  CB   . ASN A 1 100 ? -37.07000 18.47400 23.65500 1.000 37.46041  ? 100 ASN A CB   1 
ATOM   1566 C  CG   . ASN A 1 100 ? -36.61400 17.27800 22.86700 1.000 42.16735  ? 100 ASN A CG   1 
ATOM   1567 O  OD1  . ASN A 1 100 ? -37.42700 16.61100 22.24100 1.000 40.14384  ? 100 ASN A OD1  1 
ATOM   1568 N  ND2  . ASN A 1 100 ? -35.32200 16.97800 22.91600 1.000 44.60498  ? 100 ASN A ND2  1 
ATOM   1569 H  H    . ASN A 1 100 ? -39.71100 19.54500 24.40500 1.000 33.02558  ? 100 ASN A H    1 
ATOM   1570 H  HA   . ASN A 1 100 ? -38.93600 17.66100 23.91500 1.000 34.16558  ? 100 ASN A HA   1 
ATOM   1571 H  HB2  . ASN A 1 100 ? -37.26200 19.19400 23.03400 1.000 39.19558  ? 100 ASN A HB2  1 
ATOM   1572 H  HB3  . ASN A 1 100 ? -36.35400 18.73600 24.25500 1.000 39.19558  ? 100 ASN A HB3  1 
ATOM   1573 H  HD21 . ASN A 1 100 ? -35.02100 16.30100 22.47900 1.000 46.59558  ? 100 ASN A HD21 1 
ATOM   1574 H  HD22 . ASN A 1 100 ? -34.78600 17.46000 23.38400 1.000 46.59558  ? 100 ASN A HD22 1 
ATOM   1575 N  N    . GLY A 1 101 ? -38.87900 17.19100 26.61200 1.000 36.20838  ? 101 GLY A N    1 
ATOM   1576 C  CA   . GLY A 1 101 ? -38.72700 16.31600 27.75700 1.000 38.61635  ? 101 GLY A CA   1 
ATOM   1577 C  C    . GLY A 1 101 ? -37.91900 16.87300 28.90700 1.000 38.32960  ? 101 GLY A C    1 
ATOM   1578 O  O    . GLY A 1 101 ? -37.66800 16.14100 29.86300 1.000 36.32009  ? 101 GLY A O    1 
ATOM   1579 H  H    . GLY A 1 101 ? -39.62100 17.62700 26.60900 1.000 37.52558  ? 101 GLY A H    1 
ATOM   1580 H  HA2  . GLY A 1 101 ? -39.60900 16.10100 28.09800 1.000 40.16558  ? 101 GLY A HA2  1 
ATOM   1581 H  HA3  . GLY A 1 101 ? -38.29400 15.49900 27.46400 1.000 40.16558  ? 101 GLY A HA3  1 
ATOM   1582 N  N    . LEU A 1 102 ? -37.49900 18.13600 28.84100 1.000 29.07069  ? 102 LEU A N    1 
ATOM   1583 C  CA   . LEU A 1 102 ? -36.69700 18.76700 29.87900 1.000 29.64005  ? 102 LEU A CA   1 
ATOM   1584 C  C    . LEU A 1 102 ? -37.40900 19.98600 30.44400 1.000 32.07494  ? 102 LEU A C    1 
ATOM   1585 O  O    . LEU A 1 102 ? -38.19200 20.64100 29.76000 1.000 29.68543  ? 102 LEU A O    1 
ATOM   1586 C  CB   . LEU A 1 102 ? -35.34000 19.21700 29.33700 1.000 28.96884  ? 102 LEU A CB   1 
ATOM   1587 C  CG   . LEU A 1 102 ? -34.48000 18.11800 28.69300 1.000 35.07771  ? 102 LEU A CG   1 
ATOM   1588 C  CD1  . LEU A 1 102 ? -33.21900 18.71900 28.12000 1.000 39.22989  ? 102 LEU A CD1  1 
ATOM   1589 C  CD2  . LEU A 1 102 ? -34.13100 17.03600 29.67800 1.000 40.41599  ? 102 LEU A CD2  1 
ATOM   1590 H  H    . LEU A 1 102 ? -37.67300 18.66100 28.18300 1.000 30.58558  ? 102 LEU A H    1 
ATOM   1591 H  HA   . LEU A 1 102 ? -36.56400 18.12500 30.59400 1.000 32.09558  ? 102 LEU A HA   1 
ATOM   1592 H  HB2  . LEU A 1 102 ? -35.49400 19.89600 28.66100 1.000 31.58558  ? 102 LEU A HB2  1 
ATOM   1593 H  HB3  . LEU A 1 102 ? -34.82900 19.59000 30.07200 1.000 31.58558  ? 102 LEU A HB3  1 
ATOM   1594 H  HG   . LEU A 1 102 ? -34.99300 17.70700 27.98000 1.000 38.10558  ? 102 LEU A HG   1 
ATOM   1595 H  HD11 . LEU A 1 102 ? -32.69200 18.01600 27.71000 1.000 43.42558  ? 102 LEU A HD11 1 
ATOM   1596 H  HD12 . LEU A 1 102 ? -33.46000 19.38300 27.45600 1.000 43.42558  ? 102 LEU A HD12 1 
ATOM   1597 H  HD13 . LEU A 1 102 ? -32.71400 19.13600 28.83600 1.000 43.42558  ? 102 LEU A HD13 1 
ATOM   1598 H  HD21 . LEU A 1 102 ? -33.54800 16.39100 29.24600 1.000 44.05558  ? 102 LEU A HD21 1 
ATOM   1599 H  HD22 . LEU A 1 102 ? -33.67800 17.43400 30.43800 1.000 44.05558  ? 102 LEU A HD22 1 
ATOM   1600 H  HD23 . LEU A 1 102 ? -34.94700 16.60000 29.97100 1.000 44.05558  ? 102 LEU A HD23 1 
ATOM   1601 N  N    . THR A 1 103 ? -37.11400 20.30700 31.70000 1.000 26.91178  ? 103 THR A N    1 
ATOM   1602 C  CA   . THR A 1 103 ? -37.63900 21.53400 32.28300 1.000 24.74867  ? 103 THR A CA   1 
ATOM   1603 C  C    . THR A 1 103 ? -36.84600 22.71700 31.75600 1.000 26.09936  ? 103 THR A C    1 
ATOM   1604 O  O    . THR A 1 103 ? -35.62300 22.78300 31.94200 1.000 25.12746  ? 103 THR A O    1 
ATOM   1605 C  CB   . THR A 1 103 ? -37.55600 21.48000 33.80600 1.000 27.40185  ? 103 THR A CB   1 
ATOM   1606 O  OG1  . THR A 1 103 ? -38.17400 20.27600 34.25000 1.000 27.84576  ? 103 THR A OG1  1 
ATOM   1607 C  CG2  . THR A 1 103 ? -38.27100 22.66900 34.41600 1.000 25.98108  ? 103 THR A CG2  1 
ATOM   1608 H  H    . THR A 1 103 ? -36.62000 19.83800 32.22500 1.000 30.07558  ? 103 THR A H    1 
ATOM   1609 H  HA   . THR A 1 103 ? -38.57000 21.63700 32.02900 1.000 28.08558  ? 103 THR A HA   1 
ATOM   1610 H  HB   . THR A 1 103 ? -36.63000 21.50600 34.09400 1.000 31.57558  ? 103 THR A HB   1 
ATOM   1611 H  HG1  . THR A 1 103 ? -38.14800 20.23200 35.08800 1.000 31.56558  ? 103 THR A HG1  1 
ATOM   1612 H  HG21 . THR A 1 103 ? -38.31300 22.57200 35.38000 1.000 30.26558  ? 103 THR A HG21 1 
ATOM   1613 H  HG22 . THR A 1 103 ? -37.79600 23.48800 34.20300 1.000 30.26558  ? 103 THR A HG22 1 
ATOM   1614 H  HG23 . THR A 1 103 ? -39.17300 22.72900 34.06600 1.000 30.26558  ? 103 THR A HG23 1 
ATOM   1615 N  N    . SER A 1 104 ? -37.53200 23.63800 31.08000 1.000 25.17884  ? 104 SER A N    1 
ATOM   1616 C  CA   . SER A 1 104 ? -36.94600 24.88800 30.64400 1.000 24.52727  ? 104 SER A CA   1 
ATOM   1617 C  C    . SER A 1 104 ? -37.54200 26.03300 31.46000 1.000 25.13919  ? 104 SER A C    1 
ATOM   1618 O  O    . SER A 1 104 ? -38.22200 25.81100 32.47000 1.000 26.98336  ? 104 SER A O    1 
ATOM   1619 C  CB   . SER A 1 104 ? -37.16900 25.08100 29.14300 1.000 28.67439  ? 104 SER A CB   1 
ATOM   1620 O  OG   . SER A 1 104 ? -36.34300 26.13100 28.67500 1.000 26.54125  ? 104 SER A OG   1 
ATOM   1621 H  H    . SER A 1 104 ? -38.35900 23.55200 30.86100 1.000 29.07558  ? 104 SER A H    1 
ATOM   1622 H  HA   . SER A 1 104 ? -35.98900 24.85900 30.80100 1.000 28.59558  ? 104 SER A HA   1 
ATOM   1623 H  HB2  . SER A 1 104 ? -36.94300 24.26100 28.67600 1.000 33.23558  ? 104 SER A HB2  1 
ATOM   1624 H  HB3  . SER A 1 104 ? -38.09900 25.30700 28.98300 1.000 33.23558  ? 104 SER A HB3  1 
ATOM   1625 H  HG   . SER A 1 104 ? -36.47700 26.25900 27.85600 1.000 30.87558  ? 104 SER A HG   1 
ATOM   1626 N  N    . ILE A 1 105 ? -37.26800 27.26600 31.03700 1.000 26.43593  ? 105 ILE A N    1 
ATOM   1627 C  CA   . ILE A 1 105 ? -37.81300 28.45500 31.68700 1.000 24.70602  ? 105 ILE A CA   1 
ATOM   1628 C  C    . ILE A 1 105 ? -38.31500 29.38400 30.59600 1.000 26.58859  ? 105 ILE A C    1 
ATOM   1629 O  O    . ILE A 1 105 ? -37.55300 29.75200 29.69500 1.000 27.56784  ? 105 ILE A O    1 
ATOM   1630 C  CB   . ILE A 1 105 ? -36.78800 29.21100 32.55400 1.000 26.06674  ? 105 ILE A CB   1 
ATOM   1631 C  CG1  . ILE A 1 105 ? -35.91200 28.27700 33.37800 1.000 24.43902  ? 105 ILE A CG1  1 
ATOM   1632 C  CG2  . ILE A 1 105 ? -37.52500 30.16500 33.49000 1.000 25.78082  ? 105 ILE A CG2  1 
ATOM   1633 C  CD1  . ILE A 1 105 ? -34.83100 29.03000 34.15900 1.000 26.97963  ? 105 ILE A CD1  1 
ATOM   1634 H  H    . ILE A 1 105 ? -36.76100 27.44100 30.36500 1.000 31.16558  ? 105 ILE A H    1 
ATOM   1635 H  HA   . ILE A 1 105 ? -38.54600 28.17500 32.25600 1.000 29.08558  ? 105 ILE A HA   1 
ATOM   1636 H  HB   . ILE A 1 105 ? -36.20600 29.69600 31.94900 1.000 31.00558  ? 105 ILE A HB   1 
ATOM   1637 H  HG12 . ILE A 1 105 ? -36.46800 27.80100 34.01500 1.000 29.42558  ? 105 ILE A HG12 1 
ATOM   1638 H  HG13 . ILE A 1 105 ? -35.47300 27.64800 32.78400 1.000 29.42558  ? 105 ILE A HG13 1 
ATOM   1639 H  HG21 . ILE A 1 105 ? -36.88100 30.75900 33.90600 1.000 30.48558  ? 105 ILE A HG21 1 
ATOM   1640 H  HG22 . ILE A 1 105 ? -38.16600 30.68000 32.97500 1.000 30.48558  ? 105 ILE A HG22 1 
ATOM   1641 H  HG23 . ILE A 1 105 ? -37.98600 29.64800 34.16900 1.000 30.48558  ? 105 ILE A HG23 1 
ATOM   1642 H  HD11 . ILE A 1 105 ? -34.20800 28.38800 34.53400 1.000 32.69558  ? 105 ILE A HD11 1 
ATOM   1643 H  HD12 . ILE A 1 105 ? -34.36500 29.62900 33.55500 1.000 32.69558  ? 105 ILE A HD12 1 
ATOM   1644 H  HD13 . ILE A 1 105 ? -35.25100 29.53800 34.87000 1.000 32.69558  ? 105 ILE A HD13 1 
ATOM   1645 N  N    . LYS A 1 106 ? -39.58000 29.76900 30.68100 1.000 24.69378  ? 106 LYS A N    1 
ATOM   1646 C  CA   . LYS A 1 106 ? -40.09700 30.80600 29.79800 1.000 30.75088  ? 106 LYS A CA   1 
ATOM   1647 C  C    . LYS A 1 106 ? -39.37900 32.11900 30.06800 1.000 30.44918  ? 106 LYS A C    1 
ATOM   1648 O  O    . LYS A 1 106 ? -39.11900 32.47500 31.21700 1.000 30.02593  ? 106 LYS A O    1 
ATOM   1649 C  CB   . LYS A 1 106 ? -41.59500 30.97800 30.02000 1.000 31.44800  ? 106 LYS A CB   1 
ATOM   1650 C  CG   . LYS A 1 106 ? -42.24500 31.99500 29.09600 1.000 33.81309  ? 106 LYS A CG   1 
ATOM   1651 C  CD   . LYS A 1 106 ? -43.76100 32.01200 29.29800 1.000 42.80685  ? 106 LYS A CD   1 
ATOM   1652 C  CE   . LYS A 1 106 ? -44.40900 33.15600 28.51700 1.000 50.46917  ? 106 LYS A CE   1 
ATOM   1653 N  NZ   . LYS A 1 106 ? -44.42400 34.41200 29.31900 1.000 76.12209  ? 106 LYS A NZ   1 
ATOM   1654 H  H    . LYS A 1 106 ? -40.15500 29.45000 31.23500 1.000 28.29558  ? 106 LYS A H    1 
ATOM   1655 H  HA   . LYS A 1 106 ? -39.95100 30.55400 28.87300 1.000 35.05558  ? 106 LYS A HA   1 
ATOM   1656 H  HB2  . LYS A 1 106 ? -42.03100 30.12400 29.87300 1.000 35.41558  ? 106 LYS A HB2  1 
ATOM   1657 H  HB3  . LYS A 1 106 ? -41.74200 31.27200 30.93300 1.000 35.41558  ? 106 LYS A HB3  1 
ATOM   1658 H  HG2  . LYS A 1 106 ? -41.89700 32.87900 29.29100 1.000 37.56558  ? 106 LYS A HG2  1 
ATOM   1659 H  HG3  . LYS A 1 106 ? -42.05900 31.76100 28.17300 1.000 37.56558  ? 106 LYS A HG3  1 
ATOM   1660 H  HD2  . LYS A 1 106 ? -44.13800 31.17500 28.98500 1.000 47.81558  ? 106 LYS A HD2  1 
ATOM   1661 H  HD3  . LYS A 1 106 ? -43.96000 32.13300 30.24000 1.000 47.81558  ? 106 LYS A HD3  1 
ATOM   1662 H  HE2  . LYS A 1 106 ? -43.90600 33.31700 27.70300 1.000 56.17558  ? 106 LYS A HE2  1 
ATOM   1663 H  HE3  . LYS A 1 106 ? -45.32500 32.92000 28.29900 1.000 56.17558  ? 106 LYS A HE3  1 
ATOM   1664 H  HZ1  . LYS A 1 106 ? -44.79700 35.06900 28.84900 1.000 86.54558  ? 106 LYS A HZ1  1 
ATOM   1665 H  HZ2  . LYS A 1 106 ? -44.89100 34.29000 30.06700 1.000 86.54558  ? 106 LYS A HZ2  1 
ATOM   1666 H  HZ3  . LYS A 1 106 ? -43.59200 34.64600 29.53300 1.000 86.54558  ? 106 LYS A HZ3  1 
ATOM   1667 N  N    . TRP A 1 107 ? -39.06400 32.85600 29.00600 1.000 27.48333  ? 107 TRP A N    1 
ATOM   1668 C  CA   . TRP A 1 107 ? -38.24700 34.04500 29.17800 1.000 29.21826  ? 107 TRP A CA   1 
ATOM   1669 C  C    . TRP A 1 107 ? -38.94300 35.07100 30.06300 1.000 31.78917  ? 107 TRP A C    1 
ATOM   1670 O  O    . TRP A 1 107 ? -40.12700 35.38300 29.88600 1.000 31.55509  ? 107 TRP A O    1 
ATOM   1671 C  CB   . TRP A 1 107 ? -37.91300 34.71000 27.83500 1.000 29.88693  ? 107 TRP A CB   1 
ATOM   1672 C  CG   . TRP A 1 107 ? -36.94000 35.84600 28.05200 1.000 31.77890  ? 107 TRP A CG   1 
ATOM   1673 C  CD1  . TRP A 1 107 ? -35.58100 35.76600 28.04200 1.000 32.95068  ? 107 TRP A CD1  1 
ATOM   1674 C  CD2  . TRP A 1 107 ? -37.25600 37.20900 28.36300 1.000 31.95393  ? 107 TRP A CD2  1 
ATOM   1675 N  NE1  . TRP A 1 107 ? -35.03300 36.98700 28.31900 1.000 35.52233  ? 107 TRP A NE1  1 
ATOM   1676 C  CE2  . TRP A 1 107 ? -36.03800 37.89200 28.51700 1.000 33.39711  ? 107 TRP A CE2  1 
ATOM   1677 C  CE3  . TRP A 1 107 ? -38.44700 37.91500 28.53200 1.000 39.70077  ? 107 TRP A CE3  1 
ATOM   1678 C  CZ2  . TRP A 1 107 ? -35.97500 39.24900 28.82100 1.000 39.20431  ? 107 TRP A CZ2  1 
ATOM   1679 C  CZ3  . TRP A 1 107 ? -38.38200 39.27000 28.82800 1.000 43.01987  ? 107 TRP A CZ3  1 
ATOM   1680 C  CH2  . TRP A 1 107 ? -37.15900 39.91600 28.97900 1.000 38.67208  ? 107 TRP A CH2  1 
ATOM   1681 H  H    . TRP A 1 107 ? -39.30500 32.69000 28.19700 1.000 30.70558  ? 107 TRP A H    1 
ATOM   1682 H  HA   . TRP A 1 107 ? -37.41900 33.76400 29.59700 1.000 32.59558  ? 107 TRP A HA   1 
ATOM   1683 H  HB2  . TRP A 1 107 ? -37.50600 34.06000 27.24100 1.000 32.95558  ? 107 TRP A HB2  1 
ATOM   1684 H  HB3  . TRP A 1 107 ? -38.72300 35.06400 27.43500 1.000 32.95558  ? 107 TRP A HB3  1 
ATOM   1685 H  HD1  . TRP A 1 107 ? -35.09500 34.99200 27.87100 1.000 36.75558  ? 107 TRP A HD1  1 
ATOM   1686 H  HE1  . TRP A 1 107 ? -34.19100 37.15900 28.36200 1.000 39.35558  ? 107 TRP A HE1  1 
ATOM   1687 H  HE3  . TRP A 1 107 ? -39.26900 37.48700 28.44700 1.000 42.87558  ? 107 TRP A HE3  1 
ATOM   1688 H  HZ2  . TRP A 1 107 ? -35.15900 39.68500 28.91400 1.000 42.07558  ? 107 TRP A HZ2  1 
ATOM   1689 H  HZ3  . TRP A 1 107 ? -39.17000 39.75400 28.92700 1.000 45.93558  ? 107 TRP A HZ3  1 
ATOM   1690 H  HH2  . TRP A 1 107 ? -37.14600 40.82200 29.19200 1.000 40.59558  ? 107 TRP A HH2  1 
ATOM   1691 N  N    . ALA A 1 108 ? -38.17400 35.62800 30.99000 1.000 30.98340  ? 108 ALA A N    1 
ATOM   1692 C  CA   . ALA A 1 108 ? -38.59800 36.71300 31.86700 1.000 32.32975  ? 108 ALA A CA   1 
ATOM   1693 C  C    . ALA A 1 108 ? -37.34100 37.24100 32.53400 1.000 31.22678  ? 108 ALA A C    1 
ATOM   1694 O  O    . ALA A 1 108 ? -36.39900 36.49000 32.74500 1.000 32.79015  ? 108 ALA A O    1 
ATOM   1695 C  CB   . ALA A 1 108 ? -39.60200 36.24100 32.92000 1.000 38.16253  ? 108 ALA A CB   1 
ATOM   1696 H  H    . ALA A 1 108 ? -37.36300 35.38500 31.13800 1.000 34.23558  ? 108 ALA A H    1 
ATOM   1697 H  HA   . ALA A 1 108 ? -39.02700 37.41800 31.35700 1.000 35.19558  ? 108 ALA A HA   1 
ATOM   1698 H  HB1  . ALA A 1 108 ? -39.85900 36.99500 33.47300 1.000 42.28558  ? 108 ALA A HB1  1 
ATOM   1699 H  HB2  . ALA A 1 108 ? -40.38200 35.87800 32.47200 1.000 42.28558  ? 108 ALA A HB2  1 
ATOM   1700 H  HB3  . ALA A 1 108 ? -39.18600 35.55600 33.46800 1.000 42.28558  ? 108 ALA A HB3  1 
ATOM   1701 N  N    . ASP A 1 109 ? -37.32800 38.53100 32.85300 1.000 35.91974  ? 109 ASP A N    1 
ATOM   1702 C  CA   . ASP A 1 109 ? -36.29000 39.07800 33.73300 1.000 31.82615  ? 109 ASP A CA   1 
ATOM   1703 C  C    . ASP A 1 109 ? -34.88300 38.67000 33.30000 1.000 32.75329  ? 109 ASP A C    1 
ATOM   1704 O  O    . ASP A 1 109 ? -34.04000 38.30600 34.12000 1.000 30.96118  ? 109 ASP A O    1 
ATOM   1705 C  CB   . ASP A 1 109 ? -36.51800 38.65200 35.18700 1.000 32.04921  ? 109 ASP A CB   1 
ATOM   1706 C  CG   . ASP A 1 109 ? -37.85900 39.10300 35.74700 1.000 36.73326  ? 109 ASP A CG   1 
ATOM   1707 O  OD1  . ASP A 1 109 ? -38.14600 40.30800 35.65200 1.000 39.62882  ? 109 ASP A OD1  1 
ATOM   1708 O  OD2  . ASP A 1 109 ? -38.58300 38.27200 36.35000 1.000 36.50150  ? 109 ASP A OD2  1 
ATOM   1709 H  H    . ASP A 1 109 ? -37.90200 39.10800 32.57700 1.000 38.70558  ? 109 ASP A H    1 
ATOM   1710 H  HA   . ASP A 1 109 ? -36.34900 40.04400 33.66700 1.000 33.71558  ? 109 ASP A HA   1 
ATOM   1711 H  HB2  . ASP A 1 109 ? -36.48500 37.68300 35.23900 1.000 34.31558  ? 109 ASP A HB2  1 
ATOM   1712 H  HB3  . ASP A 1 109 ? -35.82100 39.03700 35.74000 1.000 34.31558  ? 109 ASP A HB3  1 
ATOM   1713 N  N    . ASN A 1 110 ? -34.61400 38.74500 31.99500 1.000 36.00228  ? 110 ASN A N    1 
ATOM   1714 C  CA   . ASN A 1 110 ? -33.27300 38.50100 31.46300 1.000 34.24887  ? 110 ASN A CA   1 
ATOM   1715 C  C    . ASN A 1 110 ? -32.71200 37.15000 31.91100 1.000 27.07583  ? 110 ASN A C    1 
ATOM   1716 O  O    . ASN A 1 110 ? -31.52500 37.01900 32.20700 1.000 31.75969  ? 110 ASN A O    1 
ATOM   1717 C  CB   . ASN A 1 110 ? -32.31600 39.63400 31.86600 1.000 37.29986  ? 110 ASN A CB   1 
ATOM   1718 C  CG   . ASN A 1 110 ? -32.81800 41.00500 31.42800 1.000 55.38171  ? 110 ASN A CG   1 
ATOM   1719 O  OD1  . ASN A 1 110 ? -33.47800 41.13600 30.39400 1.000 43.44517  ? 110 ASN A OD1  1 
ATOM   1720 N  ND2  . ASN A 1 110 ? -32.52200 42.02900 32.22300 1.000 46.30682  ? 110 ASN A ND2  1 
ATOM   1721 H  H    . ASN A 1 110 ? -35.19700 38.93800 31.39300 1.000 39.26558  ? 110 ASN A H    1 
ATOM   1722 H  HA   . ASN A 1 110 ? -33.34100 38.47400 30.49600 1.000 37.56558  ? 110 ASN A HA   1 
ATOM   1723 H  HB2  . ASN A 1 110 ? -32.22400 39.64200 32.83200 1.000 40.58558  ? 110 ASN A HB2  1 
ATOM   1724 H  HB3  . ASN A 1 110 ? -31.45300 39.48300 31.45100 1.000 40.58558  ? 110 ASN A HB3  1 
ATOM   1725 H  HD21 . ASN A 1 110 ? -32.78300 42.82200 32.01800 1.000 49.30558  ? 110 ASN A HD21 1 
ATOM   1726 H  HD22 . ASN A 1 110 ? -32.06900 41.89800 32.94200 1.000 49.30558  ? 110 ASN A HD22 1 
ATOM   1727 N  N    . ASN A 1 111 ? -33.55300 36.11300 31.91300 1.000 29.04353  ? 111 ASN A N    1 
ATOM   1728 C  CA   . ASN A 1 111 ? -33.17400 34.83800 32.50000 1.000 27.17991  ? 111 ASN A CA   1 
ATOM   1729 C  C    . ASN A 1 111 ? -32.69200 33.79600 31.48500 1.000 26.89677  ? 111 ASN A C    1 
ATOM   1730 O  O    . ASN A 1 111 ? -32.62800 32.60800 31.82300 1.000 25.32567  ? 111 ASN A O    1 
ATOM   1731 C  CB   . ASN A 1 111 ? -34.33800 34.24400 33.31500 1.000 30.56515  ? 111 ASN A CB   1 
ATOM   1732 C  CG   . ASN A 1 111 ? -35.53000 33.83200 32.44100 1.000 27.95523  ? 111 ASN A CG   1 
ATOM   1733 O  OD1  . ASN A 1 111 ? -35.49700 33.95100 31.20700 1.000 28.33408  ? 111 ASN A OD1  1 
ATOM   1734 N  ND2  . ASN A 1 111 ? -36.57500 33.32100 33.08200 1.000 26.94768  ? 111 ASN A ND2  1 
ATOM   1735 H  H    . ASN A 1 111 ? -34.34600 36.12900 31.57900 1.000 32.82558  ? 111 ASN A H    1 
ATOM   1736 H  HA   . ASN A 1 111 ? -32.43400 35.02400 33.09800 1.000 31.36558  ? 111 ASN A HA   1 
ATOM   1737 H  HB2  . ASN A 1 111 ? -34.02400 33.45600 33.78500 1.000 35.57558  ? 111 ASN A HB2  1 
ATOM   1738 H  HB3  . ASN A 1 111 ? -34.64800 34.90800 33.95100 1.000 35.57558  ? 111 ASN A HB3  1 
ATOM   1739 H  HD21 . ASN A 1 111 ? -37.27100 33.07400 32.64100 1.000 31.13558  ? 111 ASN A HD21 1 
ATOM   1740 H  HD22 . ASN A 1 111 ? -36.55600 33.23900 33.93800 1.000 31.13558  ? 111 ASN A HD22 1 
ATOM   1741 N  N    . SER A 1 112 ? -32.28600 34.19700 30.27100 1.000 27.80553  ? 112 SER A N    1 
ATOM   1742 C  CA   . SER A 1 112 ? -31.89300 33.16500 29.30600 1.000 25.91318  ? 112 SER A CA   1 
ATOM   1743 C  C    . SER A 1 112 ? -30.66600 32.37800 29.76100 1.000 26.20245  ? 112 SER A C    1 
ATOM   1744 O  O    . SER A 1 112 ? -30.56500 31.17800 29.48800 1.000 25.16920  ? 112 SER A O    1 
ATOM   1745 C  CB   . SER A 1 112 ? -31.64800 33.76900 27.91500 1.000 26.62834  ? 112 SER A CB   1 
ATOM   1746 O  OG   . SER A 1 112 ? -30.44500 34.53500 27.86700 1.000 27.38948  ? 112 SER A OG   1 
ATOM   1747 H  H    . SER A 1 112 ? -32.23400 35.01100 29.99800 1.000 32.26558  ? 112 SER A H    1 
ATOM   1748 H  HA   . SER A 1 112 ? -32.63500 32.54400 29.23100 1.000 30.27558  ? 112 SER A HA   1 
ATOM   1749 H  HB2  . SER A 1 112 ? -31.58300 33.04800 27.26900 1.000 30.72558  ? 112 SER A HB2  1 
ATOM   1750 H  HB3  . SER A 1 112 ? -32.39400 34.34800 27.69100 1.000 30.72558  ? 112 SER A HB3  1 
ATOM   1751 H  HG   . SER A 1 112 ? -30.52200 35.15600 27.30600 1.000 31.48558  ? 112 SER A HG   1 
ATOM   1752 N  N    . TYR A 1 113 ? -29.72800 33.00500 30.46800 1.000 26.15688  ? 113 TYR A N    1 
ATOM   1753 C  CA   . TYR A 1 113 ? -28.57800 32.23700 30.95400 1.000 23.30011  ? 113 TYR A CA   1 
ATOM   1754 C  C    . TYR A 1 113 ? -28.99700 31.14400 31.92800 1.000 29.31556  ? 113 TYR A C    1 
ATOM   1755 O  O    . TYR A 1 113 ? -28.39300 30.06200 31.94900 1.000 24.43894  ? 113 TYR A O    1 
ATOM   1756 C  CB   . TYR A 1 113 ? -27.53800 33.18100 31.57800 1.000 24.83849  ? 113 TYR A CB   1 
ATOM   1757 C  CG   . TYR A 1 113 ? -27.79000 33.65300 32.99800 1.000 23.53423  ? 113 TYR A CG   1 
ATOM   1758 C  CD1  . TYR A 1 113 ? -28.65200 34.71400 33.24000 1.000 28.11782  ? 113 TYR A CD1  1 
ATOM   1759 C  CD2  . TYR A 1 113 ? -27.09900 33.10500 34.09000 1.000 24.67088  ? 113 TYR A CD2  1 
ATOM   1760 C  CE1  . TYR A 1 113 ? -28.86900 35.18700 34.53700 1.000 29.73919  ? 113 TYR A CE1  1 
ATOM   1761 C  CE2  . TYR A 1 113 ? -27.31900 33.57400 35.39600 1.000 24.20013  ? 113 TYR A CE2  1 
ATOM   1762 C  CZ   . TYR A 1 113 ? -28.18500 34.62200 35.60000 1.000 27.33707  ? 113 TYR A CZ   1 
ATOM   1763 O  OH   . TYR A 1 113 ? -28.40200 35.11100 36.87800 1.000 28.02956  ? 113 TYR A OH   1 
ATOM   1764 H  H    . TYR A 1 113 ? -29.73100 33.84000 30.67400 1.000 31.01558  ? 113 TYR A H    1 
ATOM   1765 H  HA   . TYR A 1 113 ? -28.15200 31.79800 30.20200 1.000 27.92558  ? 113 TYR A HA   1 
ATOM   1766 H  HB2  . TYR A 1 113 ? -26.68400 32.72200 31.58100 1.000 29.62558  ? 113 TYR A HB2  1 
ATOM   1767 H  HB3  . TYR A 1 113 ? -27.48600 33.97500 31.02300 1.000 29.62558  ? 113 TYR A HB3  1 
ATOM   1768 H  HD1  . TYR A 1 113 ? -29.09200 35.11700 32.52700 1.000 33.09558  ? 113 TYR A HD1  1 
ATOM   1769 H  HD2  . TYR A 1 113 ? -26.48500 32.42100 33.94700 1.000 29.67558  ? 113 TYR A HD2  1 
ATOM   1770 H  HE1  . TYR A 1 113 ? -29.47200 35.87900 34.68600 1.000 34.88558  ? 113 TYR A HE1  1 
ATOM   1771 H  HE2  . TYR A 1 113 ? -26.88200 33.17900 36.11600 1.000 29.02558  ? 113 TYR A HE2  1 
ATOM   1772 H  HH   . TYR A 1 113 ? -27.90800 34.71000 37.42700 1.000 32.97558  ? 113 TYR A HH   1 
ATOM   1773 N  N    . LEU A 1 114 ? -30.03300 31.39100 32.72800 1.000 26.35793  ? 114 LEU A N    1 
ATOM   1774 C  CA   . LEU A 1 114 ? -30.49000 30.37500 33.66400 1.000 23.73297  ? 114 LEU A CA   1 
ATOM   1775 C  C    . LEU A 1 114 ? -31.19000 29.23500 32.93700 1.000 26.94762  ? 114 LEU A C    1 
ATOM   1776 O  O    . LEU A 1 114 ? -31.05900 28.07000 33.32500 1.000 23.90859  ? 114 LEU A O    1 
ATOM   1777 C  CB   . LEU A 1 114 ? -31.41700 31.00200 34.69200 1.000 25.22137  ? 114 LEU A CB   1 
ATOM   1778 C  CG   . LEU A 1 114 ? -30.75400 31.97400 35.66000 1.000 29.36260  ? 114 LEU A CG   1 
ATOM   1779 C  CD1  . LEU A 1 114 ? -31.80700 32.76500 36.42700 1.000 29.14285  ? 114 LEU A CD1  1 
ATOM   1780 C  CD2  . LEU A 1 114 ? -29.82600 31.23400 36.63300 1.000 24.96536  ? 114 LEU A CD2  1 
ATOM   1781 H  H    . LEU A 1 114 ? -30.47900 32.12600 32.74600 1.000 31.93558  ? 114 LEU A H    1 
ATOM   1782 H  HA   . LEU A 1 114 ? -29.72400 30.00700 34.13200 1.000 29.05558  ? 114 LEU A HA   1 
ATOM   1783 H  HB2  . LEU A 1 114 ? -32.11000 31.49000 34.22000 1.000 30.74558  ? 114 LEU A HB2  1 
ATOM   1784 H  HB3  . LEU A 1 114 ? -31.81200 30.29100 35.22000 1.000 30.74558  ? 114 LEU A HB3  1 
ATOM   1785 H  HG   . LEU A 1 114 ? -30.21400 32.59900 35.15100 1.000 35.60558  ? 114 LEU A HG   1 
ATOM   1786 H  HD11 . LEU A 1 114 ? -31.36200 33.37700 37.03400 1.000 35.03558  ? 114 LEU A HD11 1 
ATOM   1787 H  HD12 . LEU A 1 114 ? -32.35100 33.26100 35.79600 1.000 35.03558  ? 114 LEU A HD12 1 
ATOM   1788 H  HD13 . LEU A 1 114 ? -32.36300 32.14800 36.92800 1.000 35.03558  ? 114 LEU A HD13 1 
ATOM   1789 H  HD21 . LEU A 1 114 ? -29.51700 31.85600 37.30900 1.000 30.63558  ? 114 LEU A HD21 1 
ATOM   1790 H  HD22 . LEU A 1 114 ? -30.31900 30.51000 37.05000 1.000 30.63558  ? 114 LEU A HD22 1 
ATOM   1791 H  HD23 . LEU A 1 114 ? -29.07000 30.87800 36.13900 1.000 30.63558  ? 114 LEU A HD23 1 
ATOM   1792 N  N    . ALA A 1 115 ? -31.94800 29.55800 31.88700 1.000 24.10692  ? 115 ALA A N    1 
ATOM   1793 C  CA   . ALA A 1 115 ? -32.60600 28.51700 31.11100 1.000 25.36402  ? 115 ALA A CA   1 
ATOM   1794 C  C    . ALA A 1 115 ? -31.59000 27.52900 30.55400 1.000 23.22479  ? 115 ALA A C    1 
ATOM   1795 O  O    . ALA A 1 115 ? -31.77000 26.31300 30.66100 1.000 24.03472  ? 115 ALA A O    1 
ATOM   1796 C  CB   . ALA A 1 115 ? -33.43400 29.14000 29.98800 1.000 28.12658  ? 115 ALA A CB   1 
ATOM   1797 H  H    . ALA A 1 115 ? -32.09200 30.35900 31.61000 1.000 29.25558  ? 115 ALA A H    1 
ATOM   1798 H  HA   . ALA A 1 115 ? -33.21200 28.03100 31.69100 1.000 30.64558  ? 115 ALA A HA   1 
ATOM   1799 H  HB1  . ALA A 1 115 ? -33.86500 28.43200 29.48500 1.000 33.63558  ? 115 ALA A HB1  1 
ATOM   1800 H  HB2  . ALA A 1 115 ? -34.10300 29.72500 30.37600 1.000 33.63558  ? 115 ALA A HB2  1 
ATOM   1801 H  HB3  . ALA A 1 115 ? -32.84600 29.64800 29.40700 1.000 33.63558  ? 115 ALA A HB3  1 
ATOM   1802 N  N    . THR A 1 116 ? -30.52100 28.02200 29.92600 1.000 25.87690  ? 116 THR A N    1 
ATOM   1803 C  CA   . THR A 1 116 ? -29.61000 27.06000 29.31900 1.000 25.01627  ? 116 THR A CA   1 
ATOM   1804 C  C    . THR A 1 116 ? -28.79300 26.33200 30.38800 1.000 25.93984  ? 116 THR A C    1 
ATOM   1805 O  O    . THR A 1 116 ? -28.48900 25.15000 30.22500 1.000 26.11339  ? 116 THR A O    1 
ATOM   1806 C  CB   . THR A 1 116 ? -28.72600 27.72900 28.25500 1.000 27.90142  ? 116 THR A CB   1 
ATOM   1807 O  OG1  . THR A 1 116 ? -27.88200 26.72400 27.65700 1.000 29.36607  ? 116 THR A OG1  1 
ATOM   1808 C  CG2  . THR A 1 116 ? -27.85200 28.83200 28.81900 1.000 31.61751  ? 116 THR A CG2  1 
ATOM   1809 H  H    . THR A 1 116 ? -30.31700 28.85300 29.84300 1.000 31.21558  ? 116 THR A H    1 
ATOM   1810 H  HA   . THR A 1 116 ? -30.12300 26.38900 28.84100 1.000 30.04558  ? 116 THR A HA   1 
ATOM   1811 H  HB   . THR A 1 116 ? -29.30400 28.14000 27.59400 1.000 33.37558  ? 116 THR A HB   1 
ATOM   1812 H  HG1  . THR A 1 116 ? -27.36600 27.07900 27.09700 1.000 34.88558  ? 116 THR A HG1  1 
ATOM   1813 H  HG21 . THR A 1 116 ? -27.30600 29.21600 28.11600 1.000 38.00558  ? 116 THR A HG21 1 
ATOM   1814 H  HG22 . THR A 1 116 ? -28.40500 29.53000 29.20400 1.000 38.00558  ? 116 THR A HG22 1 
ATOM   1815 H  HG23 . THR A 1 116 ? -27.27000 28.47500 29.50900 1.000 38.00558  ? 116 THR A HG23 1 
ATOM   1816 N  N    . ALA A 1 117 ? -28.49000 26.98400 31.51500 1.000 24.06975  ? 117 ALA A N    1 
ATOM   1817 C  CA   . ALA A 1 117 ? -27.85900 26.26800 32.62800 1.000 24.85316  ? 117 ALA A CA   1 
ATOM   1818 C  C    . ALA A 1 117 ? -28.74000 25.12500 33.13300 1.000 24.34554  ? 117 ALA A C    1 
ATOM   1819 O  O    . ALA A 1 117 ? -28.26300 24.00100 33.36100 1.000 23.79096  ? 117 ALA A O    1 
ATOM   1820 C  CB   . ALA A 1 117 ? -27.54600 27.24600 33.76900 1.000 25.56656  ? 117 ALA A CB   1 
ATOM   1821 H  H    . ALA A 1 117 ? -28.63600 27.82000 31.65800 1.000 29.31558  ? 117 ALA A H    1 
ATOM   1822 H  HA   . ALA A 1 117 ? -27.02500 25.88400 32.31200 1.000 30.33558  ? 117 ALA A HA   1 
ATOM   1823 H  HB1  . ALA A 1 117 ? -27.12300 26.76000 34.49400 1.000 31.45558  ? 117 ALA A HB1  1 
ATOM   1824 H  HB2  . ALA A 1 117 ? -26.94900 27.93500 33.43900 1.000 31.45558  ? 117 ALA A HB2  1 
ATOM   1825 H  HB3  . ALA A 1 117 ? -28.37500 27.64500 34.07800 1.000 31.45558  ? 117 ALA A HB3  1 
ATOM   1826 N  N    . LEU A 1 118 ? -30.02400 25.40300 33.35000 1.000 22.37543  ? 118 LEU A N    1 
ATOM   1827 C  CA   . LEU A 1 118 ? -30.92500 24.37400 33.86200 1.000 24.66951  ? 118 LEU A CA   1 
ATOM   1828 C  C    . LEU A 1 118 ? -31.05800 23.22200 32.87200 1.000 25.10159  ? 118 LEU A C    1 
ATOM   1829 O  O    . LEU A 1 118 ? -31.05900 22.05000 33.26100 1.000 24.24247  ? 118 LEU A O    1 
ATOM   1830 C  CB   . LEU A 1 118 ? -32.29200 24.99700 34.16600 1.000 21.16737  ? 118 LEU A CB   1 
ATOM   1831 C  CG   . LEU A 1 118 ? -33.44100 24.09500 34.56000 1.000 24.77887  ? 118 LEU A CG   1 
ATOM   1832 C  CD1  . LEU A 1 118 ? -33.05900 23.30300 35.80400 1.000 28.28133  ? 118 LEU A CD1  1 
ATOM   1833 C  CD2  . LEU A 1 118 ? -34.71700 24.91100 34.80300 1.000 26.67688  ? 118 LEU A CD2  1 
ATOM   1834 H  H    . LEU A 1 118 ? -30.39300 26.16800 33.21200 1.000 27.32558  ? 118 LEU A H    1 
ATOM   1835 H  HA   . LEU A 1 118 ? -30.56800 24.01300 34.68900 1.000 29.91558  ? 118 LEU A HA   1 
ATOM   1836 H  HB2  . LEU A 1 118 ? -32.17000 25.62100 34.89900 1.000 25.82558  ? 118 LEU A HB2  1 
ATOM   1837 H  HB3  . LEU A 1 118 ? -32.57800 25.47200 33.37000 1.000 25.82558  ? 118 LEU A HB3  1 
ATOM   1838 H  HG   . LEU A 1 118 ? -33.62900 23.47300 33.84000 1.000 29.92558  ? 118 LEU A HG   1 
ATOM   1839 H  HD11 . LEU A 1 118 ? -33.82500 22.78500 36.09600 1.000 34.13558  ? 118 LEU A HD11 1 
ATOM   1840 H  HD12 . LEU A 1 118 ? -32.32100 22.71200 35.58800 1.000 34.13558  ? 118 LEU A HD12 1 
ATOM   1841 H  HD13 . LEU A 1 118 ? -32.79300 23.92200 36.50300 1.000 34.13558  ? 118 LEU A HD13 1 
ATOM   1842 H  HD21 . LEU A 1 118 ? -35.43200 24.30900 35.06300 1.000 32.27558  ? 118 LEU A HD21 1 
ATOM   1843 H  HD22 . LEU A 1 118 ? -34.55200 25.55300 35.51000 1.000 32.27558  ? 118 LEU A HD22 1 
ATOM   1844 H  HD23 . LEU A 1 118 ? -34.95600 25.37400 33.98500 1.000 32.27558  ? 118 LEU A HD23 1 
ATOM   1845 N  N    . LEU A 1 119 ? -31.19300 23.53500 31.58300 1.000 25.22850  ? 119 LEU A N    1 
ATOM   1846 C  CA   . LEU A 1 119 ? -31.29900 22.47600 30.59100 1.000 22.96033  ? 119 LEU A CA   1 
ATOM   1847 C  C    . LEU A 1 119 ? -30.03900 21.63100 30.56800 1.000 23.49686  ? 119 LEU A C    1 
ATOM   1848 O  O    . LEU A 1 119 ? -30.09800 20.40600 30.40800 1.000 27.09578  ? 119 LEU A O    1 
ATOM   1849 C  CB   . LEU A 1 119 ? -31.56300 23.08600 29.20800 1.000 26.45645  ? 119 LEU A CB   1 
ATOM   1850 C  CG   . LEU A 1 119 ? -32.92700 23.76800 29.07600 1.000 25.73434  ? 119 LEU A CG   1 
ATOM   1851 C  CD1  . LEU A 1 119 ? -32.93500 24.73200 27.86800 1.000 27.16738  ? 119 LEU A CD1  1 
ATOM   1852 C  CD2  . LEU A 1 119 ? -34.00500 22.72300 28.91100 1.000 27.38821  ? 119 LEU A CD2  1 
ATOM   1853 H  H    . LEU A 1 119 ? -31.22500 24.33400 31.26800 1.000 29.93558  ? 119 LEU A H    1 
ATOM   1854 H  HA   . LEU A 1 119 ? -32.04700 21.90100 30.81400 1.000 26.63558  ? 119 LEU A HA   1 
ATOM   1855 H  HB2  . LEU A 1 119 ? -30.88100 23.75200 29.02800 1.000 30.72558  ? 119 LEU A HB2  1 
ATOM   1856 H  HB3  . LEU A 1 119 ? -31.52000 22.38000 28.54500 1.000 30.72558  ? 119 LEU A HB3  1 
ATOM   1857 H  HG   . LEU A 1 119 ? -33.10800 24.28500 29.87600 1.000 29.96558  ? 119 LEU A HG   1 
ATOM   1858 H  HD11 . LEU A 1 119 ? -33.80700 25.15100 27.80400 1.000 31.65558  ? 119 LEU A HD11 1 
ATOM   1859 H  HD12 . LEU A 1 119 ? -32.25200 25.40900 28.00000 1.000 31.65558  ? 119 LEU A HD12 1 
ATOM   1860 H  HD13 . LEU A 1 119 ? -32.75000 24.22800 27.06100 1.000 31.65558  ? 119 LEU A HD13 1 
ATOM   1861 H  HD21 . LEU A 1 119 ? -34.86000 23.16600 28.79500 1.000 31.44558  ? 119 LEU A HD21 1 
ATOM   1862 H  HD22 . LEU A 1 119 ? -33.80400 22.18200 28.13100 1.000 31.44558  ? 119 LEU A HD22 1 
ATOM   1863 H  HD23 . LEU A 1 119 ? -34.02700 22.16400 29.70400 1.000 31.44558  ? 119 LEU A HD23 1 
ATOM   1864 N  N    . THR A 1 120 ? -28.88500 22.27800 30.70700 1.000 23.70201  ? 120 THR A N    1 
ATOM   1865 C  CA   . THR A 1 120 ? -27.62000 21.55700 30.68600 1.000 25.61721  ? 120 THR A CA   1 
ATOM   1866 C  C    . THR A 1 120 ? -27.53300 20.57500 31.84100 1.000 24.55589  ? 120 THR A C    1 
ATOM   1867 O  O    . THR A 1 120 ? -27.10200 19.43000 31.66200 1.000 26.42974  ? 120 THR A O    1 
ATOM   1868 C  CB   . THR A 1 120 ? -26.46500 22.55700 30.73000 1.000 25.94743  ? 120 THR A CB   1 
ATOM   1869 O  OG1  . THR A 1 120 ? -26.47000 23.36000 29.54300 1.000 27.89970  ? 120 THR A OG1  1 
ATOM   1870 C  CG2  . THR A 1 120 ? -25.13600 21.83400 30.83800 1.000 28.73241  ? 120 THR A CG2  1 
ATOM   1871 H  H    . THR A 1 120 ? -28.80800 23.12700 30.81300 1.000 27.48558  ? 120 THR A H    1 
ATOM   1872 H  HA   . THR A 1 120 ? -27.54900 21.04900 29.86300 1.000 29.40558  ? 120 THR A HA   1 
ATOM   1873 H  HB   . THR A 1 120 ? -26.56900 23.12900 31.50700 1.000 30.18558  ? 120 THR A HB   1 
ATOM   1874 H  HG1  . THR A 1 120 ? -27.19300 23.78300 29.48500 1.000 32.60558  ? 120 THR A HG1  1 
ATOM   1875 H  HG21 . THR A 1 120 ? -24.40600 22.46400 30.72700 1.000 33.10558  ? 120 THR A HG21 1 
ATOM   1876 H  HG22 . THR A 1 120 ? -25.05800 21.41100 31.70700 1.000 33.10558  ? 120 THR A HG22 1 
ATOM   1877 H  HG23 . THR A 1 120 ? -25.07200 21.15400 30.14900 1.000 33.10558  ? 120 THR A HG23 1 
ATOM   1878 N  N    . LEU A 1 121 ? -27.95000 20.99700 33.03800 1.000 24.29740  ? 121 LEU A N    1 
ATOM   1879 C  CA   . LEU A 1 121 ? -27.83800 20.12800 34.20100 1.000 26.49127  ? 121 LEU A CA   1 
ATOM   1880 C  C    . LEU A 1 121 ? -28.60000 18.83300 34.00900 1.000 29.05183  ? 121 LEU A C    1 
ATOM   1881 O  O    . LEU A 1 121 ? -28.17000 17.78200 34.48400 1.000 28.52297  ? 121 LEU A O    1 
ATOM   1882 C  CB   . LEU A 1 121 ? -28.36600 20.83100 35.44100 1.000 24.40253  ? 121 LEU A CB   1 
ATOM   1883 C  CG   . LEU A 1 121 ? -27.49700 21.95900 35.99500 1.000 27.18016  ? 121 LEU A CG   1 
ATOM   1884 C  CD1  . LEU A 1 121 ? -28.29000 22.72800 37.02700 1.000 26.83802  ? 121 LEU A CD1  1 
ATOM   1885 C  CD2  . LEU A 1 121 ? -26.20000 21.40000 36.61800 1.000 27.13043  ? 121 LEU A CD2  1 
ATOM   1886 H  H    . LEU A 1 121 ? -28.29400 21.76900 33.19700 1.000 28.03558  ? 121 LEU A H    1 
ATOM   1887 H  HA   . LEU A 1 121 ? -26.89700 19.92500 34.32700 1.000 30.41558  ? 121 LEU A HA   1 
ATOM   1888 H  HB2  . LEU A 1 121 ? -29.23100 21.21500 35.22500 1.000 28.51558  ? 121 LEU A HB2  1 
ATOM   1889 H  HB3  . LEU A 1 121 ? -28.46300 20.17100 36.14500 1.000 28.51558  ? 121 LEU A HB3  1 
ATOM   1890 H  HG   . LEU A 1 121 ? -27.23800 22.55600 35.27600 1.000 32.37558  ? 121 LEU A HG   1 
ATOM   1891 H  HD11 . LEU A 1 121 ? -27.73600 23.44000 37.38400 1.000 32.42558  ? 121 LEU A HD11 1 
ATOM   1892 H  HD12 . LEU A 1 121 ? -29.07800 23.10300 36.60400 1.000 32.42558  ? 121 LEU A HD12 1 
ATOM   1893 H  HD13 . LEU A 1 121 ? -28.55200 22.12400 37.73900 1.000 32.42558  ? 121 LEU A HD13 1 
ATOM   1894 H  HD21 . LEU A 1 121 ? -25.71300 22.12600 37.03800 1.000 32.04558  ? 121 LEU A HD21 1 
ATOM   1895 H  HD22 . LEU A 1 121 ? -26.43100 20.72900 37.28000 1.000 32.04558  ? 121 LEU A HD22 1 
ATOM   1896 H  HD23 . LEU A 1 121 ? -25.66000 21.00100 35.91800 1.000 32.04558  ? 121 LEU A HD23 1 
ATOM   1897 N  N    . GLN A 1 122 ? -29.76000 18.89700 33.36100 1.000 28.00326  ? 122 GLN A N    1 
ATOM   1898 C  CA   . GLN A 1 122 ? -30.55400 17.70300 33.10100 1.000 27.40184  ? 122 GLN A CA   1 
ATOM   1899 C  C    . GLN A 1 122 ? -29.93500 16.77500 32.06200 1.000 31.78507  ? 122 GLN A C    1 
ATOM   1900 O  O    . GLN A 1 122 ? -30.51800 15.72000 31.79400 1.000 33.12146  ? 122 GLN A O    1 
ATOM   1901 C  CB   . GLN A 1 122 ? -31.95200 18.13900 32.67100 1.000 27.05802  ? 122 GLN A CB   1 
ATOM   1902 C  CG   . GLN A 1 122 ? -32.67600 18.89500 33.78100 1.000 27.71570  ? 122 GLN A CG   1 
ATOM   1903 C  CD   . GLN A 1 122 ? -33.92100 19.59200 33.27900 1.000 25.72351  ? 122 GLN A CD   1 
ATOM   1904 O  OE1  . GLN A 1 122 ? -34.98200 18.97900 33.16400 1.000 28.45365  ? 122 GLN A OE1  1 
ATOM   1905 N  NE2  . GLN A 1 122 ? -33.79200 20.86800 32.95400 1.000 24.99215  ? 122 GLN A NE2  1 
ATOM   1906 H  H    . GLN A 1 122 ? -30.11000 19.62300 33.06100 1.000 31.43558  ? 122 GLN A H    1 
ATOM   1907 H  HA   . GLN A 1 122 ? -30.62900 17.18100 33.91500 1.000 29.88558  ? 122 GLN A HA   1 
ATOM   1908 H  HB2  . GLN A 1 122 ? -31.88200 18.72300 31.90000 1.000 29.67558  ? 122 GLN A HB2  1 
ATOM   1909 H  HB3  . GLN A 1 122 ? -32.47600 17.35400 32.44600 1.000 29.67558  ? 122 GLN A HB3  1 
ATOM   1910 H  HG2  . GLN A 1 122 ? -32.93800 18.26900 34.47400 1.000 31.15558  ? 122 GLN A HG2  1 
ATOM   1911 H  HG3  . GLN A 1 122 ? -32.08000 19.56600 34.14900 1.000 31.15558  ? 122 GLN A HG3  1 
ATOM   1912 H  HE21 . GLN A 1 122 ? -33.03000 21.25700 33.03400 1.000 28.71558  ? 122 GLN A HE21 1 
ATOM   1913 H  HE22 . GLN A 1 122 ? -34.47200 21.30800 32.66400 1.000 28.71558  ? 122 GLN A HE22 1 
ATOM   1914 N  N    . GLN A 1 123 ? -28.77800 17.11200 31.49300 1.000 27.73188  ? 123 GLN A N    1 
ATOM   1915 C  CA   . GLN A 1 123 ? -28.13200 16.25600 30.50500 1.000 30.51989  ? 123 GLN A CA   1 
ATOM   1916 C  C    . GLN A 1 123 ? -26.73800 15.78900 30.90200 1.000 33.53647  ? 123 GLN A C    1 
ATOM   1917 O  O    . GLN A 1 123 ? -26.10200 15.07200 30.12300 1.000 33.62796  ? 123 GLN A O    1 
ATOM   1918 C  CB   . GLN A 1 123 ? -28.04500 16.97900 29.15700 1.000 30.90109  ? 123 GLN A CB   1 
ATOM   1919 C  CG   . GLN A 1 123 ? -29.40600 17.38000 28.61900 1.000 31.22384  ? 123 GLN A CG   1 
ATOM   1920 C  CD   . GLN A 1 123 ? -29.30300 18.24100 27.39700 1.000 33.79200  ? 123 GLN A CD   1 
ATOM   1921 O  OE1  . GLN A 1 123 ? -28.86300 17.78600 26.32700 1.000 32.11536  ? 123 GLN A OE1  1 
ATOM   1922 N  NE2  . GLN A 1 123 ? -29.69500 19.50200 27.53800 1.000 31.44346  ? 123 GLN A NE2  1 
ATOM   1923 H  H    . GLN A 1 123 ? -28.34700 17.83600 31.66500 1.000 29.40558  ? 123 GLN A H    1 
ATOM   1924 H  HA   . GLN A 1 123 ? -28.68300 15.46400 30.39800 1.000 31.75558  ? 123 GLN A HA   1 
ATOM   1925 H  HB2  . GLN A 1 123 ? -27.51500 17.78400 29.26400 1.000 32.43558  ? 123 GLN A HB2  1 
ATOM   1926 H  HB3  . GLN A 1 123 ? -27.62700 16.39000 28.50900 1.000 32.43558  ? 123 GLN A HB3  1 
ATOM   1927 H  HG2  . GLN A 1 123 ? -29.90300 16.58100 28.38400 1.000 33.05558  ? 123 GLN A HG2  1 
ATOM   1928 H  HG3  . GLN A 1 123 ? -29.88300 17.87900 29.30000 1.000 33.05558  ? 123 GLN A HG3  1 
ATOM   1929 H  HE21 . GLN A 1 123 ? -29.98700 19.77900 28.29900 1.000 34.51558  ? 123 GLN A HE21 1 
ATOM   1930 H  HE22 . GLN A 1 123 ? -29.65800 20.04100 26.87000 1.000 34.51558  ? 123 GLN A HE22 1 
ATOM   1931 N  N    . ILE A 1 124 ? -26.24500 16.16800 32.08100 1.000 31.28465  ? 124 ILE A N    1 
ATOM   1932 C  CA   . ILE A 1 124 ? -24.94000 15.72800 32.55400 1.000 33.80466  ? 124 ILE A CA   1 
ATOM   1933 C  C    . ILE A 1 124 ? -25.09700 15.08400 33.92300 1.000 38.43038  ? 124 ILE A C    1 
ATOM   1934 O  O    . ILE A 1 124 ? -26.02900 15.38200 34.67000 1.000 33.04128  ? 124 ILE A O    1 
ATOM   1935 C  CB   . ILE A 1 124 ? -23.92300 16.89200 32.60500 1.000 30.53177  ? 124 ILE A CB   1 
ATOM   1936 C  CG1  . ILE A 1 124 ? -24.37900 17.98500 33.57500 1.000 31.53003  ? 124 ILE A CG1  1 
ATOM   1937 C  CG2  . ILE A 1 124 ? -23.74600 17.47200 31.21200 1.000 33.83112  ? 124 ILE A CG2  1 
ATOM   1938 C  CD1  . ILE A 1 124 ? -23.35300 19.14200 33.73200 1.000 34.12777  ? 124 ILE A CD1  1 
ATOM   1939 H  H    . ILE A 1 124 ? -26.65700 16.68600 32.63000 1.000 32.80558  ? 124 ILE A H    1 
ATOM   1940 H  HA   . ILE A 1 124 ? -24.59500 15.05400 31.94800 1.000 35.37558  ? 124 ILE A HA   1 
ATOM   1941 H  HB   . ILE A 1 124 ? -23.07600 16.54300 32.92500 1.000 32.27558  ? 124 ILE A HB   1 
ATOM   1942 H  HG12 . ILE A 1 124 ? -25.20900 18.36600 33.25000 1.000 34.58558  ? 124 ILE A HG12 1 
ATOM   1943 H  HG13 . ILE A 1 124 ? -24.51600 17.59000 34.45000 1.000 34.58558  ? 124 ILE A HG13 1 
ATOM   1944 H  HG21 . ILE A 1 124 ? -22.99800 18.09000 31.22000 1.000 36.35558  ? 124 ILE A HG21 1 
ATOM   1945 H  HG22 . ILE A 1 124 ? -23.57000 16.74900 30.58900 1.000 36.35558  ? 124 ILE A HG22 1 
ATOM   1946 H  HG23 . ILE A 1 124 ? -24.55800 17.93700 30.95800 1.000 36.35558  ? 124 ILE A HG23 1 
ATOM   1947 H  HD11 . ILE A 1 124 ? -23.65300 19.73700 34.43700 1.000 38.35558  ? 124 ILE A HD11 1 
ATOM   1948 H  HD12 . ILE A 1 124 ? -22.48800 18.76800 33.96000 1.000 38.35558  ? 124 ILE A HD12 1 
ATOM   1949 H  HD13 . ILE A 1 124 ? -23.29300 19.62600 32.89300 1.000 38.35558  ? 124 ILE A HD13 1 
ATOM   1950 N  N    . GLU A 1 125 ? -24.18600 14.17300 34.23800 1.000 32.32953  ? 125 GLU A N    1 
ATOM   1951 C  CA   . GLU A 1 125 ? -24.19600 13.48400 35.52100 1.000 31.62952  ? 125 GLU A CA   1 
ATOM   1952 C  C    . GLU A 1 125 ? -23.57200 14.38600 36.57800 1.000 33.55418  ? 125 GLU A C    1 
ATOM   1953 O  O    . GLU A 1 125 ? -22.35800 14.61200 36.57200 1.000 35.08912  ? 125 GLU A O    1 
ATOM   1954 C  CB   . GLU A 1 125 ? -23.44700 12.15700 35.41000 1.000 40.33373  ? 125 GLU A CB   1 
ATOM   1955 C  CG   . GLU A 1 125 ? -23.61700 11.27000 36.64000 1.000 46.96865  ? 125 GLU A CG   1 
ATOM   1956 C  CD   . GLU A 1 125 ? -22.64500 10.10100 36.66900 1.000 66.57186  ? 125 GLU A CD   1 
ATOM   1957 O  OE1  . GLU A 1 125 ? -22.44800 9.45700  35.61800 1.000 61.87235  ? 125 GLU A OE1  1 
ATOM   1958 O  OE2  . GLU A 1 125 ? -22.07700 9.83500  37.74800 1.000 83.82071  ? 125 GLU A OE2  1 
ATOM   1959 H  H    . GLU A 1 125 ? -23.54300 13.93400 33.72000 1.000 32.38558  ? 125 GLU A H    1 
ATOM   1960 H  HA   . GLU A 1 125 ? -25.11200 13.29900 35.78200 1.000 31.11558  ? 125 GLU A HA   1 
ATOM   1961 H  HB2  . GLU A 1 125 ? -23.78100 11.67000 34.64100 1.000 39.97558  ? 125 GLU A HB2  1 
ATOM   1962 H  HB3  . GLU A 1 125 ? -22.50000 12.33900 35.30100 1.000 39.97558  ? 125 GLU A HB3  1 
ATOM   1963 H  HG2  . GLU A 1 125 ? -23.46700 11.80400 37.43600 1.000 47.20558  ? 125 GLU A HG2  1 
ATOM   1964 H  HG3  . GLU A 1 125 ? -24.51800 10.91000 36.64600 1.000 47.20558  ? 125 GLU A HG3  1 
ATOM   1965 N  N    . LEU A 1 126 ? -24.39500 14.88000 37.50300 1.000 31.75245  ? 126 LEU A N    1 
ATOM   1966 C  CA   . LEU A 1 126 ? -23.94400 15.82700 38.51500 1.000 29.88901  ? 126 LEU A CA   1 
ATOM   1967 C  C    . LEU A 1 126 ? -24.81900 15.69000 39.75000 1.000 35.77146  ? 126 LEU A C    1 
ATOM   1968 O  O    . LEU A 1 126 ? -26.04700 15.75000 39.64300 1.000 36.52845  ? 126 LEU A O    1 
ATOM   1969 C  CB   . LEU A 1 126 ? -24.01300 17.27500 38.00200 1.000 33.57885  ? 126 LEU A CB   1 
ATOM   1970 C  CG   . LEU A 1 126 ? -23.26400 18.27500 38.87700 1.000 35.12599  ? 126 LEU A CG   1 
ATOM   1971 C  CD1  . LEU A 1 126 ? -21.76200 18.14800 38.65500 1.000 37.82739  ? 126 LEU A CD1  1 
ATOM   1972 C  CD2  . LEU A 1 126 ? -23.70300 19.68900 38.61500 1.000 31.56468  ? 126 LEU A CD2  1 
ATOM   1973 H  H    . LEU A 1 126 ? -25.22900 14.67800 37.56300 1.000 33.00558  ? 126 LEU A H    1 
ATOM   1974 H  HA   . LEU A 1 126 ? -23.02700 15.62000 38.75200 1.000 31.63558  ? 126 LEU A HA   1 
ATOM   1975 H  HB2  . LEU A 1 126 ? -23.62500 17.30800 37.11400 1.000 37.16558  ? 126 LEU A HB2  1 
ATOM   1976 H  HB3  . LEU A 1 126 ? -24.94300 17.54800 37.96700 1.000 37.16558  ? 126 LEU A HB3  1 
ATOM   1977 H  HG   . LEU A 1 126 ? -23.46800 18.07400 39.80400 1.000 39.67558  ? 126 LEU A HG   1 
ATOM   1978 H  HD11 . LEU A 1 126 ? -21.30800 18.82900 39.17500 1.000 42.48558  ? 126 LEU A HD11 1 
ATOM   1979 H  HD12 . LEU A 1 126 ? -21.47400 17.26700 38.94000 1.000 42.48558  ? 126 LEU A HD12 1 
ATOM   1980 H  HD13 . LEU A 1 126 ? -21.57100 18.27000 37.71100 1.000 42.48558  ? 126 LEU A HD13 1 
ATOM   1981 H  HD21 . LEU A 1 126 ? -23.19400 20.28800 39.18300 1.000 36.34558  ? 126 LEU A HD21 1 
ATOM   1982 H  HD22 . LEU A 1 126 ? -23.54300 19.90200 37.68200 1.000 36.34558  ? 126 LEU A HD22 1 
ATOM   1983 H  HD23 . LEU A 1 126 ? -24.64900 19.76800 38.81400 1.000 36.34558  ? 126 LEU A HD23 1 
ATOM   1984 N  N    . LYS A 1 127 ? -24.18600 15.56200 40.91400 1.000 31.45832  ? 127 LYS A N    1 
ATOM   1985 C  CA   . LYS A 1 127 ? -24.87600 15.46400 42.19400 1.000 32.17354  ? 127 LYS A CA   1 
ATOM   1986 C  C    . LYS A 1 127 ? -24.47200 16.64600 43.06400 1.000 31.41575  ? 127 LYS A C    1 
ATOM   1987 O  O    . LYS A 1 127 ? -23.28100 16.93000 43.21400 1.000 32.58164  ? 127 LYS A O    1 
ATOM   1988 C  CB   . LYS A 1 127 ? -24.53500 14.13600 42.88100 1.000 35.45384  ? 127 LYS A CB   1 
ATOM   1989 C  CG   . LYS A 1 127 ? -24.98200 14.00600 44.33200 1.000 54.18339  ? 127 LYS A CG   1 
ATOM   1990 C  CD   . LYS A 1 127 ? -26.33800 13.31300 44.45200 1.000 90.72046  ? 127 LYS A CD   1 
ATOM   1991 C  CE   . LYS A 1 127 ? -27.20500 13.90400 45.57400 1.000 78.25968  ? 127 LYS A CE   1 
ATOM   1992 N  NZ   . LYS A 1 127 ? -28.65600 13.95000 45.20700 1.000 53.02889  ? 127 LYS A NZ   1 
ATOM   1993 H  H    . LYS A 1 127 ? -23.33000 15.52900 40.98800 1.000 33.61558  ? 127 LYS A H    1 
ATOM   1994 H  HA   . LYS A 1 127 ? -25.83700 15.50200 42.06600 1.000 34.62558  ? 127 LYS A HA   1 
ATOM   1995 H  HB2  . LYS A 1 127 ? -24.96000 13.41900 42.38500 1.000 37.38558  ? 127 LYS A HB2  1 
ATOM   1996 H  HB3  . LYS A 1 127 ? -23.57200 14.02500 42.86600 1.000 37.38558  ? 127 LYS A HB3  1 
ATOM   1997 H  HG2  . LYS A 1 127 ? -24.32900 13.48200 44.82200 1.000 59.92558  ? 127 LYS A HG2  1 
ATOM   1998 H  HG3  . LYS A 1 127 ? -25.05800 14.89100 44.72300 1.000 59.92558  ? 127 LYS A HG3  1 
ATOM   1999 H  HD2  . LYS A 1 127 ? -26.82000 13.41100 43.61600 1.000 103.38558 ? 127 LYS A HD2  1 
ATOM   2000 H  HD3  . LYS A 1 127 ? -26.19800 12.37200 44.64600 1.000 103.38558 ? 127 LYS A HD3  1 
ATOM   2001 H  HE2  . LYS A 1 127 ? -27.11300 13.35800 46.37000 1.000 89.16558  ? 127 LYS A HE2  1 
ATOM   2002 H  HE3  . LYS A 1 127 ? -26.91200 14.81100 45.75800 1.000 89.16558  ? 127 LYS A HE3  1 
ATOM   2003 H  HZ1  . LYS A 1 127 ? -29.12900 14.29800 45.87600 1.000 59.10558  ? 127 LYS A HZ1  1 
ATOM   2004 H  HZ2  . LYS A 1 127 ? -28.77100 14.45100 44.48000 1.000 59.10558  ? 127 LYS A HZ2  1 
ATOM   2005 H  HZ3  . LYS A 1 127 ? -28.95400 13.12800 45.04000 1.000 59.10558  ? 127 LYS A HZ3  1 
ATOM   2006 N  N    . PHE A 1 128 ? -25.46100 17.33300 43.63000 1.000 27.86991  ? 128 PHE A N    1 
ATOM   2007 C  CA   . PHE A 1 128 ? -25.19800 18.51100 44.44200 1.000 26.61170  ? 128 PHE A CA   1 
ATOM   2008 C  C    . PHE A 1 128 ? -24.92300 18.11000 45.87700 1.000 27.58088  ? 128 PHE A C    1 
ATOM   2009 O  O    . PHE A 1 128 ? -25.37800 17.06800 46.35200 1.000 30.27786  ? 128 PHE A O    1 
ATOM   2010 C  CB   . PHE A 1 128 ? -26.38000 19.48000 44.40700 1.000 24.91962  ? 128 PHE A CB   1 
ATOM   2011 C  CG   . PHE A 1 128 ? -26.51500 20.19200 43.09900 1.000 25.78478  ? 128 PHE A CG   1 
ATOM   2012 C  CD1  . PHE A 1 128 ? -25.55600 21.10700 42.69200 1.000 26.15342  ? 128 PHE A CD1  1 
ATOM   2013 C  CD2  . PHE A 1 128 ? -27.58500 19.92600 42.26900 1.000 25.43329  ? 128 PHE A CD2  1 
ATOM   2014 C  CE1  . PHE A 1 128 ? -25.67100 21.75400 41.44800 1.000 27.45715  ? 128 PHE A CE1  1 
ATOM   2015 C  CE2  . PHE A 1 128 ? -27.71200 20.58300 41.03700 1.000 28.11323  ? 128 PHE A CE2  1 
ATOM   2016 C  CZ   . PHE A 1 128 ? -26.74200 21.49100 40.64200 1.000 27.24246  ? 128 PHE A CZ   1 
ATOM   2017 H  H    . PHE A 1 128 ? -26.29500 17.13400 43.55800 1.000 31.05558  ? 128 PHE A H    1 
ATOM   2018 H  HA   . PHE A 1 128 ? -24.42000 18.96900 44.08600 1.000 30.27558  ? 128 PHE A HA   1 
ATOM   2019 H  HB2  . PHE A 1 128 ? -27.19900 18.98300 44.56300 1.000 28.96558  ? 128 PHE A HB2  1 
ATOM   2020 H  HB3  . PHE A 1 128 ? -26.26100 20.14700 45.10100 1.000 28.96558  ? 128 PHE A HB3  1 
ATOM   2021 H  HD1  . PHE A 1 128 ? -24.83200 21.29400 43.24500 1.000 31.08558  ? 128 PHE A HD1  1 
ATOM   2022 H  HD2  . PHE A 1 128 ? -28.22800 19.30600 42.53000 1.000 29.88558  ? 128 PHE A HD2  1 
ATOM   2023 H  HE1  . PHE A 1 128 ? -25.02000 22.35900 41.17500 1.000 32.90558  ? 128 PHE A HE1  1 
ATOM   2024 H  HE2  . PHE A 1 128 ? -28.44300 20.41200 40.48900 1.000 33.36558  ? 128 PHE A HE2  1 
ATOM   2025 H  HZ   . PHE A 1 128 ? -26.82000 21.92400 39.82200 1.000 32.61558  ? 128 PHE A HZ   1 
ATOM   2026 N  N    . ASN A 1 129 ? -24.18400 18.97900 46.57900 1.000 25.86835  ? 129 ASN A N    1 
ATOM   2027 C  CA   . ASN A 1 129 ? -23.79000 18.70200 47.94600 1.000 26.88079  ? 129 ASN A CA   1 
ATOM   2028 C  C    . ASN A 1 129 ? -24.75900 19.31700 48.95200 1.000 27.57061  ? 129 ASN A C    1 
ATOM   2029 O  O    . ASN A 1 129 ? -25.24300 18.60500 49.83600 1.000 29.56554  ? 129 ASN A O    1 
ATOM   2030 C  CB   . ASN A 1 129 ? -22.36200 19.19400 48.18200 1.000 33.01189  ? 129 ASN A CB   1 
ATOM   2031 C  CG   . ASN A 1 129 ? -21.30900 18.23300 47.63900 1.000 50.50257  ? 129 ASN A CG   1 
ATOM   2032 O  OD1  . ASN A 1 129 ? -21.50100 17.01100 47.61100 1.000 43.46780  ? 129 ASN A OD1  1 
ATOM   2033 N  ND2  . ASN A 1 129 ? -20.17500 18.78100 47.24000 1.000 45.90978  ? 129 ASN A ND2  1 
ATOM   2034 H  H    . ASN A 1 129 ? -23.90300 19.73400 46.27700 1.000 29.45558  ? 129 ASN A H    1 
ATOM   2035 H  HA   . ASN A 1 129 ? -23.82100 17.74300 48.09400 1.000 30.38558  ? 129 ASN A HA   1 
ATOM   2036 H  HB2  . ASN A 1 129 ? -22.24500 20.04900 47.73900 1.000 37.69558  ? 129 ASN A HB2  1 
ATOM   2037 H  HB3  . ASN A 1 129 ? -22.21500 19.29200 49.13600 1.000 37.69558  ? 129 ASN A HB3  1 
ATOM   2038 H  HD21 . ASN A 1 129 ? -20.06500 19.63300 47.29500 1.000 52.41558  ? 129 ASN A HD21 1 
ATOM   2039 H  HD22 . ASN A 1 129 ? -19.54600 18.28700 46.92500 1.000 52.41558  ? 129 ASN A HD22 1 
ATOM   2040 N  N    . PRO A 1 130 ? -25.07600 20.60700 48.87700 1.000 27.19362  ? 130 PRO A N    1 
ATOM   2041 C  CA   . PRO A 1 130 ? -26.01600 21.19400 49.85800 1.000 25.91611  ? 130 PRO A CA   1 
ATOM   2042 C  C    . PRO A 1 130 ? -27.38300 20.55700 49.73200 1.000 25.70137  ? 130 PRO A C    1 
ATOM   2043 O  O    . PRO A 1 130 ? -27.93100 20.47200 48.62200 1.000 24.13235  ? 130 PRO A O    1 
ATOM   2044 C  CB   . PRO A 1 130 ? -26.07000 22.68100 49.46200 1.000 26.42052  ? 130 PRO A CB   1 
ATOM   2045 C  CG   . PRO A 1 130 ? -24.85900 22.90800 48.63800 1.000 29.25004  ? 130 PRO A CG   1 
ATOM   2046 C  CD   . PRO A 1 130 ? -24.66100 21.61300 47.88500 1.000 26.82332  ? 130 PRO A CD   1 
ATOM   2047 H  HA   . PRO A 1 130 ? -25.67700 21.10100 50.76200 1.000 30.64558  ? 130 PRO A HA   1 
ATOM   2048 H  HB2  . PRO A 1 130 ? -26.87600 22.85600 48.95100 1.000 31.75558  ? 130 PRO A HB2  1 
ATOM   2049 H  HB3  . PRO A 1 130 ? -26.05600 23.23400 50.25900 1.000 31.75558  ? 130 PRO A HB3  1 
ATOM   2050 H  HG2  . PRO A 1 130 ? -25.00800 23.64700 48.02700 1.000 35.12558  ? 130 PRO A HG2  1 
ATOM   2051 H  HG3  . PRO A 1 130 ? -24.09900 23.09800 49.21000 1.000 35.12558  ? 130 PRO A HG3  1 
ATOM   2052 H  HD2  . PRO A 1 130 ? -25.22300 21.57800 47.09600 1.000 31.83558  ? 130 PRO A HD2  1 
ATOM   2053 H  HD3  . PRO A 1 130 ? -23.73100 21.49400 47.63500 1.000 31.83558  ? 130 PRO A HD3  1 
ATOM   2054 N  N    . PRO A 1 131 ? -27.97600 20.11700 50.84100 1.000 24.86320  ? 131 PRO A N    1 
ATOM   2055 C  CA   . PRO A 1 131 ? -29.36400 19.61600 50.78000 1.000 25.90100  ? 131 PRO A CA   1 
ATOM   2056 C  C    . PRO A 1 131 ? -30.32500 20.56700 50.08700 1.000 24.37323  ? 131 PRO A C    1 
ATOM   2057 O  O    . PRO A 1 131 ? -31.25000 20.11800 49.40200 1.000 25.31188  ? 131 PRO A O    1 
ATOM   2058 C  CB   . PRO A 1 131 ? -29.72200 19.41500 52.26200 1.000 26.62826  ? 131 PRO A CB   1 
ATOM   2059 C  CG   . PRO A 1 131 ? -28.41300 19.10300 52.90700 1.000 28.12569  ? 131 PRO A CG   1 
ATOM   2060 C  CD   . PRO A 1 131 ? -27.38200 19.95100 52.18000 1.000 27.64965  ? 131 PRO A CD   1 
ATOM   2061 H  HA   . PRO A 1 131 ? -29.38400 18.75900 50.32600 1.000 30.25558  ? 131 PRO A HA   1 
ATOM   2062 H  HB2  . PRO A 1 131 ? -30.10800 20.22700 52.62600 1.000 30.91558  ? 131 PRO A HB2  1 
ATOM   2063 H  HB3  . PRO A 1 131 ? -30.34500 18.67800 52.35900 1.000 30.91558  ? 131 PRO A HB3  1 
ATOM   2064 H  HG2  . PRO A 1 131 ? -28.44800 19.33600 53.84800 1.000 32.37558  ? 131 PRO A HG2  1 
ATOM   2065 H  HG3  . PRO A 1 131 ? -28.21500 18.15900 52.80600 1.000 32.37558  ? 131 PRO A HG3  1 
ATOM   2066 H  HD2  . PRO A 1 131 ? -27.26800 20.80900 52.61700 1.000 32.15558  ? 131 PRO A HD2  1 
ATOM   2067 H  HD3  . PRO A 1 131 ? -26.53000 19.49000 52.12600 1.000 32.15558  ? 131 PRO A HD3  1 
ATOM   2068 N  N    . ALA A 1 132 ? -30.13400 21.87900 50.24300 1.000 23.26278  ? 132 ALA A N    1 
ATOM   2069 C  CA   . ALA A 1 132 ? -31.02600 22.83300 49.59200 1.000 22.26782  ? 132 ALA A CA   1 
ATOM   2070 C  C    . ALA A 1 132 ? -31.04000 22.63100 48.08100 1.000 23.98025  ? 132 ALA A C    1 
ATOM   2071 O  O    . ALA A 1 132 ? -32.10200 22.67900 47.45000 1.000 23.49175  ? 132 ALA A O    1 
ATOM   2072 C  CB   . ALA A 1 132 ? -30.59700 24.26000 49.91100 1.000 23.78509  ? 132 ALA A CB   1 
ATOM   2073 H  H    . ALA A 1 132 ? -29.50700 22.23400 50.71200 1.000 28.01558  ? 132 ALA A H    1 
ATOM   2074 H  HA   . ALA A 1 132 ? -31.92300 22.69500 49.93600 1.000 27.14558  ? 132 ALA A HA   1 
ATOM   2075 H  HB1  . ALA A 1 132 ? -31.23000 24.87700 49.51000 1.000 29.18558  ? 132 ALA A HB1  1 
ATOM   2076 H  HB2  . ALA A 1 132 ? -30.58400 24.37900 50.87300 1.000 29.18558  ? 132 ALA A HB2  1 
ATOM   2077 H  HB3  . ALA A 1 132 ? -29.71100 24.41300 49.54700 1.000 29.18558  ? 132 ALA A HB3  1 
ATOM   2078 N  N    . LEU A 1 133 ? -29.86800 22.42300 47.48800 1.000 23.21335  ? 133 LEU A N    1 
ATOM   2079 C  CA   . LEU A 1 133 ? -29.80000 22.23600 46.04100 1.000 24.27494  ? 133 LEU A CA   1 
ATOM   2080 C  C    . LEU A 1 133 ? -30.29000 20.84800 45.64200 1.000 23.71966  ? 133 LEU A C    1 
ATOM   2081 O  O    . LEU A 1 133 ? -30.97200 20.69600 44.62200 1.000 25.55709  ? 133 LEU A O    1 
ATOM   2082 C  CB   . LEU A 1 133 ? -28.37000 22.46000 45.55100 1.000 24.45951  ? 133 LEU A CB   1 
ATOM   2083 C  CG   . LEU A 1 133 ? -27.89600 23.90700 45.52000 1.000 22.85012  ? 133 LEU A CG   1 
ATOM   2084 C  CD1  . LEU A 1 133 ? -26.43200 24.00800 45.16100 1.000 25.05385  ? 133 LEU A CD1  1 
ATOM   2085 C  CD2  . LEU A 1 133 ? -28.71100 24.69200 44.52300 1.000 24.10687  ? 133 LEU A CD2  1 
ATOM   2086 H  H    . LEU A 1 133 ? -29.11000 22.38600 47.89300 1.000 28.30558  ? 133 LEU A H    1 
ATOM   2087 H  HA   . LEU A 1 133 ? -30.36800 22.89400 45.61000 1.000 29.58558  ? 133 LEU A HA   1 
ATOM   2088 H  HB2  . LEU A 1 133 ? -27.76900 21.97300 46.13700 1.000 29.82558  ? 133 LEU A HB2  1 
ATOM   2089 H  HB3  . LEU A 1 133 ? -28.30200 22.11600 44.64600 1.000 29.82558  ? 133 LEU A HB3  1 
ATOM   2090 H  HG   . LEU A 1 133 ? -28.01000 24.28400 46.40700 1.000 28.22558  ? 133 LEU A HG   1 
ATOM   2091 H  HD11 . LEU A 1 133 ? -26.16700 24.94100 45.17500 1.000 30.78558  ? 133 LEU A HD11 1 
ATOM   2092 H  HD12 . LEU A 1 133 ? -25.91200 23.50700 45.80900 1.000 30.78558  ? 133 LEU A HD12 1 
ATOM   2093 H  HD13 . LEU A 1 133 ? -26.29900 23.63900 44.27400 1.000 30.78558  ? 133 LEU A HD13 1 
ATOM   2094 H  HD21 . LEU A 1 133 ? -28.27600 25.54300 44.35900 1.000 29.95558  ? 133 LEU A HD21 1 
ATOM   2095 H  HD22 . LEU A 1 133 ? -28.77200 24.18700 43.69800 1.000 29.95558  ? 133 LEU A HD22 1 
ATOM   2096 H  HD23 . LEU A 1 133 ? -29.59800 24.83900 44.88700 1.000 29.95558  ? 133 LEU A HD23 1 
ATOM   2097 N  N    . GLN A 1 134 ? -29.95800 19.82600 46.43400 1.000 23.46070  ? 134 GLN A N    1 
ATOM   2098 C  CA   . GLN A 1 134 ? -30.48600 18.49200 46.16100 1.000 27.13326  ? 134 GLN A CA   1 
ATOM   2099 C  C    . GLN A 1 134 ? -32.00900 18.52500 46.09200 1.000 28.37503  ? 134 GLN A C    1 
ATOM   2100 O  O    . GLN A 1 134 ? -32.61800 18.00100 45.15200 1.000 26.24774  ? 134 GLN A O    1 
ATOM   2101 C  CB   . GLN A 1 134 ? -30.03500 17.50600 47.24100 1.000 27.12658  ? 134 GLN A CB   1 
ATOM   2102 C  CG   . GLN A 1 134 ? -28.54600 17.21300 47.26700 1.000 28.52231  ? 134 GLN A CG   1 
ATOM   2103 C  CD   . GLN A 1 134 ? -28.14700 16.36500 48.47600 1.000 38.50960  ? 134 GLN A CD   1 
ATOM   2104 O  OE1  . GLN A 1 134 ? -29.00400 15.88100 49.20800 1.000 45.70972  ? 134 GLN A OE1  1 
ATOM   2105 N  NE2  . GLN A 1 134 ? -26.85100 16.18900 48.68200 1.000 42.11940  ? 134 GLN A NE2  1 
ATOM   2106 H  H    . GLN A 1 134 ? -29.44100 19.87800 47.12000 1.000 27.68558  ? 134 GLN A H    1 
ATOM   2107 H  HA   . GLN A 1 134 ? -30.13400 18.18700 45.31000 1.000 31.44558  ? 134 GLN A HA   1 
ATOM   2108 H  HB2  . GLN A 1 134 ? -30.27400 17.87000 48.10800 1.000 30.83558  ? 134 GLN A HB2  1 
ATOM   2109 H  HB3  . GLN A 1 134 ? -30.49400 16.66300 47.09800 1.000 30.83558  ? 134 GLN A HB3  1 
ATOM   2110 H  HG2  . GLN A 1 134 ? -28.30300 16.72700 46.46300 1.000 32.19558  ? 134 GLN A HG2  1 
ATOM   2111 H  HG3  . GLN A 1 134 ? -28.05700 18.04900 47.30900 1.000 32.19558  ? 134 GLN A HG3  1 
ATOM   2112 H  HE21 . GLN A 1 134 ? -26.27900 16.54500 48.14700 1.000 47.57558  ? 134 GLN A HE21 1 
ATOM   2113 H  HE22 . GLN A 1 134 ? -26.58100 15.71900 49.35000 1.000 47.57558  ? 134 GLN A HE22 1 
ATOM   2114 N  N    . ASP A 1 135 ? -32.63500 19.08800 47.12700 1.000 25.87518  ? 135 ASP A N    1 
ATOM   2115 C  CA   . ASP A 1 135 ? -34.09300 19.10200 47.21600 1.000 28.34746  ? 135 ASP A CA   1 
ATOM   2116 C  C    . ASP A 1 135 ? -34.69900 19.94300 46.09200 1.000 24.11810  ? 135 ASP A C    1 
ATOM   2117 O  O    . ASP A 1 135 ? -35.69300 19.54900 45.45700 1.000 27.41822  ? 135 ASP A O    1 
ATOM   2118 C  CB   . ASP A 1 135 ? -34.53100 19.66700 48.56700 1.000 26.53672  ? 135 ASP A CB   1 
ATOM   2119 C  CG   . ASP A 1 135 ? -34.17400 18.78100 49.75000 1.000 35.13988  ? 135 ASP A CG   1 
ATOM   2120 O  OD1  . ASP A 1 135 ? -33.81900 17.60000 49.55800 1.000 31.72264  ? 135 ASP A OD1  1 
ATOM   2121 O  OD2  . ASP A 1 135 ? -34.25000 19.29800 50.90000 1.000 29.94371  ? 135 ASP A OD2  1 
ATOM   2122 H  H    . ASP A 1 135 ? -32.24000 19.46800 47.79000 1.000 30.27558  ? 135 ASP A H    1 
ATOM   2123 H  HA   . ASP A 1 135 ? -34.41400 18.19000 47.13800 1.000 33.21558  ? 135 ASP A HA   1 
ATOM   2124 H  HB2  . ASP A 1 135 ? -34.10000 20.52500 48.70100 1.000 31.23558  ? 135 ASP A HB2  1 
ATOM   2125 H  HB3  . ASP A 1 135 ? -35.49500 19.77700 48.56200 1.000 31.23558  ? 135 ASP A HB3  1 
ATOM   2126 N  N    . ALA A 1 136 ? -34.14700 21.12900 45.87200 1.000 23.15545  ? 136 ALA A N    1 
ATOM   2127 C  CA   . ALA A 1 136 ? -34.72200 22.02700 44.88100 1.000 23.36559  ? 136 ALA A CA   1 
ATOM   2128 C  C    . ALA A 1 136 ? -34.49600 21.51500 43.46500 1.000 22.86872  ? 136 ALA A C    1 
ATOM   2129 O  O    . ALA A 1 136 ? -35.35100 21.70400 42.59400 1.000 23.58008  ? 136 ALA A O    1 
ATOM   2130 C  CB   . ALA A 1 136 ? -34.12900 23.42700 45.03900 1.000 21.98615  ? 136 ALA A CB   1 
ATOM   2131 H  H    . ALA A 1 136 ? -33.45100 21.43400 46.27600 1.000 27.83558  ? 136 ALA A H    1 
ATOM   2132 H  HA   . ALA A 1 136 ? -35.67900 22.08800 45.03000 1.000 28.35558  ? 136 ALA A HA   1 
ATOM   2133 H  HB1  . ALA A 1 136 ? -34.52700 24.01500 44.37800 1.000 27.07558  ? 136 ALA A HB1  1 
ATOM   2134 H  HB2  . ALA A 1 136 ? -34.32300 23.75300 45.93200 1.000 27.07558  ? 136 ALA A HB2  1 
ATOM   2135 H  HB3  . ALA A 1 136 ? -33.16900 23.38000 44.90500 1.000 27.07558  ? 136 ALA A HB3  1 
ATOM   2136 N  N    . TYR A 1 137 ? -33.35700 20.86800 43.21700 1.000 22.87792  ? 137 TYR A N    1 
ATOM   2137 C  CA   . TYR A 1 137 ? -33.09100 20.34600 41.87900 1.000 22.32783  ? 137 TYR A CA   1 
ATOM   2138 C  C    . TYR A 1 137 ? -34.02300 19.18400 41.55200 1.000 25.42380  ? 137 TYR A C    1 
ATOM   2139 O  O    . TYR A 1 137 ? -34.50500 19.05800 40.42000 1.000 27.02271  ? 137 TYR A O    1 
ATOM   2140 C  CB   . TYR A 1 137 ? -31.63200 19.91500 41.76400 1.000 22.62318  ? 137 TYR A CB   1 
ATOM   2141 C  CG   . TYR A 1 137 ? -31.29700 19.45400 40.37100 1.000 24.78683  ? 137 TYR A CG   1 
ATOM   2142 C  CD1  . TYR A 1 137 ? -31.58500 20.25900 39.28600 1.000 26.66538  ? 137 TYR A CD1  1 
ATOM   2143 C  CD2  . TYR A 1 137 ? -30.73400 18.20900 40.13800 1.000 30.50671  ? 137 TYR A CD2  1 
ATOM   2144 C  CE1  . TYR A 1 137 ? -31.30600 19.84900 37.99900 1.000 25.07887  ? 137 TYR A CE1  1 
ATOM   2145 C  CE2  . TYR A 1 137 ? -30.44000 17.79400 38.83900 1.000 30.74034  ? 137 TYR A CE2  1 
ATOM   2146 C  CZ   . TYR A 1 137 ? -30.73800 18.61900 37.78400 1.000 32.42011  ? 137 TYR A CZ   1 
ATOM   2147 O  OH   . TYR A 1 137 ? -30.47000 18.22300 36.48000 1.000 33.56968  ? 137 TYR A OH   1 
ATOM   2148 H  H    . TYR A 1 137 ? -32.73500 20.72100 43.79400 1.000 27.42558  ? 137 TYR A H    1 
ATOM   2149 H  HA   . TYR A 1 137 ? -33.24400 21.05000 41.22900 1.000 26.49558  ? 137 TYR A HA   1 
ATOM   2150 H  HB2  . TYR A 1 137 ? -31.05900 20.66600 41.98300 1.000 26.66558  ? 137 TYR A HB2  1 
ATOM   2151 H  HB3  . TYR A 1 137 ? -31.46700 19.18100 42.37600 1.000 26.66558  ? 137 TYR A HB3  1 
ATOM   2152 H  HD1  . TYR A 1 137 ? -31.97300 21.09300 39.42700 1.000 31.48558  ? 137 TYR A HD1  1 
ATOM   2153 H  HD2  . TYR A 1 137 ? -30.55000 17.64500 40.85500 1.000 35.05558  ? 137 TYR A HD2  1 
ATOM   2154 H  HE1  . TYR A 1 137 ? -31.50200 20.40500 37.27900 1.000 29.23558  ? 137 TYR A HE1  1 
ATOM   2155 H  HE2  . TYR A 1 137 ? -30.04600 16.96500 38.68900 1.000 34.90558  ? 137 TYR A HE2  1 
ATOM   2156 H  HH   . TYR A 1 137 ? -30.11000 17.46500 36.47700 1.000 38.25558  ? 137 TYR A HH   1 
ATOM   2157 N  N    . TYR A 1 138 ? -34.29600 18.32900 42.53400 1.000 26.92424  ? 138 TYR A N    1 
ATOM   2158 C  CA   . TYR A 1 138 ? -35.27800 17.26600 42.34900 1.000 30.23566  ? 138 TYR A CA   1 
ATOM   2159 C  C    . TYR A 1 138 ? -36.63100 17.83300 41.94300 1.000 28.68128  ? 138 TYR A C    1 
ATOM   2160 O  O    . TYR A 1 138 ? -37.28100 17.33500 41.01100 1.000 29.59062  ? 138 TYR A O    1 
ATOM   2161 C  CB   . TYR A 1 138 ? -35.38900 16.46400 43.64900 1.000 32.84084  ? 138 TYR A CB   1 
ATOM   2162 C  CG   . TYR A 1 138 ? -36.36300 15.31500 43.58900 1.000 32.31482  ? 138 TYR A CG   1 
ATOM   2163 C  CD1  . TYR A 1 138 ? -35.98000 14.08400 43.08600 1.000 44.88984  ? 138 TYR A CD1  1 
ATOM   2164 C  CD2  . TYR A 1 138 ? -37.65500 15.45800 44.07100 1.000 39.33297  ? 138 TYR A CD2  1 
ATOM   2165 C  CE1  . TYR A 1 138 ? -36.87300 13.02500 43.03600 1.000 54.24881  ? 138 TYR A CE1  1 
ATOM   2166 C  CE2  . TYR A 1 138 ? -38.55300 14.40800 44.02600 1.000 51.29618  ? 138 TYR A CE2  1 
ATOM   2167 C  CZ   . TYR A 1 138 ? -38.15700 13.19600 43.51100 1.000 56.91478  ? 138 TYR A CZ   1 
ATOM   2168 O  OH   . TYR A 1 138 ? -39.05800 12.15500 43.47500 1.000 76.30723  ? 138 TYR A OH   1 
ATOM   2169 H  H    . TYR A 1 138 ? -33.92900 18.34300 43.31200 1.000 30.97558  ? 138 TYR A H    1 
ATOM   2170 H  HA   . TYR A 1 138 ? -34.98700 16.67100 41.64000 1.000 34.24558  ? 138 TYR A HA   1 
ATOM   2171 H  HB2  . TYR A 1 138 ? -34.51600 16.09800 43.86200 1.000 36.93558  ? 138 TYR A HB2  1 
ATOM   2172 H  HB3  . TYR A 1 138 ? -35.68100 17.06000 44.35600 1.000 36.93558  ? 138 TYR A HB3  1 
ATOM   2173 H  HD1  . TYR A 1 138 ? -35.11100 13.96600 42.77800 1.000 49.51558  ? 138 TYR A HD1  1 
ATOM   2174 H  HD2  . TYR A 1 138 ? -37.92200 16.27400 44.43000 1.000 43.85558  ? 138 TYR A HD2  1 
ATOM   2175 H  HE1  . TYR A 1 138 ? -36.60800 12.20500 42.68500 1.000 59.75558  ? 138 TYR A HE1  1 
ATOM   2176 H  HE2  . TYR A 1 138 ? -39.42000 14.52100 44.34400 1.000 57.31558  ? 138 TYR A HE2  1 
ATOM   2177 H  HH   . TYR A 1 138 ? -38.71300 11.48900 43.09700 1.000 85.25558  ? 138 TYR A HH   1 
ATOM   2178 N  N    . ARG A 1 139 ? -37.07300 18.89300 42.62500 1.000 25.53104  ? 139 ARG A N    1 
ATOM   2179 C  CA   . ARG A 1 139 ? -38.32800 19.53600 42.24800 1.000 26.43604  ? 139 ARG A CA   1 
ATOM   2180 C  C    . ARG A 1 139 ? -38.24500 20.12700 40.84600 1.000 26.90753  ? 139 ARG A C    1 
ATOM   2181 O  O    . ARG A 1 139 ? -39.21300 20.06800 40.07900 1.000 29.59948  ? 139 ARG A O    1 
ATOM   2182 C  CB   . ARG A 1 139 ? -38.68000 20.63000 43.25000 1.000 27.36741  ? 139 ARG A CB   1 
ATOM   2183 C  CG   . ARG A 1 139 ? -38.87100 20.12600 44.67200 1.000 32.86232  ? 139 ARG A CG   1 
ATOM   2184 C  CD   . ARG A 1 139 ? -39.54300 21.18500 45.55800 1.000 39.79688  ? 139 ARG A CD   1 
ATOM   2185 N  NE   . ARG A 1 139 ? -40.84400 21.56900 45.02500 1.000 65.57506  ? 139 ARG A NE   1 
ATOM   2186 C  CZ   . ARG A 1 139 ? -41.50500 22.67200 45.34700 1.000 65.31267  ? 139 ARG A CZ   1 
ATOM   2187 N  NH1  . ARG A 1 139 ? -41.02700 23.53200 46.23600 1.000 59.14724  ? 139 ARG A NH1  1 
ATOM   2188 N  NH2  . ARG A 1 139 ? -42.68100 22.91400 44.76900 1.000 65.92460  ? 139 ARG A NH2  1 
ATOM   2189 H  H    . ARG A 1 139 ? -36.67200 19.25100 43.29700 1.000 29.37558  ? 139 ARG A H    1 
ATOM   2190 H  HA   . ARG A 1 139 ? -39.03200 18.86800 42.26200 1.000 30.57558  ? 139 ARG A HA   1 
ATOM   2191 H  HB2  . ARG A 1 139 ? -37.96300 21.28300 43.26100 1.000 32.14558  ? 139 ARG A HB2  1 
ATOM   2192 H  HB3  . ARG A 1 139 ? -39.50800 21.05100 42.97200 1.000 32.14558  ? 139 ARG A HB3  1 
ATOM   2193 H  HG2  . ARG A 1 139 ? -39.43400 19.33700 44.66000 1.000 38.57558  ? 139 ARG A HG2  1 
ATOM   2194 H  HG3  . ARG A 1 139 ? -38.00700 19.91200 45.05600 1.000 38.57558  ? 139 ARG A HG3  1 
ATOM   2195 H  HD2  . ARG A 1 139 ? -39.67100 20.82400 46.45000 1.000 47.16558  ? 139 ARG A HD2  1 
ATOM   2196 H  HD3  . ARG A 1 139 ? -38.98200 21.97500 45.59800 1.000 47.16558  ? 139 ARG A HD3  1 
ATOM   2197 H  HE   . ARG A 1 139 ? -41.21200 21.03900 44.45600 1.000 77.94558  ? 139 ARG A HE   1 
ATOM   2198 H  HH11 . ARG A 1 139 ? -40.27100 23.38000 46.61700 1.000 70.59558  ? 139 ARG A HH11 1 
ATOM   2199 H  HH12 . ARG A 1 139 ? -41.47200 24.24100 46.43000 1.000 70.59558  ? 139 ARG A HH12 1 
ATOM   2200 H  HH21 . ARG A 1 139 ? -43.00100 22.35900 44.19600 1.000 78.21558  ? 139 ARG A HH21 1 
ATOM   2201 H  HH22 . ARG A 1 139 ? -43.12000 23.62600 44.96900 1.000 78.21558  ? 139 ARG A HH22 1 
ATOM   2202 N  N    . ALA A 1 140 ? -37.10000 20.72600 40.50400 1.000 24.08029  ? 140 ALA A N    1 
ATOM   2203 C  CA   . ALA A 1 140 ? -36.94600 21.33800 39.18800 1.000 23.61328  ? 140 ALA A CA   1 
ATOM   2204 C  C    . ALA A 1 140 ? -37.05300 20.29400 38.08400 1.000 24.43574  ? 140 ALA A C    1 
ATOM   2205 O  O    . ALA A 1 140 ? -37.66000 20.54700 37.03300 1.000 25.99472  ? 140 ALA A O    1 
ATOM   2206 C  CB   . ALA A 1 140 ? -35.60500 22.05700 39.09100 1.000 25.21965  ? 140 ALA A CB   1 
ATOM   2207 H  H    . ALA A 1 140 ? -36.40800 20.79000 41.01100 1.000 28.29558  ? 140 ALA A H    1 
ATOM   2208 H  HA   . ALA A 1 140 ? -37.65200 21.99200 39.06900 1.000 27.86558  ? 140 ALA A HA   1 
ATOM   2209 H  HB1  . ALA A 1 140 ? -35.51900 22.44600 38.20700 1.000 30.21558  ? 140 ALA A HB1  1 
ATOM   2210 H  HB2  . ALA A 1 140 ? -35.57200 22.75500 39.76400 1.000 30.21558  ? 140 ALA A HB2  1 
ATOM   2211 H  HB3  . ALA A 1 140 ? -34.89200 21.41800 39.24300 1.000 30.21558  ? 140 ALA A HB3  1 
ATOM   2212 N  N    . ARG A 1 141 ? -36.45700 19.11700 38.30100 1.000 25.16782  ? 141 ARG A N    1 
ATOM   2213 C  CA   . ARG A 1 141 ? -36.57800 18.03000 37.33000 1.000 30.49702  ? 141 ARG A CA   1 
ATOM   2214 C  C    . ARG A 1 141 ? -38.02300 17.58900 37.15900 1.000 38.31368  ? 141 ARG A C    1 
ATOM   2215 O  O    . ARG A 1 141 ? -38.42100 17.16300 36.07000 1.000 34.88884  ? 141 ARG A O    1 
ATOM   2216 C  CB   . ARG A 1 141 ? -35.72700 16.83700 37.77000 1.000 34.15403  ? 141 ARG A CB   1 
ATOM   2217 C  CG   . ARG A 1 141 ? -34.23700 17.03600 37.56900 1.000 33.89211  ? 141 ARG A CG   1 
ATOM   2218 C  CD   . ARG A 1 141 ? -33.44200 15.95200 38.25700 1.000 40.96780  ? 141 ARG A CD   1 
ATOM   2219 N  NE   . ARG A 1 141 ? -33.58500 14.69600 37.53500 1.000 47.39542  ? 141 ARG A NE   1 
ATOM   2220 C  CZ   . ARG A 1 141 ? -33.90700 13.53500 38.09000 1.000 81.31071  ? 141 ARG A CZ   1 
ATOM   2221 N  NH1  . ARG A 1 141 ? -34.08000 13.41300 39.40000 1.000 60.10784  ? 141 ARG A NH1  1 
ATOM   2222 N  NH2  . ARG A 1 141 ? -34.06100 12.46600 37.30900 1.000 59.18913  ? 141 ARG A NH2  1 
ATOM   2223 H  H    . ARG A 1 141 ? -35.98300 18.92600 38.99300 1.000 28.68558  ? 141 ARG A H    1 
ATOM   2224 H  HA   . ARG A 1 141 ? -36.25000 18.34600 36.47400 1.000 34.31558  ? 141 ARG A HA   1 
ATOM   2225 H  HB2  . ARG A 1 141 ? -35.88000 16.67700 38.71400 1.000 38.07558  ? 141 ARG A HB2  1 
ATOM   2226 H  HB3  . ARG A 1 141 ? -35.99300 16.05900 37.25500 1.000 38.07558  ? 141 ARG A HB3  1 
ATOM   2227 H  HG2  . ARG A 1 141 ? -34.03300 17.01000 36.62100 1.000 37.96558  ? 141 ARG A HG2  1 
ATOM   2228 H  HG3  . ARG A 1 141 ? -33.97300 17.89200 37.94200 1.000 37.96558  ? 141 ARG A HG3  1 
ATOM   2229 H  HD2  . ARG A 1 141 ? -32.50300 16.19600 38.27400 1.000 45.81558  ? 141 ARG A HD2  1 
ATOM   2230 H  HD3  . ARG A 1 141 ? -33.77000 15.83000 39.16100 1.000 45.81558  ? 141 ARG A HD3  1 
ATOM   2231 H  HE   . ARG A 1 141 ? -33.45000 14.70800 36.68600 1.000 52.37558  ? 141 ARG A HE   1 
ATOM   2232 H  HH11 . ARG A 1 141 ? -33.98400 14.09800 39.91200 1.000 66.79558  ? 141 ARG A HH11 1 
ATOM   2233 H  HH12 . ARG A 1 141 ? -34.28900 12.65000 39.73800 1.000 66.79558  ? 141 ARG A HH12 1 
ATOM   2234 H  HH21 . ARG A 1 141 ? -33.95200 12.53600 36.45900 1.000 64.40558  ? 141 ARG A HH21 1 
ATOM   2235 H  HH22 . ARG A 1 141 ? -34.27000 11.70700 37.65500 1.000 64.40558  ? 141 ARG A HH22 1 
ATOM   2236 N  N    . ALA A 1 142 ? -38.81200 17.65600 38.22300 1.000 33.20366  ? 142 ALA A N    1 
ATOM   2237 C  CA   . ALA A 1 142 ? -40.23400 17.35100 38.15400 1.000 37.88307  ? 142 ALA A CA   1 
ATOM   2238 C  C    . ALA A 1 142 ? -41.04200 18.48700 37.55300 1.000 37.26544  ? 142 ALA A C    1 
ATOM   2239 O  O    . ALA A 1 142 ? -42.23600 18.31100 37.30300 1.000 44.53084  ? 142 ALA A O    1 
ATOM   2240 C  CB   . ALA A 1 142 ? -40.76400 17.03100 39.55200 1.000 36.38469  ? 142 ALA A CB   1 
ATOM   2241 H  H    . ALA A 1 142 ? -38.54400 17.87800 39.00900 1.000 37.15558  ? 142 ALA A H    1 
ATOM   2242 H  HA   . ALA A 1 142 ? -40.36300 16.56700 37.59900 1.000 42.31558  ? 142 ALA A HA   1 
ATOM   2243 H  HB1  . ALA A 1 142 ? -41.71300 16.83900 39.49500 1.000 40.42558  ? 142 ALA A HB1  1 
ATOM   2244 H  HB2  . ALA A 1 142 ? -40.29100 16.25800 39.90000 1.000 40.42558  ? 142 ALA A HB2  1 
ATOM   2245 H  HB3  . ALA A 1 142 ? -40.61600 17.79600 40.12900 1.000 40.42558  ? 142 ALA A HB3  1 
ATOM   2246 N  N    . GLY A 1 143 ? -40.42600 19.64200 37.32800 1.000 34.65204  ? 143 GLY A N    1 
ATOM   2247 C  CA   . GLY A 1 143 ? -41.07300 20.75800 36.66900 1.000 33.98592  ? 143 GLY A CA   1 
ATOM   2248 C  C    . GLY A 1 143 ? -41.34100 21.96600 37.54000 1.000 33.63850  ? 143 GLY A C    1 
ATOM   2249 O  O    . GLY A 1 143 ? -41.83400 22.97600 37.02700 1.000 37.78531  ? 143 GLY A O    1 
ATOM   2250 H  H    . GLY A 1 143 ? -39.61300 19.80200 37.55400 1.000 39.53558  ? 143 GLY A H    1 
ATOM   2251 H  HA2  . GLY A 1 143 ? -40.51200 21.04700 35.93300 1.000 38.96558  ? 143 GLY A HA2  1 
ATOM   2252 H  HA3  . GLY A 1 143 ? -41.92500 20.45600 36.31800 1.000 38.96558  ? 143 GLY A HA3  1 
ATOM   2253 N  N    A GLU A 1 144 ? -41.05600 21.89400 38.83800 0.490 28.91391  ? 144 GLU A N    1 
ATOM   2254 N  N    B GLU A 1 144 ? -41.05100 21.90600 38.83800 0.510 28.86303  ? 144 GLU A N    1 
ATOM   2255 C  CA   A GLU A 1 144 ? -41.28700 22.99300 39.77000 0.490 32.16408  ? 144 GLU A CA   1 
ATOM   2256 C  CA   B GLU A 1 144 ? -41.29900 23.01800 39.75400 0.510 32.11860  ? 144 GLU A CA   1 
ATOM   2257 C  C    A GLU A 1 144 ? -39.92500 23.58300 40.14100 0.490 28.90602  ? 144 GLU A C    1 
ATOM   2258 C  C    B GLU A 1 144 ? -39.94800 23.60900 40.15000 0.510 28.81089  ? 144 GLU A C    1 
ATOM   2259 O  O    A GLU A 1 144 ? -39.35500 23.27400 41.18700 0.490 28.78271  ? 144 GLU A O    1 
ATOM   2260 O  O    B GLU A 1 144 ? -39.40900 23.33100 41.22100 0.510 28.70789  ? 144 GLU A O    1 
ATOM   2261 C  CB   A GLU A 1 144 ? -42.05700 22.48600 41.01100 0.490 35.11725  ? 144 GLU A CB   1 
ATOM   2262 C  CB   B GLU A 1 144 ? -42.11100 22.53600 40.96700 0.510 35.42720  ? 144 GLU A CB   1 
ATOM   2263 C  CG   A GLU A 1 144 ? -43.52600 22.11000 40.74200 0.490 40.69944  ? 144 GLU A CG   1 
ATOM   2264 C  CG   B GLU A 1 144 ? -43.56700 22.23500 40.60800 0.510 40.60002  ? 144 GLU A CG   1 
ATOM   2265 C  CD   A GLU A 1 144 ? -43.69900 20.83800 39.91800 0.490 56.10954  ? 144 GLU A CD   1 
ATOM   2266 C  CD   B GLU A 1 144 ? -44.36100 21.62600 41.74900 0.510 48.54542  ? 144 GLU A CD   1 
ATOM   2267 O  OE1  A GLU A 1 144 ? -43.17100 19.77900 40.32000 0.490 37.70402  ? 144 GLU A OE1  1 
ATOM   2268 O  OE1  B GLU A 1 144 ? -43.81100 21.47200 42.85900 0.510 56.71252  ? 144 GLU A OE1  1 
ATOM   2269 O  OE2  A GLU A 1 144 ? -44.38200 20.89600 38.87000 0.490 62.90652  ? 144 GLU A OE2  1 
ATOM   2270 O  OE2  B GLU A 1 144 ? -45.54400 21.28900 41.52400 0.510 69.37922  ? 144 GLU A OE2  1 
ATOM   2271 H  H    A GLU A 1 144 ? -40.71800 21.19800 39.21200 0.490 33.59558  ? 144 GLU A H    1 
ATOM   2272 H  H    B GLU A 1 144 ? -40.70400 21.21800 39.21900 0.510 33.53558  ? 144 GLU A H    1 
ATOM   2273 H  HA   A GLU A 1 144 ? -41.81300 23.68600 39.34100 0.490 37.81558  ? 144 GLU A HA   1 
ATOM   2274 H  HA   B GLU A 1 144 ? -41.80900 23.71000 39.30400 0.510 37.76558  ? 144 GLU A HA   1 
ATOM   2275 H  HB2  A GLU A 1 144 ? -41.61000 21.69500 41.35000 0.490 41.14558  ? 144 GLU A HB2  1 
ATOM   2276 H  HB2  B GLU A 1 144 ? -41.71100 21.72300 41.31300 0.510 41.51558  ? 144 GLU A HB2  1 
ATOM   2277 H  HB3  A GLU A 1 144 ? -42.05200 23.18400 41.68400 0.490 41.14558  ? 144 GLU A HB3  1 
ATOM   2278 H  HB3  B GLU A 1 144 ? -42.10300 23.22600 41.64800 0.510 41.51558  ? 144 GLU A HB3  1 
ATOM   2279 H  HG2  A GLU A 1 144 ? -43.97300 21.97400 41.59200 0.490 47.31558  ? 144 GLU A HG2  1 
ATOM   2280 H  HG2  B GLU A 1 144 ? -44.00400 23.06300 40.35300 0.510 47.21558  ? 144 GLU A HG2  1 
ATOM   2281 H  HG3  A GLU A 1 144 ? -43.94900 22.83600 40.25700 0.490 47.31558  ? 144 GLU A HG3  1 
ATOM   2282 H  HG3  B GLU A 1 144 ? -43.58500 21.60900 39.86800 0.510 47.21558  ? 144 GLU A HG3  1 
ATOM   2283 N  N    . ALA A 1 145 ? -39.40300 24.44400 39.26600 1.000 26.06043  ? 145 ALA A N    1 
ATOM   2284 C  CA   . ALA A 1 145 ? -38.02200 24.89600 39.35600 1.000 25.19736  ? 145 ALA A CA   1 
ATOM   2285 C  C    . ALA A 1 145 ? -37.83700 26.24400 40.04200 1.000 25.28315  ? 145 ALA A C    1 
ATOM   2286 O  O    . ALA A 1 145 ? -36.70800 26.74800 40.08000 1.000 23.43952  ? 145 ALA A O    1 
ATOM   2287 C  CB   . ALA A 1 145 ? -37.40900 24.95600 37.95900 1.000 27.28257  ? 145 ALA A CB   1 
ATOM   2288 H  H    A ALA A 1 145 ? -39.83800 24.78300 38.60500 0.490 31.15558  ? 145 ALA A H    1 
ATOM   2289 H  H    B ALA A 1 145 ? -39.82600 24.76900 38.59100 0.510 31.15558  ? 145 ALA A H    1 
ATOM   2290 H  HA   . ALA A 1 145 ? -37.54400 24.24300 39.89200 1.000 30.47558  ? 145 ALA A HA   1 
ATOM   2291 H  HB1  . ALA A 1 145 ? -36.49800 25.28100 38.02800 1.000 32.97558  ? 145 ALA A HB1  1 
ATOM   2292 H  HB2  . ALA A 1 145 ? -37.41500 24.06600 37.57300 1.000 32.97558  ? 145 ALA A HB2  1 
ATOM   2293 H  HB3  . ALA A 1 145 ? -37.93500 25.55900 37.41000 1.000 32.97558  ? 145 ALA A HB3  1 
ATOM   2294 N  N    . ALA A 1 146 ? -38.88900 26.82700 40.61800 1.000 26.79319  ? 146 ALA A N    1 
ATOM   2295 C  CA   . ALA A 1 146 ? -38.75500 28.17400 41.17800 1.000 26.45623  ? 146 ALA A CA   1 
ATOM   2296 C  C    . ALA A 1 146 ? -37.71000 28.23000 42.29100 1.000 25.74791  ? 146 ALA A C    1 
ATOM   2297 O  O    . ALA A 1 146 ? -36.89100 29.15100 42.34300 1.000 22.78827  ? 146 ALA A O    1 
ATOM   2298 C  CB   . ALA A 1 146 ? -40.10400 28.66400 41.69500 1.000 27.17550  ? 146 ALA A CB   1 
ATOM   2299 H  H    . ALA A 1 146 ? -39.67000 26.47500 40.69700 1.000 32.37558  ? 146 ALA A H    1 
ATOM   2300 H  HA   . ALA A 1 146 ? -38.46300 28.76600 40.46700 1.000 31.90558  ? 146 ALA A HA   1 
ATOM   2301 H  HB1  . ALA A 1 146 ? -40.00100 29.56300 42.04500 1.000 32.38558  ? 146 ALA A HB1  1 
ATOM   2302 H  HB2  . ALA A 1 146 ? -40.74100 28.66500 40.96300 1.000 32.38558  ? 146 ALA A HB2  1 
ATOM   2303 H  HB3  . ALA A 1 146 ? -40.40900 28.06800 42.39800 1.000 32.38558  ? 146 ALA A HB3  1 
ATOM   2304 N  N    . ASN A 1 147 ? -37.75400 27.28800 43.23400 1.000 26.75808  ? 147 ASN A N    1 
ATOM   2305 C  CA   . ASN A 1 147 ? -36.79400 27.36300 44.33600 1.000 23.82368  ? 147 ASN A CA   1 
ATOM   2306 C  C    . ASN A 1 147 ? -35.37700 27.14200 43.83600 1.000 24.24190  ? 147 ASN A C    1 
ATOM   2307 O  O    . ASN A 1 147 ? -34.44900 27.82600 44.27200 1.000 22.94556  ? 147 ASN A O    1 
ATOM   2308 C  CB   . ASN A 1 147 ? -37.16400 26.36000 45.41200 1.000 27.21375  ? 147 ASN A CB   1 
ATOM   2309 C  CG   . ASN A 1 147 ? -38.30800 26.88100 46.28900 1.000 29.56102  ? 147 ASN A CG   1 
ATOM   2310 O  OD1  . ASN A 1 147 ? -38.08900 27.60000 47.27000 1.000 40.65792  ? 147 ASN A OD1  1 
ATOM   2311 N  ND2  . ASN A 1 147 ? -39.51100 26.61400 45.87500 1.000 34.05116  ? 147 ASN A ND2  1 
ATOM   2312 H  H    . ASN A 1 147 ? -38.30200 26.62600 43.25900 1.000 32.57558  ? 147 ASN A H    1 
ATOM   2313 H  HA   . ASN A 1 147 ? -36.83000 28.24600 44.73600 1.000 29.21558  ? 147 ASN A HA   1 
ATOM   2314 H  HB2  . ASN A 1 147 ? -37.45000 25.53200 44.99500 1.000 33.23558  ? 147 ASN A HB2  1 
ATOM   2315 H  HB3  . ASN A 1 147 ? -36.39300 26.19800 45.97900 1.000 33.23558  ? 147 ASN A HB3  1 
ATOM   2316 H  HD21 . ASN A 1 147 ? -39.62600 26.16900 45.14800 1.000 40.96558  ? 147 ASN A HD21 1 
ATOM   2317 H  HD22 . ASN A 1 147 ? -40.19100 26.88100 46.32800 1.000 40.96558  ? 147 ASN A HD22 1 
ATOM   2318 N  N    . PHE A 1 148 ? -35.19300 26.20000 42.90900 1.000 23.08403  ? 148 PHE A N    1 
ATOM   2319 C  CA   . PHE A 1 148 ? -33.86600 25.95900 42.36000 1.000 21.80235  ? 148 PHE A CA   1 
ATOM   2320 C  C    . PHE A 1 148 ? -33.31800 27.21000 41.67900 1.000 23.04000  ? 148 PHE A C    1 
ATOM   2321 O  O    . PHE A 1 148 ? -32.17000 27.59800 41.91100 1.000 23.10107  ? 148 PHE A O    1 
ATOM   2322 C  CB   . PHE A 1 148 ? -33.90400 24.78500 41.38400 1.000 20.94218  ? 148 PHE A CB   1 
ATOM   2323 C  CG   . PHE A 1 148 ? -32.54800 24.36500 40.90500 1.000 24.97344  ? 148 PHE A CG   1 
ATOM   2324 C  CD1  . PHE A 1 148 ? -31.63800 23.77300 41.76300 1.000 23.94011  ? 148 PHE A CD1  1 
ATOM   2325 C  CD2  . PHE A 1 148 ? -32.18300 24.56200 39.58700 1.000 26.31737  ? 148 PHE A CD2  1 
ATOM   2326 C  CE1  . PHE A 1 148 ? -30.38700 23.37600 41.30900 1.000 25.47251  ? 148 PHE A CE1  1 
ATOM   2327 C  CE2  . PHE A 1 148 ? -30.92500 24.16300 39.12700 1.000 26.52798  ? 148 PHE A CE2  1 
ATOM   2328 C  CZ   . PHE A 1 148 ? -30.03600 23.58200 39.99300 1.000 25.90257  ? 148 PHE A CZ   1 
ATOM   2329 H  H    . PHE A 1 148 ? -35.81200 25.69600 42.58900 1.000 28.61558  ? 148 PHE A H    1 
ATOM   2330 H  HA   . PHE A 1 148 ? -33.26800 25.72300 43.08600 1.000 27.20558  ? 148 PHE A HA   1 
ATOM   2331 H  HB2  . PHE A 1 148 ? -34.31200 24.02400 41.82500 1.000 26.04558  ? 148 PHE A HB2  1 
ATOM   2332 H  HB3  . PHE A 1 148 ? -34.42700 25.04000 40.60800 1.000 26.04558  ? 148 PHE A HB3  1 
ATOM   2333 H  HD1  . PHE A 1 148 ? -31.86700 23.63900 42.65500 1.000 29.59558  ? 148 PHE A HD1  1 
ATOM   2334 H  HD2  . PHE A 1 148 ? -32.78200 24.96400 38.99900 1.000 32.48558  ? 148 PHE A HD2  1 
ATOM   2335 H  HE1  . PHE A 1 148 ? -29.78700 22.97200 41.89300 1.000 31.34558  ? 148 PHE A HE1  1 
ATOM   2336 H  HE2  . PHE A 1 148 ? -30.69200 24.29100 38.23600 1.000 32.67558  ? 148 PHE A HE2  1 
ATOM   2337 H  HZ   . PHE A 1 148 ? -29.19400 23.32700 39.69200 1.000 31.85558  ? 148 PHE A HZ   1 
ATOM   2338 N  N    . CYS A 1 149 ? -34.13600 27.87100 40.84700 1.000 25.82096  ? 149 CYS A N    1 
ATOM   2339 C  CA   . CYS A 1 149 ? -33.66500 29.07900 40.17200 1.000 24.44020  ? 149 CYS A CA   1 
ATOM   2340 C  C    . CYS A 1 149 ? -33.32300 30.18100 41.17000 1.000 26.31232  ? 149 CYS A C    1 
ATOM   2341 O  O    . CYS A 1 149 ? -32.30800 30.87500 41.01900 1.000 21.61274  ? 149 CYS A O    1 
ATOM   2342 C  CB   . CYS A 1 149 ? -34.71000 29.56700 39.16800 1.000 24.78161  ? 149 CYS A CB   1 
ATOM   2343 S  SG   . CYS A 1 149 ? -34.83300 28.44800 37.76000 1.000 26.92529  ? 149 CYS A SG   1 
ATOM   2344 H  H    . CYS A 1 149 ? -34.94500 27.64500 40.66300 1.000 31.96558  ? 149 CYS A H    1 
ATOM   2345 H  HA   . CYS A 1 149 ? -32.85700 28.86200 39.68100 1.000 30.21558  ? 149 CYS A HA   1 
ATOM   2346 H  HB2  . CYS A 1 149 ? -35.57700 29.61000 39.60100 1.000 30.38558  ? 149 CYS A HB2  1 
ATOM   2347 H  HB3  . CYS A 1 149 ? -34.45800 30.44500 38.84100 1.000 30.38558  ? 149 CYS A HB3  1 
ATOM   2348 H  HG   . CYS A 1 149 ? -35.67400 28.85700 37.00800 1.000 33.02558  ? 149 CYS A HG   1 
ATOM   2349 N  N    . ALA A 1 150 ? -34.15400 30.36500 42.19500 1.000 23.62192  ? 150 ALA A N    1 
ATOM   2350 C  CA   . ALA A 1 150 ? -33.84600 31.37600 43.19700 1.000 21.89043  ? 150 ALA A CA   1 
ATOM   2351 C  C    . ALA A 1 150 ? -32.56300 31.03400 43.95200 1.000 23.29392  ? 150 ALA A C    1 
ATOM   2352 O  O    . ALA A 1 150 ? -31.79000 31.93200 44.30100 1.000 23.90589  ? 150 ALA A O    1 
ATOM   2353 C  CB   . ALA A 1 150 ? -35.02300 31.54900 44.15600 1.000 25.11953  ? 150 ALA A CB   1 
ATOM   2354 H  H    . ALA A 1 150 ? -34.88200 29.92700 42.32900 1.000 28.91558  ? 150 ALA A H    1 
ATOM   2355 H  HA   . ALA A 1 150 ? -33.70800 32.22700 42.75100 1.000 26.55558  ? 150 ALA A HA   1 
ATOM   2356 H  HB1  . ALA A 1 150 ? -34.79900 32.22700 44.81200 1.000 30.15558  ? 150 ALA A HB1  1 
ATOM   2357 H  HB2  . ALA A 1 150 ? -35.80500 31.82400 43.65100 1.000 30.15558  ? 150 ALA A HB2  1 
ATOM   2358 H  HB3  . ALA A 1 150 ? -35.19700 30.70400 44.59900 1.000 30.15558  ? 150 ALA A HB3  1 
ATOM   2359 N  N    . LEU A 1 151 ? -32.30500 29.74200 44.20100 1.000 23.61050  ? 151 LEU A N    1 
ATOM   2360 C  CA   . LEU A 1 151 ? -31.04800 29.36500 44.84800 1.000 22.97141  ? 151 LEU A CA   1 
ATOM   2361 C  C    . LEU A 1 151 ? -29.84400 29.63300 43.94300 1.000 25.80272  ? 151 LEU A C    1 
ATOM   2362 O  O    . LEU A 1 151 ? -28.81000 30.12200 44.41800 1.000 24.26774  ? 151 LEU A O    1 
ATOM   2363 C  CB   . LEU A 1 151 ? -31.07400 27.89100 45.27400 1.000 21.63196  ? 151 LEU A CB   1 
ATOM   2364 C  CG   . LEU A 1 151 ? -31.94500 27.58800 46.49100 1.000 23.31002  ? 151 LEU A CG   1 
ATOM   2365 C  CD1  . LEU A 1 151 ? -32.15700 26.06700 46.65000 1.000 28.13561  ? 151 LEU A CD1  1 
ATOM   2366 C  CD2  . LEU A 1 151 ? -31.36800 28.19400 47.78200 1.000 24.68851  ? 151 LEU A CD2  1 
ATOM   2367 H  H    . LEU A 1 151 ? -32.82700 29.08600 44.00900 1.000 29.16558  ? 151 LEU A H    1 
ATOM   2368 H  HA   . LEU A 1 151 ? -30.95200 29.90500 45.64800 1.000 28.50558  ? 151 LEU A HA   1 
ATOM   2369 H  HB2  . LEU A 1 151 ? -31.41400 27.36400 44.53400 1.000 27.07558  ? 151 LEU A HB2  1 
ATOM   2370 H  HB3  . LEU A 1 151 ? -30.16900 27.61700 45.48800 1.000 27.07558  ? 151 LEU A HB3  1 
ATOM   2371 H  HG   . LEU A 1 151 ? -32.81000 28.00300 46.34600 1.000 28.98558  ? 151 LEU A HG   1 
ATOM   2372 H  HD11 . LEU A 1 151 ? -32.73400 25.90700 47.41300 1.000 34.80558  ? 151 LEU A HD11 1 
ATOM   2373 H  HD12 . LEU A 1 151 ? -32.57000 25.71900 45.84400 1.000 34.80558  ? 151 LEU A HD12 1 
ATOM   2374 H  HD13 . LEU A 1 151 ? -31.29600 25.64100 46.79100 1.000 34.80558  ? 151 LEU A HD13 1 
ATOM   2375 H  HD21 . LEU A 1 151 ? -31.89300 27.88600 48.53700 1.000 30.48558  ? 151 LEU A HD21 1 
ATOM   2376 H  HD22 . LEU A 1 151 ? -30.44700 27.90700 47.88000 1.000 30.48558  ? 151 LEU A HD22 1 
ATOM   2377 H  HD23 . LEU A 1 151 ? -31.40900 29.16100 47.72200 1.000 30.48558  ? 151 LEU A HD23 1 
ATOM   2378 N  N    . ILE A 1 152 ? -29.94200 29.32400 42.64500 1.000 23.92563  ? 152 ILE A N    1 
ATOM   2379 C  CA   . ILE A 1 152 ? -28.82700 29.64100 41.74800 1.000 22.68385  ? 152 ILE A CA   1 
ATOM   2380 C  C    . ILE A 1 152 ? -28.47100 31.11700 41.86900 1.000 22.58473  ? 152 ILE A C    1 
ATOM   2381 O  O    . ILE A 1 152 ? -27.29500 31.49200 41.99400 1.000 23.18553  ? 152 ILE A O    1 
ATOM   2382 C  CB   . ILE A 1 152 ? -29.16500 29.28000 40.29100 1.000 25.86846  ? 152 ILE A CB   1 
ATOM   2383 C  CG1  . ILE A 1 152 ? -29.45400 27.78500 40.13300 1.000 32.03991  ? 152 ILE A CG1  1 
ATOM   2384 C  CG2  . ILE A 1 152 ? -28.01300 29.71200 39.37400 1.000 27.88624  ? 152 ILE A CG2  1 
ATOM   2385 C  CD1  . ILE A 1 152 ? -29.89700 27.41900 38.72600 1.000 38.51267  ? 152 ILE A CD1  1 
ATOM   2386 H  H    . ILE A 1 152 ? -30.61800 28.94400 42.27300 1.000 29.80558  ? 152 ILE A H    1 
ATOM   2387 H  HA   . ILE A 1 152 ? -28.06200 29.10800 42.01700 1.000 28.30558  ? 152 ILE A HA   1 
ATOM   2388 H  HB   . ILE A 1 152 ? -29.97200 29.75400 40.03900 1.000 32.19558  ? 152 ILE A HB   1 
ATOM   2389 H  HG12 . ILE A 1 152 ? -28.64800 27.28400 40.33400 1.000 39.70558  ? 152 ILE A HG12 1 
ATOM   2390 H  HG13 . ILE A 1 152 ? -30.16300 27.53400 40.74600 1.000 39.70558  ? 152 ILE A HG13 1 
ATOM   2391 H  HG21 . ILE A 1 152 ? -28.12700 29.29600 38.50500 1.000 34.54558  ? 152 ILE A HG21 1 
ATOM   2392 H  HG22 . ILE A 1 152 ? -28.02700 30.67800 39.28200 1.000 34.54558  ? 152 ILE A HG22 1 
ATOM   2393 H  HG23 . ILE A 1 152 ? -27.17200 29.43000 39.76800 1.000 34.54558  ? 152 ILE A HG23 1 
ATOM   2394 H  HD11 . ILE A 1 152 ? -30.68200 26.85200 38.78000 1.000 47.42558  ? 152 ILE A HD11 1 
ATOM   2395 H  HD12 . ILE A 1 152 ? -30.10800 28.23100 38.24100 1.000 47.42558  ? 152 ILE A HD12 1 
ATOM   2396 H  HD13 . ILE A 1 152 ? -29.17600 26.94600 38.28200 1.000 47.42558  ? 152 ILE A HD13 1 
ATOM   2397 N  N    . LEU A 1 153 ? -29.49200 31.97900 41.78900 1.000 23.01996  ? 153 LEU A N    1 
ATOM   2398 C  CA   . LEU A 1 153 ? -29.27200 33.41800 41.87700 1.000 23.49113  ? 153 LEU A CA   1 
ATOM   2399 C  C    . LEU A 1 153 ? -28.59400 33.77600 43.19000 1.000 25.91844  ? 153 LEU A C    1 
ATOM   2400 O  O    . LEU A 1 153 ? -27.61900 34.53400 43.22000 1.000 26.16966  ? 153 LEU A O    1 
ATOM   2401 C  CB   . LEU A 1 153 ? -30.60800 34.14600 41.72700 1.000 23.42031  ? 153 LEU A CB   1 
ATOM   2402 C  CG   . LEU A 1 153 ? -31.18800 34.12800 40.30500 1.000 23.77983  ? 153 LEU A CG   1 
ATOM   2403 C  CD1  . LEU A 1 153 ? -32.67600 34.41700 40.30700 1.000 25.69090  ? 153 LEU A CD1  1 
ATOM   2404 C  CD2  . LEU A 1 153 ? -30.46200 35.13000 39.42100 1.000 28.28651  ? 153 LEU A CD2  1 
ATOM   2405 H  H    . LEU A 1 153 ? -30.31500 31.75300 41.68400 1.000 28.12558  ? 153 LEU A H    1 
ATOM   2406 H  HA   . LEU A 1 153 ? -28.69200 33.70600 41.15500 1.000 28.16558  ? 153 LEU A HA   1 
ATOM   2407 H  HB2  . LEU A 1 153 ? -31.25600 33.72500 42.31300 1.000 27.67558  ? 153 LEU A HB2  1 
ATOM   2408 H  HB3  . LEU A 1 153 ? -30.48400 35.07400 41.98100 1.000 27.67558  ? 153 LEU A HB3  1 
ATOM   2409 H  HG   . LEU A 1 153 ? -31.06100 33.23800 39.93800 1.000 28.13558  ? 153 LEU A HG   1 
ATOM   2410 H  HD11 . LEU A 1 153 ? -33.00500 34.38700 39.39500 1.000 30.12558  ? 153 LEU A HD11 1 
ATOM   2411 H  HD12 . LEU A 1 153 ? -33.12800 33.74700 40.84300 1.000 30.12558  ? 153 LEU A HD12 1 
ATOM   2412 H  HD13 . LEU A 1 153 ? -32.82600 35.29800 40.68300 1.000 30.12558  ? 153 LEU A HD13 1 
ATOM   2413 H  HD21 . LEU A 1 153 ? -30.86700 35.12600 38.54000 1.000 33.12558  ? 153 LEU A HD21 1 
ATOM   2414 H  HD22 . LEU A 1 153 ? -30.53800 36.01300 39.81600 1.000 33.12558  ? 153 LEU A HD22 1 
ATOM   2415 H  HD23 . LEU A 1 153 ? -29.52800 34.87600 39.35600 1.000 33.12558  ? 153 LEU A HD23 1 
ATOM   2416 N  N    . ALA A 1 154 ? -29.08000 33.20700 44.29500 1.000 23.05175  ? 154 ALA A N    1 
ATOM   2417 C  CA   . ALA A 1 154 ? -28.48400 33.51800 45.58800 1.000 22.60101  ? 154 ALA A CA   1 
ATOM   2418 C  C    . ALA A 1 154 ? -27.03600 33.04700 45.66400 1.000 20.82945  ? 154 ALA A C    1 
ATOM   2419 O  O    . ALA A 1 154 ? -26.15500 33.79400 46.11600 1.000 28.02970  ? 154 ALA A O    1 
ATOM   2420 C  CB   . ALA A 1 154 ? -29.31200 32.88100 46.70300 1.000 24.77594  ? 154 ALA A CB   1 
ATOM   2421 H  H    . ALA A 1 154 ? -29.73600 32.65200 44.32000 1.000 27.55558  ? 154 ALA A H    1 
ATOM   2422 H  HA   . ALA A 1 154 ? -28.49000 34.48100 45.70800 1.000 26.75558  ? 154 ALA A HA   1 
ATOM   2423 H  HB1  . ALA A 1 154 ? -28.91100 33.10200 47.55900 1.000 29.49558  ? 154 ALA A HB1  1 
ATOM   2424 H  HB2  . ALA A 1 154 ? -30.21700 33.22800 46.66200 1.000 29.49558  ? 154 ALA A HB2  1 
ATOM   2425 H  HB3  . ALA A 1 154 ? -29.32000 31.91900 46.58000 1.000 29.49558  ? 154 ALA A HB3  1 
ATOM   2426 N  N    . TYR A 1 155 ? -26.77100 31.80100 45.25800 1.000 22.03347  ? 155 TYR A N    1 
ATOM   2427 C  CA   . TYR A 1 155 ? -25.41400 31.27200 45.34600 1.000 22.97536  ? 155 TYR A CA   1 
ATOM   2428 C  C    . TYR A 1 155 ? -24.46000 32.05000 44.43800 1.000 31.75331  ? 155 TYR A C    1 
ATOM   2429 O  O    . TYR A 1 155 ? -23.29200 32.26800 44.78400 1.000 28.20077  ? 155 TYR A O    1 
ATOM   2430 C  CB   . TYR A 1 155 ? -25.38700 29.79400 44.96600 1.000 22.42457  ? 155 TYR A CB   1 
ATOM   2431 C  CG   . TYR A 1 155 ? -25.83400 28.84600 46.05400 1.000 22.63398  ? 155 TYR A CG   1 
ATOM   2432 C  CD1  . TYR A 1 155 ? -25.08400 28.68200 47.21800 1.000 25.05347  ? 155 TYR A CD1  1 
ATOM   2433 C  CD2  . TYR A 1 155 ? -26.98100 28.10200 45.90700 1.000 22.61133  ? 155 TYR A CD2  1 
ATOM   2434 C  CE1  . TYR A 1 155 ? -25.49400 27.79300 48.21500 1.000 23.24316  ? 155 TYR A CE1  1 
ATOM   2435 C  CE2  . TYR A 1 155 ? -27.39600 27.22600 46.89500 1.000 21.33841  ? 155 TYR A CE2  1 
ATOM   2436 C  CZ   . TYR A 1 155 ? -26.64700 27.07200 48.03700 1.000 21.34035  ? 155 TYR A CZ   1 
ATOM   2437 O  OH   . TYR A 1 155 ? -27.10400 26.18100 48.98700 1.000 23.90925  ? 155 TYR A OH   1 
ATOM   2438 H  H    . TYR A 1 155 ? -27.35000 31.25400 44.93400 1.000 26.75558  ? 155 TYR A H    1 
ATOM   2439 H  HA   . TYR A 1 155 ? -25.11700 31.35600 46.26600 1.000 27.95558  ? 155 TYR A HA   1 
ATOM   2440 H  HB2  . TYR A 1 155 ? -25.97400 29.66200 44.20500 1.000 27.65558  ? 155 TYR A HB2  1 
ATOM   2441 H  HB3  . TYR A 1 155 ? -24.47700 29.55500 44.72800 1.000 27.65558  ? 155 TYR A HB3  1 
ATOM   2442 H  HD1  . TYR A 1 155 ? -24.30100 29.17000 47.33200 1.000 30.71558  ? 155 TYR A HD1  1 
ATOM   2443 H  HD2  . TYR A 1 155 ? -27.48700 28.18900 45.13100 1.000 28.13558  ? 155 TYR A HD2  1 
ATOM   2444 H  HE1  . TYR A 1 155 ? -24.99100 27.69100 48.99100 1.000 28.55558  ? 155 TYR A HE1  1 
ATOM   2445 H  HE2  . TYR A 1 155 ? -28.18200 26.74100 46.78600 1.000 26.58558  ? 155 TYR A HE2  1 
ATOM   2446 H  HH   . TYR A 1 155 ? -26.58300 26.17200 49.64600 1.000 29.42558  ? 155 TYR A HH   1 
ATOM   2447 N  N    . CYS A 1 156 ? -24.93900 32.46600 43.26900 1.000 26.67472  ? 156 CYS A N    1 
ATOM   2448 C  CA   . CYS A 1 156 ? -24.11000 33.23300 42.33800 1.000 26.70723  ? 156 CYS A CA   1 
ATOM   2449 C  C    . CYS A 1 156 ? -24.04300 34.71900 42.65600 1.000 33.74156  ? 156 CYS A C    1 
ATOM   2450 O  O    . CYS A 1 156 ? -23.33600 35.45100 41.95500 1.000 32.15151  ? 156 CYS A O    1 
ATOM   2451 C  CB   . CYS A 1 156 ? -24.62600 33.06100 40.90700 1.000 27.32005  ? 156 CYS A CB   1 
ATOM   2452 S  SG   . CYS A 1 156 ? -24.47700 31.38000 40.31200 1.000 29.30570  ? 156 CYS A SG   1 
ATOM   2453 H  H    . CYS A 1 156 ? -25.73900 32.31800 42.99100 1.000 32.17558  ? 156 CYS A H    1 
ATOM   2454 H  HA   . CYS A 1 156 ? -23.20800 32.87800 42.39100 1.000 31.94558  ? 156 CYS A HA   1 
ATOM   2455 H  HB2  . CYS A 1 156 ? -25.56400 33.30700 40.87800 1.000 32.86558  ? 156 CYS A HB2  1 
ATOM   2456 H  HB3  . CYS A 1 156 ? -24.11500 33.63500 40.31600 1.000 32.86558  ? 156 CYS A HB3  1 
ATOM   2457 H  HG   . CYS A 1 156 ? -25.12200 30.65700 41.01900 1.000 35.75558  ? 156 CYS A HG   1 
ATOM   2458 N  N    . ASN A 1 157 ? -24.75200 35.18200 43.68100 1.000 27.12146  ? 157 ASN A N    1 
ATOM   2459 C  CA   . ASN A 1 157 ? -24.80700 36.60200 44.01700 1.000 28.21402  ? 157 ASN A CA   1 
ATOM   2460 C  C    . ASN A 1 157 ? -25.28700 37.42400 42.83000 1.000 34.93455  ? 157 ASN A C    1 
ATOM   2461 O  O    . ASN A 1 157 ? -24.73800 38.48200 42.50500 1.000 31.72994  ? 157 ASN A O    1 
ATOM   2462 C  CB   . ASN A 1 157 ? -23.44900 37.07500 44.51700 1.000 39.04689  ? 157 ASN A CB   1 
ATOM   2463 C  CG   . ASN A 1 157 ? -23.32600 36.92400 45.99800 1.000 62.20396  ? 157 ASN A CG   1 
ATOM   2464 O  OD1  . ASN A 1 157 ? -22.66000 36.00600 46.47500 1.000 44.80757  ? 157 ASN A OD1  1 
ATOM   2465 N  ND2  . ASN A 1 157 ? -23.95100 37.84000 46.74600 1.000 43.30402  ? 157 ASN A ND2  1 
ATOM   2466 H  H    . ASN A 1 157 ? -25.21900 34.68600 44.20600 1.000 31.48558  ? 157 ASN A H    1 
ATOM   2467 H  HA   . ASN A 1 157 ? -25.45100 36.74100 44.72800 1.000 31.94558  ? 157 ASN A HA   1 
ATOM   2468 H  HB2  . ASN A 1 157 ? -22.75200 36.54800 44.09700 1.000 44.48558  ? 157 ASN A HB2  1 
ATOM   2469 H  HB3  . ASN A 1 157 ? -23.33500 38.01300 44.29500 1.000 44.48558  ? 157 ASN A HB3  1 
ATOM   2470 H  HD21 . ASN A 1 157 ? -24.39500 38.47300 46.36900 1.000 48.74558  ? 157 ASN A HD21 1 
ATOM   2471 H  HD22 . ASN A 1 157 ? -23.90900 37.79500 47.60400 1.000 48.74558  ? 157 ASN A HD22 1 
ATOM   2472 N  N    . LYS A 1 158 ? -26.32700 36.93800 42.18200 1.000 28.58566  ? 158 LYS A N    1 
ATOM   2473 C  CA   . LYS A 1 158 ? -26.98500 37.64500 41.09600 1.000 28.40392  ? 158 LYS A CA   1 
ATOM   2474 C  C    . LYS A 1 158 ? -28.41000 37.95500 41.52400 1.000 31.83593  ? 158 LYS A C    1 
ATOM   2475 O  O    . LYS A 1 158 ? -29.06000 37.12900 42.16100 1.000 32.48732  ? 158 LYS A O    1 
ATOM   2476 C  CB   . LYS A 1 158 ? -26.99400 36.80700 39.82500 1.000 31.81867  ? 158 LYS A CB   1 
ATOM   2477 C  CG   . LYS A 1 158 ? -25.63400 36.64600 39.20100 1.000 37.60756  ? 158 LYS A CG   1 
ATOM   2478 C  CD   . LYS A 1 158 ? -25.20100 37.93500 38.52600 1.000 45.83694  ? 158 LYS A CD   1 
ATOM   2479 C  CE   . LYS A 1 158 ? -23.82200 37.81100 37.92200 1.000 51.13719  ? 158 LYS A CE   1 
ATOM   2480 N  NZ   . LYS A 1 158 ? -22.78600 37.91900 38.98300 1.000 55.92168  ? 158 LYS A NZ   1 
ATOM   2481 H  H    . LYS A 1 158 ? -26.68300 36.17500 42.35700 1.000 32.42558  ? 158 LYS A H    1 
ATOM   2482 H  HA   . LYS A 1 158 ? -26.52300 38.47500 40.90100 1.000 31.82558  ? 158 LYS A HA   1 
ATOM   2483 H  HB2  . LYS A 1 158 ? -27.33100 35.92200 40.03600 1.000 36.56558  ? 158 LYS A HB2  1 
ATOM   2484 H  HB3  . LYS A 1 158 ? -27.57100 37.23500 39.17300 1.000 36.56558  ? 158 LYS A HB3  1 
ATOM   2485 H  HG2  . LYS A 1 158 ? -24.98600 36.42400 39.88700 1.000 43.62558  ? 158 LYS A HG2  1 
ATOM   2486 H  HG3  . LYS A 1 158 ? -25.66400 35.94300 38.53300 1.000 43.62558  ? 158 LYS A HG3  1 
ATOM   2487 H  HD2  . LYS A 1 158 ? -25.82600 38.15200 37.81700 1.000 52.70558  ? 158 LYS A HD2  1 
ATOM   2488 H  HD3  . LYS A 1 158 ? -25.18300 38.65000 39.18200 1.000 52.70558  ? 158 LYS A HD3  1 
ATOM   2489 H  HE2  . LYS A 1 158 ? -23.73300 36.94900 37.48700 1.000 59.12558  ? 158 LYS A HE2  1 
ATOM   2490 H  HE3  . LYS A 1 158 ? -23.68200 38.52400 37.27800 1.000 59.12558  ? 158 LYS A HE3  1 
ATOM   2491 H  HZ1  . LYS A 1 158 ? -21.98200 37.74400 38.64300 1.000 64.68558  ? 158 LYS A HZ1  1 
ATOM   2492 H  HZ2  . LYS A 1 158 ? -22.78300 38.74100 39.32400 1.000 64.68558  ? 158 LYS A HZ2  1 
ATOM   2493 H  HZ3  . LYS A 1 158 ? -22.95600 37.33700 39.63500 1.000 64.68558  ? 158 LYS A HZ3  1 
ATOM   2494 N  N    . THR A 1 159 ? -28.88500 39.14500 41.19900 1.000 30.87399  ? 159 THR A N    1 
ATOM   2495 C  CA   . THR A 1 159 ? -30.28500 39.45200 41.44000 1.000 32.68703  ? 159 THR A CA   1 
ATOM   2496 C  C    . THR A 1 159 ? -31.10500 39.14500 40.19800 1.000 30.77451  ? 159 THR A C    1 
ATOM   2497 O  O    . THR A 1 159 ? -30.59100 39.06900 39.07700 1.000 32.74680  ? 159 THR A O    1 
ATOM   2498 C  CB   . THR A 1 159 ? -30.48100 40.91400 41.82300 1.000 38.54198  ? 159 THR A CB   1 
ATOM   2499 O  OG1  . THR A 1 159 ? -30.00300 41.74300 40.76500 1.000 41.03534  ? 159 THR A OG1  1 
ATOM   2500 C  CG2  . THR A 1 159 ? -29.73200 41.21800 43.10800 1.000 46.67610  ? 159 THR A CG2  1 
ATOM   2501 H  H    . THR A 1 159 ? -28.42600 39.78000 40.84500 1.000 33.59558  ? 159 THR A H    1 
ATOM   2502 H  HA   . THR A 1 159 ? -30.60000 38.90900 42.17900 1.000 35.37558  ? 159 THR A HA   1 
ATOM   2503 H  HB   . THR A 1 159 ? -31.42100 41.10300 41.97100 1.000 41.04558  ? 159 THR A HB   1 
ATOM   2504 H  HG1  . THR A 1 159 ? -30.10000 42.55300 40.96800 1.000 43.39558  ? 159 THR A HG1  1 
ATOM   2505 H  HG21 . THR A 1 159 ? -29.87100 42.14400 43.36100 1.000 50.43558  ? 159 THR A HG21 1 
ATOM   2506 H  HG22 . THR A 1 159 ? -30.05300 40.64500 43.82200 1.000 50.43558  ? 159 THR A HG22 1 
ATOM   2507 H  HG23 . THR A 1 159 ? -28.78300 41.06500 42.98200 1.000 50.43558  ? 159 THR A HG23 1 
ATOM   2508 N  N    . VAL A 1 160 ? -32.40700 38.97100 40.40600 1.000 31.04634  ? 160 VAL A N    1 
ATOM   2509 C  CA   . VAL A 1 160 ? -33.30800 38.82600 39.27100 1.000 31.19078  ? 160 VAL A CA   1 
ATOM   2510 C  C    . VAL A 1 160 ? -33.14100 40.02600 38.34700 1.000 35.86443  ? 160 VAL A C    1 
ATOM   2511 O  O    . VAL A 1 160 ? -33.17900 41.18300 38.78800 1.000 37.81429  ? 160 VAL A O    1 
ATOM   2512 C  CB   . VAL A 1 160 ? -34.75200 38.68900 39.77200 1.000 33.94065  ? 160 VAL A CB   1 
ATOM   2513 C  CG1  . VAL A 1 160 ? -35.74000 38.78400 38.62500 1.000 37.33536  ? 160 VAL A CG1  1 
ATOM   2514 C  CG2  . VAL A 1 160 ? -34.92100 37.37300 40.50200 1.000 33.25092  ? 160 VAL A CG2  1 
ATOM   2515 H  H    . VAL A 1 160 ? -32.78500 38.93400 41.17700 1.000 33.60558  ? 160 VAL A H    1 
ATOM   2516 H  HA   . VAL A 1 160 ? -33.08200 38.02500 38.77300 1.000 33.81558  ? 160 VAL A HA   1 
ATOM   2517 H  HB   . VAL A 1 160 ? -34.94000 39.41700 40.38500 1.000 36.92558  ? 160 VAL A HB   1 
ATOM   2518 H  HG11 . VAL A 1 160 ? -36.60700 38.47200 38.92900 1.000 40.74558  ? 160 VAL A HG11 1 
ATOM   2519 H  HG12 . VAL A 1 160 ? -35.80300 39.70800 38.33900 1.000 40.74558  ? 160 VAL A HG12 1 
ATOM   2520 H  HG13 . VAL A 1 160 ? -35.42700 38.23100 37.89300 1.000 40.74558  ? 160 VAL A HG13 1 
ATOM   2521 H  HG21 . VAL A 1 160 ? -35.75300 37.39200 41.00000 1.000 37.02558  ? 160 VAL A HG21 1 
ATOM   2522 H  HG22 . VAL A 1 160 ? -34.94100 36.65200 39.85200 1.000 37.02558  ? 160 VAL A HG22 1 
ATOM   2523 H  HG23 . VAL A 1 160 ? -34.17500 37.25000 41.10900 1.000 37.02558  ? 160 VAL A HG23 1 
ATOM   2524 N  N    . GLY A 1 161 ? -32.94800 39.75600 37.05500 1.000 35.23010  ? 161 GLY A N    1 
ATOM   2525 C  CA   . GLY A 1 161 ? -32.78300 40.78900 36.05700 1.000 34.51173  ? 161 GLY A CA   1 
ATOM   2526 C  C    . GLY A 1 161 ? -31.34400 41.12300 35.71700 1.000 37.86622  ? 161 GLY A C    1 
ATOM   2527 O  O    . GLY A 1 161 ? -31.08400 41.73200 34.66700 1.000 39.64881  ? 161 GLY A O    1 
ATOM   2528 H  H    . GLY A 1 161 ? -32.90800 38.95900 36.73400 1.000 38.02558  ? 161 GLY A H    1 
ATOM   2529 H  HA2  . GLY A 1 161 ? -33.22200 40.50400 35.24000 1.000 36.31558  ? 161 GLY A HA2  1 
ATOM   2530 H  HA3  . GLY A 1 161 ? -33.20800 41.60000 36.37700 1.000 36.31558  ? 161 GLY A HA3  1 
ATOM   2531 N  N    . GLU A 1 162 ? -30.40800 40.73000 36.56300 1.000 35.16420  ? 162 GLU A N    1 
ATOM   2532 C  CA   . GLU A 1 162 ? -29.00200 41.03700 36.36100 1.000 35.88272  ? 162 GLU A CA   1 
ATOM   2533 C  C    . GLU A 1 162 ? -28.41600 40.13500 35.28100 1.000 36.54483  ? 162 GLU A C    1 
ATOM   2534 O  O    . GLU A 1 162 ? -28.76000 38.95500 35.18800 1.000 35.92654  ? 162 GLU A O    1 
ATOM   2535 C  CB   . GLU A 1 162 ? -28.26000 40.84800 37.67500 1.000 36.60796  ? 162 GLU A CB   1 
ATOM   2536 C  CG   . GLU A 1 162 ? -26.78800 41.17700 37.64200 1.000 50.41900  ? 162 GLU A CG   1 
ATOM   2537 C  CD   . GLU A 1 162 ? -26.19300 41.32800 39.03900 1.000 52.36456  ? 162 GLU A CD   1 
ATOM   2538 O  OE1  . GLU A 1 162 ? -26.91400 41.09800 40.05100 1.000 40.87391  ? 162 GLU A OE1  1 
ATOM   2539 O  OE2  . GLU A 1 162 ? -24.99700 41.68200 39.12100 1.000 59.90991  ? 162 GLU A OE2  1 
ATOM   2540 H  H    . GLU A 1 162 ? -30.56300 40.27600 37.27700 1.000 37.50558  ? 162 GLU A H    1 
ATOM   2541 H  HA   . GLU A 1 162 ? -28.89100 41.95500 36.06900 1.000 38.26558  ? 162 GLU A HA   1 
ATOM   2542 H  HB2  . GLU A 1 162 ? -28.66900 41.42200 38.34200 1.000 39.31558  ? 162 GLU A HB2  1 
ATOM   2543 H  HB3  . GLU A 1 162 ? -28.34200 39.91900 37.94100 1.000 39.31558  ? 162 GLU A HB3  1 
ATOM   2544 H  HG2  . GLU A 1 162 ? -26.31300 40.46300 37.18800 1.000 55.68558  ? 162 GLU A HG2  1 
ATOM   2545 H  HG3  . GLU A 1 162 ? -26.66000 42.01400 37.16800 1.000 55.68558  ? 162 GLU A HG3  1 
ATOM   2546 N  N    . LEU A 1 163 ? -27.52600 40.69500 34.46300 1.000 37.14784  ? 163 LEU A N    1 
ATOM   2547 C  CA   . LEU A 1 163 ? -26.88700 39.91400 33.41000 1.000 37.78927  ? 163 LEU A CA   1 
ATOM   2548 C  C    . LEU A 1 163 ? -26.00300 38.84500 34.03100 1.000 36.70155  ? 163 LEU A C    1 
ATOM   2549 O  O    . LEU A 1 163 ? -25.27300 39.10700 34.99300 1.000 39.59865  ? 163 LEU A O    1 
ATOM   2550 C  CB   . LEU A 1 163 ? -26.05700 40.82200 32.50400 1.000 41.65998  ? 163 LEU A CB   1 
ATOM   2551 C  CG   . LEU A 1 163 ? -26.85700 41.93500 31.81000 1.000 79.18683  ? 163 LEU A CG   1 
ATOM   2552 C  CD1  . LEU A 1 163 ? -26.13200 42.41000 30.56000 1.000 63.14014  ? 163 LEU A CD1  1 
ATOM   2553 C  CD2  . LEU A 1 163 ? -28.29000 41.52100 31.44300 1.000 69.18371  ? 163 LEU A CD2  1 
ATOM   2554 H  H    . LEU A 1 163 ? -27.27800 41.51700 34.49700 1.000 40.21558  ? 163 LEU A H    1 
ATOM   2555 H  HA   . LEU A 1 163 ? -27.56100 39.48400 32.86100 1.000 41.62558  ? 163 LEU A HA   1 
ATOM   2556 H  HB2  . LEU A 1 163 ? -25.36800 41.24600 33.03900 1.000 45.55558  ? 163 LEU A HB2  1 
ATOM   2557 H  HB3  . LEU A 1 163 ? -25.65000 40.27700 31.81100 1.000 45.55558  ? 163 LEU A HB3  1 
ATOM   2558 H  HG   . LEU A 1 163 ? -26.93100 42.66300 32.44700 1.000 89.55558  ? 163 LEU A HG   1 
ATOM   2559 H  HD11 . LEU A 1 163 ? -26.65500 43.11100 30.14000 1.000 69.85558  ? 163 LEU A HD11 1 
ATOM   2560 H  HD12 . LEU A 1 163 ? -25.26100 42.75300 30.81200 1.000 69.85558  ? 163 LEU A HD12 1 
ATOM   2561 H  HD13 . LEU A 1 163 ? -26.03000 41.66300 29.95100 1.000 69.85558  ? 163 LEU A HD13 1 
ATOM   2562 H  HD21 . LEU A 1 163 ? -28.71500 42.24700 30.96100 1.000 77.79558  ? 163 LEU A HD21 1 
ATOM   2563 H  HD22 . LEU A 1 163 ? -28.25600 40.72800 30.88500 1.000 77.79558  ? 163 LEU A HD22 1 
ATOM   2564 H  HD23 . LEU A 1 163 ? -28.78200 41.33100 32.25800 1.000 77.79558  ? 163 LEU A HD23 1 
ATOM   2565 N  N    . GLY A 1 164 ? -26.08200 37.63500 33.48900 1.000 31.97665  ? 164 GLY A N    1 
ATOM   2566 C  CA   . GLY A 1 164 ? -25.26700 36.53500 33.96700 1.000 26.90665  ? 164 GLY A CA   1 
ATOM   2567 C  C    . GLY A 1 164 ? -24.51500 35.85800 32.84000 1.000 30.94411  ? 164 GLY A C    1 
ATOM   2568 O  O    . GLY A 1 164 ? -24.91700 35.90400 31.67600 1.000 30.60308  ? 164 GLY A O    1 
ATOM   2569 H  H    . GLY A 1 164 ? -26.60400 37.42800 32.83800 1.000 36.27558  ? 164 GLY A H    1 
ATOM   2570 H  HA2  . GLY A 1 164 ? -24.62300 36.86600 34.61100 1.000 30.84558  ? 164 GLY A HA2  1 
ATOM   2571 H  HA3  . GLY A 1 164 ? -25.83400 35.87600 34.39700 1.000 30.84558  ? 164 GLY A HA3  1 
ATOM   2572 N  N    . ASP A 1 165 ? -23.39800 35.23000 33.20900 1.000 27.64779  ? 165 ASP A N    1 
ATOM   2573 C  CA   . ASP A 1 165 ? -22.55900 34.45500 32.30100 1.000 27.10499  ? 165 ASP A CA   1 
ATOM   2574 C  C    . ASP A 1 165 ? -22.76300 32.97200 32.59300 1.000 28.92915  ? 165 ASP A C    1 
ATOM   2575 O  O    . ASP A 1 165 ? -22.73300 32.55400 33.75300 1.000 25.56499  ? 165 ASP A O    1 
ATOM   2576 C  CB   . ASP A 1 165 ? -21.09300 34.86400 32.48400 1.000 28.15705  ? 165 ASP A CB   1 
ATOM   2577 C  CG   . ASP A 1 165 ? -20.14400 34.07800 31.61700 1.000 37.29443  ? 165 ASP A CG   1 
ATOM   2578 O  OD1  . ASP A 1 165 ? -20.00400 34.38300 30.41400 1.000 41.80574  ? 165 ASP A OD1  1 
ATOM   2579 O  OD2  . ASP A 1 165 ? -19.50700 33.15800 32.15600 1.000 31.94494  ? 165 ASP A OD2  1 
ATOM   2580 H  H    . ASP A 1 165 ? -23.09500 35.24100 34.01400 1.000 32.26558  ? 165 ASP A H    1 
ATOM   2581 H  HA   . ASP A 1 165 ? -22.80500 34.60800 31.37600 1.000 31.80558  ? 165 ASP A HA   1 
ATOM   2582 H  HB2  . ASP A 1 165 ? -20.99800 35.80200 32.25500 1.000 32.76558  ? 165 ASP A HB2  1 
ATOM   2583 H  HB3  . ASP A 1 165 ? -20.84000 34.72100 33.40900 1.000 32.76558  ? 165 ASP A HB3  1 
ATOM   2584 N  N    . VAL A 1 166 ? -22.96900 32.17500 31.53700 1.000 24.72697  ? 166 VAL A N    1 
ATOM   2585 C  CA   . VAL A 1 166 ? -23.26600 30.75900 31.73100 1.000 23.80422  ? 166 VAL A CA   1 
ATOM   2586 C  C    . VAL A 1 166 ? -22.06100 30.01900 32.30200 1.000 22.93245  ? 166 VAL A C    1 
ATOM   2587 O  O    . VAL A 1 166 ? -22.20100 29.18800 33.21400 1.000 24.80207  ? 166 VAL A O    1 
ATOM   2588 C  CB   . VAL A 1 166 ? -23.74500 30.12500 30.40400 1.000 27.03371  ? 166 VAL A CB   1 
ATOM   2589 C  CG1  . VAL A 1 166 ? -23.66800 28.62300 30.48800 1.000 30.71477  ? 166 VAL A CG1  1 
ATOM   2590 C  CG2  . VAL A 1 166 ? -25.16600 30.55500 30.13500 1.000 26.57714  ? 166 VAL A CG2  1 
ATOM   2591 H  H    . VAL A 1 166 ? -22.94200 32.42800 30.71500 1.000 29.57558  ? 166 VAL A H    1 
ATOM   2592 H  HA   . VAL A 1 166 ? -23.98600 30.69000 32.37700 1.000 28.75558  ? 166 VAL A HA   1 
ATOM   2593 H  HB   . VAL A 1 166 ? -23.17700 30.41900 29.67500 1.000 32.56558  ? 166 VAL A HB   1 
ATOM   2594 H  HG11 . VAL A 1 166 ? -24.21200 28.23900 29.78300 1.000 37.01558  ? 166 VAL A HG11 1 
ATOM   2595 H  HG12 . VAL A 1 166 ? -22.74400 28.34800 30.38100 1.000 37.01558  ? 166 VAL A HG12 1 
ATOM   2596 H  HG13 . VAL A 1 166 ? -23.99900 28.33800 31.35400 1.000 37.01558  ? 166 VAL A HG13 1 
ATOM   2597 H  HG21 . VAL A 1 166 ? -25.42400 30.25700 29.24900 1.000 32.03558  ? 166 VAL A HG21 1 
ATOM   2598 H  HG22 . VAL A 1 166 ? -25.74800 30.15600 30.80100 1.000 32.03558  ? 166 VAL A HG22 1 
ATOM   2599 H  HG23 . VAL A 1 166 ? -25.21900 31.52200 30.18800 1.000 32.03558  ? 166 VAL A HG23 1 
ATOM   2600 N  N    . ARG A 1 167 ? -20.85600 30.30600 31.79800 1.000 24.79552  ? 167 ARG A N    1 
ATOM   2601 C  CA   . ARG A 1 167 ? -19.67700 29.60600 32.30700 1.000 23.64759  ? 167 ARG A CA   1 
ATOM   2602 C  C    . ARG A 1 167 ? -19.48900 29.87800 33.79600 1.000 24.43984  ? 167 ARG A C    1 
ATOM   2603 O  O    . ARG A 1 167 ? -19.22800 28.96300 34.58400 1.000 25.04205  ? 167 ARG A O    1 
ATOM   2604 C  CB   . ARG A 1 167 ? -18.43100 30.03900 31.53800 1.000 26.42872  ? 167 ARG A CB   1 
ATOM   2605 C  CG   . ARG A 1 167 ? -17.20200 29.21600 31.87200 1.000 27.02908  ? 167 ARG A CG   1 
ATOM   2606 C  CD   . ARG A 1 167 ? -15.94900 30.06200 32.00500 1.000 30.89579  ? 167 ARG A CD   1 
ATOM   2607 N  NE   . ARG A 1 167 ? -15.90800 30.72500 33.30100 1.000 35.28136  ? 167 ARG A NE   1 
ATOM   2608 C  CZ   . ARG A 1 167 ? -15.36700 30.22100 34.39600 1.000 34.24253  ? 167 ARG A CZ   1 
ATOM   2609 N  NH1  . ARG A 1 167 ? -14.74000 29.05600 34.38700 1.000 32.70890  ? 167 ARG A NH1  1 
ATOM   2610 N  NH2  . ARG A 1 167 ? -15.49900 30.88300 35.54200 1.000 39.08778  ? 167 ARG A NH2  1 
ATOM   2611 H  H    . ARG A 1 167 ? -20.70000 30.88400 31.18100 1.000 29.69558  ? 167 ARG A H    1 
ATOM   2612 H  HA   . ARG A 1 167 ? -19.79900 28.65300 32.17300 1.000 28.21558  ? 167 ARG A HA   1 
ATOM   2613 H  HB2  . ARG A 1 167 ? -18.60200 29.94700 30.58800 1.000 31.19558  ? 167 ARG A HB2  1 
ATOM   2614 H  HB3  . ARG A 1 167 ? -18.23700 30.96400 31.75200 1.000 31.19558  ? 167 ARG A HB3  1 
ATOM   2615 H  HG2  . ARG A 1 167 ? -17.34600 28.75900 32.71600 1.000 31.67558  ? 167 ARG A HG2  1 
ATOM   2616 H  HG3  . ARG A 1 167 ? -17.05300 28.56800 31.16600 1.000 31.67558  ? 167 ARG A HG3  1 
ATOM   2617 H  HD2  . ARG A 1 167 ? -15.16600 29.49500 31.92400 1.000 36.00558  ? 167 ARG A HD2  1 
ATOM   2618 H  HD3  . ARG A 1 167 ? -15.94100 30.74000 31.31100 1.000 36.00558  ? 167 ARG A HD3  1 
ATOM   2619 H  HE   . ARG A 1 167 ? -16.26400 31.50600 33.35700 1.000 41.34558  ? 167 ARG A HE   1 
ATOM   2620 H  HH11 . ARG A 1 167 ? -14.67700 28.60800 33.65600 1.000 38.02558  ? 167 ARG A HH11 1 
ATOM   2621 H  HH12 . ARG A 1 167 ? -14.39500 28.74800 35.11200 1.000 38.02558  ? 167 ARG A HH12 1 
ATOM   2622 H  HH21 . ARG A 1 167 ? -15.93100 31.62600 35.56300 1.000 45.89558  ? 167 ARG A HH21 1 
ATOM   2623 H  HH22 . ARG A 1 167 ? -15.15300 30.56800 36.26400 1.000 45.89558  ? 167 ARG A HH22 1 
ATOM   2624 N  N    . GLU A 1 168 ? -19.65000 31.13400 34.19700 1.000 24.77408  ? 168 GLU A N    1 
ATOM   2625 C  CA   . GLU A 1 168 ? -19.50400 31.49200 35.61000 1.000 25.22957  ? 168 GLU A CA   1 
ATOM   2626 C  C    . GLU A 1 168 ? -20.57600 30.83400 36.46500 1.000 24.67160  ? 168 GLU A C    1 
ATOM   2627 O  O    . GLU A 1 168 ? -20.29200 30.35000 37.57300 1.000 25.01109  ? 168 GLU A O    1 
ATOM   2628 C  CB   . GLU A 1 168 ? -19.54400 33.01100 35.74800 1.000 27.00769  ? 168 GLU A CB   1 
ATOM   2629 C  CG   . GLU A 1 168 ? -19.24200 33.49800 37.15100 1.000 29.00656  ? 168 GLU A CG   1 
ATOM   2630 C  CD   . GLU A 1 168 ? -17.75800 33.63000 37.42300 1.000 39.80237  ? 168 GLU A CD   1 
ATOM   2631 O  OE1  . GLU A 1 168 ? -16.94000 33.24000 36.55100 1.000 29.69952  ? 168 GLU A OE1  1 
ATOM   2632 O  OE2  . GLU A 1 168 ? -17.41400 34.12100 38.52600 1.000 35.96748  ? 168 GLU A OE2  1 
ATOM   2633 H  H    . GLU A 1 168 ? -19.84100 31.79500 33.68000 1.000 29.59558  ? 168 GLU A H    1 
ATOM   2634 H  HA   . GLU A 1 168 ? -18.64600 31.17700 35.93500 1.000 30.13558  ? 168 GLU A HA   1 
ATOM   2635 H  HB2  . GLU A 1 168 ? -18.88500 33.39700 35.15100 1.000 31.93558  ? 168 GLU A HB2  1 
ATOM   2636 H  HB3  . GLU A 1 168 ? -20.43100 33.32300 35.51000 1.000 31.93558  ? 168 GLU A HB3  1 
ATOM   2637 H  HG2  . GLU A 1 168 ? -19.64700 34.37100 37.27600 1.000 34.15558  ? 168 GLU A HG2  1 
ATOM   2638 H  HG3  . GLU A 1 168 ? -19.60800 32.86700 37.79100 1.000 34.15558  ? 168 GLU A HG3  1 
ATOM   2639 N  N    . THR A 1 169 ? -21.81400 30.80200 35.97500 1.000 22.32337  ? 169 THR A N    1 
ATOM   2640 C  CA   . THR A 1 169 ? -22.89900 30.15300 36.70700 1.000 24.47871  ? 169 THR A CA   1 
ATOM   2641 C  C    . THR A 1 169 ? -22.63100 28.66600 36.89600 1.000 24.70091  ? 169 THR A C    1 
ATOM   2642 O  O    . THR A 1 169 ? -22.81700 28.12400 37.99400 1.000 24.35779  ? 169 THR A O    1 
ATOM   2643 C  CB   . THR A 1 169 ? -24.21800 30.38200 35.96100 1.000 23.04315  ? 169 THR A CB   1 
ATOM   2644 O  OG1  . THR A 1 169 ? -24.46100 31.79300 35.86100 1.000 26.70899  ? 169 THR A OG1  1 
ATOM   2645 C  CG2  . THR A 1 169 ? -25.37000 29.74300 36.66200 1.000 25.01405  ? 169 THR A CG2  1 
ATOM   2646 H  H    . THR A 1 169 ? -22.05200 31.14700 35.22400 1.000 27.14558  ? 169 THR A H    1 
ATOM   2647 H  HA   . THR A 1 169 ? -22.97300 30.54800 37.59000 1.000 29.99558  ? 169 THR A HA   1 
ATOM   2648 H  HB   . THR A 1 169 ? -24.15200 29.98300 35.07900 1.000 28.33558  ? 169 THR A HB   1 
ATOM   2649 H  HG1  . THR A 1 169 ? -23.81500 32.17000 35.47700 1.000 32.49558  ? 169 THR A HG1  1 
ATOM   2650 H  HG21 . THR A 1 169 ? -26.20400 30.04100 36.26800 1.000 30.91558  ? 169 THR A HG21 1 
ATOM   2651 H  HG22 . THR A 1 169 ? -25.31100 28.77800 36.58500 1.000 30.91558  ? 169 THR A HG22 1 
ATOM   2652 H  HG23 . THR A 1 169 ? -25.36200 29.98500 37.60200 1.000 30.91558  ? 169 THR A HG23 1 
ATOM   2653 N  N    . MET A 1 170 ? -22.18600 27.98900 35.84400 1.000 23.34863  ? 170 MET A N    1 
ATOM   2654 C  CA   . MET A 1 170 ? -21.84700 26.57900 35.97700 1.000 27.50602  ? 170 MET A CA   1 
ATOM   2655 C  C    . MET A 1 170 ? -20.70700 26.38300 36.97300 1.000 27.39164  ? 170 MET A C    1 
ATOM   2656 O  O    . MET A 1 170 ? -20.70400 25.41300 37.74700 1.000 26.01063  ? 170 MET A O    1 
ATOM   2657 C  CB   . MET A 1 170 ? -21.47100 26.00700 34.61000 1.000 25.15522  ? 170 MET A CB   1 
ATOM   2658 C  CG   . MET A 1 170 ? -22.58600 25.99200 33.54000 1.000 25.77389  ? 170 MET A CG   1 
ATOM   2659 S  SD   . MET A 1 170 ? -24.18900 25.34400 34.04500 1.000 30.26027  ? 170 MET A SD   1 
ATOM   2660 C  CE   . MET A 1 170 ? -23.83400 23.60200 34.17800 1.000 27.73213  ? 170 MET A CE   1 
ATOM   2661 H  H    . MET A 1 170 ? -22.07400 28.31600 35.05700 1.000 28.57558  ? 170 MET A H    1 
ATOM   2662 H  HA   . MET A 1 170 ? -22.62600 26.09800 36.29600 1.000 33.38558  ? 170 MET A HA   1 
ATOM   2663 H  HB2  . MET A 1 170 ? -20.74100 26.53500 34.25200 1.000 30.28558  ? 170 MET A HB2  1 
ATOM   2664 H  HB3  . MET A 1 170 ? -21.18600 25.08900 34.73600 1.000 30.28558  ? 170 MET A HB3  1 
ATOM   2665 H  HG2  . MET A 1 170 ? -22.73100 26.90500 33.24500 1.000 31.07558  ? 170 MET A HG2  1 
ATOM   2666 H  HG3  . MET A 1 170 ? -22.28300 25.44800 32.79700 1.000 31.07558  ? 170 MET A HG3  1 
ATOM   2667 H  HE1  . MET A 1 170 ? -24.63300 23.13900 34.47300 1.000 33.05558  ? 170 MET A HE1  1 
ATOM   2668 H  HE2  . MET A 1 170 ? -23.55900 23.26900 33.31000 1.000 33.05558  ? 170 MET A HE2  1 
ATOM   2669 H  HE3  . MET A 1 170 ? -23.12000 23.47400 34.82300 1.000 33.05558  ? 170 MET A HE3  1 
ATOM   2670 N  N    A SER A 1 171 ? -19.72400 27.28700 36.97300 0.310 25.35244  ? 171 SER A N    1 
ATOM   2671 N  N    B SER A 1 171 ? -19.72600 27.28600 36.96800 0.690 25.06021  ? 171 SER A N    1 
ATOM   2672 C  CA   A SER A 1 171 ? -18.61400 27.14500 37.91000 0.310 23.32226  ? 171 SER A CA   1 
ATOM   2673 C  CA   B SER A 1 171 ? -18.61400 27.15400 37.90200 0.690 22.99046  ? 171 SER A CA   1 
ATOM   2674 C  C    A SER A 1 171 ? -19.11300 27.16300 39.35100 0.310 27.60030  ? 171 SER A C    1 
ATOM   2675 C  C    B SER A 1 171 ? -19.10600 27.17200 39.34700 0.690 27.93197  ? 171 SER A C    1 
ATOM   2676 O  O    A SER A 1 171 ? -18.67500 26.35600 40.17800 0.310 26.62507  ? 171 SER A O    1 
ATOM   2677 O  O    B SER A 1 171 ? -18.65700 26.37000 40.17500 0.690 26.59631  ? 171 SER A O    1 
ATOM   2678 C  CB   A SER A 1 171 ? -17.57500 28.24100 37.67500 0.310 30.23832  ? 171 SER A CB   1 
ATOM   2679 C  CB   B SER A 1 171 ? -17.59700 28.26200 37.65400 0.690 30.50859  ? 171 SER A CB   1 
ATOM   2680 O  OG   A SER A 1 171 ? -18.01300 29.49900 38.15700 0.310 30.44821  ? 171 SER A OG   1 
ATOM   2681 O  OG   B SER A 1 171 ? -16.50500 28.14300 38.54200 0.690 31.86140  ? 171 SER A OG   1 
ATOM   2682 H  H    A SER A 1 171 ? -19.67900 27.97200 36.45500 0.310 30.54558  ? 171 SER A H    1 
ATOM   2683 H  H    B SER A 1 171 ? -19.68300 27.96800 36.44600 0.690 30.19558  ? 171 SER A H    1 
ATOM   2684 H  HA   A SER A 1 171 ? -18.17600 26.29300 37.75400 0.310 27.88558  ? 171 SER A HA   1 
ATOM   2685 H  HA   B SER A 1 171 ? -18.16900 26.30500 37.75300 0.690 27.49558  ? 171 SER A HA   1 
ATOM   2686 H  HB2  A SER A 1 171 ? -16.75700 27.99900 38.13600 0.310 35.99558  ? 171 SER A HB2  1 
ATOM   2687 H  HB2  B SER A 1 171 ? -17.27200 28.19500 36.74200 0.690 36.33558  ? 171 SER A HB2  1 
ATOM   2688 H  HB3  A SER A 1 171 ? -17.40900 28.31400 36.72200 0.310 35.99558  ? 171 SER A HB3  1 
ATOM   2689 H  HB3  B SER A 1 171 ? -18.02500 29.12100 37.79100 0.690 36.33558  ? 171 SER A HB3  1 
ATOM   2690 H  HG   A SER A 1 171 ? -18.74000 29.70900 37.79300 0.310 36.36558  ? 171 SER A HG   1 
ATOM   2691 H  HG   B SER A 1 171 ? -15.95600 28.76500 38.40700 0.690 37.67558  ? 171 SER A HG   1 
ATOM   2692 N  N    . TYR A 1 172 ? -20.05100 28.06000 39.66600 1.000 25.30665  ? 172 TYR A N    1 
ATOM   2693 C  CA   . TYR A 1 172 ? -20.62600 28.08700 41.01100 1.000 25.70760  ? 172 TYR A CA   1 
ATOM   2694 C  C    . TYR A 1 172 ? -21.38700 26.80200 41.31600 1.000 28.12517  ? 172 TYR A C    1 
ATOM   2695 O  O    . TYR A 1 172 ? -21.27100 26.23600 42.40600 1.000 29.15472  ? 172 TYR A O    1 
ATOM   2696 C  CB   . TYR A 1 172 ? -21.57600 29.27500 41.15300 1.000 28.66305  ? 172 TYR A CB   1 
ATOM   2697 C  CG   . TYR A 1 172 ? -20.93500 30.57100 41.53800 1.000 28.86936  ? 172 TYR A CG   1 
ATOM   2698 C  CD1  . TYR A 1 172 ? -20.63100 30.84600 42.86800 1.000 36.39057  ? 172 TYR A CD1  1 
ATOM   2699 C  CD2  . TYR A 1 172 ? -20.67000 31.54100 40.59500 1.000 35.11333  ? 172 TYR A CD2  1 
ATOM   2700 C  CE1  . TYR A 1 172 ? -20.06100 32.04500 43.23400 1.000 36.26696  ? 172 TYR A CE1  1 
ATOM   2701 C  CE2  . TYR A 1 172 ? -20.08500 32.74500 40.95400 1.000 39.42920  ? 172 TYR A CE2  1 
ATOM   2702 C  CZ   . TYR A 1 172 ? -19.78900 32.98800 42.27700 1.000 39.58103  ? 172 TYR A CZ   1 
ATOM   2703 O  OH   . TYR A 1 172 ? -19.21600 34.18200 42.64800 1.000 34.50490  ? 172 TYR A OH   1 
ATOM   2704 H  H    A TYR A 1 172 ? -20.36500 28.65300 39.12800 0.310 30.67558  ? 172 TYR A H    1 
ATOM   2705 H  H    B TYR A 1 172 ? -20.37200 28.65000 39.12800 0.690 30.67558  ? 172 TYR A H    1 
ATOM   2706 H  HA   . TYR A 1 172 ? -19.89800 28.18100 41.64500 1.000 31.26558  ? 172 TYR A HA   1 
ATOM   2707 H  HB2  . TYR A 1 172 ? -22.02000 29.41400 40.30100 1.000 34.94558  ? 172 TYR A HB2  1 
ATOM   2708 H  HB3  . TYR A 1 172 ? -22.23000 29.06200 41.83700 1.000 34.94558  ? 172 TYR A HB3  1 
ATOM   2709 H  HD1  . TYR A 1 172 ? -20.81600 30.20900 43.52100 1.000 43.74558  ? 172 TYR A HD1  1 
ATOM   2710 H  HD2  . TYR A 1 172 ? -20.88800 31.38500 39.70400 1.000 42.19558  ? 172 TYR A HD2  1 
ATOM   2711 H  HE1  . TYR A 1 172 ? -19.86000 32.21300 44.12700 1.000 43.17558  ? 172 TYR A HE1  1 
ATOM   2712 H  HE2  . TYR A 1 172 ? -19.89400 33.38500 40.30700 1.000 46.93558  ? 172 TYR A HE2  1 
ATOM   2713 H  HH   . TYR A 1 172 ? -19.10500 34.66900 41.97300 1.000 40.21558  ? 172 TYR A HH   1 
ATOM   2714 N  N    . LEU A 1 173 ? -22.21800 26.35600 40.37900 1.000 24.89663  ? 173 LEU A N    1 
ATOM   2715 C  CA   . LEU A 1 173 ? -22.95600 25.11300 40.58300 1.000 27.79216  ? 173 LEU A CA   1 
ATOM   2716 C  C    . LEU A 1 173 ? -22.00000 23.94500 40.81700 1.000 26.63118  ? 173 LEU A C    1 
ATOM   2717 O  O    . LEU A 1 173 ? -22.21300 23.12900 41.72700 1.000 28.04706  ? 173 LEU A O    1 
ATOM   2718 C  CB   . LEU A 1 173 ? -23.86500 24.85500 39.38400 1.000 27.70913  ? 173 LEU A CB   1 
ATOM   2719 C  CG   . LEU A 1 173 ? -25.04600 25.83800 39.24900 1.000 33.34547  ? 173 LEU A CG   1 
ATOM   2720 C  CD1  . LEU A 1 173 ? -25.73800 25.64100 37.91000 1.000 40.22259  ? 173 LEU A CD1  1 
ATOM   2721 C  CD2  . LEU A 1 173 ? -26.01300 25.67900 40.39800 1.000 46.10562  ? 173 LEU A CD2  1 
ATOM   2722 H  H    . LEU A 1 173 ? -22.37100 26.74700 39.62800 1.000 30.47558  ? 173 LEU A H    1 
ATOM   2723 H  HA   . LEU A 1 173 ? -23.52000 25.19200 41.36800 1.000 33.88558  ? 173 LEU A HA   1 
ATOM   2724 H  HB2  . LEU A 1 173 ? -23.33400 24.92200 38.57500 1.000 33.83558  ? 173 LEU A HB2  1 
ATOM   2725 H  HB3  . LEU A 1 173 ? -24.23500 23.96200 39.46500 1.000 33.83558  ? 173 LEU A HB3  1 
ATOM   2726 H  HG   . LEU A 1 173 ? -24.71100 26.74700 39.28100 1.000 40.92558  ? 173 LEU A HG   1 
ATOM   2727 H  HD11 . LEU A 1 173 ? -26.55300 26.16800 37.89600 1.000 49.13558  ? 173 LEU A HD11 1 
ATOM   2728 H  HD12 . LEU A 1 173 ? -25.14400 25.93200 37.20100 1.000 49.13558  ? 173 LEU A HD12 1 
ATOM   2729 H  HD13 . LEU A 1 173 ? -25.95100 24.70100 37.80000 1.000 49.13558  ? 173 LEU A HD13 1 
ATOM   2730 H  HD21 . LEU A 1 173 ? -26.84000 26.13900 40.18000 1.000 56.33558  ? 173 LEU A HD21 1 
ATOM   2731 H  HD22 . LEU A 1 173 ? -26.18700 24.73500 40.53700 1.000 56.33558  ? 173 LEU A HD22 1 
ATOM   2732 H  HD23 . LEU A 1 173 ? -25.62100 26.06500 41.19700 1.000 56.33558  ? 173 LEU A HD23 1 
ATOM   2733 N  N    . PHE A 1 174 ? -20.91500 23.88100 40.03700 1.000 26.12208  ? 174 PHE A N    1 
ATOM   2734 C  CA   . PHE A 1 174 ? -19.93800 22.80900 40.19400 1.000 27.32137  ? 174 PHE A CA   1 
ATOM   2735 C  C    . PHE A 1 174 ? -19.19800 22.91300 41.52300 1.000 29.59749  ? 174 PHE A C    1 
ATOM   2736 O  O    . PHE A 1 174 ? -18.78900 21.88400 42.08600 1.000 29.09623  ? 174 PHE A O    1 
ATOM   2737 C  CB   . PHE A 1 174 ? -18.93200 22.84200 39.04300 1.000 28.52405  ? 174 PHE A CB   1 
ATOM   2738 C  CG   . PHE A 1 174 ? -19.51800 22.50800 37.69000 1.000 29.63563  ? 174 PHE A CG   1 
ATOM   2739 C  CD1  . PHE A 1 174 ? -20.74800 21.88700 37.55800 1.000 30.87236  ? 174 PHE A CD1  1 
ATOM   2740 C  CD2  . PHE A 1 174 ? -18.81000 22.82000 36.54800 1.000 29.90251  ? 174 PHE A CD2  1 
ATOM   2741 C  CE1  . PHE A 1 174 ? -21.27000 21.60400 36.29700 1.000 32.38814  ? 174 PHE A CE1  1 
ATOM   2742 C  CE2  . PHE A 1 174 ? -19.30800 22.52200 35.29300 1.000 34.42310  ? 174 PHE A CE2  1 
ATOM   2743 C  CZ   . PHE A 1 174 ? -20.53700 21.91600 35.16700 1.000 30.95375  ? 174 PHE A CZ   1 
ATOM   2744 H  H    . PHE A 1 174 ? -20.72500 24.44400 39.41500 1.000 31.18558  ? 174 PHE A H    1 
ATOM   2745 H  HA   . PHE A 1 174 ? -20.40600 21.96000 40.16800 1.000 32.04558  ? 174 PHE A HA   1 
ATOM   2746 H  HB2  . PHE A 1 174 ? -18.55600 23.73400 38.98700 1.000 33.18558  ? 174 PHE A HB2  1 
ATOM   2747 H  HB3  . PHE A 1 174 ? -18.23100 22.19700 39.22700 1.000 33.18558  ? 174 PHE A HB3  1 
ATOM   2748 H  HD1  . PHE A 1 174 ? -21.23100 21.65700 38.31900 1.000 35.95558  ? 174 PHE A HD1  1 
ATOM   2749 H  HD2  . PHE A 1 174 ? -17.98300 23.23900 36.62400 1.000 34.62558  ? 174 PHE A HD2  1 
ATOM   2750 H  HE1  . PHE A 1 174 ? -22.10800 21.20700 36.21600 1.000 37.61558  ? 174 PHE A HE1  1 
ATOM   2751 H  HE2  . PHE A 1 174 ? -18.81300 22.73200 34.53400 1.000 39.90558  ? 174 PHE A HE2  1 
ATOM   2752 H  HZ   . PHE A 1 174 ? -20.87300 21.71600 34.32300 1.000 35.76558  ? 174 PHE A HZ   1 
ATOM   2753 N  N    . GLN A 1 175 ? -18.98900 24.13500 42.02700 1.000 27.94137  ? 175 GLN A N    1 
ATOM   2754 C  CA   . GLN A 1 175 ? -18.35500 24.29800 43.33200 1.000 31.35324  ? 175 GLN A CA   1 
ATOM   2755 C  C    . GLN A 1 175 ? -19.18900 23.65900 44.43800 1.000 31.12485  ? 175 GLN A C    1 
ATOM   2756 O  O    . GLN A 1 175 ? -18.64600 23.27100 45.47700 1.000 31.90318  ? 175 GLN A O    1 
ATOM   2757 C  CB   . GLN A 1 175 ? -18.14000 25.78400 43.64800 1.000 29.91118  ? 175 GLN A CB   1 
ATOM   2758 C  CG   . GLN A 1 175 ? -17.04300 26.46700 42.82300 1.000 42.18342  ? 175 GLN A CG   1 
ATOM   2759 C  CD   . GLN A 1 175 ? -15.63900 26.08500 43.24000 1.000 76.38071  ? 175 GLN A CD   1 
ATOM   2760 O  OE1  . GLN A 1 175 ? -15.44100 25.17500 44.04700 1.000 74.97946  ? 175 GLN A OE1  1 
ATOM   2761 N  NE2  . GLN A 1 175 ? -14.65000 26.78100 42.68500 1.000 78.62187  ? 175 GLN A NE2  1 
ATOM   2762 H  H    . GLN A 1 175 ? -19.20200 24.87200 41.63700 1.000 32.99558  ? 175 GLN A H    1 
ATOM   2763 H  HA   . GLN A 1 175 ? -17.48700 23.86700 43.30400 1.000 36.93558  ? 175 GLN A HA   1 
ATOM   2764 H  HB2  . GLN A 1 175 ? -18.96900 26.25800 43.47800 1.000 35.44558  ? 175 GLN A HB2  1 
ATOM   2765 H  HB3  . GLN A 1 175 ? -17.89600 25.86800 44.58300 1.000 35.44558  ? 175 GLN A HB3  1 
ATOM   2766 H  HG2  . GLN A 1 175 ? -17.15200 26.22000 41.89100 1.000 49.99558  ? 175 GLN A HG2  1 
ATOM   2767 H  HG3  . GLN A 1 175 ? -17.12900 27.42800 42.92300 1.000 49.99558  ? 175 GLN A HG3  1 
ATOM   2768 H  HE21 . GLN A 1 175 ? -14.82800 27.40900 42.12400 1.000 92.99558  ? 175 GLN A HE21 1 
ATOM   2769 H  HE22 . GLN A 1 175 ? -13.83300 26.60400 42.88800 1.000 92.99558  ? 175 GLN A HE22 1 
ATOM   2770 N  N    . HIS A 1 176 ? -20.50600 23.56000 44.23600 1.000 25.92935  ? 176 HIS A N    1 
ATOM   2771 C  CA   . HIS A 1 176 ? -21.43000 22.96500 45.18600 1.000 31.02426  ? 176 HIS A CA   1 
ATOM   2772 C  C    . HIS A 1 176 ? -21.85500 21.56100 44.78000 1.000 28.28463  ? 176 HIS A C    1 
ATOM   2773 O  O    . HIS A 1 176 ? -22.92500 21.09600 45.19200 1.000 27.35655  ? 176 HIS A O    1 
ATOM   2774 C  CB   . HIS A 1 176 ? -22.65200 23.86600 45.34800 1.000 27.40996  ? 176 HIS A CB   1 
ATOM   2775 C  CG   . HIS A 1 176 ? -22.32300 25.20500 45.93700 1.000 34.21988  ? 176 HIS A CG   1 
ATOM   2776 N  ND1  . HIS A 1 176 ? -22.20500 25.40800 47.29600 1.000 42.18744  ? 176 HIS A ND1  1 
ATOM   2777 C  CD2  . HIS A 1 176 ? -22.06100 26.39900 45.35000 1.000 31.37017  ? 176 HIS A CD2  1 
ATOM   2778 C  CE1  . HIS A 1 176 ? -21.90200 26.67700 47.52000 1.000 28.85119  ? 176 HIS A CE1  1 
ATOM   2779 N  NE2  . HIS A 1 176 ? -21.81100 27.29800 46.36000 1.000 39.19583  ? 176 HIS A NE2  1 
ATOM   2780 H  H    . HIS A 1 176 ? -20.89800 23.84400 43.52500 1.000 30.75558  ? 176 HIS A H    1 
ATOM   2781 H  HA   . HIS A 1 176 ? -20.99100 22.89700 46.04800 1.000 36.86558  ? 176 HIS A HA   1 
ATOM   2782 H  HB2  . HIS A 1 176 ? -23.05200 24.01300 44.47700 1.000 33.01558  ? 176 HIS A HB2  1 
ATOM   2783 H  HB3  . HIS A 1 176 ? -23.28800 23.43000 45.93600 1.000 33.01558  ? 176 HIS A HB3  1 
ATOM   2784 H  HD1  . HIS A 1 176 ? -22.31000 24.80600 47.90100 1.000 50.81558  ? 176 HIS A HD1  1 
ATOM   2785 H  HD2  . HIS A 1 176 ? -22.05100 26.57600 44.43700 1.000 38.07558  ? 176 HIS A HD2  1 
ATOM   2786 H  HE1  . HIS A 1 176 ? -21.77500 27.06600 48.35500 1.000 34.84558  ? 176 HIS A HE1  1 
ATOM   2787 N  N    . ALA A 1 177 ? -21.03900 20.87800 43.98200 1.000 30.15419  ? 177 ALA A N    1 
ATOM   2788 C  CA   . ALA A 1 177 ? -21.34900 19.54200 43.50500 1.000 26.93626  ? 177 ALA A CA   1 
ATOM   2789 C  C    . ALA A 1 177 ? -20.22000 18.61500 43.90200 1.000 31.67048  ? 177 ALA A C    1 
ATOM   2790 O  O    . ALA A 1 177 ? -19.11100 19.05500 44.22500 1.000 29.09899  ? 177 ALA A O    1 
ATOM   2791 C  CB   . ALA A 1 177 ? -21.55000 19.50800 41.98300 1.000 27.24307  ? 177 ALA A CB   1 
ATOM   2792 H  H    . ALA A 1 177 ? -20.28400 21.17700 43.69900 1.000 33.36558  ? 177 ALA A H    1 
ATOM   2793 H  HA   . ALA A 1 177 ? -22.17400 19.23200 43.90900 1.000 30.78558  ? 177 ALA A HA   1 
ATOM   2794 H  HB1  . ALA A 1 177 ? -21.75700 18.60000 41.71200 1.000 32.46558  ? 177 ALA A HB1  1 
ATOM   2795 H  HB2  . ALA A 1 177 ? -22.28300 20.09800 41.74800 1.000 32.46558  ? 177 ALA A HB2  1 
ATOM   2796 H  HB3  . ALA A 1 177 ? -20.73400 19.80500 41.55000 1.000 32.46558  ? 177 ALA A HB3  1 
ATOM   2797 N  N    . ASN A 1 178 ? -20.50200 17.32200 43.88600 1.000 30.28303  ? 178 ASN A N    1 
ATOM   2798 C  CA   . ASN A 1 178 ? -19.49000 16.33800 44.26000 1.000 28.65195  ? 178 ASN A CA   1 
ATOM   2799 C  C    . ASN A 1 178 ? -18.75100 15.92800 43.00000 1.000 29.92924  ? 178 ASN A C    1 
ATOM   2800 O  O    . ASN A 1 178 ? -19.21500 15.06700 42.24900 1.000 32.05441  ? 178 ASN A O    1 
ATOM   2801 C  CB   . ASN A 1 178 ? -20.10800 15.12700 44.93800 1.000 34.96615  ? 178 ASN A CB   1 
ATOM   2802 C  CG   . ASN A 1 178 ? -19.04800 14.15700 45.45000 1.000 60.77195  ? 178 ASN A CG   1 
ATOM   2803 O  OD1  . ASN A 1 178 ? -17.88000 14.22600 45.04700 1.000 45.04760  ? 178 ASN A OD1  1 
ATOM   2804 N  ND2  . ASN A 1 178 ? -19.45400 13.23600 46.31600 1.000 63.51624  ? 178 ASN A ND2  1 
ATOM   2805 H  H    . ASN A 1 178 ? -21.26400 16.99000 43.66500 1.000 35.22558  ? 178 ASN A H    1 
ATOM   2806 H  HA   . ASN A 1 178 ? -18.87100 16.75200 44.88100 1.000 32.95558  ? 178 ASN A HA   1 
ATOM   2807 H  HB2  . ASN A 1 178 ? -20.64000 15.42100 45.69400 1.000 40.74558  ? 178 ASN A HB2  1 
ATOM   2808 H  HB3  . ASN A 1 178 ? -20.66800 14.65500 44.30100 1.000 40.74558  ? 178 ASN A HB3  1 
ATOM   2809 H  HD21 . ASN A 1 178 ? -20.27800 13.20800 46.55900 1.000 74.23558  ? 178 ASN A HD21 1 
ATOM   2810 H  HD22 . ASN A 1 178 ? -18.89300 12.66600 46.63300 1.000 74.23558  ? 178 ASN A HD22 1 
ATOM   2811 N  N    . LEU A 1 179 ? -17.57500 16.52000 42.78300 1.000 29.62411  ? 179 LEU A N    1 
ATOM   2812 C  CA   . LEU A 1 179 ? -16.73300 16.21000 41.63400 1.000 30.58992  ? 179 LEU A CA   1 
ATOM   2813 C  C    . LEU A 1 179 ? -15.40100 15.62400 42.08400 1.000 31.75074  ? 179 LEU A C    1 
ATOM   2814 O  O    . LEU A 1 179 ? -14.40900 15.68900 41.35200 1.000 31.76128  ? 179 LEU A O    1 
ATOM   2815 C  CB   . LEU A 1 179 ? -16.51500 17.46800 40.79400 1.000 31.98852  ? 179 LEU A CB   1 
ATOM   2816 C  CG   . LEU A 1 179 ? -17.76500 17.98200 40.07500 1.000 32.76580  ? 179 LEU A CG   1 
ATOM   2817 C  CD1  . LEU A 1 179 ? -17.46100 19.32900 39.43800 1.000 41.05961  ? 179 LEU A CD1  1 
ATOM   2818 C  CD2  . LEU A 1 179 ? -18.25400 17.00300 39.01200 1.000 32.66480  ? 179 LEU A CD2  1 
ATOM   2819 H  H    . LEU A 1 179 ? -17.23900 17.11900 43.30000 1.000 34.34558  ? 179 LEU A H    1 
ATOM   2820 H  HA   . LEU A 1 179 ? -17.17300 15.55400 41.07100 1.000 36.01558  ? 179 LEU A HA   1 
ATOM   2821 H  HB2  . LEU A 1 179 ? -16.20000 18.17700 41.37700 1.000 37.81558  ? 179 LEU A HB2  1 
ATOM   2822 H  HB3  . LEU A 1 179 ? -15.84700 17.27400 40.11700 1.000 37.81558  ? 179 LEU A HB3  1 
ATOM   2823 H  HG   . LEU A 1 179 ? -18.47800 18.07800 40.72400 1.000 39.56558  ? 179 LEU A HG   1 
ATOM   2824 H  HD11 . LEU A 1 179 ? -18.25400 19.64700 38.97900 1.000 49.39558  ? 179 LEU A HD11 1 
ATOM   2825 H  HD12 . LEU A 1 179 ? -17.20600 19.95600 40.13200 1.000 49.39558  ? 179 LEU A HD12 1 
ATOM   2826 H  HD13 . LEU A 1 179 ? -16.73300 19.22200 38.80500 1.000 49.39558  ? 179 LEU A HD13 1 
ATOM   2827 H  HD21 . LEU A 1 179 ? -18.95800 17.42400 38.49500 1.000 40.46558  ? 179 LEU A HD21 1 
ATOM   2828 H  HD22 . LEU A 1 179 ? -17.51200 16.76900 38.43200 1.000 40.46558  ? 179 LEU A HD22 1 
ATOM   2829 H  HD23 . LEU A 1 179 ? -18.59500 16.20700 39.44900 1.000 40.46558  ? 179 LEU A HD23 1 
ATOM   2830 N  N    . ASP A 1 180 ? -15.36400 15.06400 43.29200 1.000 31.08602  ? 180 ASP A N    1 
ATOM   2831 C  CA   . ASP A 1 180 ? -14.11300 14.58700 43.86300 1.000 36.38837  ? 180 ASP A CA   1 
ATOM   2832 C  C    . ASP A 1 180 ? -13.54300 13.39400 43.10000 1.000 37.82520  ? 180 ASP A C    1 
ATOM   2833 O  O    . ASP A 1 180 ? -12.34500 13.12500 43.20700 1.000 44.66536  ? 180 ASP A O    1 
ATOM   2834 C  CB   . ASP A 1 180 ? -14.33100 14.21800 45.33000 1.000 38.74888  ? 180 ASP A CB   1 
ATOM   2835 C  CG   . ASP A 1 180 ? -14.45000 15.44000 46.23700 1.000 51.17288  ? 180 ASP A CG   1 
ATOM   2836 O  OD1  . ASP A 1 180 ? -14.22000 16.58200 45.77000 1.000 47.82018  ? 180 ASP A OD1  1 
ATOM   2837 O  OD2  . ASP A 1 180 ? -14.78600 15.24000 47.42400 1.000 53.78676  ? 180 ASP A OD2  1 
ATOM   2838 H  H    . ASP A 1 180 ? -16.04900 14.94900 43.79800 1.000 35.07558  ? 180 ASP A H    1 
ATOM   2839 H  HA   . ASP A 1 180 ? -13.45500 15.29800 43.82300 1.000 40.46558  ? 180 ASP A HA   1 
ATOM   2840 H  HB2  . ASP A 1 180 ? -15.15100 13.70600 45.40800 1.000 42.26558  ? 180 ASP A HB2  1 
ATOM   2841 H  HB3  . ASP A 1 180 ? -13.57800 13.68900 45.63700 1.000 42.26558  ? 180 ASP A HB3  1 
ATOM   2842 N  N    . SER A 1 181 ? -14.36700 12.68400 42.33400 1.000 40.48104  ? 181 SER A N    1 
ATOM   2843 C  CA   . SER A 1 181 ? -13.89300 11.59800 41.48100 1.000 41.45426  ? 181 SER A CA   1 
ATOM   2844 C  C    . SER A 1 181 ? -13.32400 12.07200 40.14600 1.000 48.02766  ? 181 SER A C    1 
ATOM   2845 O  O    . SER A 1 181 ? -12.89800 11.23300 39.34200 1.000 45.37554  ? 181 SER A O    1 
ATOM   2846 C  CB   . SER A 1 181 ? -15.04200 10.62300 41.20600 1.000 41.38084  ? 181 SER A CB   1 
ATOM   2847 O  OG   . SER A 1 181 ? -15.39400 9.92400  42.38600 1.000 49.78719  ? 181 SER A OG   1 
ATOM   2848 H  H    . SER A 1 181 ? -15.21600 12.81300 42.29000 1.000 46.92558  ? 181 SER A H    1 
ATOM   2849 H  HA   . SER A 1 181 ? -13.18700 11.13100 41.95400 1.000 48.40558  ? 181 SER A HA   1 
ATOM   2850 H  HB2  . SER A 1 181 ? -15.81300 11.12100 40.89200 1.000 49.12558  ? 181 SER A HB2  1 
ATOM   2851 H  HB3  . SER A 1 181 ? -14.76200 9.98500  40.53200 1.000 49.12558  ? 181 SER A HB3  1 
ATOM   2852 H  HG   . SER A 1 181 ? -16.02900 9.39700  42.22900 1.000 58.87558  ? 181 SER A HG   1 
ATOM   2853 N  N    . CYS A 1 182 ? -13.30500 13.37600 39.88100 1.000 34.23560  ? 182 CYS A N    1 
ATOM   2854 C  CA   . CYS A 1 182 ? -12.89100 13.89300 38.58100 1.000 32.65967  ? 182 CYS A CA   1 
ATOM   2855 C  C    . CYS A 1 182 ? -11.40900 14.24000 38.57500 1.000 32.47355  ? 182 CYS A C    1 
ATOM   2856 O  O    . CYS A 1 182 ? -10.92100 14.94700 39.46400 1.000 34.82796  ? 182 CYS A O    1 
ATOM   2857 C  CB   . CYS A 1 182 ? -13.71600 15.12300 38.21200 1.000 30.12941  ? 182 CYS A CB   1 
ATOM   2858 S  SG   . CYS A 1 182 ? -15.44100 14.72500 37.88500 1.000 32.50343  ? 182 CYS A SG   1 
ATOM   2859 H  H    . CYS A 1 182 ? -13.52900 13.98700 40.44400 1.000 40.13558  ? 182 CYS A H    1 
ATOM   2860 H  HA   . CYS A 1 182 ? -13.03400 13.20300 37.91500 1.000 38.58558  ? 182 CYS A HA   1 
ATOM   2861 H  HB2  . CYS A 1 182 ? -13.68600 15.75600 38.94700 1.000 36.07558  ? 182 CYS A HB2  1 
ATOM   2862 H  HB3  . CYS A 1 182 ? -13.34200 15.52600 37.41300 1.000 36.07558  ? 182 CYS A HB3  1 
ATOM   2863 H  HG   . CYS A 1 182 ? -15.92900 14.25700 38.87700 1.000 39.86558  ? 182 CYS A HG   1 
ATOM   2864 N  N    . LYS A 1 183 ? -10.69800 13.75000 37.56000 1.000 30.43713  ? 183 LYS A N    1 
ATOM   2865 C  CA   . LYS A 1 183 ? -9.26500  13.95500 37.44800 1.000 29.63276  ? 183 LYS A CA   1 
ATOM   2866 C  C    . LYS A 1 183 ? -8.90200  14.29000 36.01300 1.000 33.85939  ? 183 LYS A C    1 
ATOM   2867 O  O    . LYS A 1 183 ? -9.48000  13.74200 35.07200 1.000 35.63603  ? 183 LYS A O    1 
ATOM   2868 C  CB   . LYS A 1 183 ? -8.47000  12.71400 37.89500 1.000 33.71172  ? 183 LYS A CB   1 
ATOM   2869 C  CG   . LYS A 1 183 ? -6.95900  12.94100 37.84400 1.000 43.27517  ? 183 LYS A CG   1 
ATOM   2870 C  CD   . LYS A 1 183 ? -6.15900  11.86100 38.58400 1.000 54.90934  ? 183 LYS A CD   1 
ATOM   2871 C  CE   . LYS A 1 183 ? -5.94700  10.63200 37.72500 1.000 72.65898  ? 183 LYS A CE   1 
ATOM   2872 N  NZ   . LYS A 1 183 ? -4.83800  9.77500  38.25500 1.000 75.74785  ? 183 LYS A NZ   1 
ATOM   2873 H  H    . LYS A 1 183 ? -11.03400 13.28900 36.91600 1.000 35.16558  ? 183 LYS A H    1 
ATOM   2874 H  HA   . LYS A 1 183 ? -9.01300  14.70200 38.01200 1.000 33.49558  ? 183 LYS A HA   1 
ATOM   2875 H  HB2  . LYS A 1 183 ? -8.71200  12.49500 38.80800 1.000 37.64558  ? 183 LYS A HB2  1 
ATOM   2876 H  HB3  . LYS A 1 183 ? -8.68400  11.97200 37.30800 1.000 37.64558  ? 183 LYS A HB3  1 
ATOM   2877 H  HG2  . LYS A 1 183 ? -6.67200  12.94100 36.91700 1.000 48.29558  ? 183 LYS A HG2  1 
ATOM   2878 H  HG3  . LYS A 1 183 ? -6.75600  13.79600 38.25400 1.000 48.29558  ? 183 LYS A HG3  1 
ATOM   2879 H  HD2  . LYS A 1 183 ? -5.29000  12.21600 38.82600 1.000 61.29558  ? 183 LYS A HD2  1 
ATOM   2880 H  HD3  . LYS A 1 183 ? -6.64300  11.59400 39.38200 1.000 61.29558  ? 183 LYS A HD3  1 
ATOM   2881 H  HE2  . LYS A 1 183 ? -6.76100  10.10500 37.71300 1.000 82.48558  ? 183 LYS A HE2  1 
ATOM   2882 H  HE3  . LYS A 1 183 ? -5.71600  10.90700 36.82400 1.000 82.48558  ? 183 LYS A HE3  1 
ATOM   2883 H  HZ1  . LYS A 1 183 ? -4.73300  9.05900  37.73700 1.000 85.05558  ? 183 LYS A HZ1  1 
ATOM   2884 H  HZ2  . LYS A 1 183 ? -4.07600  10.23600 38.26800 1.000 85.05558  ? 183 LYS A HZ2  1 
ATOM   2885 H  HZ3  . LYS A 1 183 ? -5.02800  9.50800  39.08200 1.000 85.05558  ? 183 LYS A HZ3  1 
ATOM   2886 N  N    . ARG A 1 184 ? -7.94700  15.20400 35.85600 1.000 33.37331  ? 184 ARG A N    1 
ATOM   2887 C  CA   . ARG A 1 184 ? -7.46500  15.62900 34.55100 1.000 31.63640  ? 184 ARG A CA   1 
ATOM   2888 C  C    . ARG A 1 184 ? -5.95000  15.71300 34.61900 1.000 35.90775  ? 184 ARG A C    1 
ATOM   2889 O  O    . ARG A 1 184 ? -5.41100  16.26100 35.58200 1.000 35.62818  ? 184 ARG A O    1 
ATOM   2890 C  CB   . ARG A 1 184 ? -8.04500  16.99000 34.16000 1.000 28.62441  ? 184 ARG A CB   1 
ATOM   2891 C  CG   . ARG A 1 184 ? -7.39800  17.61000 32.94500 1.000 30.84007  ? 184 ARG A CG   1 
ATOM   2892 C  CD   . ARG A 1 184 ? -8.21600  18.77000 32.43700 1.000 32.96586  ? 184 ARG A CD   1 
ATOM   2893 N  NE   . ARG A 1 184 ? -9.38400  18.27400 31.71600 1.000 29.32352  ? 184 ARG A NE   1 
ATOM   2894 C  CZ   . ARG A 1 184 ? -10.36900 19.03300 31.26400 1.000 34.08587  ? 184 ARG A CZ   1 
ATOM   2895 N  NH1  . ARG A 1 184 ? -10.35800 20.34600 31.41700 1.000 30.96263  ? 184 ARG A NH1  1 
ATOM   2896 N  NH2  . ARG A 1 184 ? -11.39200 18.46000 30.64400 1.000 31.04674  ? 184 ARG A NH2  1 
ATOM   2897 H  H    . ARG A 1 184 ? -7.55400  15.60100 36.51000 1.000 37.97558  ? 184 ARG A H    1 
ATOM   2898 H  HA   . ARG A 1 184 ? -7.72300  14.98500 33.87300 1.000 36.07558  ? 184 ARG A HA   1 
ATOM   2899 H  HB2  . ARG A 1 184 ? -8.98900  16.88100 33.96800 1.000 33.03558  ? 184 ARG A HB2  1 
ATOM   2900 H  HB3  . ARG A 1 184 ? -7.92500  17.60300 34.90200 1.000 33.03558  ? 184 ARG A HB3  1 
ATOM   2901 H  HG2  . ARG A 1 184 ? -6.51500  17.93500 33.17800 1.000 35.76558  ? 184 ARG A HG2  1 
ATOM   2902 H  HG3  . ARG A 1 184 ? -7.33300  16.94700 32.23900 1.000 35.76558  ? 184 ARG A HG3  1 
ATOM   2903 H  HD2  . ARG A 1 184 ? -8.51700  19.31100 33.18400 1.000 38.91558  ? 184 ARG A HD2  1 
ATOM   2904 H  HD3  . ARG A 1 184 ? -7.68200  19.30800 31.83200 1.000 38.91558  ? 184 ARG A HD3  1 
ATOM   2905 H  HE   . ARG A 1 184 ? -9.43600  17.42700 31.57500 1.000 35.04558  ? 184 ARG A HE   1 
ATOM   2906 H  HH11 . ARG A 1 184 ? -9.69900  20.72600 31.81800 1.000 37.61558  ? 184 ARG A HH11 1 
ATOM   2907 H  HH12 . ARG A 1 184 ? -11.00900 20.81900 31.11500 1.000 37.61558  ? 184 ARG A HH12 1 
ATOM   2908 H  HH21 . ARG A 1 184 ? -11.40800 17.60700 30.54100 1.000 37.93558  ? 184 ARG A HH21 1 
ATOM   2909 H  HH22 . ARG A 1 184 ? -12.03800 18.94200 30.34600 1.000 37.93558  ? 184 ARG A HH22 1 
ATOM   2910 N  N    . VAL A 1 185 ? -5.26800  15.16100 33.61800 1.000 34.80382  ? 185 VAL A N    1 
ATOM   2911 C  CA   . VAL A 1 185 ? -3.81600  15.27900 33.50500 1.000 33.54429  ? 185 VAL A CA   1 
ATOM   2912 C  C    . VAL A 1 185 ? -3.51600  15.95200 32.18200 1.000 36.99854  ? 185 VAL A C    1 
ATOM   2913 O  O    . VAL A 1 185 ? -3.97900  15.49300 31.12500 1.000 36.16424  ? 185 VAL A O    1 
ATOM   2914 C  CB   . VAL A 1 185 ? -3.10700  13.92100 33.61000 1.000 33.84545  ? 185 VAL A CB   1 
ATOM   2915 C  CG1  . VAL A 1 185 ? -1.56800  14.11600 33.50000 1.000 39.37547  ? 185 VAL A CG1  1 
ATOM   2916 C  CG2  . VAL A 1 185 ? -3.46700  13.23400 34.92400 1.000 40.04849  ? 185 VAL A CG2  1 
ATOM   2917 H  H    . VAL A 1 185 ? -5.63000  14.70700 32.98300 1.000 38.84558  ? 185 VAL A H    1 
ATOM   2918 H  HA   . VAL A 1 185 ? -3.48300  15.84000 34.22300 1.000 36.62558  ? 185 VAL A HA   1 
ATOM   2919 H  HB   . VAL A 1 185 ? -3.39900  13.35000 32.88200 1.000 36.14558  ? 185 VAL A HB   1 
ATOM   2920 H  HG11 . VAL A 1 185 ? -1.12900  13.27300 33.69100 1.000 41.99558  ? 185 VAL A HG11 1 
ATOM   2921 H  HG12 . VAL A 1 185 ? -1.35000  14.40700 32.60100 1.000 41.99558  ? 185 VAL A HG12 1 
ATOM   2922 H  HG13 . VAL A 1 185 ? -1.28800  14.78800 34.14200 1.000 41.99558  ? 185 VAL A HG13 1 
ATOM   2923 H  HG21 . VAL A 1 185 ? -2.98200  12.39600 34.98600 1.000 43.32558  ? 185 VAL A HG21 1 
ATOM   2924 H  HG22 . VAL A 1 185 ? -3.22100  13.81400 35.66200 1.000 43.32558  ? 185 VAL A HG22 1 
ATOM   2925 H  HG23 . VAL A 1 185 ? -4.42200  13.06500 34.94100 1.000 43.32558  ? 185 VAL A HG23 1 
ATOM   2926 N  N    . LEU A 1 186 ? -2.76800  17.05200 32.24500 1.000 36.52586  ? 186 LEU A N    1 
ATOM   2927 C  CA   . LEU A 1 186 ? -2.36900  17.82300 31.08100 1.000 33.43939  ? 186 LEU A CA   1 
ATOM   2928 C  C    . LEU A 1 186 ? -0.85300  17.80700 30.93100 1.000 39.36644  ? 186 LEU A C    1 
ATOM   2929 O  O    . LEU A 1 186 ? -0.11600  17.63900 31.90500 1.000 42.17128  ? 186 LEU A O    1 
ATOM   2930 C  CB   . LEU A 1 186 ? -2.83900  19.28800 31.16800 1.000 39.69711  ? 186 LEU A CB   1 
ATOM   2931 C  CG   . LEU A 1 186 ? -4.33600  19.50100 31.37300 1.000 40.53913  ? 186 LEU A CG   1 
ATOM   2932 C  CD1  . LEU A 1 186 ? -4.65200  20.93900 31.77500 1.000 44.42802  ? 186 LEU A CD1  1 
ATOM   2933 C  CD2  . LEU A 1 186 ? -5.08100  19.10600 30.10100 1.000 41.81370  ? 186 LEU A CD2  1 
ATOM   2934 H  H    . LEU A 1 186 ? -2.47000  17.38100 32.98200 1.000 40.41558  ? 186 LEU A H    1 
ATOM   2935 H  HA   . LEU A 1 186 ? -2.76900  17.41600 30.29600 1.000 36.90558  ? 186 LEU A HA   1 
ATOM   2936 H  HB2  . LEU A 1 186 ? -2.38500  19.70700 31.91500 1.000 45.03558  ? 186 LEU A HB2  1 
ATOM   2937 H  HB3  . LEU A 1 186 ? -2.59700  19.73200 30.34000 1.000 45.03558  ? 186 LEU A HB3  1 
ATOM   2938 H  HG   . LEU A 1 186 ? -4.64200  18.94100 32.10400 1.000 46.70558  ? 186 LEU A HG   1 
ATOM   2939 H  HD11 . LEU A 1 186 ? -5.61000  21.02900 31.90000 1.000 51.66558  ? 186 LEU A HD11 1 
ATOM   2940 H  HD12 . LEU A 1 186 ? -4.19000  21.14500 32.60300 1.000 51.66558  ? 186 LEU A HD12 1 
ATOM   2941 H  HD13 . LEU A 1 186 ? -4.35300  21.53700 31.07200 1.000 51.66558  ? 186 LEU A HD13 1 
ATOM   2942 H  HD21 . LEU A 1 186 ? -6.02700  19.28400 30.22100 1.000 48.60558  ? 186 LEU A HD21 1 
ATOM   2943 H  HD22 . LEU A 1 186 ? -4.73800  19.62800 29.35900 1.000 48.60558  ? 186 LEU A HD22 1 
ATOM   2944 H  HD23 . LEU A 1 186 ? -4.94100  18.16100 29.93400 1.000 48.60558  ? 186 LEU A HD23 1 
ATOM   2945 N  N    . ASN A 1 187 ? -0.39800  17.98200 29.69700 1.000 36.25016  ? 187 ASN A N    1 
ATOM   2946 C  CA   . ASN A 1 187 ? 1.01800   18.13800 29.39900 1.000 41.18047  ? 187 ASN A CA   1 
ATOM   2947 C  C    . ASN A 1 187 ? 1.19800   19.36300 28.51600 1.000 47.39271  ? 187 ASN A C    1 
ATOM   2948 O  O    . ASN A 1 187 ? 0.42800   19.57500 27.57400 1.000 42.14723  ? 187 ASN A O    1 
ATOM   2949 C  CB   . ASN A 1 187 ? 1.57200   16.89600 28.70800 1.000 42.65000  ? 187 ASN A CB   1 
ATOM   2950 C  CG   . ASN A 1 187 ? 3.07600   16.83300 28.75100 1.000 49.97350  ? 187 ASN A CG   1 
ATOM   2951 O  OD1  . ASN A 1 187 ? 3.71200   17.47300 29.58800 1.000 47.33911  ? 187 ASN A OD1  1 
ATOM   2952 N  ND2  . ASN A 1 187 ? 3.65900   16.05700 27.84300 1.000 52.72858  ? 187 ASN A ND2  1 
ATOM   2953 H  H    . ASN A 1 187 ? -0.90200  18.01500 29.00100 1.000 39.50558  ? 187 ASN A H    1 
ATOM   2954 H  HA   . ASN A 1 187 ? 1.52400   18.27300 30.21500 1.000 44.80558  ? 187 ASN A HA   1 
ATOM   2955 H  HB2  . ASN A 1 187 ? 1.22500   16.10500 29.15000 1.000 45.73558  ? 187 ASN A HB2  1 
ATOM   2956 H  HB3  . ASN A 1 187 ? 1.29800   16.90200 27.77700 1.000 45.73558  ? 187 ASN A HB3  1 
ATOM   2957 H  HD21 . ASN A 1 187 ? 4.51600   15.98600 27.82500 1.000 56.20558  ? 187 ASN A HD21 1 
ATOM   2958 H  HD22 . ASN A 1 187 ? 3.17900   15.62600 27.27400 1.000 56.20558  ? 187 ASN A HD22 1 
ATOM   2959 N  N    . VAL A 1 188 ? 2.20400   20.17800 28.83900 1.000 43.50166  ? 188 VAL A N    1 
ATOM   2960 C  CA   . VAL A 1 188 ? 2.55300   21.36000 28.06400 1.000 36.13711  ? 188 VAL A CA   1 
ATOM   2961 C  C    . VAL A 1 188 ? 3.97200   21.17400 27.54500 1.000 42.95438  ? 188 VAL A C    1 
ATOM   2962 O  O    . VAL A 1 188 ? 4.89300   20.91300 28.32500 1.000 47.10828  ? 188 VAL A O    1 
ATOM   2963 C  CB   . VAL A 1 188 ? 2.44600   22.64800 28.90100 1.000 50.23145  ? 188 VAL A CB   1 
ATOM   2964 C  CG1  . VAL A 1 188 ? 2.79900   23.86000 28.04500 1.000 52.57908  ? 188 VAL A CG1  1 
ATOM   2965 C  CG2  . VAL A 1 188 ? 1.04500   22.79400 29.49300 1.000 48.79583  ? 188 VAL A CG2  1 
ATOM   2966 H  H    . VAL A 1 188 ? 2.71000   20.06000 29.52400 1.000 47.89558  ? 188 VAL A H    1 
ATOM   2967 H  HA   . VAL A 1 188 ? 1.95000   21.44000 27.30800 1.000 39.42558  ? 188 VAL A HA   1 
ATOM   2968 H  HB   . VAL A 1 188 ? 3.07500   22.59900 29.63800 1.000 56.71558  ? 188 VAL A HB   1 
ATOM   2969 H  HG11 . VAL A 1 188 ? 2.56000   24.66700 28.52700 1.000 59.89558  ? 188 VAL A HG11 1 
ATOM   2970 H  HG12 . VAL A 1 188 ? 3.75200   23.85200 27.86500 1.000 59.89558  ? 188 VAL A HG12 1 
ATOM   2971 H  HG13 . VAL A 1 188 ? 2.30500   23.81300 27.21200 1.000 59.89558  ? 188 VAL A HG13 1 
ATOM   2972 H  HG21 . VAL A 1 188 ? 0.99000   23.63700 29.97000 1.000 55.49558  ? 188 VAL A HG21 1 
ATOM   2973 H  HG22 . VAL A 1 188 ? 0.39500   22.77800 28.77400 1.000 55.49558  ? 188 VAL A HG22 1 
ATOM   2974 H  HG23 . VAL A 1 188 ? 0.88200   22.05800 30.10300 1.000 55.49558  ? 188 VAL A HG23 1 
ATOM   2975 N  N    . VAL A 1 189 ? 4.14300   21.30200 26.23500 1.000 41.23310  ? 189 VAL A N    1 
ATOM   2976 C  CA   . VAL A 1 189 ? 5.39400   20.98300 25.56000 1.000 45.76688  ? 189 VAL A CA   1 
ATOM   2977 C  C    . VAL A 1 189 ? 5.89700   22.23800 24.86000 1.000 45.70007  ? 189 VAL A C    1 
ATOM   2978 O  O    . VAL A 1 189 ? 5.21500   22.78300 23.98400 1.000 45.31586  ? 189 VAL A O    1 
ATOM   2979 C  CB   . VAL A 1 189 ? 5.20700   19.83400 24.55700 1.000 51.67311  ? 189 VAL A CB   1 
ATOM   2980 C  CG1  . VAL A 1 189 ? 6.49500   19.56800 23.79700 1.000 62.93024  ? 189 VAL A CG1  1 
ATOM   2981 C  CG2  . VAL A 1 189 ? 4.72200   18.58600 25.27400 1.000 49.46468  ? 189 VAL A CG2  1 
ATOM   2982 H  H    . VAL A 1 189 ? 3.53000   21.58000 25.70000 1.000 44.86558  ? 189 VAL A H    1 
ATOM   2983 H  HA   . VAL A 1 189 ? 6.05800   20.72400 26.21800 1.000 49.54558  ? 189 VAL A HA   1 
ATOM   2984 H  HB   . VAL A 1 189 ? 4.53400   20.08600 23.90600 1.000 55.92558  ? 189 VAL A HB   1 
ATOM   2985 H  HG11 . VAL A 1 189 ? 6.40600   18.73600 23.30700 1.000 68.49558  ? 189 VAL A HG11 1 
ATOM   2986 H  HG12 . VAL A 1 189 ? 6.65600   20.29900 23.18100 1.000 68.49558  ? 189 VAL A HG12 1 
ATOM   2987 H  HG13 . VAL A 1 189 ? 7.22700   19.50200 24.43000 1.000 68.49558  ? 189 VAL A HG13 1 
ATOM   2988 H  HG21 . VAL A 1 189 ? 4.79200   17.82800 24.67300 1.000 52.88558  ? 189 VAL A HG21 1 
ATOM   2989 H  HG22 . VAL A 1 189 ? 5.27400   18.43800 26.05800 1.000 52.88558  ? 189 VAL A HG22 1 
ATOM   2990 H  HG23 . VAL A 1 189 ? 3.79800   18.71300 25.54000 1.000 52.88558  ? 189 VAL A HG23 1 
ATOM   2991 N  N    . CYS A 1 190 ? 7.09500   22.68200 25.23400 1.000 48.25175  ? 190 CYS A N    1 
ATOM   2992 C  CA   . CYS A 1 190 ? 7.76900   23.80600 24.59800 1.000 46.04261  ? 190 CYS A CA   1 
ATOM   2993 C  C    . CYS A 1 190 ? 9.11000   23.34200 24.04300 1.000 50.00891  ? 190 CYS A C    1 
ATOM   2994 O  O    . CYS A 1 190 ? 9.85600   22.64200 24.73200 1.000 51.18255  ? 190 CYS A O    1 
ATOM   2995 C  CB   . CYS A 1 190 ? 7.99100   24.94700 25.59100 1.000 44.29466  ? 190 CYS A CB   1 
ATOM   2996 S  SG   . CYS A 1 190 ? 8.86200   26.35900 24.84300 1.000 42.33174  ? 190 CYS A SG   1 
ATOM   2997 H  H    . CYS A 1 190 ? 7.55100   22.33400 25.87500 1.000 52.65558  ? 190 CYS A H    1 
ATOM   2998 H  HA   . CYS A 1 190 ? 7.22400   24.13200 23.86500 1.000 50.27558  ? 190 CYS A HA   1 
ATOM   2999 H  HB2  . CYS A 1 190 ? 7.13100   25.25900 25.91300 1.000 48.59558  ? 190 CYS A HB2  1 
ATOM   3000 H  HB3  . CYS A 1 190 ? 8.52500   24.62200 26.33300 1.000 48.59558  ? 190 CYS A HB3  1 
ATOM   3001 N  N    . ASP A 1 191 ? 9.41200   23.73300 22.80000 1.000 47.16396  ? 191 ASP A N    1 
ATOM   3002 C  CA   . ASP A 1 191 ? 10.68500  23.34500 22.19100 1.000 50.43365  ? 191 ASP A CA   1 
ATOM   3003 C  C    . ASP A 1 191 ? 11.86800  23.85500 23.00100 1.000 57.44077  ? 191 ASP A C    1 
ATOM   3004 O  O    . ASP A 1 191 ? 12.92200  23.20700 23.05200 1.000 56.15942  ? 191 ASP A O    1 
ATOM   3005 C  CB   . ASP A 1 191 ? 10.76800  23.87300 20.75900 1.000 57.07175  ? 191 ASP A CB   1 
ATOM   3006 C  CG   . ASP A 1 191 ? 9.77900   23.18700 19.82000 1.000 74.24014  ? 191 ASP A CG   1 
ATOM   3007 O  OD1  . ASP A 1 191 ? 9.84200   21.94900 19.67700 1.000 74.01462  ? 191 ASP A OD1  1 
ATOM   3008 O  OD2  . ASP A 1 191 ? 8.93400   23.89000 19.23000 1.000 61.52328  ? 191 ASP A OD2  1 
ATOM   3009 H  H    . ASP A 1 191 ? 8.90700   24.21600 22.29900 1.000 50.74558  ? 191 ASP A H    1 
ATOM   3010 H  HA   . ASP A 1 191 ? 10.73000  22.37700 22.15900 1.000 53.79558  ? 191 ASP A HA   1 
ATOM   3011 H  HB2  . ASP A 1 191 ? 10.57100  24.82300 20.76000 1.000 61.75558  ? 191 ASP A HB2  1 
ATOM   3012 H  HB3  . ASP A 1 191 ? 11.66200  23.72000 20.41600 1.000 61.75558  ? 191 ASP A HB3  1 
ATOM   3013 N  N    . THR A 1 192 ? 11.71700  25.01500 23.63700 1.000 46.93082  ? 192 THR A N    1 
ATOM   3014 C  CA   . THR A 1 192 ? 12.78300  25.54300 24.48100 1.000 49.34366  ? 192 THR A CA   1 
ATOM   3015 C  C    . THR A 1 192 ? 12.71900  24.93400 25.87500 1.000 53.23623  ? 192 THR A C    1 
ATOM   3016 O  O    . THR A 1 192 ? 13.68600  24.32100 26.33600 1.000 55.88538  ? 192 THR A O    1 
ATOM   3017 C  CB   . THR A 1 192 ? 12.69500  27.07300 24.55300 1.000 48.40636  ? 192 THR A CB   1 
ATOM   3018 O  OG1  . THR A 1 192 ? 13.01200  27.63500 23.27400 1.000 46.50357  ? 192 THR A OG1  1 
ATOM   3019 C  CG2  . THR A 1 192 ? 13.66000  27.62300 25.57600 1.000 55.60103  ? 192 THR A CG2  1 
ATOM   3020 H  H    . THR A 1 192 ? 11.01500  25.50900 23.59700 1.000 50.31558  ? 192 THR A H    1 
ATOM   3021 H  HA   . THR A 1 192 ? 13.63900  25.31600 24.08600 1.000 53.01558  ? 192 THR A HA   1 
ATOM   3022 H  HB   . THR A 1 192 ? 11.79400  27.32300 24.81200 1.000 52.70558  ? 192 THR A HB   1 
ATOM   3023 H  HG1  . THR A 1 192 ? 12.95000  28.47300 23.30500 1.000 50.48558  ? 192 THR A HG1  1 
ATOM   3024 H  HG21 . THR A 1 192 ? 13.79900  28.57100 25.42400 1.000 60.61558  ? 192 THR A HG21 1 
ATOM   3025 H  HG22 . THR A 1 192 ? 13.30400  27.49700 26.47000 1.000 60.61558  ? 192 THR A HG22 1 
ATOM   3026 H  HG23 . THR A 1 192 ? 14.51200  27.16500 25.50900 1.000 60.61558  ? 192 THR A HG23 1 
ATOM   3027 N  N    . CYS A 1 193 ? 11.57200  25.05600 26.54700 1.000 45.84025  ? 193 CYS A N    1 
ATOM   3028 C  CA   . CYS A 1 193 ? 11.49400  24.76600 27.97700 1.000 56.83156  ? 193 CYS A CA   1 
ATOM   3029 C  C    . CYS A 1 193 ? 11.17100  23.31000 28.30300 1.000 60.34053  ? 193 CYS A C    1 
ATOM   3030 O  O    . CYS A 1 193 ? 11.16400  22.94800 29.48300 1.000 55.88411  ? 193 CYS A O    1 
ATOM   3031 C  CB   . CYS A 1 193 ? 10.45000  25.66900 28.64000 1.000 50.85506  ? 193 CYS A CB   1 
ATOM   3032 S  SG   . CYS A 1 193 ? 10.60900  27.40700 28.17300 1.000 47.01704  ? 193 CYS A SG   1 
ATOM   3033 H  H    . CYS A 1 193 ? 10.82800  25.30500 26.19600 1.000 48.81558  ? 193 CYS A H    1 
ATOM   3034 H  HA   . CYS A 1 193 ? 12.36300  24.95900 28.36100 1.000 61.55558  ? 193 CYS A HA   1 
ATOM   3035 H  HB2  . CYS A 1 193 ? 9.56500   25.37000 28.38000 1.000 55.00558  ? 193 CYS A HB2  1 
ATOM   3036 H  HB3  . CYS A 1 193 ? 10.55100  25.60900 29.60300 1.000 55.00558  ? 193 CYS A HB3  1 
ATOM   3037 N  N    . GLY A 1 194 ? 10.90400  22.47300 27.30800 1.000 53.30215  ? 194 GLY A N    1 
ATOM   3038 C  CA   . GLY A 1 194 ? 10.64600  21.07400 27.57600 1.000 50.10211  ? 194 GLY A CA   1 
ATOM   3039 C  C    . GLY A 1 194 ? 9.19800   20.79700 27.92400 1.000 62.26515  ? 194 GLY A C    1 
ATOM   3040 O  O    . GLY A 1 194 ? 8.29300   21.49800 27.45700 1.000 61.72912  ? 194 GLY A O    1 
ATOM   3041 H  H    . GLY A 1 194 ? 10.86700  22.69300 26.47800 1.000 56.68558  ? 194 GLY A H    1 
ATOM   3042 H  HA2  . GLY A 1 194 ? 10.87500  20.55200 26.79100 1.000 52.19558  ? 194 GLY A HA2  1 
ATOM   3043 H  HA3  . GLY A 1 194 ? 11.19700  20.78500 28.32000 1.000 52.19558  ? 194 GLY A HA3  1 
ATOM   3044 N  N    . GLN A 1 195 ? 8.97000   19.78400 28.75600 1.000 49.27402  ? 195 GLN A N    1 
ATOM   3045 C  CA   . GLN A 1 195 ? 7.63700   19.28000 29.05200 1.000 54.49577  ? 195 GLN A CA   1 
ATOM   3046 C  C    . GLN A 1 195 ? 7.27400   19.54800 30.50300 1.000 49.82228  ? 195 GLN A C    1 
ATOM   3047 O  O    . GLN A 1 195 ? 8.11100   19.41100 31.40000 1.000 49.88237  ? 195 GLN A O    1 
ATOM   3048 C  CB   . GLN A 1 195 ? 7.55100   17.77600 28.79400 1.000 55.00686  ? 195 GLN A CB   1 
ATOM   3049 C  CG   . GLN A 1 195 ? 7.78000   17.37800 27.36100 1.000 69.31121  ? 195 GLN A CG   1 
ATOM   3050 C  CD   . GLN A 1 195 ? 7.41600   15.93800 27.11200 1.000 67.74075  ? 195 GLN A CD   1 
ATOM   3051 O  OE1  . GLN A 1 195 ? 6.43100   15.43200 27.65300 1.000 61.05143  ? 195 GLN A OE1  1 
ATOM   3052 N  NE2  . GLN A 1 195 ? 8.20700   15.26600 26.28700 1.000 77.46511  ? 195 GLN A NE2  1 
ATOM   3053 H  H    . GLN A 1 195 ? 9.59300   19.36100 29.17300 1.000 51.24558  ? 195 GLN A H    1 
ATOM   3054 H  HA   . GLN A 1 195 ? 6.99800   19.74000 28.48500 1.000 57.93558  ? 195 GLN A HA   1 
ATOM   3055 H  HB2  . GLN A 1 195 ? 8.22300   17.33100 29.33300 1.000 57.81558  ? 195 GLN A HB2  1 
ATOM   3056 H  HB3  . GLN A 1 195 ? 6.66600   17.46800 29.04600 1.000 57.81558  ? 195 GLN A HB3  1 
ATOM   3057 H  HG2  . GLN A 1 195 ? 7.23300   17.93400 26.78400 1.000 74.60558  ? 195 GLN A HG2  1 
ATOM   3058 H  HG3  . GLN A 1 195 ? 8.71800   17.49600 27.14300 1.000 74.60558  ? 195 GLN A HG3  1 
ATOM   3059 H  HE21 . GLN A 1 195 ? 8.88400   15.65600 25.92700 1.000 82.53558  ? 195 GLN A HE21 1 
ATOM   3060 H  HE22 . GLN A 1 195 ? 8.04300   14.44100 26.11100 1.000 82.53558  ? 195 GLN A HE22 1 
ATOM   3061 N  N    . GLN A 1 196 ? 6.01200   19.88000 30.73400 1.000 51.83878  ? 196 GLN A N    1 
ATOM   3062 C  CA   . GLN A 1 196 ? 5.51000   20.13700 32.07700 1.000 44.69894  ? 196 GLN A CA   1 
ATOM   3063 C  C    . GLN A 1 196 ? 4.12400   19.52300 32.19400 1.000 49.20816  ? 196 GLN A C    1 
ATOM   3064 O  O    . GLN A 1 196 ? 3.19700   19.94600 31.50100 1.000 46.31162  ? 196 GLN A O    1 
ATOM   3065 C  CB   . GLN A 1 196 ? 5.46000   21.64000 32.36100 1.000 54.32416  ? 196 GLN A CB   1 
ATOM   3066 C  CG   . GLN A 1 196 ? 5.03900   21.98800 33.77500 1.000 52.75764  ? 196 GLN A CG   1 
ATOM   3067 C  CD   . GLN A 1 196 ? 5.95400   21.38000 34.81000 1.000 72.33761  ? 196 GLN A CD   1 
ATOM   3068 O  OE1  . GLN A 1 196 ? 7.10000   21.80300 34.96000 1.000 73.50683  ? 196 GLN A OE1  1 
ATOM   3069 N  NE2  . GLN A 1 196 ? 5.45800   20.37400 35.52900 1.000 81.92503  ? 196 GLN A NE2  1 
ATOM   3070 H  H    . GLN A 1 196 ? 5.41700   19.96400 30.11900 1.000 55.55558  ? 196 GLN A H    1 
ATOM   3071 H  HA   . GLN A 1 196 ? 6.09000   19.71900 32.73300 1.000 46.93558  ? 196 GLN A HA   1 
ATOM   3072 H  HB2  . GLN A 1 196 ? 6.34300   22.01300 32.21600 1.000 58.86558  ? 196 GLN A HB2  1 
ATOM   3073 H  HB3  . GLN A 1 196 ? 4.82200   22.04900 31.75500 1.000 58.86558  ? 196 GLN A HB3  1 
ATOM   3074 H  HG2  . GLN A 1 196 ? 5.05800   22.95200 33.88400 1.000 56.58558  ? 196 GLN A HG2  1 
ATOM   3075 H  HG3  . GLN A 1 196 ? 4.14200   21.65400 33.93200 1.000 56.58558  ? 196 GLN A HG3  1 
ATOM   3076 H  HE21 . GLN A 1 196 ? 4.65300   20.10400 35.39100 1.000 90.00558  ? 196 GLN A HE21 1 
ATOM   3077 H  HE22 . GLN A 1 196 ? 5.94200   19.99600 36.13100 1.000 90.00558  ? 196 GLN A HE22 1 
ATOM   3078 N  N    . GLN A 1 197 ? 3.98800   18.52900 33.06100 1.000 44.80547  ? 197 GLN A N    1 
ATOM   3079 C  CA   . GLN A 1 197 ? 2.71200   17.87800 33.31000 1.000 46.32430  ? 197 GLN A CA   1 
ATOM   3080 C  C    . GLN A 1 197 ? 2.04200   18.50700 34.52500 1.000 51.97525  ? 197 GLN A C    1 
ATOM   3081 O  O    . GLN A 1 197 ? 2.70600   18.92800 35.47400 1.000 51.34332  ? 197 GLN A O    1 
ATOM   3082 C  CB   . GLN A 1 197 ? 2.91400   16.37900 33.52900 1.000 50.66349  ? 197 GLN A CB   1 
ATOM   3083 C  CG   . GLN A 1 197 ? 1.65000   15.62000 33.86500 1.000 49.23561  ? 197 GLN A CG   1 
ATOM   3084 C  CD   . GLN A 1 197 ? 1.92300   14.16200 34.15600 1.000 51.36831  ? 197 GLN A CD   1 
ATOM   3085 O  OE1  . GLN A 1 197 ? 2.20300   13.37800 33.24800 1.000 53.04297  ? 197 GLN A OE1  1 
ATOM   3086 N  NE2  . GLN A 1 197 ? 1.86200   13.79500 35.42800 1.000 51.13304  ? 197 GLN A NE2  1 
ATOM   3087 H  H    . GLN A 1 197 ? 4.63500   18.20800 33.52800 1.000 47.00558  ? 197 GLN A H    1 
ATOM   3088 H  HA   . GLN A 1 197 ? 2.12200   17.99200 32.54800 1.000 49.24558  ? 197 GLN A HA   1 
ATOM   3089 H  HB2  . GLN A 1 197 ? 3.27900   15.99400 32.71700 1.000 53.75558  ? 197 GLN A HB2  1 
ATOM   3090 H  HB3  . GLN A 1 197 ? 3.53400   16.25500 34.26400 1.000 53.75558  ? 197 GLN A HB3  1 
ATOM   3091 H  HG2  . GLN A 1 197 ? 1.24100   16.01500 34.65100 1.000 52.40558  ? 197 GLN A HG2  1 
ATOM   3092 H  HG3  . GLN A 1 197 ? 1.03900   15.67000 33.11300 1.000 52.40558  ? 197 GLN A HG3  1 
ATOM   3093 H  HE21 . GLN A 1 197 ? 1.67400   14.37600 36.03400 1.000 53.39558  ? 197 GLN A HE21 1 
ATOM   3094 H  HE22 . GLN A 1 197 ? 2.00900   12.97700 35.64700 1.000 53.39558  ? 197 GLN A HE22 1 
ATOM   3095 N  N    . THR A 1 198 ? 0.71500   18.58300 34.48000 1.000 46.66582  ? 198 THR A N    1 
ATOM   3096 C  CA   . THR A 1 198 ? -0.05600  19.09400 35.60400 1.000 39.28941  ? 198 THR A CA   1 
ATOM   3097 C  C    . THR A 1 198 ? -1.29600  18.23500 35.79600 1.000 44.21024  ? 198 THR A C    1 
ATOM   3098 O  O    . THR A 1 198 ? -1.86000  17.70900 34.83400 1.000 41.85024  ? 198 THR A O    1 
ATOM   3099 C  CB   . THR A 1 198 ? -0.47300  20.56200 35.41000 1.000 59.30683  ? 198 THR A CB   1 
ATOM   3100 O  OG1  . THR A 1 198 ? -1.45600  20.64600 34.38000 1.000 61.55249  ? 198 THR A OG1  1 
ATOM   3101 C  CG2  . THR A 1 198 ? 0.71500   21.43000 35.01900 1.000 56.60241  ? 198 THR A CG2  1 
ATOM   3102 H  H    . THR A 1 198 ? 0.23700   18.34400 33.80600 1.000 50.49558  ? 198 THR A H    1 
ATOM   3103 H  HA   . THR A 1 198 ? 0.48800   19.04200 36.40600 1.000 41.62558  ? 198 THR A HA   1 
ATOM   3104 H  HB   . THR A 1 198 ? -0.83300  20.89600 36.24700 1.000 66.13558  ? 198 THR A HB   1 
ATOM   3105 H  HG1  . THR A 1 198 ? -1.68100  21.44700 34.26200 1.000 69.84558  ? 198 THR A HG1  1 
ATOM   3106 H  HG21 . THR A 1 198 ? 0.44800   22.36200 34.98400 1.000 62.61558  ? 198 THR A HG21 1 
ATOM   3107 H  HG22 . THR A 1 198 ? 1.42700   21.33100 35.67000 1.000 62.61558  ? 198 THR A HG22 1 
ATOM   3108 H  HG23 . THR A 1 198 ? 1.04700   21.16500 34.14700 1.000 62.61558  ? 198 THR A HG23 1 
ATOM   3109 N  N    . THR A 1 199 ? -1.70600  18.09400 37.04900 1.000 41.90987  ? 199 THR A N    1 
ATOM   3110 C  CA   . THR A 1 199 ? -2.88400  17.32000 37.42300 1.000 42.25122  ? 199 THR A CA   1 
ATOM   3111 C  C    . THR A 1 199 ? -3.88900  18.26600 38.06100 1.000 47.21456  ? 199 THR A C    1 
ATOM   3112 O  O    . THR A 1 199 ? -3.53100  19.06100 38.93500 1.000 42.35103  ? 199 THR A O    1 
ATOM   3113 C  CB   . THR A 1 199 ? -2.51700  16.18300 38.38000 1.000 45.38892  ? 199 THR A CB   1 
ATOM   3114 O  OG1  . THR A 1 199 ? -1.61400  15.28700 37.71200 1.000 48.27187  ? 199 THR A OG1  1 
ATOM   3115 C  CG2  . THR A 1 199 ? -3.74800  15.40000 38.83400 1.000 49.55829  ? 199 THR A CG2  1 
ATOM   3116 H  H    . THR A 1 199 ? -1.30600  18.44800 37.72200 1.000 44.74558  ? 199 THR A H    1 
ATOM   3117 H  HA   . THR A 1 199 ? -3.29000  16.91900 36.63800 1.000 45.52558  ? 199 THR A HA   1 
ATOM   3118 H  HB   . THR A 1 199 ? -2.10200  16.55900 39.17300 1.000 48.41558  ? 199 THR A HB   1 
ATOM   3119 H  HG1  . THR A 1 199 ? -1.40800  14.65300 38.22300 1.000 51.57558  ? 199 THR A HG1  1 
ATOM   3120 H  HG21 . THR A 1 199 ? -3.47600  14.59800 39.30600 1.000 53.79558  ? 199 THR A HG21 1 
ATOM   3121 H  HG22 . THR A 1 199 ? -4.28800  15.94600 39.42700 1.000 53.79558  ? 199 THR A HG22 1 
ATOM   3122 H  HG23 . THR A 1 199 ? -4.28200  15.14700 38.06500 1.000 53.79558  ? 199 THR A HG23 1 
ATOM   3123 N  N    . LEU A 1 200 ? -5.13000  18.18400 37.60100 1.000 41.29184  ? 200 LEU A N    1 
ATOM   3124 C  CA   . LEU A 1 200 ? -6.23900  18.99000 38.08500 1.000 35.14772  ? 200 LEU A CA   1 
ATOM   3125 C  C    . LEU A 1 200 ? -7.31700  18.07400 38.64200 1.000 38.80459  ? 200 LEU A C    1 
ATOM   3126 O  O    . LEU A 1 200 ? -7.49500  16.94400 38.18100 1.000 35.74400  ? 200 LEU A O    1 
ATOM   3127 C  CB   . LEU A 1 200 ? -6.82000  19.85600 36.95400 1.000 34.00448  ? 200 LEU A CB   1 
ATOM   3128 C  CG   . LEU A 1 200 ? -5.80200  20.71800 36.21100 1.000 36.08149  ? 200 LEU A CG   1 
ATOM   3129 C  CD1  . LEU A 1 200 ? -6.45000  21.35900 34.99000 1.000 39.73312  ? 200 LEU A CD1  1 
ATOM   3130 C  CD2  . LEU A 1 200 ? -5.20900  21.78300 37.11400 1.000 48.39279  ? 200 LEU A CD2  1 
ATOM   3131 H  H    . LEU A 1 200 ? -5.36600  17.64000 36.97800 1.000 45.50558  ? 200 LEU A H    1 
ATOM   3132 H  HA   . LEU A 1 200 ? -5.94100  19.58100 38.79400 1.000 38.39558  ? 200 LEU A HA   1 
ATOM   3133 H  HB2  . LEU A 1 200 ? -7.23600  19.27000 36.30300 1.000 37.92558  ? 200 LEU A HB2  1 
ATOM   3134 H  HB3  . LEU A 1 200 ? -7.48300  20.45200 37.33600 1.000 37.92558  ? 200 LEU A HB3  1 
ATOM   3135 H  HG   . LEU A 1 200 ? -5.07400  20.15000 35.91600 1.000 40.33558  ? 200 LEU A HG   1 
ATOM   3136 H  HD11 . LEU A 1 200 ? -5.79000  21.90000 34.52900 1.000 45.60558  ? 200 LEU A HD11 1 
ATOM   3137 H  HD12 . LEU A 1 200 ? -6.77500  20.66000 34.40200 1.000 45.60558  ? 200 LEU A HD12 1 
ATOM   3138 H  HD13 . LEU A 1 200 ? -7.18900  21.91700 35.28100 1.000 45.60558  ? 200 LEU A HD13 1 
ATOM   3139 H  HD21 . LEU A 1 200 ? -4.58100  22.31600 36.60300 1.000 54.23558  ? 200 LEU A HD21 1 
ATOM   3140 H  HD22 . LEU A 1 200 ? -5.92400  22.34500 37.45100 1.000 54.23558  ? 200 LEU A HD22 1 
ATOM   3141 H  HD23 . LEU A 1 200 ? -4.75100  21.35100 37.85300 1.000 54.23558  ? 200 LEU A HD23 1 
ATOM   3142 N  N    . LYS A 1 201 ? -8.04100  18.56200 39.64400 1.000 34.98365  ? 201 LYS A N    1 
ATOM   3143 C  CA   . LYS A 1 201 ? -9.05300  17.76400 40.31900 1.000 31.30534  ? 201 LYS A CA   1 
ATOM   3144 C  C    . LYS A 1 201 ? -10.33300 18.56900 40.48200 1.000 36.69302  ? 201 LYS A C    1 
ATOM   3145 O  O    . LYS A 1 201 ? -10.31400 19.80200 40.52100 1.000 35.35593  ? 201 LYS A O    1 
ATOM   3146 C  CB   . LYS A 1 201 ? -8.55100  17.28500 41.69900 1.000 38.81728  ? 201 LYS A CB   1 
ATOM   3147 C  CG   . LYS A 1 201 ? -7.25700  16.48200 41.60600 1.000 49.90009  ? 201 LYS A CG   1 
ATOM   3148 C  CD   . LYS A 1 201 ? -7.53200  14.99500 41.39700 1.000 58.33511  ? 201 LYS A CD   1 
ATOM   3149 C  CE   . LYS A 1 201 ? -7.22000  14.19300 42.65300 1.000 75.11486  ? 201 LYS A CE   1 
ATOM   3150 N  NZ   . LYS A 1 201 ? -5.74600  13.99700 42.81600 1.000 87.61292  ? 201 LYS A NZ   1 
ATOM   3151 H  H    . LYS A 1 201 ? -7.96200  19.36100 39.95200 1.000 38.08558  ? 201 LYS A H    1 
ATOM   3152 H  HA   . LYS A 1 201 ? -9.26600  16.98600 39.78100 1.000 33.79558  ? 201 LYS A HA   1 
ATOM   3153 H  HB2  . LYS A 1 201 ? -8.38500  18.05800 42.26100 1.000 41.58558  ? 201 LYS A HB2  1 
ATOM   3154 H  HB3  . LYS A 1 201 ? -9.22700  16.72000 42.10300 1.000 41.58558  ? 201 LYS A HB3  1 
ATOM   3155 H  HG2  . LYS A 1 201 ? -6.73300  16.80300 40.85500 1.000 54.34558  ? 201 LYS A HG2  1 
ATOM   3156 H  HG3  . LYS A 1 201 ? -6.75400  16.58600 42.42900 1.000 54.34558  ? 201 LYS A HG3  1 
ATOM   3157 H  HD2  . LYS A 1 201 ? -8.46900  14.86800 41.17900 1.000 64.89558  ? 201 LYS A HD2  1 
ATOM   3158 H  HD3  . LYS A 1 201 ? -6.97500  14.66200 40.67600 1.000 64.89558  ? 201 LYS A HD3  1 
ATOM   3159 H  HE2  . LYS A 1 201 ? -7.55400  14.66800 43.43000 1.000 83.94558  ? 201 LYS A HE2  1 
ATOM   3160 H  HE3  . LYS A 1 201 ? -7.64000  13.32100 42.59100 1.000 83.94558  ? 201 LYS A HE3  1 
ATOM   3161 H  HZ1  . LYS A 1 201 ? -5.58100  13.53600 43.56000 1.000 97.90558  ? 201 LYS A HZ1  1 
ATOM   3162 H  HZ2  . LYS A 1 201 ? -5.41900  13.54900 42.12000 1.000 97.90558  ? 201 LYS A HZ2  1 
ATOM   3163 H  HZ3  . LYS A 1 201 ? -5.33800  14.78600 42.86900 1.000 97.90558  ? 201 LYS A HZ3  1 
ATOM   3164 N  N    . GLY A 1 202 ? -11.45100 17.85300 40.55300 1.000 31.70020  ? 202 GLY A N    1 
ATOM   3165 C  CA   . GLY A 1 202 ? -12.71200 18.51000 40.87000 1.000 33.42314  ? 202 GLY A CA   1 
ATOM   3166 C  C    . GLY A 1 202 ? -13.15900 19.41400 39.74000 1.000 32.39216  ? 202 GLY A C    1 
ATOM   3167 O  O    . GLY A 1 202 ? -13.09200 19.04700 38.56000 1.000 31.13332  ? 202 GLY A O    1 
ATOM   3168 H  H    . GLY A 1 202 ? -11.50600 17.00500 40.42600 1.000 35.26558  ? 202 GLY A H    1 
ATOM   3169 H  HA2  . GLY A 1 202 ? -13.39800 17.84100 41.02200 1.000 37.54558  ? 202 GLY A HA2  1 
ATOM   3170 H  HA3  . GLY A 1 202 ? -12.60900 19.04400 41.67200 1.000 37.54558  ? 202 GLY A HA3  1 
ATOM   3171 N  N    . VAL A 1 203 ? -13.61600 20.62200 40.09700 1.000 32.25036  ? 203 VAL A N    1 
ATOM   3172 C  CA   . VAL A 1 203 ? -14.18500 21.51800 39.08400 1.000 29.39774  ? 203 VAL A CA   1 
ATOM   3173 C  C    . VAL A 1 203 ? -13.14500 21.84600 38.01600 1.000 31.47608  ? 203 VAL A C    1 
ATOM   3174 O  O    . VAL A 1 203 ? -13.46200 21.93200 36.82200 1.000 29.11767  ? 203 VAL A O    1 
ATOM   3175 C  CB   . VAL A 1 203 ? -14.75600 22.79500 39.73900 1.000 41.14124  ? 203 VAL A CB   1 
ATOM   3176 C  CG1  . VAL A 1 203 ? -13.77900 23.40100 40.73100 1.000 58.43650  ? 203 VAL A CG1  1 
ATOM   3177 C  CG2  . VAL A 1 203 ? -15.14900 23.82400 38.66800 1.000 34.63935  ? 203 VAL A CG2  1 
ATOM   3178 H  H    . VAL A 1 203 ? -13.60900 20.93700 40.89700 1.000 36.51558  ? 203 VAL A H    1 
ATOM   3179 H  HA   . VAL A 1 203 ? -14.92000 21.05600 38.65100 1.000 33.74558  ? 203 VAL A HA   1 
ATOM   3180 H  HB   . VAL A 1 203 ? -15.55300 22.54700 40.23200 1.000 47.10558  ? 203 VAL A HB   1 
ATOM   3181 H  HG11 . VAL A 1 203 ? -14.16300 24.21300 41.09700 1.000 66.45558  ? 203 VAL A HG11 1 
ATOM   3182 H  HG12 . VAL A 1 203 ? -13.61400 22.76300 41.44200 1.000 66.45558  ? 203 VAL A HG12 1 
ATOM   3183 H  HG13 . VAL A 1 203 ? -12.94900 23.60600 40.27200 1.000 66.45558  ? 203 VAL A HG13 1 
ATOM   3184 H  HG21 . VAL A 1 203 ? -15.53900 24.59800 39.10300 1.000 39.83558  ? 203 VAL A HG21 1 
ATOM   3185 H  HG22 . VAL A 1 203 ? -14.35500 24.08600 38.17600 1.000 39.83558  ? 203 VAL A HG22 1 
ATOM   3186 H  HG23 . VAL A 1 203 ? -15.79400 23.42200 38.06600 1.000 39.83558  ? 203 VAL A HG23 1 
ATOM   3187 N  N    A GLU A 1 204 ? -11.88600 22.02800 38.42200 0.490 29.06011  ? 204 GLU A N    1 
ATOM   3188 N  N    B GLU A 1 204 ? -11.88600 22.03200 38.43200 0.510 28.96469  ? 204 GLU A N    1 
ATOM   3189 C  CA   A GLU A 1 204 ? -10.84600 22.33500 37.44500 0.490 30.91618  ? 204 GLU A CA   1 
ATOM   3190 C  CA   B GLU A 1 204 ? -10.80600 22.31800 37.49300 0.510 31.23139  ? 204 GLU A CA   1 
ATOM   3191 C  C    A GLU A 1 204 ? -10.56300 21.16400 36.51600 0.490 31.79852  ? 204 GLU A C    1 
ATOM   3192 C  C    B GLU A 1 204 ? -10.56300 21.16700 36.52700 0.510 31.81853  ? 204 GLU A C    1 
ATOM   3193 O  O    A GLU A 1 204 ? -9.95400  21.35900 35.45800 0.490 31.96390  ? 204 GLU A O    1 
ATOM   3194 O  O    B GLU A 1 204 ? -9.99000  21.37900 35.45200 0.510 32.08693  ? 204 GLU A O    1 
ATOM   3195 C  CB   A GLU A 1 204 ? -9.55600  22.73700 38.15400 0.490 36.06024  ? 204 GLU A CB   1 
ATOM   3196 C  CB   B GLU A 1 204 ? -9.51800  22.61900 38.26500 0.510 35.81338  ? 204 GLU A CB   1 
ATOM   3197 C  CG   A GLU A 1 204 ? -9.58900  24.13100 38.75300 0.490 41.92010  ? 204 GLU A CG   1 
ATOM   3198 C  CG   B GLU A 1 204 ? -9.49200  23.98800 38.93800 0.510 49.60948  ? 204 GLU A CG   1 
ATOM   3199 C  CD   A GLU A 1 204 ? -10.14500 24.16000 40.17500 0.490 54.85062  ? 204 GLU A CD   1 
ATOM   3200 C  CD   B GLU A 1 204 ? -8.08000  24.41100 39.37300 0.510 46.04044  ? 204 GLU A CD   1 
ATOM   3201 O  OE1  A GLU A 1 204 ? -10.34100 23.07200 40.77200 0.490 37.65652  ? 204 GLU A OE1  1 
ATOM   3202 O  OE1  B GLU A 1 204 ? -7.49100  23.71700 40.22900 0.510 42.97464  ? 204 GLU A OE1  1 
ATOM   3203 O  OE2  A GLU A 1 204 ? -10.35700 25.27900 40.70300 0.490 49.06165  ? 204 GLU A OE2  1 
ATOM   3204 O  OE2  B GLU A 1 204 ? -7.56200  25.43100 38.85700 0.510 59.29000  ? 204 GLU A OE2  1 
ATOM   3205 H  H    A GLU A 1 204 ? -11.61700 21.98100 39.23700 0.490 32.81558  ? 204 GLU A H    1 
ATOM   3206 H  H    B GLU A 1 204 ? -11.63500 21.99700 39.25400 0.510 32.69558  ? 204 GLU A H    1 
ATOM   3207 H  HA   A GLU A 1 204 ? -11.14400 23.08600 36.90900 0.490 35.23558  ? 204 GLU A HA   1 
ATOM   3208 H  HA   B GLU A 1 204 ? -11.04300 23.10100 36.97200 0.510 35.57558  ? 204 GLU A HA   1 
ATOM   3209 H  HB2  A GLU A 1 204 ? -9.38900  22.11000 38.87400 0.490 40.34558  ? 204 GLU A HB2  1 
ATOM   3210 H  HB2  B GLU A 1 204 ? -9.41000  21.94900 38.95800 0.510 39.97558  ? 204 GLU A HB2  1 
ATOM   3211 H  HB3  A GLU A 1 204 ? -8.82800  22.70800 37.51400 0.490 40.34558  ? 204 GLU A HB3  1 
ATOM   3212 H  HB3  B GLU A 1 204 ? -8.77100  22.58100 37.64700 0.510 39.97558  ? 204 GLU A HB3  1 
ATOM   3213 H  HG2  A GLU A 1 204 ? -8.68600  24.48400 38.77900 0.490 46.54558  ? 204 GLU A HG2  1 
ATOM   3214 H  HG2  B GLU A 1 204 ? -9.82600  24.65300 38.31600 0.510 55.62558  ? 204 GLU A HG2  1 
ATOM   3215 H  HG3  A GLU A 1 204 ? -10.15100 24.69800 38.20200 0.490 46.54558  ? 204 GLU A HG3  1 
ATOM   3216 H  HG3  B GLU A 1 204 ? -10.05400 23.96300 39.72900 0.510 55.62558  ? 204 GLU A HG3  1 
ATOM   3217 N  N    . ALA A 1 205 ? -10.97500 19.95300 36.88800 1.000 27.90288  ? 205 ALA A N    1 
ATOM   3218 C  CA   . ALA A 1 205 ? -10.78300 18.80400 36.01300 1.000 27.45383  ? 205 ALA A CA   1 
ATOM   3219 C  C    . ALA A 1 205 ? -11.82400 18.72800 34.90400 1.000 27.43240  ? 205 ALA A C    1 
ATOM   3220 O  O    . ALA A 1 205 ? -11.61900 17.99100 33.93900 1.000 31.03689  ? 205 ALA A O    1 
ATOM   3221 C  CB   . ALA A 1 205 ? -10.82100 17.50400 36.81600 1.000 34.91477  ? 205 ALA A CB   1 
ATOM   3222 H  H    . ALA A 1 205 ? -11.36700 19.77200 37.63300 1.000 32.40558  ? 205 ALA A H    1 
ATOM   3223 H  HA   . ALA A 1 205 ? -9.90600  18.88200 35.60600 1.000 32.29558  ? 205 ALA A HA   1 
ATOM   3224 H  HB1  . ALA A 1 205 ? -10.68300 16.75700 36.21300 1.000 40.97558  ? 205 ALA A HB1  1 
ATOM   3225 H  HB2  . ALA A 1 205 ? -10.11800 17.52500 37.48400 1.000 40.97558  ? 205 ALA A HB2  1 
ATOM   3226 H  HB3  . ALA A 1 205 ? -11.68600 17.42500 37.24900 1.000 40.97558  ? 205 ALA A HB3  1 
ATOM   3227 N  N    . VAL A 1 206 ? -12.94300 19.44500 35.01500 1.000 26.51069  ? 206 VAL A N    1 
ATOM   3228 C  CA   . VAL A 1 206 ? -14.00100 19.32600 34.01800 1.000 26.41421  ? 206 VAL A CA   1 
ATOM   3229 C  C    . VAL A 1 206 ? -14.21900 20.59600 33.21700 1.000 28.39660  ? 206 VAL A C    1 
ATOM   3230 O  O    . VAL A 1 206 ? -15.01300 20.57300 32.26700 1.000 30.39849  ? 206 VAL A O    1 
ATOM   3231 C  CB   . VAL A 1 206 ? -15.33700 18.86300 34.64200 1.000 25.70597  ? 206 VAL A CB   1 
ATOM   3232 C  CG1  . VAL A 1 206 ? -15.15800 17.52000 35.33600 1.000 27.42698  ? 206 VAL A CG1  1 
ATOM   3233 C  CG2  . VAL A 1 206 ? -15.91700 19.90500 35.60500 1.000 26.83819  ? 206 VAL A CG2  1 
ATOM   3234 H  H    . VAL A 1 206 ? -13.10800 19.99900 35.65100 1.000 32.33558  ? 206 VAL A H    1 
ATOM   3235 H  HA   . VAL A 1 206 ? -13.72400 18.63900 33.39100 1.000 32.89558  ? 206 VAL A HA   1 
ATOM   3236 H  HB   . VAL A 1 206 ? -15.98100 18.75800 33.92500 1.000 32.37558  ? 206 VAL A HB   1 
ATOM   3237 H  HG11 . VAL A 1 206 ? -16.01400 17.22900 35.68600 1.000 34.28558  ? 206 VAL A HG11 1 
ATOM   3238 H  HG12 . VAL A 1 206 ? -14.82700 16.87400 34.69300 1.000 34.28558  ? 206 VAL A HG12 1 
ATOM   3239 H  HG13 . VAL A 1 206 ? -14.52100 17.62100 36.06000 1.000 34.28558  ? 206 VAL A HG13 1 
ATOM   3240 H  HG21 . VAL A 1 206 ? -16.67100 19.51500 36.07600 1.000 33.49558  ? 206 VAL A HG21 1 
ATOM   3241 H  HG22 . VAL A 1 206 ? -15.23100 20.16700 36.23900 1.000 33.49558  ? 206 VAL A HG22 1 
ATOM   3242 H  HG23 . VAL A 1 206 ? -16.20900 20.67700 35.09600 1.000 33.49558  ? 206 VAL A HG23 1 
ATOM   3243 N  N    . MET A 1 207 ? -13.54500 21.69100 33.54900 1.000 28.94290  ? 207 MET A N    1 
ATOM   3244 C  CA   . MET A 1 207 ? -13.74300 22.96600 32.87000 1.000 26.49986  ? 207 MET A CA   1 
ATOM   3245 C  C    . MET A 1 207 ? -12.46200 23.37000 32.16000 1.000 33.91634  ? 207 MET A C    1 
ATOM   3246 O  O    . MET A 1 207 ? -11.36300 23.21200 32.69300 1.000 31.86018  ? 207 MET A O    1 
ATOM   3247 C  CB   . MET A 1 207 ? -14.16800 24.07200 33.86700 1.000 26.04891  ? 207 MET A CB   1 
ATOM   3248 C  CG   . MET A 1 207 ? -15.60100 23.89400 34.40600 1.000 30.18042  ? 207 MET A CG   1 
ATOM   3249 S  SD   . MET A 1 207 ? -16.08400 25.22700 35.53500 1.000 35.91518  ? 207 MET A SD   1 
ATOM   3250 C  CE   . MET A 1 207 ? -16.54500 26.41000 34.26900 1.000 34.57169  ? 207 MET A CE   1 
ATOM   3251 H  H    . MET A 1 207 ? -12.95600 21.72100 34.17500 1.000 35.71558  ? 207 MET A H    1 
ATOM   3252 H  HA   . MET A 1 207 ? -14.45200 22.87100 32.21400 1.000 32.87558  ? 207 MET A HA   1 
ATOM   3253 H  HB2  . MET A 1 207 ? -13.56100 24.06100 34.62400 1.000 31.89558  ? 207 MET A HB2  1 
ATOM   3254 H  HB3  . MET A 1 207 ? -14.12300 24.93100 33.41900 1.000 31.89558  ? 207 MET A HB3  1 
ATOM   3255 H  HG2  . MET A 1 207 ? -16.22200 23.89000 33.66100 1.000 37.03558  ? 207 MET A HG2  1 
ATOM   3256 H  HG3  . MET A 1 207 ? -15.65600 23.05400 34.88900 1.000 37.03558  ? 207 MET A HG3  1 
ATOM   3257 H  HE1  . MET A 1 207 ? -16.83600 27.23100 34.69500 1.000 41.79558  ? 207 MET A HE1  1 
ATOM   3258 H  HE2  . MET A 1 207 ? -15.77600 26.58400 33.70400 1.000 41.79558  ? 207 MET A HE2  1 
ATOM   3259 H  HE3  . MET A 1 207 ? -17.26800 26.03900 33.73900 1.000 41.79558  ? 207 MET A HE3  1 
ATOM   3260 N  N    . TYR A 1 208 ? -12.60300 23.88700 30.95100 1.000 27.98780  ? 208 TYR A N    1 
ATOM   3261 C  CA   . TYR A 1 208 ? -11.46800 24.43500 30.22100 1.000 26.13593  ? 208 TYR A CA   1 
ATOM   3262 C  C    . TYR A 1 208 ? -11.92400 25.64800 29.42900 1.000 27.94428  ? 208 TYR A C    1 
ATOM   3263 O  O    . TYR A 1 208 ? -12.98000 25.61600 28.80100 1.000 30.84990  ? 208 TYR A O    1 
ATOM   3264 C  CB   . TYR A 1 208 ? -10.82900 23.42600 29.25500 1.000 26.68872  ? 208 TYR A CB   1 
ATOM   3265 C  CG   . TYR A 1 208 ? -9.61700  24.04400 28.61300 1.000 28.00925  ? 208 TYR A CG   1 
ATOM   3266 C  CD1  . TYR A 1 208 ? -8.43800  24.19800 29.33400 1.000 33.08213  ? 208 TYR A CD1  1 
ATOM   3267 C  CD2  . TYR A 1 208 ? -9.67600  24.55000 27.31700 1.000 28.43086  ? 208 TYR A CD2  1 
ATOM   3268 C  CE1  . TYR A 1 208 ? -7.34100  24.80600 28.77800 1.000 33.78931  ? 208 TYR A CE1  1 
ATOM   3269 C  CE2  . TYR A 1 208 ? -8.57000  25.15900 26.74700 1.000 29.17050  ? 208 TYR A CE2  1 
ATOM   3270 C  CZ   . TYR A 1 208 ? -7.40200  25.27800 27.48700 1.000 32.38006  ? 208 TYR A CZ   1 
ATOM   3271 O  OH   . TYR A 1 208 ? -6.27500  25.88200 26.95800 1.000 35.95942  ? 208 TYR A OH   1 
ATOM   3272 H  H    . TYR A 1 208 ? -13.35000 23.93300 30.52800 1.000 34.75558  ? 208 TYR A H    1 
ATOM   3273 H  HA   . TYR A 1 208 ? -10.79200 24.69800 30.86600 1.000 32.36558  ? 208 TYR A HA   1 
ATOM   3274 H  HB2  . TYR A 1 208 ? -10.55700 22.63300 29.74200 1.000 33.00558  ? 208 TYR A HB2  1 
ATOM   3275 H  HB3  . TYR A 1 208 ? -11.46500 23.18800 28.56200 1.000 33.00558  ? 208 TYR A HB3  1 
ATOM   3276 H  HD1  . TYR A 1 208 ? -8.39300  23.88400 30.20800 1.000 40.07558  ? 208 TYR A HD1  1 
ATOM   3277 H  HD2  . TYR A 1 208 ? -10.46500 24.47900 26.83000 1.000 34.95558  ? 208 TYR A HD2  1 
ATOM   3278 H  HE1  . TYR A 1 208 ? -6.55900  24.89800 29.27300 1.000 40.73558  ? 208 TYR A HE1  1 
ATOM   3279 H  HE2  . TYR A 1 208 ? -8.60900  25.48500 25.87700 1.000 35.63558  ? 208 TYR A HE2  1 
ATOM   3280 H  HH   . TYR A 1 208 ? -6.41400  26.09900 26.15800 1.000 43.32558  ? 208 TYR A HH   1 
ATOM   3281 N  N    . MET A 1 209 ? -11.12700 26.71100 29.47400 1.000 27.75877  ? 209 MET A N    1 
ATOM   3282 C  CA   . MET A 1 209 ? -11.41300 27.96300 28.78500 1.000 27.82362  ? 209 MET A CA   1 
ATOM   3283 C  C    . MET A 1 209 ? -10.35300 28.19500 27.71800 1.000 40.82920  ? 209 MET A C    1 
ATOM   3284 O  O    . MET A 1 209 ? -9.16900  28.37100 28.04100 1.000 31.52520  ? 209 MET A O    1 
ATOM   3285 C  CB   . MET A 1 209 ? -11.43000 29.12300 29.77800 1.000 28.00859  ? 209 MET A CB   1 
ATOM   3286 C  CG   . MET A 1 209 ? -11.35900 30.50400 29.14700 1.000 43.23573  ? 209 MET A CG   1 
ATOM   3287 S  SD   . MET A 1 209 ? -12.79300 30.83900 28.11900 1.000 43.06026  ? 209 MET A SD   1 
ATOM   3288 C  CE   . MET A 1 209 ? -14.15100 30.79400 29.24800 1.000 55.60563  ? 209 MET A CE   1 
ATOM   3289 H  H    . MET A 1 209 ? -10.38800 26.73100 29.91300 1.000 34.19558  ? 209 MET A H    1 
ATOM   3290 H  HA   . MET A 1 209 ? -12.28200 27.90400 28.35800 1.000 34.31558  ? 209 MET A HA   1 
ATOM   3291 H  HB2  . MET A 1 209 ? -12.25300 29.07800 30.28900 1.000 34.09558  ? 209 MET A HB2  1 
ATOM   3292 H  HB3  . MET A 1 209 ? -10.66600 29.03400 30.36900 1.000 34.09558  ? 209 MET A HB3  1 
ATOM   3293 H  HG2  . MET A 1 209 ? -11.32300 31.17400 29.84700 1.000 52.25558  ? 209 MET A HG2  1 
ATOM   3294 H  HG3  . MET A 1 209 ? -10.56600 30.56100 28.59100 1.000 52.25558  ? 209 MET A HG3  1 
ATOM   3295 H  HE1  . MET A 1 209 ? -14.97000 30.98500 28.76500 1.000 67.27558  ? 209 MET A HE1  1 
ATOM   3296 H  HE2  . MET A 1 209 ? -14.20000 29.91200 29.64800 1.000 67.27558  ? 209 MET A HE2  1 
ATOM   3297 H  HE3  . MET A 1 209 ? -14.01000 31.46200 29.93700 1.000 67.27558  ? 209 MET A HE3  1 
ATOM   3298 N  N    . GLY A 1 210 ? -10.77100 28.19400 26.45000 1.000 30.09861  ? 210 GLY A N    1 
ATOM   3299 C  CA   . GLY A 1 210 ? -9.85800  28.54000 25.37400 1.000 30.44494  ? 210 GLY A CA   1 
ATOM   3300 C  C    . GLY A 1 210 ? -10.21700 27.90000 24.05000 1.000 33.57812  ? 210 GLY A C    1 
ATOM   3301 O  O    . GLY A 1 210 ? -9.90000  28.44300 22.98700 1.000 35.84541  ? 210 GLY A O    1 
ATOM   3302 H  H    . GLY A 1 210 ? -11.56900 27.99900 26.19600 1.000 37.22558  ? 210 GLY A H    1 
ATOM   3303 H  HA2  . GLY A 1 210 ? -9.86000  29.50200 25.25400 1.000 37.54558  ? 210 GLY A HA2  1 
ATOM   3304 H  HA3  . GLY A 1 210 ? -8.96300  28.25300 25.61400 1.000 37.54558  ? 210 GLY A HA3  1 
ATOM   3305 N  N    . THR A 1 211 ? -10.84600 26.73000 24.10300 1.000 30.41318  ? 211 THR A N    1 
ATOM   3306 C  CA   . THR A 1 211 ? -11.33500 26.08400 22.89300 1.000 31.45666  ? 211 THR A CA   1 
ATOM   3307 C  C    . THR A 1 211 ? -12.62700 25.35700 23.20900 1.000 32.06412  ? 211 THR A C    1 
ATOM   3308 O  O    . THR A 1 211 ? -12.83300 24.86500 24.32400 1.000 27.95441  ? 211 THR A O    1 
ATOM   3309 C  CB   . THR A 1 211 ? -10.33800 25.09000 22.28100 1.000 38.91602  ? 211 THR A CB   1 
ATOM   3310 O  OG1  . THR A 1 211 ? -10.88500 24.55900 21.05200 1.000 35.58101  ? 211 THR A OG1  1 
ATOM   3311 C  CG2  . THR A 1 211 ? -10.05300 23.95100 23.21400 1.000 39.73228  ? 211 THR A CG2  1 
ATOM   3312 H  H    . THR A 1 211 ? -11.00100 26.29200 24.82600 1.000 37.43558  ? 211 THR A H    1 
ATOM   3313 H  HA   . THR A 1 211 ? -11.50000 26.77700 22.23500 1.000 38.38558  ? 211 THR A HA   1 
ATOM   3314 H  HB   . THR A 1 211 ? -9.50300  25.55200 22.10700 1.000 46.81558  ? 211 THR A HB   1 
ATOM   3315 H  HG1  . THR A 1 211 ? -10.35100 24.00400 20.71700 1.000 42.25558  ? 211 THR A HG1  1 
ATOM   3316 H  HG21 . THR A 1 211 ? -9.28400  23.45000 22.90000 1.000 47.81558  ? 211 THR A HG21 1 
ATOM   3317 H  HG22 . THR A 1 211 ? -9.86800  24.28900 24.10400 1.000 47.81558  ? 211 THR A HG22 1 
ATOM   3318 H  HG23 . THR A 1 211 ? -10.81900 23.35700 23.25600 1.000 47.81558  ? 211 THR A HG23 1 
ATOM   3319 N  N    . LEU A 1 212 ? -13.50100 25.32200 22.21600 1.000 27.76874  ? 212 LEU A N    1 
ATOM   3320 C  CA   . LEU A 1 212 ? -14.75700 24.60500 22.33300 1.000 28.51795  ? 212 LEU A CA   1 
ATOM   3321 C  C    . LEU A 1 212 ? -14.61700 23.13500 21.98800 1.000 31.25404  ? 212 LEU A C    1 
ATOM   3322 O  O    . LEU A 1 212 ? -15.49500 22.34800 22.35100 1.000 30.63234  ? 212 LEU A O    1 
ATOM   3323 C  CB   . LEU A 1 212 ? -15.81700 25.21300 21.42400 1.000 32.08493  ? 212 LEU A CB   1 
ATOM   3324 C  CG   . LEU A 1 212 ? -16.20600 26.66500 21.68200 1.000 30.95083  ? 212 LEU A CG   1 
ATOM   3325 C  CD1  . LEU A 1 212 ? -17.19300 27.11200 20.65100 1.000 27.93607  ? 212 LEU A CD1  1 
ATOM   3326 C  CD2  . LEU A 1 212 ? -16.78100 26.81700 23.08300 1.000 28.04702  ? 212 LEU A CD2  1 
ATOM   3327 H  H    . LEU A 1 212 ? -13.38900 25.71000 21.45700 1.000 33.86558  ? 212 LEU A H    1 
ATOM   3328 H  HA   . LEU A 1 212 ? -15.07000 24.68800 23.24700 1.000 34.82558  ? 212 LEU A HA   1 
ATOM   3329 H  HB2  . LEU A 1 212 ? -15.48900 25.16700 20.51200 1.000 38.88558  ? 212 LEU A HB2  1 
ATOM   3330 H  HB3  . LEU A 1 212 ? -16.62500 24.68400 21.51400 1.000 38.88558  ? 212 LEU A HB3  1 
ATOM   3331 H  HG   . LEU A 1 212 ? -15.42100 27.23100 21.62200 1.000 37.82558  ? 212 LEU A HG   1 
ATOM   3332 H  HD11 . LEU A 1 212 ? -17.47600 28.01700 20.85600 1.000 33.81558  ? 212 LEU A HD11 1 
ATOM   3333 H  HD12 . LEU A 1 212 ? -16.77100 27.08900 19.77800 1.000 33.81558  ? 212 LEU A HD12 1 
ATOM   3334 H  HD13 . LEU A 1 212 ? -17.95700 26.51500 20.66500 1.000 33.81558  ? 212 LEU A HD13 1 
ATOM   3335 H  HD21 . LEU A 1 212 ? -17.13000 27.71700 23.18500 1.000 34.88558  ? 212 LEU A HD21 1 
ATOM   3336 H  HD22 . LEU A 1 212 ? -17.49400 26.17100 23.20400 1.000 34.88558  ? 212 LEU A HD22 1 
ATOM   3337 H  HD23 . LEU A 1 212 ? -16.07800 26.66000 23.73200 1.000 34.88558  ? 212 LEU A HD23 1 
ATOM   3338 N  N    . SER A 1 213 ? -13.54600 22.75800 21.29300 1.000 33.58302  ? 213 SER A N    1 
ATOM   3339 C  CA   . SER A 1 213 ? -13.41900 21.42800 20.71000 1.000 32.00162  ? 213 SER A CA   1 
ATOM   3340 C  C    . SER A 1 213 ? -12.69200 20.48000 21.65500 1.000 30.88954  ? 213 SER A C    1 
ATOM   3341 O  O    . SER A 1 213 ? -11.51400 20.68000 21.95200 1.000 31.33233  ? 213 SER A O    1 
ATOM   3342 C  CB   . SER A 1 213 ? -12.66400 21.50900 19.38300 1.000 37.22050  ? 213 SER A CB   1 
ATOM   3343 O  OG   . SER A 1 213 ? -12.42300 20.21500 18.89100 1.000 35.07537  ? 213 SER A OG   1 
ATOM   3344 H  H    . SER A 1 213 ? -12.86800 23.26500 21.14300 1.000 39.85558  ? 213 SER A H    1 
ATOM   3345 H  HA   . SER A 1 213 ? -14.31100 21.07400 20.56500 1.000 37.15558  ? 213 SER A HA   1 
ATOM   3346 H  HB2  . SER A 1 213 ? -13.19800 22.00100 18.74100 1.000 42.42558  ? 213 SER A HB2  1 
ATOM   3347 H  HB3  . SER A 1 213 ? -11.81600 21.95900 19.52500 1.000 42.42558  ? 213 SER A HB3  1 
ATOM   3348 H  HG   . SER A 1 213 ? -13.15100 19.82000 18.75300 1.000 38.87558  ? 213 SER A HG   1 
ATOM   3349 N  N    . TYR A 1 214 ? -13.38500 19.42900 22.09600 1.000 30.24926  ? 214 TYR A N    1 
ATOM   3350 C  CA   . TYR A 1 214 ? -12.72900 18.42300 22.92800 1.000 34.61651  ? 214 TYR A CA   1 
ATOM   3351 C  C    . TYR A 1 214 ? -11.68000 17.67800 22.12300 1.000 37.34961  ? 214 TYR A C    1 
ATOM   3352 O  O    . TYR A 1 214 ? -10.58900 17.38000 22.62600 1.000 33.61674  ? 214 TYR A O    1 
ATOM   3353 C  CB   . TYR A 1 214 ? -13.77800 17.46300 23.49400 1.000 32.46871  ? 214 TYR A CB   1 
ATOM   3354 C  CG   . TYR A 1 214 ? -13.35200 16.57400 24.65400 1.000 32.23275  ? 214 TYR A CG   1 
ATOM   3355 C  CD1  . TYR A 1 214 ? -12.39300 16.97900 25.56900 1.000 31.28580  ? 214 TYR A CD1  1 
ATOM   3356 C  CD2  . TYR A 1 214 ? -13.95400 15.33900 24.85100 1.000 32.72458  ? 214 TYR A CD2  1 
ATOM   3357 C  CE1  . TYR A 1 214 ? -12.03600 16.17500 26.63400 1.000 32.21373  ? 214 TYR A CE1  1 
ATOM   3358 C  CE2  . TYR A 1 214 ? -13.60000 14.52600 25.90500 1.000 36.57228  ? 214 TYR A CE2  1 
ATOM   3359 C  CZ   . TYR A 1 214 ? -12.63800 14.95400 26.80100 1.000 31.99210  ? 214 TYR A CZ   1 
ATOM   3360 O  OH   . TYR A 1 214 ? -12.28000 14.15200 27.86600 1.000 35.32573  ? 214 TYR A OH   1 
ATOM   3361 H  H    . TYR A 1 214 ? -14.21500 19.27900 21.93100 1.000 35.19558  ? 214 TYR A H    1 
ATOM   3362 H  HA   . TYR A 1 214 ? -12.28700 18.84900 23.67800 1.000 40.38558  ? 214 TYR A HA   1 
ATOM   3363 H  HB2  . TYR A 1 214 ? -14.53000 17.99200 23.80500 1.000 38.02558  ? 214 TYR A HB2  1 
ATOM   3364 H  HB3  . TYR A 1 214 ? -14.06100 16.87400 22.77700 1.000 38.02558  ? 214 TYR A HB3  1 
ATOM   3365 H  HD1  . TYR A 1 214 ? -11.98300 17.80700 25.46400 1.000 37.09558  ? 214 TYR A HD1  1 
ATOM   3366 H  HD2  . TYR A 1 214 ? -14.61100 15.05400 24.25800 1.000 38.31558  ? 214 TYR A HD2  1 
ATOM   3367 H  HE1  . TYR A 1 214 ? -11.38800 16.46100 27.23700 1.000 38.23558  ? 214 TYR A HE1  1 
ATOM   3368 H  HE2  . TYR A 1 214 ? -14.00400 13.69600 26.01400 1.000 43.04558  ? 214 TYR A HE2  1 
ATOM   3369 H  HH   . TYR A 1 214 ? -12.71300 13.43300 27.84300 1.000 41.77558  ? 214 TYR A HH   1 
ATOM   3370 N  N    . GLU A 1 215 ? -11.98600 17.37300 20.85900 1.000 33.37553  ? 215 GLU A N    1 
ATOM   3371 C  CA   . GLU A 1 215 ? -11.00000 16.69400 20.03100 1.000 35.15835  ? 215 GLU A CA   1 
ATOM   3372 C  C    . GLU A 1 215 ? -9.73900  17.53600 19.87100 1.000 35.91202  ? 215 GLU A C    1 
ATOM   3373 O  O    . GLU A 1 215 ? -8.62100  17.01200 19.93000 1.000 40.32779  ? 215 GLU A O    1 
ATOM   3374 C  CB   . GLU A 1 215 ? -11.60900 16.36100 18.67200 1.000 45.24126  ? 215 GLU A CB   1 
ATOM   3375 C  CG   . GLU A 1 215 ? -12.07300 14.90800 18.54100 1.000 77.72787  ? 215 GLU A CG   1 
ATOM   3376 C  CD   . GLU A 1 215 ? -10.96800 13.89100 18.83800 1.000 68.02076  ? 215 GLU A CD   1 
ATOM   3377 O  OE1  . GLU A 1 215 ? -9.78000  14.16500 18.53500 1.000 79.76390  ? 215 GLU A OE1  1 
ATOM   3378 O  OE2  . GLU A 1 215 ? -11.29500 12.81300 19.37700 1.000 83.28038  ? 215 GLU A OE2  1 
ATOM   3379 H  H    . GLU A 1 215 ? -12.73500 17.54400 20.47200 1.000 36.86558  ? 215 GLU A H    1 
ATOM   3380 H  HA   . GLU A 1 215 ? -10.74600 15.86100 20.45900 1.000 37.72558  ? 215 GLU A HA   1 
ATOM   3381 H  HB2  . GLU A 1 215 ? -12.37900 16.93200 18.52700 1.000 48.56558  ? 215 GLU A HB2  1 
ATOM   3382 H  HB3  . GLU A 1 215 ? -10.94300 16.52300 17.98500 1.000 48.56558  ? 215 GLU A HB3  1 
ATOM   3383 H  HG2  . GLU A 1 215 ? -12.79700 14.75200 19.16700 1.000 86.58558  ? 215 GLU A HG2  1 
ATOM   3384 H  HG3  . GLU A 1 215 ? -12.38000 14.75700 17.63400 1.000 86.58558  ? 215 GLU A HG3  1 
ATOM   3385 N  N    . GLN A 1 216 ? -9.88900  18.84500 19.67900 1.000 35.10973  ? 216 GLN A N    1 
ATOM   3386 C  CA   . GLN A 1 216 ? -8.70600  19.69100 19.54000 1.000 36.38358  ? 216 GLN A CA   1 
ATOM   3387 C  C    . GLN A 1 216 ? -7.88700  19.72500 20.82600 1.000 35.57324  ? 216 GLN A C    1 
ATOM   3388 O  O    . GLN A 1 216 ? -6.64900  19.76100 20.78600 1.000 37.35511  ? 216 GLN A O    1 
ATOM   3389 C  CB   . GLN A 1 216 ? -9.11700  21.10300 19.13100 1.000 37.52075  ? 216 GLN A CB   1 
ATOM   3390 C  CG   . GLN A 1 216 ? -7.93600  21.96700 18.68500 1.000 48.74428  ? 216 GLN A CG   1 
ATOM   3391 C  CD   . GLN A 1 216 ? -7.16900  21.35600 17.51600 1.000 57.63471  ? 216 GLN A CD   1 
ATOM   3392 O  OE1  . GLN A 1 216 ? -7.70200  21.20800 16.41300 1.000 53.89470  ? 216 GLN A OE1  1 
ATOM   3393 N  NE2  . GLN A 1 216 ? -5.90600  21.00700 17.75400 1.000 57.88019  ? 216 GLN A NE2  1 
ATOM   3394 H  H    . GLN A 1 216 ? -10.64200 19.25700 19.62600 1.000 38.31558  ? 216 GLN A H    1 
ATOM   3395 H  HA   . GLN A 1 216 ? -8.14500  19.32300 18.84000 1.000 39.92558  ? 216 GLN A HA   1 
ATOM   3396 H  HB2  . GLN A 1 216 ? -9.74200  21.04600 18.39100 1.000 41.81558  ? 216 GLN A HB2  1 
ATOM   3397 H  HB3  . GLN A 1 216 ? -9.53800  21.53900 19.88800 1.000 41.81558  ? 216 GLN A HB3  1 
ATOM   3398 H  HG2  . GLN A 1 216 ? -8.26700  22.83500 18.40500 1.000 55.16558  ? 216 GLN A HG2  1 
ATOM   3399 H  HG3  . GLN A 1 216 ? -7.32100  22.07100 19.42700 1.000 55.16558  ? 216 GLN A HG3  1 
ATOM   3400 H  HE21 . GLN A 1 216 ? -5.56500  21.13200 18.53400 1.000 64.48558  ? 216 GLN A HE21 1 
ATOM   3401 H  HE22 . GLN A 1 216 ? -5.43100  20.65800 17.12800 1.000 64.48558  ? 216 GLN A HE22 1 
ATOM   3402 N  N    . PHE A 1 217 ? -8.56400  19.73000 21.97500 1.000 32.34327  ? 217 PHE A N    1 
ATOM   3403 C  CA   . PHE A 1 217 ? -7.88000  19.70000 23.26700 1.000 30.86598  ? 217 PHE A CA   1 
ATOM   3404 C  C    . PHE A 1 217 ? -7.06400  18.42300 23.41500 1.000 33.03330  ? 217 PHE A C    1 
ATOM   3405 O  O    . PHE A 1 217 ? -5.96300  18.44100 23.97900 1.000 35.68001  ? 217 PHE A O    1 
ATOM   3406 C  CB   . PHE A 1 217 ? -8.95200  19.84200 24.35100 1.000 29.09204  ? 217 PHE A CB   1 
ATOM   3407 C  CG   . PHE A 1 217 ? -8.44200  20.11600 25.74100 1.000 30.01280  ? 217 PHE A CG   1 
ATOM   3408 C  CD1  . PHE A 1 217 ? -7.59600  21.17300 26.00200 1.000 35.70876  ? 217 PHE A CD1  1 
ATOM   3409 C  CD2  . PHE A 1 217 ? -8.90400  19.36100 26.80500 1.000 36.67325  ? 217 PHE A CD2  1 
ATOM   3410 C  CE1  . PHE A 1 217 ? -7.17400  21.43400 27.30000 1.000 40.77802  ? 217 PHE A CE1  1 
ATOM   3411 C  CE2  . PHE A 1 217 ? -8.48700  19.61400 28.10200 1.000 33.87625  ? 217 PHE A CE2  1 
ATOM   3412 C  CZ   . PHE A 1 217 ? -7.61900  20.64800 28.34700 1.000 39.17086  ? 217 PHE A CZ   1 
ATOM   3413 H  H    . PHE A 1 217 ? -9.42200  19.75000 22.03500 1.000 36.62558  ? 217 PHE A H    1 
ATOM   3414 H  HA   . PHE A 1 217 ? -7.25100  20.43300 23.35900 1.000 35.29558  ? 217 PHE A HA   1 
ATOM   3415 H  HB2  . PHE A 1 217 ? -9.53500  20.57900 24.10800 1.000 33.97558  ? 217 PHE A HB2  1 
ATOM   3416 H  HB3  . PHE A 1 217 ? -9.45900  19.01600 24.38700 1.000 33.97558  ? 217 PHE A HB3  1 
ATOM   3417 H  HD1  . PHE A 1 217 ? -7.30500  21.71500 25.30400 1.000 42.41558  ? 217 PHE A HD1  1 
ATOM   3418 H  HD2  . PHE A 1 217 ? -9.50600  18.67100 26.64700 1.000 43.63558  ? 217 PHE A HD2  1 
ATOM   3419 H  HE1  . PHE A 1 217 ? -6.59100  22.14000 27.46500 1.000 48.62558  ? 217 PHE A HE1  1 
ATOM   3420 H  HE2  . PHE A 1 217 ? -8.79400  19.08600 28.80300 1.000 40.41558  ? 217 PHE A HE2  1 
ATOM   3421 H  HZ   . PHE A 1 217 ? -7.33100  20.81900 29.21400 1.000 46.74558  ? 217 PHE A HZ   1 
ATOM   3422 N  N    . LYS A 1 218 ? -7.56700  17.30700 22.87800 1.000 36.07351  ? 218 LYS A N    1 
ATOM   3423 C  CA   . LYS A 1 218 ? -6.80700  16.05900 22.91800 1.000 36.78784  ? 218 LYS A CA   1 
ATOM   3424 C  C    . LYS A 1 218 ? -5.62400  16.09000 21.95900 1.000 42.43808  ? 218 LYS A C    1 
ATOM   3425 O  O    . LYS A 1 218 ? -4.57900  15.48700 22.23500 1.000 42.36620  ? 218 LYS A O    1 
ATOM   3426 C  CB   . LYS A 1 218 ? -7.70500  14.87800 22.56700 1.000 39.07150  ? 218 LYS A CB   1 
ATOM   3427 C  CG   . LYS A 1 218 ? -8.79300  14.55800 23.58200 1.000 36.42237  ? 218 LYS A CG   1 
ATOM   3428 C  CD   . LYS A 1 218 ? -9.77900  13.57300 22.96100 1.000 38.07675  ? 218 LYS A CD   1 
ATOM   3429 C  CE   . LYS A 1 218 ? -10.80500 13.05700 23.96700 1.000 42.32003  ? 218 LYS A CE   1 
ATOM   3430 N  NZ   . LYS A 1 218 ? -11.79100 12.14400 23.31700 1.000 44.65541  ? 218 LYS A NZ   1 
ATOM   3431 H  H    . LYS A 1 218 ? -8.33300  17.24800 22.49100 1.000 40.11558  ? 218 LYS A H    1 
ATOM   3432 H  HA   . LYS A 1 218 ? -6.47500  15.93700 23.82100 1.000 40.04558  ? 218 LYS A HA   1 
ATOM   3433 H  HB2  . LYS A 1 218 ? -8.14500  15.06900 21.72400 1.000 42.18558  ? 218 LYS A HB2  1 
ATOM   3434 H  HB3  . LYS A 1 218 ? -7.15000  14.08800 22.47900 1.000 42.18558  ? 218 LYS A HB3  1 
ATOM   3435 H  HG2  . LYS A 1 218 ? -8.39900  14.15400 24.37200 1.000 39.86558  ? 218 LYS A HG2  1 
ATOM   3436 H  HG3  . LYS A 1 218 ? -9.26700  15.36800 23.82600 1.000 39.86558  ? 218 LYS A HG3  1 
ATOM   3437 H  HD2  . LYS A 1 218 ? -10.25900 14.01500 22.24300 1.000 41.20558  ? 218 LYS A HD2  1 
ATOM   3438 H  HD3  . LYS A 1 218 ? -9.29000  12.81100 22.61400 1.000 41.20558  ? 218 LYS A HD3  1 
ATOM   3439 H  HE2  . LYS A 1 218 ? -10.34900 12.56600 24.66800 1.000 47.07558  ? 218 LYS A HE2  1 
ATOM   3440 H  HE3  . LYS A 1 218 ? -11.28700 13.80800 24.34700 1.000 47.07558  ? 218 LYS A HE3  1 
ATOM   3441 H  HZ1  . LYS A 1 218 ? -12.37700 11.85000 23.91900 1.000 49.23558  ? 218 LYS A HZ1  1 
ATOM   3442 H  HZ2  . LYS A 1 218 ? -12.23100 12.57700 22.67500 1.000 49.23558  ? 218 LYS A HZ2  1 
ATOM   3443 H  HZ3  . LYS A 1 218 ? -11.37000 11.44600 22.95800 1.000 49.23558  ? 218 LYS A HZ3  1 
ATOM   3444 N  N    . LYS A 1 219 ? -5.77500  16.76700 20.82700 1.000 39.96601  ? 219 LYS A N    1 
ATOM   3445 C  CA   . LYS A 1 219 ? -4.68700  16.84600 19.86600 1.000 41.39759  ? 219 LYS A CA   1 
ATOM   3446 C  C    . LYS A 1 219 ? -3.61100  17.80700 20.34400 1.000 46.82057  ? 219 LYS A C    1 
ATOM   3447 O  O    . LYS A 1 219 ? -2.41600  17.52900 20.21100 1.000 48.43663  ? 219 LYS A O    1 
ATOM   3448 C  CB   . LYS A 1 219 ? -5.22300  17.30800 18.51300 1.000 45.54840  ? 219 LYS A CB   1 
ATOM   3449 C  CG   . LYS A 1 219 ? -5.96300  16.24300 17.72500 1.000 50.85456  ? 219 LYS A CG   1 
ATOM   3450 C  CD   . LYS A 1 219 ? -6.14800  16.69400 16.27400 1.000 73.06159  ? 219 LYS A CD   1 
ATOM   3451 C  CE   . LYS A 1 219 ? -7.23300  15.92200 15.51900 1.000 74.15676  ? 219 LYS A CE   1 
ATOM   3452 N  NZ   . LYS A 1 219 ? -8.13200  15.09900 16.37500 1.000 98.13527  ? 219 LYS A NZ   1 
ATOM   3453 H  H    . LYS A 1 219 ? -6.49000  17.18400 20.59500 1.000 42.58558  ? 219 LYS A H    1 
ATOM   3454 H  HA   . LYS A 1 219 ? -4.29600  15.96500 19.75700 1.000 43.28558  ? 219 LYS A HA   1 
ATOM   3455 H  HB2  . LYS A 1 219 ? -5.83800  18.04300 18.66000 1.000 47.67558  ? 219 LYS A HB2  1 
ATOM   3456 H  HB3  . LYS A 1 219 ? -4.47500  17.60500 17.97100 1.000 47.67558  ? 219 LYS A HB3  1 
ATOM   3457 H  HG2  . LYS A 1 219 ? -5.45300  15.41800 17.73100 1.000 52.75558  ? 219 LYS A HG2  1 
ATOM   3458 H  HG3  . LYS A 1 219 ? -6.83800  16.09500 18.11800 1.000 52.75558  ? 219 LYS A HG3  1 
ATOM   3459 H  HD2  . LYS A 1 219 ? -6.39500  17.63200 16.26800 1.000 78.36558  ? 219 LYS A HD2  1 
ATOM   3460 H  HD3  . LYS A 1 219 ? -5.31200  16.56800 15.79900 1.000 78.36558  ? 219 LYS A HD3  1 
ATOM   3461 H  HE2  . LYS A 1 219 ? -7.79000  16.55900 15.04400 1.000 78.51558  ? 219 LYS A HE2  1 
ATOM   3462 H  HE3  . LYS A 1 219 ? -6.80300  15.32300 14.88900 1.000 78.51558  ? 219 LYS A HE3  1 
ATOM   3463 H  HZ1  . LYS A 1 219 ? -8.73900  14.68600 15.87100 1.000 107.82558 ? 219 LYS A HZ1  1 
ATOM   3464 H  HZ2  . LYS A 1 219 ? -7.65700  14.48700 16.81400 1.000 107.82558 ? 219 LYS A HZ2  1 
ATOM   3465 H  HZ3  . LYS A 1 219 ? -8.55100  15.61700 16.96500 1.000 107.82558 ? 219 LYS A HZ3  1 
ATOM   3466 N  N    . GLY A 1 220 ? -4.02900  18.94100 20.88700 1.000 41.49133  ? 220 GLY A N    1 
ATOM   3467 C  CA   . GLY A 1 220 ? -3.11400  19.97800 21.29700 1.000 48.21657  ? 220 GLY A CA   1 
ATOM   3468 C  C    . GLY A 1 220 ? -3.59500  21.35400 20.89500 1.000 45.80938  ? 220 GLY A C    1 
ATOM   3469 O  O    . GLY A 1 220 ? -4.02900  21.56900 19.75700 1.000 44.62326  ? 220 GLY A O    1 
ATOM   3470 H  H    . GLY A 1 220 ? -4.85500  19.13300 21.03000 1.000 45.24558  ? 220 GLY A H    1 
ATOM   3471 H  HA2  . GLY A 1 220 ? -3.01500  19.95700 22.26200 1.000 53.86558  ? 220 GLY A HA2  1 
ATOM   3472 H  HA3  . GLY A 1 220 ? -2.24800  19.82400 20.88800 1.000 53.86558  ? 220 GLY A HA3  1 
ATOM   3473 N  N    . VAL A 1 221 ? -3.53200  22.29000 21.83100 1.000 41.43660  ? 221 VAL A N    1 
ATOM   3474 C  CA   . VAL A 1 221 ? -3.85300  23.68800 21.58300 1.000 43.34746  ? 221 VAL A CA   1 
ATOM   3475 C  C    . VAL A 1 221 ? -2.60000  24.50600 21.84700 1.000 55.28293  ? 221 VAL A C    1 
ATOM   3476 O  O    . VAL A 1 221 ? -1.85100  24.22600 22.79100 1.000 48.37294  ? 221 VAL A O    1 
ATOM   3477 C  CB   . VAL A 1 221 ? -5.02200  24.18200 22.45800 1.000 44.72951  ? 221 VAL A CB   1 
ATOM   3478 C  CG1  . VAL A 1 221 ? -6.27000  23.35800 22.18900 1.000 50.38242  ? 221 VAL A CG1  1 
ATOM   3479 C  CG2  . VAL A 1 221 ? -4.66600  24.11300 23.92800 1.000 44.69153  ? 221 VAL A CG2  1 
ATOM   3480 H  H    . VAL A 1 221 ? -3.29800  22.13500 22.64400 1.000 47.29558  ? 221 VAL A H    1 
ATOM   3481 H  HA   . VAL A 1 221 ? -4.11500  23.79700 20.65500 1.000 50.17558  ? 221 VAL A HA   1 
ATOM   3482 H  HB   . VAL A 1 221 ? -5.20200  25.10800 22.23100 1.000 52.60558  ? 221 VAL A HB   1 
ATOM   3483 H  HG11 . VAL A 1 221 ? -7.00500  23.72100 22.70700 1.000 59.28558  ? 221 VAL A HG11 1 
ATOM   3484 H  HG12 . VAL A 1 221 ? -6.47800  23.40100 21.24300 1.000 59.28558  ? 221 VAL A HG12 1 
ATOM   3485 H  HG13 . VAL A 1 221 ? -6.10300  22.43900 22.45000 1.000 59.28558  ? 221 VAL A HG13 1 
ATOM   3486 H  HG21 . VAL A 1 221 ? -5.46300  24.28300 24.45500 1.000 52.83558  ? 221 VAL A HG21 1 
ATOM   3487 H  HG22 . VAL A 1 221 ? -4.32000  23.23000 24.12800 1.000 52.83558  ? 221 VAL A HG22 1 
ATOM   3488 H  HG23 . VAL A 1 221 ? -3.99200  24.78400 24.12200 1.000 52.83558  ? 221 VAL A HG23 1 
ATOM   3489 N  N    . ASP A 1 222 ? -2.37000  25.50600 21.00400 1.000 44.98911  ? 222 ASP A N    1 
ATOM   3490 C  CA   . ASP A 1 222 ? -1.22700  26.39000 21.16800 1.000 52.84262  ? 222 ASP A CA   1 
ATOM   3491 C  C    . ASP A 1 222 ? -1.53400  27.44000 22.22400 1.000 57.35957  ? 222 ASP A C    1 
ATOM   3492 O  O    . ASP A 1 222 ? -2.56700  28.11100 22.16500 1.000 51.38212  ? 222 ASP A O    1 
ATOM   3493 C  CB   . ASP A 1 222 ? -0.87700  27.05000 19.84000 1.000 53.18920  ? 222 ASP A CB   1 
ATOM   3494 C  CG   . ASP A 1 222 ? -0.52000  26.04100 18.77700 1.000 77.55457  ? 222 ASP A CG   1 
ATOM   3495 O  OD1  . ASP A 1 222 ? 0.01200   24.97200 19.14400 1.000 67.30830  ? 222 ASP A OD1  1 
ATOM   3496 O  OD2  . ASP A 1 222 ? -0.76200  26.31600 17.58200 1.000 95.56857  ? 222 ASP A OD2  1 
ATOM   3497 H  H    . ASP A 1 222 ? -2.86400  25.69300 20.32600 1.000 52.32558  ? 222 ASP A H    1 
ATOM   3498 H  HA   . ASP A 1 222 ? -0.45700  25.88000 21.46300 1.000 61.87558  ? 222 ASP A HA   1 
ATOM   3499 H  HB2  . ASP A 1 222 ? -1.64100  27.56000 19.52700 1.000 62.05558  ? 222 ASP A HB2  1 
ATOM   3500 H  HB3  . ASP A 1 222 ? -0.11600  27.63700 19.96800 1.000 62.05558  ? 222 ASP A HB3  1 
ATOM   3501 N  N    . ILE A 1 223 ? -0.64400  27.56000 23.20300 1.000 44.11130  ? 223 ILE A N    1 
ATOM   3502 C  CA   . ILE A 1 223 ? -0.76700  28.58800 24.23400 1.000 38.89412  ? 223 ILE A CA   1 
ATOM   3503 C  C    . ILE A 1 223 ? 0.56800   29.30900 24.34700 1.000 49.99205  ? 223 ILE A C    1 
ATOM   3504 O  O    . ILE A 1 223 ? 1.61700   28.78100 23.94600 1.000 47.80706  ? 223 ILE A O    1 
ATOM   3505 C  CB   . ILE A 1 223 ? -1.19100  27.99200 25.59600 1.000 50.86770  ? 223 ILE A CB   1 
ATOM   3506 C  CG1  . ILE A 1 223 ? -0.06200  27.13700 26.17900 1.000 50.38261  ? 223 ILE A CG1  1 
ATOM   3507 C  CG2  . ILE A 1 223 ? -2.49800  27.20700 25.45400 1.000 60.88215  ? 223 ILE A CG2  1 
ATOM   3508 C  CD1  . ILE A 1 223 ? -0.41500  26.47500 27.49800 1.000 51.01713  ? 223 ILE A CD1  1 
ATOM   3509 H  H    . ILE A 1 223 ? 0.04600   27.05400 23.29500 1.000 52.05558  ? 223 ILE A H    1 
ATOM   3510 H  HA   . ILE A 1 223 ? -1.44200  29.23000 23.96400 1.000 46.09558  ? 223 ILE A HA   1 
ATOM   3511 H  HB   . ILE A 1 223 ? -1.35600  28.71600 26.22000 1.000 60.39558  ? 223 ILE A HB   1 
ATOM   3512 H  HG12 . ILE A 1 223 ? 0.15900   26.43700 25.54500 1.000 59.29558  ? 223 ILE A HG12 1 
ATOM   3513 H  HG13 . ILE A 1 223 ? 0.71200   27.70300 26.33000 1.000 59.29558  ? 223 ILE A HG13 1 
ATOM   3514 H  HG21 . ILE A 1 223 ? -2.75900  26.86700 26.32400 1.000 72.58558  ? 223 ILE A HG21 1 
ATOM   3515 H  HG22 . ILE A 1 223 ? -3.18600  27.79900 25.11100 1.000 72.58558  ? 223 ILE A HG22 1 
ATOM   3516 H  HG23 . ILE A 1 223 ? -2.35900  26.47000 24.83900 1.000 72.58558  ? 223 ILE A HG23 1 
ATOM   3517 H  HD11 . ILE A 1 223 ? 0.35300   25.97500 27.81600 1.000 59.84558  ? 223 ILE A HD11 1 
ATOM   3518 H  HD12 . ILE A 1 223 ? -0.65400  27.16000 28.14100 1.000 59.84558  ? 223 ILE A HD12 1 
ATOM   3519 H  HD13 . ILE A 1 223 ? -1.16500  25.87500 27.35900 1.000 59.84558  ? 223 ILE A HD13 1 
ATOM   3520 N  N    . PRO A 1 224 ? 0.56400   30.52300 24.89200 1.000 59.21934  ? 224 PRO A N    1 
ATOM   3521 C  CA   . PRO A 1 224 ? 1.83100   31.23200 25.09700 1.000 52.70793  ? 224 PRO A CA   1 
ATOM   3522 C  C    . PRO A 1 224 ? 2.65700   30.55900 26.18200 1.000 44.86566  ? 224 PRO A C    1 
ATOM   3523 O  O    . PRO A 1 224 ? 2.13600   30.15100 27.22100 1.000 48.23896  ? 224 PRO A O    1 
ATOM   3524 C  CB   . PRO A 1 224 ? 1.39900   32.64600 25.51700 1.000 54.74970  ? 224 PRO A CB   1 
ATOM   3525 C  CG   . PRO A 1 224 ? -0.10200  32.68300 25.43500 1.000 65.55439  ? 224 PRO A CG   1 
ATOM   3526 C  CD   . PRO A 1 224 ? -0.59000  31.27100 25.42200 1.000 63.62570  ? 224 PRO A CD   1 
ATOM   3527 H  HA   . PRO A 1 224 ? 2.33900   31.28400 24.27200 1.000 62.44558  ? 224 PRO A HA   1 
ATOM   3528 H  HB2  . PRO A 1 224 ? 1.69500   32.81800 26.42400 1.000 64.99558  ? 224 PRO A HB2  1 
ATOM   3529 H  HB3  . PRO A 1 224 ? 1.78900   33.29600 24.91100 1.000 64.99558  ? 224 PRO A HB3  1 
ATOM   3530 H  HG2  . PRO A 1 224 ? -0.45300  33.15300 26.20700 1.000 78.26558  ? 224 PRO A HG2  1 
ATOM   3531 H  HG3  . PRO A 1 224 ? -0.36700  33.13800 24.62000 1.000 78.26558  ? 224 PRO A HG3  1 
ATOM   3532 H  HD2  . PRO A 1 224 ? -0.81300  30.97400 26.31800 1.000 75.96558  ? 224 PRO A HD2  1 
ATOM   3533 H  HD3  . PRO A 1 224 ? -1.36100  31.17700 24.84100 1.000 75.96558  ? 224 PRO A HD3  1 
ATOM   3534 N  N    . CYS A 1 225 ? 3.94500   30.40600 25.91600 1.000 41.71784  ? 225 CYS A N    1 
ATOM   3535 C  CA   . CYS A 1 225 ? 4.89400   30.00800 26.94300 1.000 34.99300  ? 225 CYS A CA   1 
ATOM   3536 C  C    . CYS A 1 225 ? 5.54700   31.24500 27.53400 1.000 40.06592  ? 225 CYS A C    1 
ATOM   3537 O  O    . CYS A 1 225 ? 5.62500   32.30500 26.89900 1.000 40.17442  ? 225 CYS A O    1 
ATOM   3538 C  CB   . CYS A 1 225 ? 5.96700   29.07100 26.39200 1.000 38.19905  ? 225 CYS A CB   1 
ATOM   3539 S  SG   . CYS A 1 225 ? 7.04100   28.37700 27.67900 1.000 41.87722  ? 225 CYS A SG   1 
ATOM   3540 H  H    . CYS A 1 225 ? 4.29700   30.52800 25.14100 1.000 48.43558  ? 225 CYS A H    1 
ATOM   3541 H  HA   . CYS A 1 225 ? 4.42400   29.52600 27.64100 1.000 39.74558  ? 225 CYS A HA   1 
ATOM   3542 H  HB2  . CYS A 1 225 ? 5.53400   28.33400 25.93400 1.000 43.24558  ? 225 CYS A HB2  1 
ATOM   3543 H  HB3  . CYS A 1 225 ? 6.52500   29.56500 25.77100 1.000 43.24558  ? 225 CYS A HB3  1 
ATOM   3544 N  N    . THR A 1 226 ? 6.03600   31.09500 28.76700 1.000 45.47110  ? 226 THR A N    1 
ATOM   3545 C  CA   . THR A 1 226 ? 6.68500   32.21800 29.42200 1.000 44.41732  ? 226 THR A CA   1 
ATOM   3546 C  C    . THR A 1 226 ? 7.91500   32.67100 28.64800 1.000 49.01676  ? 226 THR A C    1 
ATOM   3547 O  O    . THR A 1 226 ? 8.27600   33.85000 28.69300 1.000 46.68778  ? 226 THR A O    1 
ATOM   3548 C  CB   . THR A 1 226 ? 7.06000   31.85000 30.86100 1.000 51.65431  ? 226 THR A CB   1 
ATOM   3549 O  OG1  . THR A 1 226 ? 7.89600   32.87800 31.40100 1.000 73.90705  ? 226 THR A OG1  1 
ATOM   3550 C  CG2  . THR A 1 226 ? 7.79300   30.50900 30.93000 1.000 52.60099  ? 226 THR A CG2  1 
ATOM   3551 H  H    . THR A 1 226 ? 6.00300   30.37100 29.23000 1.000 51.32558  ? 226 THR A H    1 
ATOM   3552 H  HA   . THR A 1 226 ? 6.06300   32.96100 29.46200 1.000 49.54558  ? 226 THR A HA   1 
ATOM   3553 H  HB   . THR A 1 226 ? 6.25100   31.76400 31.38800 1.000 57.16558  ? 226 THR A HB   1 
ATOM   3554 H  HG1  . THR A 1 226 ? 8.11500   32.68600 32.18900 1.000 83.15558  ? 226 THR A HG1  1 
ATOM   3555 H  HG21 . THR A 1 226 ? 8.22300   30.41100 31.79300 1.000 57.96558  ? 226 THR A HG21 1 
ATOM   3556 H  HG22 . THR A 1 226 ? 7.16400   29.78100 30.80600 1.000 57.96558  ? 226 THR A HG22 1 
ATOM   3557 H  HG23 . THR A 1 226 ? 8.46800   30.46400 30.23500 1.000 57.96558  ? 226 THR A HG23 1 
ATOM   3558 N  N    . CYS A 1 227 ? 8.56000   31.75900 27.91900 1.000 43.45634  ? 227 CYS A N    1 
ATOM   3559 C  CA   . CYS A 1 227 ? 9.73300   32.13300 27.13900 1.000 42.00584  ? 227 CYS A CA   1 
ATOM   3560 C  C    . CYS A 1 227 ? 9.37700   32.94900 25.90700 1.000 37.91438  ? 227 CYS A C    1 
ATOM   3561 O  O    . CYS A 1 227 ? 10.28800  33.48900 25.27100 1.000 42.93188  ? 227 CYS A O    1 
ATOM   3562 C  CB   . CYS A 1 227 ? 10.50800  30.88500 26.72300 1.000 39.49167  ? 227 CYS A CB   1 
ATOM   3563 S  SG   . CYS A 1 227 ? 9.71400   29.97900 25.39800 1.000 38.13271  ? 227 CYS A SG   1 
ATOM   3564 H  H    . CYS A 1 227 ? 8.34000   30.93000 27.86200 1.000 48.60558  ? 227 CYS A H    1 
ATOM   3565 H  HA   . CYS A 1 227 ? 10.31600  32.67100 27.69600 1.000 46.79558  ? 227 CYS A HA   1 
ATOM   3566 H  HB2  . CYS A 1 227 ? 11.39000  31.14900 26.41800 1.000 43.48558  ? 227 CYS A HB2  1 
ATOM   3567 H  HB3  . CYS A 1 227 ? 10.58400  30.29200 27.48700 1.000 43.48558  ? 227 CYS A HB3  1 
ATOM   3568 N  N    . GLY A 1 228 ? 8.08800   33.06100 25.56800 1.000 34.65898  ? 228 GLY A N    1 
ATOM   3569 C  CA   . GLY A 1 228 ? 7.62300   33.83200 24.43200 1.000 34.11473  ? 228 GLY A CA   1 
ATOM   3570 C  C    . GLY A 1 228 ? 7.19900   33.00400 23.24000 1.000 33.45619  ? 228 GLY A C    1 
ATOM   3571 O  O    . GLY A 1 228 ? 6.44400   33.50200 22.40400 1.000 32.85297  ? 228 GLY A O    1 
ATOM   3572 H  H    . GLY A 1 228 ? 7.44900   32.68300 26.00100 1.000 39.36558  ? 228 GLY A H    1 
ATOM   3573 H  HA2  . GLY A 1 228 ? 6.86200   34.36600 24.70800 1.000 39.17558  ? 228 GLY A HA2  1 
ATOM   3574 H  HA3  . GLY A 1 228 ? 8.33600   34.42400 24.14400 1.000 39.17558  ? 228 GLY A HA3  1 
ATOM   3575 N  N    . ARG A 1 229 ? 7.67400   31.75900 23.13700 1.000 33.92809  ? 229 ARG A N    1 
ATOM   3576 C  CA   . ARG A 1 229 ? 7.23600   30.84900 22.09400 1.000 34.28073  ? 229 ARG A CA   1 
ATOM   3577 C  C    . ARG A 1 229 ? 5.81500   30.38200 22.36800 1.000 42.41056  ? 229 ARG A C    1 
ATOM   3578 O  O    . ARG A 1 229 ? 5.26500   30.59300 23.45100 1.000 38.06637  ? 229 ARG A O    1 
ATOM   3579 C  CB   . ARG A 1 229 ? 8.15400   29.62200 22.02800 1.000 41.70374  ? 229 ARG A CB   1 
ATOM   3580 C  CG   . ARG A 1 229 ? 9.57600   29.90900 21.59900 1.000 41.46420  ? 229 ARG A CG   1 
ATOM   3581 C  CD   . ARG A 1 229 ? 10.42900  28.63200 21.58000 1.000 43.03467  ? 229 ARG A CD   1 
ATOM   3582 N  NE   . ARG A 1 229 ? 9.91600   27.60200 20.68000 1.000 44.30406  ? 229 ARG A NE   1 
ATOM   3583 C  CZ   . ARG A 1 229 ? 9.98200   27.66100 19.35400 1.000 56.26583  ? 229 ARG A CZ   1 
ATOM   3584 N  NH1  . ARG A 1 229 ? 10.54700  28.68200 18.73700 1.000 45.03507  ? 229 ARG A NH1  1 
ATOM   3585 N  NH2  . ARG A 1 229 ? 9.50000   26.65400 18.63100 1.000 54.21915  ? 229 ARG A NH2  1 
ATOM   3586 H  H    . ARG A 1 229 ? 8.25900   31.42000 23.66900 1.000 38.98558  ? 229 ARG A H    1 
ATOM   3587 H  HA   . ARG A 1 229 ? 7.26600   31.31200 21.24200 1.000 39.33558  ? 229 ARG A HA   1 
ATOM   3588 H  HB2  . ARG A 1 229 ? 8.19200   29.21900 22.91000 1.000 47.54558  ? 229 ARG A HB2  1 
ATOM   3589 H  HB3  . ARG A 1 229 ? 7.78000   28.99200 21.39200 1.000 47.54558  ? 229 ARG A HB3  1 
ATOM   3590 H  HG2  . ARG A 1 229 ? 9.57100   30.28600 20.70500 1.000 46.96558  ? 229 ARG A HG2  1 
ATOM   3591 H  HG3  . ARG A 1 229 ? 9.97800   30.53500 22.22100 1.000 46.96558  ? 229 ARG A HG3  1 
ATOM   3592 H  HD2  . ARG A 1 229 ? 11.32600  28.85900 21.29000 1.000 47.99558  ? 229 ARG A HD2  1 
ATOM   3593 H  HD3  . ARG A 1 229 ? 10.45400  28.25800 22.47500 1.000 47.99558  ? 229 ARG A HD3  1 
ATOM   3594 H  HE   . ARG A 1 229 ? 9.54700   26.90900 21.03200 1.000 49.05558  ? 229 ARG A HE   1 
ATOM   3595 H  HH11 . ARG A 1 229 ? 10.58000  28.70100 17.87800 1.000 49.96558  ? 229 ARG A HH11 1 
ATOM   3596 H  HH12 . ARG A 1 229 ? 10.88300  29.32800 19.19400 1.000 49.96558  ? 229 ARG A HH12 1 
ATOM   3597 H  HH21 . ARG A 1 229 ? 9.14900   25.97300 19.02200 1.000 60.01558  ? 229 ARG A HH21 1 
ATOM   3598 H  HH22 . ARG A 1 229 ? 9.53800   26.68400 17.77200 1.000 60.01558  ? 229 ARG A HH22 1 
ATOM   3599 N  N    . ARG A 1 230 ? 5.25400   29.65700 21.38800 1.000 39.16792  ? 230 ARG A N    1 
ATOM   3600 C  CA   . ARG A 1 230 ? 3.91700   29.03600 21.54300 1.000 45.09968  ? 230 ARG A CA   1 
ATOM   3601 C  C    . ARG A 1 230 ? 4.12500   27.55900 21.90900 1.000 47.06806  ? 230 ARG A C    1 
ATOM   3602 O  O    . ARG A 1 230 ? 4.66700   26.81700 21.05900 1.000 50.81677  ? 230 ARG A O    1 
ATOM   3603 C  CB   . ARG A 1 230 ? 3.08300   29.21200 20.26900 1.000 53.44957  ? 230 ARG A CB   1 
ATOM   3604 C  CG   . ARG A 1 230 ? 2.84800   30.66800 19.89600 1.000 61.38023  ? 230 ARG A CG   1 
ATOM   3605 C  CD   . ARG A 1 230 ? 1.87300   31.36200 20.82600 1.000 64.00988  ? 230 ARG A CD   1 
ATOM   3606 N  NE   . ARG A 1 230 ? 1.61000   32.75200 20.44000 1.000 89.65398  ? 230 ARG A NE   1 
ATOM   3607 C  CZ   . ARG A 1 230 ? 2.49200   33.74200 20.33600 1.000 80.49216  ? 230 ARG A CZ   1 
ATOM   3608 N  NH1  . ARG A 1 230 ? 3.77700   33.56400 20.58900 1.000 66.12096  ? 230 ARG A NH1  1 
ATOM   3609 N  NH2  . ARG A 1 230 ? 2.07200   34.93900 19.97800 1.000 45.16974  ? 230 ARG A NH2  1 
ATOM   3610 H  H    . ARG A 1 230 ? 5.64900   29.52500 20.58700 1.000 45.25558  ? 230 ARG A H    1 
ATOM   3611 H  HA   . ARG A 1 230 ? 3.44100   29.48200 22.28100 1.000 52.44558  ? 230 ARG A HA   1 
ATOM   3612 H  HB2  . ARG A 1 230 ? 3.54400   28.76600 19.52800 1.000 62.44558  ? 230 ARG A HB2  1 
ATOM   3613 H  HB3  . ARG A 1 230 ? 2.21500   28.77500 20.39000 1.000 62.44558  ? 230 ARG A HB3  1 
ATOM   3614 H  HG2  . ARG A 1 230 ? 3.70300   31.14600 19.92300 1.000 72.46558  ? 230 ARG A HG2  1 
ATOM   3615 H  HG3  . ARG A 1 230 ? 2.50500   30.71500 18.97900 1.000 72.46558  ? 230 ARG A HG3  1 
ATOM   3616 H  HD2  . ARG A 1 230 ? 1.03400   30.86200 20.84000 1.000 76.08558  ? 230 ARG A HD2  1 
ATOM   3617 H  HD3  . ARG A 1 230 ? 2.24200   31.35100 21.73100 1.000 76.08558  ? 230 ARG A HD3  1 
ATOM   3618 H  HE   . ARG A 1 230 ? 0.78700   32.95400 20.25100 1.000 107.24558 ? 230 ARG A HE   1 
ATOM   3619 H  HH11 . ARG A 1 230 ? 4.35300   34.16600 20.29900 1.000 54.24558  ? 230 ARG A HH11 1 
ATOM   3620 H  HH12 . ARG A 1 230 ? 4.06200   32.87300 21.05500 1.000 54.24558  ? 230 ARG A HH12 1 
ATOM   3621 H  HH21 . ARG A 1 230 ? 1.90000   35.11000 19.13000 1.000 79.28558  ? 230 ARG A HH21 1 
ATOM   3622 H  HH22 . ARG A 1 230 ? 1.95300   35.56100 20.59500 1.000 79.28558  ? 230 ARG A HH22 1 
ATOM   3623 N  N    . ALA A 1 231 ? 3.74100   27.15000 23.11700 1.000 43.63794  ? 231 ALA A N    1 
ATOM   3624 C  CA   . ALA A 1 231 ? 3.80300   25.77900 23.58600 1.000 53.87049  ? 231 ALA A CA   1 
ATOM   3625 C  C    . ALA A 1 231 ? 2.52400   25.05900 23.17300 1.000 61.94630  ? 231 ALA A C    1 
ATOM   3626 O  O    . ALA A 1 231 ? 1.53500   25.68000 22.77900 1.000 48.79622  ? 231 ALA A O    1 
ATOM   3627 C  CB   . ALA A 1 231 ? 3.97600   25.74800 25.10000 1.000 45.41405  ? 231 ALA A CB   1 
ATOM   3628 H  H    . ALA A 1 231 ? 3.24500   27.65200 23.60800 1.000 50.21558  ? 231 ALA A H    1 
ATOM   3629 H  HA   . ALA A 1 231 ? 4.56300   25.32100 23.19400 1.000 61.96558  ? 231 ALA A HA   1 
ATOM   3630 H  HB1  . ALA A 1 231 ? 4.02400   24.82500 25.39400 1.000 51.78558  ? 231 ALA A HB1  1 
ATOM   3631 H  HB2  . ALA A 1 231 ? 4.79500   26.21300 25.33300 1.000 51.78558  ? 231 ALA A HB2  1 
ATOM   3632 H  HB3  . ALA A 1 231 ? 3.21700   26.18800 25.51300 1.000 51.78558  ? 231 ALA A HB3  1 
ATOM   3633 N  N    . THR A 1 232 ? 2.55400   23.73200 23.26900 1.000 47.43811  ? 232 THR A N    1 
ATOM   3634 C  CA   . THR A 1 232 ? 1.40300   22.89100 22.96500 1.000 44.11793  ? 232 THR A CA   1 
ATOM   3635 C  C    . THR A 1 232 ? 0.89600   22.29000 24.26700 1.000 44.70054  ? 232 THR A C    1 
ATOM   3636 O  O    . THR A 1 232 ? 1.65900   21.64200 24.99300 1.000 42.70877  ? 232 THR A O    1 
ATOM   3637 C  CB   . THR A 1 232 ? 1.76100   21.78800 21.96600 1.000 52.13723  ? 232 THR A CB   1 
ATOM   3638 O  OG1  . THR A 1 232 ? 2.17900   22.37200 20.72600 1.000 58.47120  ? 232 THR A OG1  1 
ATOM   3639 C  CG2  . THR A 1 232 ? 0.55700   20.87800 21.71000 1.000 55.31352  ? 232 THR A CG2  1 
ATOM   3640 H  H    . THR A 1 232 ? 3.24800   23.28700 23.51500 1.000 53.73558  ? 232 THR A H    1 
ATOM   3641 H  HA   . THR A 1 232 ? 0.70100   23.43100 22.57000 1.000 49.66558  ? 232 THR A HA   1 
ATOM   3642 H  HB   . THR A 1 232 ? 2.48200   21.25100 22.33100 1.000 58.27558  ? 232 THR A HB   1 
ATOM   3643 H  HG1  . THR A 1 232 ? 2.35100   21.76900 20.16800 1.000 65.59558  ? 232 THR A HG1  1 
ATOM   3644 H  HG21 . THR A 1 232 ? 0.71800   20.32500 20.93000 1.000 61.89558  ? 232 THR A HG21 1 
ATOM   3645 H  HG22 . THR A 1 232 ? 0.40600   20.30300 22.47700 1.000 61.89558  ? 232 THR A HG22 1 
ATOM   3646 H  HG23 . THR A 1 232 ? -0.23800  21.41300 21.55800 1.000 61.89558  ? 232 THR A HG23 1 
ATOM   3647 N  N    . LYS A 1 233 ? -0.37900  22.52400 24.56800 1.000 39.52516  ? 233 LYS A N    1 
ATOM   3648 C  CA   . LYS A 1 233 ? -1.05400  21.93100 25.71300 1.000 41.27347  ? 233 LYS A CA   1 
ATOM   3649 C  C    . LYS A 1 233 ? -2.01800  20.86900 25.20400 1.000 39.24677  ? 233 LYS A C    1 
ATOM   3650 O  O    . LYS A 1 233 ? -2.79600  21.13300 24.28300 1.000 39.91037  ? 233 LYS A O    1 
ATOM   3651 C  CB   . LYS A 1 233 ? -1.81000  22.99100 26.51900 1.000 41.12160  ? 233 LYS A CB   1 
ATOM   3652 C  CG   . LYS A 1 233 ? -2.76900  22.42900 27.56300 1.000 48.91094  ? 233 LYS A CG   1 
ATOM   3653 C  CD   . LYS A 1 233 ? -3.51000  23.53400 28.29700 1.000 51.75461  ? 233 LYS A CD   1 
ATOM   3654 C  CE   . LYS A 1 233 ? -2.72100  24.02500 29.49000 1.000 52.42935  ? 233 LYS A CE   1 
ATOM   3655 N  NZ   . LYS A 1 233 ? -3.40700  25.13800 30.20200 1.000 50.40826  ? 233 LYS A NZ   1 
ATOM   3656 H  H    . LYS A 1 233 ? -0.88800  23.04200 24.10700 1.000 44.92558  ? 233 LYS A H    1 
ATOM   3657 H  HA   . LYS A 1 233 ? -0.40600  21.51500 26.30400 1.000 47.18558  ? 233 LYS A HA   1 
ATOM   3658 H  HB2  . LYS A 1 233 ? -1.16300  23.54500 26.98400 1.000 47.68558  ? 233 LYS A HB2  1 
ATOM   3659 H  HB3  . LYS A 1 233 ? -2.33000  23.53200 25.90500 1.000 47.68558  ? 233 LYS A HB3  1 
ATOM   3660 H  HG2  . LYS A 1 233 ? -3.42300  21.86300 27.12600 1.000 57.20558  ? 233 LYS A HG2  1 
ATOM   3661 H  HG3  . LYS A 1 233 ? -2.26800  21.91500 28.21500 1.000 57.20558  ? 233 LYS A HG3  1 
ATOM   3662 H  HD2  . LYS A 1 233 ? -3.65200  24.28200 27.69600 1.000 61.06558  ? 233 LYS A HD2  1 
ATOM   3663 H  HD3  . LYS A 1 233 ? -4.36300  23.19600 28.61300 1.000 61.06558  ? 233 LYS A HD3  1 
ATOM   3664 H  HE2  . LYS A 1 233 ? -2.60400  23.29400 30.11600 1.000 61.50558  ? 233 LYS A HE2  1 
ATOM   3665 H  HE3  . LYS A 1 233 ? -1.85700  24.34700 29.18900 1.000 61.50558  ? 233 LYS A HE3  1 
ATOM   3666 H  HZ1  . LYS A 1 233 ? -2.91700  25.40300 30.89600 1.000 59.23558  ? 233 LYS A HZ1  1 
ATOM   3667 H  HZ2  . LYS A 1 233 ? -3.52200  25.82700 29.65000 1.000 59.23558  ? 233 LYS A HZ2  1 
ATOM   3668 H  HZ3  . LYS A 1 233 ? -4.20200  24.86800 30.49600 1.000 59.23558  ? 233 LYS A HZ3  1 
ATOM   3669 N  N    . TYR A 1 234 ? -1.96400  19.67300 25.78100 1.000 37.88865  ? 234 TYR A N    1 
ATOM   3670 C  CA   . TYR A 1 234 ? -2.86400  18.61600 25.34700 1.000 38.48802  ? 234 TYR A CA   1 
ATOM   3671 C  C    . TYR A 1 234 ? -3.27500  17.75000 26.52700 1.000 40.52272  ? 234 TYR A C    1 
ATOM   3672 O  O    . TYR A 1 234 ? -2.62700  17.71500 27.57500 1.000 39.22021  ? 234 TYR A O    1 
ATOM   3673 C  CB   . TYR A 1 234 ? -2.23000  17.79100 24.22300 1.000 43.32308  ? 234 TYR A CB   1 
ATOM   3674 C  CG   . TYR A 1 234 ? -1.09900  16.90300 24.66000 1.000 42.64066  ? 234 TYR A CG   1 
ATOM   3675 C  CD1  . TYR A 1 234 ? -1.34600  15.66000 25.22300 1.000 44.77802  ? 234 TYR A CD1  1 
ATOM   3676 C  CD2  . TYR A 1 234 ? 0.22200   17.31700 24.53000 1.000 41.97675  ? 234 TYR A CD2  1 
ATOM   3677 C  CE1  . TYR A 1 234 ? -0.30700  14.84200 25.62600 1.000 45.28323  ? 234 TYR A CE1  1 
ATOM   3678 C  CE2  . TYR A 1 234 ? 1.26500   16.51100 24.93700 1.000 46.67811  ? 234 TYR A CE2  1 
ATOM   3679 C  CZ   . TYR A 1 234 ? 0.99500   15.27500 25.48400 1.000 49.92043  ? 234 TYR A CZ   1 
ATOM   3680 O  OH   . TYR A 1 234 ? 2.03700   14.46300 25.89100 1.000 53.35026  ? 234 TYR A OH   1 
ATOM   3681 H  H    . TYR A 1 234 ? -1.42500  19.45600 26.41500 1.000 42.54558  ? 234 TYR A H    1 
ATOM   3682 H  HA   . TYR A 1 234 ? -3.68600  19.00400 25.00900 1.000 43.02558  ? 234 TYR A HA   1 
ATOM   3683 H  HB2  . TYR A 1 234 ? -2.91300  17.22400 23.83300 1.000 47.77558  ? 234 TYR A HB2  1 
ATOM   3684 H  HB3  . TYR A 1 234 ? -1.88200  18.40000 23.55200 1.000 47.77558  ? 234 TYR A HB3  1 
ATOM   3685 H  HD1  . TYR A 1 234 ? -2.22400  15.37300 25.33000 1.000 48.27558  ? 234 TYR A HD1  1 
ATOM   3686 H  HD2  . TYR A 1 234 ? 0.40500   18.15100 24.16300 1.000 44.97558  ? 234 TYR A HD2  1 
ATOM   3687 H  HE1  . TYR A 1 234 ? -0.48500  14.00600 25.99100 1.000 48.02558  ? 234 TYR A HE1  1 
ATOM   3688 H  HE2  . TYR A 1 234 ? 2.14400   16.79900 24.84300 1.000 49.77558  ? 234 TYR A HE2  1 
ATOM   3689 H  HH   . TYR A 1 234 ? 2.77200   14.81700 25.69100 1.000 56.35558  ? 234 TYR A HH   1 
ATOM   3690 N  N    . LEU A 1 235 ? -4.40300  17.07000 26.34300 1.000 36.43563  ? 235 LEU A N    1 
ATOM   3691 C  CA   . LEU A 1 235 ? -5.00100  16.24600 27.38000 1.000 33.36657  ? 235 LEU A CA   1 
ATOM   3692 C  C    . LEU A 1 235 ? -4.32500  14.88000 27.43500 1.000 37.54268  ? 235 LEU A C    1 
ATOM   3693 O  O    . LEU A 1 235 ? -4.34800  14.12900 26.45200 1.000 40.31876  ? 235 LEU A O    1 
ATOM   3694 C  CB   . LEU A 1 235 ? -6.48600  16.09100 27.09400 1.000 35.11068  ? 235 LEU A CB   1 
ATOM   3695 C  CG   . LEU A 1 235 ? -7.28400  15.26500 28.07900 1.000 33.15850  ? 235 LEU A CG   1 
ATOM   3696 C  CD1  . LEU A 1 235 ? -7.20500  15.81300 29.48700 1.000 32.57614  ? 235 LEU A CD1  1 
ATOM   3697 C  CD2  . LEU A 1 235 ? -8.71700  15.24900 27.60500 1.000 29.18950  ? 235 LEU A CD2  1 
ATOM   3698 H  H    . LEU A 1 235 ? -4.85000  17.07200 25.60800 1.000 40.72558  ? 235 LEU A H    1 
ATOM   3699 H  HA   . LEU A 1 235 ? -4.87400  16.67000 28.24400 1.000 37.18558  ? 235 LEU A HA   1 
ATOM   3700 H  HB2  . LEU A 1 235 ? -6.88200  16.97600 27.07800 1.000 39.75558  ? 235 LEU A HB2  1 
ATOM   3701 H  HB3  . LEU A 1 235 ? -6.58100  15.66800 26.22600 1.000 39.75558  ? 235 LEU A HB3  1 
ATOM   3702 H  HG   . LEU A 1 235 ? -6.92200  14.36600 28.12100 1.000 37.64558  ? 235 LEU A HG   1 
ATOM   3703 H  HD11 . LEU A 1 235 ? -7.78800  15.29300 30.06100 1.000 37.39558  ? 235 LEU A HD11 1 
ATOM   3704 H  HD12 . LEU A 1 235 ? -6.28900  15.74700 29.79900 1.000 37.39558  ? 235 LEU A HD12 1 
ATOM   3705 H  HD13 . LEU A 1 235 ? -7.48700  16.74100 29.48100 1.000 37.39558  ? 235 LEU A HD13 1 
ATOM   3706 H  HD21 . LEU A 1 235 ? -9.24900  14.72700 28.22500 1.000 33.35558  ? 235 LEU A HD21 1 
ATOM   3707 H  HD22 . LEU A 1 235 ? -9.04800  16.16000 27.57000 1.000 33.35558  ? 235 LEU A HD22 1 
ATOM   3708 H  HD23 . LEU A 1 235 ? -8.75200  14.85000 26.72200 1.000 33.35558  ? 235 LEU A HD23 1 
ATOM   3709 N  N    . VAL A 1 236 ? -3.74200  14.55500 28.58100 1.000 39.00360  ? 236 VAL A N    1 
ATOM   3710 C  CA   . VAL A 1 236 ? -3.08600  13.26000 28.76800 1.000 39.62392  ? 236 VAL A CA   1 
ATOM   3711 C  C    . VAL A 1 236 ? -4.07900  12.21000 29.23700 1.000 42.97365  ? 236 VAL A C    1 
ATOM   3712 O  O    . VAL A 1 236 ? -4.10700  11.08700 28.72700 1.000 41.32758  ? 236 VAL A O    1 
ATOM   3713 C  CB   . VAL A 1 236 ? -1.91500  13.39100 29.76900 1.000 42.29722  ? 236 VAL A CB   1 
ATOM   3714 C  CG1  . VAL A 1 236 ? -1.32300  12.02100 30.08200 1.000 44.56291  ? 236 VAL A CG1  1 
ATOM   3715 C  CG2  . VAL A 1 236 ? -0.83800  14.31300 29.23500 1.000 38.28803  ? 236 VAL A CG2  1 
ATOM   3716 H  H    . VAL A 1 236 ? -3.71000  15.06600 29.27100 1.000 42.83558  ? 236 VAL A H    1 
ATOM   3717 H  HA   . VAL A 1 236 ? -2.72100  12.98000 27.91400 1.000 42.61558  ? 236 VAL A HA   1 
ATOM   3718 H  HB   . VAL A 1 236 ? -2.26000  13.77600 30.58900 1.000 45.45558  ? 236 VAL A HB   1 
ATOM   3719 H  HG11 . VAL A 1 236 ? -0.44900  12.14000 30.48600 1.000 47.12558  ? 236 VAL A HG11 1 
ATOM   3720 H  HG12 . VAL A 1 236 ? -1.91100  11.55600 30.69800 1.000 47.12558  ? 236 VAL A HG12 1 
ATOM   3721 H  HG13 . VAL A 1 236 ? -1.24100  11.51600 29.25800 1.000 47.12558  ? 236 VAL A HG13 1 
ATOM   3722 H  HG21 . VAL A 1 236 ? -0.11500  14.36100 29.88000 1.000 40.46558  ? 236 VAL A HG21 1 
ATOM   3723 H  HG22 . VAL A 1 236 ? -0.50900  13.96000 28.39400 1.000 40.46558  ? 236 VAL A HG22 1 
ATOM   3724 H  HG23 . VAL A 1 236 ? -1.21700  15.19500 29.09800 1.000 40.46558  ? 236 VAL A HG23 1 
ATOM   3725 N  N    . GLN A 1 237 ? -4.89800  12.56100 30.22400 1.000 37.45830  ? 237 GLN A N    1 
ATOM   3726 C  CA   . GLN A 1 237 ? -5.80100  11.60900 30.85300 1.000 34.02991  ? 237 GLN A CA   1 
ATOM   3727 C  C    . GLN A 1 237 ? -6.98600  12.35800 31.43800 1.000 38.44799  ? 237 GLN A C    1 
ATOM   3728 O  O    . GLN A 1 237 ? -6.82500  13.44200 32.00200 1.000 34.51639  ? 237 GLN A O    1 
ATOM   3729 C  CB   . GLN A 1 237 ? -5.09200  10.82200 31.95300 1.000 40.11387  ? 237 GLN A CB   1 
ATOM   3730 C  CG   . GLN A 1 237 ? -6.01900  9.91200  32.74700 1.000 56.56979  ? 237 GLN A CG   1 
ATOM   3731 C  CD   . GLN A 1 237 ? -5.26400  8.93500  33.62200 1.000 82.10574  ? 237 GLN A CD   1 
ATOM   3732 O  OE1  . GLN A 1 237 ? -4.20600  9.25800  34.17300 1.000 68.26947  ? 237 GLN A OE1  1 
ATOM   3733 N  NE2  . GLN A 1 237 ? -5.81400  7.73700  33.77200 1.000 99.82964  ? 237 GLN A NE2  1 
ATOM   3734 H  H    . GLN A 1 237 ? -4.94800  13.35600 30.55000 1.000 40.88558  ? 237 GLN A H    1 
ATOM   3735 H  HA   . GLN A 1 237 ? -6.13200  10.98600 30.18700 1.000 36.89558  ? 237 GLN A HA   1 
ATOM   3736 H  HB2  . GLN A 1 237 ? -4.40700  10.26700 31.54900 1.000 43.56558  ? 237 GLN A HB2  1 
ATOM   3737 H  HB3  . GLN A 1 237 ? -4.68800  11.44800 32.57400 1.000 43.56558  ? 237 GLN A HB3  1 
ATOM   3738 H  HG2  . GLN A 1 237 ? -6.58200  10.45500 33.32000 1.000 63.50558  ? 237 GLN A HG2  1 
ATOM   3739 H  HG3  . GLN A 1 237 ? -6.56700  9.40200  32.13000 1.000 63.50558  ? 237 GLN A HG3  1 
ATOM   3740 H  HE21 . GLN A 1 237 ? -6.55800  7.55400  33.38200 1.000 114.31558 ? 237 GLN A HE21 1 
ATOM   3741 H  HE22 . GLN A 1 237 ? -5.42600  7.14400  34.25900 1.000 114.31558 ? 237 GLN A HE22 1 
ATOM   3742 N  N    . GLN A 1 238 ? -8.16800  11.76000 31.31600 1.000 35.25875  ? 238 GLN A N    1 
ATOM   3743 C  CA   . GLN A 1 238 ? -9.40300  12.35400 31.80300 1.000 30.80438  ? 238 GLN A CA   1 
ATOM   3744 C  C    . GLN A 1 238 ? -10.23700 11.28100 32.48200 1.000 36.52952  ? 238 GLN A C    1 
ATOM   3745 O  O    . GLN A 1 238 ? -10.45800 10.21500 31.91100 1.000 37.93167  ? 238 GLN A O    1 
ATOM   3746 C  CB   . GLN A 1 238 ? -10.20100 12.99500 30.66700 1.000 32.79215  ? 238 GLN A CB   1 
ATOM   3747 C  CG   . GLN A 1 238 ? -11.43200 13.75800 31.16200 1.000 29.76732  ? 238 GLN A CG   1 
ATOM   3748 C  CD   . GLN A 1 238 ? -11.07300 15.06400 31.85100 1.000 31.22564  ? 238 GLN A CD   1 
ATOM   3749 O  OE1  . GLN A 1 238 ? -10.04100 15.65600 31.57400 1.000 31.49276  ? 238 GLN A OE1  1 
ATOM   3750 N  NE2  . GLN A 1 238 ? -11.93000 15.50500 32.76600 1.000 28.07138  ? 238 GLN A NE2  1 
ATOM   3751 H  H    . GLN A 1 238 ? -8.28000  10.99200 30.94600 1.000 39.77558  ? 238 GLN A H    1 
ATOM   3752 H  HA   . GLN A 1 238 ? -9.19300  13.04100 32.45500 1.000 35.34558  ? 238 GLN A HA   1 
ATOM   3753 H  HB2  . GLN A 1 238 ? -9.63000  13.62100 30.19500 1.000 38.17558  ? 238 GLN A HB2  1 
ATOM   3754 H  HB3  . GLN A 1 238 ? -10.50200 12.30000 30.06100 1.000 38.17558  ? 238 GLN A HB3  1 
ATOM   3755 H  HG2  . GLN A 1 238 ? -12.00200 13.96400 30.40600 1.000 35.43558  ? 238 GLN A HG2  1 
ATOM   3756 H  HG3  . GLN A 1 238 ? -11.91100 13.20400 31.79900 1.000 35.43558  ? 238 GLN A HG3  1 
ATOM   3757 H  HE21 . GLN A 1 238 ? -12.64200 15.05500 32.94000 1.000 34.06558  ? 238 GLN A HE21 1 
ATOM   3758 H  HE22 . GLN A 1 238 ? -11.77200 16.24000 33.18400 1.000 34.06558  ? 238 GLN A HE22 1 
ATOM   3759 N  N    . GLU A 1 239 ? -10.70000 11.56600 33.69600 1.000 31.38214  ? 239 GLU A N    1 
ATOM   3760 C  CA   . GLU A 1 239 ? -11.61600 10.68600 34.42000 1.000 30.12798  ? 239 GLU A CA   1 
ATOM   3761 C  C    . GLU A 1 239 ? -12.74600 11.56900 34.93000 1.000 30.53681  ? 239 GLU A C    1 
ATOM   3762 O  O    . GLU A 1 239 ? -12.57400 12.26300 35.93700 1.000 29.96757  ? 239 GLU A O    1 
ATOM   3763 C  CB   . GLU A 1 239 ? -10.93000 9.97400  35.58400 1.000 36.47559  ? 239 GLU A CB   1 
ATOM   3764 C  CG   . GLU A 1 239 ? -9.70400  9.17900  35.22300 1.000 58.57690  ? 239 GLU A CG   1 
ATOM   3765 C  CD   . GLU A 1 239 ? -10.04300 7.83700  34.62300 1.000 68.63651  ? 239 GLU A CD   1 
ATOM   3766 O  OE1  . GLU A 1 239 ? -11.11200 7.28900  34.97100 1.000 67.80455  ? 239 GLU A OE1  1 
ATOM   3767 O  OE2  . GLU A 1 239 ? -9.25200  7.35000  33.77900 1.000 77.50176  ? 239 GLU A OE2  1 
ATOM   3768 H  H    . GLU A 1 239 ? -10.49400 12.27900 34.13100 1.000 36.54558  ? 239 GLU A H    1 
ATOM   3769 H  HA   . GLU A 1 239 ? -11.95800 10.01000 33.81500 1.000 35.28558  ? 239 GLU A HA   1 
ATOM   3770 H  HB2  . GLU A 1 239 ? -10.66000 10.64100 36.23400 1.000 42.28558  ? 239 GLU A HB2  1 
ATOM   3771 H  HB3  . GLU A 1 239 ? -11.56500 9.35900  35.98300 1.000 42.28558  ? 239 GLU A HB3  1 
ATOM   3772 H  HG2  . GLU A 1 239 ? -9.18300  9.67600  34.57300 1.000 67.86558  ? 239 GLU A HG2  1 
ATOM   3773 H  HG3  . GLU A 1 239 ? -9.17800  9.02700  36.02300 1.000 67.86558  ? 239 GLU A HG3  1 
ATOM   3774 N  N    . SER A 1 240 ? -13.87200 11.57400 34.22800 1.000 29.69928  ? 240 SER A N    1 
ATOM   3775 C  CA   . SER A 1 240 ? -15.03500 12.35300 34.62500 1.000 26.94990  ? 240 SER A CA   1 
ATOM   3776 C  C    . SER A 1 240 ? -16.22000 11.91100 33.76900 1.000 26.81663  ? 240 SER A C    1 
ATOM   3777 O  O    . SER A 1 240 ? -16.03400 11.31900 32.70500 1.000 29.66462  ? 240 SER A O    1 
ATOM   3778 C  CB   . SER A 1 240 ? -14.78700 13.86400 34.46300 1.000 32.65456  ? 240 SER A CB   1 
ATOM   3779 O  OG   . SER A 1 240 ? -14.56400 14.19100 33.11200 1.000 28.75040  ? 240 SER A OG   1 
ATOM   3780 H  H    . SER A 1 240 ? -13.98800 11.12500 33.50400 1.000 36.13558  ? 240 SER A H    1 
ATOM   3781 H  HA   . SER A 1 240 ? -15.24500 12.17600 35.55500 1.000 33.52558  ? 240 SER A HA   1 
ATOM   3782 H  HB2  . SER A 1 240 ? -15.56600 14.34800 34.78100 1.000 40.46558  ? 240 SER A HB2  1 
ATOM   3783 H  HB3  . SER A 1 240 ? -14.00700 14.11400 34.98200 1.000 40.46558  ? 240 SER A HB3  1 
ATOM   3784 H  HG   . SER A 1 240 ? -15.24900 14.01800 32.65700 1.000 35.77558  ? 240 SER A HG   1 
ATOM   3785 N  N    . PRO A 1 241 ? -17.44200 12.17900 34.22300 1.000 26.82094  ? 241 PRO A N    1 
ATOM   3786 C  CA   . PRO A 1 241 ? -18.61600 11.78900 33.42700 1.000 27.10196  ? 241 PRO A CA   1 
ATOM   3787 C  C    . PRO A 1 241 ? -18.98100 12.78400 32.34600 1.000 26.75983  ? 241 PRO A C    1 
ATOM   3788 O  O    . PRO A 1 241 ? -19.83800 12.47600 31.50300 1.000 27.46108  ? 241 PRO A O    1 
ATOM   3789 C  CB   . PRO A 1 241 ? -19.73000 11.69400 34.47100 1.000 30.28796  ? 241 PRO A CB   1 
ATOM   3790 C  CG   . PRO A 1 241 ? -19.29900 12.58600 35.59500 1.000 31.16550  ? 241 PRO A CG   1 
ATOM   3791 C  CD   . PRO A 1 241 ? -17.79300 12.69500 35.55500 1.000 29.71639  ? 241 PRO A CD   1 
ATOM   3792 H  HA   . PRO A 1 241 ? -18.47500 10.91500 33.03000 1.000 35.15558  ? 241 PRO A HA   1 
ATOM   3793 H  HB2  . PRO A 1 241 ? -20.56700 12.00000 34.08700 1.000 39.50558  ? 241 PRO A HB2  1 
ATOM   3794 H  HB3  . PRO A 1 241 ? -19.82000 10.77600 34.77300 1.000 39.50558  ? 241 PRO A HB3  1 
ATOM   3795 H  HG2  . PRO A 1 241 ? -19.70100 13.46100 35.47900 1.000 40.43558  ? 241 PRO A HG2  1 
ATOM   3796 H  HG3  . PRO A 1 241 ? -19.58400 12.19800 36.43700 1.000 40.43558  ? 241 PRO A HG3  1 
ATOM   3797 H  HD2  . PRO A 1 241 ? -17.51300 13.61900 35.65100 1.000 38.06558  ? 241 PRO A HD2  1 
ATOM   3798 H  HD3  . PRO A 1 241 ? -17.39100 12.15300 36.25100 1.000 38.06558  ? 241 PRO A HD3  1 
ATOM   3799 N  N    . PHE A 1 242 ? -18.40700 13.97800 32.38700 1.000 26.52494  ? 242 PHE A N    1 
ATOM   3800 C  CA   . PHE A 1 242 ? -18.61700 14.98400 31.36400 1.000 25.81932  ? 242 PHE A CA   1 
ATOM   3801 C  C    . PHE A 1 242 ? -17.39600 15.89000 31.36700 1.000 24.81668  ? 242 PHE A C    1 
ATOM   3802 O  O    . PHE A 1 242 ? -16.58700 15.87900 32.29800 1.000 25.37813  ? 242 PHE A O    1 
ATOM   3803 C  CB   . PHE A 1 242 ? -19.91000 15.77900 31.61300 1.000 25.91464  ? 242 PHE A CB   1 
ATOM   3804 C  CG   . PHE A 1 242 ? -19.84500 16.63700 32.83400 1.000 20.42023  ? 242 PHE A CG   1 
ATOM   3805 C  CD1  . PHE A 1 242 ? -19.35300 17.91400 32.75800 1.000 24.81751  ? 242 PHE A CD1  1 
ATOM   3806 C  CD2  . PHE A 1 242 ? -20.26100 16.15300 34.05700 1.000 24.70042  ? 242 PHE A CD2  1 
ATOM   3807 C  CE1  . PHE A 1 242 ? -19.27800 18.69900 33.86600 1.000 25.44223  ? 242 PHE A CE1  1 
ATOM   3808 C  CE2  . PHE A 1 242 ? -20.17200 16.93000 35.17700 1.000 22.93227  ? 242 PHE A CE2  1 
ATOM   3809 C  CZ   . PHE A 1 242 ? -19.68300 18.20600 35.08700 1.000 25.88645  ? 242 PHE A CZ   1 
ATOM   3810 H  H    . PHE A 1 242 ? -17.87800 14.23500 33.01500 1.000 34.54558  ? 242 PHE A H    1 
ATOM   3811 H  HA   . PHE A 1 242 ? -18.69800 14.56700 30.49100 1.000 33.74558  ? 242 PHE A HA   1 
ATOM   3812 H  HB2  . PHE A 1 242 ? -20.07500 16.35700 30.85200 1.000 34.37558  ? 242 PHE A HB2  1 
ATOM   3813 H  HB3  . PHE A 1 242 ? -20.64500 15.15700 31.72400 1.000 34.37558  ? 242 PHE A HB3  1 
ATOM   3814 H  HD1  . PHE A 1 242 ? -19.06600 18.24700 31.93800 1.000 32.93558  ? 242 PHE A HD1  1 
ATOM   3815 H  HD2  . PHE A 1 242 ? -20.60400 15.29100 34.12000 1.000 33.09558  ? 242 PHE A HD2  1 
ATOM   3816 H  HE1  . PHE A 1 242 ? -18.95400 19.56800 33.80000 1.000 33.48558  ? 242 PHE A HE1  1 
ATOM   3817 H  HE2  . PHE A 1 242 ? -20.44400 16.59300 36.00000 1.000 30.74558  ? 242 PHE A HE2  1 
ATOM   3818 H  HZ   . PHE A 1 242 ? -19.62500 18.73800 35.84700 1.000 33.97558  ? 242 PHE A HZ   1 
ATOM   3819 N  N    . VAL A 1 243 ? -17.26200 16.68200 30.31200 1.000 24.47582  ? 243 VAL A N    1 
ATOM   3820 C  CA   . VAL A 1 243 ? -16.32600 17.80200 30.31100 1.000 23.63847  ? 243 VAL A CA   1 
ATOM   3821 C  C    . VAL A 1 243 ? -17.05500 18.98900 29.70600 1.000 24.78867  ? 243 VAL A C    1 
ATOM   3822 O  O    . VAL A 1 243 ? -17.96000 18.82400 28.88300 1.000 26.37765  ? 243 VAL A O    1 
ATOM   3823 C  CB   . VAL A 1 243 ? -15.03100 17.52100 29.52300 1.000 26.87970  ? 243 VAL A CB   1 
ATOM   3824 C  CG1  . VAL A 1 243 ? -14.24800 16.40100 30.15600 1.000 28.90795  ? 243 VAL A CG1  1 
ATOM   3825 C  CG2  . VAL A 1 243 ? -15.34000 17.18000 28.07600 1.000 30.01004  ? 243 VAL A CG2  1 
ATOM   3826 H  H    . VAL A 1 243 ? -17.70300 16.59100 29.57900 1.000 31.73558  ? 243 VAL A H    1 
ATOM   3827 H  HA   . VAL A 1 243 ? -16.06500 17.99400 31.22600 1.000 30.55558  ? 243 VAL A HA   1 
ATOM   3828 H  HB   . VAL A 1 243 ? -14.48800 18.32400 29.54200 1.000 33.90558  ? 243 VAL A HB   1 
ATOM   3829 H  HG11 . VAL A 1 243 ? -13.43200 16.26000 29.65000 1.000 35.99558  ? 243 VAL A HG11 1 
ATOM   3830 H  HG12 . VAL A 1 243 ? -14.03200 16.64300 31.07000 1.000 35.99558  ? 243 VAL A HG12 1 
ATOM   3831 H  HG13 . VAL A 1 243 ? -14.78700 15.59400 30.14600 1.000 35.99558  ? 243 VAL A HG13 1 
ATOM   3832 H  HG21 . VAL A 1 243 ? -14.52000 16.90800 27.63300 1.000 37.38558  ? 243 VAL A HG21 1 
ATOM   3833 H  HG22 . VAL A 1 243 ? -15.98400 16.45600 28.05200 1.000 37.38558  ? 243 VAL A HG22 1 
ATOM   3834 H  HG23 . VAL A 1 243 ? -15.70700 17.96500 27.63800 1.000 37.38558  ? 243 VAL A HG23 1 
ATOM   3835 N  N    . MET A 1 244 ? -16.65100 20.18400 30.11400 1.000 23.18577  ? 244 MET A N    1 
ATOM   3836 C  CA   . MET A 1 244 ? -17.20900 21.43100 29.60300 1.000 22.64935  ? 244 MET A CA   1 
ATOM   3837 C  C    . MET A 1 244 ? -16.08100 22.25600 28.99800 1.000 24.08378  ? 244 MET A C    1 
ATOM   3838 O  O    . MET A 1 244 ? -15.11600 22.59200 29.69200 1.000 25.81438  ? 244 MET A O    1 
ATOM   3839 C  CB   . MET A 1 244 ? -17.92300 22.19300 30.72300 1.000 25.91074  ? 244 MET A CB   1 
ATOM   3840 C  CG   . MET A 1 244 ? -18.32700 23.61800 30.37200 1.000 24.87664  ? 244 MET A CG   1 
ATOM   3841 S  SD   . MET A 1 244 ? -18.85500 24.51500 31.84700 1.000 27.68903  ? 244 MET A SD   1 
ATOM   3842 C  CE   . MET A 1 244 ? -19.63200 25.93300 31.13700 1.000 30.00624  ? 244 MET A CE   1 
ATOM   3843 H  H    . MET A 1 244 ? -16.03700 20.30400 30.70400 1.000 30.19558  ? 244 MET A H    1 
ATOM   3844 H  HA   . MET A 1 244 ? -17.85900 21.24500 28.90700 1.000 29.65558  ? 244 MET A HA   1 
ATOM   3845 H  HB2  . MET A 1 244 ? -18.73100 21.71000 30.95700 1.000 33.64558  ? 244 MET A HB2  1 
ATOM   3846 H  HB3  . MET A 1 244 ? -17.33000 22.23800 31.49000 1.000 33.64558  ? 244 MET A HB3  1 
ATOM   3847 H  HG2  . MET A 1 244 ? -17.57000 24.08300 29.98300 1.000 32.32558  ? 244 MET A HG2  1 
ATOM   3848 H  HG3  . MET A 1 244 ? -19.06400 23.60000 29.74200 1.000 32.32558  ? 244 MET A HG3  1 
ATOM   3849 H  HE1  . MET A 1 244 ? -19.95800 26.50400 31.85000 1.000 38.04558  ? 244 MET A HE1  1 
ATOM   3850 H  HE2  . MET A 1 244 ? -18.98200 26.41300 30.60000 1.000 38.04558  ? 244 MET A HE2  1 
ATOM   3851 H  HE3  . MET A 1 244 ? -20.37200 25.64300 30.58100 1.000 38.04558  ? 244 MET A HE3  1 
ATOM   3852 N  N    . MET A 1 245 ? -16.20600 22.56800 27.71200 1.000 24.23323  ? 245 MET A N    1 
ATOM   3853 C  CA   . MET A 1 245 ? -15.22800 23.34400 26.95900 1.000 24.48776  ? 245 MET A CA   1 
ATOM   3854 C  C    . MET A 1 245 ? -15.81900 24.71000 26.65400 1.000 25.90837  ? 245 MET A C    1 
ATOM   3855 O  O    . MET A 1 245 ? -16.93400 24.80400 26.13900 1.000 28.19155  ? 245 MET A O    1 
ATOM   3856 C  CB   . MET A 1 245 ? -14.83200 22.62200 25.66800 1.000 29.03876  ? 245 MET A CB   1 
ATOM   3857 C  CG   . MET A 1 245 ? -14.49700 21.16200 25.90800 1.000 29.60458  ? 245 MET A CG   1 
ATOM   3858 S  SD   . MET A 1 245 ? -12.86600 20.91400 26.66900 1.000 29.25513  ? 245 MET A SD   1 
ATOM   3859 C  CE   . MET A 1 245 ? -11.82000 22.00900 25.72100 1.000 26.92017  ? 245 MET A CE   1 
ATOM   3860 H  H    . MET A 1 245 ? -16.88000 22.33000 27.23300 1.000 31.19558  ? 245 MET A H    1 
ATOM   3861 H  HA   . MET A 1 245 ? -14.42100 23.45800 27.48700 1.000 31.23558  ? 245 MET A HA   1 
ATOM   3862 H  HB2  . MET A 1 245 ? -15.57000 22.66400 25.04100 1.000 36.32558  ? 245 MET A HB2  1 
ATOM   3863 H  HB3  . MET A 1 245 ? -14.05000 23.05400 25.29000 1.000 36.32558  ? 245 MET A HB3  1 
ATOM   3864 H  HG2  . MET A 1 245 ? -15.16300 20.78100 26.50100 1.000 36.81558  ? 245 MET A HG2  1 
ATOM   3865 H  HG3  . MET A 1 245 ? -14.50300 20.69500 25.05800 1.000 36.81558  ? 245 MET A HG3  1 
ATOM   3866 H  HE1  . MET A 1 245 ? -10.89300 21.75900 25.85900 1.000 33.10558  ? 245 MET A HE1  1 
ATOM   3867 H  HE2  . MET A 1 245 ? -12.04800 21.92800 24.78100 1.000 33.10558  ? 245 MET A HE2  1 
ATOM   3868 H  HE3  . MET A 1 245 ? -11.96500 22.92100 26.01800 1.000 33.10558  ? 245 MET A HE3  1 
ATOM   3869 N  N    . SER A 1 246 ? -15.08500 25.77100 26.97900 1.000 24.20230  ? 246 SER A N    1 
ATOM   3870 C  CA   . SER A 1 246 ? -15.61900 27.11900 26.82700 1.000 26.34916  ? 246 SER A CA   1 
ATOM   3871 C  C    . SER A 1 246 ? -14.63500 28.00700 26.08600 1.000 27.16142  ? 246 SER A C    1 
ATOM   3872 O  O    . SER A 1 246 ? -13.43100 27.76600 26.08600 1.000 27.77335  ? 246 SER A O    1 
ATOM   3873 C  CB   . SER A 1 246 ? -15.94500 27.75100 28.19400 1.000 30.78135  ? 246 SER A CB   1 
ATOM   3874 O  OG   . SER A 1 246 ? -16.83100 26.91400 28.91900 1.000 28.72357  ? 246 SER A OG   1 
ATOM   3875 H  H    . SER A 1 246 ? -14.28300 25.73400 27.28800 1.000 30.84558  ? 246 SER A H    1 
ATOM   3876 H  HA   . SER A 1 246 ? -16.42900 27.06900 26.29700 1.000 33.37558  ? 246 SER A HA   1 
ATOM   3877 H  HB2  . SER A 1 246 ? -15.12400 27.86000 28.70000 1.000 38.58558  ? 246 SER A HB2  1 
ATOM   3878 H  HB3  . SER A 1 246 ? -16.36500 28.61400 28.05400 1.000 38.58558  ? 246 SER A HB3  1 
ATOM   3879 H  HG   . SER A 1 246 ? -16.94300 27.21800 29.69400 1.000 36.29558  ? 246 SER A HG   1 
ATOM   3880 N  N    . ALA A 1 247 ? -15.17300 29.05100 25.45100 1.000 27.54144  ? 247 ALA A N    1 
ATOM   3881 C  CA   . ALA A 1 247 ? -14.34900 30.02800 24.75200 1.000 28.28070  ? 247 ALA A CA   1 
ATOM   3882 C  C    . ALA A 1 247 ? -15.16500 31.29100 24.56200 1.000 28.97352  ? 247 ALA A C    1 
ATOM   3883 O  O    . ALA A 1 247 ? -16.39700 31.24700 24.61300 1.000 32.12635  ? 247 ALA A O    1 
ATOM   3884 C  CB   . ALA A 1 247 ? -13.87300 29.48600 23.39800 1.000 31.37143  ? 247 ALA A CB   1 
ATOM   3885 H  H    . ALA A 1 247 ? -16.01600 29.21200 25.41400 1.000 34.51558  ? 247 ALA A H    1 
ATOM   3886 H  HA   . ALA A 1 247 ? -13.57000 30.24200 25.28900 1.000 35.21558  ? 247 ALA A HA   1 
ATOM   3887 H  HB1  . ALA A 1 247 ? -13.32600 30.15900 22.96300 1.000 38.79558  ? 247 ALA A HB1  1 
ATOM   3888 H  HB2  . ALA A 1 247 ? -13.35200 28.68100 23.54500 1.000 38.79558  ? 247 ALA A HB2  1 
ATOM   3889 H  HB3  . ALA A 1 247 ? -14.64700 29.28400 22.84900 1.000 38.79558  ? 247 ALA A HB3  1 
ATOM   3890 N  N    . PRO A 1 248 ? -14.51900 32.43200 24.32700 1.000 28.40227  ? 248 PRO A N    1 
ATOM   3891 C  CA   . PRO A 1 248 ? -15.28800 33.62200 23.95300 1.000 29.92233  ? 248 PRO A CA   1 
ATOM   3892 C  C    . PRO A 1 248 ? -16.15000 33.32700 22.75100 1.000 34.02765  ? 248 PRO A C    1 
ATOM   3893 O  O    . PRO A 1 248 ? -15.76100 32.53900 21.86300 1.000 31.40558  ? 248 PRO A O    1 
ATOM   3894 C  CB   . PRO A 1 248 ? -14.20000 34.65900 23.63100 1.000 32.40245  ? 248 PRO A CB   1 
ATOM   3895 C  CG   . PRO A 1 248 ? -13.00500 34.18800 24.39300 1.000 36.15904  ? 248 PRO A CG   1 
ATOM   3896 C  CD   . PRO A 1 248 ? -13.07200 32.69100 24.32800 1.000 33.21573  ? 248 PRO A CD   1 
ATOM   3897 H  HA   . PRO A 1 248 ? -15.83500 33.93700 24.69000 1.000 36.54558  ? 248 PRO A HA   1 
ATOM   3898 H  HB2  . PRO A 1 248 ? -14.02400 34.67100 22.67800 1.000 39.34558  ? 248 PRO A HB2  1 
ATOM   3899 H  HB3  . PRO A 1 248 ? -14.48000 35.53800 23.92900 1.000 39.34558  ? 248 PRO A HB3  1 
ATOM   3900 H  HG2  . PRO A 1 248 ? -12.19500 34.51900 23.97500 1.000 43.96558  ? 248 PRO A HG2  1 
ATOM   3901 H  HG3  . PRO A 1 248 ? -13.05500 34.49800 25.31100 1.000 43.96558  ? 248 PRO A HG3  1 
ATOM   3902 H  HD2  . PRO A 1 248 ? -12.65900 32.36000 23.51500 1.000 40.72558  ? 248 PRO A HD2  1 
ATOM   3903 H  HD3  . PRO A 1 248 ? -12.64700 32.29100 25.10300 1.000 40.72558  ? 248 PRO A HD3  1 
ATOM   3904 N  N    . PRO A 1 249 ? -17.33700 33.94200 22.66000 1.000 28.90925  ? 249 PRO A N    1 
ATOM   3905 C  CA   . PRO A 1 249 ? -18.28200 33.57500 21.59400 1.000 29.16752  ? 249 PRO A CA   1 
ATOM   3906 C  C    . PRO A 1 249 ? -17.66300 33.76500 20.22200 1.000 34.03184  ? 249 PRO A C    1 
ATOM   3907 O  O    . PRO A 1 249 ? -17.08600 34.81100 19.92700 1.000 36.59120  ? 249 PRO A O    1 
ATOM   3908 C  CB   . PRO A 1 249 ? -19.46400 34.52600 21.79600 1.000 32.82158  ? 249 PRO A CB   1 
ATOM   3909 C  CG   . PRO A 1 249 ? -19.23300 35.25700 23.03700 1.000 37.91246  ? 249 PRO A CG   1 
ATOM   3910 C  CD   . PRO A 1 249 ? -17.89700 34.92700 23.60300 1.000 30.57253  ? 249 PRO A CD   1 
ATOM   3911 H  HA   . PRO A 1 249 ? -18.57500 32.65800 21.71100 1.000 35.19558  ? 249 PRO A HA   1 
ATOM   3912 H  HB2  . PRO A 1 249 ? -19.51300 35.14000 21.04600 1.000 39.25558  ? 249 PRO A HB2  1 
ATOM   3913 H  HB3  . PRO A 1 249 ? -20.28400 34.01000 21.85500 1.000 39.25558  ? 249 PRO A HB3  1 
ATOM   3914 H  HG2  . PRO A 1 249 ? -19.28000 36.20700 22.84700 1.000 45.31558  ? 249 PRO A HG2  1 
ATOM   3915 H  HG3  . PRO A 1 249 ? -19.92400 35.01000 23.67100 1.000 45.31558  ? 249 PRO A HG3  1 
ATOM   3916 H  HD2  . PRO A 1 249 ? -17.33800 35.71800 23.64200 1.000 36.78558  ? 249 PRO A HD2  1 
ATOM   3917 H  HD3  . PRO A 1 249 ? -17.98700 34.54000 24.48800 1.000 36.78558  ? 249 PRO A HD3  1 
ATOM   3918 N  N    . ALA A 1 250 ? -17.80000 32.74600 19.38400 1.000 34.38152  ? 250 ALA A N    1 
ATOM   3919 C  CA   . ALA A 1 250 ? -17.31000 32.81800 18.01400 1.000 37.69491  ? 250 ALA A CA   1 
ATOM   3920 C  C    . ALA A 1 250 ? -18.15000 31.88600 17.15800 1.000 36.89985  ? 250 ALA A C    1 
ATOM   3921 O  O    . ALA A 1 250 ? -18.64400 30.86400 17.63600 1.000 34.58904  ? 250 ALA A O    1 
ATOM   3922 C  CB   . ALA A 1 250 ? -15.83200 32.44100 17.92400 1.000 37.79351  ? 250 ALA A CB   1 
ATOM   3923 H  H    . ALA A 1 250 ? -18.17500 31.99900 19.58500 1.000 40.97558  ? 250 ALA A H    1 
ATOM   3924 H  HA   . ALA A 1 250 ? -17.40700 33.72200 17.67500 1.000 44.40558  ? 250 ALA A HA   1 
ATOM   3925 H  HB1  . ALA A 1 250 ? -15.54900 32.49400 16.99700 1.000 44.64558  ? 250 ALA A HB1  1 
ATOM   3926 H  HB2  . ALA A 1 250 ? -15.31500 33.05800 18.46400 1.000 44.64558  ? 250 ALA A HB2  1 
ATOM   3927 H  HB3  . ALA A 1 250 ? -15.71700 31.53500 18.25300 1.000 44.64558  ? 250 ALA A HB3  1 
ATOM   3928 N  N    . GLN A 1 251 ? -18.30400 32.24000 15.88500 1.000 37.19547  ? 251 GLN A N    1 
ATOM   3929 C  CA   . GLN A 1 251 ? -19.01900 31.36600 14.96700 1.000 35.94720  ? 251 GLN A CA   1 
ATOM   3930 C  C    . GLN A 1 251 ? -18.40200 29.97500 14.99600 1.000 34.83364  ? 251 GLN A C    1 
ATOM   3931 O  O    . GLN A 1 251 ? -17.18900 29.81500 14.84300 1.000 37.52192  ? 251 GLN A O    1 
ATOM   3932 C  CB   . GLN A 1 251 ? -18.96800 31.94500 13.55100 1.000 43.57305  ? 251 GLN A CB   1 
ATOM   3933 C  CG   . GLN A 1 251 ? -19.87300 33.14000 13.34100 1.000 49.31761  ? 251 GLN A CG   1 
ATOM   3934 C  CD   . GLN A 1 251 ? -21.32600 32.87000 13.69900 1.000 49.36597  ? 251 GLN A CD   1 
ATOM   3935 O  OE1  . GLN A 1 251 ? -21.91400 31.88300 13.26000 1.000 53.99020  ? 251 GLN A OE1  1 
ATOM   3936 N  NE2  . GLN A 1 251 ? -21.90300 33.74400 14.51800 1.000 57.49811  ? 251 GLN A NE2  1 
ATOM   3937 H  H    . GLN A 1 251 ? -18.00800 32.96900 15.53600 1.000 42.44558  ? 251 GLN A H    1 
ATOM   3938 H  HA   . GLN A 1 251 ? -19.95100 31.30100 15.22800 1.000 40.11558  ? 251 GLN A HA   1 
ATOM   3939 H  HB2  . GLN A 1 251 ? -18.05900 32.22700 13.36300 1.000 48.18558  ? 251 GLN A HB2  1 
ATOM   3940 H  HB3  . GLN A 1 251 ? -19.23900 31.25600 12.92300 1.000 48.18558  ? 251 GLN A HB3  1 
ATOM   3941 H  HG2  . GLN A 1 251 ? -19.56100 33.87000 13.89800 1.000 54.86558  ? 251 GLN A HG2  1 
ATOM   3942 H  HG3  . GLN A 1 251 ? -19.84000 33.39700 12.40600 1.000 54.86558  ? 251 GLN A HG3  1 
ATOM   3943 H  HE21 . GLN A 1 251 ? -21.45500 34.41600 14.81400 1.000 65.17558  ? 251 GLN A HE21 1 
ATOM   3944 H  HE22 . GLN A 1 251 ? -22.72300 33.63800 14.75100 1.000 65.17558  ? 251 GLN A HE22 1 
ATOM   3945 N  N    . TYR A 1 252 ? -19.24400 28.96500 15.17200 1.000 35.42871  ? 252 TYR A N    1 
ATOM   3946 C  CA   . TYR A 1 252 ? -18.78300 27.60300 15.39200 1.000 33.79192  ? 252 TYR A CA   1 
ATOM   3947 C  C    . TYR A 1 252 ? -19.84400 26.62700 14.91900 1.000 37.16016  ? 252 TYR A C    1 
ATOM   3948 O  O    . TYR A 1 252 ? -21.04000 26.84300 15.13800 1.000 36.18284  ? 252 TYR A O    1 
ATOM   3949 C  CB   . TYR A 1 252 ? -18.49500 27.37500 16.87700 1.000 32.40410  ? 252 TYR A CB   1 
ATOM   3950 C  CG   . TYR A 1 252 ? -17.88100 26.05200 17.22900 1.000 30.82887  ? 252 TYR A CG   1 
ATOM   3951 C  CD1  . TYR A 1 252 ? -16.51100 25.84200 17.09200 1.000 37.61438  ? 252 TYR A CD1  1 
ATOM   3952 C  CD2  . TYR A 1 252 ? -18.65100 25.02000 17.73100 1.000 33.25995  ? 252 TYR A CD2  1 
ATOM   3953 C  CE1  . TYR A 1 252 ? -15.93500 24.63700 17.43800 1.000 40.51692  ? 252 TYR A CE1  1 
ATOM   3954 C  CE2  . TYR A 1 252 ? -18.08300 23.81200 18.09800 1.000 34.26076  ? 252 TYR A CE2  1 
ATOM   3955 C  CZ   . TYR A 1 252 ? -16.72300 23.62500 17.94400 1.000 41.83145  ? 252 TYR A CZ   1 
ATOM   3956 O  OH   . TYR A 1 252 ? -16.15100 22.43000 18.29900 1.000 42.11577  ? 252 TYR A OH   1 
ATOM   3957 H  H    . TYR A 1 252 ? -20.10000 29.04400 15.16900 1.000 39.29558  ? 252 TYR A H    1 
ATOM   3958 H  HA   . TYR A 1 252 ? -17.97700 27.43900 14.87700 1.000 37.29558  ? 252 TYR A HA   1 
ATOM   3959 H  HB2  . TYR A 1 252 ? -17.88200 28.06500 17.17700 1.000 36.81558  ? 252 TYR A HB2  1 
ATOM   3960 H  HB3  . TYR A 1 252 ? -19.33200 27.44100 17.36300 1.000 36.81558  ? 252 TYR A HB3  1 
ATOM   3961 H  HD1  . TYR A 1 252 ? -15.97500 26.52600 16.76100 1.000 42.93558  ? 252 TYR A HD1  1 
ATOM   3962 H  HD2  . TYR A 1 252 ? -19.56800 25.13900 17.82400 1.000 38.00558  ? 252 TYR A HD2  1 
ATOM   3963 H  HE1  . TYR A 1 252 ? -15.02000 24.50800 17.33000 1.000 46.33558  ? 252 TYR A HE1  1 
ATOM   3964 H  HE2  . TYR A 1 252 ? -18.61300 23.13200 18.44600 1.000 39.18558  ? 252 TYR A HE2  1 
ATOM   3965 H  HH   . TYR A 1 252 ? -16.74000 21.90200 18.58200 1.000 48.22558  ? 252 TYR A HH   1 
ATOM   3966 N  N    . GLU A 1 253 ? -19.40500 25.55000 14.27200 1.000 36.78847  ? 253 GLU A N    1 
ATOM   3967 C  CA   . GLU A 1 253 ? -20.32600 24.55700 13.73600 1.000 37.25307  ? 253 GLU A CA   1 
ATOM   3968 C  C    . GLU A 1 253 ? -20.46800 23.41700 14.73600 1.000 44.02562  ? 253 GLU A C    1 
ATOM   3969 O  O    . GLU A 1 253 ? -19.46900 22.80500 15.12900 1.000 42.00453  ? 253 GLU A O    1 
ATOM   3970 C  CB   . GLU A 1 253 ? -19.84600 24.02400 12.38700 1.000 48.53513  ? 253 GLU A CB   1 
ATOM   3971 C  CG   . GLU A 1 253 ? -20.64300 22.81600 11.92800 1.000 50.77371  ? 253 GLU A CG   1 
ATOM   3972 C  CD   . GLU A 1 253 ? -20.69500 22.68200 10.41900 1.000 76.82138  ? 253 GLU A CD   1 
ATOM   3973 O  OE1  . GLU A 1 253 ? -19.76700 23.18400 9.74900  1.000 69.01981  ? 253 GLU A OE1  1 
ATOM   3974 O  OE2  . GLU A 1 253 ? -21.66600 22.07300 9.91200  1.000 77.54195  ? 253 GLU A OE2  1 
ATOM   3975 H  H    . GLU A 1 253 ? -18.57500 25.37400 14.13100 1.000 39.21558  ? 253 GLU A H    1 
ATOM   3976 H  HA   . GLU A 1 253 ? -21.19500 24.97000 13.60800 1.000 38.80558  ? 253 GLU A HA   1 
ATOM   3977 H  HB2  . GLU A 1 253 ? -19.94100 24.72000 11.71800 1.000 50.56558  ? 253 GLU A HB2  1 
ATOM   3978 H  HB3  . GLU A 1 253 ? -18.91600 23.76100 12.46200 1.000 50.56558  ? 253 GLU A HB3  1 
ATOM   3979 H  HG2  . GLU A 1 253 ? -20.23400 22.01300 12.28600 1.000 52.07558  ? 253 GLU A HG2  1 
ATOM   3980 H  HG3  . GLU A 1 253 ? -21.55400 22.89700 12.25300 1.000 52.07558  ? 253 GLU A HG3  1 
ATOM   3981 N  N    . LEU A 1 254 ? -21.70500 23.14700 15.15400 1.000 38.37489  ? 254 LEU A N    1 
ATOM   3982 C  CA   . LEU A 1 254 ? -22.02500 22.01600 16.02000 1.000 40.18871  ? 254 LEU A CA   1 
ATOM   3983 C  C    . LEU A 1 254 ? -22.49300 20.84700 15.15900 1.000 41.60328  ? 254 LEU A C    1 
ATOM   3984 O  O    . LEU A 1 254 ? -23.49900 20.96000 14.45000 1.000 43.27725  ? 254 LEU A O    1 
ATOM   3985 C  CB   . LEU A 1 254 ? -23.11400 22.39000 17.02800 1.000 37.49282  ? 254 LEU A CB   1 
ATOM   3986 C  CG   . LEU A 1 254 ? -22.70000 23.36900 18.13300 1.000 36.14748  ? 254 LEU A CG   1 
ATOM   3987 C  CD1  . LEU A 1 254 ? -23.92900 23.84300 18.91800 1.000 29.95498  ? 254 LEU A CD1  1 
ATOM   3988 C  CD2  . LEU A 1 254 ? -21.67600 22.77200 19.08000 1.000 35.78720  ? 254 LEU A CD2  1 
ATOM   3989 H  H    . LEU A 1 254 ? -22.39200 23.61900 14.94300 1.000 41.13558  ? 254 LEU A H    1 
ATOM   3990 H  HA   . LEU A 1 254 ? -21.22800 21.75200 16.50500 1.000 43.84558  ? 254 LEU A HA   1 
ATOM   3991 H  HB2  . LEU A 1 254 ? -23.84800 22.79700 16.54300 1.000 41.74558  ? 254 LEU A HB2  1 
ATOM   3992 H  HB3  . LEU A 1 254 ? -23.41400 21.57700 17.46300 1.000 41.74558  ? 254 LEU A HB3  1 
ATOM   3993 H  HG   . LEU A 1 254 ? -22.28200 24.13300 17.70600 1.000 41.39558  ? 254 LEU A HG   1 
ATOM   3994 H  HD11 . LEU A 1 254 ? -23.64400 24.46800 19.60300 1.000 34.67558  ? 254 LEU A HD11 1 
ATOM   3995 H  HD12 . LEU A 1 254 ? -24.54400 24.28000 18.30800 1.000 34.67558  ? 254 LEU A HD12 1 
ATOM   3996 H  HD13 . LEU A 1 254 ? -24.35800 23.07600 19.32700 1.000 34.67558  ? 254 LEU A HD13 1 
ATOM   3997 H  HD21 . LEU A 1 254 ? -21.50100 23.40400 19.79500 1.000 41.63558  ? 254 LEU A HD21 1 
ATOM   3998 H  HD22 . LEU A 1 254 ? -22.03000 21.94700 19.44800 1.000 41.63558  ? 254 LEU A HD22 1 
ATOM   3999 H  HD23 . LEU A 1 254 ? -20.85900 22.59200 18.58900 1.000 41.63558  ? 254 LEU A HD23 1 
ATOM   4000 N  N    . LYS A 1 255 ? -21.78000 19.72800 15.23700 1.000 41.90188  ? 255 LYS A N    1 
ATOM   4001 C  CA   . LYS A 1 255 ? -22.08600 18.55600 14.42700 1.000 47.69991  ? 255 LYS A CA   1 
ATOM   4002 C  C    . LYS A 1 255 ? -22.88600 17.55100 15.24300 1.000 43.66478  ? 255 LYS A C    1 
ATOM   4003 O  O    . LYS A 1 255 ? -22.47700 17.15300 16.34100 1.000 39.25806  ? 255 LYS A O    1 
ATOM   4004 C  CB   . LYS A 1 255 ? -20.81000 17.89900 13.89800 1.000 52.50834  ? 255 LYS A CB   1 
ATOM   4005 C  CG   . LYS A 1 255 ? -20.00500 18.75400 12.92400 1.000 72.00435  ? 255 LYS A CG   1 
ATOM   4006 C  CD   . LYS A 1 255 ? -20.82900 19.17200 11.69900 1.000 91.24771  ? 255 LYS A CD   1 
ATOM   4007 C  CE   . LYS A 1 255 ? -20.74600 18.15400 10.57000 1.000 95.85736  ? 255 LYS A CE   1 
ATOM   4008 N  NZ   . LYS A 1 255 ? -21.05600 18.77600 9.25000  1.000 99.81607  ? 255 LYS A NZ   1 
ATOM   4009 H  H    . LYS A 1 255 ? -21.10500 19.62200 15.75900 1.000 44.11558  ? 255 LYS A H    1 
ATOM   4010 H  HA   . LYS A 1 255 ? -22.62600 18.83200 13.66900 1.000 49.49558  ? 255 LYS A HA   1 
ATOM   4011 H  HB2  . LYS A 1 255 ? -20.23400 17.69500 14.65200 1.000 54.14558  ? 255 LYS A HB2  1 
ATOM   4012 H  HB3  . LYS A 1 255 ? -21.05300 17.08200 13.43600 1.000 54.14558  ? 255 LYS A HB3  1 
ATOM   4013 H  HG2  . LYS A 1 255 ? -19.70800 19.55900 13.37800 1.000 76.67558  ? 255 LYS A HG2  1 
ATOM   4014 H  HG3  . LYS A 1 255 ? -19.23900 18.24700 12.61400 1.000 76.67558  ? 255 LYS A HG3  1 
ATOM   4015 H  HD2  . LYS A 1 255 ? -21.76000 19.26100 11.95700 1.000 98.31558  ? 255 LYS A HD2  1 
ATOM   4016 H  HD3  . LYS A 1 255 ? -20.49500 20.02000 11.36500 1.000 98.31558  ? 255 LYS A HD3  1 
ATOM   4017 H  HE2  . LYS A 1 255 ? -19.84800 17.78900 10.53100 1.000 101.45558 ? 255 LYS A HE2  1 
ATOM   4018 H  HE3  . LYS A 1 255 ? -21.38600 17.44300 10.73000 1.000 101.45558 ? 255 LYS A HE3  1 
ATOM   4019 H  HZ1  . LYS A 1 255 ? -21.00400 18.16400 8.60500  1.000 104.51558 ? 255 LYS A HZ1  1 
ATOM   4020 H  HZ2  . LYS A 1 255 ? -21.87900 19.11500 9.25900  1.000 104.51558 ? 255 LYS A HZ2  1 
ATOM   4021 H  HZ3  . LYS A 1 255 ? -20.47600 19.42800 9.07700  1.000 104.51558 ? 255 LYS A HZ3  1 
ATOM   4022 N  N    . HIS A 1 256 ? -24.01600 17.14100 14.69100 1.000 44.78036  ? 256 HIS A N    1 
ATOM   4023 C  CA   . HIS A 1 256 ? -24.89500 16.19100 15.35500 1.000 41.94393  ? 256 HIS A CA   1 
ATOM   4024 C  C    . HIS A 1 256 ? -24.14200 14.93200 15.76600 1.000 44.16536  ? 256 HIS A C    1 
ATOM   4025 O  O    . HIS A 1 256 ? -23.40400 14.34800 14.97100 1.000 44.21254  ? 256 HIS A O    1 
ATOM   4026 C  CB   . HIS A 1 256 ? -26.04500 15.84600 14.40600 1.000 45.69897  ? 256 HIS A CB   1 
ATOM   4027 C  CG   . HIS A 1 256 ? -26.92300 14.74600 14.89600 1.000 49.48899  ? 256 HIS A CG   1 
ATOM   4028 N  ND1  . HIS A 1 256 ? -27.02800 13.53600 14.24600 1.000 54.03309  ? 256 HIS A ND1  1 
ATOM   4029 C  CD2  . HIS A 1 256 ? -27.74000 14.67000 15.97100 1.000 48.57800  ? 256 HIS A CD2  1 
ATOM   4030 C  CE1  . HIS A 1 256 ? -27.87800 12.76400 14.89700 1.000 61.23743  ? 256 HIS A CE1  1 
ATOM   4031 N  NE2  . HIS A 1 256 ? -28.32300 13.42700 15.94800 1.000 52.12127  ? 256 HIS A NE2  1 
ATOM   4032 H  H    . HIS A 1 256 ? -24.30200 17.40100 13.92300 1.000 45.66558  ? 256 HIS A H    1 
ATOM   4033 H  HA   . HIS A 1 256 ? -25.25600 16.58500 16.16500 1.000 42.71558  ? 256 HIS A HA   1 
ATOM   4034 H  HB2  . HIS A 1 256 ? -26.59700 16.63400 14.28600 1.000 45.75558  ? 256 HIS A HB2  1 
ATOM   4035 H  HB3  . HIS A 1 256 ? -25.67300 15.56900 13.55400 1.000 45.75558  ? 256 HIS A HB3  1 
ATOM   4036 H  HD2  . HIS A 1 256 ? -27.88100 15.33500 16.60600 1.000 50.88558  ? 256 HIS A HD2  1 
ATOM   4037 H  HE1  . HIS A 1 256 ? -28.12300 11.90000 14.65500 1.000 63.46558  ? 256 HIS A HE1  1 
ATOM   4038 H  HE2  . HIS A 1 256 ? -28.88600 13.12800 16.52600 1.000 54.49558  ? 256 HIS A HE2  1 
ATOM   4039 N  N    . GLY A 1 257 ? -24.32800 14.52600 17.02100 1.000 41.39528  ? 257 GLY A N    1 
ATOM   4040 C  CA   . GLY A 1 257 ? -23.76300 13.29600 17.53200 1.000 45.46856  ? 257 GLY A CA   1 
ATOM   4041 C  C    . GLY A 1 257 ? -22.35500 13.39800 18.07700 1.000 43.04740  ? 257 GLY A C    1 
ATOM   4042 O  O    . GLY A 1 257 ? -21.80300 12.37700 18.50200 1.000 43.85789  ? 257 GLY A O    1 
ATOM   4043 H  H    . GLY A 1 257 ? -24.78900 14.96000 17.60300 1.000 43.31558  ? 257 GLY A H    1 
ATOM   4044 H  HA2  . GLY A 1 257 ? -24.33100 12.97100 18.24800 1.000 48.10558  ? 257 GLY A HA2  1 
ATOM   4045 H  HA3  . GLY A 1 257 ? -23.75300 12.64200 16.81600 1.000 48.10558  ? 257 GLY A HA3  1 
ATOM   4046 N  N    . THR A 1 258 ? -21.75200 14.58600 18.07100 1.000 35.28883  ? 258 THR A N    1 
ATOM   4047 C  CA   . THR A 1 258 ? -20.37000 14.75200 18.48700 1.000 34.91443  ? 258 THR A CA   1 
ATOM   4048 C  C    . THR A 1 258 ? -20.25800 15.48100 19.81700 1.000 36.32414  ? 258 THR A C    1 
ATOM   4049 O  O    . THR A 1 258 ? -19.14300 15.71200 20.29200 1.000 32.69066  ? 258 THR A O    1 
ATOM   4050 C  CB   . THR A 1 258 ? -19.57400 15.51200 17.42500 1.000 40.09052  ? 258 THR A CB   1 
ATOM   4051 O  OG1  . THR A 1 258 ? -20.03400 16.86500 17.34500 1.000 43.55123  ? 258 THR A OG1  1 
ATOM   4052 C  CG2  . THR A 1 258 ? -19.70100 14.84000 16.05000 1.000 44.82142  ? 258 THR A CG2  1 
ATOM   4053 H  H    . THR A 1 258 ? -22.13200 15.31700 17.82600 1.000 36.96558  ? 258 THR A H    1 
ATOM   4054 H  HA   . THR A 1 258 ? -19.96700 13.87400 18.57800 1.000 36.86558  ? 258 THR A HA   1 
ATOM   4055 H  HB   . THR A 1 258 ? -18.63500 15.50800 17.67100 1.000 42.15558  ? 258 THR A HB   1 
ATOM   4056 H  HG1  . THR A 1 258 ? -20.84700 16.88000 17.13300 1.000 47.00558  ? 258 THR A HG1  1 
ATOM   4057 H  HG21 . THR A 1 258 ? -19.10700 15.27000 15.41500 1.000 45.77558  ? 258 THR A HG21 1 
ATOM   4058 H  HG22 . THR A 1 258 ? -19.46500 13.90200 16.11700 1.000 45.77558  ? 258 THR A HG22 1 
ATOM   4059 H  HG23 . THR A 1 258 ? -20.61300 14.91300 15.72900 1.000 45.77558  ? 258 THR A HG23 1 
ATOM   4060 N  N    . PHE A 1 259 ? -21.38200 15.85300 20.41400 1.000 31.42306  ? 259 PHE A N    1 
ATOM   4061 C  CA   . PHE A 1 259 ? -21.40900 16.60500 21.66500 1.000 29.96289  ? 259 PHE A CA   1 
ATOM   4062 C  C    . PHE A 1 259 ? -22.74300 16.32800 22.34400 1.000 30.85488  ? 259 PHE A C    1 
ATOM   4063 O  O    . PHE A 1 259 ? -23.67000 15.79700 21.73400 1.000 31.36592  ? 259 PHE A O    1 
ATOM   4064 C  CB   . PHE A 1 259 ? -21.21000 18.11100 21.41300 1.000 29.71758  ? 259 PHE A CB   1 
ATOM   4065 C  CG   . PHE A 1 259 ? -22.39400 18.77200 20.76500 1.000 29.13888  ? 259 PHE A CG   1 
ATOM   4066 C  CD1  . PHE A 1 259 ? -22.64600 18.59000 19.40700 1.000 30.04113  ? 259 PHE A CD1  1 
ATOM   4067 C  CD2  . PHE A 1 259 ? -23.26900 19.55300 21.50800 1.000 27.99434  ? 259 PHE A CD2  1 
ATOM   4068 C  CE1  . PHE A 1 259 ? -23.75100 19.17900 18.81400 1.000 32.54925  ? 259 PHE A CE1  1 
ATOM   4069 C  CE2  . PHE A 1 259 ? -24.36500 20.13100 20.92700 1.000 31.03535  ? 259 PHE A CE2  1 
ATOM   4070 C  CZ   . PHE A 1 259 ? -24.60500 19.95200 19.56600 1.000 30.46346  ? 259 PHE A CZ   1 
ATOM   4071 H  H    . PHE A 1 259 ? -22.16700 15.67700 20.10800 1.000 35.36558  ? 259 PHE A H    1 
ATOM   4072 H  HA   . PHE A 1 259 ? -20.69500 16.30300 22.24800 1.000 35.00558  ? 259 PHE A HA   1 
ATOM   4073 H  HB2  . PHE A 1 259 ? -21.05100 18.55200 22.26200 1.000 34.96558  ? 259 PHE A HB2  1 
ATOM   4074 H  HB3  . PHE A 1 259 ? -20.44500 18.23200 20.82800 1.000 34.96558  ? 259 PHE A HB3  1 
ATOM   4075 H  HD1  . PHE A 1 259 ? -22.06900 18.07000 18.89600 1.000 33.93558  ? 259 PHE A HD1  1 
ATOM   4076 H  HD2  . PHE A 1 259 ? -23.10900 19.68500 22.41500 1.000 33.57558  ? 259 PHE A HD2  1 
ATOM   4077 H  HE1  . PHE A 1 259 ? -23.91500 19.05100 17.90700 1.000 36.63558  ? 259 PHE A HE1  1 
ATOM   4078 H  HE2  . PHE A 1 259 ? -24.94900 20.64200 21.43900 1.000 36.96558  ? 259 PHE A HE2  1 
ATOM   4079 H  HZ   . PHE A 1 259 ? -25.34200 20.35500 19.16600 1.000 35.09558  ? 259 PHE A HZ   1 
ATOM   4080 N  N    . THR A 1 260 ? -22.84000 16.71000 23.61900 1.000 23.29163  ? 260 THR A N    1 
ATOM   4081 C  CA   . THR A 1 260 ? -24.09200 16.56200 24.35300 1.000 23.35586  ? 260 THR A CA   1 
ATOM   4082 C  C    . THR A 1 260 ? -24.99500 17.78000 24.18100 1.000 24.47720  ? 260 THR A C    1 
ATOM   4083 O  O    . THR A 1 260 ? -26.13300 17.65900 23.71500 1.000 27.39549  ? 260 THR A O    1 
ATOM   4084 C  CB   . THR A 1 260 ? -23.80400 16.32300 25.84600 1.000 27.61113  ? 260 THR A CB   1 
ATOM   4085 O  OG1  . THR A 1 260 ? -22.98200 15.16100 25.98300 1.000 29.48533  ? 260 THR A OG1  1 
ATOM   4086 C  CG2  . THR A 1 260 ? -25.08700 16.12800 26.61700 1.000 30.23179  ? 260 THR A CG2  1 
ATOM   4087 H  H    . THR A 1 260 ? -22.19800 17.05500 24.07600 1.000 28.77558  ? 260 THR A H    1 
ATOM   4088 H  HA   . THR A 1 260 ? -24.55800 15.78700 24.00300 1.000 29.52558  ? 260 THR A HA   1 
ATOM   4089 H  HB   . THR A 1 260 ? -23.34800 17.09400 26.21800 1.000 35.45558  ? 260 THR A HB   1 
ATOM   4090 H  HG1  . THR A 1 260 ? -22.81000 15.02500 26.79400 1.000 37.40558  ? 260 THR A HG1  1 
ATOM   4091 H  HG21 . THR A 1 260 ? -24.89200 15.79900 27.50900 1.000 39.23558  ? 260 THR A HG21 1 
ATOM   4092 H  HG22 . THR A 1 260 ? -25.56100 16.97100 26.69000 1.000 39.23558  ? 260 THR A HG22 1 
ATOM   4093 H  HG23 . THR A 1 260 ? -25.65400 15.48700 26.16200 1.000 39.23558  ? 260 THR A HG23 1 
ATOM   4094 N  N    . CYS A 1 261 ? -24.52200 18.94900 24.59800 1.000 26.18652  ? 261 CYS A N    1 
ATOM   4095 C  CA   . CYS A 1 261 ? -25.31000 20.17000 24.47300 1.000 23.30231  ? 261 CYS A CA   1 
ATOM   4096 C  C    . CYS A 1 261 ? -24.35500 21.35000 24.49600 1.000 25.50421  ? 261 CYS A C    1 
ATOM   4097 O  O    . CYS A 1 261 ? -23.16100 21.20000 24.77000 1.000 24.96105  ? 261 CYS A O    1 
ATOM   4098 C  CB   . CYS A 1 261 ? -26.36100 20.27800 25.57900 1.000 20.71159  ? 261 CYS A CB   1 
ATOM   4099 S  SG   . CYS A 1 261 ? -25.66600 20.27400 27.28800 1.000 24.85745  ? 261 CYS A SG   1 
ATOM   4100 H  H    . CYS A 1 261 ? -23.74900 19.06200 24.95600 1.000 33.49558  ? 261 CYS A H    1 
ATOM   4101 H  HA   . CYS A 1 261 ? -25.77700 20.17000 23.62200 1.000 30.13558  ? 261 CYS A HA   1 
ATOM   4102 H  HB2  . CYS A 1 261 ? -26.85000 21.10800 25.46300 1.000 27.68558  ? 261 CYS A HB2  1 
ATOM   4103 H  HB3  . CYS A 1 261 ? -26.96600 19.52300 25.50600 1.000 27.68558  ? 261 CYS A HB3  1 
ATOM   4104 H  HG   . CYS A 1 261 ? -26.56900 20.31400 28.07700 1.000 33.29558  ? 261 CYS A HG   1 
ATOM   4105 N  N    . ALA A 1 262 ? -24.88900 22.53100 24.19700 1.000 25.03216  ? 262 ALA A N    1 
ATOM   4106 C  CA   . ALA A 1 262 ? -24.05000 23.71400 24.08900 1.000 24.65087  ? 262 ALA A CA   1 
ATOM   4107 C  C    . ALA A 1 262 ? -24.87600 24.95700 24.36700 1.000 23.96234  ? 262 ALA A C    1 
ATOM   4108 O  O    . ALA A 1 262 ? -26.11100 24.93100 24.34400 1.000 24.59382  ? 262 ALA A O    1 
ATOM   4109 C  CB   . ALA A 1 262 ? -23.41200 23.80000 22.69700 1.000 28.85520  ? 262 ALA A CB   1 
ATOM   4110 H  H    . ALA A 1 262 ? -25.72600 22.66900 24.05600 1.000 32.08558  ? 262 ALA A H    1 
ATOM   4111 H  HA   . ALA A 1 262 ? -23.35000 23.67300 24.75900 1.000 31.51558  ? 262 ALA A HA   1 
ATOM   4112 H  HB1  . ALA A 1 262 ? -22.86800 24.60100 22.64800 1.000 35.87558  ? 262 ALA A HB1  1 
ATOM   4113 H  HB2  . ALA A 1 262 ? -22.85900 23.01600 22.55400 1.000 35.87558  ? 262 ALA A HB2  1 
ATOM   4114 H  HB3  . ALA A 1 262 ? -24.11500 23.83500 22.02900 1.000 35.87558  ? 262 ALA A HB3  1 
ATOM   4115 N  N    . SER A 1 263 ? -24.17400 26.05600 24.63200 1.000 23.72784  ? 263 SER A N    1 
ATOM   4116 C  CA   . SER A 1 263 ? -24.80400 27.35500 24.81400 1.000 23.64179  ? 263 SER A CA   1 
ATOM   4117 C  C    . SER A 1 263 ? -24.28200 28.31700 23.75600 1.000 23.47604  ? 263 SER A C    1 
ATOM   4118 O  O    . SER A 1 263 ? -23.09200 28.31900 23.42800 1.000 25.29585  ? 263 SER A O    1 
ATOM   4119 C  CB   . SER A 1 263 ? -24.55100 27.92600 26.20800 1.000 25.49321  ? 263 SER A CB   1 
ATOM   4120 O  OG   . SER A 1 263 ? -25.19900 27.12900 27.19400 1.000 29.56341  ? 263 SER A OG   1 
ATOM   4121 H  H    . SER A 1 263 ? -23.31800 26.07100 24.71300 1.000 30.39558  ? 263 SER A H    1 
ATOM   4122 H  HA   . SER A 1 263 ? -25.76300 27.26200 24.70800 1.000 30.10558  ? 263 SER A HA   1 
ATOM   4123 H  HB2  . SER A 1 263 ? -23.59600 27.93100 26.38100 1.000 32.48558  ? 263 SER A HB2  1 
ATOM   4124 H  HB3  . SER A 1 263 ? -24.90000 28.83000 26.25000 1.000 32.48558  ? 263 SER A HB3  1 
ATOM   4125 H  HG   . SER A 1 263 ? -24.90000 26.34400 27.17200 1.000 37.69558  ? 263 SER A HG   1 
ATOM   4126 N  N    . GLU A 1 264 ? -25.19400 29.11500 23.23300 1.000 26.18099  ? 264 GLU A N    1 
ATOM   4127 C  CA   . GLU A 1 264 ? -24.91800 30.09400 22.19700 1.000 29.14536  ? 264 GLU A CA   1 
ATOM   4128 C  C    . GLU A 1 264 ? -25.23900 31.46600 22.75700 1.000 31.03442  ? 264 GLU A C    1 
ATOM   4129 O  O    . GLU A 1 264 ? -26.29000 31.64900 23.36900 1.000 28.62005  ? 264 GLU A O    1 
ATOM   4130 C  CB   . GLU A 1 264 ? -25.77300 29.80200 20.97600 1.000 31.27370  ? 264 GLU A CB   1 
ATOM   4131 C  CG   . GLU A 1 264 ? -25.72100 30.86600 19.88000 1.000 32.34337  ? 264 GLU A CG   1 
ATOM   4132 C  CD   . GLU A 1 264 ? -26.87800 30.72900 18.90700 1.000 37.92577  ? 264 GLU A CD   1 
ATOM   4133 O  OE1  . GLU A 1 264 ? -27.99100 31.21200 19.22100 1.000 35.98911  ? 264 GLU A OE1  1 
ATOM   4134 O  OE2  . GLU A 1 264 ? -26.67600 30.13700 17.82700 1.000 43.81099  ? 264 GLU A OE2  1 
ATOM   4135 H  H    . GLU A 1 264 ? -26.02000 29.10700 23.47200 1.000 32.29558  ? 264 GLU A H    1 
ATOM   4136 H  HA   . GLU A 1 264 ? -23.98500 30.07800 21.93300 1.000 35.30558  ? 264 GLU A HA   1 
ATOM   4137 H  HB2  . GLU A 1 264 ? -25.47400 28.96700 20.58500 1.000 37.31558  ? 264 GLU A HB2  1 
ATOM   4138 H  HB3  . GLU A 1 264 ? -26.69700 29.72400 21.26100 1.000 37.31558  ? 264 GLU A HB3  1 
ATOM   4139 H  HG2  . GLU A 1 264 ? -25.76700 31.74600 20.28600 1.000 37.88558  ? 264 GLU A HG2  1 
ATOM   4140 H  HG3  . GLU A 1 264 ? -24.89300 30.77200 19.38300 1.000 37.88558  ? 264 GLU A HG3  1 
ATOM   4141 N  N    . TYR A 1 265 ? -24.33600 32.42300 22.56000 1.000 27.33389  ? 265 TYR A N    1 
ATOM   4142 C  CA   . TYR A 1 265 ? -24.54400 33.79000 23.00900 1.000 27.36195  ? 265 TYR A CA   1 
ATOM   4143 C  C    . TYR A 1 265 ? -24.49100 34.74000 21.82500 1.000 28.67865  ? 265 TYR A C    1 
ATOM   4144 O  O    . TYR A 1 265 ? -23.44700 34.86000 21.17700 1.000 31.57278  ? 265 TYR A O    1 
ATOM   4145 C  CB   . TYR A 1 265 ? -23.48600 34.20100 24.04100 1.000 27.77670  ? 265 TYR A CB   1 
ATOM   4146 C  CG   . TYR A 1 265 ? -23.69100 35.59800 24.57700 1.000 28.07238  ? 265 TYR A CG   1 
ATOM   4147 C  CD1  . TYR A 1 265 ? -24.64400 35.85600 25.55700 1.000 28.58239  ? 265 TYR A CD1  1 
ATOM   4148 C  CD2  . TYR A 1 265 ? -22.93200 36.66300 24.11000 1.000 32.35322  ? 265 TYR A CD2  1 
ATOM   4149 C  CE1  . TYR A 1 265 ? -24.83900 37.12400 26.03900 1.000 30.02544  ? 265 TYR A CE1  1 
ATOM   4150 C  CE2  . TYR A 1 265 ? -23.12200 37.93400 24.59400 1.000 36.68938  ? 265 TYR A CE2  1 
ATOM   4151 C  CZ   . TYR A 1 265 ? -24.06500 38.15800 25.56700 1.000 32.31719  ? 265 TYR A CZ   1 
ATOM   4152 O  OH   . TYR A 1 265 ? -24.25800 39.42100 26.05700 1.000 41.69874  ? 265 TYR A OH   1 
ATOM   4153 H  H    . TYR A 1 265 ? -23.58400 32.29900 22.16100 1.000 32.72558  ? 265 TYR A H    1 
ATOM   4154 H  HA   . TYR A 1 265 ? -25.42600 33.84700 23.40900 1.000 32.36558  ? 265 TYR A HA   1 
ATOM   4155 H  HB2  . TYR A 1 265 ? -23.52200 33.58500 24.78900 1.000 32.99558  ? 265 TYR A HB2  1 
ATOM   4156 H  HB3  . TYR A 1 265 ? -22.61100 34.16600 23.62400 1.000 32.99558  ? 265 TYR A HB3  1 
ATOM   4157 H  HD1  . TYR A 1 265 ? -25.15800 35.15600 25.89000 1.000 32.98558  ? 265 TYR A HD1  1 
ATOM   4158 H  HD2  . TYR A 1 265 ? -22.28500 36.51300 23.45900 1.000 37.49558  ? 265 TYR A HD2  1 
ATOM   4159 H  HE1  . TYR A 1 265 ? -25.49100 37.28400 26.68200 1.000 33.88558  ? 265 TYR A HE1  1 
ATOM   4160 H  HE2  . TYR A 1 265 ? -22.61400 38.64000 24.26400 1.000 41.97558  ? 265 TYR A HE2  1 
ATOM   4161 H  HH   . TYR A 1 265 ? -23.72100 39.95500 25.69400 1.000 46.56558  ? 265 TYR A HH   1 
ATOM   4162 N  N    . THR A 1 266 ? -25.60200 35.42900 21.57200 1.000 29.87205  ? 266 THR A N    1 
ATOM   4163 C  CA   . THR A 1 266 ? -25.70700 36.44000 20.52800 1.000 31.43059  ? 266 THR A CA   1 
ATOM   4164 C  C    . THR A 1 266 ? -25.74500 37.80400 21.19500 1.000 35.32036  ? 266 THR A C    1 
ATOM   4165 O  O    . THR A 1 266 ? -26.63500 38.07600 22.00100 1.000 38.45055  ? 266 THR A O    1 
ATOM   4166 C  CB   . THR A 1 266 ? -26.96300 36.21700 19.68500 1.000 32.54146  ? 266 THR A CB   1 
ATOM   4167 O  OG1  . THR A 1 266 ? -26.93900 34.87500 19.17700 1.000 37.86162  ? 266 THR A OG1  1 
ATOM   4168 C  CG2  . THR A 1 266 ? -27.03100 37.20500 18.54700 1.000 41.49098  ? 266 THR A CG2  1 
ATOM   4169 H  H    . THR A 1 266 ? -26.33500 35.32300 22.01000 1.000 34.26558  ? 266 THR A H    1 
ATOM   4170 H  HA   . THR A 1 266 ? -24.93400 36.39700 19.94300 1.000 35.45558  ? 266 THR A HA   1 
ATOM   4171 H  HB   . THR A 1 266 ? -27.75700 36.34800 20.22600 1.000 36.28558  ? 266 THR A HB   1 
ATOM   4172 H  HG1  . THR A 1 266 ? -27.63500 34.72300 18.73300 1.000 42.93558  ? 266 THR A HG1  1 
ATOM   4173 H  HG21 . THR A 1 266 ? -27.76000 36.97300 17.95000 1.000 46.19558  ? 266 THR A HG21 1 
ATOM   4174 H  HG22 . THR A 1 266 ? -27.17900 38.09900 18.89200 1.000 46.19558  ? 266 THR A HG22 1 
ATOM   4175 H  HG23 . THR A 1 266 ? -26.20000 37.19300 18.04700 1.000 46.19558  ? 266 THR A HG23 1 
ATOM   4176 N  N    . GLY A 1 267 ? -24.80800 38.67000 20.83000 1.000 39.02884  ? 267 GLY A N    1 
ATOM   4177 C  CA   . GLY A 1 267 ? -24.76500 39.99600 21.41600 1.000 42.23696  ? 267 GLY A CA   1 
ATOM   4178 C  C    . GLY A 1 267 ? -23.34700 40.44500 21.70400 1.000 44.34146  ? 267 GLY A C    1 
ATOM   4179 O  O    . GLY A 1 267 ? -22.41400 40.01400 21.02500 1.000 45.21102  ? 267 GLY A O    1 
ATOM   4180 H  H    . GLY A 1 267 ? -24.19200 38.51300 20.25000 1.000 43.92558  ? 267 GLY A H    1 
ATOM   4181 H  HA2  . GLY A 1 267 ? -25.17000 40.63200 20.80600 1.000 47.18558  ? 267 GLY A HA2  1 
ATOM   4182 H  HA3  . GLY A 1 267 ? -25.26200 39.99600 22.24900 1.000 47.18558  ? 267 GLY A HA3  1 
ATOM   4183 N  N    . ASN A 1 268 ? -23.17400 41.29500 22.71200 1.000 42.31088  ? 268 ASN A N    1 
ATOM   4184 C  CA   . ASN A 1 268 ? -21.86300 41.82300 23.06200 1.000 44.31714  ? 268 ASN A CA   1 
ATOM   4185 C  C    . ASN A 1 268 ? -21.72300 41.81000 24.58000 1.000 50.42831  ? 268 ASN A C    1 
ATOM   4186 O  O    . ASN A 1 268 ? -22.57400 41.28500 25.31000 1.000 49.47377  ? 268 ASN A O    1 
ATOM   4187 C  CB   . ASN A 1 268 ? -21.68500 43.22500 22.46500 1.000 44.09824  ? 268 ASN A CB   1 
ATOM   4188 C  CG   . ASN A 1 268 ? -22.76800 44.17500 22.89300 1.000 51.14810  ? 268 ASN A CG   1 
ATOM   4189 O  OD1  . ASN A 1 268 ? -23.00300 44.36900 24.08400 1.000 51.30054  ? 268 ASN A OD1  1 
ATOM   4190 N  ND2  . ASN A 1 268 ? -23.45400 44.76800 21.92000 1.000 66.20243  ? 268 ASN A ND2  1 
ATOM   4191 H  H    . ASN A 1 268 ? -23.81000 41.58400 23.21300 1.000 46.98558  ? 268 ASN A H    1 
ATOM   4192 H  HA   . ASN A 1 268 ? -21.18100 41.23800 22.69800 1.000 49.40558  ? 268 ASN A HA   1 
ATOM   4193 H  HB2  . ASN A 1 268 ? -20.83400 43.58800 22.75700 1.000 48.42558  ? 268 ASN A HB2  1 
ATOM   4194 H  HB3  . ASN A 1 268 ? -21.70400 43.16200 21.49700 1.000 48.42558  ? 268 ASN A HB3  1 
ATOM   4195 H  HD21 . ASN A 1 268 ? -23.26700 44.60000 21.09800 1.000 73.40558  ? 268 ASN A HD21 1 
ATOM   4196 H  HD22 . ASN A 1 268 ? -24.08400 45.32000 22.11300 1.000 73.40558  ? 268 ASN A HD22 1 
ATOM   4197 N  N    . TYR A 1 269 ? -20.63900 42.41300 25.06700 1.000 49.45743  ? 269 TYR A N    1 
ATOM   4198 C  CA   . TYR A 1 269 ? -20.32200 42.32800 26.48800 1.000 56.73373  ? 269 TYR A CA   1 
ATOM   4199 C  C    . TYR A 1 269 ? -21.34500 43.02400 27.37400 1.000 58.64883  ? 269 TYR A C    1 
ATOM   4200 O  O    . TYR A 1 269 ? -21.34000 42.79100 28.58800 1.000 53.85047  ? 269 TYR A O    1 
ATOM   4201 C  CB   . TYR A 1 269 ? -18.92800 42.91400 26.74200 1.000 66.54393  ? 269 TYR A CB   1 
ATOM   4202 C  CG   . TYR A 1 269 ? -18.85700 44.43100 26.68700 1.000 79.94826  ? 269 TYR A CG   1 
ATOM   4203 C  CD1  . TYR A 1 269 ? -19.08300 45.11500 25.49400 1.000 60.78077  ? 269 TYR A CD1  1 
ATOM   4204 C  CD2  . TYR A 1 269 ? -18.54400 45.17600 27.82300 1.000 60.55833  ? 269 TYR A CD2  1 
ATOM   4205 C  CE1  . TYR A 1 269 ? -19.01500 46.50000 25.43200 1.000 70.21654  ? 269 TYR A CE1  1 
ATOM   4206 C  CE2  . TYR A 1 269 ? -18.46900 46.56400 27.77200 1.000 61.90835  ? 269 TYR A CE2  1 
ATOM   4207 C  CZ   . TYR A 1 269 ? -18.70500 47.22100 26.57000 1.000 73.97488  ? 269 TYR A CZ   1 
ATOM   4208 O  OH   . TYR A 1 269 ? -18.63300 48.59700 26.50200 1.000 63.14576  ? 269 TYR A OH   1 
ATOM   4209 H  H    . TYR A 1 269 ? -20.08000 42.87000 24.60100 1.000 55.02558  ? 269 TYR A H    1 
ATOM   4210 H  HA   . TYR A 1 269 ? -20.30900 41.39300 26.74500 1.000 63.34558  ? 269 TYR A HA   1 
ATOM   4211 H  HB2  . TYR A 1 269 ? -18.63500 42.63900 27.62500 1.000 74.89558  ? 269 TYR A HB2  1 
ATOM   4212 H  HB3  . TYR A 1 269 ? -18.32100 42.56900 26.06900 1.000 74.89558  ? 269 TYR A HB3  1 
ATOM   4213 H  HD1  . TYR A 1 269 ? -19.28400 44.63400 24.72300 1.000 66.91558  ? 269 TYR A HD1  1 
ATOM   4214 H  HD2  . TYR A 1 269 ? -18.38200 44.73900 28.62800 1.000 65.42558  ? 269 TYR A HD2  1 
ATOM   4215 H  HE1  . TYR A 1 269 ? -19.17600 46.94000 24.62900 1.000 77.20558  ? 269 TYR A HE1  1 
ATOM   4216 H  HE2  . TYR A 1 269 ? -18.26300 47.05000 28.53800 1.000 65.90558  ? 269 TYR A HE2  1 
ATOM   4217 H  HH   . TYR A 1 269 ? -18.47200 48.91400 27.26200 1.000 66.40558  ? 269 TYR A HH   1 
ATOM   4218 N  N    . GLN A 1 270 ? -22.22200 43.85600 26.81400 1.000 44.67071  ? 270 GLN A N    1 
ATOM   4219 C  CA   . GLN A 1 270 ? -23.21400 44.56100 27.61500 1.000 50.05578  ? 270 GLN A CA   1 
ATOM   4220 C  C    . GLN A 1 270 ? -24.63200 44.04600 27.43500 1.000 64.14196  ? 270 GLN A C    1 
ATOM   4221 O  O    . GLN A 1 270 ? -25.43600 44.15900 28.36300 1.000 50.54282  ? 270 GLN A O    1 
ATOM   4222 C  CB   . GLN A 1 270 ? -23.18700 46.06000 27.28300 1.000 57.10451  ? 270 GLN A CB   1 
ATOM   4223 C  CG   . GLN A 1 270 ? -21.91000 46.74600 27.76000 1.000 84.10571  ? 270 GLN A CG   1 
ATOM   4224 C  CD   . GLN A 1 270 ? -22.01000 48.25600 27.76400 1.000 82.06761  ? 270 GLN A CD   1 
ATOM   4225 O  OE1  . GLN A 1 270 ? -21.86900 48.89200 28.80900 1.000 77.96657  ? 270 GLN A OE1  1 
ATOM   4226 N  NE2  . GLN A 1 270 ? -22.24800 48.84000 26.59200 1.000 69.63780  ? 270 GLN A NE2  1 
ATOM   4227 H  H    . GLN A 1 270 ? -22.26000 44.02700 25.97200 1.000 47.06558  ? 270 GLN A H    1 
ATOM   4228 H  HA   . GLN A 1 270 ? -22.98500 44.45700 28.55100 1.000 52.21558  ? 270 GLN A HA   1 
ATOM   4229 H  HB2  . GLN A 1 270 ? -23.24800 46.17100 26.32100 1.000 59.51558  ? 270 GLN A HB2  1 
ATOM   4230 H  HB3  . GLN A 1 270 ? -23.94000 46.49200 27.71500 1.000 59.51558  ? 270 GLN A HB3  1 
ATOM   4231 H  HG2  . GLN A 1 270 ? -21.71700 46.45700 28.66500 1.000 91.37558  ? 270 GLN A HG2  1 
ATOM   4232 H  HG3  . GLN A 1 270 ? -21.18100 46.49700 27.17000 1.000 91.37558  ? 270 GLN A HG3  1 
ATOM   4233 H  HE21 . GLN A 1 270 ? -22.33700 48.36100 25.88300 1.000 72.65558  ? 270 GLN A HE21 1 
ATOM   4234 H  HE22 . GLN A 1 270 ? -22.31400 49.69600 26.54400 1.000 72.65558  ? 270 GLN A HE22 1 
ATOM   4235 N  N    . SER A 1 271 ? -24.96200 43.49400 26.27000 1.000 50.17668  ? 271 SER A N    1 
ATOM   4236 C  CA   . SER A 1 271 ? -26.32800 43.07100 25.99000 1.000 48.12913  ? 271 SER A CA   1 
ATOM   4237 C  C    . SER A 1 271 ? -26.28800 41.89000 25.03800 1.000 47.49290  ? 271 SER A C    1 
ATOM   4238 O  O    . SER A 1 271 ? -25.65500 41.96300 23.98200 1.000 43.18680  ? 271 SER A O    1 
ATOM   4239 C  CB   . SER A 1 271 ? -27.15900 44.21100 25.38100 1.000 57.03103  ? 271 SER A CB   1 
ATOM   4240 O  OG   . SER A 1 271 ? -26.79600 44.44900 24.03700 1.000 61.96429  ? 271 SER A OG   1 
ATOM   4241 H  H    . SER A 1 271 ? -24.41100 43.35500 25.62500 1.000 53.41558  ? 271 SER A H    1 
ATOM   4242 H  HA   . SER A 1 271 ? -26.75200 42.79300 26.81700 1.000 50.98558  ? 271 SER A HA   1 
ATOM   4243 H  HB2  . SER A 1 271 ? -28.09700 43.96800 25.41400 1.000 60.63558  ? 271 SER A HB2  1 
ATOM   4244 H  HB3  . SER A 1 271 ? -27.00700 45.01900 25.89500 1.000 60.63558  ? 271 SER A HB3  1 
ATOM   4245 H  HG   . SER A 1 271 ? -25.97900 44.63800 23.98900 1.000 66.88558  ? 271 SER A HG   1 
ATOM   4246 N  N    . GLY A 1 272 ? -26.96100 40.81600 25.41100 1.000 37.44656  ? 272 GLY A N    1 
ATOM   4247 C  CA   . GLY A 1 272 ? -27.06900 39.68500 24.52400 1.000 38.07071  ? 272 GLY A CA   1 
ATOM   4248 C  C    . GLY A 1 272 ? -28.20500 38.78600 24.91700 1.000 36.38812  ? 272 GLY A C    1 
ATOM   4249 O  O    . GLY A 1 272 ? -29.13300 39.19300 25.62100 1.000 39.13372  ? 272 GLY A O    1 
ATOM   4250 H  H    . GLY A 1 272 ? -27.36000 40.72200 26.16700 1.000 42.39558  ? 272 GLY A H    1 
ATOM   4251 H  HA2  . GLY A 1 272 ? -27.21900 39.99700 23.61700 1.000 43.06558  ? 272 GLY A HA2  1 
ATOM   4252 H  HA3  . GLY A 1 272 ? -26.24500 39.17300 24.54900 1.000 43.06558  ? 272 GLY A HA3  1 
ATOM   4253 N  N    . HIS A 1 273 ? -28.11000 37.54100 24.46100 1.000 31.67614  ? 273 HIS A N    1 
ATOM   4254 C  CA   . HIS A 1 273 ? -29.13300 36.53800 24.72400 1.000 27.46281  ? 273 HIS A CA   1 
ATOM   4255 C  C    . HIS A 1 273 ? -28.51300 35.16600 24.50400 1.000 29.06479  ? 273 HIS A C    1 
ATOM   4256 O  O    . HIS A 1 273 ? -27.75000 34.97000 23.55600 1.000 27.82099  ? 273 HIS A O    1 
ATOM   4257 C  CB   . HIS A 1 273 ? -30.33500 36.73300 23.80000 1.000 30.23240  ? 273 HIS A CB   1 
ATOM   4258 C  CG   . HIS A 1 273 ? -31.47700 35.81700 24.08900 1.000 31.18516  ? 273 HIS A CG   1 
ATOM   4259 N  ND1  . HIS A 1 273 ? -32.40000 36.06500 25.08400 1.000 33.73073  ? 273 HIS A ND1  1 
ATOM   4260 C  CD2  . HIS A 1 273 ? -31.84500 34.64900 23.51400 1.000 36.58187  ? 273 HIS A CD2  1 
ATOM   4261 C  CE1  . HIS A 1 273 ? -33.28500 35.08400 25.11200 1.000 34.21286  ? 273 HIS A CE1  1 
ATOM   4262 N  NE2  . HIS A 1 273 ? -32.97100 34.21300 24.17200 1.000 30.59975  ? 273 HIS A NE2  1 
ATOM   4263 H  H    . HIS A 1 273 ? -27.45200 37.24800 23.98900 1.000 35.68558  ? 273 HIS A H    1 
ATOM   4264 H  HA   . HIS A 1 273 ? -29.43900 36.59800 25.64200 1.000 30.82558  ? 273 HIS A HA   1 
ATOM   4265 H  HB2  . HIS A 1 273 ? -30.65600 37.64400 23.89600 1.000 33.43558  ? 273 HIS A HB2  1 
ATOM   4266 H  HB3  . HIS A 1 273 ? -30.05400 36.57500 22.88500 1.000 33.43558  ? 273 HIS A HB3  1 
ATOM   4267 H  HD1  . HIS A 1 273 ? -32.39900 36.75000 25.60400 1.000 38.11558  ? 273 HIS A HD1  1 
ATOM   4268 H  HD2  . HIS A 1 273 ? -31.41800 34.22200 22.80800 1.000 41.30558  ? 273 HIS A HD2  1 
ATOM   4269 H  HE1  . HIS A 1 273 ? -34.00600 35.01900 25.69600 1.000 38.93558  ? 273 HIS A HE1  1 
ATOM   4270 H  HE2  . HIS A 1 273 ? -33.40200 33.48900 23.99800 1.000 34.47558  ? 273 HIS A HE2  1 
ATOM   4271 N  N    . TYR A 1 274 ? -28.84500 34.23300 25.38300 1.000 26.47862  ? 274 TYR A N    1 
ATOM   4272 C  CA   . TYR A 1 274 ? -28.38400 32.85800 25.28900 1.000 26.22457  ? 274 TYR A CA   1 
ATOM   4273 C  C    . TYR A 1 274 ? -29.46000 31.94400 24.69700 1.000 28.20912  ? 274 TYR A C    1 
ATOM   4274 O  O    . TYR A 1 274 ? -30.65000 32.10800 24.97800 1.000 27.09469  ? 274 TYR A O    1 
ATOM   4275 C  CB   . TYR A 1 274 ? -28.02100 32.33900 26.67100 1.000 24.93188  ? 274 TYR A CB   1 
ATOM   4276 C  CG   . TYR A 1 274 ? -26.64900 32.69900 27.19000 1.000 22.22561  ? 274 TYR A CG   1 
ATOM   4277 C  CD1  . TYR A 1 274 ? -25.51700 32.00600 26.77100 1.000 23.71639  ? 274 TYR A CD1  1 
ATOM   4278 C  CD2  . TYR A 1 274 ? -26.49500 33.68200 28.14900 1.000 25.87991  ? 274 TYR A CD2  1 
ATOM   4279 C  CE1  . TYR A 1 274 ? -24.27300 32.30100 27.28200 1.000 24.76137  ? 274 TYR A CE1  1 
ATOM   4280 C  CE2  . TYR A 1 274 ? -25.24700 33.97300 28.67900 1.000 27.59869  ? 274 TYR A CE2  1 
ATOM   4281 C  CZ   . TYR A 1 274 ? -24.15500 33.28100 28.24800 1.000 28.63649  ? 274 TYR A CZ   1 
ATOM   4282 O  OH   . TYR A 1 274 ? -22.93400 33.56900 28.78600 1.000 27.81871  ? 274 TYR A OH   1 
ATOM   4283 H  H    . TYR A 1 274 ? -29.35200 34.37600 26.06300 1.000 30.68558  ? 274 TYR A H    1 
ATOM   4284 H  HA   . TYR A 1 274 ? -27.61200 32.83100 24.70300 1.000 30.78558  ? 274 TYR A HA   1 
ATOM   4285 H  HB2  . TYR A 1 274 ? -28.66600 32.69300 27.30400 1.000 30.12558  ? 274 TYR A HB2  1 
ATOM   4286 H  HB3  . TYR A 1 274 ? -28.07300 31.37100 26.65200 1.000 30.12558  ? 274 TYR A HB3  1 
ATOM   4287 H  HD1  . TYR A 1 274 ? -25.60200 31.33300 26.13500 1.000 28.98558  ? 274 TYR A HD1  1 
ATOM   4288 H  HD2  . TYR A 1 274 ? -27.23900 34.15600 28.44400 1.000 31.70558  ? 274 TYR A HD2  1 
ATOM   4289 H  HE1  . TYR A 1 274 ? -23.52000 31.84500 26.98000 1.000 30.50558  ? 274 TYR A HE1  1 
ATOM   4290 H  HE2  . TYR A 1 274 ? -25.15500 34.63600 29.32500 1.000 34.03558  ? 274 TYR A HE2  1 
ATOM   4291 H  HH   . TYR A 1 274 ? -22.99200 34.24300 29.28400 1.000 34.67558  ? 274 TYR A HH   1 
ATOM   4292 N  N    . LYS A 1 275 ? -29.02200 30.95900 23.90300 1.000 26.29833  ? 275 LYS A N    1 
ATOM   4293 C  CA   . LYS A 1 275 ? -29.85600 29.84300 23.48500 1.000 27.27560  ? 275 LYS A CA   1 
ATOM   4294 C  C    . LYS A 1 275 ? -29.12700 28.54900 23.82500 1.000 27.19976  ? 275 LYS A C    1 
ATOM   4295 O  O    . LYS A 1 275 ? -27.90700 28.52800 23.97800 1.000 27.47501  ? 275 LYS A O    1 
ATOM   4296 C  CB   . LYS A 1 275 ? -30.17900 29.88000 21.97300 1.000 27.04803  ? 275 LYS A CB   1 
ATOM   4297 C  CG   . LYS A 1 275 ? -31.04900 31.03300 21.56500 1.000 31.09421  ? 275 LYS A CG   1 
ATOM   4298 C  CD   . LYS A 1 275 ? -31.41500 30.97200 20.07000 1.000 33.37890  ? 275 LYS A CD   1 
ATOM   4299 C  CE   . LYS A 1 275 ? -32.12900 32.24400 19.65100 1.000 38.83303  ? 275 LYS A CE   1 
ATOM   4300 N  NZ   . LYS A 1 275 ? -32.18400 32.36400 18.15900 1.000 47.51300  ? 275 LYS A NZ   1 
ATOM   4301 H  H    . LYS A 1 275 ? -28.22300 30.92100 23.58800 1.000 30.54558  ? 275 LYS A H    1 
ATOM   4302 H  HA   . LYS A 1 275 ? -30.70100 29.87400 23.96100 1.000 31.73558  ? 275 LYS A HA   1 
ATOM   4303 H  HB2  . LYS A 1 275 ? -29.34700 29.94900 21.47900 1.000 30.46558  ? 275 LYS A HB2  1 
ATOM   4304 H  HB3  . LYS A 1 275 ? -30.64100 29.06200 21.73300 1.000 30.46558  ? 275 LYS A HB3  1 
ATOM   4305 H  HG2  . LYS A 1 275 ? -31.87100 31.01300 22.08000 1.000 34.69558  ? 275 LYS A HG2  1 
ATOM   4306 H  HG3  . LYS A 1 275 ? -30.57600 31.86500 21.72800 1.000 34.69558  ? 275 LYS A HG3  1 
ATOM   4307 H  HD2  . LYS A 1 275 ? -30.60800 30.88100 19.54000 1.000 36.42558  ? 275 LYS A HD2  1 
ATOM   4308 H  HD3  . LYS A 1 275 ? -32.00400 30.21800 19.90900 1.000 36.42558  ? 275 LYS A HD3  1 
ATOM   4309 H  HE2  . LYS A 1 275 ? -33.03700 32.23100 19.99200 1.000 42.30558  ? 275 LYS A HE2  1 
ATOM   4310 H  HE3  . LYS A 1 275 ? -31.65300 33.01200 20.00300 1.000 42.30558  ? 275 LYS A HE3  1 
ATOM   4311 H  HZ1  . LYS A 1 275 ? -32.60500 33.11400 17.93000 1.000 51.65558  ? 275 LYS A HZ1  1 
ATOM   4312 H  HZ2  . LYS A 1 275 ? -31.36000 32.38100 17.82500 1.000 51.65558  ? 275 LYS A HZ2  1 
ATOM   4313 H  HZ3  . LYS A 1 275 ? -32.62100 31.67000 17.81400 1.000 51.65558  ? 275 LYS A HZ3  1 
ATOM   4314 N  N    . HIS A 1 276 ? -29.88700 27.45900 23.85000 1.000 25.89017  ? 276 HIS A N    1 
ATOM   4315 C  CA   . HIS A 1 276 ? -29.38900 26.13400 24.20100 1.000 25.10710  ? 276 HIS A CA   1 
ATOM   4316 C  C    . HIS A 1 276 ? -29.51100 25.21800 22.99000 1.000 29.35023  ? 276 HIS A C    1 
ATOM   4317 O  O    . HIS A 1 276 ? -30.55000 25.20600 22.33600 1.000 29.56791  ? 276 HIS A O    1 
ATOM   4318 C  CB   . HIS A 1 276 ? -30.20300 25.56300 25.37300 1.000 23.72073  ? 276 HIS A CB   1 
ATOM   4319 C  CG   . HIS A 1 276 ? -29.72400 24.22700 25.83400 1.000 24.86460  ? 276 HIS A CG   1 
ATOM   4320 N  ND1  . HIS A 1 276 ? -28.77000 24.08600 26.81600 1.000 24.35824  ? 276 HIS A ND1  1 
ATOM   4321 C  CD2  . HIS A 1 276 ? -30.05700 22.97300 25.44700 1.000 25.68004  ? 276 HIS A CD2  1 
ATOM   4322 C  CE1  . HIS A 1 276 ? -28.52000 22.80100 27.00400 1.000 23.38605  ? 276 HIS A CE1  1 
ATOM   4323 N  NE2  . HIS A 1 276 ? -29.28900 22.10300 26.18500 1.000 25.78872  ? 276 HIS A NE2  1 
ATOM   4324 H  H    . HIS A 1 276 ? -30.72600 27.46200 23.65900 1.000 30.95558  ? 276 HIS A H    1 
ATOM   4325 H  HA   . HIS A 1 276 ? -28.45400 26.18300 24.45400 1.000 30.59558  ? 276 HIS A HA   1 
ATOM   4326 H  HB2  . HIS A 1 276 ? -30.14300 26.17500 26.12300 1.000 29.93558  ? 276 HIS A HB2  1 
ATOM   4327 H  HB3  . HIS A 1 276 ? -31.12700 25.46700 25.09500 1.000 29.93558  ? 276 HIS A HB3  1 
ATOM   4328 H  HD1  . HIS A 1 276 ? -28.39400 24.73200 27.24100 1.000 31.99558  ? 276 HIS A HD1  1 
ATOM   4329 H  HD2  . HIS A 1 276 ? -30.68600 22.74300 24.80300 1.000 33.11558  ? 276 HIS A HD2  1 
ATOM   4330 H  HE1  . HIS A 1 276 ? -27.90900 22.44800 27.60900 1.000 31.29558  ? 276 HIS A HE1  1 
ATOM   4331 N  N    . ILE A 1 277 ? -28.46200 24.45300 22.68800 1.000 25.88958  ? 277 ILE A N    1 
ATOM   4332 C  CA   . ILE A 1 277 ? -28.51600 23.45200 21.62800 1.000 27.54619  ? 277 ILE A CA   1 
ATOM   4333 C  C    . ILE A 1 277 ? -28.24000 22.08800 22.23400 1.000 28.21706  ? 277 ILE A C    1 
ATOM   4334 O  O    . ILE A 1 277 ? -27.24200 21.90500 22.94300 1.000 27.07549  ? 277 ILE A O    1 
ATOM   4335 C  CB   . ILE A 1 277 ? -27.52700 23.76300 20.49600 1.000 31.63403  ? 277 ILE A CB   1 
ATOM   4336 C  CG1  . ILE A 1 277 ? -27.88000 25.11500 19.88300 1.000 36.90115  ? 277 ILE A CG1  1 
ATOM   4337 C  CG2  . ILE A 1 277 ? -27.60800 22.69100 19.39700 1.000 31.58715  ? 277 ILE A CG2  1 
ATOM   4338 C  CD1  . ILE A 1 277 ? -27.03300 26.22900 20.38200 1.000 39.46415  ? 277 ILE A CD1  1 
ATOM   4339 H  H    . ILE A 1 277 ? -27.70200 24.49700 23.08900 1.000 30.80558  ? 277 ILE A H    1 
ATOM   4340 H  HA   . ILE A 1 277 ? -29.41000 23.43800 21.25100 1.000 32.19558  ? 277 ILE A HA   1 
ATOM   4341 H  HB   . ILE A 1 277 ? -26.63100 23.77800 20.86600 1.000 36.05558  ? 277 ILE A HB   1 
ATOM   4342 H  HG12 . ILE A 1 277 ? -27.76400 25.06100 18.92100 1.000 41.71558  ? 277 ILE A HG12 1 
ATOM   4343 H  HG13 . ILE A 1 277 ? -28.80300 25.32400 20.09500 1.000 41.71558  ? 277 ILE A HG13 1 
ATOM   4344 H  HG21 . ILE A 1 277 ? -27.05900 22.96700 18.64600 1.000 35.25558  ? 277 ILE A HG21 1 
ATOM   4345 H  HG22 . ILE A 1 277 ? -27.28300 21.84900 19.75300 1.000 35.25558  ? 277 ILE A HG22 1 
ATOM   4346 H  HG23 . ILE A 1 277 ? -28.53100 22.59700 19.11500 1.000 35.25558  ? 277 ILE A HG23 1 
ATOM   4347 H  HD11 . ILE A 1 277 ? -27.29700 27.05000 19.93700 1.000 44.96558  ? 277 ILE A HD11 1 
ATOM   4348 H  HD12 . ILE A 1 277 ? -27.16000 26.31700 21.34000 1.000 44.96558  ? 277 ILE A HD12 1 
ATOM   4349 H  HD13 . ILE A 1 277 ? -26.10400 26.03100 20.18800 1.000 44.96558  ? 277 ILE A HD13 1 
ATOM   4350 N  N    . THR A 1 278 ? -29.12600 21.13200 21.96800 1.000 27.75807  ? 278 THR A N    1 
ATOM   4351 C  CA   . THR A 1 278 ? -28.96700 19.77300 22.46600 1.000 27.17647  ? 278 THR A CA   1 
ATOM   4352 C  C    . THR A 1 278 ? -28.96000 18.80600 21.28800 1.000 29.10856  ? 278 THR A C    1 
ATOM   4353 O  O    . THR A 1 278 ? -29.73800 18.96000 20.33600 1.000 29.24319  ? 278 THR A O    1 
ATOM   4354 C  CB   . THR A 1 278 ? -30.06600 19.44100 23.49000 1.000 27.89712  ? 278 THR A CB   1 
ATOM   4355 O  OG1  . THR A 1 278 ? -29.93600 18.08400 23.91600 1.000 32.17986  ? 278 THR A OG1  1 
ATOM   4356 C  CG2  . THR A 1 278 ? -31.44900 19.65000 22.91300 1.000 31.21080  ? 278 THR A CG2  1 
ATOM   4357 H  H    . THR A 1 278 ? -29.83400 21.25100 21.49500 1.000 33.26558  ? 278 THR A H    1 
ATOM   4358 H  HA   . THR A 1 278 ? -28.11800 19.66400 22.92100 1.000 33.23558  ? 278 THR A HA   1 
ATOM   4359 H  HB   . THR A 1 278 ? -29.97000 20.03600 24.25000 1.000 35.24558  ? 278 THR A HB   1 
ATOM   4360 H  HG1  . THR A 1 278 ? -30.54100 17.89600 24.46700 1.000 41.06558  ? 278 THR A HG1  1 
ATOM   4361 H  HG21 . THR A 1 278 ? -32.12100 19.47000 23.58900 1.000 38.95558  ? 278 THR A HG21 1 
ATOM   4362 H  HG22 . THR A 1 278 ? -31.54700 20.56500 22.60800 1.000 38.95558  ? 278 THR A HG22 1 
ATOM   4363 H  HG23 . THR A 1 278 ? -31.58900 19.05100 22.16200 1.000 38.95558  ? 278 THR A HG23 1 
ATOM   4364 N  N    . SER A 1 279 ? -28.02000 17.85700 21.31100 1.000 27.95583  ? 279 SER A N    1 
ATOM   4365 C  CA   . SER A 1 279 ? -27.85700 16.88800 20.22700 1.000 29.79062  ? 279 SER A CA   1 
ATOM   4366 C  C    . SER A 1 279 ? -28.54000 15.58900 20.64000 1.000 34.39377  ? 279 SER A C    1 
ATOM   4367 O  O    . SER A 1 279 ? -28.03000 14.85600 21.49100 1.000 33.74844  ? 279 SER A O    1 
ATOM   4368 C  CB   . SER A 1 279 ? -26.38400 16.64500 19.90100 1.000 33.01102  ? 279 SER A CB   1 
ATOM   4369 O  OG   . SER A 1 279 ? -26.24900 15.65200 18.87900 1.000 36.10401  ? 279 SER A OG   1 
ATOM   4370 H  H    . SER A 1 279 ? -27.45900 17.75400 21.95400 1.000 33.34558  ? 279 SER A H    1 
ATOM   4371 H  HA   . SER A 1 279 ? -28.28600 17.23600 19.43000 1.000 34.66558  ? 279 SER A HA   1 
ATOM   4372 H  HB2  . SER A 1 279 ? -25.98800 17.47400 19.59100 1.000 37.90558  ? 279 SER A HB2  1 
ATOM   4373 H  HB3  . SER A 1 279 ? -25.93000 16.33800 20.70200 1.000 37.90558  ? 279 SER A HB3  1 
ATOM   4374 H  HG   . SER A 1 279 ? -26.53900 14.91300 19.15600 1.000 40.68558  ? 279 SER A HG   1 
ATOM   4375 N  N    . LYS A 1 280 ? -29.69200 15.31200 20.03500 1.000 36.84386  ? 280 LYS A N    1 
ATOM   4376 C  CA   . LYS A 1 280 ? -30.45700 14.10200 20.31300 1.000 30.36935  ? 280 LYS A CA   1 
ATOM   4377 C  C    . LYS A 1 280 ? -30.64000 13.34500 19.00500 1.000 33.59031  ? 280 LYS A C    1 
ATOM   4378 O  O    . LYS A 1 280 ? -29.65500 13.08100 18.31300 1.000 38.04918  ? 280 LYS A O    1 
ATOM   4379 C  CB   . LYS A 1 280 ? -31.79000 14.45400 20.96700 1.000 31.37386  ? 280 LYS A CB   1 
ATOM   4380 C  CG   . LYS A 1 280 ? -31.65100 15.40600 22.15600 1.000 32.97332  ? 280 LYS A CG   1 
ATOM   4381 C  CD   . LYS A 1 280 ? -30.90800 14.76900 23.31200 1.000 36.11257  ? 280 LYS A CD   1 
ATOM   4382 C  CE   . LYS A 1 280 ? -31.66300 13.58700 23.89000 1.000 54.16474  ? 280 LYS A CE   1 
ATOM   4383 N  NZ   . LYS A 1 280 ? -31.07800 13.17200 25.19600 1.000 53.81241  ? 280 LYS A NZ   1 
ATOM   4384 H  H    . LYS A 1 280 ? -30.05900 15.82100 19.44600 1.000 43.66558  ? 280 LYS A H    1 
ATOM   4385 H  HA   . LYS A 1 280 ? -29.99500 13.52600 20.94200 1.000 36.62558  ? 280 LYS A HA   1 
ATOM   4386 H  HB2  . LYS A 1 280 ? -32.35900 14.88300 20.30800 1.000 38.79558  ? 280 LYS A HB2  1 
ATOM   4387 H  HB3  . LYS A 1 280 ? -32.20800 13.63900 21.28500 1.000 38.79558  ? 280 LYS A HB3  1 
ATOM   4388 H  HG2  . LYS A 1 280 ? -31.15900 16.19400 21.87800 1.000 41.58558  ? 280 LYS A HG2  1 
ATOM   4389 H  HG3  . LYS A 1 280 ? -32.53400 15.65900 22.46700 1.000 41.58558  ? 280 LYS A HG3  1 
ATOM   4390 H  HD2  . LYS A 1 280 ? -30.04400 14.45400 23.00200 1.000 46.37558  ? 280 LYS A HD2  1 
ATOM   4391 H  HD3  . LYS A 1 280 ? -30.78800 15.42600 24.01600 1.000 46.37558  ? 280 LYS A HD3  1 
ATOM   4392 H  HE2  . LYS A 1 280 ? -32.59000 13.83400 24.03300 1.000 69.13558  ? 280 LYS A HE2  1 
ATOM   4393 H  HE3  . LYS A 1 280 ? -31.61000 12.83700 23.27700 1.000 69.13558  ? 280 LYS A HE3  1 
ATOM   4394 H  HZ1  . LYS A 1 280 ? -30.22700 12.93300 25.08700 1.000 69.85558  ? 280 LYS A HZ1  1 
ATOM   4395 H  HZ2  . LYS A 1 280 ? -31.53100 12.48200 25.52800 1.000 69.85558  ? 280 LYS A HZ2  1 
ATOM   4396 H  HZ3  . LYS A 1 280 ? -31.11600 13.84700 25.77500 1.000 69.85558  ? 280 LYS A HZ3  1 
ATOM   4397 N  N    . GLU A 1 281 ? -31.88000 12.99200 18.65000 1.000 35.97872  ? 281 GLU A N    1 
ATOM   4398 C  CA   . GLU A 1 281 ? -32.12300 12.37600 17.34700 1.000 38.48120  ? 281 GLU A CA   1 
ATOM   4399 C  C    . GLU A 1 281 ? -31.85700 13.35500 16.21200 1.000 40.38051  ? 281 GLU A C    1 
ATOM   4400 O  O    . GLU A 1 281 ? -31.60400 12.93200 15.07700 1.000 42.41396  ? 281 GLU A O    1 
ATOM   4401 C  CB   . GLU A 1 281 ? -33.56600 11.86000 17.28400 1.000 38.00406  ? 281 GLU A CB   1 
ATOM   4402 C  CG   . GLU A 1 281 ? -34.61500 12.96600 17.46200 1.000 51.63688  ? 281 GLU A CG   1 
ATOM   4403 C  CD   . GLU A 1 281 ? -35.17100 13.02800 18.88400 1.000 51.54405  ? 281 GLU A CD   1 
ATOM   4404 O  OE1  . GLU A 1 281 ? -34.39000 12.78400 19.83700 1.000 35.39619  ? 281 GLU A OE1  1 
ATOM   4405 O  OE2  . GLU A 1 281 ? -36.38900 13.30200 19.05100 1.000 45.09644  ? 281 GLU A OE2  1 
ATOM   4406 H  H    . GLU A 1 281 ? -32.58200 13.09600 19.13700 1.000 42.30558  ? 281 GLU A H    1 
ATOM   4407 H  HA   . GLU A 1 281 ? -31.53500 11.61400 17.22800 1.000 44.09558  ? 281 GLU A HA   1 
ATOM   4408 H  HB2  . GLU A 1 281 ? -33.71400 11.44600 16.41900 1.000 44.02558  ? 281 GLU A HB2  1 
ATOM   4409 H  HB3  . GLU A 1 281 ? -33.69700 11.20900 17.99100 1.000 44.02558  ? 281 GLU A HB3  1 
ATOM   4410 H  HG2  . GLU A 1 281 ? -34.20900 13.82300 17.26000 1.000 60.68558  ? 281 GLU A HG2  1 
ATOM   4411 H  HG3  . GLU A 1 281 ? -35.35600 12.79900 16.85700 1.000 60.68558  ? 281 GLU A HG3  1 
ATOM   4412 N  N    . THR A 1 282 ? -31.95500 14.65000 16.49200 1.000 38.79619  ? 282 THR A N    1 
ATOM   4413 C  CA   . THR A 1 282 ? -31.49400 15.71100 15.61600 1.000 37.70031  ? 282 THR A CA   1 
ATOM   4414 C  C    . THR A 1 282 ? -30.98500 16.82600 16.52500 1.000 38.88581  ? 282 THR A C    1 
ATOM   4415 O  O    . THR A 1 282 ? -30.87300 16.63900 17.73700 1.000 34.88271  ? 282 THR A O    1 
ATOM   4416 C  CB   . THR A 1 282 ? -32.60900 16.14100 14.65800 1.000 42.78314  ? 282 THR A CB   1 
ATOM   4417 O  OG1  . THR A 1 282 ? -32.07900 17.06400 13.69800 1.000 43.96754  ? 282 THR A OG1  1 
ATOM   4418 C  CG2  . THR A 1 282 ? -33.76100 16.77500 15.40700 1.000 37.86633  ? 282 THR A CG2  1 
ATOM   4419 H  H    . THR A 1 282 ? -32.30200 14.95000 17.22000 1.000 43.11558  ? 282 THR A H    1 
ATOM   4420 H  HA   . THR A 1 282 ? -30.75900 15.40600 15.06100 1.000 40.59558  ? 282 THR A HA   1 
ATOM   4421 H  HB   . THR A 1 282 ? -32.95900 15.36200 14.19700 1.000 45.86558  ? 282 THR A HB   1 
ATOM   4422 H  HG1  . THR A 1 282 ? -32.68700 17.31800 13.17700 1.000 46.01558  ? 282 THR A HG1  1 
ATOM   4423 H  HG21 . THR A 1 282 ? -34.49900 16.94400 14.80000 1.000 40.93558  ? 282 THR A HG21 1 
ATOM   4424 H  HG22 . THR A 1 282 ? -34.06400 16.18300 16.11300 1.000 40.93558  ? 282 THR A HG22 1 
ATOM   4425 H  HG23 . THR A 1 282 ? -33.47900 17.61600 15.80000 1.000 40.93558  ? 282 THR A HG23 1 
ATOM   4426 N  N    . LEU A 1 283 ? -30.65000 17.97900 15.94600 1.000 35.27207  ? 283 LEU A N    1 
ATOM   4427 C  CA   . LEU A 1 283 ? -30.22700 19.13800 16.72800 1.000 33.13372  ? 283 LEU A CA   1 
ATOM   4428 C  C    . LEU A 1 283 ? -31.44400 19.98500 17.09000 1.000 33.30721  ? 283 LEU A C    1 
ATOM   4429 O  O    . LEU A 1 283 ? -32.14000 20.48900 16.20800 1.000 34.76973  ? 283 LEU A O    1 
ATOM   4430 C  CB   . LEU A 1 283 ? -29.21500 19.97500 15.95500 1.000 35.40899  ? 283 LEU A CB   1 
ATOM   4431 C  CG   . LEU A 1 283 ? -27.87800 19.28600 15.66500 1.000 39.16916  ? 283 LEU A CG   1 
ATOM   4432 C  CD1  . LEU A 1 283 ? -27.00400 20.19200 14.82700 1.000 43.39299  ? 283 LEU A CD1  1 
ATOM   4433 C  CD2  . LEU A 1 283 ? -27.16900 18.89900 16.95500 1.000 41.17512  ? 283 LEU A CD2  1 
ATOM   4434 H  H    . LEU A 1 283 ? -30.66100 18.11500 15.09700 1.000 37.54558  ? 283 LEU A H    1 
ATOM   4435 H  HA   . LEU A 1 283 ? -29.81000 18.82700 17.54800 1.000 35.53558  ? 283 LEU A HA   1 
ATOM   4436 H  HB2  . LEU A 1 283 ? -29.60800 20.21700 15.10100 1.000 37.24558  ? 283 LEU A HB2  1 
ATOM   4437 H  HB3  . LEU A 1 283 ? -29.02400 20.77500 16.47000 1.000 37.24558  ? 283 LEU A HB3  1 
ATOM   4438 H  HG   . LEU A 1 283 ? -28.04400 18.46900 15.17000 1.000 41.32558  ? 283 LEU A HG   1 
ATOM   4439 H  HD11 . LEU A 1 283 ? -26.17600 19.73000 14.62300 1.000 45.40558  ? 283 LEU A HD11 1 
ATOM   4440 H  HD12 . LEU A 1 283 ? -27.47200 20.41100 14.00700 1.000 45.40558  ? 283 LEU A HD12 1 
ATOM   4441 H  HD13 . LEU A 1 283 ? -26.81700 21.00100 15.32800 1.000 45.40558  ? 283 LEU A HD13 1 
ATOM   4442 H  HD21 . LEU A 1 283 ? -26.26400 18.61700 16.74600 1.000 44.87558  ? 283 LEU A HD21 1 
ATOM   4443 H  HD22 . LEU A 1 283 ? -27.14800 19.66700 17.54700 1.000 44.87558  ? 283 LEU A HD22 1 
ATOM   4444 H  HD23 . LEU A 1 283 ? -27.65300 18.17100 17.37500 1.000 44.87558  ? 283 LEU A HD23 1 
ATOM   4445 N  N    . TYR A 1 284 ? -31.69900 20.12800 18.38400 1.000 29.71168  ? 284 TYR A N    1 
ATOM   4446 C  CA   . TYR A 1 284 ? -32.78900 20.94300 18.89500 1.000 28.75831  ? 284 TYR A CA   1 
ATOM   4447 C  C    . TYR A 1 284 ? -32.22800 22.22200 19.49200 1.000 30.18326  ? 284 TYR A C    1 
ATOM   4448 O  O    . TYR A 1 284 ? -31.28200 22.18100 20.28200 1.000 30.70674  ? 284 TYR A O    1 
ATOM   4449 C  CB   . TYR A 1 284 ? -33.57800 20.17900 19.95300 1.000 30.99785  ? 284 TYR A CB   1 
ATOM   4450 C  CG   . TYR A 1 284 ? -34.37200 19.04000 19.38000 1.000 30.45269  ? 284 TYR A CG   1 
ATOM   4451 C  CD1  . TYR A 1 284 ? -35.42400 19.27600 18.51300 1.000 36.42789  ? 284 TYR A CD1  1 
ATOM   4452 C  CD2  . TYR A 1 284 ? -34.05900 17.72500 19.68600 1.000 33.61941  ? 284 TYR A CD2  1 
ATOM   4453 C  CE1  . TYR A 1 284 ? -36.15000 18.23300 17.97100 1.000 34.53625  ? 284 TYR A CE1  1 
ATOM   4454 C  CE2  . TYR A 1 284 ? -34.78500 16.66900 19.14800 1.000 34.87190  ? 284 TYR A CE2  1 
ATOM   4455 C  CZ   . TYR A 1 284 ? -35.82600 16.93400 18.29100 1.000 33.83050  ? 284 TYR A CZ   1 
ATOM   4456 O  OH   . TYR A 1 284 ? -36.55200 15.89400 17.75500 1.000 36.90988  ? 284 TYR A OH   1 
ATOM   4457 H  H    . TYR A 1 284 ? -31.23800 19.75100 19.00400 1.000 33.07558  ? 284 TYR A H    1 
ATOM   4458 H  HA   . TYR A 1 284 ? -33.38600 21.17900 18.16800 1.000 32.39558  ? 284 TYR A HA   1 
ATOM   4459 H  HB2  . TYR A 1 284 ? -32.96000 19.81500 20.60600 1.000 36.34558  ? 284 TYR A HB2  1 
ATOM   4460 H  HB3  . TYR A 1 284 ? -34.19700 20.78800 20.38600 1.000 36.34558  ? 284 TYR A HB3  1 
ATOM   4461 H  HD1  . TYR A 1 284 ? -35.64600 20.15200 18.29200 1.000 42.08558  ? 284 TYR A HD1  1 
ATOM   4462 H  HD2  . TYR A 1 284 ? -33.35100 17.54600 20.26200 1.000 40.00558  ? 284 TYR A HD2  1 
ATOM   4463 H  HE1  . TYR A 1 284 ? -36.85600 18.40900 17.39200 1.000 39.72558  ? 284 TYR A HE1  1 
ATOM   4464 H  HE2  . TYR A 1 284 ? -34.56700 15.79100 19.36500 1.000 41.43558  ? 284 TYR A HE2  1 
ATOM   4465 H  HH   . TYR A 1 284 ? -36.27600 15.16300 18.06300 1.000 43.11558  ? 284 TYR A HH   1 
ATOM   4466 N  N    . CYS A 1 285 ? -32.82300 23.35400 19.14800 1.000 31.15090  ? 285 CYS A N    1 
ATOM   4467 C  CA   . CYS A 1 285 ? -32.40400 24.63000 19.71700 1.000 28.91768  ? 285 CYS A CA   1 
ATOM   4468 C  C    . CYS A 1 285 ? -33.53100 25.08000 20.63100 1.000 30.53685  ? 285 CYS A C    1 
ATOM   4469 O  O    . CYS A 1 285 ? -34.65000 25.33400 20.17100 1.000 28.92638  ? 285 CYS A O    1 
ATOM   4470 C  CB   . CYS A 1 285 ? -32.08900 25.65100 18.62800 1.000 35.26101  ? 285 CYS A CB   1 
ATOM   4471 S  SG   . CYS A 1 285 ? -31.72800 27.29900 19.26200 1.000 38.11304  ? 285 CYS A SG   1 
ATOM   4472 H  H    . CYS A 1 285 ? -33.47200 23.41000 18.58600 1.000 34.91558  ? 285 CYS A H    1 
ATOM   4473 H  HA   . CYS A 1 285 ? -31.59300 24.52800 20.23900 1.000 32.36558  ? 285 CYS A HA   1 
ATOM   4474 H  HB2  . CYS A 1 285 ? -31.31300 25.34800 18.13200 1.000 38.83558  ? 285 CYS A HB2  1 
ATOM   4475 H  HB3  . CYS A 1 285 ? -32.85400 25.72300 18.03700 1.000 38.83558  ? 285 CYS A HB3  1 
ATOM   4476 H  HG   . CYS A 1 285 ? -32.69500 27.71800 19.83600 1.000 42.37558  ? 285 CYS A HG   1 
ATOM   4477 N  N    . ILE A 1 286 ? -33.26800 25.08400 21.92800 1.000 28.66687  ? 286 ILE A N    1 
ATOM   4478 C  CA   . ILE A 1 286 ? -34.25500 25.46400 22.92700 1.000 26.76634  ? 286 ILE A CA   1 
ATOM   4479 C  C    . ILE A 1 286 ? -33.93000 26.87900 23.38500 1.000 28.93203  ? 286 ILE A C    1 
ATOM   4480 O  O    . ILE A 1 286 ? -32.82800 27.14600 23.86900 1.000 27.20450  ? 286 ILE A O    1 
ATOM   4481 C  CB   . ILE A 1 286 ? -34.25700 24.49100 24.12100 1.000 26.22541  ? 286 ILE A CB   1 
ATOM   4482 C  CG1  . ILE A 1 286 ? -34.58200 23.06800 23.65300 1.000 27.93850  ? 286 ILE A CG1  1 
ATOM   4483 C  CG2  . ILE A 1 286 ? -35.26300 24.95300 25.18300 1.000 26.32441  ? 286 ILE A CG2  1 
ATOM   4484 C  CD1  . ILE A 1 286 ? -34.40000 22.00500 24.71800 1.000 30.26079  ? 286 ILE A CD1  1 
ATOM   4485 H  H    . ILE A 1 286 ? -32.50600 24.86600 22.26200 1.000 33.74558  ? 286 ILE A H    1 
ATOM   4486 H  HA   . ILE A 1 286 ? -35.13800 25.45700 22.52600 1.000 32.15558  ? 286 ILE A HA   1 
ATOM   4487 H  HB   . ILE A 1 286 ? -33.37000 24.48700 24.51400 1.000 32.73558  ? 286 ILE A HB   1 
ATOM   4488 H  HG12 . ILE A 1 286 ? -35.50800 23.04100 23.36700 1.000 35.00558  ? 286 ILE A HG12 1 
ATOM   4489 H  HG13 . ILE A 1 286 ? -33.99800 22.84500 22.91200 1.000 35.00558  ? 286 ILE A HG13 1 
ATOM   4490 H  HG21 . ILE A 1 286 ? -35.32300 24.27700 25.87600 1.000 33.53558  ? 286 ILE A HG21 1 
ATOM   4491 H  HG22 . ILE A 1 286 ? -34.95800 25.79100 25.56300 1.000 33.53558  ? 286 ILE A HG22 1 
ATOM   4492 H  HG23 . ILE A 1 286 ? -36.13000 25.07500 24.76500 1.000 33.53558  ? 286 ILE A HG23 1 
ATOM   4493 H  HD11 . ILE A 1 286 ? -34.46500 21.13000 24.30400 1.000 38.99558  ? 286 ILE A HD11 1 
ATOM   4494 H  HD12 . ILE A 1 286 ? -33.52600 22.11400 25.12600 1.000 38.99558  ? 286 ILE A HD12 1 
ATOM   4495 H  HD13 . ILE A 1 286 ? -35.09300 22.10700 25.38800 1.000 38.99558  ? 286 ILE A HD13 1 
ATOM   4496 N  N    . ASP A 1 287 ? -34.88100 27.78300 23.22000 1.000 27.79110  ? 287 ASP A N    1 
ATOM   4497 C  CA   . ASP A 1 287 ? -34.73900 29.17900 23.60900 1.000 30.52825  ? 287 ASP A CA   1 
ATOM   4498 C  C    . ASP A 1 287 ? -35.86000 29.47400 24.59200 1.000 26.59911  ? 287 ASP A C    1 
ATOM   4499 O  O    . ASP A 1 287 ? -36.91100 29.98200 24.20300 1.000 29.37284  ? 287 ASP A O    1 
ATOM   4500 C  CB   . ASP A 1 287 ? -34.81100 30.08400 22.38200 1.000 33.30481  ? 287 ASP A CB   1 
ATOM   4501 C  CG   . ASP A 1 287 ? -34.50300 31.53300 22.70100 1.000 37.72165  ? 287 ASP A CG   1 
ATOM   4502 O  OD1  . ASP A 1 287 ? -34.19100 31.85000 23.87500 1.000 32.12500  ? 287 ASP A OD1  1 
ATOM   4503 O  OD2  . ASP A 1 287 ? -34.60000 32.35900 21.76500 1.000 37.17684  ? 287 ASP A OD2  1 
ATOM   4504 H  H    . ASP A 1 287 ? -35.64700 27.60600 22.87100 1.000 32.77558  ? 287 ASP A H    1 
ATOM   4505 H  HA   . ASP A 1 287 ? -33.88700 29.32400 24.04800 1.000 35.79558  ? 287 ASP A HA   1 
ATOM   4506 H  HB2  . ASP A 1 287 ? -34.16500 29.77800 21.72600 1.000 37.97558  ? 287 ASP A HB2  1 
ATOM   4507 H  HB3  . ASP A 1 287 ? -35.70600 30.04300 22.01000 1.000 37.97558  ? 287 ASP A HB3  1 
ATOM   4508 N  N    . GLY A 1 288 ? -35.62500 29.17300 25.85500 1.000 26.78819  ? 288 GLY A N    1 
ATOM   4509 C  CA   . GLY A 1 288 ? -36.68700 29.28700 26.84700 1.000 27.49368  ? 288 GLY A CA   1 
ATOM   4510 C  C    . GLY A 1 288 ? -37.82800 28.34400 26.51100 1.000 24.81463  ? 288 GLY A C    1 
ATOM   4511 O  O    . GLY A 1 288 ? -37.67000 27.11700 26.52700 1.000 26.61143  ? 288 GLY A O    1 
ATOM   4512 H  H    . GLY A 1 288 ? -34.86900 28.90300 26.16600 1.000 32.74558  ? 288 GLY A H    1 
ATOM   4513 H  HA2  . GLY A 1 288 ? -36.34300 29.06300 27.72500 1.000 34.13558  ? 288 GLY A HA2  1 
ATOM   4514 H  HA3  . GLY A 1 288 ? -37.02600 30.19600 26.86300 1.000 34.13558  ? 288 GLY A HA3  1 
ATOM   4515 N  N    . ALA A 1 289 ? -38.99200 28.91900 26.22500 1.000 27.42342  ? 289 ALA A N    1 
ATOM   4516 C  CA   . ALA A 1 289 ? -40.17000 28.16100 25.82300 1.000 26.61070  ? 289 ALA A CA   1 
ATOM   4517 C  C    . ALA A 1 289 ? -40.16700 27.77900 24.35000 1.000 29.84896  ? 289 ALA A C    1 
ATOM   4518 O  O    . ALA A 1 289 ? -41.02100 26.98700 23.92700 1.000 31.94616  ? 289 ALA A O    1 
ATOM   4519 C  CB   . ALA A 1 289 ? -41.42700 28.97600 26.11500 1.000 30.13973  ? 289 ALA A CB   1 
ATOM   4520 H  H    . ALA A 1 289 ? -39.12800 29.76700 26.25800 1.000 33.84558  ? 289 ALA A H    1 
ATOM   4521 H  HA   . ALA A 1 289 ? -40.19800 27.34300 26.34300 1.000 33.00558  ? 289 ALA A HA   1 
ATOM   4522 H  HB1  . ALA A 1 289 ? -42.20400 28.46900 25.83300 1.000 36.98558  ? 289 ALA A HB1  1 
ATOM   4523 H  HB2  . ALA A 1 289 ? -41.47400 29.15200 27.06800 1.000 36.98558  ? 289 ALA A HB2  1 
ATOM   4524 H  HB3  . ALA A 1 289 ? -41.38200 29.81200 25.62600 1.000 36.98558  ? 289 ALA A HB3  1 
ATOM   4525 N  N    . LEU A 1 290 ? -39.27400 28.36200 23.55600 1.000 28.37767  ? 290 LEU A N    1 
ATOM   4526 C  CA   . LEU A 1 290 ? -39.27800 28.17800 22.11200 1.000 28.46469  ? 290 LEU A CA   1 
ATOM   4527 C  C    . LEU A 1 290 ? -38.43500 26.97400 21.73300 1.000 30.19606  ? 290 LEU A C    1 
ATOM   4528 O  O    . LEU A 1 290 ? -37.43900 26.66100 22.38800 1.000 30.15519  ? 290 LEU A O    1 
ATOM   4529 C  CB   . LEU A 1 290 ? -38.73400 29.41600 21.39400 1.000 35.54699  ? 290 LEU A CB   1 
ATOM   4530 C  CG   . LEU A 1 290 ? -39.37300 30.74600 21.78800 1.000 49.47739  ? 290 LEU A CG   1 
ATOM   4531 C  CD1  . LEU A 1 290 ? -38.83500 31.87800 20.94100 1.000 53.30320  ? 290 LEU A CD1  1 
ATOM   4532 C  CD2  . LEU A 1 290 ? -40.86200 30.66300 21.63500 1.000 47.33994  ? 290 LEU A CD2  1 
ATOM   4533 H  H    . LEU A 1 290 ? -38.64500 28.87700 23.83600 1.000 33.47558  ? 290 LEU A H    1 
ATOM   4534 H  HA   . LEU A 1 290 ? -40.19100 28.03300 21.81700 1.000 32.62558  ? 290 LEU A HA   1 
ATOM   4535 H  HB2  . LEU A 1 290 ? -37.78500 29.48400 21.58300 1.000 40.06558  ? 290 LEU A HB2  1 
ATOM   4536 H  HB3  . LEU A 1 290 ? -38.87500 29.30000 20.44100 1.000 40.06558  ? 290 LEU A HB3  1 
ATOM   4537 H  HG   . LEU A 1 290 ? -39.15600 30.93400 22.71500 1.000 56.43558  ? 290 LEU A HG   1 
ATOM   4538 H  HD11 . LEU A 1 290 ? -39.25100 32.70800 21.22200 1.000 59.98558  ? 290 LEU A HD11 1 
ATOM   4539 H  HD12 . LEU A 1 290 ? -37.87400 31.93300 21.06100 1.000 59.98558  ? 290 LEU A HD12 1 
ATOM   4540 H  HD13 . LEU A 1 290 ? -39.04200 31.70200 20.01000 1.000 59.98558  ? 290 LEU A HD13 1 
ATOM   4541 H  HD21 . LEU A 1 290 ? -41.23800 31.55300 21.71900 1.000 53.71558  ? 290 LEU A HD21 1 
ATOM   4542 H  HD22 . LEU A 1 290 ? -41.06900 30.29800 20.76100 1.000 53.71558  ? 290 LEU A HD22 1 
ATOM   4543 H  HD23 . LEU A 1 290 ? -41.21900 30.08600 22.32800 1.000 53.71558  ? 290 LEU A HD23 1 
ATOM   4544 N  N    . LEU A 1 291 ? -38.83500 26.30900 20.64400 1.000 28.57628  ? 291 LEU A N    1 
ATOM   4545 C  CA   . LEU A 1 291 ? -38.11600 25.14000 20.16500 1.000 29.73229  ? 291 LEU A CA   1 
ATOM   4546 C  C    . LEU A 1 291 ? -38.06700 25.14100 18.64300 1.000 29.27881  ? 291 LEU A C    1 
ATOM   4547 O  O    . LEU A 1 291 ? -39.09900 25.29600 17.99000 1.000 30.98845  ? 291 LEU A O    1 
ATOM   4548 C  CB   . LEU A 1 291 ? -38.79200 23.86200 20.65900 1.000 33.80121  ? 291 LEU A CB   1 
ATOM   4549 C  CG   . LEU A 1 291 ? -38.23800 22.53200 20.16300 1.000 30.71801  ? 291 LEU A CG   1 
ATOM   4550 C  CD1  . LEU A 1 291 ? -36.85400 22.29900 20.67500 1.000 31.02177  ? 291 LEU A CD1  1 
ATOM   4551 C  CD2  . LEU A 1 291 ? -39.17000 21.39600 20.57200 1.000 33.04883  ? 291 LEU A CD2  1 
ATOM   4552 H  H    . LEU A 1 291 ? -39.52100 26.52000 20.17100 1.000 32.44558  ? 291 LEU A H    1 
ATOM   4553 H  HA   . LEU A 1 291 ? -37.20100 25.17100 20.48700 1.000 33.87558  ? 291 LEU A HA   1 
ATOM   4554 H  HB2  . LEU A 1 291 ? -38.72900 23.84900 21.62700 1.000 39.72558  ? 291 LEU A HB2  1 
ATOM   4555 H  HB3  . LEU A 1 291 ? -39.72300 23.89600 20.38800 1.000 39.72558  ? 291 LEU A HB3  1 
ATOM   4556 H  HG   . LEU A 1 291 ? -38.18400 22.55100 19.19500 1.000 36.06558  ? 291 LEU A HG   1 
ATOM   4557 H  HD11 . LEU A 1 291 ? -36.53100 21.44900 20.33700 1.000 36.80558  ? 291 LEU A HD11 1 
ATOM   4558 H  HD12 . LEU A 1 291 ? -36.27800 23.01700 20.36800 1.000 36.80558  ? 291 LEU A HD12 1 
ATOM   4559 H  HD13 . LEU A 1 291 ? -36.87400 22.28400 21.64500 1.000 36.80558  ? 291 LEU A HD13 1 
ATOM   4560 H  HD21 . LEU A 1 291 ? -38.76600 20.55000 20.32100 1.000 39.79558  ? 291 LEU A HD21 1 
ATOM   4561 H  HD22 . LEU A 1 291 ? -39.30300 21.42700 21.53200 1.000 39.79558  ? 291 LEU A HD22 1 
ATOM   4562 H  HD23 . LEU A 1 291 ? -40.01900 21.50500 20.11700 1.000 39.79558  ? 291 LEU A HD23 1 
ATOM   4563 N  N    . THR A 1 292 ? -36.87500 24.94700 18.09000 1.000 29.72809  ? 292 THR A N    1 
ATOM   4564 C  CA   . THR A 1 292 ? -36.68500 24.72400 16.66000 1.000 31.49195  ? 292 THR A CA   1 
ATOM   4565 C  C    . THR A 1 292 ? -35.73000 23.54900 16.48500 1.000 32.78223  ? 292 THR A C    1 
ATOM   4566 O  O    . THR A 1 292 ? -35.03900 23.15000 17.42100 1.000 32.51647  ? 292 THR A O    1 
ATOM   4567 C  CB   . THR A 1 292 ? -36.12400 25.96100 15.94300 1.000 34.93782  ? 292 THR A CB   1 
ATOM   4568 O  OG1  . THR A 1 292 ? -34.86400 26.33100 16.52900 1.000 35.44108  ? 292 THR A OG1  1 
ATOM   4569 C  CG2  . THR A 1 292 ? -37.07800 27.12400 16.05200 1.000 40.44932  ? 292 THR A CG2  1 
ATOM   4570 H  H    . THR A 1 292 ? -36.14000 24.93900 18.53500 1.000 32.12558  ? 292 THR A H    1 
ATOM   4571 H  HA   . THR A 1 292 ? -37.53700 24.51400 16.24700 1.000 33.03558  ? 292 THR A HA   1 
ATOM   4572 H  HB   . THR A 1 292 ? -36.00000 25.75500 15.00300 1.000 36.17558  ? 292 THR A HB   1 
ATOM   4573 H  HG1  . THR A 1 292 ? -34.57800 27.03700 16.17500 1.000 37.18558  ? 292 THR A HG1  1 
ATOM   4574 H  HG21 . THR A 1 292 ? -36.72800 27.88700 15.56400 1.000 42.55558  ? 292 THR A HG21 1 
ATOM   4575 H  HG22 . THR A 1 292 ? -37.94000 26.88200 15.68000 1.000 42.55558  ? 292 THR A HG22 1 
ATOM   4576 H  HG23 . THR A 1 292 ? -37.19400 27.37200 16.98200 1.000 42.55558  ? 292 THR A HG23 1 
ATOM   4577 N  N    . LYS A 1 293 ? -35.69100 22.99200 15.27100 1.000 35.61243  ? 293 LYS A N    1 
ATOM   4578 C  CA   . LYS A 1 293 ? -34.80500 21.87200 14.99000 1.000 34.95606  ? 293 LYS A CA   1 
ATOM   4579 C  C    . LYS A 1 293 ? -34.04800 22.11500 13.68800 1.000 38.11736  ? 293 LYS A C    1 
ATOM   4580 O  O    . LYS A 1 293 ? -34.48500 22.87800 12.82000 1.000 37.89349  ? 293 LYS A O    1 
ATOM   4581 C  CB   . LYS A 1 293 ? -35.59600 20.55400 14.90700 1.000 34.81042  ? 293 LYS A CB   1 
ATOM   4582 C  CG   . LYS A 1 293 ? -36.31500 20.36200 13.59000 1.000 38.70813  ? 293 LYS A CG   1 
ATOM   4583 C  CD   . LYS A 1 293 ? -37.10900 19.05800 13.56000 1.000 51.26107  ? 293 LYS A CD   1 
ATOM   4584 C  CE   . LYS A 1 293 ? -37.66900 18.80500 12.16600 1.000 56.88658  ? 293 LYS A CE   1 
ATOM   4585 N  NZ   . LYS A 1 293 ? -38.14600 17.40000 11.99800 1.000 71.38227  ? 293 LYS A NZ   1 
ATOM   4586 H  H    . LYS A 1 293 ? -36.16800 23.24800 14.60300 1.000 37.07558  ? 293 LYS A H    1 
ATOM   4587 H  HA   . LYS A 1 293 ? -34.14700 21.79600 15.69800 1.000 36.18558  ? 293 LYS A HA   1 
ATOM   4588 H  HB2  . LYS A 1 293 ? -34.98100 19.81200 15.02000 1.000 36.29558  ? 293 LYS A HB2  1 
ATOM   4589 H  HB3  . LYS A 1 293 ? -36.26100 20.54300 15.61300 1.000 36.29558  ? 293 LYS A HB3  1 
ATOM   4590 H  HG2  . LYS A 1 293 ? -36.93300 21.09700 13.45300 1.000 39.76558  ? 293 LYS A HG2  1 
ATOM   4591 H  HG3  . LYS A 1 293 ? -35.66400 20.33800 12.87100 1.000 39.76558  ? 293 LYS A HG3  1 
ATOM   4592 H  HD2  . LYS A 1 293 ? -36.52900 18.31800 13.79800 1.000 55.19558  ? 293 LYS A HD2  1 
ATOM   4593 H  HD3  . LYS A 1 293 ? -37.84900 19.11300 14.18500 1.000 55.19558  ? 293 LYS A HD3  1 
ATOM   4594 H  HE2  . LYS A 1 293 ? -38.41900 19.40000 12.01200 1.000 60.56558  ? 293 LYS A HE2  1 
ATOM   4595 H  HE3  . LYS A 1 293 ? -36.97500 18.97000 11.50900 1.000 60.56558  ? 293 LYS A HE3  1 
ATOM   4596 H  HZ1  . LYS A 1 293 ? -37.47000 16.83300 12.11400 1.000 78.15558  ? 293 LYS A HZ1  1 
ATOM   4597 H  HZ2  . LYS A 1 293 ? -38.78100 17.22000 12.59500 1.000 78.15558  ? 293 LYS A HZ2  1 
ATOM   4598 H  HZ3  . LYS A 1 293 ? -38.48000 17.28800 11.18000 1.000 78.15558  ? 293 LYS A HZ3  1 
ATOM   4599 N  N    . SER A 1 294 ? -32.90600 21.44600 13.55000 1.000 40.71843  ? 294 SER A N    1 
ATOM   4600 C  CA   . SER A 1 294 ? -32.15100 21.52300 12.29500 1.000 41.38552  ? 294 SER A CA   1 
ATOM   4601 C  C    . SER A 1 294 ? -31.19000 20.34800 12.21700 1.000 41.16470  ? 294 SER A C    1 
ATOM   4602 O  O    . SER A 1 294 ? -30.86700 19.72600 13.22900 1.000 42.29553  ? 294 SER A O    1 
ATOM   4603 C  CB   . SER A 1 294 ? -31.39300 22.84400 12.18500 1.000 45.20747  ? 294 SER A CB   1 
ATOM   4604 O  OG   . SER A 1 294 ? -30.44100 22.94900 13.22700 1.000 44.09870  ? 294 SER A OG   1 
ATOM   4605 H  H    . SER A 1 294 ? -32.55100 20.94900 14.15500 1.000 41.54558  ? 294 SER A H    1 
ATOM   4606 H  HA   . SER A 1 294 ? -32.76600 21.45500 11.54800 1.000 40.98558  ? 294 SER A HA   1 
ATOM   4607 H  HB2  . SER A 1 294 ? -30.93500 22.87800 11.33000 1.000 45.27558  ? 294 SER A HB2  1 
ATOM   4608 H  HB3  . SER A 1 294 ? -32.02200 23.57900 12.25400 1.000 45.27558  ? 294 SER A HB3  1 
ATOM   4609 H  HG   . SER A 1 294 ? -30.04800 23.69000 13.18300 1.000 44.90558  ? 294 SER A HG   1 
ATOM   4610 N  N    . SER A 1 295 ? -30.76100 20.02800 10.99000 1.000 43.32308  ? 295 SER A N    1 
ATOM   4611 C  CA   . SER A 1 295 ? -29.80100 18.93800 10.82800 1.000 45.94515  ? 295 SER A CA   1 
ATOM   4612 C  C    . SER A 1 295 ? -28.37400 19.41800 11.05800 1.000 49.31903  ? 295 SER A C    1 
ATOM   4613 O  O    . SER A 1 295 ? -27.52300 18.63700 11.49600 1.000 52.36201  ? 295 SER A O    1 
ATOM   4614 C  CB   . SER A 1 295 ? -29.93700 18.31400 9.43800  1.000 54.09904  ? 295 SER A CB   1 
ATOM   4615 O  OG   . SER A 1 295 ? -29.91900 19.31300 8.44500  1.000 61.31332  ? 295 SER A OG   1 
ATOM   4616 H  H    . SER A 1 295 ? -31.00400 20.41500 10.26100 1.000 41.88558  ? 295 SER A H    1 
ATOM   4617 H  HA   . SER A 1 295 ? -29.99600 18.24300 11.47600 1.000 44.74558  ? 295 SER A HA   1 
ATOM   4618 H  HB2  . SER A 1 295 ? -29.19500 17.70600 9.28900  1.000 52.99558  ? 295 SER A HB2  1 
ATOM   4619 H  HB3  . SER A 1 295 ? -30.77700 17.83100 9.38700  1.000 52.99558  ? 295 SER A HB3  1 
ATOM   4620 H  HG   . SER A 1 295 ? -29.20000 19.74600 8.48600  1.000 60.54558  ? 295 SER A HG   1 
ATOM   4621 N  N    . GLU A 1 296 ? -28.10700 20.69600 10.79200 1.000 46.89336  ? 296 GLU A N    1 
ATOM   4622 C  CA   . GLU A 1 296 ? -26.82200 21.32700 11.06800 1.000 49.71328  ? 296 GLU A CA   1 
ATOM   4623 C  C    . GLU A 1 296 ? -27.04800 22.58000 11.90400 1.000 47.83196  ? 296 GLU A C    1 
ATOM   4624 O  O    . GLU A 1 296 ? -28.14700 23.14200 11.93700 1.000 47.75211  ? 296 GLU A O    1 
ATOM   4625 C  CB   . GLU A 1 296 ? -26.08800 21.69800 9.76400  1.000 62.63393  ? 296 GLU A CB   1 
ATOM   4626 C  CG   . GLU A 1 296 ? -25.14000 20.61900 9.24500  1.000 81.69119  ? 296 GLU A CG   1 
ATOM   4627 C  CD   . GLU A 1 296 ? -25.84300 19.53900 8.44100  1.000 93.97444  ? 296 GLU A CD   1 
ATOM   4628 O  OE1  . GLU A 1 296 ? -27.05000 19.69300 8.15100  1.000 104.72631 ? 296 GLU A OE1  1 
ATOM   4629 O  OE2  . GLU A 1 296 ? -25.18300 18.53100 8.09500  1.000 103.40958 ? 296 GLU A OE2  1 
ATOM   4630 H  H    . GLU A 1 296 ? -28.67500 21.23600 10.43800 1.000 45.63558  ? 296 GLU A H    1 
ATOM   4631 H  HA   . GLU A 1 296 ? -26.26200 20.71700 11.57300 1.000 49.19558  ? 296 GLU A HA   1 
ATOM   4632 H  HB2  . GLU A 1 296 ? -26.74900 21.86400 9.07300  1.000 63.31558  ? 296 GLU A HB2  1 
ATOM   4633 H  HB3  . GLU A 1 296 ? -25.56300 22.49800 9.92100  1.000 63.31558  ? 296 GLU A HB3  1 
ATOM   4634 H  HG2  . GLU A 1 296 ? -24.47700 21.03300 8.67200  1.000 85.42558  ? 296 GLU A HG2  1 
ATOM   4635 H  HG3  . GLU A 1 296 ? -24.70600 20.19300 10.00100 1.000 85.42558  ? 296 GLU A HG3  1 
ATOM   4636 N  N    . TYR A 1 297 ? -25.99500 23.03000 12.58000 1.000 48.09171  ? 297 TYR A N    1 
ATOM   4637 C  CA   . TYR A 1 297 ? -26.11100 24.23400 13.39300 1.000 42.07320  ? 297 TYR A CA   1 
ATOM   4638 C  C    . TYR A 1 297 ? -24.79300 24.98600 13.38600 1.000 48.77011  ? 297 TYR A C    1 
ATOM   4639 O  O    . TYR A 1 297 ? -23.72800 24.39400 13.59200 1.000 45.90282  ? 297 TYR A O    1 
ATOM   4640 C  CB   . TYR A 1 297 ? -26.52100 23.92200 14.83400 1.000 43.14304  ? 297 TYR A CB   1 
ATOM   4641 C  CG   . TYR A 1 297 ? -27.08200 25.13400 15.54700 1.000 37.61315  ? 297 TYR A CG   1 
ATOM   4642 C  CD1  . TYR A 1 297 ? -26.24000 26.07400 16.14700 1.000 40.73434  ? 297 TYR A CD1  1 
ATOM   4643 C  CD2  . TYR A 1 297 ? -28.44700 25.36700 15.57500 1.000 51.34040  ? 297 TYR A CD2  1 
ATOM   4644 C  CE1  . TYR A 1 297 ? -26.75000 27.19900 16.77100 1.000 38.51608  ? 297 TYR A CE1  1 
ATOM   4645 C  CE2  . TYR A 1 297 ? -28.97000 26.48300 16.19700 1.000 48.19141  ? 297 TYR A CE2  1 
ATOM   4646 C  CZ   . TYR A 1 297 ? -28.12100 27.39700 16.79700 1.000 48.25536  ? 297 TYR A CZ   1 
ATOM   4647 O  OH   . TYR A 1 297 ? -28.67200 28.50200 17.41200 1.000 44.11908  ? 297 TYR A OH   1 
ATOM   4648 H  H    . TYR A 1 297 ? -25.21800 22.66200 12.58400 1.000 48.75558  ? 297 TYR A H    1 
ATOM   4649 H  HA   . TYR A 1 297 ? -26.79200 24.80000 12.99600 1.000 42.34558  ? 297 TYR A HA   1 
ATOM   4650 H  HB2  . TYR A 1 297 ? -27.20400 23.23300 14.82800 1.000 44.96558  ? 297 TYR A HB2  1 
ATOM   4651 H  HB3  . TYR A 1 297 ? -25.74400 23.61400 15.32600 1.000 44.96558  ? 297 TYR A HB3  1 
ATOM   4652 H  HD1  . TYR A 1 297 ? -25.32000 25.94100 16.12800 1.000 43.13558  ? 297 TYR A HD1  1 
ATOM   4653 H  HD2  . TYR A 1 297 ? -29.02200 24.76000 15.16700 1.000 55.46558  ? 297 TYR A HD2  1 
ATOM   4654 H  HE1  . TYR A 1 297 ? -26.17800 27.81600 17.16800 1.000 40.92558  ? 297 TYR A HE1  1 
ATOM   4655 H  HE2  . TYR A 1 297 ? -29.89000 26.61900 16.21300 1.000 52.12558  ? 297 TYR A HE2  1 
ATOM   4656 H  HH   . TYR A 1 297 ? -28.07500 29.07300 17.56600 1.000 47.98558  ? 297 TYR A HH   1 
ATOM   4657 N  N    . LYS A 1 298 ? -24.88100 26.29000 13.15400 1.000 43.19299  ? 298 LYS A N    1 
ATOM   4658 C  CA   . LYS A 1 298 ? -23.73400 27.18100 13.22500 1.000 41.30044  ? 298 LYS A CA   1 
ATOM   4659 C  C    . LYS A 1 298 ? -24.18400 28.45300 13.92300 1.000 45.63522  ? 298 LYS A C    1 
ATOM   4660 O  O    . LYS A 1 298 ? -25.24700 28.99500 13.61100 1.000 45.17852  ? 298 LYS A O    1 
ATOM   4661 C  CB   . LYS A 1 298 ? -23.18700 27.47600 11.82600 1.000 44.82211  ? 298 LYS A CB   1 
ATOM   4662 C  CG   . LYS A 1 298 ? -21.89600 28.28600 11.78600 1.000 76.37670  ? 298 LYS A CG   1 
ATOM   4663 C  CD   . LYS A 1 298 ? -21.27900 28.27700 10.36300 1.000 75.26311  ? 298 LYS A CD   1 
ATOM   4664 C  CE   . LYS A 1 298 ? -20.42600 29.51900 10.02800 1.000 79.27200  ? 298 LYS A CE   1 
ATOM   4665 N  NZ   . LYS A 1 298 ? -20.76100 30.76600 10.78200 1.000 87.43226  ? 298 LYS A NZ   1 
ATOM   4666 H  H    . LYS A 1 298 ? -25.61400 26.69100 12.94800 1.000 43.50558  ? 298 LYS A H    1 
ATOM   4667 H  HA   . LYS A 1 298 ? -23.01400 26.78600 13.74000 1.000 41.35558  ? 298 LYS A HA   1 
ATOM   4668 H  HB2  . LYS A 1 298 ? -23.01200 26.63100 11.38200 1.000 44.40558  ? 298 LYS A HB2  1 
ATOM   4669 H  HB3  . LYS A 1 298 ? -23.85700 27.97600 11.33400 1.000 44.40558  ? 298 LYS A HB3  1 
ATOM   4670 H  HG2  . LYS A 1 298 ? -22.08300 29.20500 12.03400 1.000 82.38558  ? 298 LYS A HG2  1 
ATOM   4671 H  HG3  . LYS A 1 298 ? -21.25300 27.90000 12.40200 1.000 82.38558  ? 298 LYS A HG3  1 
ATOM   4672 H  HD2  . LYS A 1 298 ? -20.70700 27.49800 10.27800 1.000 79.84558  ? 298 LYS A HD2  1 
ATOM   4673 H  HD3  . LYS A 1 298 ? -21.99800 28.23300 9.71300  1.000 79.84558  ? 298 LYS A HD3  1 
ATOM   4674 H  HE2  . LYS A 1 298 ? -19.49800 29.31000 10.21900 1.000 84.64558  ? 298 LYS A HE2  1 
ATOM   4675 H  HE3  . LYS A 1 298 ? -20.53400 29.71700 9.08500  1.000 84.64558  ? 298 LYS A HE3  1 
ATOM   4676 H  HZ1  . LYS A 1 298 ? -20.20500 31.42000 10.55000 1.000 95.27558  ? 298 LYS A HZ1  1 
ATOM   4677 H  HZ2  . LYS A 1 298 ? -21.59500 31.01700 10.59800 1.000 95.27558  ? 298 LYS A HZ2  1 
ATOM   4678 H  HZ3  . LYS A 1 298 ? -20.68900 30.62100 11.65700 1.000 95.27558  ? 298 LYS A HZ3  1 
ATOM   4679 N  N    . GLY A 1 299 ? -23.39900 28.90400 14.88700 1.000 43.13148  ? 299 GLY A N    1 
ATOM   4680 C  CA   . GLY A 1 299 ? -23.72900 30.09500 15.62800 1.000 42.26465  ? 299 GLY A CA   1 
ATOM   4681 C  C    . GLY A 1 299 ? -22.60000 30.49000 16.55200 1.000 37.44746  ? 299 GLY A C    1 
ATOM   4682 O  O    . GLY A 1 299 ? -21.54900 29.84300 16.58800 1.000 37.66607  ? 299 GLY A O    1 
ATOM   4683 H  H    . GLY A 1 299 ? -22.66300 28.53100 15.13000 1.000 45.02558  ? 299 GLY A H    1 
ATOM   4684 H  HA2  . GLY A 1 299 ? -23.89800 30.82600 15.01300 1.000 44.57558  ? 299 GLY A HA2  1 
ATOM   4685 H  HA3  . GLY A 1 299 ? -24.52500 29.93900 16.15900 1.000 44.57558  ? 299 GLY A HA3  1 
ATOM   4686 N  N    . PRO A 1 300 ? -22.78300 31.58900 17.29500 1.000 36.66263  ? 300 PRO A N    1 
ATOM   4687 C  CA   . PRO A 1 300 ? -21.75400 32.07100 18.24700 1.000 35.06597  ? 300 PRO A CA   1 
ATOM   4688 C  C    . PRO A 1 300 ? -21.76900 31.27600 19.54800 1.000 34.60826  ? 300 PRO A C    1 
ATOM   4689 O  O    . PRO A 1 300 ? -22.33800 31.65600 20.57400 1.000 35.41329  ? 300 PRO A O    1 
ATOM   4690 C  CB   . PRO A 1 300 ? -22.14700 33.53500 18.45800 1.000 42.12705  ? 300 PRO A CB   1 
ATOM   4691 C  CG   . PRO A 1 300 ? -23.61400 33.56800 18.24500 1.000 37.69111  ? 300 PRO A CG   1 
ATOM   4692 C  CD   . PRO A 1 300 ? -23.93300 32.51200 17.21300 1.000 42.44631  ? 300 PRO A CD   1 
ATOM   4693 H  HA   . PRO A 1 300 ? -20.87000 32.03900 17.84800 1.000 37.98558  ? 300 PRO A HA   1 
ATOM   4694 H  HB2  . PRO A 1 300 ? -21.92000 33.81200 19.35900 1.000 46.54558  ? 300 PRO A HB2  1 
ATOM   4695 H  HB3  . PRO A 1 300 ? -21.68900 34.09700 17.81300 1.000 46.54558  ? 300 PRO A HB3  1 
ATOM   4696 H  HG2  . PRO A 1 300 ? -24.06600 33.37300 19.08100 1.000 40.87558  ? 300 PRO A HG2  1 
ATOM   4697 H  HG3  . PRO A 1 300 ? -23.87400 34.44500 17.92400 1.000 40.87558  ? 300 PRO A HG3  1 
ATOM   4698 H  HD2  . PRO A 1 300 ? -24.75800 32.05300 17.43400 1.000 45.89558  ? 300 PRO A HD2  1 
ATOM   4699 H  HD3  . PRO A 1 300 ? -23.99800 32.90300 16.32800 1.000 45.89558  ? 300 PRO A HD3  1 
ATOM   4700 N  N    . ILE A 1 301 ? -21.10300 30.13900 19.51100 1.000 32.59166  ? 301 ILE A N    1 
ATOM   4701 C  CA   . ILE A 1 301 ? -21.11100 29.21000 20.63400 1.000 29.70240  ? 301 ILE A CA   1 
ATOM   4702 C  C    . ILE A 1 301 ? -20.09200 29.65700 21.67000 1.000 31.13540  ? 301 ILE A C    1 
ATOM   4703 O  O    . ILE A 1 301 ? -18.99200 30.11500 21.33400 1.000 30.26592  ? 301 ILE A O    1 
ATOM   4704 C  CB   . ILE A 1 301 ? -20.82100 27.78800 20.12200 1.000 32.96959  ? 301 ILE A CB   1 
ATOM   4705 C  CG1  . ILE A 1 301 ? -21.80300 27.42300 19.00600 1.000 34.77283  ? 301 ILE A CG1  1 
ATOM   4706 C  CG2  . ILE A 1 301 ? -20.88700 26.77400 21.26900 1.000 34.49806  ? 301 ILE A CG2  1 
ATOM   4707 C  CD1  . ILE A 1 301 ? -23.26900 27.71800 19.32900 1.000 35.94197  ? 301 ILE A CD1  1 
ATOM   4708 H  H    . ILE A 1 301 ? -20.63200 29.87400 18.84200 1.000 35.89558  ? 301 ILE A H    1 
ATOM   4709 H  HA   . ILE A 1 301 ? -21.98200 29.21500 21.06000 1.000 33.17558  ? 301 ILE A HA   1 
ATOM   4710 H  HB   . ILE A 1 301 ? -19.92200 27.76600 19.75900 1.000 36.77558  ? 301 ILE A HB   1 
ATOM   4711 H  HG12 . ILE A 1 301 ? -21.57000 27.92900 18.21200 1.000 38.14558  ? 301 ILE A HG12 1 
ATOM   4712 H  HG13 . ILE A 1 301 ? -21.72800 26.47300 18.82700 1.000 38.14558  ? 301 ILE A HG13 1 
ATOM   4713 H  HG21 . ILE A 1 301 ? -20.83100 25.87800 20.90100 1.000 39.42558  ? 301 ILE A HG21 1 
ATOM   4714 H  HG22 . ILE A 1 301 ? -20.14400 26.93100 21.87200 1.000 39.42558  ? 301 ILE A HG22 1 
ATOM   4715 H  HG23 . ILE A 1 301 ? -21.72700 26.88600 21.74100 1.000 39.42558  ? 301 ILE A HG23 1 
ATOM   4716 H  HD11 . ILE A 1 301 ? -23.83200 27.26600 18.68100 1.000 39.78558  ? 301 ILE A HD11 1 
ATOM   4717 H  HD12 . ILE A 1 301 ? -23.46700 27.39600 20.22200 1.000 39.78558  ? 301 ILE A HD12 1 
ATOM   4718 H  HD13 . ILE A 1 301 ? -23.41500 28.67600 19.28300 1.000 39.78558  ? 301 ILE A HD13 1 
ATOM   4719 N  N    . THR A 1 302 ? -20.46100 29.51700 22.95000 1.000 28.07290  ? 302 THR A N    1 
ATOM   4720 C  CA   . THR A 1 302 ? -19.58400 29.85800 24.06000 1.000 33.18478  ? 302 THR A CA   1 
ATOM   4721 C  C    . THR A 1 302 ? -19.23200 28.67600 24.96200 1.000 26.46533  ? 302 THR A C    1 
ATOM   4722 O  O    . THR A 1 302 ? -18.18900 28.72500 25.62000 1.000 27.88015  ? 302 THR A O    1 
ATOM   4723 C  CB   . THR A 1 302 ? -20.21500 30.96700 24.92900 1.000 36.02536  ? 302 THR A CB   1 
ATOM   4724 O  OG1  . THR A 1 302 ? -21.45500 30.51000 25.47900 1.000 30.27833  ? 302 THR A OG1  1 
ATOM   4725 C  CG2  . THR A 1 302 ? -20.51100 32.18700 24.11900 1.000 43.06615  ? 302 THR A CG2  1 
ATOM   4726 H  H    . THR A 1 302 ? -21.22900 29.22100 23.19700 1.000 32.69558  ? 302 THR A H    1 
ATOM   4727 H  HA   . THR A 1 302 ? -18.75400 30.20500 23.69600 1.000 39.48558  ? 302 THR A HA   1 
ATOM   4728 H  HB   . THR A 1 302 ? -19.58800 31.19300 25.63400 1.000 43.27558  ? 302 THR A HB   1 
ATOM   4729 H  HG1  . THR A 1 302 ? -21.32700 29.82400 25.94500 1.000 36.65558  ? 302 THR A HG1  1 
ATOM   4730 H  HG21 . THR A 1 302 ? -20.88300 32.88000 24.68700 1.000 51.17558  ? 302 THR A HG21 1 
ATOM   4731 H  HG22 . THR A 1 302 ? -19.69600 32.51900 23.71100 1.000 51.17558  ? 302 THR A HG22 1 
ATOM   4732 H  HG23 . THR A 1 302 ? -21.14900 31.97500 23.42100 1.000 51.17558  ? 302 THR A HG23 1 
ATOM   4733 N  N    . ASP A 1 303 ? -20.05500 27.63200 25.01900 1.000 26.12896  ? 303 ASP A N    1 
ATOM   4734 C  CA   . ASP A 1 303 ? -19.79000 26.50500 25.90400 1.000 27.84426  ? 303 ASP A CA   1 
ATOM   4735 C  C    . ASP A 1 303 ? -20.31400 25.24800 25.23500 1.000 29.69869  ? 303 ASP A C    1 
ATOM   4736 O  O    . ASP A 1 303 ? -21.42100 25.27100 24.68900 1.000 29.00774  ? 303 ASP A O    1 
ATOM   4737 C  CB   . ASP A 1 303 ? -20.51000 26.67100 27.24500 1.000 29.60808  ? 303 ASP A CB   1 
ATOM   4738 C  CG   . ASP A 1 303 ? -20.19900 27.99800 27.91700 1.000 30.65513  ? 303 ASP A CG   1 
ATOM   4739 O  OD1  . ASP A 1 303 ? -19.10000 28.12300 28.51300 1.000 30.11539  ? 303 ASP A OD1  1 
ATOM   4740 O  OD2  . ASP A 1 303 ? -21.05400 28.92100 27.82300 1.000 32.62053  ? 303 ASP A OD2  1 
ATOM   4741 H  H    . ASP A 1 303 ? -20.77400 27.55400 24.55400 1.000 31.71558  ? 303 ASP A H    1 
ATOM   4742 H  HA   . ASP A 1 303 ? -18.83600 26.42900 26.05900 1.000 34.38558  ? 303 ASP A HA   1 
ATOM   4743 H  HB2  . ASP A 1 303 ? -21.46700 26.62500 27.09800 1.000 37.30558  ? 303 ASP A HB2  1 
ATOM   4744 H  HB3  . ASP A 1 303 ? -20.23200 25.95900 27.84300 1.000 37.30558  ? 303 ASP A HB3  1 
ATOM   4745 N  N    . VAL A 1 304 ? -19.55600 24.15200 25.31900 1.000 28.77901  ? 304 VAL A N    1 
ATOM   4746 C  CA   . VAL A 1 304 ? -19.97600 22.86000 24.79300 1.000 25.14113  ? 304 VAL A CA   1 
ATOM   4747 C  C    . VAL A 1 304 ? -19.67900 21.77000 25.82100 1.000 25.10895  ? 304 VAL A C    1 
ATOM   4748 O  O    . VAL A 1 304 ? -18.56400 21.69600 26.35100 1.000 27.07482  ? 304 VAL A O    1 
ATOM   4749 C  CB   . VAL A 1 304 ? -19.26900 22.52100 23.45900 1.000 26.79103  ? 304 VAL A CB   1 
ATOM   4750 C  CG1  . VAL A 1 304 ? -19.82800 21.22100 22.88600 1.000 29.95985  ? 304 VAL A CG1  1 
ATOM   4751 C  CG2  . VAL A 1 304 ? -19.42300 23.65500 22.45500 1.000 30.99765  ? 304 VAL A CG2  1 
ATOM   4752 H  H    . VAL A 1 304 ? -18.77800 24.13600 25.68500 1.000 35.29558  ? 304 VAL A H    1 
ATOM   4753 H  HA   . VAL A 1 304 ? -20.93400 22.89100 24.64900 1.000 30.70558  ? 304 VAL A HA   1 
ATOM   4754 H  HB   . VAL A 1 304 ? -18.32100 22.40400 23.62900 1.000 31.67558  ? 304 VAL A HB   1 
ATOM   4755 H  HG11 . VAL A 1 304 ? -19.48100 21.09600 21.98900 1.000 35.15558  ? 304 VAL A HG11 1 
ATOM   4756 H  HG12 . VAL A 1 304 ? -19.55300 20.48300 23.45300 1.000 35.15558  ? 304 VAL A HG12 1 
ATOM   4757 H  HG13 . VAL A 1 304 ? -20.79600 21.27700 22.86200 1.000 35.15558  ? 304 VAL A HG13 1 
ATOM   4758 H  HG21 . VAL A 1 304 ? -19.02400 23.38800 21.61200 1.000 36.00558  ? 304 VAL A HG21 1 
ATOM   4759 H  HG22 . VAL A 1 304 ? -20.36800 23.83900 22.32900 1.000 36.00558  ? 304 VAL A HG22 1 
ATOM   4760 H  HG23 . VAL A 1 304 ? -18.97600 24.44400 22.79800 1.000 36.00558  ? 304 VAL A HG23 1 
ATOM   4761 N  N    . PHE A 1 305 ? -20.64500 20.88900 26.03200 1.000 25.90856  ? 305 PHE A N    1 
ATOM   4762 C  CA   . PHE A 1 305 ? -20.55400 19.78200 26.97000 1.000 24.84999  ? 305 PHE A CA   1 
ATOM   4763 C  C    . PHE A 1 305 ? -20.46000 18.47500 26.20500 1.000 27.75246  ? 305 PHE A C    1 
ATOM   4764 O  O    . PHE A 1 305 ? -21.14900 18.28700 25.19800 1.000 26.71045  ? 305 PHE A O    1 
ATOM   4765 C  CB   . PHE A 1 305 ? -21.77300 19.75900 27.89100 1.000 24.25342  ? 305 PHE A CB   1 
ATOM   4766 C  CG   . PHE A 1 305 ? -21.84200 20.94500 28.80200 1.000 23.00278  ? 305 PHE A CG   1 
ATOM   4767 C  CD1  . PHE A 1 305 ? -22.32000 22.16000 28.33400 1.000 27.08728  ? 305 PHE A CD1  1 
ATOM   4768 C  CD2  . PHE A 1 305 ? -21.39400 20.86000 30.10300 1.000 27.51747  ? 305 PHE A CD2  1 
ATOM   4769 C  CE1  . PHE A 1 305 ? -22.36600 23.26100 29.13700 1.000 30.37877  ? 305 PHE A CE1  1 
ATOM   4770 C  CE2  . PHE A 1 305 ? -21.43900 21.97600 30.92400 1.000 27.02151  ? 305 PHE A CE2  1 
ATOM   4771 C  CZ   . PHE A 1 305 ? -21.91800 23.16900 30.43900 1.000 24.21352  ? 305 PHE A CZ   1 
ATOM   4772 H  H    . PHE A 1 305 ? -21.40100 20.91400 25.62300 1.000 32.75558  ? 305 PHE A H    1 
ATOM   4773 H  HA   . PHE A 1 305 ? -19.75700 19.87400 27.51600 1.000 32.23558  ? 305 PHE A HA   1 
ATOM   4774 H  HB2  . PHE A 1 305 ? -22.57700 19.75100 27.34800 1.000 32.42558  ? 305 PHE A HB2  1 
ATOM   4775 H  HB3  . PHE A 1 305 ? -21.73700 18.96100 28.44200 1.000 32.42558  ? 305 PHE A HB3  1 
ATOM   4776 H  HD1  . PHE A 1 305 ? -22.61500 22.22600 27.45500 1.000 35.82558  ? 305 PHE A HD1  1 
ATOM   4777 H  HD2  . PHE A 1 305 ? -21.06200 20.05500 30.43000 1.000 37.53558  ? 305 PHE A HD2  1 
ATOM   4778 H  HE1  . PHE A 1 305 ? -22.69600 24.06700 28.81000 1.000 40.07558  ? 305 PHE A HE1  1 
ATOM   4779 H  HE2  . PHE A 1 305 ? -21.14500 21.91800 31.80500 1.000 37.22558  ? 305 PHE A HE2  1 
ATOM   4780 H  HZ   . PHE A 1 305 ? -21.94100 23.91700 30.99100 1.000 33.40558  ? 305 PHE A HZ   1 
ATOM   4781 N  N    . TYR A 1 306 ? -19.59400 17.58800 26.68500 1.000 26.54195  ? 306 TYR A N    1 
ATOM   4782 C  CA   . TYR A 1 306 ? -19.31800 16.30100 26.06600 1.000 26.80554  ? 306 TYR A CA   1 
ATOM   4783 C  C    . TYR A 1 306 ? -19.40800 15.20700 27.11700 1.000 31.31756  ? 306 TYR A C    1 
ATOM   4784 O  O    . TYR A 1 306 ? -19.05400 15.41900 28.27700 1.000 28.18541  ? 306 TYR A O    1 
ATOM   4785 C  CB   . TYR A 1 306 ? -17.91600 16.24100 25.46800 1.000 28.15066  ? 306 TYR A CB   1 
ATOM   4786 C  CG   . TYR A 1 306 ? -17.62600 17.27600 24.43600 1.000 26.56523  ? 306 TYR A CG   1 
ATOM   4787 C  CD1  . TYR A 1 306 ? -17.19700 18.54100 24.78700 1.000 27.72790  ? 306 TYR A CD1  1 
ATOM   4788 C  CD2  . TYR A 1 306 ? -17.75100 16.97600 23.09600 1.000 31.42547  ? 306 TYR A CD2  1 
ATOM   4789 C  CE1  . TYR A 1 306 ? -16.92800 19.48600 23.84400 1.000 29.22383  ? 306 TYR A CE1  1 
ATOM   4790 C  CE2  . TYR A 1 306 ? -17.47800 17.90100 22.13800 1.000 35.24688  ? 306 TYR A CE2  1 
ATOM   4791 C  CZ   . TYR A 1 306 ? -17.06300 19.15500 22.49800 1.000 32.93970  ? 306 TYR A CZ   1 
ATOM   4792 O  OH   . TYR A 1 306 ? -16.78100 20.07100 21.52000 1.000 32.32581  ? 306 TYR A OH   1 
ATOM   4793 H  H    . TYR A 1 306 ? -19.13400 17.71700 27.40000 1.000 34.03558  ? 306 TYR A H    1 
ATOM   4794 H  HA   . TYR A 1 306 ? -19.97300 16.15100 25.36600 1.000 33.90558  ? 306 TYR A HA   1 
ATOM   4795 H  HB2  . TYR A 1 306 ? -17.27200 16.35600 26.18400 1.000 34.65558  ? 306 TYR A HB2  1 
ATOM   4796 H  HB3  . TYR A 1 306 ? -17.79800 15.37300 25.05100 1.000 34.65558  ? 306 TYR A HB3  1 
ATOM   4797 H  HD1  . TYR A 1 306 ? -17.09000 18.75200 25.68700 1.000 33.42558  ? 306 TYR A HD1  1 
ATOM   4798 H  HD2  . TYR A 1 306 ? -18.02700 16.12500 22.84200 1.000 36.62558  ? 306 TYR A HD2  1 
ATOM   4799 H  HE1  . TYR A 1 306 ? -16.65800 20.34000 24.09500 1.000 34.46558  ? 306 TYR A HE1  1 
ATOM   4800 H  HE2  . TYR A 1 306 ? -17.57400 17.68300 21.23900 1.000 40.39558  ? 306 TYR A HE2  1 
ATOM   4801 H  HH   . TYR A 1 306 ? -16.56100 20.80400 21.86700 1.000 36.39558  ? 306 TYR A HH   1 
ATOM   4802 N  N    . LYS A 1 307 ? -19.82500 14.02200 26.69500 1.000 30.80630  ? 307 LYS A N    1 
ATOM   4803 C  CA   . LYS A 1 307 ? -19.79200 12.87100 27.58800 1.000 30.24050  ? 307 LYS A CA   1 
ATOM   4804 C  C    . LYS A 1 307 ? -18.37100 12.34500 27.72000 1.000 32.68286  ? 307 LYS A C    1 
ATOM   4805 O  O    . LYS A 1 307 ? -17.55400 12.45300 26.80300 1.000 31.42117  ? 307 LYS A O    1 
ATOM   4806 C  CB   . LYS A 1 307 ? -20.70200 11.74800 27.07600 1.000 37.51442  ? 307 LYS A CB   1 
ATOM   4807 C  CG   . LYS A 1 307 ? -22.17500 11.93800 27.36800 1.000 49.02316  ? 307 LYS A CG   1 
ATOM   4808 C  CD   . LYS A 1 307 ? -23.06300 11.10300 26.42200 1.000 79.75193  ? 307 LYS A CD   1 
ATOM   4809 C  CE   . LYS A 1 307 ? -24.36700 11.83500 26.03200 1.000 88.66899  ? 307 LYS A CE   1 
ATOM   4810 N  NZ   . LYS A 1 307 ? -24.25900 12.61800 24.75100 1.000 62.27011  ? 307 LYS A NZ   1 
ATOM   4811 H  H    . LYS A 1 307 ? -20.12800 13.85800 25.90700 1.000 39.51558  ? 307 LYS A H    1 
ATOM   4812 H  HA   . LYS A 1 307 ? -20.11300 13.14100 28.46200 1.000 39.65558  ? 307 LYS A HA   1 
ATOM   4813 H  HB2  . LYS A 1 307 ? -20.60100 11.68600 26.11300 1.000 48.40558  ? 307 LYS A HB2  1 
ATOM   4814 H  HB3  . LYS A 1 307 ? -20.42700 10.91600 27.49300 1.000 48.40558  ? 307 LYS A HB3  1 
ATOM   4815 H  HG2  . LYS A 1 307 ? -22.35900 11.66000 28.27900 1.000 63.01558  ? 307 LYS A HG2  1 
ATOM   4816 H  HG3  . LYS A 1 307 ? -22.40600 12.87300 27.25300 1.000 63.01558  ? 307 LYS A HG3  1 
ATOM   4817 H  HD2  . LYS A 1 307 ? -22.56900 10.91400 25.60800 1.000 99.53558  ? 307 LYS A HD2  1 
ATOM   4818 H  HD3  . LYS A 1 307 ? -23.30500 10.27300 26.86300 1.000 99.53558  ? 307 LYS A HD3  1 
ATOM   4819 H  HE2  . LYS A 1 307 ? -25.07300 11.18000 25.92000 1.000 110.28558 ? 307 LYS A HE2  1 
ATOM   4820 H  HE3  . LYS A 1 307 ? -24.60000 12.45700 26.73900 1.000 110.28558 ? 307 LYS A HE3  1 
ATOM   4821 H  HZ1  . LYS A 1 307 ? -23.62500 13.23700 24.82500 1.000 77.29558  ? 307 LYS A HZ1  1 
ATOM   4822 H  HZ2  . LYS A 1 307 ? -24.05400 12.07300 24.07800 1.000 77.29558  ? 307 LYS A HZ2  1 
ATOM   4823 H  HZ3  . LYS A 1 307 ? -25.03400 13.01700 24.57200 1.000 77.29558  ? 307 LYS A HZ3  1 
ATOM   4824 N  N    . GLU A 1 308 ? -18.07500 11.77600 28.88200 1.000 25.76457  ? 308 GLU A N    1 
ATOM   4825 C  CA   . GLU A 1 308 ? -16.77200 11.17400 29.12100 1.000 24.59657  ? 308 GLU A CA   1 
ATOM   4826 C  C    . GLU A 1 308 ? -16.95500 10.05700 30.13400 1.000 29.57112  ? 308 GLU A C    1 
ATOM   4827 O  O    . GLU A 1 308 ? -17.99100 9.95200  30.79600 1.000 27.01772  ? 308 GLU A O    1 
ATOM   4828 C  CB   . GLU A 1 308 ? -15.76000 12.22900 29.60700 1.000 31.34158  ? 308 GLU A CB   1 
ATOM   4829 C  CG   . GLU A 1 308 ? -14.31400 11.74900 29.74500 1.000 29.58753  ? 308 GLU A CG   1 
ATOM   4830 C  CD   . GLU A 1 308 ? -13.80400 11.05500 28.49300 1.000 40.74760  ? 308 GLU A CD   1 
ATOM   4831 O  OE1  . GLU A 1 308 ? -13.28100 11.74300 27.59100 1.000 33.88207  ? 308 GLU A OE1  1 
ATOM   4832 O  OE2  . GLU A 1 308 ? -13.96400 9.82000  28.40300 1.000 33.87972  ? 308 GLU A OE2  1 
ATOM   4833 H  H    . GLU A 1 308 ? -18.61500 11.72600 29.55000 1.000 34.76558  ? 308 GLU A H    1 
ATOM   4834 H  HA   . GLU A 1 308 ? -16.42100 10.78600 28.30400 1.000 33.05558  ? 308 GLU A HA   1 
ATOM   4835 H  HB2  . GLU A 1 308 ? -15.76000 12.96400 28.97400 1.000 41.06558  ? 308 GLU A HB2  1 
ATOM   4836 H  HB3  . GLU A 1 308 ? -16.04300 12.54300 30.48000 1.000 41.06558  ? 308 GLU A HB3  1 
ATOM   4837 H  HG2  . GLU A 1 308 ? -13.74300 12.51300 29.91800 1.000 38.50558  ? 308 GLU A HG2  1 
ATOM   4838 H  HG3  . GLU A 1 308 ? -14.25900 11.12000 30.48100 1.000 38.50558  ? 308 GLU A HG3  1 
ATOM   4839 N  N    A ASN A 1 309 ? -15.95800 9.17700  30.19200 0.500 30.31617  ? 309 ASN A N    1 
ATOM   4840 N  N    B ASN A 1 309 ? -15.93600 9.21400  30.24000 0.500 30.07628  ? 309 ASN A N    1 
ATOM   4841 C  CA   A ASN A 1 309 ? -15.85000 8.20800  31.27500 0.500 31.51346  ? 309 ASN A CA   1 
ATOM   4842 C  CA   B ASN A 1 309 ? -15.82900 8.26900  31.34300 0.500 31.38798  ? 309 ASN A CA   1 
ATOM   4843 C  C    A ASN A 1 309 ? -14.38500 8.13200  31.68200 0.500 31.30536  ? 309 ASN A C    1 
ATOM   4844 C  C    B ASN A 1 309 ? -14.35400 8.15800  31.69900 0.500 31.30900  ? 309 ASN A C    1 
ATOM   4845 O  O    A ASN A 1 309 ? -13.99700 8.63300  32.73900 0.500 30.41554  ? 309 ASN A O    1 
ATOM   4846 O  O    B ASN A 1 309 ? -13.92400 8.66300  32.73800 0.500 30.51377  ? 309 ASN A O    1 
ATOM   4847 C  CB   A ASN A 1 309 ? -16.40000 6.82200  30.89000 0.500 34.35582  ? 309 ASN A CB   1 
ATOM   4848 C  CB   B ASN A 1 309 ? -16.43100 6.91100  30.98600 0.500 33.76763  ? 309 ASN A CB   1 
ATOM   4849 C  CG   A ASN A 1 309 ? -16.14800 6.43600  29.42000 0.500 46.32680  ? 309 ASN A CG   1 
ATOM   4850 C  CG   B ASN A 1 309 ? -16.52100 5.98000  32.18500 0.500 42.61288  ? 309 ASN A CG   1 
ATOM   4851 O  OD1  A ASN A 1 309 ? -15.04000 6.57100  28.89200 0.500 34.48373  ? 309 ASN A OD1  1 
ATOM   4852 O  OD1  B ASN A 1 309 ? -15.80600 6.14900  33.17200 0.500 48.20620  ? 309 ASN A OD1  1 
ATOM   4853 N  ND2  A ASN A 1 309 ? -17.18800 5.92200  28.76800 0.500 44.26680  ? 309 ASN A ND2  1 
ATOM   4854 N  ND2  B ASN A 1 309 ? -17.40400 4.98900  32.10200 0.500 56.40890  ? 309 ASN A ND2  1 
ATOM   4855 H  H    A ASN A 1 309 ? -15.32700 9.12200  29.61100 0.500 40.52558  ? 309 ASN A H    1 
ATOM   4856 H  H    B ASN A 1 309 ? -15.28500 9.16800  29.67900 0.500 40.26558  ? 309 ASN A H    1 
ATOM   4857 H  HA   A ASN A 1 309 ? -16.39400 8.48800  32.02700 0.500 42.84558  ? 309 ASN A HA   1 
ATOM   4858 H  HA   B ASN A 1 309 ? -16.33400 8.57400  32.11300 0.500 42.73558  ? 309 ASN A HA   1 
ATOM   4859 H  HB2  A ASN A 1 309 ? -15.97500 6.15200  31.44700 0.500 46.30558  ? 309 ASN A HB2  1 
ATOM   4860 H  HB2  B ASN A 1 309 ? -17.32700 7.04200  30.63900 0.500 45.69558  ? 309 ASN A HB2  1 
ATOM   4861 H  HB3  A ASN A 1 309 ? -17.35900 6.81600  31.03600 0.500 46.30558  ? 309 ASN A HB3  1 
ATOM   4862 H  HB3  B ASN A 1 309 ? -15.87500 6.48400  30.31500 0.500 45.69558  ? 309 ASN A HB3  1 
ATOM   4863 H  HD21 A ASN A 1 309 ? -17.10600 5.68800  27.94400 0.500 56.79558  ? 309 ASN A HD21 1 
ATOM   4864 H  HD21 B ASN A 1 309 ? -17.49200 4.43600  32.75500 0.500 74.50558  ? 309 ASN A HD21 1 
ATOM   4865 H  HD22 A ASN A 1 309 ? -17.94200 5.82400  29.17000 0.500 56.79558  ? 309 ASN A HD22 1 
ATOM   4866 H  HD22 B ASN A 1 309 ? -17.88700 4.90100  31.39600 0.500 74.50558  ? 309 ASN A HD22 1 
ATOM   4867 N  N    . SER A 1 310 ? -13.56100 7.54000  30.82400 1.000 29.18422  ? 310 SER A N    1 
ATOM   4868 C  CA   . SER A 1 310 ? -12.12500 7.46200  31.03600 1.000 27.08579  ? 310 SER A CA   1 
ATOM   4869 C  C    . SER A 1 310 ? -11.43400 7.63100  29.69200 1.000 35.69458  ? 310 SER A C    1 
ATOM   4870 O  O    . SER A 1 310 ? -11.77500 6.94000  28.73200 1.000 39.72172  ? 310 SER A O    1 
ATOM   4871 C  CB   . SER A 1 310 ? -11.73300 6.12000  31.67400 1.000 35.85237  ? 310 SER A CB   1 
ATOM   4872 O  OG   . SER A 1 310 ? -10.33400 6.05000  31.86900 1.000 45.29956  ? 310 SER A OG   1 
ATOM   4873 H  H    A SER A 1 310 ? -13.81900 7.16800  30.09300 0.500 38.55558  ? 310 SER A H    1 
ATOM   4874 H  H    B SER A 1 310 ? -13.83500 7.16100  30.10200 0.500 38.55558  ? 310 SER A H    1 
ATOM   4875 H  HA   . SER A 1 310 ? -11.83500 8.17400  31.62900 1.000 35.47558  ? 310 SER A HA   1 
ATOM   4876 H  HB2  . SER A 1 310 ? -12.17600 6.03600  32.53300 1.000 46.27558  ? 310 SER A HB2  1 
ATOM   4877 H  HB3  . SER A 1 310 ? -12.00700 5.39800  31.08700 1.000 46.27558  ? 310 SER A HB3  1 
ATOM   4878 H  HG   . SER A 1 310 ? -10.07200 6.71400  32.31200 1.000 57.00558  ? 310 SER A HG   1 
ATOM   4879 N  N    . TYR A 1 311 ? -10.47900 8.55400  29.62100 1.000 35.47184  ? 311 TYR A N    1 
ATOM   4880 C  CA   . TYR A 1 311 ? -9.72900  8.80200  28.39700 1.000 42.76057  ? 311 TYR A CA   1 
ATOM   4881 C  C    . TYR A 1 311 ? -8.24100  8.82000  28.71200 1.000 41.71204  ? 311 TYR A C    1 
ATOM   4882 O  O    . TYR A 1 311 ? -7.81200  9.42300  29.70100 1.000 33.52616  ? 311 TYR A O    1 
ATOM   4883 C  CB   . TYR A 1 311 ? -10.14600 10.13400 27.72200 1.000 32.92860  ? 311 TYR A CB   1 
ATOM   4884 C  CG   . TYR A 1 311 ? -9.20300  10.52700 26.61700 1.000 39.36967  ? 311 TYR A CG   1 
ATOM   4885 C  CD1  . TYR A 1 311 ? -9.31000  9.95900  25.35000 1.000 43.18128  ? 311 TYR A CD1  1 
ATOM   4886 C  CD2  . TYR A 1 311 ? -8.18600  11.44300 26.83900 1.000 32.39967  ? 311 TYR A CD2  1 
ATOM   4887 C  CE1  . TYR A 1 311 ? -8.42100  10.30200 24.33300 1.000 44.10842  ? 311 TYR A CE1  1 
ATOM   4888 C  CE2  . TYR A 1 311 ? -7.30000  11.79200 25.83000 1.000 32.94224  ? 311 TYR A CE2  1 
ATOM   4889 C  CZ   . TYR A 1 311 ? -7.42700  11.21400 24.57800 1.000 41.48078  ? 311 TYR A CZ   1 
ATOM   4890 O  OH   . TYR A 1 311 ? -6.55600  11.55500 23.57400 1.000 41.22881  ? 311 TYR A OH   1 
ATOM   4891 H  H    . TYR A 1 311 ? -10.24500 9.05500  30.28000 1.000 43.63558  ? 311 TYR A H    1 
ATOM   4892 H  HA   . TYR A 1 311 ? -9.90100  8.08500  27.76600 1.000 51.04558  ? 311 TYR A HA   1 
ATOM   4893 H  HB2  . TYR A 1 311 ? -11.03300 10.03500 27.34300 1.000 39.04558  ? 311 TYR A HB2  1 
ATOM   4894 H  HB3  . TYR A 1 311 ? -10.14600 10.84100 28.38600 1.000 39.04558  ? 311 TYR A HB3  1 
ATOM   4895 H  HD1  . TYR A 1 311 ? -9.98400  9.34100  25.18000 1.000 48.96558  ? 311 TYR A HD1  1 
ATOM   4896 H  HD2  . TYR A 1 311 ? -8.09600  11.83000 27.67900 1.000 37.08558  ? 311 TYR A HD2  1 
ATOM   4897 H  HE1  . TYR A 1 311 ? -8.50200  9.91400  23.49100 1.000 48.88558  ? 311 TYR A HE1  1 
ATOM   4898 H  HE2  . TYR A 1 311 ? -6.62600  12.41100 25.99300 1.000 36.63558  ? 311 TYR A HE2  1 
ATOM   4899 H  HH   . TYR A 1 311 ? -5.99200  12.11000 23.85800 1.000 44.34558  ? 311 TYR A HH   1 
ATOM   4900 N  N    . THR A 1 312 ? -7.45700  8.15000  27.86600 1.000 35.79688  ? 312 THR A N    1 
ATOM   4901 C  CA   . THR A 1 312 ? -6.00300  8.19600  27.95300 1.000 41.93247  ? 312 THR A CA   1 
ATOM   4902 C  C    . THR A 1 312 ? -5.41800  8.37500  26.56000 1.000 38.14765  ? 312 THR A C    1 
ATOM   4903 O  O    . THR A 1 312 ? -5.80200  7.66500  25.62500 1.000 43.87244  ? 312 THR A O    1 
ATOM   4904 C  CB   . THR A 1 312 ? -5.45500  6.92200  28.60100 1.000 47.72986  ? 312 THR A CB   1 
ATOM   4905 O  OG1  . THR A 1 312 ? -5.97200  6.81200  29.93200 1.000 48.32814  ? 312 THR A OG1  1 
ATOM   4906 C  CG2  . THR A 1 312 ? -3.93100  6.96200  28.65600 1.000 50.72706  ? 312 THR A CG2  1 
ATOM   4907 H  H    . THR A 1 312 ? -7.75000  7.65600  27.22600 1.000 41.06558  ? 312 THR A H    1 
ATOM   4908 H  HA   . THR A 1 312 ? -5.73400  8.95800  28.49100 1.000 47.80558  ? 312 THR A HA   1 
ATOM   4909 H  HB   . THR A 1 312 ? -5.72000  6.14900  28.07900 1.000 54.75558  ? 312 THR A HB   1 
ATOM   4910 H  HG1  . THR A 1 312 ? -5.67500  6.11800  30.29900 1.000 56.81558  ? 312 THR A HG1  1 
ATOM   4911 H  HG21 . THR A 1 312 ? -3.60200  6.26400  29.24300 1.000 57.62558  ? 312 THR A HG21 1 
ATOM   4912 H  HG22 . THR A 1 312 ? -3.56400  6.82600  27.76800 1.000 57.62558  ? 312 THR A HG22 1 
ATOM   4913 H  HG23 . THR A 1 312 ? -3.63400  7.82200  28.99100 1.000 57.62558  ? 312 THR A HG23 1 
ATOM   4914 N  N    . THR A 1 313 ? -4.50800  9.33200  26.41600 1.000 39.98200  ? 313 THR A N    1 
ATOM   4915 C  CA   . THR A 1 313 ? -3.90800  9.58900  25.11400 1.000 41.82149  ? 313 THR A CA   1 
ATOM   4916 C  C    . THR A 1 313 ? -3.03700  8.40500  24.70000 1.000 50.21823  ? 313 THR A C    1 
ATOM   4917 O  O    . THR A 1 313 ? -2.41200  7.75200  25.53500 1.000 43.42952  ? 313 THR A O    1 
ATOM   4918 C  CB   . THR A 1 313 ? -3.06800  10.87100 25.14800 1.000 47.29342  ? 313 THR A CB   1 
ATOM   4919 O  OG1  . THR A 1 313 ? -2.63700  11.20500 23.82600 1.000 52.52477  ? 313 THR A OG1  1 
ATOM   4920 C  CG2  . THR A 1 313 ? -1.85000  10.70400 26.02400 1.000 48.82226  ? 313 THR A CG2  1 
ATOM   4921 H  H    . THR A 1 313 ? -4.22400  9.84000  27.04900 1.000 43.77558  ? 313 THR A H    1 
ATOM   4922 H  HA   . THR A 1 313 ? -4.60500  9.71100  24.45000 1.000 44.69558  ? 313 THR A HA   1 
ATOM   4923 H  HB   . THR A 1 313 ? -3.61200  11.58700 25.51100 1.000 51.35558  ? 313 THR A HB   1 
ATOM   4924 H  HG1  . THR A 1 313 ? -2.08600  11.83800 23.85500 1.000 56.46558  ? 313 THR A HG1  1 
ATOM   4925 H  HG21 . THR A 1 313 ? -1.46900  11.57200 26.23100 1.000 53.34558  ? 313 THR A HG21 1 
ATOM   4926 H  HG22 . THR A 1 313 ? -2.09500  10.26300 26.85200 1.000 53.34558  ? 313 THR A HG22 1 
ATOM   4927 H  HG23 . THR A 1 313 ? -1.18300  10.16900 25.56700 1.000 53.34558  ? 313 THR A HG23 1 
ATOM   4928 N  N    . THR A 1 314 ? -3.01100  8.13000  23.39800 1.000 63.99471  ? 314 THR A N    1 
ATOM   4929 C  CA   . THR A 1 314 ? -2.19300  7.06100  22.83700 1.000 70.09325  ? 314 THR A CA   1 
ATOM   4930 C  C    . THR A 1 314 ? -0.93200  7.57400  22.16200 1.000 81.03396  ? 314 THR A C    1 
ATOM   4931 O  O    . THR A 1 314 ? -0.13700  6.76600  21.67000 1.000 84.24577  ? 314 THR A O    1 
ATOM   4932 C  CB   . THR A 1 314 ? -2.99700  6.25200  21.81300 1.000 72.59051  ? 314 THR A CB   1 
ATOM   4933 O  OG1  . THR A 1 314 ? -3.44100  7.12300  20.76100 1.000 77.05256  ? 314 THR A OG1  1 
ATOM   4934 C  CG2  . THR A 1 314 ? -4.19600  5.58700  22.47300 1.000 85.03858  ? 314 THR A CG2  1 
ATOM   4935 H  H    . THR A 1 314 ? -3.46800  8.55800  22.80900 1.000 68.87558  ? 314 THR A H    1 
ATOM   4936 H  HA   . THR A 1 314 ? -1.93700  6.47000  23.56200 1.000 74.87558  ? 314 THR A HA   1 
ATOM   4937 H  HB   . THR A 1 314 ? -2.43900  5.55200  21.43800 1.000 76.94558  ? 314 THR A HB   1 
ATOM   4938 H  HG1  . THR A 1 314 ? -3.93000  7.72900  21.07700 1.000 81.84558  ? 314 THR A HG1  1 
ATOM   4939 H  HG21 . THR A 1 314 ? -4.72900  5.12700  21.80600 1.000 92.88558  ? 314 THR A HG21 1 
ATOM   4940 H  HG22 . THR A 1 314 ? -3.89700  4.94300  23.13500 1.000 92.88558  ? 314 THR A HG22 1 
ATOM   4941 H  HG23 . THR A 1 314 ? -4.74700  6.25500  22.91100 1.000 92.88558  ? 314 THR A HG23 1 
ATOM   4942 N  N    . ILE A 1 315 ? -0.79900  8.89700  22.08000 1.000 63.04566  ? 315 ILE A N    1 
ATOM   4943 C  CA   . ILE A 1 315 ? 0.32600   9.52900  21.34400 1.000 80.77580  ? 315 ILE A CA   1 
ATOM   4944 C  C    . ILE A 1 315 ? 1.35400   10.07300 22.34300 1.000 69.72802  ? 315 ILE A C    1 
ATOM   4945 O  O    . ILE A 1 315 ? 0.96600   10.42500 23.46200 1.000 60.32472  ? 315 ILE A O    1 
ATOM   4946 C  CB   . ILE A 1 315 ? -0.24600  10.59500 20.40300 1.000 89.41276  ? 315 ILE A CB   1 
ATOM   4947 C  CG1  . ILE A 1 315 ? -1.03000  9.95200  19.27100 1.000 86.28647  ? 315 ILE A CG1  1 
ATOM   4948 C  CG2  . ILE A 1 315 ? 0.84600   11.50900 19.86000 1.000 98.62930  ? 315 ILE A CG2  1 
ATOM   4949 C  CD1  . ILE A 1 315 ? -2.27600  10.71800 18.88400 1.000 90.67880  ? 315 ILE A CD1  1 
ATOM   4950 H  H    . ILE A 1 315 ? -1.37600  9.47500  22.46400 1.000 65.85558  ? 315 ILE A H    1 
ATOM   4951 H  HA   . ILE A 1 315 ? 0.76300   8.85500  20.79600 1.000 86.27558  ? 315 ILE A HA   1 
ATOM   4952 H  HB   . ILE A 1 315 ? -0.86800  11.13700 20.91600 1.000 96.52558  ? 315 ILE A HB   1 
ATOM   4953 H  HG12 . ILE A 1 315 ? -0.44700  9.88300  18.48900 1.000 91.71558  ? 315 ILE A HG12 1 
ATOM   4954 H  HG13 . ILE A 1 315 ? -1.28600  9.04600  19.53600 1.000 91.71558  ? 315 ILE A HG13 1 
ATOM   4955 H  HG21 . ILE A 1 315 ? 0.53600   11.93800 19.04600 1.000 107.13558 ? 315 ILE A HG21 1 
ATOM   4956 H  HG22 . ILE A 1 315 ? 1.06600   12.18700 20.51500 1.000 107.13558 ? 315 ILE A HG22 1 
ATOM   4957 H  HG23 . ILE A 1 315 ? 1.63500   10.98000 19.66500 1.000 107.13558 ? 315 ILE A HG23 1 
ATOM   4958 H  HD11 . ILE A 1 315 ? -2.81200  10.86300 19.68400 1.000 97.46558  ? 315 ILE A HD11 1 
ATOM   4959 H  HD12 . ILE A 1 315 ? -2.02300  11.57900 18.50100 1.000 97.46558  ? 315 ILE A HD12 1 
ATOM   4960 H  HD13 . ILE A 1 315 ? -2.79400  10.20900 18.23200 1.000 97.46558  ? 315 ILE A HD13 1 
ATOM   4961 N  N    . LYS A 1 316 ? 2.63800   10.03100 21.98300 1.000 72.05700  ? 316 LYS A N    1 
ATOM   4962 C  CA   . LYS A 1 316 ? 3.70000   10.55100 22.83100 1.000 70.19445  ? 316 LYS A CA   1 
ATOM   4963 C  C    . LYS A 1 316 ? 3.78900   12.06900 22.70200 1.000 92.28695  ? 316 LYS A C    1 
ATOM   4964 O  O    . LYS A 1 316 ? 3.32100   12.64600 21.71800 1.000 86.95708  ? 316 LYS A O    1 
ATOM   4965 C  CB   . LYS A 1 316 ? 5.03400   9.91300  22.45800 1.000 62.93883  ? 316 LYS A CB   1 
ATOM   4966 H  H    . LYS A 1 316 ? 2.91800   9.67300  21.25300 1.000 75.67558  ? 316 LYS A H    1 
ATOM   4967 H  HA   . LYS A 1 316 ? 3.51500   10.33300 23.75800 1.000 74.00558  ? 316 LYS A HA   1 
ATOM   4968 N  N    . PRO A 1 317 ? 4.40100   12.74300 23.68300 1.000 80.90561  ? 317 PRO A N    1 
ATOM   4969 C  CA   . PRO A 1 317 ? 4.35600   14.22100 23.68800 1.000 79.80335  ? 317 PRO A CA   1 
ATOM   4970 C  C    . PRO A 1 317 ? 4.91200   14.87000 22.43000 1.000 105.70526 ? 317 PRO A C    1 
ATOM   4971 O  O    . PRO A 1 317 ? 4.25800   15.75100 21.85200 1.000 83.19420  ? 317 PRO A O    1 
ATOM   4972 C  CB   . PRO A 1 317 ? 5.18700   14.58500 24.92900 1.000 81.43628  ? 317 PRO A CB   1 
ATOM   4973 C  CG   . PRO A 1 317 ? 5.10600   13.37900 25.80600 1.000 79.73863  ? 317 PRO A CG   1 
ATOM   4974 C  CD   . PRO A 1 317 ? 5.08300   12.20300 24.87100 1.000 75.98517  ? 317 PRO A CD   1 
ATOM   4975 H  HA   . PRO A 1 317 ? 3.43600   14.50400 23.80700 1.000 87.90558  ? 317 PRO A HA   1 
ATOM   4976 H  HB2  . PRO A 1 317 ? 6.10400   14.76800 24.67200 1.000 90.70558  ? 317 PRO A HB2  1 
ATOM   4977 H  HB3  . PRO A 1 317 ? 4.80400   15.36100 25.36800 1.000 90.70558  ? 317 PRO A HB3  1 
ATOM   4978 H  HG2  . PRO A 1 317 ? 5.88200   13.34300 26.38700 1.000 88.71558  ? 317 PRO A HG2  1 
ATOM   4979 H  HG3  . PRO A 1 317 ? 4.29500   13.41300 26.33800 1.000 88.71558  ? 317 PRO A HG3  1 
ATOM   4980 H  HD2  . PRO A 1 317 ? 5.98400   11.91500 24.65400 1.000 82.91558  ? 317 PRO A HD2  1 
ATOM   4981 H  HD3  . PRO A 1 317 ? 4.58300   11.46500 25.25400 1.000 82.91558  ? 317 PRO A HD3  1 
ATOM   4982 N  N    . VAL A 1 318 ? 6.11400   14.47100 21.99700 1.000 88.36842  ? 318 VAL A N    1 
ATOM   4983 C  CA   . VAL A 1 318 ? 6.72500   15.08400 20.82100 1.000 93.23473  ? 318 VAL A CA   1 
ATOM   4984 C  C    . VAL A 1 318 ? 5.81200   14.96100 19.60700 1.000 92.23411  ? 318 VAL A C    1 
ATOM   4985 O  O    . VAL A 1 318 ? 5.84300   15.81100 18.70800 1.000 84.65127  ? 318 VAL A O    1 
ATOM   4986 C  CB   . VAL A 1 318 ? 8.10900   14.45400 20.55200 1.000 72.72409  ? 318 VAL A CB   1 
ATOM   4987 H  H    . VAL A 1 318 ? 6.58900   13.85600 22.36500 1.000 96.46558  ? 318 VAL A H    1 
ATOM   4988 H  HA   . VAL A 1 318 ? 6.85400   16.02900 20.99900 1.000 101.56558 ? 318 VAL A HA   1 
ATOM   4989 N  N    . THR A 1 319 ? 4.98000   13.91500 19.56000 1.000 87.23850  ? 319 THR A N    1 
ATOM   4990 C  CA   . THR A 1 319 ? 4.06500   13.74800 18.43400 1.000 91.85045  ? 319 THR A CA   1 
ATOM   4991 C  C    . THR A 1 319 ? 2.90800   14.74600 18.49900 1.000 96.60390  ? 319 THR A C    1 
ATOM   4992 O  O    . THR A 1 319 ? 2.45900   15.24400 17.46000 1.000 93.21613  ? 319 THR A O    1 
ATOM   4993 C  CB   . THR A 1 319 ? 3.53900   12.31200 18.39400 1.000 74.86857  ? 319 THR A CB   1 
ATOM   4994 H  H    . THR A 1 319 ? 4.92800   13.29900 20.15800 1.000 93.15558  ? 319 THR A H    1 
ATOM   4995 H  HA   . THR A 1 319 ? 4.55100   13.91300 17.61100 1.000 97.90558  ? 319 THR A HA   1 
ATOM   4996 N  N    . HIS A 1 320 ? 2.42300   15.04800 19.70400 1.000 93.27737  ? 320 HIS A N    1 
ATOM   4997 C  CA   . HIS A 1 320 ? 1.36700   16.07200 19.87800 1.000 86.69228  ? 320 HIS A CA   1 
ATOM   4998 C  C    . HIS A 1 320 ? 1.93000   17.43200 19.50300 1.000 90.27911  ? 320 HIS A C    1 
ATOM   4999 O  O    . HIS A 1 320 ? 1.30000   18.20500 18.81100 1.000 89.67302  ? 320 HIS A O    1 
ATOM   5000 C  CB   . HIS A 1 320 ? 0.89800   16.18200 21.32400 1.000 85.03247  ? 320 HIS A CB   1 
ATOM   5001 C  CG   . HIS A 1 320 ? 0.17100   14.97400 21.76500 1.000 90.52270  ? 320 HIS A CG   1 
ATOM   5002 N  ND1  . HIS A 1 320 ? -1.13300  14.69600 21.42500 1.000 76.09830  ? 320 HIS A ND1  1 
ATOM   5003 C  CD2  . HIS A 1 320 ? 0.60600   13.95300 22.48700 1.000 81.52966  ? 320 HIS A CD2  1 
ATOM   5004 C  CE1  . HIS A 1 320 ? -1.46600  13.53700 21.95700 1.000 63.83321  ? 320 HIS A CE1  1 
ATOM   5005 N  NE2  . HIS A 1 320 ? -0.41900  13.07200 22.60400 1.000 79.81627  ? 320 HIS A NE2  1 
ATOM   5006 H  H    . HIS A 1 320 ? 2.70900   14.66300 20.46900 1.000 101.96558 ? 320 HIS A H    1 
ATOM   5007 H  HA   . HIS A 1 320 ? 0.60200   15.86800 19.28700 1.000 95.04558  ? 320 HIS A HA   1 
ATOM   5008 H  HB2  . HIS A 1 320 ? 1.67800   16.31500 21.90300 1.000 94.39558  ? 320 HIS A HB2  1 
ATOM   5009 H  HB3  . HIS A 1 320 ? 0.30800   16.96300 21.41100 1.000 94.39558  ? 320 HIS A HB3  1 
ATOM   5010 H  HD2  . HIS A 1 320 ? 1.45600   13.86000 22.86600 1.000 90.14558  ? 320 HIS A HD2  1 
ATOM   5011 H  HE1  . HIS A 1 320 ? -2.30300  13.11400 21.88400 1.000 68.97558  ? 320 HIS A HE1  1 
ATOM   5012 H  HE2  . HIS A 1 320 ? -0.37500  12.32100 23.04500 1.000 88.13558  ? 320 HIS A HE2  1 
ATOM   5013 N  N    . HIS A 1 321 ? 3.14700   17.77200 19.94100 1.000 94.59797  ? 321 HIS A N    1 
ATOM   5014 C  CA   . HIS A 1 321 ? 3.71100   19.09800 19.70700 1.000 95.50182  ? 321 HIS A CA   1 
ATOM   5015 C  C    . HIS A 1 321 ? 3.80900   19.40500 18.21800 1.000 99.94625  ? 321 HIS A C    1 
ATOM   5016 O  O    . HIS A 1 321 ? 3.54600   20.53400 17.79100 1.000 99.74458  ? 321 HIS A O    1 
ATOM   5017 C  CB   . HIS A 1 321 ? 5.08900   19.20900 20.36300 1.000 95.75523  ? 321 HIS A CB   1 
ATOM   5018 C  CG   . HIS A 1 321 ? 5.55300   20.62000 20.56100 1.000 95.74527  ? 321 HIS A CG   1 
ATOM   5019 N  ND1  . HIS A 1 321 ? 4.71500   21.62300 21.00000 1.000 93.24186  ? 321 HIS A ND1  1 
ATOM   5020 C  CD2  . HIS A 1 321 ? 6.76500   21.19600 20.37800 1.000 89.60659  ? 321 HIS A CD2  1 
ATOM   5021 C  CE1  . HIS A 1 321 ? 5.39000   22.75600 21.08000 1.000 84.19805  ? 321 HIS A CE1  1 
ATOM   5022 N  NE2  . HIS A 1 321 ? 6.63700   22.52400 20.71000 1.000 85.63607  ? 321 HIS A NE2  1 
ATOM   5023 H  H    . HIS A 1 321 ? 3.65800   17.23800 20.38100 1.000 105.06558 ? 321 HIS A H    1 
ATOM   5024 H  HA   . HIS A 1 321 ? 3.12700   19.75700 20.11400 1.000 106.60558 ? 321 HIS A HA   1 
ATOM   5025 H  HB2  . HIS A 1 321 ? 5.05400   18.78400 21.23500 1.000 107.17558 ? 321 HIS A HB2  1 
ATOM   5026 H  HB3  . HIS A 1 321 ? 5.73900   18.76000 19.80100 1.000 107.17558 ? 321 HIS A HB3  1 
ATOM   5027 H  HD2  . HIS A 1 321 ? 7.53900   20.77300 20.08300 1.000 100.72558 ? 321 HIS A HD2  1 
ATOM   5028 H  HE1  . HIS A 1 321 ? 5.04700   23.57600 21.35100 1.000 95.83558  ? 321 HIS A HE1  1 
ATOM   5029 H  HE2  . HIS A 1 321 ? 7.26700   23.10900 20.68100 1.000 97.00558  ? 321 HIS A HE2  1 
ATOM   5030 N  N    . HIS A 1 322 ? 4.18200   18.41200 17.41200 1.000 106.14295 ? 322 HIS A N    1 
ATOM   5031 C  CA   . HIS A 1 322 ? 4.41100   18.61500 15.98900 1.000 114.34607 ? 322 HIS A CA   1 
ATOM   5032 C  C    . HIS A 1 322 ? 3.19400   18.28900 15.13000 1.000 114.14365 ? 322 HIS A C    1 
ATOM   5033 O  O    . HIS A 1 322 ? 3.20100   18.60400 13.93500 1.000 111.87379 ? 322 HIS A O    1 
ATOM   5034 C  CB   . HIS A 1 322 ? 5.60300   17.76100 15.52100 1.000 121.90967 ? 322 HIS A CB   1 
ATOM   5035 C  CG   . HIS A 1 322 ? 6.85500   17.96500 16.32200 1.000 122.89598 ? 322 HIS A CG   1 
ATOM   5036 N  ND1  . HIS A 1 322 ? 6.99900   18.98800 17.23600 1.000 127.87755 ? 322 HIS A ND1  1 
ATOM   5037 C  CD2  . HIS A 1 322 ? 8.02000   17.27300 16.34800 1.000 119.49195 ? 322 HIS A CD2  1 
ATOM   5038 C  CE1  . HIS A 1 322 ? 8.19900   18.92000 17.78600 1.000 117.62302 ? 322 HIS A CE1  1 
ATOM   5039 N  NE2  . HIS A 1 322 ? 8.83800   17.88800 17.26500 1.000 113.67395 ? 322 HIS A NE2  1 
ATOM   5040 H  H    . HIS A 1 322 ? 4.30900   17.60200 17.67300 1.000 117.08558 ? 322 HIS A H    1 
ATOM   5041 H  HA   . HIS A 1 322 ? 4.63200   19.54800 15.84400 1.000 125.84558 ? 322 HIS A HA   1 
ATOM   5042 H  HB2  . HIS A 1 322 ? 5.36000   16.82400 15.58800 1.000 133.69558 ? 322 HIS A HB2  1 
ATOM   5043 H  HB3  . HIS A 1 322 ? 5.80300   17.98600 14.59900 1.000 133.69558 ? 322 HIS A HB3  1 
ATOM   5044 H  HD2  . HIS A 1 322 ? 8.22700   16.52200 15.84000 1.000 130.62558 ? 322 HIS A HD2  1 
ATOM   5045 H  HE1  . HIS A 1 322 ? 8.53600   19.50000 18.43000 1.000 130.68558 ? 322 HIS A HE1  1 
ATOM   5046 H  HE2  . HIS A 1 322 ? 9.63600   17.64100 17.46800 1.000 124.66558 ? 322 HIS A HE2  1 
ATOM   5047 N  N    . HIS A 1 323 ? 2.14500   17.67500 15.70500 1.000 102.42678 ? 323 HIS A N    1 
ATOM   5048 C  CA   . HIS A 1 323 ? 0.99200   17.19200 14.93500 1.000 112.53377 ? 323 HIS A CA   1 
ATOM   5049 C  C    . HIS A 1 323 ? -0.27500  17.41100 15.76700 1.000 101.49473 ? 323 HIS A C    1 
ATOM   5050 O  O    . HIS A 1 323 ? -0.83400  16.48300 16.35700 1.000 94.82432  ? 323 HIS A O    1 
ATOM   5051 C  CB   . HIS A 1 323 ? 1.17400   15.72400 14.54700 1.000 116.18237 ? 323 HIS A CB   1 
ATOM   5052 C  CG   . HIS A 1 323 ? 2.53200   15.41500 13.99700 1.000 128.13443 ? 323 HIS A CG   1 
ATOM   5053 N  ND1  . HIS A 1 323 ? 2.88400   15.67800 12.69000 1.000 118.10471 ? 323 HIS A ND1  1 
ATOM   5054 C  CD2  . HIS A 1 323 ? 3.63300   14.88700 14.58300 1.000 123.73333 ? 323 HIS A CD2  1 
ATOM   5055 C  CE1  . HIS A 1 323 ? 4.13800   15.31400 12.49100 1.000 119.13551 ? 323 HIS A CE1  1 
ATOM   5056 N  NE2  . HIS A 1 323 ? 4.61600   14.83100 13.62400 1.000 129.47613 ? 323 HIS A NE2  1 
ATOM   5057 H  H    . HIS A 1 323 ? 2.08000   17.52800 16.55000 1.000 111.14558 ? 323 HIS A H    1 
ATOM   5058 H  HA   . HIS A 1 323 ? 0.90400   17.72300 14.12900 1.000 122.55558 ? 323 HIS A HA   1 
ATOM   5059 H  HB2  . HIS A 1 323 ? 1.04000   15.17300 15.33400 1.000 125.63558 ? 323 HIS A HB2  1 
ATOM   5060 H  HB3  . HIS A 1 323 ? 0.52000   15.49700 13.86800 1.000 125.63558 ? 323 HIS A HB3  1 
ATOM   5061 H  HD2  . HIS A 1 323 ? 3.71000   14.61300 15.46900 1.000 133.55558 ? 323 HIS A HD2  1 
ATOM   5062 H  HE1  . HIS A 1 323 ? 4.60500   15.38600 11.69000 1.000 126.21558 ? 323 HIS A HE1  1 
ATOM   5063 H  HE2  . HIS A 1 323 ? 5.41300   14.53100 13.74200 1.000 139.23558 ? 323 HIS A HE2  1 
ATOM   5064 N  N    . HIS A 1 324 ? -0.73100  18.66000 15.80200 1.000 103.50005 ? 324 HIS A N    1 
ATOM   5065 C  CA   . HIS A 1 324 ? -1.95200  19.02300 16.51000 1.000 95.23655  ? 324 HIS A CA   1 
ATOM   5066 C  C    . HIS A 1 324 ? -2.76800  19.99300 15.65900 1.000 79.29644  ? 324 HIS A C    1 
ATOM   5067 O  O    . HIS A 1 324 ? -3.98000  19.83900 15.51700 1.000 71.29168  ? 324 HIS A O    1 
ATOM   5068 C  CB   . HIS A 1 324 ? -1.62600  19.64000 17.87400 1.000 74.24172  ? 324 HIS A CB   1 
ATOM   5069 C  CG   . HIS A 1 324 ? -0.90000  20.94500 17.78900 1.000 88.72416  ? 324 HIS A CG   1 
ATOM   5070 N  ND1  . HIS A 1 324 ? 0.40500   21.09700 18.20800 1.000 96.48635  ? 324 HIS A ND1  1 
ATOM   5071 C  CD2  . HIS A 1 324 ? -1.29800  22.16100 17.34600 1.000 90.09413  ? 324 HIS A CD2  1 
ATOM   5072 C  CE1  . HIS A 1 324 ? 0.78200   22.34800 18.01600 1.000 103.13532 ? 324 HIS A CE1  1 
ATOM   5073 N  NE2  . HIS A 1 324 ? -0.23200  23.01500 17.49400 1.000 109.51005 ? 324 HIS A NE2  1 
ATOM   5074 H  H    . HIS A 1 324 ? -0.34400  19.32500 15.41700 1.000 113.68558 ? 324 HIS A H    1 
ATOM   5075 H  HA   . HIS A 1 324 ? -2.48600  18.23100 16.67900 1.000 104.78558 ? 324 HIS A HA   1 
ATOM   5076 H  HB2  . HIS A 1 324 ? -2.45600  19.79400 18.35200 1.000 80.95558  ? 324 HIS A HB2  1 
ATOM   5077 H  HB3  . HIS A 1 324 ? -1.06700  19.02200 18.37000 1.000 80.95558  ? 324 HIS A HB3  1 
ATOM   5078 H  HD1  . HIS A 1 324 ? 0.89600   20.47500 18.54200 1.000 108.31558 ? 324 HIS A HD1  1 
ATOM   5079 H  HD2  . HIS A 1 324 ? -2.13500  22.37700 17.00500 1.000 100.76558 ? 324 HIS A HD2  1 
ATOM   5080 H  HE1  . HIS A 1 324 ? 1.62000   22.70000 18.21400 1.000 116.77558 ? 324 HIS A HE1  1 
ATOM   5081 H  HE2  . HIS A 1 324 ? -0.22600  23.84800 17.28200 1.000 124.49558 ? 324 HIS A HE2  1 
HETATM 5082 ZN ZN   . ZN  B 2 .   ? 9.04800   27.97800 26.49400 1.000 48.12558  ? 401 ZN  A ZN   1 
HETATM 5083 C  C1   . MLA C 3 .   ? -32.48000 14.41900 33.99700 1.000 62.87558  ? 402 MLA A C1   1 
HETATM 5084 O  O1A  . MLA C 3 .   ? -32.69700 15.52500 34.48700 1.000 60.51558  ? 402 MLA A O1A  1 
HETATM 5085 O  O1B  . MLA C 3 .   ? -31.67000 13.60900 34.46400 1.000 51.37558  ? 402 MLA A O1B  1 
HETATM 5086 C  C2   . MLA C 3 .   ? -33.24600 14.02900 32.73900 1.000 81.46558  ? 402 MLA A C2   1 
HETATM 5087 C  C3   . MLA C 3 .   ? -34.44400 13.12000 32.99600 1.000 86.15558  ? 402 MLA A C3   1 
HETATM 5088 O  O3A  . MLA C 3 .   ? -34.55700 12.60300 34.10800 1.000 63.19558  ? 402 MLA A O3A  1 
HETATM 5089 O  O3B  . MLA C 3 .   ? -35.24700 12.93800 32.07700 1.000 77.00558  ? 402 MLA A O3B  1 
HETATM 5090 H  HC21 . MLA C 3 .   ? -32.63400 13.57500 32.13200 1.000 97.90558  ? 402 MLA A HC21 1 
HETATM 5091 H  HC22 . MLA C 3 .   ? -33.55900 14.84400 32.30000 1.000 97.90558  ? 402 MLA A HC22 1 
HETATM 5092 C  C1   . MLA D 3 .   ? -31.19200 37.83900 28.27800 1.000 35.39558  ? 403 MLA A C1   1 
HETATM 5093 O  O1A  . MLA D 3 .   ? -31.94900 37.08900 28.85300 1.000 31.75558  ? 403 MLA A O1A  1 
HETATM 5094 O  O1B  . MLA D 3 .   ? -30.13300 37.48100 27.81900 1.000 41.01558  ? 403 MLA A O1B  1 
HETATM 5095 C  C2   . MLA D 3 .   ? -31.55900 39.31200 28.17100 1.000 37.72558  ? 403 MLA A C2   1 
HETATM 5096 C  C3   . MLA D 3 .   ? -32.61200 39.67400 27.13100 1.000 55.31558  ? 403 MLA A C3   1 
HETATM 5097 O  O3A  . MLA D 3 .   ? -33.14700 38.77100 26.49500 1.000 35.97558  ? 403 MLA A O3A  1 
HETATM 5098 O  O3B  . MLA D 3 .   ? -32.88800 40.86700 26.98000 1.000 47.72558  ? 403 MLA A O3B  1 
HETATM 5099 H  HC21 . MLA D 3 .   ? -30.74700 39.81400 27.97100 1.000 45.41558  ? 403 MLA A HC21 1 
HETATM 5100 H  HC22 . MLA D 3 .   ? -31.87700 39.60500 29.04000 1.000 45.41558  ? 403 MLA A HC22 1 
HETATM 5101 NA NA   . NA  E 4 .   ? -27.99300 15.75400 35.71800 1.000 37.66558  ? 404 NA  A NA   1 
HETATM 5102 NA NA   . NA  F 4 .   ? -17.20500 19.80200 45.62900 1.000 43.62558  ? 405 NA  A NA   1 
HETATM 5103 NA NA   . NA  G 4 .   ? -37.68900 15.63200 34.33800 1.000 47.77558  ? 406 NA  A NA   1 
HETATM 5104 CL CL   . CL  H 5 .   ? -28.60400 16.35800 43.42700 1.000 31.44558  ? 407 CL  A CL   1 
HETATM 5105 CL CL   . CL  I 5 .   ? -21.29500 22.61200 48.92100 1.000 40.28558  ? 408 CL  A CL   1 
HETATM 5106 O  O    . HOH J 6 .   ? -37.19000 14.98700 31.91800 1.000 44.94558  ? 501 HOH A O    1 
HETATM 5107 O  O    . HOH J 6 .   ? -42.85700 22.01000 34.09000 1.000 40.61558  ? 502 HOH A O    1 
HETATM 5108 O  O    . HOH J 6 .   ? -43.26100 39.63500 70.10700 1.000 54.65558  ? 503 HOH A O    1 
HETATM 5109 O  O    . HOH J 6 .   ? -10.301   23.575   43.176   1.000 44.54558  ? 504 HOH A O    1 
HETATM 5110 O  O    . HOH J 6 .   ? 1.62000   12.08300 26.35400 1.000 52.00558  ? 505 HOH A O    1 
HETATM 5111 O  O    . HOH J 6 .   ? -14.697   16.881   49.296   1.000 34.29558  ? 506 HOH A O    1 
HETATM 5112 O  O    . HOH J 6 .   ? -24.88500 39.98700 45.87400 1.000 55.54558  ? 507 HOH A O    1 
HETATM 5113 O  O    . HOH J 6 .   ? -61.195   40.574   77.077   1.000 47.25558  ? 508 HOH A O    1 
HETATM 5114 O  O    . HOH J 6 .   ? -13.31400 10.87200 25.22800 1.000 39.93558  ? 509 HOH A O    1 
HETATM 5115 O  O    . HOH J 6 .   ? -52.47000 42.99000 62.91100 1.000 47.28558  ? 510 HOH A O    1 
HETATM 5116 O  O    . HOH J 6 .   ? -30.81200 29.50600 16.47700 1.000 47.90558  ? 511 HOH A O    1 
HETATM 5117 O  O    . HOH J 6 .   ? -23.74900 21.11500 11.91900 1.000 42.03558  ? 512 HOH A O    1 
HETATM 5118 O  O    . HOH J 6 .   ? -24.40500 16.54600 51.08700 1.000 54.05558  ? 513 HOH A O    1 
HETATM 5119 O  O    . HOH J 6 .   ? -3.84400  18.82000 41.46200 1.000 51.66558  ? 514 HOH A O    1 
HETATM 5120 O  O    . HOH J 6 .   ? -40.03900 16.98300 13.67900 1.000 37.10558  ? 515 HOH A O    1 
HETATM 5121 O  O    . HOH J 6 .   ? -34.62400 40.69200 50.91000 1.000 47.90558  ? 516 HOH A O    1 
HETATM 5122 O  O    . HOH J 6 .   ? -32.92700 40.30000 54.52000 1.000 42.89558  ? 517 HOH A O    1 
HETATM 5123 O  O    . HOH J 6 .   ? -46.45800 35.46800 50.33600 1.000 55.00558  ? 518 HOH A O    1 
HETATM 5124 O  O    . HOH J 6 .   ? -18.95700 50.20900 24.51000 1.000 58.10558  ? 519 HOH A O    1 
HETATM 5125 O  O    . HOH J 6 .   ? 10.534    35.875   24.309   1.000 40.12558  ? 520 HOH A O    1 
HETATM 5126 O  O    . HOH J 6 .   ? -35.65400 34.71900 21.93600 1.000 36.59558  ? 521 HOH A O    1 
HETATM 5127 O  O    . HOH J 6 .   ? -34.23300 42.33500 40.85500 1.000 47.08558  ? 522 HOH A O    1 
HETATM 5128 O  O    . HOH J 6 .   ? -44.64800 28.35100 37.31300 1.000 49.26558  ? 523 HOH A O    1 
HETATM 5129 O  O    . HOH J 6 .   ? -4.75700  13.40900 23.98900 1.000 37.30558  ? 524 HOH A O    1 
HETATM 5130 O  O    . HOH J 6 .   ? -12.14800 4.39800  28.34200 1.000 53.90558  ? 525 HOH A O    1 
HETATM 5131 O  O    . HOH J 6 .   ? -27.75100 38.41100 28.30800 1.000 40.60558  ? 526 HOH A O    1 
HETATM 5132 O  O    . HOH J 6 .   ? -27.23800 14.58900 23.95900 1.000 37.56558  ? 527 HOH A O    1 
HETATM 5133 O  O    . HOH J 6 .   ? -37.19000 41.29600 48.95800 1.000 42.10558  ? 528 HOH A O    1 
HETATM 5134 O  O    . HOH J 6 .   ? -13.26800 8.14900  26.51900 1.000 55.97558  ? 529 HOH A O    1 
HETATM 5135 O  O    . HOH J 6 .   ? -23.90200 33.82300 48.22200 1.000 40.83558  ? 530 HOH A O    1 
HETATM 5136 O  O    . HOH J 6 .   ? -37.26300 26.44700 68.43200 1.000 36.24558  ? 531 HOH A O    1 
HETATM 5137 O  O    . HOH J 6 .   ? -37.66400 43.66700 50.21600 1.000 48.54558  ? 532 HOH A O    1 
HETATM 5138 O  O    . HOH J 6 .   ? -43.35800 23.01100 25.80500 1.000 34.02558  ? 533 HOH A O    1 
HETATM 5139 O  O    . HOH J 6 .   ? -15.69600 18.22300 44.35500 1.000 38.60558  ? 534 HOH A O    1 
HETATM 5140 O  O    . HOH J 6 .   ? -41.32500 16.32000 30.17000 1.000 40.95558  ? 535 HOH A O    1 
HETATM 5141 O  O    . HOH J 6 .   ? -21.74300 35.43800 39.87200 1.000 45.70558  ? 536 HOH A O    1 
HETATM 5142 O  O    . HOH J 6 .   ? -35.56500 32.01700 19.34900 1.000 46.95558  ? 537 HOH A O    1 
HETATM 5143 O  O    . HOH J 6 .   ? -23.75900 41.05000 35.91700 1.000 43.74558  ? 538 HOH A O    1 
HETATM 5144 O  O    . HOH J 6 .   ? -42.10600 36.91000 30.71000 1.000 41.20558  ? 539 HOH A O    1 
HETATM 5145 O  O    . HOH J 6 .   ? -35.45500 26.55100 52.08500 1.000 32.61558  ? 540 HOH A O    1 
HETATM 5146 O  O    . HOH J 6 .   ? -42.32900 19.19000 42.75300 1.000 51.56558  ? 541 HOH A O    1 
HETATM 5147 O  O    . HOH J 6 .   ? -31.34000 10.41700 14.30800 1.000 54.40558  ? 542 HOH A O    1 
HETATM 5148 O  O    . HOH J 6 .   ? -27.00000 34.40200 16.57400 1.000 46.18558  ? 543 HOH A O    1 
HETATM 5149 O  O    . HOH J 6 .   ? -35.37000 30.07100 66.73700 1.000 50.07558  ? 544 HOH A O    1 
HETATM 5150 O  O    . HOH J 6 .   ? -26.26200 30.45000 56.82800 1.000 36.50558  ? 545 HOH A O    1 
HETATM 5151 O  O    . HOH J 6 .   ? -31.29800 23.32200 15.70500 1.000 35.13558  ? 546 HOH A O    1 
HETATM 5152 O  O    . HOH J 6 .   ? -34.88600 14.00700 22.13400 1.000 39.06558  ? 547 HOH A O    1 
HETATM 5153 O  O    . HOH J 6 .   ? -28.03700 33.25100 20.96100 1.000 33.44558  ? 548 HOH A O    1 
HETATM 5154 O  O    . HOH J 6 .   ? -16.28000 30.14900 20.83800 1.000 38.53558  ? 549 HOH A O    1 
HETATM 5155 O  O    . HOH J 6 .   ? -21.90600 36.78700 20.20500 1.000 40.48558  ? 550 HOH A O    1 
HETATM 5156 O  O    . HOH J 6 .   ? -18.61400 20.92100 47.03800 1.000 39.97558  ? 551 HOH A O    1 
HETATM 5157 O  O    . HOH J 6 .   ? -6.97500  7.22000  23.28300 1.000 50.23558  ? 552 HOH A O    1 
HETATM 5158 O  O    . HOH J 6 .   ? -42.04700 39.79800 42.13100 1.000 49.33558  ? 553 HOH A O    1 
HETATM 5159 O  O    . HOH J 6 .   ? -34.80100 25.94600 49.69400 1.000 41.74558  ? 554 HOH A O    1 
HETATM 5160 O  O    . HOH J 6 .   ? -38.27800 17.54000 32.98500 1.000 34.71558  ? 555 HOH A O    1 
HETATM 5161 O  O    . HOH J 6 .   ? -44.12200 24.35300 36.98700 1.000 41.25558  ? 556 HOH A O    1 
HETATM 5162 O  O    . HOH J 6 .   ? -31.85300 22.05800 65.08700 1.000 50.57558  ? 557 HOH A O    1 
HETATM 5163 O  O    . HOH J 6 .   ? -24.36900 13.32300 20.99100 1.000 47.71558  ? 558 HOH A O    1 
HETATM 5164 O  O    . HOH J 6 .   ? -25.16900 19.41900 55.01900 1.000 33.53558  ? 559 HOH A O    1 
HETATM 5165 O  O    . HOH J 6 .   ? -29.95900 37.29800 36.92200 1.000 30.86558  ? 560 HOH A O    1 
HETATM 5166 O  O    . HOH J 6 .   ? -17.96400 20.50800 19.15300 1.000 44.10558  ? 561 HOH A O    1 
HETATM 5167 O  O    . HOH J 6 .   ? -31.78800 43.46300 38.54300 1.000 51.42558  ? 562 HOH A O    1 
HETATM 5168 O  O    . HOH J 6 .   ? -52.02300 27.98400 58.55100 1.000 45.32558  ? 563 HOH A O    1 
HETATM 5169 O  O    . HOH J 6 .   ? -31.58900 16.15000 43.50100 1.000 32.42558  ? 564 HOH A O    1 
HETATM 5170 O  O    . HOH J 6 .   ? -40.63600 39.03300 37.90500 1.000 41.46558  ? 565 HOH A O    1 
HETATM 5171 O  O    . HOH J 6 .   ? -30.34800 15.54500 36.31800 1.000 31.63558  ? 566 HOH A O    1 
HETATM 5172 O  O    . HOH J 6 .   ? -39.36200 39.89300 48.35100 1.000 35.67558  ? 567 HOH A O    1 
HETATM 5173 O  O    . HOH J 6 .   ? -1.67500  9.71700  33.38300 1.000 61.80558  ? 568 HOH A O    1 
HETATM 5174 O  O    . HOH J 6 .   ? -26.57400 33.01800 56.34400 1.000 35.22558  ? 569 HOH A O    1 
HETATM 5175 O  O    . HOH J 6 .   ? -23.80300 13.73800 29.69100 1.000 42.24558  ? 570 HOH A O    1 
HETATM 5176 O  O    . HOH J 6 .   ? -41.745   20.601   58.368   1.000 27.60558  ? 571 HOH A O    1 
HETATM 5177 O  O    . HOH J 6 .   ? -25.35700 30.06200 59.35200 1.000 38.81558  ? 572 HOH A O    1 
HETATM 5178 O  O    . HOH J 6 .   ? -36.86200 23.01900 52.10400 1.000 34.71558  ? 573 HOH A O    1 
HETATM 5179 O  O    . HOH J 6 .   ? -27.08800 37.12300 30.63600 1.000 39.13558  ? 574 HOH A O    1 
HETATM 5180 O  O    . HOH J 6 .   ? -13.06600 13.64200 21.23900 1.000 48.74558  ? 575 HOH A O    1 
HETATM 5181 O  O    . HOH J 6 .   ? 12.33500  30.22400 23.66700 1.000 36.30558  ? 576 HOH A O    1 
HETATM 5182 O  O    . HOH J 6 .   ? -31.09400 22.37300 58.18200 1.000 28.15558  ? 577 HOH A O    1 
HETATM 5183 O  O    . HOH J 6 .   ? -13.38400 18.87000 46.95000 1.000 49.23558  ? 578 HOH A O    1 
HETATM 5184 O  O    . HOH J 6 .   ? -15.42000 8.85400  35.03100 1.000 44.52558  ? 579 HOH A O    1 
HETATM 5185 O  O    . HOH J 6 .   ? -8.88300  22.13700 32.84000 1.000 47.42558  ? 580 HOH A O    1 
HETATM 5186 O  O    . HOH J 6 .   ? -37.47500 15.26400 15.28900 1.000 37.86558  ? 581 HOH A O    1 
HETATM 5187 O  O    . HOH J 6 .   ? -38.04800 11.29800 18.29700 1.000 44.96558  ? 582 HOH A O    1 
HETATM 5188 O  O    . HOH J 6 .   ? -32.91800 36.97900 36.20500 1.000 31.44558  ? 583 HOH A O    1 
HETATM 5189 O  O    . HOH J 6 .   ? -44.97800 29.55100 45.61800 1.000 60.89558  ? 584 HOH A O    1 
HETATM 5190 O  O    . HOH J 6 .   ? -23.17400 34.33700 59.28300 1.000 41.80558  ? 585 HOH A O    1 
HETATM 5191 O  O    . HOH J 6 .   ? 2.62200   13.90500 30.60900 1.000 57.23558  ? 586 HOH A O    1 
HETATM 5192 O  O    . HOH J 6 .   ? -7.45300  28.35500 30.15800 1.000 40.60558  ? 587 HOH A O    1 
HETATM 5193 O  O    . HOH J 6 .   ? -21.54500 14.63300 40.90100 1.000 32.70558  ? 588 HOH A O    1 
HETATM 5194 O  O    . HOH J 6 .   ? -34.73600 37.84000 60.64500 1.000 30.47558  ? 589 HOH A O    1 
HETATM 5195 O  O    . HOH J 6 .   ? 1.03800   15.92100 37.60300 1.000 50.76558  ? 590 HOH A O    1 
HETATM 5196 O  O    . HOH J 6 .   ? -28.46000 14.99800 40.67300 1.000 34.11558  ? 591 HOH A O    1 
HETATM 5197 O  O    . HOH J 6 .   ? -38.35300 40.21800 45.64200 1.000 34.64558  ? 592 HOH A O    1 
HETATM 5198 O  O    . HOH J 6 .   ? -49.93500 38.31100 53.85600 1.000 53.74558  ? 593 HOH A O    1 
HETATM 5199 O  O    . HOH J 6 .   ? -39.02000 23.82100 67.30000 1.000 32.79558  ? 594 HOH A O    1 
HETATM 5200 O  O    . HOH J 6 .   ? -40.46100 21.18200 53.53400 1.000 46.66558  ? 595 HOH A O    1 
HETATM 5201 O  O    . HOH J 6 .   ? -25.21900 24.28400 27.28100 1.000 30.71558  ? 596 HOH A O    1 
HETATM 5202 O  O    . HOH J 6 .   ? -33.48400 17.66200 52.96900 1.000 37.38558  ? 597 HOH A O    1 
HETATM 5203 O  O    . HOH J 6 .   ? -35.24300 14.72900 26.70700 1.000 42.26558  ? 598 HOH A O    1 
HETATM 5204 O  O    . HOH J 6 .   ? -32.79800 25.44700 14.94300 1.000 33.30558  ? 599 HOH A O    1 
HETATM 5205 O  O    . HOH J 6 .   ? -37.07600 32.60000 25.03300 1.000 30.82558  ? 600 HOH A O    1 
HETATM 5206 O  O    . HOH J 6 .   ? -27.34200 30.89500 15.26600 1.000 41.92558  ? 601 HOH A O    1 
HETATM 5207 O  O    . HOH J 6 .   ? -16.81900 22.31900 14.55000 1.000 43.26558  ? 602 HOH A O    1 
HETATM 5208 O  O    . HOH J 6 .   ? -5.15200  24.46500 32.22600 1.000 49.07558  ? 603 HOH A O    1 
HETATM 5209 O  O    . HOH J 6 .   ? -28.78400 37.43000 44.88700 1.000 34.41558  ? 604 HOH A O    1 
HETATM 5210 O  O    . HOH J 6 .   ? -39.87100 25.23700 43.51000 1.000 30.51558  ? 605 HOH A O    1 
HETATM 5211 O  O    . HOH J 6 .   ? -32.54900 14.77100 41.25400 1.000 36.85558  ? 606 HOH A O    1 
HETATM 5212 O  O    . HOH J 6 .   ? -31.58600 38.22000 45.24900 1.000 29.66558  ? 607 HOH A O    1 
HETATM 5213 O  O    . HOH J 6 .   ? -26.98700 12.99500 19.05800 1.000 34.91558  ? 608 HOH A O    1 
HETATM 5214 O  O    . HOH J 6 .   ? -35.29900 16.33300 33.90000 1.000 35.56558  ? 609 HOH A O    1 
HETATM 5215 O  O    . HOH J 6 .   ? -38.98600 27.88700 49.87100 1.000 41.22558  ? 610 HOH A O    1 
HETATM 5216 O  O    . HOH J 6 .   ? -29.53200 32.20700 17.14900 1.000 41.37558  ? 611 HOH A O    1 
HETATM 5217 O  O    . HOH J 6 .   ? -20.66900 13.68900 38.56400 1.000 37.05558  ? 612 HOH A O    1 
HETATM 5218 O  O    . HOH J 6 .   ? -33.90900 12.89400 29.65000 1.000 51.26558  ? 613 HOH A O    1 
HETATM 5219 O  O    . HOH J 6 .   ? -17.66800 33.24500 29.44900 1.000 42.63558  ? 614 HOH A O    1 
HETATM 5220 O  O    . HOH J 6 .   ? -15.40300 25.60200 30.90100 1.000 31.01558  ? 615 HOH A O    1 
HETATM 5221 O  O    . HOH J 6 .   ? -38.57800 41.84900 37.91800 1.000 54.61558  ? 616 HOH A O    1 
HETATM 5222 O  O    . HOH J 6 .   ? -51.59700 32.93200 70.09600 1.000 56.22558  ? 617 HOH A O    1 
HETATM 5223 O  O    . HOH J 6 .   ? -33.87800 18.07200 11.84100 1.000 41.31558  ? 618 HOH A O    1 
HETATM 5224 O  O    . HOH J 6 .   ? -45.07500 42.04000 51.14300 1.000 55.23558  ? 619 HOH A O    1 
HETATM 5225 O  O    . HOH J 6 .   ? -8.44300  5.55700  29.76800 1.000 51.80558  ? 620 HOH A O    1 
HETATM 5226 O  O    . HOH J 6 .   ? -16.74900 20.99300 43.74800 1.000 39.90558  ? 621 HOH A O    1 
HETATM 5227 O  O    . HOH J 6 .   ? -34.46600 23.37800 48.73100 1.000 27.18558  ? 622 HOH A O    1 
HETATM 5228 O  O    . HOH J 6 .   ? -42.48700 31.22900 53.94700 1.000 29.51558  ? 623 HOH A O    1 
HETATM 5229 O  O    . HOH J 6 .   ? -35.18600 26.11700 60.21200 1.000 29.69558  ? 624 HOH A O    1 
HETATM 5230 O  O    . HOH J 6 .   ? -28.58000 15.03100 26.06400 1.000 31.86558  ? 625 HOH A O    1 
HETATM 5231 O  O    . HOH J 6 .   ? -13.21300 32.64900 20.74600 1.000 45.38558  ? 626 HOH A O    1 
HETATM 5232 O  O    . HOH J 6 .   ? 5.27400   15.64900 30.99900 1.000 52.03558  ? 627 HOH A O    1 
HETATM 5233 O  O    . HOH J 6 .   ? -26.97200 35.62900 60.22600 1.000 44.35558  ? 628 HOH A O    1 
HETATM 5234 O  O    . HOH J 6 .   ? -35.59300 31.87800 29.34800 1.000 25.97558  ? 629 HOH A O    1 
HETATM 5235 O  O    . HOH J 6 .   ? -37.04600 23.97500 42.58200 1.000 24.64558  ? 630 HOH A O    1 
HETATM 5236 O  O    . HOH J 6 .   ? -10.73900 10.01000 21.86300 1.000 50.21558  ? 631 HOH A O    1 
HETATM 5237 O  O    . HOH J 6 .   ? -17.63000 17.64800 47.09900 1.000 38.55558  ? 632 HOH A O    1 
HETATM 5238 O  O    . HOH J 6 .   ? -39.27800 28.65800 69.24800 1.000 42.54558  ? 633 HOH A O    1 
HETATM 5239 O  O    . HOH J 6 .   ? -27.44100 13.58300 28.17700 1.000 31.32558  ? 634 HOH A O    1 
HETATM 5240 O  O    . HOH J 6 .   ? -36.14200 42.25200 35.60700 1.000 62.46558  ? 635 HOH A O    1 
HETATM 5241 O  O    . HOH J 6 .   ? -41.01700 25.21200 68.43700 1.000 28.84558  ? 636 HOH A O    1 
HETATM 5242 O  O    . HOH J 6 .   ? 15.557    23.356   23.983   1.000 66.55558  ? 637 HOH A O    1 
HETATM 5243 O  O    . HOH J 6 .   ? -28.12200 31.67300 70.09600 1.000 45.19558  ? 638 HOH A O    1 
HETATM 5244 O  O    . HOH J 6 .   ? -1.52200  12.55800 38.33100 1.000 54.94558  ? 639 HOH A O    1 
HETATM 5245 O  O    . HOH J 6 .   ? -13.01200 20.65200 29.99100 1.000 30.59558  ? 640 HOH A O    1 
HETATM 5246 O  O    . HOH J 6 .   ? -18.99800 35.65200 40.26400 1.000 43.57558  ? 641 HOH A O    1 
HETATM 5247 O  O    . HOH J 6 .   ? -20.79700 31.40500 29.10500 1.000 30.23558  ? 642 HOH A O    1 
HETATM 5248 O  O    . HOH J 6 .   ? -52.11900 35.05000 54.54900 1.000 51.01558  ? 643 HOH A O    1 
HETATM 5249 O  O    . HOH J 6 .   ? -28.81400 34.57300 55.55600 1.000 29.07558  ? 644 HOH A O    1 
HETATM 5250 O  O    . HOH J 6 .   ? -18.00300 30.65500 27.96700 1.000 34.31558  ? 645 HOH A O    1 
HETATM 5251 O  O    . HOH J 6 .   ? 7.81900   25.80300 21.75000 1.000 46.24558  ? 646 HOH A O    1 
HETATM 5252 O  O    . HOH J 6 .   ? -41.69900 35.15600 27.56000 1.000 33.56558  ? 647 HOH A O    1 
HETATM 5253 O  O    . HOH J 6 .   ? -4.88800  27.26500 28.98500 1.000 45.34558  ? 648 HOH A O    1 
HETATM 5254 O  O    . HOH J 6 .   ? -36.10000 15.52800 12.52800 1.000 53.93558  ? 649 HOH A O    1 
HETATM 5255 O  O    . HOH J 6 .   ? -25.91100 41.24800 42.68800 1.000 43.97558  ? 650 HOH A O    1 
HETATM 5256 O  O    . HOH J 6 .   ? -17.04800 29.96900 40.77200 1.000 45.24558  ? 651 HOH A O    1 
HETATM 5257 O  O    . HOH J 6 .   ? -30.68200 13.68700 47.16100 1.000 58.03558  ? 652 HOH A O    1 
HETATM 5258 O  O    . HOH J 6 .   ? -22.02400 15.54300 28.61700 1.000 43.25558  ? 653 HOH A O    1 
HETATM 5259 O  O    . HOH J 6 .   ? -33.10600 28.09500 26.55900 1.000 25.72558  ? 654 HOH A O    1 
HETATM 5260 O  O    . HOH J 6 .   ? -42.53000 44.50900 54.36000 1.000 40.47558  ? 655 HOH A O    1 
HETATM 5261 O  O    . HOH J 6 .   ? -31.47500 14.22200 29.57300 1.000 35.91558  ? 656 HOH A O    1 
HETATM 5262 O  O    . HOH J 6 .   ? -8.06200  30.93900 27.50800 1.000 45.37558  ? 657 HOH A O    1 
HETATM 5263 O  O    . HOH J 6 .   ? -22.64600 19.86100 56.53400 1.000 56.64558  ? 658 HOH A O    1 
HETATM 5264 O  O    . HOH J 6 .   ? -31.44600 16.42600 50.61800 1.000 41.61558  ? 659 HOH A O    1 
HETATM 5265 O  O    . HOH J 6 .   ? -40.50900 47.01300 61.09800 1.000 49.01558  ? 660 HOH A O    1 
HETATM 5266 O  O    . HOH J 6 .   ? -36.21300 34.54700 64.77700 1.000 51.66558  ? 661 HOH A O    1 
HETATM 5267 O  O    . HOH J 6 .   ? -19.34300 19.62000 17.01300 1.000 40.54558  ? 662 HOH A O    1 
HETATM 5268 O  O    . HOH J 6 .   ? -33.37800 15.38900 47.79800 1.000 45.35558  ? 663 HOH A O    1 
HETATM 5269 O  O    . HOH J 6 .   ? -37.73700 14.65500 40.11700 1.000 38.73558  ? 664 HOH A O    1 
HETATM 5270 O  O    . HOH J 6 .   ? -43.35600 25.06300 56.25900 1.000 37.01558  ? 665 HOH A O    1 
HETATM 5271 O  O    . HOH J 6 .   ? -37.04100 42.42600 44.09900 1.000 47.64558  ? 666 HOH A O    1 
HETATM 5272 O  O    . HOH J 6 .   ? -41.42000 32.84500 32.91900 1.000 29.47558  ? 667 HOH A O    1 
HETATM 5273 O  O    . HOH J 6 .   ? -42.95400 25.63100 25.55500 1.000 33.87558  ? 668 HOH A O    1 
HETATM 5274 O  O    . HOH J 6 .   ? -6.83300  27.42400 24.60400 1.000 40.37558  ? 669 HOH A O    1 
HETATM 5275 O  O    . HOH J 6 .   ? -29.51600 36.07800 30.38600 1.000 31.22558  ? 670 HOH A O    1 
HETATM 5276 O  O    . HOH J 6 .   ? 0.120     36.005   21.793   1.000 48.34558  ? 671 HOH A O    1 
HETATM 5277 O  O    . HOH J 6 .   ? -41.73700 17.33300 26.92900 1.000 39.38558  ? 672 HOH A O    1 
HETATM 5278 O  O    . HOH J 6 .   ? -44.61700 26.39500 35.21200 1.000 34.23558  ? 673 HOH A O    1 
HETATM 5279 O  O    . HOH J 6 .   ? -35.10100 27.94900 19.04600 1.000 35.94558  ? 674 HOH A O    1 
HETATM 5280 O  O    . HOH J 6 .   ? -13.72600 27.46500 32.20400 1.000 28.63558  ? 675 HOH A O    1 
HETATM 5281 O  O    . HOH J 6 .   ? -24.73000 18.23800 12.11500 1.000 35.48558  ? 676 HOH A O    1 
HETATM 5282 O  O    . HOH J 6 .   ? -22.62000 13.05800 32.02000 1.000 29.10558  ? 677 HOH A O    1 
HETATM 5283 O  O    . HOH J 6 .   ? 1.79100   27.20600 16.56400 1.000 53.24558  ? 678 HOH A O    1 
HETATM 5284 O  O    . HOH J 6 .   ? -14.83300 29.04900 16.33400 1.000 39.09558  ? 679 HOH A O    1 
HETATM 5285 O  O    . HOH J 6 .   ? 0.06100   19.11900 39.09600 1.000 50.02558  ? 680 HOH A O    1 
HETATM 5286 O  O    . HOH J 6 .   ? -42.49900 22.53300 56.51600 1.000 28.84558  ? 681 HOH A O    1 
HETATM 5287 O  O    . HOH J 6 .   ? 6.85000   23.40500 29.09900 1.000 55.05558  ? 682 HOH A O    1 
HETATM 5288 O  O    . HOH J 6 .   ? -22.08500 35.70100 35.75400 1.000 30.57558  ? 683 HOH A O    1 
HETATM 5289 O  O    . HOH J 6 .   ? -39.35400 31.88200 26.28500 1.000 27.13558  ? 684 HOH A O    1 
HETATM 5290 O  O    . HOH J 6 .   ? -20.74800 44.31000 30.99300 1.000 47.78558  ? 685 HOH A O    1 
HETATM 5291 O  O    . HOH J 6 .   ? -28.11400 37.24900 58.84000 1.000 38.78558  ? 686 HOH A O    1 
HETATM 5292 O  O    . HOH J 6 .   ? -16.79500 34.47100 14.79400 1.000 43.44558  ? 687 HOH A O    1 
HETATM 5293 O  O    . HOH J 6 .   ? -39.66900 40.16300 32.29900 1.000 34.70558  ? 688 HOH A O    1 
HETATM 5294 O  O    . HOH J 6 .   ? -37.40000 17.60400 46.78600 1.000 39.64558  ? 689 HOH A O    1 
HETATM 5295 O  O    . HOH J 6 .   ? 11.23500  18.58300 30.13200 1.000 51.74558  ? 690 HOH A O    1 
HETATM 5296 O  O    . HOH J 6 .   ? -31.59400 30.17700 26.94400 1.000 39.86558  ? 691 HOH A O    1 
HETATM 5297 O  O    . HOH J 6 .   ? -45.04600 22.28500 29.59700 1.000 35.84558  ? 692 HOH A O    1 
HETATM 5298 O  O    . HOH J 6 .   ? -27.55000 17.00200 37.47300 1.000 37.38558  ? 693 HOH A O    1 
HETATM 5299 O  O    . HOH J 6 .   ? -42.42900 28.57200 53.32300 1.000 35.80558  ? 694 HOH A O    1 
HETATM 5300 O  O    . HOH J 6 .   ? -54.49800 36.57300 71.84100 1.000 48.51558  ? 695 HOH A O    1 
HETATM 5301 O  O    . HOH J 6 .   ? -19.44900 8.22300  32.66200 1.000 43.23558  ? 696 HOH A O    1 
HETATM 5302 O  O    . HOH J 6 .   ? -46.96700 28.20200 55.55800 1.000 40.58558  ? 697 HOH A O    1 
HETATM 5303 O  O    . HOH J 6 .   ? -28.65400 11.65700 24.52100 1.000 58.09558  ? 698 HOH A O    1 
HETATM 5304 O  O    . HOH J 6 .   ? -40.51500 41.12500 44.27700 1.000 46.06558  ? 699 HOH A O    1 
HETATM 5305 O  O    . HOH J 6 .   ? -41.73000 26.04500 40.71200 1.000 30.24558  ? 700 HOH A O    1 
HETATM 5306 O  O    . HOH J 6 .   ? -30.28200 28.91900 69.60900 1.000 48.37558  ? 701 HOH A O    1 
HETATM 5307 O  O    . HOH J 6 .   ? -18.09100 8.06400  26.93400 1.000 57.21558  ? 702 HOH A O    1 
HETATM 5308 O  O    . HOH J 6 .   ? -32.36700 15.19900 26.92800 1.000 46.21558  ? 703 HOH A O    1 
HETATM 5309 O  O    . HOH J 6 .   ? -41.46400 27.20200 19.59800 1.000 32.48558  ? 704 HOH A O    1 
HETATM 5310 O  O    . HOH J 6 .   ? -23.01800 40.33200 40.93600 1.000 58.72558  ? 705 HOH A O    1 
HETATM 5311 O  O    . HOH J 6 .   ? -36.94300 30.84100 68.45700 1.000 51.34558  ? 706 HOH A O    1 
HETATM 5312 O  O    . HOH J 6 .   ? -0.41600  7.91800  27.74800 1.000 60.87558  ? 707 HOH A O    1 
HETATM 5313 O  O    . HOH J 6 .   ? -41.50600 41.43300 48.66000 1.000 37.13558  ? 708 HOH A O    1 
HETATM 5314 O  O    . HOH J 6 .   ? -28.78900 14.20600 33.95200 1.000 39.99558  ? 709 HOH A O    1 
HETATM 5315 O  O    . HOH J 6 .   ? 6.39900   17.39200 34.41700 1.000 51.83558  ? 710 HOH A O    1 
HETATM 5316 O  O    . HOH J 6 .   ? -20.59000 13.77300 23.80500 1.000 32.98558  ? 711 HOH A O    1 
HETATM 5317 O  O    . HOH J 6 .   ? -26.81400 43.59200 34.78300 0.800 39.10558  ? 712 HOH A O    1 
HETATM 5318 O  O    . HOH J 6 .   ? -4.51300  25.76300 18.91800 1.000 52.06558  ? 713 HOH A O    1 
HETATM 5319 O  O    . HOH J 6 .   ? -17.27200 12.88700 41.53600 1.000 37.87558  ? 714 HOH A O    1 
HETATM 5320 O  O    . HOH J 6 .   ? 10.468    35.775   27.949   1.000 55.86558  ? 715 HOH A O    1 
HETATM 5321 O  O    . HOH J 6 .   ? -13.93100 20.68600 43.09300 1.000 40.16558  ? 716 HOH A O    1 
HETATM 5322 O  O    . HOH J 6 .   ? -13.01600 26.94000 19.71800 1.000 32.50558  ? 717 HOH A O    1 
HETATM 5323 O  O    . HOH J 6 .   ? -8.93300  6.16300  26.13700 1.000 46.44558  ? 718 HOH A O    1 
HETATM 5324 O  O    . HOH J 6 .   ? -33.42200 39.06800 43.25200 1.000 28.15558  ? 719 HOH A O    1 
HETATM 5325 O  O    . HOH J 6 .   ? -27.43000 27.13900 11.75500 1.000 41.20558  ? 720 HOH A O    1 
HETATM 5326 O  O    . HOH J 6 .   ? -29.55600 23.43700 64.99200 1.000 41.87558  ? 721 HOH A O    1 
HETATM 5327 O  O    . HOH J 6 .   ? -49.85200 45.73000 58.43100 1.000 47.66558  ? 722 HOH A O    1 
HETATM 5328 O  O    . HOH J 6 .   ? -39.93800 18.29300 9.71000  1.000 48.44558  ? 723 HOH A O    1 
HETATM 5329 O  O    . HOH J 6 .   ? -23.03600 33.85800 37.59000 1.000 39.08558  ? 724 HOH A O    1 
HETATM 5330 O  O    . HOH J 6 .   ? -39.60800 45.56900 53.71500 1.000 51.69558  ? 725 HOH A O    1 
HETATM 5331 O  O    . HOH J 6 .   ? -42.07200 28.21200 46.42900 1.000 56.42558  ? 726 HOH A O    1 
HETATM 5332 O  O    . HOH J 6 .   ? -14.99200 10.17000 37.36000 1.000 43.41558  ? 727 HOH A O    1 
HETATM 5333 O  O    . HOH J 6 .   ? 7.92100   12.43400 23.42200 1.000 59.75558  ? 728 HOH A O    1 
HETATM 5334 O  O    . HOH J 6 .   ? -7.82700  25.18500 35.80300 1.000 49.53558  ? 729 HOH A O    1 
HETATM 5335 O  O    . HOH J 6 .   ? -34.88800 32.55800 26.78900 1.000 27.91558  ? 730 HOH A O    1 
HETATM 5336 O  O    . HOH J 6 .   ? -27.27700 13.80000 37.27700 1.000 34.59558  ? 731 HOH A O    1 
HETATM 5337 O  O    . HOH J 6 .   ? -32.40900 21.36000 8.73700  1.000 45.66558  ? 732 HOH A O    1 
HETATM 5338 O  O    . HOH J 6 .   ? -16.40200 25.53900 13.49300 1.000 38.69558  ? 733 HOH A O    1 
HETATM 5339 O  O    . HOH J 6 .   ? -8.88000  26.72600 31.61600 1.000 34.28558  ? 734 HOH A O    1 
HETATM 5340 O  O    . HOH J 6 .   ? -37.17900 13.64300 35.42800 1.000 49.72558  ? 735 HOH A O    1 
HETATM 5341 O  O    . HOH J 6 .   ? -40.59600 15.65400 34.40700 1.000 50.19558  ? 736 HOH A O    1 
HETATM 5342 O  O    . HOH J 6 .   ? -29.79500 22.49500 8.86500  1.000 46.68558  ? 737 HOH A O    1 
HETATM 5343 O  O    . HOH J 6 .   ? -43.963   18.794   26.568   1.000 43.00558  ? 738 HOH A O    1 
HETATM 5344 O  O    . HOH J 6 .   ? -21.40800 46.97200 31.24500 1.000 60.42558  ? 739 HOH A O    1 
HETATM 5345 O  O    . HOH J 6 .   ? -7.78500  10.76200 20.80000 1.000 52.90558  ? 740 HOH A O    1 
HETATM 5346 O  O    . HOH J 6 .   ? -4.61200  10.23700 21.49000 1.000 54.95558  ? 741 HOH A O    1 
HETATM 5347 O  O    . HOH J 6 .   ? -21.34300 36.75000 28.81400 1.000 56.31558  ? 742 HOH A O    1 
HETATM 5348 O  O    . HOH J 6 .   ? -35.90200 13.70400 28.87000 1.000 45.49558  ? 743 HOH A O    1 
HETATM 5349 O  O    . HOH J 6 .   ? -37.26000 18.55000 51.59800 1.000 64.27558  ? 744 HOH A O    1 
HETATM 5350 O  O    . HOH J 6 .   ? -33.84700 26.01200 12.49800 1.000 50.82558  ? 745 HOH A O    1 
HETATM 5351 O  O    . HOH J 6 .   ? -11.26000 16.94700 44.53500 1.000 55.45558  ? 746 HOH A O    1 
HETATM 5352 O  O    . HOH J 6 .   ? -15.00600 18.26600 19.15200 1.000 49.47558  ? 747 HOH A O    1 
HETATM 5353 O  O    . HOH J 6 .   ? -36.48100 22.28300 10.28200 1.000 47.55558  ? 748 HOH A O    1 
HETATM 5354 O  O    . HOH J 6 .   ? -9.99100  31.74600 23.22500 1.000 53.94558  ? 749 HOH A O    1 
HETATM 5355 O  O    . HOH J 6 .   ? -4.51000  12.80000 20.27800 1.000 54.84558  ? 750 HOH A O    1 
HETATM 5356 O  O    . HOH J 6 .   ? -26.21000 25.62100 68.11100 1.000 50.70558  ? 751 HOH A O    1 
HETATM 5357 O  O    . HOH J 6 .   ? -28.91000 10.19100 16.68100 1.000 63.26558  ? 752 HOH A O    1 
HETATM 5358 O  O    . HOH J 6 .   ? -39.103   14.212   11.466   1.000 58.65558  ? 753 HOH A O    1 
HETATM 5359 O  O    . HOH J 6 .   ? -29.57900 26.20400 12.03700 1.000 53.95558  ? 754 HOH A O    1 
HETATM 5360 O  O    . HOH J 6 .   ? -40.50800 13.52400 40.72900 1.000 55.92558  ? 755 HOH A O    1 
HETATM 5361 O  O    . HOH J 6 .   ? 3.00700   27.57100 29.24700 1.000 46.32558  ? 756 HOH A O    1 
HETATM 5362 O  O    . HOH J 6 .   ? -34.95200 43.29100 47.32000 1.000 62.22558  ? 757 HOH A O    1 
HETATM 5363 O  O    . HOH J 6 .   ? -31.83300 40.95200 49.26300 1.000 41.55558  ? 758 HOH A O    1 
HETATM 5364 O  O    . HOH J 6 .   ? -38.52500 24.69400 50.33600 1.000 48.76558  ? 759 HOH A O    1 
HETATM 5365 O  O    . HOH J 6 .   ? -50.73500 44.78400 55.63800 1.000 61.51558  ? 760 HOH A O    1 
HETATM 5366 O  O    . HOH J 6 .   ? -11.323   26.608   33.118   1.000 33.12558  ? 761 HOH A O    1 
HETATM 5367 O  O    . HOH J 6 .   ? -26.46500 15.48600 52.01100 1.000 67.12558  ? 762 HOH A O    1 
HETATM 5368 O  O    . HOH J 6 .   ? -6.94100  12.42900 19.37000 1.000 54.82558  ? 763 HOH A O    1 
HETATM 5369 O  O    . HOH J 6 .   ? -36.86700 22.58500 47.46900 1.000 33.98558  ? 764 HOH A O    1 
HETATM 5370 O  O    . HOH J 6 .   ? -19.66800 22.52700 52.89600 1.000 45.49558  ? 765 HOH A O    1 
HETATM 5371 O  O    . HOH J 6 .   ? -36.191   25.747   11.791   1.000 43.93558  ? 766 HOH A O    1 
HETATM 5372 O  O    . HOH J 6 .   ? -27.19600 39.59800 44.75400 1.000 42.03558  ? 767 HOH A O    1 
HETATM 5373 O  O    . HOH J 6 .   ? -42.57900 26.13000 43.35500 1.000 46.88558  ? 768 HOH A O    1 
HETATM 5374 O  O    . HOH J 6 .   ? -26.81900 12.33700 32.25000 1.000 54.63558  ? 769 HOH A O    1 
HETATM 5375 O  O    . HOH J 6 .   ? -30.31300 14.31800 38.85200 1.000 40.08558  ? 770 HOH A O    1 
HETATM 5376 O  O    . HOH J 6 .   ? -32.38300 14.46100 45.66600 1.000 48.64558  ? 771 HOH A O    1 
HETATM 5377 O  O    . HOH J 6 .   ? -21.78000 12.36400 22.16800 1.000 56.27558  ? 772 HOH A O    1 
HETATM 5378 O  O    . HOH J 6 .   ? -41.23800 14.48300 25.87400 1.000 47.73558  ? 773 HOH A O    1 
HETATM 5379 O  O    . HOH J 6 .   ? -30.75600 11.48700 38.63300 1.000 55.00558  ? 774 HOH A O    1 
HETATM 5380 O  O    . HOH J 6 .   ? -30.21400 20.13100 56.40700 1.000 35.03558  ? 775 HOH A O    1 
HETATM 5381 O  O    . HOH J 6 .   ? -42.20500 37.63800 35.49500 1.000 54.02558  ? 776 HOH A O    1 
HETATM 5382 O  O    . HOH J 6 .   ? -41.84600 14.50600 42.28600 1.000 55.10558  ? 777 HOH A O    1 
HETATM 5383 O  O    . HOH J 6 .   ? -30.63100 20.84500 60.36300 1.000 39.27558  ? 778 HOH A O    1 
HETATM 5384 O  O    . HOH J 6 .   ? -37.70900 13.60900 37.81000 1.000 47.76558  ? 779 HOH A O    1 
HETATM 5385 O  O    . HOH J 6 .   ? -35.95200 44.57900 60.75900 1.000 50.45558  ? 780 HOH A O    1 
HETATM 5386 O  O    . HOH J 6 .   ? -25.76400 33.87400 58.75400 1.000 43.76558  ? 781 HOH A O    1 
HETATM 5387 O  O    . HOH J 6 .   ? -1.07800  30.69000 18.49900 1.000 63.22558  ? 782 HOH A O    1 
HETATM 5388 O  O    . HOH J 6 .   ? -29.75000 31.38500 14.99700 1.000 49.03558  ? 783 HOH A O    1 
HETATM 5389 O  O    . HOH J 6 .   ? -37.83100 46.25800 61.27200 1.000 59.71558  ? 784 HOH A O    1 
HETATM 5390 O  O    . HOH J 6 .   ? -36.48300 43.23600 39.32700 1.000 59.49558  ? 785 HOH A O    1 
HETATM 5391 O  O    . HOH J 6 .   ? -18.19600 12.86800 39.14400 1.000 41.46558  ? 786 HOH A O    1 
HETATM 5392 O  O    . HOH J 6 .   ? -29.26200 21.52400 62.73300 1.000 44.03558  ? 787 HOH A O    1 
HETATM 5393 O  O    . HOH J 6 .   ? -0.894    37.485   19.262   1.000 36.91558  ? 788 HOH A O    1 
HETATM 5394 O  O    . HOH J 6 .   ? -39.04200 13.32200 25.69900 1.000 48.24558  ? 789 HOH A O    1 
HETATM 5395 O  O    . HOH J 6 .   ? -34.48100 41.33900 43.50200 1.000 48.15558  ? 790 HOH A O    1 
HETATM 5396 O  O    . HOH J 6 .   ? -31.42400 40.63400 46.63400 1.000 31.27558  ? 791 HOH A O    1 
HETATM 5397 O  O    . HOH J 6 .   ? -45.75500 26.55000 30.94300 1.000 52.27558  ? 792 HOH A O    1 
HETATM 5398 O  O    . HOH J 6 .   ? -38.16600 20.63600 51.79000 1.000 51.39558  ? 793 HOH A O    1 
HETATM 5399 O  O    . HOH J 6 .   ? -35.05700 12.76200 24.68000 1.000 46.47558  ? 794 HOH A O    1 
HETATM 5400 O  O    . HOH J 6 .   ? -36.02900 14.98500 47.35600 1.000 49.62558  ? 795 HOH A O    1 
HETATM 5401 O  O    . HOH J 6 .   ? -36.97000 34.52000 19.23800 1.000 47.15558  ? 796 HOH A O    1 
HETATM 5402 O  O    . HOH J 6 .   ? -40.52400 13.69000 36.83000 1.000 60.11558  ? 797 HOH A O    1 
HETATM 5403 O  O    . HOH J 6 .   ? -38.92400 12.36300 33.88000 1.000 59.96558  ? 798 HOH A O    1 
HETATM 5404 O  O    . HOH J 6 .   ? -7.46100  24.58400 32.90000 1.000 46.89558  ? 799 HOH A O    1 
HETATM 5405 O  O    . HOH J 6 .   ? -7.435    31.552   24.187   1.000 48.12558  ? 800 HOH A O    1 
HETATM 5406 O  O    . HOH J 6 .   ? -38.04600 20.40700 48.87700 1.000 42.88558  ? 801 HOH A O    1 
HETATM 5407 O  O    . HOH J 6 .   ? -40.37800 44.31900 49.18000 1.000 58.90558  ? 802 HOH A O    1 
HETATM 5408 O  O    . HOH J 6 .   ? -29.53600 12.35000 29.35200 1.000 55.04558  ? 803 HOH A O    1 
HETATM 5409 O  O    . HOH J 6 .   ? -32.82700 42.44400 45.52300 1.000 45.33558  ? 804 HOH A O    1 
HETATM 5410 O  O    . HOH J 6 .   ? -40.53600 18.95200 54.57300 1.000 54.13558  ? 805 HOH A O    1 
HETATM 5411 O  O    . HOH J 6 .   ? -43.23100 28.14000 44.34900 1.000 57.08558  ? 806 HOH A O    1 
HETATM 5412 O  O    . HOH J 6 .   ? -41.00900 17.10600 43.35900 1.000 51.99558  ? 807 HOH A O    1 
HETATM 5413 O  O    . HOH J 6 .   ? -27.67300 23.42100 67.04500 1.000 49.76558  ? 808 HOH A O    1 
HETATM 5414 O  O    . HOH J 6 .   ? -16.02000 14.06200 17.60400 1.000 49.51558  ? 809 HOH A O    1 
HETATM 5415 O  O    . HOH J 6 .   ? -12.54900 30.61100 19.42200 1.000 45.74558  ? 810 HOH A O    1 
HETATM 5416 O  O    . HOH J 6 .   ? -35.222   28.469   12.604   1.000 51.80558  ? 811 HOH A O    1 
HETATM 5417 O  O    . HOH J 6 .   ? -23.841   26.044   68.185   1.000 47.78558  ? 812 HOH A O    1 
HETATM 5418 O  O    . HOH J 6 .   ? -44.58500 28.40900 29.12700 1.000 46.25558  ? 813 HOH A O    1 
HETATM 5419 O  O    . HOH J 6 .   ? -43.88500 26.81200 39.42400 1.000 44.85558  ? 814 HOH A O    1 
HETATM 5420 O  O    . HOH J 6 .   ? -25.87800 16.86000 54.21300 1.000 50.09558  ? 815 HOH A O    1 
HETATM 5421 O  O    . HOH J 6 .   ? -40.05700 17.06100 46.03100 1.000 45.40558  ? 816 HOH A O    1 
HETATM 5422 O  O    . HOH J 6 .   ? -14.51200 29.02000 19.02600 1.000 36.36558  ? 817 HOH A O    1 
HETATM 5423 O  O    . HOH J 6 .   ? -9.70600  7.24000  22.95300 1.000 56.74558  ? 818 HOH A O    1 
HETATM 5424 O  O    . HOH J 6 .   ? -44.75900 27.20300 26.93900 1.000 37.64558  ? 819 HOH A O    1 
HETATM 5425 O  O    . HOH J 6 .   ? -31.96200 18.45900 55.21500 1.000 41.14558  ? 820 HOH A O    1 
HETATM 5426 O  O    . HOH J 6 .   ? 5.56000   25.97100 28.69700 1.000 45.42558  ? 821 HOH A O    1 
HETATM 5427 O  O    . HOH J 6 .   ? -27.13100 19.77800 62.83600 1.000 52.79558  ? 822 HOH A O    1 
HETATM 5428 O  O    . HOH J 6 .   ? -31.631   17.578   63.751   1.000 49.41558  ? 823 HOH A O    1 
HETATM 5429 O  O    . HOH J 6 .   ? -28.76700 41.57400 46.44800 1.000 42.85558  ? 824 HOH A O    1 
HETATM 5430 O  O    . HOH J 6 .   ? -21.157   48.031   33.797   1.000 54.99558  ? 825 HOH A O    1 
HETATM 5431 O  O    . HOH J 6 .   ? -1.22500  36.13300 24.38100 1.000 54.40558  ? 826 HOH A O    1 
HETATM 5432 O  O    . HOH J 6 .   ? -46.64200 25.42000 27.67100 1.000 61.95558  ? 827 HOH A 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   . GLU A 2   ? 0.86238 0.84526 0.97437 -0.08907 0.12457  -0.04737 2   GLU A N   
2    C CA  . GLU A 2   ? 1.03051 1.01016 1.13596 -0.09145 0.12281  -0.04752 2   GLU A CA  
3    C C   . GLU A 2   ? 0.89293 0.87426 0.99747 -0.09034 0.12310  -0.04642 2   GLU A C   
4    O O   . GLU A 2   ? 0.85517 0.83902 0.96591 -0.08721 0.12368  -0.04352 2   GLU A O   
5    C CB  . GLU A 2   ? 0.98769 0.96400 1.09474 -0.09176 0.12063  -0.04485 2   GLU A CB  
6    C CG  . GLU A 2   ? 1.09657 1.06800 1.19537 -0.09481 0.11862  -0.04566 2   GLU A CG  
7    C CD  . GLU A 2   ? 0.99578 0.96331 1.09460 -0.09594 0.11656  -0.04468 2   GLU A CD  
8    O OE1 . GLU A 2   ? 0.87995 0.84789 0.98488 -0.09428 0.11546  -0.04130 2   GLU A OE1 
9    O OE2 . GLU A 2   ? 0.97019 0.93438 1.06300 -0.09848 0.11611  -0.04729 2   GLU A OE2 
15   N N   . VAL A 3   ? 0.70827 0.68803 0.80488 -0.09291 0.12284  -0.04866 3   VAL A N   
16   C CA  . VAL A 3   ? 0.93099 0.91215 1.02578 -0.09210 0.12339  -0.04798 3   VAL A CA  
17   C C   . VAL A 3   ? 0.83610 0.81264 0.92762 -0.09306 0.12145  -0.04553 3   VAL A C   
18   O O   . VAL A 3   ? 0.80919 0.78065 0.89349 -0.09630 0.11981  -0.04678 3   VAL A O   
19   C CB  . VAL A 3   ? 0.81394 0.79635 0.90179 -0.09446 0.12443  -0.05183 3   VAL A CB  
20   C CG1 . VAL A 3   ? 0.73792 0.72061 0.82233 -0.09419 0.12477  -0.05101 3   VAL A CG1 
21   C CG2 . VAL A 3   ? 1.03199 1.01948 1.12374 -0.09308 0.12636  -0.05396 3   VAL A CG2 
31   N N   . ARG A 4   ? 0.71139 0.68917 0.80762 -0.09031 0.12165  -0.04206 4   ARG A N   
32   C CA  . ARG A 4   ? 0.57118 0.54446 0.66446 -0.09108 0.11993  -0.03947 4   ARG A CA  
33   C C   . ARG A 4   ? 0.55791 0.53115 0.64629 -0.09093 0.12117  -0.03950 4   ARG A C   
34   O O   . ARG A 4   ? 0.53063 0.50903 0.62261 -0.08824 0.12347  -0.03962 4   ARG A O   
35   C CB  . ARG A 4   ? 0.65185 0.62622 0.75374 -0.08833 0.11931  -0.03521 4   ARG A CB  
38   N N   . THR A 5   ? 0.55441 0.52132 0.63389 -0.09378 0.11969  -0.03950 5   THR A N   
39   C CA  . THR A 5   ? 0.52874 0.49444 0.60197 -0.09401 0.12100  -0.03942 5   THR A CA  
40   C C   . THR A 5   ? 0.49896 0.45700 0.56662 -0.09511 0.11918  -0.03650 5   THR A C   
41   O O   . THR A 5   ? 0.53172 0.48464 0.59814 -0.09671 0.11637  -0.03565 5   THR A O   
42   C CB  . THR A 5   ? 0.69333 0.65768 0.75706 -0.09744 0.12141  -0.04338 5   THR A CB  
43   O OG1 . THR A 5   ? 0.63143 0.58747 0.68617 -0.10143 0.11864  -0.04441 5   THR A OG1 
44   C CG2 . THR A 5   ? 0.71507 0.68615 0.78333 -0.09695 0.12283  -0.04652 5   THR A CG2 
52   N N   . ILE A 6   ? 0.50551 0.46354 0.56537 -0.08871 0.11549  -0.03459 6   ILE A N   
53   C CA  . ILE A 6   ? 0.54850 0.49929 0.59561 -0.08460 0.10846  -0.03198 6   ILE A CA  
54   C C   . ILE A 6   ? 0.50466 0.45403 0.53820 -0.08022 0.10464  -0.03298 6   ILE A C   
55   O O   . ILE A 6   ? 0.52056 0.47573 0.55619 -0.07907 0.10718  -0.03487 6   ILE A O   
56   C CB  . ILE A 6   ? 0.58848 0.53996 0.64014 -0.08029 0.10719  -0.02747 6   ILE A CB  
57   C CG1 . ILE A 6   ? 0.47962 0.43780 0.53650 -0.07562 0.10989  -0.02651 6   ILE A CG1 
58   C CG2 . ILE A 6   ? 0.68496 0.63742 0.74958 -0.08429 0.11016  -0.02599 6   ILE A CG2 
59   C CD1 . ILE A 6   ? 0.54046 0.49821 0.59842 -0.07058 0.10778  -0.02198 6   ILE A CD1 
71   N N   . LYS A 7   ? 0.49382 0.43546 0.51367 -0.07783 0.09864  -0.03172 7   LYS A N   
72   C CA  . LYS A 7   ? 0.46304 0.40223 0.46951 -0.07301 0.09451  -0.03185 7   LYS A CA  
73   C C   . LYS A 7   ? 0.42403 0.36345 0.42897 -0.06671 0.09232  -0.02836 7   LYS A C   
74   O O   . LYS A 7   ? 0.44992 0.38584 0.45466 -0.06585 0.09024  -0.02547 7   LYS A O   
75   C CB  . LYS A 7   ? 0.48917 0.41914 0.48119 -0.07395 0.08974  -0.03241 7   LYS A CB  
76   C CG  . LYS A 7   ? 0.51284 0.43971 0.49079 -0.06920 0.08564  -0.03246 7   LYS A CG  
77   C CD  . LYS A 7   ? 0.56077 0.47760 0.52440 -0.06941 0.08107  -0.03221 7   LYS A CD  
78   C CE  . LYS A 7   ? 0.55862 0.47032 0.52049 -0.06829 0.07858  -0.02927 7   LYS A CE  
79   N NZ  . LYS A 7   ? 0.55908 0.46093 0.50671 -0.06865 0.07470  -0.02950 7   LYS A NZ  
93   N N   . VAL A 8   ? 0.44220 0.38559 0.44586 -0.06244 0.09276  -0.02873 8   VAL A N   
94   C CA  . VAL A 8   ? 0.43371 0.37601 0.43343 -0.05626 0.09042  -0.02581 8   VAL A CA  
95   C C   . VAL A 8   ? 0.38353 0.32417 0.37192 -0.05237 0.08755  -0.02696 8   VAL A C   
96   O O   . VAL A 8   ? 0.42336 0.36518 0.40874 -0.05431 0.08775  -0.02986 8   VAL A O   
97   C CB  . VAL A 8   ? 0.41768 0.36720 0.43036 -0.05437 0.09501  -0.02470 8   VAL A CB  
98   C CG1 . VAL A 8   ? 0.47175 0.42366 0.49696 -0.05838 0.09841  -0.02354 8   VAL A CG1 
99   C CG2 . VAL A 8   ? 0.47230 0.42917 0.49044 -0.05415 0.09908  -0.02790 8   VAL A CG2 
109  N N   . PHE A 9   ? 0.36340 0.30114 0.34545 -0.04694 0.08485  -0.02457 9   PHE A N   
110  C CA  . PHE A 9   ? 0.39173 0.32810 0.36433 -0.04263 0.08246  -0.02526 9   PHE A CA  
111  C C   . PHE A 9   ? 0.43350 0.37510 0.41209 -0.03826 0.08497  -0.02489 9   PHE A C   
112  O O   . PHE A 9   ? 0.43171 0.37341 0.41500 -0.03655 0.08607  -0.02245 9   PHE A O   
113  C CB  . PHE A 9   ? 0.36756 0.29450 0.32568 -0.04004 0.07716  -0.02308 9   PHE A CB  
114  C CG  . PHE A 9   ? 0.39775 0.31885 0.34927 -0.04407 0.07493  -0.02366 9   PHE A CG  
115  C CD1 . PHE A 9   ? 0.40211 0.32253 0.34834 -0.04597 0.07430  -0.02624 9   PHE A CD1 
116  C CD2 . PHE A 9   ? 0.43770 0.35415 0.38858 -0.04612 0.07360  -0.02177 9   PHE A CD2 
117  C CE1 . PHE A 9   ? 0.44076 0.35509 0.38061 -0.04984 0.07264  -0.02699 9   PHE A CE1 
118  C CE2 . PHE A 9   ? 0.50073 0.41150 0.44578 -0.04998 0.07191  -0.02269 9   PHE A CE2 
119  C CZ  . PHE A 9   ? 0.47253 0.38191 0.41196 -0.05188 0.07162  -0.02537 9   PHE A CZ  
129  N N   . THR A 10  ? 0.36893 0.31482 0.34727 -0.03647 0.08590  -0.02738 10  THR A N   
130  C CA  . THR A 10  ? 0.37385 0.32362 0.35594 -0.03178 0.08788  -0.02743 10  THR A CA  
131  C C   . THR A 10  ? 0.38757 0.33194 0.35743 -0.02685 0.08368  -0.02657 10  THR A C   
132  O O   . THR A 10  ? 0.38629 0.32575 0.34579 -0.02717 0.07987  -0.02662 10  THR A O   
133  C CB  . THR A 10  ? 0.40512 0.36458 0.39747 -0.03313 0.09262  -0.03113 10  THR A CB  
134  O OG1 . THR A 10  ? 0.39754 0.35805 0.38463 -0.03512 0.09082  -0.03375 10  THR A OG1 
135  C CG2 . THR A 10  ? 0.41178 0.37658 0.41761 -0.03764 0.09786  -0.03170 10  THR A CG2 
143  N N   . THR A 11  ? 0.37411 0.31899 0.34534 -0.02224 0.08474  -0.02569 11  THR A N   
144  C CA  . THR A 11  ? 0.37698 0.31614 0.33755 -0.01738 0.08134  -0.02451 11  THR A CA  
145  C C   . THR A 11  ? 0.38837 0.33118 0.35461 -0.01316 0.08438  -0.02514 11  THR A C   
146  O O   . THR A 11  ? 0.34720 0.29507 0.32414 -0.01376 0.08873  -0.02557 11  THR A O   
147  C CB  . THR A 11  ? 0.37043 0.30008 0.32139 -0.01664 0.07775  -0.02091 11  THR A CB  
148  O OG1 . THR A 11  ? 0.39521 0.31888 0.33505 -0.01259 0.07461  -0.02006 11  THR A OG1 
149  C CG2 . THR A 11  ? 0.35363 0.28310 0.31029 -0.01563 0.07985  -0.01861 11  THR A CG2 
157  N N   . VAL A 12  ? 0.36553 0.30564 0.32480 -0.00891 0.08238  -0.02532 12  VAL A N   
158  C CA  . VAL A 12  ? 0.40282 0.34310 0.36460 -0.00435 0.08453  -0.02525 12  VAL A CA  
159  C C   . VAL A 12  ? 0.41626 0.34666 0.36709 -0.00098 0.08140  -0.02209 12  VAL A C   
160  O O   . VAL A 12  ? 0.40757 0.33633 0.35978 0.00234  0.08328  -0.02143 12  VAL A O   
161  C CB  . VAL A 12  ? 0.38045 0.32717 0.34597 -0.00197 0.08604  -0.02873 12  VAL A CB  
162  C CG1 . VAL A 12  ? 0.41025 0.36733 0.38799 -0.00540 0.09030  -0.03209 12  VAL A CG1 
163  C CG2 . VAL A 12  ? 0.45294 0.39674 0.40844 -0.00077 0.08153  -0.02892 12  VAL A CG2 
173  N N   . ASP A 13  ? 0.44725 0.37066 0.38709 -0.00188 0.07707  -0.02026 13  ASP A N   
174  C CA  . ASP A 13  ? 0.44029 0.35417 0.36923 0.00101  0.07443  -0.01750 13  ASP A CA  
175  C C   . ASP A 13  ? 0.47497 0.38210 0.39717 -0.00166 0.07187  -0.01464 13  ASP A C   
176  O O   . ASP A 13  ? 0.46561 0.36459 0.37833 0.00015  0.06984  -0.01236 13  ASP A O   
177  C CB  . ASP A 13  ? 0.43504 0.34567 0.35529 0.00374  0.07177  -0.01803 13  ASP A CB  
178  C CG  . ASP A 13  ? 0.44831 0.35892 0.36370 0.00087  0.06901  -0.01869 13  ASP A CG  
179  O OD1 . ASP A 13  ? 0.46032 0.37079 0.37636 -0.00332 0.06853  -0.01830 13  ASP A OD1 
180  O OD2 . ASP A 13  ? 0.49048 0.40097 0.40129 0.00290  0.06735  -0.01956 13  ASP A OD2 
185  N N   . ASN A 14  ? 0.39193 0.30226 0.31919 -0.00603 0.07221  -0.01480 14  ASN A N   
186  C CA  . ASN A 14  ? 0.39743 0.30244 0.31983 -0.00902 0.06990  -0.01248 14  ASN A CA  
187  C C   . ASN A 14  ? 0.42959 0.32706 0.33906 -0.00946 0.06605  -0.01191 14  ASN A C   
188  O O   . ASN A 14  ? 0.44005 0.33146 0.34307 -0.01114 0.06390  -0.00995 14  ASN A O   
189  C CB  . ASN A 14  ? 0.45221 0.35343 0.37378 -0.00761 0.07010  -0.00960 14  ASN A CB  
190  C CG  . ASN A 14  ? 0.54204 0.44281 0.46593 -0.01140 0.06927  -0.00779 14  ASN A CG  
191  O OD1 . ASN A 14  ? 0.47682 0.38280 0.40850 -0.01489 0.07046  -0.00897 14  ASN A OD1 
192  N ND2 . ASN A 14  ? 0.57143 0.46591 0.48851 -0.01095 0.06721  -0.00498 14  ASN A ND2 
199  N N   . ILE A 15  ? 0.41329 0.31114 0.31894 -0.00795 0.06526  -0.01360 15  ILE A N   
200  C CA  . ILE A 15  ? 0.40195 0.29292 0.29565 -0.00816 0.06211  -0.01317 15  ILE A CA  
201  C C   . ILE A 15  ? 0.48144 0.37676 0.37723 -0.01092 0.06193  -0.01559 15  ILE A C   
202  O O   . ILE A 15  ? 0.44648 0.33894 0.33872 -0.01459 0.06063  -0.01571 15  ILE A O   
203  C CB  . ILE A 15  ? 0.46162 0.34789 0.34747 -0.00332 0.06117  -0.01242 15  ILE A CB  
204  C CG1 . ILE A 15  ? 0.43382 0.31477 0.31673 -0.00123 0.06154  -0.01007 15  ILE A CG1 
205  C CG2 . ILE A 15  ? 0.51568 0.39532 0.38985 -0.00336 0.05845  -0.01201 15  ILE A CG2 
206  C CD1 . ILE A 15  ? 0.49603 0.37357 0.37443 0.00363  0.06183  -0.00967 15  ILE A CD1 
218  N N   . ASN A 16  ? 0.44034 0.34272 0.34216 -0.00941 0.06341  -0.01773 16  ASN A N   
219  C CA  . ASN A 16  ? 0.40215 0.30944 0.30613 -0.01202 0.06339  -0.02021 16  ASN A CA  
220  C C   . ASN A 16  ? 0.40663 0.32109 0.32257 -0.01641 0.06640  -0.02184 16  ASN A C   
221  O O   . ASN A 16  ? 0.43496 0.35568 0.36109 -0.01561 0.06953  -0.02253 16  ASN A O   
222  C CB  . ASN A 16  ? 0.49672 0.40867 0.40155 -0.00841 0.06342  -0.02177 16  ASN A CB  
223  C CG  . ASN A 16  ? 0.70995 0.61446 0.60329 -0.00406 0.06066  -0.01991 16  ASN A CG  
224  O OD1 . ASN A 16  ? 0.76883 0.66867 0.65314 -0.00453 0.05819  -0.01946 16  ASN A OD1 
225  N ND2 . ASN A 16  ? 0.65412 0.55695 0.54769 0.00013  0.06141  -0.01879 16  ASN A ND2 
232  N N   . LEU A 17  ? 0.41330 0.32642 0.32811 -0.02109 0.06583  -0.02248 17  LEU A N   
233  C CA  . LEU A 17  ? 0.39272 0.31118 0.31835 -0.02584 0.06875  -0.02370 17  LEU A CA  
234  C C   . LEU A 17  ? 0.45423 0.37888 0.38401 -0.02900 0.07015  -0.02693 17  LEU A C   
235  O O   . LEU A 17  ? 0.46774 0.39027 0.38941 -0.02868 0.06783  -0.02778 17  LEU A O   
236  C CB  . LEU A 17  ? 0.40328 0.31553 0.32558 -0.02941 0.06747  -0.02226 17  LEU A CB  
237  C CG  . LEU A 17  ? 0.44449 0.35008 0.36113 -0.02691 0.06561  -0.01908 17  LEU A CG  
238  C CD1 . LEU A 17  ? 0.50240 0.40335 0.41741 -0.03087 0.06454  -0.01809 17  LEU A CD1 
239  C CD2 . LEU A 17  ? 0.43717 0.34744 0.36260 -0.02439 0.06805  -0.01802 17  LEU A CD2 
251  N N   . HIS A 18  ? 0.42307 0.35523 0.36539 -0.03222 0.07413  -0.02862 18  HIS A N   
252  C CA  . HIS A 18  ? 0.43278 0.37178 0.38058 -0.03588 0.07632  -0.03198 18  HIS A CA  
253  C C   . HIS A 18  ? 0.44124 0.38175 0.39728 -0.04187 0.07927  -0.03273 18  HIS A C   
254  O O   . HIS A 18  ? 0.41104 0.35503 0.37735 -0.04246 0.08254  -0.03203 18  HIS A O   
255  C CB  . HIS A 18  ? 0.44129 0.38945 0.39766 -0.03348 0.07930  -0.03395 18  HIS A CB  
256  C CG  . HIS A 18  ? 0.45170 0.39849 0.40090 -0.02760 0.07654  -0.03333 18  HIS A CG  
257  N ND1 . HIS A 18  ? 0.55975 0.50726 0.50222 -0.02663 0.07398  -0.03466 18  HIS A ND1 
258  C CD2 . HIS A 18  ? 0.45594 0.40007 0.40328 -0.02242 0.07588  -0.03133 18  HIS A CD2 
259  C CE1 . HIS A 18  ? 0.54614 0.49196 0.48381 -0.02098 0.07200  -0.03352 18  HIS A CE1 
260  N NE2 . HIS A 18  ? 0.53067 0.47420 0.47113 -0.01848 0.07327  -0.03164 18  HIS A NE2 
269  N N   . THR A 19  ? 0.41431 0.35177 0.36583 -0.04627 0.07827  -0.03403 19  THR A N   
270  C CA  . THR A 19  ? 0.40541 0.34311 0.36419 -0.05223 0.08100  -0.03478 19  THR A CA  
271  C C   . THR A 19  ? 0.47832 0.42597 0.45111 -0.05539 0.08648  -0.03742 19  THR A C   
272  O O   . THR A 19  ? 0.47187 0.42515 0.44547 -0.05559 0.08750  -0.04003 19  THR A O   
273  C CB  . THR A 19  ? 0.41995 0.35162 0.37017 -0.05637 0.07904  -0.03606 19  THR A CB  
274  O OG1 . THR A 19  ? 0.45657 0.37906 0.39285 -0.05322 0.07430  -0.03399 19  THR A OG1 
275  C CG2 . THR A 19  ? 0.47988 0.41029 0.43724 -0.06225 0.08164  -0.03651 19  THR A CG2 
283  N N   . GLN A 20  ? 0.41685 0.36675 0.40079 -0.05806 0.09013  -0.03676 20  GLN A N   
284  C CA  . GLN A 20  ? 0.43009 0.38889 0.42826 -0.06161 0.09622  -0.03912 20  GLN A CA  
285  C C   . GLN A 20  ? 0.49271 0.45021 0.49826 -0.06769 0.09903  -0.03923 20  GLN A C   
286  O O   . GLN A 20  ? 0.49443 0.44629 0.49860 -0.06759 0.09715  -0.03655 20  GLN A O   
287  C CB  . GLN A 20  ? 0.43727 0.40179 0.44492 -0.05774 0.09938  -0.03795 20  GLN A CB  
288  C CG  . GLN A 20  ? 0.42374 0.38937 0.42568 -0.05140 0.09716  -0.03771 20  GLN A CG  
289  C CD  . GLN A 20  ? 0.50882 0.47974 0.50896 -0.05175 0.09744  -0.04124 20  GLN A CD  
290  O OE1 . GLN A 20  ? 0.50780 0.48395 0.51398 -0.05684 0.10085  -0.04431 20  GLN A OE1 
291  N NE2 . GLN A 20  ? 0.57270 0.54241 0.56461 -0.04644 0.09390  -0.04084 20  GLN A NE2 
300  N N   . VAL A 21  ? 0.46417 0.42703 0.47783 -0.07311 0.10368  -0.04241 21  VAL A N   
301  C CA  . VAL A 21  ? 0.45867 0.42158 0.48221 -0.07920 0.10775  -0.04283 21  VAL A CA  
302  C C   . VAL A 21  ? 0.55417 0.52620 0.59350 -0.07989 0.11446  -0.04349 21  VAL A C   
303  O O   . VAL A 21  ? 0.57876 0.55779 0.62235 -0.08117 0.11799  -0.04662 21  VAL A O   
304  C CB  . VAL A 21  ? 0.60631 0.56711 0.62653 -0.08568 0.10845  -0.04612 21  VAL A CB  
305  C CG1 . VAL A 21  ? 0.64394 0.60518 0.67599 -0.09225 0.11353  -0.04683 21  VAL A CG1 
306  C CG2 . VAL A 21  ? 0.70817 0.65926 0.71225 -0.08456 0.10207  -0.04533 21  VAL A CG2 
316  N N   . VAL A 22  ? 0.48299 0.45516 0.53082 -0.07882 0.11626  -0.04053 22  VAL A N   
317  C CA  . VAL A 22  ? 0.48148 0.46158 0.54381 -0.07837 0.12263  -0.04046 22  VAL A CA  
318  C C   . VAL A 22  ? 0.55562 0.53765 0.63114 -0.08472 0.12836  -0.04093 22  VAL A C   
319  O O   . VAL A 22  ? 0.57281 0.54919 0.64753 -0.08747 0.12652  -0.03945 22  VAL A O   
320  C CB  . VAL A 22  ? 0.53033 0.50992 0.59352 -0.07187 0.12117  -0.03649 22  VAL A CB  
321  C CG1 . VAL A 22  ? 0.57231 0.55062 0.62407 -0.06587 0.11671  -0.03648 22  VAL A CG1 
322  C CG2 . VAL A 22  ? 0.51784 0.49073 0.57888 -0.07158 0.11756  -0.03260 22  VAL A CG2 
332  N N   . ASP A 23  ? 0.51692 0.50570 0.60084 -0.08338 0.13070  -0.04269 23  ASP A N   
333  C CA  . ASP A 23  ? 0.53101 0.52073 0.62210 -0.08294 0.12955  -0.04243 23  ASP A CA  
334  C C   . ASP A 23  ? 0.54542 0.53582 0.64436 -0.07891 0.12991  -0.03821 23  ASP A C   
335  O O   . ASP A 23  ? 0.58557 0.57947 0.68785 -0.07499 0.13185  -0.03717 23  ASP A O   
336  C CB  . ASP A 23  ? 0.63033 0.62549 0.72398 -0.08237 0.13059  -0.04593 23  ASP A CB  
337  C CG  . ASP A 23  ? 0.73547 0.73108 0.83515 -0.08200 0.12990  -0.04590 23  ASP A CG  
338  O OD1 . ASP A 23  ? 0.58686 0.58079 0.69162 -0.08043 0.12919  -0.04262 23  ASP A OD1 
339  O OD2 . ASP A 23  ? 0.68160 0.67952 0.78085 -0.08322 0.13027  -0.04917 23  ASP A OD2 
344  N N   . MET A 24  ? 0.51175 0.49887 0.61346 -0.07976 0.12802  -0.03579 24  MET A N   
345  C CA  . MET A 24  ? 0.51405 0.50160 0.62267 -0.07646 0.12822  -0.03138 24  MET A CA  
346  C C   . MET A 24  ? 0.58883 0.58111 0.70588 -0.07291 0.12949  -0.03093 24  MET A C   
347  O O   . MET A 24  ? 0.55300 0.54609 0.67594 -0.06988 0.13000  -0.02725 24  MET A O   
348  C CB  . MET A 24  ? 0.60348 0.58638 0.71247 -0.07863 0.12555  -0.02892 24  MET A CB  
349  C CG  . MET A 24  ? 0.67910 0.65548 0.77870 -0.08215 0.12399  -0.02891 24  MET A CG  
350  S SD  . MET A 24  ? 0.77264 0.74312 0.87213 -0.08486 0.12025  -0.02674 24  MET A SD  
351  C CE  . MET A 24  ? 0.70273 0.67319 0.80750 -0.08182 0.12068  -0.02107 24  MET A CE  
361  N N   . SER A 25  ? 0.56603 0.56092 0.68318 -0.07338 0.13006  -0.03447 25  SER A N   
362  C CA  . SER A 25  ? 0.59595 0.59424 0.71950 -0.07037 0.13135  -0.03444 25  SER A CA  
363  C C   . SER A 25  ? 0.64994 0.65172 0.77360 -0.06738 0.13341  -0.03559 25  SER A C   
364  O O   . SER A 25  ? 0.59873 0.60268 0.72696 -0.06485 0.13449  -0.03559 25  SER A O   
365  C CB  . SER A 25  ? 0.55694 0.55537 0.68027 -0.07266 0.13083  -0.03756 25  SER A CB  
366  O OG  . SER A 25  ? 0.62233 0.62200 0.74000 -0.07477 0.13123  -0.04171 25  SER A OG  
372  N N   . MET A 26  ? 0.59789 0.59992 0.71612 -0.06775 0.13394  -0.03672 26  MET A N   
373  C CA  . MET A 26  ? 0.52736 0.53290 0.64509 -0.06473 0.13578  -0.03809 26  MET A CA  
374  C C   . MET A 26  ? 0.53869 0.54313 0.65560 -0.06181 0.13688  -0.03490 26  MET A C   
375  O O   . MET A 26  ? 0.46532 0.46622 0.57913 -0.06367 0.13613  -0.03294 26  MET A O   
376  C CB  . MET A 26  ? 0.55437 0.56182 0.66601 -0.06734 0.13579  -0.04250 26  MET A CB  
377  C CG  . MET A 26  ? 0.77829 0.78717 0.89022 -0.06994 0.13515  -0.04590 26  MET A CG  
378  S SD  . MET A 26  ? 0.76730 0.77838 0.87157 -0.07379 0.13502  -0.05078 26  MET A SD  
379  C CE  . MET A 26  ? 0.91676 0.93298 1.02179 -0.06941 0.13674  -0.05165 26  MET A CE  
389  N N   . THR A 27  ? 0.48794 0.49469 0.60702 -0.05747 0.13857  -0.03436 27  THR A N   
390  C CA  . THR A 27  ? 0.51784 0.52326 0.63566 -0.05408 0.14003  -0.03137 27  THR A CA  
391  C C   . THR A 27  ? 0.49155 0.49683 0.60154 -0.05497 0.14065  -0.03354 27  THR A C   
392  O O   . THR A 27  ? 0.43162 0.43933 0.53863 -0.05720 0.14018  -0.03757 27  THR A O   
393  C CB  . THR A 27  ? 0.52283 0.53006 0.64470 -0.04897 0.14163  -0.03030 27  THR A CB  
394  O OG1 . THR A 27  ? 0.49159 0.50218 0.61147 -0.04822 0.14199  -0.03436 27  THR A OG1 
395  C CG2 . THR A 27  ? 0.53463 0.54180 0.66358 -0.04811 0.14136  -0.02824 27  THR A CG2 
403  N N   . TYR A 28  ? 0.43524 0.43754 0.54139 -0.05326 0.14186  -0.03083 28  TYR A N   
404  C CA  . TYR A 28  ? 0.41748 0.41735 0.51151 -0.05126 0.13830  -0.03236 28  TYR A CA  
405  C C   . TYR A 28  ? 0.38505 0.39095 0.48111 -0.04917 0.14201  -0.03635 28  TYR A C   
406  O O   . TYR A 28  ? 0.43939 0.44611 0.52828 -0.04963 0.13935  -0.03952 28  TYR A O   
407  C CB  . TYR A 28  ? 0.43119 0.42361 0.51505 -0.04587 0.13200  -0.02799 28  TYR A CB  
408  C CG  . TYR A 28  ? 0.41914 0.40511 0.49732 -0.04811 0.12661  -0.02500 28  TYR A CG  
409  C CD1 . TYR A 28  ? 0.44529 0.42737 0.51353 -0.05069 0.12173  -0.02659 28  TYR A CD1 
410  C CD2 . TYR A 28  ? 0.40362 0.38753 0.48658 -0.04775 0.12657  -0.02070 28  TYR A CD2 
411  C CE1 . TYR A 28  ? 0.46392 0.43994 0.52702 -0.05287 0.11722  -0.02433 28  TYR A CE1 
412  C CE2 . TYR A 28  ? 0.40514 0.38359 0.48333 -0.04999 0.12167  -0.01834 28  TYR A CE2 
413  C CZ  . TYR A 28  ? 0.41882 0.39323 0.48714 -0.05262 0.11720  -0.02036 28  TYR A CZ  
414  O OH  . TYR A 28  ? 0.43658 0.40532 0.50003 -0.05491 0.11270  -0.01846 28  TYR A OH  
424  N N   . GLY A 29  ? 0.46908 0.47765 0.57219 -0.04568 0.14441  -0.03582 29  GLY A N   
425  C CA  . GLY A 29  ? 0.46998 0.48259 0.57298 -0.04268 0.14473  -0.03917 29  GLY A CA  
426  C C   . GLY A 29  ? 0.52622 0.54319 0.63006 -0.04633 0.14331  -0.04339 29  GLY A C   
427  O O   . GLY A 29  ? 0.49096 0.51146 0.59168 -0.04567 0.14329  -0.04689 29  GLY A O   
431  N N   . GLN A 30  ? 0.52511 0.54180 0.63293 -0.04999 0.14210  -0.04315 30  GLN A N   
432  C CA  . GLN A 30  ? 0.51011 0.53007 0.61783 -0.05371 0.14095  -0.04703 30  GLN A CA  
433  C C   . GLN A 30  ? 0.52927 0.55003 0.63016 -0.05719 0.14061  -0.04969 30  GLN A C   
434  O O   . GLN A 30  ? 0.61122 0.63581 0.71072 -0.05945 0.14005  -0.05344 30  GLN A O   
435  C CB  . GLN A 30  ? 0.54328 0.56144 0.65510 -0.05676 0.13985  -0.04617 30  GLN A CB  
436  C CG  . GLN A 30  ? 0.70153 0.71904 0.81977 -0.05396 0.14024  -0.04392 30  GLN A CG  
437  C CD  . GLN A 30  ? 0.62252 0.63787 0.74395 -0.05669 0.13925  -0.04298 30  GLN A CD  
438  O OE1 . GLN A 30  ? 0.65882 0.67136 0.78328 -0.05587 0.13916  -0.03937 30  GLN A OE1 
439  N NE2 . GLN A 30  ? 1.03499 1.05174 1.15576 -0.05978 0.13856  -0.04623 30  GLN A NE2 
448  N N   . GLN A 31  ? 0.50668 0.52360 0.60274 -0.05795 0.14104  -0.04773 31  GLN A N   
449  C CA  . GLN A 31  ? 0.48511 0.50125 0.57339 -0.06198 0.14080  -0.04974 31  GLN A CA  
450  C C   . GLN A 31  ? 0.57721 0.59056 0.65366 -0.05632 0.13541  -0.04938 31  GLN A C   
451  O O   . GLN A 31  ? 0.48632 0.50028 0.55494 -0.05702 0.13195  -0.05179 31  GLN A O   
452  C CB  . GLN A 31  ? 0.47749 0.48653 0.56253 -0.06508 0.13813  -0.04659 31  GLN A CB  
453  C CG  . GLN A 31  ? 0.51306 0.52197 0.60614 -0.06803 0.13815  -0.04608 31  GLN A CG  
454  C CD  . GLN A 31  ? 0.52095 0.52377 0.61240 -0.07169 0.13660  -0.04363 31  GLN A CD  
455  O OE1 . GLN A 31  ? 0.55432 0.55449 0.63997 -0.07642 0.13538  -0.04532 31  GLN A OE1 
456  N NE2 . GLN A 31  ? 0.49802 0.49840 0.59442 -0.06957 0.13641  -0.03962 31  GLN A NE2 
465  N N   . PHE A 32  ? 0.47075 0.48050 0.54518 -0.05039 0.13384  -0.04618 32  PHE A N   
466  C CA  . PHE A 32  ? 0.43221 0.43773 0.49497 -0.04447 0.12799  -0.04522 32  PHE A CA  
467  C C   . PHE A 32  ? 0.45466 0.46424 0.52161 -0.03948 0.13125  -0.04653 32  PHE A C   
468  O O   . PHE A 32  ? 0.49956 0.50681 0.55795 -0.03490 0.12714  -0.04665 32  PHE A O   
469  C CB  . PHE A 32  ? 0.44423 0.44011 0.49830 -0.04147 0.12243  -0.04018 32  PHE A CB  
470  C CG  . PHE A 32  ? 0.43976 0.43004 0.48769 -0.04542 0.11831  -0.03868 32  PHE A CG  
471  C CD1 . PHE A 32  ? 0.49671 0.48836 0.54172 -0.04993 0.11735  -0.04156 32  PHE A CD1 
472  C CD2 . PHE A 32  ? 0.45904 0.44237 0.50356 -0.04457 0.11527  -0.03442 32  PHE A CD2 
473  C CE1 . PHE A 32  ? 0.51523 0.50096 0.55430 -0.05349 0.11388  -0.04037 32  PHE A CE1 
474  C CE2 . PHE A 32  ? 0.53841 0.51637 0.57734 -0.04812 0.11163  -0.03333 32  PHE A CE2 
475  C CZ  . PHE A 32  ? 0.52853 0.50743 0.56479 -0.05258 0.11112  -0.03638 32  PHE A CZ  
485  N N   . GLY A 33  ? 0.45464 0.46964 0.53442 -0.04008 0.13867  -0.04741 33  GLY A N   
486  C CA  . GLY A 33  ? 0.47745 0.49375 0.56067 -0.03478 0.14176  -0.04749 33  GLY A CA  
487  C C   . GLY A 33  ? 0.42787 0.43634 0.50751 -0.03097 0.13937  -0.04222 33  GLY A C   
488  O O   . GLY A 33  ? 0.42350 0.42736 0.50129 -0.03308 0.13680  -0.03877 33  GLY A O   
492  N N   . PRO A 34  ? 0.39467 0.40143 0.47316 -0.02544 0.14017  -0.04161 34  PRO A N   
493  C CA  . PRO A 34  ? 0.38358 0.38265 0.45771 -0.02181 0.13776  -0.03657 34  PRO A CA  
494  C C   . PRO A 34  ? 0.40585 0.39685 0.46741 -0.02210 0.12953  -0.03316 34  PRO A C   
495  O O   . PRO A 34  ? 0.41808 0.40640 0.46953 -0.02112 0.12437  -0.03418 34  PRO A O   
496  C CB  . PRO A 34  ? 0.46480 0.46254 0.53622 -0.01596 0.13862  -0.03757 34  PRO A CB  
497  C CG  . PRO A 34  ? 0.43968 0.44673 0.52044 -0.01701 0.14484  -0.04313 34  PRO A CG  
498  C CD  . PRO A 34  ? 0.45524 0.46657 0.53553 -0.02228 0.14295  -0.04561 34  PRO A CD  
506  N N   . THR A 35  ? 0.36799 0.35516 0.43038 -0.02335 0.12847  -0.02905 35  THR A N   
507  C CA  . THR A 35  ? 0.37984 0.35996 0.43189 -0.02461 0.12145  -0.02607 35  THR A CA  
508  C C   . THR A 35  ? 0.38832 0.36234 0.43744 -0.02194 0.11937  -0.02108 35  THR A C   
509  O O   . THR A 35  ? 0.38521 0.36161 0.44377 -0.02170 0.12385  -0.01932 35  THR A O   
510  C CB  . THR A 35  ? 0.40337 0.38592 0.46022 -0.03083 0.12197  -0.02671 35  THR A CB  
511  O OG1 . THR A 35  ? 0.45410 0.44279 0.51422 -0.03380 0.12448  -0.03143 35  THR A OG1 
512  C CG2 . THR A 35  ? 0.38193 0.35701 0.42740 -0.03218 0.11484  -0.02439 35  THR A CG2 
520  N N   . TYR A 36  ? 0.36674 0.33291 0.40273 -0.02011 0.11268  -0.01874 36  TYR A N   
521  C CA  . TYR A 36  ? 0.33821 0.29819 0.36950 -0.01760 0.11002  -0.01415 36  TYR A CA  
522  C C   . TYR A 36  ? 0.43085 0.38464 0.45257 -0.01972 0.10358  -0.01180 36  TYR A C   
523  O O   . TYR A 36  ? 0.40093 0.35226 0.41437 -0.02085 0.09991  -0.01352 36  TYR A O   
524  C CB  . TYR A 36  ? 0.34512 0.30059 0.36877 -0.01210 0.10902  -0.01369 36  TYR A CB  
525  C CG  . TYR A 36  ? 0.38066 0.34156 0.41259 -0.00966 0.11526  -0.01662 36  TYR A CG  
526  C CD1 . TYR A 36  ? 0.38203 0.34735 0.41496 -0.00971 0.11670  -0.02117 36  TYR A CD1 
527  C CD2 . TYR A 36  ? 0.39793 0.35947 0.43644 -0.00724 0.11973  -0.01488 36  TYR A CD2 
528  C CE1 . TYR A 36  ? 0.44491 0.41559 0.48581 -0.00765 0.12263  -0.02428 36  TYR A CE1 
529  C CE2 . TYR A 36  ? 0.41411 0.38031 0.46023 -0.00502 0.12597  -0.01791 36  TYR A CE2 
530  C CZ  . TYR A 36  ? 0.48168 0.45256 0.52914 -0.00533 0.12743  -0.02276 36  TYR A CZ  
531  O OH  . TYR A 36  ? 0.48715 0.46291 0.54242 -0.00326 0.13376  -0.02611 36  TYR A OH  
541  N N   . LEU A 37  ? 0.37302 0.32433 0.39586 -0.02011 0.10232  -0.00783 37  LEU A N   
542  C CA  . LEU A 37  ? 0.33863 0.28423 0.35332 -0.02212 0.09654  -0.00538 37  LEU A CA  
543  C C   . LEU A 37  ? 0.47253 0.41172 0.47853 -0.01842 0.09324  -0.00171 37  LEU A C   
544  O O   . LEU A 37  ? 0.43011 0.37013 0.44146 -0.01738 0.09473  0.00141  37  LEU A O   
545  C CB  . LEU A 37  ? 0.41814 0.36712 0.44272 -0.02654 0.09788  -0.00407 37  LEU A CB  
546  C CG  . LEU A 37  ? 0.41533 0.35896 0.43279 -0.02903 0.09224  -0.00190 37  LEU A CG  
547  C CD1 . LEU A 37  ? 0.44919 0.38846 0.45536 -0.03037 0.08839  -0.00452 37  LEU A CD1 
548  C CD2 . LEU A 37  ? 0.45714 0.40481 0.48634 -0.03344 0.09428  -0.00097 37  LEU A CD2 
560  N N   . ASP A 38  ? 0.45673 0.38954 0.44941 -0.01644 0.08906  -0.00206 38  ASP A N   
561  C CA  . ASP A 38  ? 0.53945 0.46546 0.52242 -0.01312 0.08613  0.00090  38  ASP A CA  
562  C C   . ASP A 38  ? 0.46026 0.38806 0.44917 -0.00962 0.09027  0.00218  38  ASP A C   
563  O O   . ASP A 38  ? 0.48452 0.40953 0.47193 -0.00845 0.08925  0.00582  38  ASP A O   
564  C CB  . ASP A 38  ? 0.56648 0.48843 0.54466 -0.01530 0.08165  0.00435  38  ASP A CB  
565  C CG  . ASP A 38  ? 1.01011 0.92388 0.97494 -0.01270 0.07774  0.00673  38  ASP A CG  
566  O OD1 . ASP A 38  ? 0.62736 0.53718 0.58413 -0.01004 0.07736  0.00518  38  ASP A OD1 
567  O OD2 . ASP A 38  ? 0.72684 0.63816 0.68925 -0.01351 0.07505  0.01012  38  ASP A OD2 
572  N N   . GLY A 39  ? 0.40722 0.33962 0.40257 -0.00797 0.09501  -0.00096 39  GLY A N   
573  C CA  . GLY A 39  ? 0.41837 0.35223 0.41920 -0.00446 0.09972  -0.00065 39  GLY A CA  
574  C C   . GLY A 39  ? 0.41529 0.35658 0.43121 -0.00574 0.10544  -0.00039 39  GLY A C   
575  O O   . GLY A 39  ? 0.43564 0.38009 0.45844 -0.00331 0.11097  -0.00183 39  GLY A O   
579  N N   . ALA A 40  ? 0.40918 0.35325 0.43075 -0.00954 0.10466  0.00121  40  ALA A N   
580  C CA  . ALA A 40  ? 0.44198 0.39290 0.47843 -0.01101 0.11033  0.00180  40  ALA A CA  
581  C C   . ALA A 40  ? 0.45140 0.40948 0.49703 -0.01319 0.11540  -0.00299 40  ALA A C   
582  O O   . ALA A 40  ? 0.43451 0.39323 0.47703 -0.01604 0.11314  -0.00566 40  ALA A O   
583  C CB  . ALA A 40  ? 0.50718 0.45845 0.54690 -0.01445 0.10769  0.00518  40  ALA A CB  
589  N N   . ASP A 41  ? 0.41114 0.37449 0.46781 -0.01195 0.12244  -0.00410 41  ASP A N   
590  C CA  . ASP A 41  ? 0.38268 0.35348 0.44889 -0.01406 0.12817  -0.00886 41  ASP A CA  
591  C C   . ASP A 41  ? 0.41558 0.39134 0.49208 -0.01934 0.13028  -0.00867 41  ASP A C   
592  O O   . ASP A 41  ? 0.46276 0.44095 0.54912 -0.01981 0.13405  -0.00593 41  ASP A O   
593  C CB  . ASP A 41  ? 0.44426 0.41852 0.51864 -0.01087 0.13548  -0.01015 41  ASP A CB  
594  C CG  . ASP A 41  ? 0.60320 0.58483 0.68537 -0.01250 0.14113  -0.01582 41  ASP A CG  
595  O OD1 . ASP A 41  ? 0.44991 0.43543 0.53497 -0.01705 0.14084  -0.01808 41  ASP A OD1 
596  O OD2 . ASP A 41  ? 0.53461 0.51832 0.62058 -0.00947 0.14629  -0.01809 41  ASP A OD2 
601  N N   . VAL A 42  ? 0.39652 0.37369 0.47110 -0.02332 0.12825  -0.01156 42  VAL A N   
602  C CA  . VAL A 42  ? 0.41438 0.39566 0.49823 -0.02888 0.13042  -0.01197 42  VAL A CA  
603  C C   . VAL A 42  ? 0.43536 0.42410 0.52812 -0.03197 0.13661  -0.01710 42  VAL A C   
604  O O   . VAL A 42  ? 0.44522 0.43688 0.54360 -0.03721 0.13809  -0.01858 42  VAL A O   
605  C CB  . VAL A 42  ? 0.43896 0.41537 0.51396 -0.03196 0.12347  -0.01108 42  VAL A CB  
606  C CG1 . VAL A 42  ? 0.48707 0.45734 0.55580 -0.03000 0.11818  -0.00596 42  VAL A CG1 
607  C CG2 . VAL A 42  ? 0.40354 0.37725 0.46659 -0.03162 0.11925  -0.01434 42  VAL A CG2 
617  N N   . THR A 43  ? 0.40962 0.40142 0.50368 -0.02903 0.14039  -0.02005 43  THR A N   
618  C CA  . THR A 43  ? 0.41777 0.41702 0.51934 -0.03198 0.14596  -0.02534 43  THR A CA  
619  C C   . THR A 43  ? 0.47750 0.48041 0.58978 -0.03534 0.14750  -0.02524 43  THR A C   
620  O O   . THR A 43  ? 0.48357 0.48925 0.59701 -0.03895 0.14594  -0.02847 43  THR A O   
621  C CB  . THR A 43  ? 0.42998 0.43192 0.53281 -0.02768 0.14980  -0.02803 43  THR A CB  
622  O OG1 . THR A 43  ? 0.40280 0.39910 0.49228 -0.02344 0.14375  -0.02782 43  THR A OG1 
623  C CG2 . THR A 43  ? 0.46408 0.47130 0.56933 -0.02962 0.14819  -0.03278 43  THR A CG2 
631  N N   . LYS A 44  ? 0.44641 0.44800 0.56403 -0.03329 0.14806  -0.02135 44  LYS A N   
632  C CA  . LYS A 44  ? 0.51343 0.51672 0.63847 -0.03462 0.14700  -0.02091 44  LYS A CA  
633  C C   . LYS A 44  ? 0.56276 0.56462 0.69104 -0.03803 0.14570  -0.01789 44  LYS A C   
634  O O   . LYS A 44  ? 0.54840 0.55095 0.68285 -0.03834 0.14509  -0.01660 44  LYS A O   
635  C CB  . LYS A 44  ? 0.52203 0.52476 0.65085 -0.03006 0.14849  -0.01873 44  LYS A CB  
636  C CG  . LYS A 44  ? 0.52001 0.52404 0.64626 -0.02719 0.14914  -0.02210 44  LYS A CG  
637  C CD  . LYS A 44  ? 0.89193 0.89538 1.02241 -0.02410 0.15013  -0.02081 44  LYS A CD  
638  C CE  . LYS A 44  ? 0.91694 0.91967 1.04367 -0.02012 0.15113  -0.02237 44  LYS A CE  
639  N NZ  . LYS A 44  ? 1.02659 1.02890 1.15680 -0.01813 0.15184  -0.02218 44  LYS A NZ  
653  N N   . ILE A 45  ? 0.46006 0.45955 0.58387 -0.04070 0.14515  -0.01682 45  ILE A N   
654  C CA  . ILE A 45  ? 0.48511 0.48245 0.61118 -0.04422 0.14340  -0.01375 45  ILE A CA  
655  C C   . ILE A 45  ? 0.46733 0.46471 0.59046 -0.04945 0.14125  -0.01741 45  ILE A C   
656  O O   . ILE A 45  ? 0.50596 0.50371 0.62291 -0.05060 0.14158  -0.02092 45  ILE A O   
657  C CB  . ILE A 45  ? 0.70490 0.69685 0.82391 -0.04249 0.14089  -0.00932 45  ILE A CB  
658  C CG1 . ILE A 45  ? 0.67940 0.67114 0.80466 -0.03924 0.14239  -0.00404 45  ILE A CG1 
659  C CG2 . ILE A 45  ? 0.60458 0.59192 0.71676 -0.04600 0.13445  -0.00861 45  ILE A CG2 
660  C CD1 . ILE A 45  ? 0.90399 0.89920 1.03529 -0.03522 0.14723  -0.00470 45  ILE A CD1 
672  N N   . LYS A 46  ? 0.49760 0.49456 0.62503 -0.05249 0.13904  -0.01664 46  LYS A N   
673  C CA  . LYS A 46  ? 0.44360 0.43939 0.56723 -0.05749 0.13693  -0.01975 46  LYS A CA  
674  C C   . LYS A 46  ? 0.46087 0.45148 0.57986 -0.06079 0.13537  -0.01734 46  LYS A C   
675  O O   . LYS A 46  ? 0.53538 0.52382 0.65671 -0.05973 0.13520  -0.01276 46  LYS A O   
676  C CB  . LYS A 46  ? 0.49851 0.49576 0.62763 -0.05899 0.13537  -0.02081 46  LYS A CB  
677  C CG  . LYS A 46  ? 0.53247 0.53337 0.66594 -0.05606 0.13677  -0.02251 46  LYS A CG  
678  C CD  . LYS A 46  ? 0.63667 0.63827 0.77197 -0.05854 0.13554  -0.02510 46  LYS A CD  
679  C CE  . LYS A 46  ? 0.69906 0.70344 0.83634 -0.05652 0.13692  -0.02757 46  LYS A CE  
680  N NZ  . LYS A 46  ? 0.80413 0.80844 0.94611 -0.05707 0.13650  -0.02753 46  LYS A NZ  
694  N N   . PRO A 47  ? 0.48196 0.46988 0.59381 -0.06506 0.13405  -0.02026 47  PRO A N   
695  C CA  . PRO A 47  ? 0.47956 0.46001 0.58017 -0.06534 0.12721  -0.01837 47  PRO A CA  
696  C C   . PRO A 47  ? 0.63035 0.60875 0.73731 -0.06778 0.12630  -0.01498 47  PRO A C   
697  O O   . PRO A 47  ? 0.60866 0.59004 0.72514 -0.07036 0.12831  -0.01562 47  PRO A O   
698  C CB  . PRO A 47  ? 0.50967 0.48804 0.60237 -0.06930 0.12550  -0.02273 47  PRO A CB  
699  C CG  . PRO A 47  ? 0.48823 0.47279 0.58411 -0.06917 0.13034  -0.02650 47  PRO A CG  
700  C CD  . PRO A 47  ? 0.52137 0.51176 0.62951 -0.06658 0.13437  -0.02541 47  PRO A CD  
708  N N   . HIS A 48  ? 0.57875 0.55170 0.67680 -0.06462 0.11975  -0.01153 48  HIS A N   
709  C CA  . HIS A 48  ? 0.55782 0.52811 0.65915 -0.06657 0.11716  -0.00840 48  HIS A CA  
710  C C   . HIS A 48  ? 0.52102 0.48455 0.61091 -0.06951 0.11160  -0.01019 48  HIS A C   
711  O O   . HIS A 48  ? 0.52955 0.48905 0.60570 -0.06777 0.10771  -0.01206 48  HIS A O   
712  C CB  . HIS A 48  ? 0.57277 0.54164 0.67153 -0.06131 0.11348  -0.00334 48  HIS A CB  
713  C CG  . HIS A 48  ? 0.70979 0.68434 0.81938 -0.05812 0.11879  -0.00100 48  HIS A CG  
714  N ND1 . HIS A 48  ? 0.89235 0.87304 1.01307 -0.05961 0.12656  -0.00349 48  HIS A ND1 
715  C CD2 . HIS A 48  ? 0.90312 0.87792 1.01374 -0.05353 0.11768  0.00354  48  HIS A CD2 
716  C CE1 . HIS A 48  ? 0.88689 0.87119 1.01529 -0.05594 0.13028  -0.00062 48  HIS A CE1 
717  N NE2 . HIS A 48  ? 0.85971 0.84040 0.98199 -0.05213 0.12489  0.00377  48  HIS A NE2 
725  N N   . ASN A 49  ? 0.57034 0.53247 0.66620 -0.07386 0.11140  -0.00954 49  ASN A N   
726  C CA  . ASN A 49  ? 0.58772 0.54282 0.67297 -0.07656 0.10624  -0.01105 49  ASN A CA  
727  C C   . ASN A 49  ? 0.54912 0.49856 0.61841 -0.07183 0.09910  -0.00929 49  ASN A C   
728  O O   . ASN A 49  ? 0.52752 0.47136 0.58364 -0.07222 0.09552  -0.01166 49  ASN A O   
729  C CB  . ASN A 49  ? 0.64973 0.60412 0.74428 -0.08078 0.10645  -0.00965 49  ASN A CB  
730  C CG  . ASN A 49  ? 0.80625 0.76399 0.91281 -0.08616 0.11220  -0.01248 49  ASN A CG  
731  O OD1 . ASN A 49  ? 0.98861 0.94687 1.09073 -0.08708 0.11313  -0.01651 49  ASN A OD1 
732  N ND2 . ASN A 49  ? 0.95129 0.91275 1.06758 -0.08520 0.11104  -0.01032 49  ASN A ND2 
739  N N   . SER A 50  ? 0.53933 0.48989 0.60948 -0.06749 0.09716  -0.00505 50  SER A N   
740  C CA  . SER A 50  ? 0.67294 0.61811 0.72852 -0.06330 0.09078  -0.00314 50  SER A CA  
741  C C   . SER A 50  ? 0.54453 0.48777 0.58845 -0.05976 0.08984  -0.00513 50  SER A C   
742  O O   . SER A 50  ? 0.50247 0.44011 0.53278 -0.05700 0.08479  -0.00439 50  SER A O   
743  C CB  . SER A 50  ? 0.70730 0.65473 0.76724 -0.05957 0.08970  0.00182  50  SER A CB  
744  O OG  . SER A 50  ? 0.63753 0.58976 0.70283 -0.05596 0.09386  0.00263  50  SER A OG  
750  N N   . HIS A 51  ? 0.50292 0.45075 0.55207 -0.05986 0.09470  -0.00768 51  HIS A N   
751  C CA  . HIS A 51  ? 0.49939 0.44606 0.53853 -0.05651 0.09385  -0.00970 51  HIS A CA  
752  C C   . HIS A 51  ? 0.50483 0.44646 0.53265 -0.05876 0.09106  -0.01305 51  HIS A C   
753  O O   . HIS A 51  ? 0.45344 0.39300 0.47110 -0.05568 0.08918  -0.01427 51  HIS A O   
754  C CB  . HIS A 51  ? 0.42796 0.38195 0.47714 -0.05596 0.10013  -0.01152 51  HIS A CB  
755  C CG  . HIS A 51  ? 0.42219 0.38029 0.47970 -0.05230 0.10294  -0.00838 51  HIS A CG  
756  N ND1 . HIS A 51  ? 0.44451 0.40961 0.51383 -0.05215 0.10963  -0.00956 51  HIS A ND1 
757  C CD2 . HIS A 51  ? 0.47765 0.43362 0.53290 -0.04868 0.10015  -0.00418 51  HIS A CD2 
758  C CE1 . HIS A 51  ? 0.52724 0.49403 0.60132 -0.04839 0.11098  -0.00612 51  HIS A CE1 
759  N NE2 . HIS A 51  ? 0.46422 0.42554 0.52969 -0.04621 0.10512  -0.00273 51  HIS A NE2 
767  N N   . GLU A 52  ? 0.53669 0.47598 0.56593 -0.06394 0.09084  -0.01449 52  GLU A N   
768  C CA  . GLU A 52  ? 0.45200 0.38637 0.47078 -0.06627 0.08886  -0.01782 52  GLU A CA  
769  C C   . GLU A 52  ? 0.47211 0.39938 0.47434 -0.06241 0.08304  -0.01685 52  GLU A C   
770  O O   . GLU A 52  ? 0.47778 0.40121 0.47573 -0.06098 0.07953  -0.01414 52  GLU A O   
771  C CB  . GLU A 52  ? 0.52285 0.45448 0.54511 -0.07238 0.08937  -0.01930 52  GLU A CB  
772  C CG  . GLU A 52  ? 0.58202 0.50863 0.59414 -0.07521 0.08824  -0.02303 52  GLU A CG  
773  C CD  . GLU A 52  ? 1.02599 0.95377 1.04679 -0.08196 0.09244  -0.02601 52  GLU A CD  
774  O OE1 . GLU A 52  ? 0.74413 0.67210 0.77425 -0.08524 0.09383  -0.02506 52  GLU A OE1 
775  O OE2 . GLU A 52  ? 0.74089 0.66929 0.75910 -0.08408 0.09432  -0.02931 52  GLU A OE2 
782  N N   . GLY A 53  ? 0.48769 0.41341 0.48078 -0.06081 0.08219  -0.01908 53  GLY A N   
783  C CA  . GLY A 53  ? 0.47122 0.39006 0.44869 -0.05734 0.07738  -0.01848 53  GLY A CA  
784  C C   . GLY A 53  ? 0.44010 0.35944 0.41416 -0.05145 0.07604  -0.01596 53  GLY A C   
785  O O   . GLY A 53  ? 0.43368 0.34716 0.39497 -0.04840 0.07239  -0.01529 53  GLY A O   
789  N N   . LYS A 54  ? 0.41725 0.34293 0.40221 -0.04985 0.07921  -0.01458 54  LYS A N   
790  C CA  . LYS A 54  ? 0.42781 0.35353 0.41002 -0.04445 0.07837  -0.01218 54  LYS A CA  
791  C C   . LYS A 54  ? 0.40903 0.33749 0.38932 -0.04133 0.07996  -0.01427 54  LYS A C   
792  O O   . LYS A 54  ? 0.40567 0.33827 0.39017 -0.04351 0.08260  -0.01734 54  LYS A O   
793  C CB  . LYS A 54  ? 0.46070 0.39142 0.45515 -0.04393 0.08116  -0.00955 54  LYS A CB  
794  C CG  . LYS A 54  ? 0.50704 0.43435 0.50081 -0.04522 0.07814  -0.00644 54  LYS A CG  
795  C CD  . LYS A 54  ? 0.55582 0.48742 0.55949 -0.04337 0.08013  -0.00305 54  LYS A CD  
796  C CE  . LYS A 54  ? 0.65532 0.58561 0.66187 -0.04579 0.07775  -0.00031 54  LYS A CE  
797  N NZ  . LYS A 54  ? 0.85519 0.78600 0.86288 -0.04236 0.07665  0.00392  54  LYS A NZ  
811  N N   . THR A 55  ? 0.40360 0.32959 0.37731 -0.03635 0.07830  -0.01265 55  THR A N   
812  C CA  . THR A 55  ? 0.38821 0.31615 0.35946 -0.03274 0.07934  -0.01438 55  THR A CA  
813  C C   . THR A 55  ? 0.40237 0.33645 0.38412 -0.03024 0.08363  -0.01390 55  THR A C   
814  O O   . THR A 55  ? 0.38239 0.31518 0.36562 -0.02827 0.08357  -0.01092 55  THR A O   
815  C CB  . THR A 55  ? 0.42190 0.34231 0.37875 -0.02882 0.07513  -0.01314 55  THR A CB  
816  O OG1 . THR A 55  ? 0.45129 0.36617 0.39840 -0.03101 0.07185  -0.01401 55  THR A OG1 
817  C CG2 . THR A 55  ? 0.42775 0.35041 0.38331 -0.02463 0.07636  -0.01467 55  THR A CG2 
825  N N   . PHE A 56  ? 0.33627 0.27681 0.32470 -0.03028 0.08735  -0.01692 56  PHE A N   
826  C CA  . PHE A 56  ? 0.38439 0.33105 0.38287 -0.02792 0.09219  -0.01731 56  PHE A CA  
827  C C   . PHE A 56  ? 0.36454 0.31191 0.35850 -0.02382 0.09224  -0.01933 56  PHE A C   
828  O O   . PHE A 56  ? 0.37978 0.32743 0.36872 -0.02442 0.09065  -0.02179 56  PHE A O   
829  C CB  . PHE A 56  ? 0.38048 0.33528 0.39293 -0.03210 0.09766  -0.01961 56  PHE A CB  
830  C CG  . PHE A 56  ? 0.38325 0.33798 0.40228 -0.03599 0.09837  -0.01756 56  PHE A CG  
831  C CD1 . PHE A 56  ? 0.41120 0.36239 0.42599 -0.04016 0.09543  -0.01785 56  PHE A CD1 
832  C CD2 . PHE A 56  ? 0.41116 0.36912 0.44070 -0.03539 0.10206  -0.01530 56  PHE A CD2 
833  C CE1 . PHE A 56  ? 0.42188 0.37309 0.44345 -0.04378 0.09614  -0.01611 56  PHE A CE1 
834  C CE2 . PHE A 56  ? 0.38844 0.34662 0.42469 -0.03880 0.10258  -0.01318 56  PHE A CE2 
835  C CZ  . PHE A 56  ? 0.42136 0.37628 0.45389 -0.04304 0.09958  -0.01366 56  PHE A CZ  
845  N N   . TYR A 57  ? 0.39015 0.33778 0.38605 -0.01961 0.09415  -0.01832 57  TYR A N   
846  C CA  . TYR A 57  ? 0.33229 0.28186 0.32677 -0.01589 0.09530  -0.02073 57  TYR A CA  
847  C C   . TYR A 57  ? 0.35431 0.31356 0.36142 -0.01744 0.10111  -0.02436 57  TYR A C   
848  O O   . TYR A 57  ? 0.39055 0.35424 0.40863 -0.01938 0.10561  -0.02408 57  TYR A O   
849  C CB  . TYR A 57  ? 0.35355 0.29930 0.34545 -0.01095 0.09571  -0.01874 57  TYR A CB  
850  C CG  . TYR A 57  ? 0.38035 0.31675 0.35842 -0.00845 0.09048  -0.01621 57  TYR A CG  
851  C CD1 . TYR A 57  ? 0.37412 0.30468 0.34642 -0.01005 0.08706  -0.01285 57  TYR A CD1 
852  C CD2 . TYR A 57  ? 0.42335 0.35679 0.39449 -0.00451 0.08926  -0.01723 57  TYR A CD2 
853  C CE1 . TYR A 57  ? 0.43195 0.35392 0.39152 -0.00803 0.08278  -0.01072 57  TYR A CE1 
854  C CE2 . TYR A 57  ? 0.38468 0.30915 0.34330 -0.00235 0.08510  -0.01489 57  TYR A CE2 
855  C CZ  . TYR A 57  ? 0.38352 0.30231 0.33625 -0.00425 0.08200  -0.01172 57  TYR A CZ  
856  O OH  . TYR A 57  ? 0.43033 0.34025 0.37060 -0.00249 0.07833  -0.00957 57  TYR A OH  
866  N N   . VAL A 58  ? 0.39514 0.35777 0.40084 -0.01647 0.10117  -0.02773 58  VAL A N   
867  C CA  . VAL A 58  ? 0.35954 0.33162 0.37629 -0.01758 0.10665  -0.03170 58  VAL A CA  
868  C C   . VAL A 58  ? 0.37728 0.35053 0.39197 -0.01277 0.10700  -0.03373 58  VAL A C   
869  O O   . VAL A 58  ? 0.40494 0.37158 0.40963 -0.00902 0.10294  -0.03206 58  VAL A O   
870  C CB  . VAL A 58  ? 0.40240 0.37926 0.42095 -0.02261 0.10663  -0.03459 58  VAL A CB  
871  C CG1 . VAL A 58  ? 0.41082 0.38693 0.43347 -0.02767 0.10738  -0.03302 58  VAL A CG1 
872  C CG2 . VAL A 58  ? 0.42443 0.39692 0.43033 -0.02166 0.10063  -0.03479 58  VAL A CG2 
882  N N   . LEU A 59  ? 0.40160 0.38339 0.42624 -0.01309 0.11220  -0.03753 59  LEU A N   
883  C CA  . LEU A 59  ? 0.44557 0.42938 0.46916 -0.00885 0.11261  -0.04008 59  LEU A CA  
884  C C   . LEU A 59  ? 0.46532 0.45141 0.48310 -0.00967 0.10871  -0.04239 59  LEU A C   
885  O O   . LEU A 59  ? 0.50805 0.49680 0.52605 -0.01424 0.10780  -0.04328 59  LEU A O   
886  C CB  . LEU A 59  ? 0.44591 0.43816 0.48269 -0.00866 0.12011  -0.04360 59  LEU A CB  
887  C CG  . LEU A 59  ? 0.42477 0.41546 0.46834 -0.00770 0.12485  -0.04145 59  LEU A CG  
888  C CD1 . LEU A 59  ? 0.45297 0.45147 0.50874 -0.00686 0.13263  -0.04536 59  LEU A CD1 
889  C CD2 . LEU A 59  ? 0.44889 0.42964 0.48330 -0.00310 0.12143  -0.03747 59  LEU A CD2 
901  N N   . PRO A 60  ? 0.47778 0.46255 0.49012 -0.00526 0.10632  -0.04326 60  PRO A N   
902  C CA  . PRO A 60  ? 0.46818 0.45548 0.47512 -0.00565 0.10243  -0.04515 60  PRO A CA  
903  C C   . PRO A 60  ? 0.55505 0.55386 0.57178 -0.00874 0.10631  -0.04996 60  PRO A C   
904  O O   . PRO A 60  ? 0.59357 0.59838 0.61590 -0.00633 0.10899  -0.05320 60  PRO A O   
905  C CB  . PRO A 60  ? 0.54441 0.52745 0.54480 0.00028  0.09971  -0.04461 60  PRO A CB  
906  C CG  . PRO A 60  ? 0.55086 0.52730 0.55098 0.00326  0.10145  -0.04201 60  PRO A CG  
907  C CD  . PRO A 60  ? 0.48074 0.46107 0.49119 0.00022  0.10689  -0.04234 60  PRO A CD  
915  N N   . ASN A 61  ? 0.64593 0.64785 0.66476 -0.01439 0.10679  -0.05070 61  ASN A N   
916  C CA  . ASN A 61  ? 0.73237 0.74540 0.76108 -0.01848 0.11125  -0.05541 61  ASN A CA  
917  C C   . ASN A 61  ? 0.77548 0.79180 0.79800 -0.01934 0.10688  -0.05738 61  ASN A C   
918  O O   . ASN A 61  ? 0.85293 0.87811 0.88106 -0.01902 0.10899  -0.06143 61  ASN A O   
919  C CB  . ASN A 61  ? 0.86868 0.88367 0.90465 -0.02447 0.11535  -0.05542 61  ASN A CB  
920  C CG  . ASN A 61  ? 0.87687 0.88470 0.90442 -0.02757 0.11082  -0.05234 61  ASN A CG  
921  O OD1 . ASN A 61  ? 0.99130 1.00116 1.01590 -0.03154 0.10903  -0.05390 61  ASN A OD1 
922  N ND2 . ASN A 61  ? 0.70094 0.70036 0.72446 -0.02600 0.10903  -0.04814 61  ASN A ND2 
929  N N   . ASP A 62  ? 0.61355 0.62282 0.62443 -0.01963 0.10084  -0.05460 62  ASP A N   
930  C CA  . ASP A 62  ? 0.61136 0.62308 0.61541 -0.02045 0.09644  -0.05599 62  ASP A CA  
931  C C   . ASP A 62  ? 0.68386 0.69108 0.67911 -0.01405 0.09145  -0.05421 62  ASP A C   
932  O O   . ASP A 62  ? 0.56800 0.56969 0.56230 -0.00987 0.09168  -0.05202 62  ASP A O   
933  C CB  . ASP A 62  ? 0.45296 0.45956 0.44967 -0.02512 0.09345  -0.05430 62  ASP A CB  
934  C CG  . ASP A 62  ? 0.44889 0.44357 0.43647 -0.02322 0.08995  -0.04958 62  ASP A CG  
935  O OD1 . ASP A 62  ? 0.45204 0.44112 0.43206 -0.01788 0.08634  -0.04731 62  ASP A OD1 
936  O OD2 . ASP A 62  ? 0.44318 0.43350 0.43072 -0.02693 0.09068  -0.04798 62  ASP A OD2 
941  N N   . ASP A 63  ? 0.58063 0.63032 0.60150 -0.06810 0.01874  -0.00728 63  ASP A N   
942  C CA  . ASP A 63  ? 0.53207 0.58109 0.55000 -0.06655 0.01656  -0.00553 63  ASP A CA  
943  C C   . ASP A 63  ? 0.57730 0.62177 0.59201 -0.06371 0.01070  -0.00352 63  ASP A C   
944  O O   . ASP A 63  ? 0.47432 0.51412 0.48480 -0.06025 0.00875  -0.00208 63  ASP A O   
945  C CB  . ASP A 63  ? 0.58720 0.64555 0.60871 -0.07089 0.01676  -0.00564 63  ASP A CB  
946  C CG  . ASP A 63  ? 0.86817 0.93232 0.89249 -0.07425 0.02264  -0.00757 63  ASP A CG  
947  O OD1 . ASP A 63  ? 0.64556 0.70516 0.66806 -0.07291 0.02664  -0.00869 63  ASP A OD1 
948  O OD2 . ASP A 63  ? 0.74756 0.82099 0.77580 -0.07834 0.02321  -0.00786 63  ASP A OD2 
953  N N   . THR A 64  ? 0.49511 0.54125 0.51142 -0.06526 0.00757  -0.00341 64  THR A N   
954  C CA  . THR A 64  ? 0.50179 0.54378 0.51466 -0.06322 0.00229  -0.00167 64  THR A CA  
955  C C   . THR A 64  ? 0.47349 0.50690 0.48167 -0.05808 0.00246  -0.00113 64  THR A C   
956  O O   . THR A 64  ? 0.42595 0.45460 0.43018 -0.05518 -0.00049 0.00030  64  THR A O   
957  C CB  . THR A 64  ? 0.49226 0.53884 0.50742 -0.06643 -0.00110 -0.00170 64  THR A CB  
958  O OG1 . THR A 64  ? 0.50257 0.55693 0.52152 -0.07075 -0.00268 -0.00142 64  THR A OG1 
959  C CG2 . THR A 64  ? 0.52532 0.56672 0.53586 -0.06425 -0.00601 -0.00011 64  THR A CG2 
967  N N   . LEU A 65  ? 0.40187 0.43352 0.41066 -0.05687 0.00614  -0.00229 65  LEU A N   
968  C CA  . LEU A 65  ? 0.38238 0.40687 0.38747 -0.05197 0.00695  -0.00172 65  LEU A CA  
969  C C   . LEU A 65  ? 0.40638 0.42711 0.40917 -0.04895 0.00885  -0.00132 65  LEU A C   
970  O O   . LEU A 65  ? 0.37607 0.39158 0.37530 -0.04478 0.00730  -0.00021 65  LEU A O   
971  C CB  . LEU A 65  ? 0.47368 0.49773 0.48022 -0.05154 0.01074  -0.00295 65  LEU A CB  
972  C CG  . LEU A 65  ? 0.49810 0.52562 0.50581 -0.05332 0.00874  -0.00327 65  LEU A CG  
973  C CD1 . LEU A 65  ? 0.51763 0.54420 0.52633 -0.05215 0.01305  -0.00454 65  LEU A CD1 
974  C CD2 . LEU A 65  ? 0.46252 0.48760 0.46628 -0.05128 0.00391  -0.00156 65  LEU A CD2 
986  N N   . ARG A 66  ? 0.38184 0.40593 0.38655 -0.05112 0.01215  -0.00226 66  ARG A N   
987  C CA  . ARG A 66  ? 0.38966 0.41146 0.39179 -0.04860 0.01399  -0.00192 66  ARG A CA  
988  C C   . ARG A 66  ? 0.39425 0.41444 0.39304 -0.04626 0.00940  -0.00033 66  ARG A C   
989  O O   . ARG A 66  ? 0.39178 0.40782 0.38729 -0.04218 0.00903  0.00037  66  ARG A O   
990  C CB  . ARG A 66  ? 0.49010 0.51728 0.49458 -0.05225 0.01821  -0.00324 66  ARG A CB  
991  C CG  . ARG A 66  ? 0.60792 0.63425 0.61414 -0.05339 0.02348  -0.00486 66  ARG A CG  
992  C CD  . ARG A 66  ? 0.86573 0.89870 0.87496 -0.05835 0.02727  -0.00650 66  ARG A CD  
993  N NE  . ARG A 66  ? 0.98564 1.01794 0.99720 -0.06030 0.03180  -0.00839 66  ARG A NE  
994  C CZ  . ARG A 66  ? 1.18240 1.22064 1.19808 -0.06512 0.03449  -0.01031 66  ARG A CZ  
995  N NH1 . ARG A 66  ? 0.98042 1.02674 0.99898 -0.06877 0.03310  -0.01046 66  ARG A NH1 
996  N NH2 . ARG A 66  ? 0.85790 0.89414 0.87500 -0.06623 0.03853  -0.01208 66  ARG A NH2 
1010 N N   . VAL A 67  ? 0.39616 0.41970 0.39584 -0.04876 0.00604  0.00021  67  VAL A N   
1011 C CA  . VAL A 67  ? 0.37556 0.39679 0.37175 -0.04657 0.00158  0.00172  67  VAL A CA  
1012 C C   . VAL A 67  ? 0.35349 0.36822 0.34648 -0.04318 -0.00204 0.00261  67  VAL A C   
1013 O O   . VAL A 67  ? 0.37218 0.38246 0.36133 -0.03918 -0.00403 0.00341  67  VAL A O   
1014 C CB  . VAL A 67  ? 0.50442 0.53092 0.50265 -0.05047 -0.00095 0.00224  67  VAL A CB  
1015 C CG1 . VAL A 67  ? 0.45258 0.47512 0.44668 -0.04803 -0.00593 0.00391  67  VAL A CG1 
1016 C CG2 . VAL A 67  ? 0.55563 0.58944 0.55669 -0.05344 0.00283  0.00149  67  VAL A CG2 
1026 N N   . GLU A 68  ? 0.39230 0.40703 0.38663 -0.04475 -0.00300 0.00243  68  GLU A N   
1027 C CA  . GLU A 68  ? 0.38820 0.39773 0.37922 -0.04192 -0.00608 0.00325  68  GLU A CA  
1028 C C   . GLU A 68  ? 0.37698 0.38229 0.36617 -0.03714 -0.00376 0.00322  68  GLU A C   
1029 O O   . GLU A 68  ? 0.33317 0.33419 0.31895 -0.03366 -0.00632 0.00401  68  GLU A O   
1030 C CB  . GLU A 68  ? 0.34078 0.35241 0.33326 -0.04448 -0.00688 0.00301  68  GLU A CB  
1031 C CG  . GLU A 68  ? 0.41390 0.42983 0.40777 -0.04909 -0.01038 0.00336  68  GLU A CG  
1032 C CD  . GLU A 68  ? 0.49723 0.51693 0.49267 -0.05197 -0.01120 0.00299  68  GLU A CD  
1033 O OE1 . GLU A 68  ? 0.43385 0.45320 0.42967 -0.05042 -0.00833 0.00228  68  GLU A OE1 
1034 O OE2 . GLU A 68  ? 0.45885 0.48235 0.45511 -0.05580 -0.01477 0.00348  68  GLU A OE2 
1041 N N   . ALA A 69  ? 0.35201 0.35861 0.34348 -0.03702 0.00108  0.00232  69  ALA A N   
1042 C CA  . ALA A 69  ? 0.32554 0.32871 0.31568 -0.03271 0.00339  0.00251  69  ALA A CA  
1043 C C   . ALA A 69  ? 0.33825 0.34003 0.32589 -0.02980 0.00251  0.00297  69  ALA A C   
1044 O O   . ALA A 69  ? 0.33365 0.33223 0.31901 -0.02564 0.00123  0.00363  69  ALA A O   
1045 C CB  . ALA A 69  ? 0.35509 0.35947 0.34794 -0.03365 0.00880  0.00150  69  ALA A CB  
1051 N N   . PHE A 70  ? 0.32370 0.32863 0.31169 -0.03184 0.00311  0.00263  70  PHE A N   
1052 C CA  . PHE A 70  ? 0.34189 0.34625 0.32688 -0.02880 0.00209  0.00310  70  PHE A CA  
1053 C C   . PHE A 70  ? 0.37531 0.37625 0.35702 -0.02626 -0.00319 0.00403  70  PHE A C   
1054 O O   . PHE A 70  ? 0.35018 0.34861 0.32914 -0.02198 -0.00464 0.00442  70  PHE A O   
1055 C CB  . PHE A 70  ? 0.37779 0.38714 0.36320 -0.03142 0.00383  0.00270  70  PHE A CB  
1056 C CG  . PHE A 70  ? 0.36118 0.37070 0.34286 -0.02793 0.00283  0.00320  70  PHE A CG  
1057 C CD1 . PHE A 70  ? 0.37055 0.37976 0.35105 -0.02522 0.00519  0.00306  70  PHE A CD1 
1058 C CD2 . PHE A 70  ? 0.42085 0.43071 0.39991 -0.02700 -0.00078 0.00393  70  PHE A CD2 
1059 C CE1 . PHE A 70  ? 0.41717 0.42735 0.39399 -0.02178 0.00387  0.00350  70  PHE A CE1 
1060 C CE2 . PHE A 70  ? 0.46836 0.47859 0.44348 -0.02317 -0.00191 0.00434  70  PHE A CE2 
1061 C CZ  . PHE A 70  ? 0.40702 0.41790 0.38104 -0.02064 0.00036  0.00405  70  PHE A CZ  
1071 N N   . GLU A 71  ? 0.33745 0.33837 0.31934 -0.02895 -0.00622 0.00436  71  GLU A N   
1072 C CA  . GLU A 71  ? 0.34822 0.34493 0.32641 -0.02685 -0.01125 0.00521  71  GLU A CA  
1073 C C   . GLU A 71  ? 0.33702 0.32929 0.31344 -0.02352 -0.01265 0.00539  71  GLU A C   
1074 O O   . GLU A 71  ? 0.38022 0.36876 0.35320 -0.02015 -0.01576 0.00576  71  GLU A O   
1075 C CB  . GLU A 71  ? 0.38523 0.38275 0.36393 -0.03092 -0.01423 0.00569  71  GLU A CB  
1076 C CG  . GLU A 71  ? 0.49552 0.49748 0.47526 -0.03340 -0.01393 0.00591  71  GLU A CG  
1077 C CD  . GLU A 71  ? 0.78956 0.78998 0.76547 -0.02956 -0.01518 0.00642  71  GLU A CD  
1078 O OE1 . GLU A 71  ? 0.93905 0.93384 0.91091 -0.02643 -0.01911 0.00703  71  GLU A OE1 
1079 O OE2 . GLU A 71  ? 0.58942 0.59456 0.56608 -0.02970 -0.01216 0.00613  71  GLU A OE2 
1086 N N   . TYR A 72  ? 0.33469 0.32765 0.31333 -0.02427 -0.01029 0.00511  72  TYR A N   
1087 C CA  . TYR A 72  ? 0.32621 0.31619 0.30335 -0.02133 -0.01130 0.00544  72  TYR A CA  
1088 C C   . TYR A 72  ? 0.30622 0.29589 0.28349 -0.01686 -0.00895 0.00540  72  TYR A C   
1089 O O   . TYR A 72  ? 0.31826 0.30561 0.29345 -0.01327 -0.01098 0.00570  72  TYR A O   
1090 C CB  . TYR A 72  ? 0.33261 0.32414 0.31156 -0.02370 -0.00990 0.00538  72  TYR A CB  
1091 C CG  . TYR A 72  ? 0.30295 0.29224 0.27944 -0.02177 -0.01198 0.00592  72  TYR A CG  
1092 C CD1 . TYR A 72  ? 0.35299 0.33937 0.32587 -0.02226 -0.01669 0.00631  72  TYR A CD1 
1093 C CD2 . TYR A 72  ? 0.32610 0.31629 0.30364 -0.01944 -0.00905 0.00609  72  TYR A CD2 
1094 C CE1 . TYR A 72  ? 0.36742 0.35213 0.33765 -0.02077 -0.01838 0.00667  72  TYR A CE1 
1095 C CE2 . TYR A 72  ? 0.32085 0.31015 0.29612 -0.01766 -0.01059 0.00662  72  TYR A CE2 
1096 C CZ  . TYR A 72  ? 0.33115 0.31786 0.30269 -0.01851 -0.01525 0.00682  72  TYR A CZ  
1097 O OH  . TYR A 72  ? 0.34925 0.33552 0.31821 -0.01714 -0.01656 0.00721  72  TYR A OH  
1107 N N   . TYR A 73  ? 0.33838 0.33065 0.31811 -0.01720 -0.00472 0.00502  73  TYR A N   
1108 C CA  . TYR A 73  ? 0.32802 0.32050 0.30823 -0.01346 -0.00226 0.00518  73  TYR A CA  
1109 C C   . TYR A 73  ? 0.29064 0.28463 0.26961 -0.01176 -0.00197 0.00503  73  TYR A C   
1110 O O   . TYR A 73  ? 0.30663 0.30106 0.28541 -0.00821 -0.00116 0.00531  73  TYR A O   
1111 C CB  . TYR A 73  ? 0.30551 0.29931 0.28881 -0.01465 0.00266  0.00500  73  TYR A CB  
1112 C CG  . TYR A 73  ? 0.31450 0.30777 0.29878 -0.01572 0.00295  0.00519  73  TYR A CG  
1113 C CD1 . TYR A 73  ? 0.33348 0.32577 0.31708 -0.01253 0.00229  0.00595  73  TYR A CD1 
1114 C CD2 . TYR A 73  ? 0.33838 0.33313 0.32425 -0.01989 0.00399  0.00458  73  TYR A CD2 
1115 C CE1 . TYR A 73  ? 0.32507 0.31783 0.30892 -0.01343 0.00268  0.00622  73  TYR A CE1 
1116 C CE2 . TYR A 73  ? 0.33162 0.32674 0.31787 -0.02071 0.00407  0.00475  73  TYR A CE2 
1117 C CZ  . TYR A 73  ? 0.33387 0.32799 0.31882 -0.01750 0.00346  0.00561  73  TYR A CZ  
1118 O OH  . TYR A 73  ? 0.33914 0.33456 0.32388 -0.01834 0.00367  0.00583  73  TYR A OH  
1128 N N   . HIS A 74  ? 0.29405 0.28975 0.27225 -0.01424 -0.00245 0.00470  74  HIS A N   
1129 C CA  . HIS A 74  ? 0.31513 0.31343 0.29153 -0.01293 -0.00197 0.00460  74  HIS A CA  
1130 C C   . HIS A 74  ? 0.40804 0.40893 0.38603 -0.01331 0.00277  0.00433  74  HIS A C   
1131 O O   . HIS A 74  ? 0.36038 0.36307 0.33669 -0.01064 0.00307  0.00451  74  HIS A O   
1132 C CB  . HIS A 74  ? 0.35667 0.35341 0.32974 -0.00799 -0.00578 0.00496  74  HIS A CB  
1133 C CG  . HIS A 74  ? 0.38241 0.37611 0.35282 -0.00766 -0.01042 0.00515  74  HIS A CG  
1134 N ND1 . HIS A 74  ? 0.39377 0.38549 0.36066 -0.00338 -0.01418 0.00525  74  HIS A ND1 
1135 C CD2 . HIS A 74  ? 0.40956 0.40177 0.38015 -0.01111 -0.01201 0.00528  74  HIS A CD2 
1136 C CE1 . HIS A 74  ? 0.40199 0.39022 0.36670 -0.00422 -0.01773 0.00545  74  HIS A CE1 
1137 N NE2 . HIS A 74  ? 0.40672 0.39538 0.37367 -0.00900 -0.01657 0.00558  74  HIS A NE2 
1145 N N   . THR A 75  ? 0.33381 0.33487 0.31482 -0.01664 0.00636  0.00391  75  THR A N   
1146 C CA  . THR A 75  ? 0.34905 0.35176 0.33129 -0.01788 0.01116  0.00354  75  THR A CA  
1147 C C   . THR A 75  ? 0.36737 0.37161 0.35207 -0.02310 0.01427  0.00255  75  THR A C   
1148 O O   . THR A 75  ? 0.38501 0.38865 0.37133 -0.02512 0.01299  0.00232  75  THR A O   
1149 C CB  . THR A 75  ? 0.39391 0.39419 0.37751 -0.01512 0.01302  0.00413  75  THR A CB  
1150 O OG1 . THR A 75  ? 0.40052 0.40158 0.38503 -0.01682 0.01780  0.00381  75  THR A OG1 
1151 C CG2 . THR A 75  ? 0.44333 0.44108 0.42893 -0.01560 0.01282  0.00423  75  THR A CG2 
1159 N N   . THR A 76  ? 0.33549 0.34227 0.32030 -0.02550 0.01827  0.00187  76  THR A N   
1160 C CA  . THR A 76  ? 0.39164 0.39992 0.37913 -0.03044 0.02207  0.00064  76  THR A CA  
1161 C C   . THR A 76  ? 0.35639 0.36259 0.34463 -0.03084 0.02687  0.00027  76  THR A C   
1162 O O   . THR A 76  ? 0.43838 0.44610 0.42785 -0.03495 0.03085  -0.00098 76  THR A O   
1163 C CB  . THR A 76  ? 0.38680 0.40068 0.37382 -0.03424 0.02296  -0.00011 76  THR A CB  
1164 O OG1 . THR A 76  ? 0.37898 0.39532 0.36262 -0.03301 0.02387  0.00018  76  THR A OG1 
1165 C CG2 . THR A 76  ? 0.44757 0.46319 0.43449 -0.03446 0.01858  0.00034  76  THR A CG2 
1173 N N   . ASP A 77  ? 0.36866 0.37154 0.35620 -0.02672 0.02665  0.00134  77  ASP A N   
1174 C CA  . ASP A 77  ? 0.37806 0.37821 0.36628 -0.02677 0.03109  0.00131  77  ASP A CA  
1175 C C   . ASP A 77  ? 0.40803 0.40561 0.39908 -0.02857 0.03325  0.00056  77  ASP A C   
1176 O O   . ASP A 77  ? 0.37087 0.36716 0.36295 -0.02662 0.03075  0.00109  77  ASP A O   
1177 C CB  . ASP A 77  ? 0.39257 0.39062 0.37999 -0.02174 0.03012  0.00290  77  ASP A CB  
1178 C CG  . ASP A 77  ? 0.48408 0.47890 0.47223 -0.02165 0.03476  0.00320  77  ASP A CG  
1179 O OD1 . ASP A 77  ? 0.61857 0.61318 0.60643 -0.02558 0.03862  0.00208  77  ASP A OD1 
1180 O OD2 . ASP A 77  ? 0.60514 0.59780 0.59406 -0.01779 0.03465  0.00455  77  ASP A OD2 
1185 N N   . PRO A 78  ? 0.45722 0.45435 0.44928 -0.03234 0.03774  -0.00079 78  PRO A N   
1186 C CA  . PRO A 78  ? 0.48795 0.48358 0.48267 -0.03419 0.03941  -0.00182 78  PRO A CA  
1187 C C   . PRO A 78  ? 0.45570 0.44708 0.45098 -0.03015 0.03954  -0.00069 78  PRO A C   
1188 O O   . PRO A 78  ? 0.51417 0.50563 0.51099 -0.03040 0.03868  -0.00107 78  PRO A O   
1189 C CB  . PRO A 78  ? 0.59035 0.58552 0.58540 -0.03838 0.04473  -0.00348 78  PRO A CB  
1190 C CG  . PRO A 78  ? 0.59441 0.59339 0.58724 -0.04034 0.04487  -0.00362 78  PRO A CG  
1191 C CD  . PRO A 78  ? 0.53989 0.53859 0.53042 -0.03556 0.04135  -0.00164 78  PRO A CD  
1199 N N   . SER A 79  ? 0.47517 0.46371 0.46921 -0.02648 0.04054  0.00076  79  SER A N   
1200 C CA  . SER A 79  ? 0.45974 0.44493 0.45442 -0.02256 0.04138  0.00201  79  SER A CA  
1201 C C   . SER A 79  ? 0.54106 0.52767 0.53544 -0.01851 0.03697  0.00356  79  SER A C   
1202 O O   . SER A 79  ? 0.47315 0.45818 0.46797 -0.01508 0.03759  0.00476  79  SER A O   
1203 C CB  . SER A 79  ? 0.52930 0.51091 0.52327 -0.02076 0.04520  0.00298  79  SER A CB  
1204 O OG  . SER A 79  ? 0.53400 0.51753 0.52655 -0.01905 0.04334  0.00409  79  SER A OG  
1210 N N   . PHE A 80  ? 0.38321 0.37281 0.37665 -0.01883 0.03275  0.00352  80  PHE A N   
1211 C CA  . PHE A 80  ? 0.35676 0.34725 0.34947 -0.01500 0.02865  0.00484  80  PHE A CA  
1212 C C   . PHE A 80  ? 0.36249 0.35260 0.35582 -0.01388 0.02771  0.00523  80  PHE A C   
1213 O O   . PHE A 80  ? 0.37790 0.36776 0.37117 -0.01001 0.02736  0.00661  80  PHE A O   
1214 C CB  . PHE A 80  ? 0.38120 0.37416 0.37243 -0.01593 0.02425  0.00447  80  PHE A CB  
1215 C CG  . PHE A 80  ? 0.33815 0.33142 0.32827 -0.01216 0.02001  0.00555  80  PHE A CG  
1216 C CD1 . PHE A 80  ? 0.37386 0.36785 0.36316 -0.00855 0.01901  0.00645  80  PHE A CD1 
1217 C CD2 . PHE A 80  ? 0.33148 0.32472 0.32127 -0.01241 0.01702  0.00559  80  PHE A CD2 
1218 C CE1 . PHE A 80  ? 0.33303 0.32754 0.32149 -0.00523 0.01523  0.00716  80  PHE A CE1 
1219 C CE2 . PHE A 80  ? 0.34866 0.34192 0.33709 -0.00933 0.01338  0.00640  80  PHE A CE2 
1220 C CZ  . PHE A 80  ? 0.33675 0.33058 0.32468 -0.00566 0.01259  0.00710  80  PHE A CZ  
1230 N N   . LEU A 81  ? 0.33032 0.32139 0.32420 -0.01732 0.02715  0.00405  81  LEU A N   
1231 C CA  . LEU A 81  ? 0.35494 0.34672 0.34868 -0.01651 0.02568  0.00444  81  LEU A CA  
1232 C C   . LEU A 81  ? 0.40121 0.39125 0.39549 -0.01371 0.02960  0.00522  81  LEU A C   
1233 O O   . LEU A 81  ? 0.39198 0.38288 0.38547 -0.01073 0.02871  0.00643  81  LEU A O   
1234 C CB  . LEU A 81  ? 0.39131 0.38537 0.38575 -0.02101 0.02431  0.00303  81  LEU A CB  
1235 C CG  . LEU A 81  ? 0.65190 0.64823 0.64535 -0.02308 0.01914  0.00291  81  LEU A CG  
1236 C CD1 . LEU A 81  ? 0.64930 0.64522 0.64047 -0.01995 0.01558  0.00426  81  LEU A CD1 
1237 C CD2 . LEU A 81  ? 0.80147 0.79820 0.79479 -0.02451 0.01833  0.00247  81  LEU A CD2 
1249 N N   . GLY A 82  ? 0.43368 0.42131 0.42900 -0.01459 0.03413  0.00461  82  GLY A N   
1250 C CA  . GLY A 82  ? 0.46870 0.45389 0.46424 -0.01146 0.03809  0.00557  82  GLY A CA  
1251 C C   . GLY A 82  ? 0.47036 0.45521 0.46567 -0.00665 0.03828  0.00773  82  GLY A C   
1252 O O   . GLY A 82  ? 0.41376 0.39886 0.40898 -0.00310 0.03962  0.00915  82  GLY A O   
1256 N N   . ARG A 83  ? 0.38744 0.37258 0.38272 -0.00639 0.03697  0.00805  83  ARG A N   
1257 C CA  . ARG A 83  ? 0.38762 0.37357 0.38326 -0.00196 0.03686  0.01001  83  ARG A CA  
1258 C C   . ARG A 83  ? 0.40937 0.39869 0.40454 0.00053  0.03304  0.01087  83  ARG A C   
1259 O O   . ARG A 83  ? 0.36277 0.35357 0.35861 0.00447  0.03397  0.01257  83  ARG A O   
1260 C CB  . ARG A 83  ? 0.44651 0.43271 0.44196 -0.00251 0.03625  0.00995  83  ARG A CB  
1261 C CG  . ARG A 83  ? 0.50603 0.48881 0.50147 -0.00495 0.04076  0.00934  83  ARG A CG  
1262 C CD  . ARG A 83  ? 0.59155 0.57499 0.58615 -0.00580 0.04089  0.00943  83  ARG A CD  
1263 N NE  . ARG A 83  ? 0.64772 0.63382 0.64092 -0.00867 0.03775  0.00804  83  ARG A NE  
1264 C CZ  . ARG A 83  ? 0.50847 0.49792 0.50102 -0.00676 0.03334  0.00841  83  ARG A CZ  
1265 N NH1 . ARG A 83  ? 0.41289 0.40381 0.40633 -0.00239 0.03148  0.00990  83  ARG A NH1 
1266 N NH2 . ARG A 83  ? 0.47860 0.47020 0.46951 -0.00920 0.03090  0.00726  83  ARG A NH2 
1280 N N   . TYR A 84  ? 0.35934 0.35003 0.35328 -0.00187 0.02890  0.00976  84  TYR A N   
1281 C CA  . TYR A 84  ? 0.31681 0.31005 0.30960 -0.00029 0.02520  0.01034  84  TYR A CA  
1282 C C   . TYR A 84  ? 0.35440 0.34888 0.34677 0.00081  0.02675  0.01102  84  TYR A C   
1283 O O   . TYR A 84  ? 0.33158 0.32858 0.32371 0.00414  0.02656  0.01241  84  TYR A O   
1284 C CB  . TYR A 84  ? 0.32009 0.31354 0.31131 -0.00373 0.02078  0.00899  84  TYR A CB  
1285 C CG  . TYR A 84  ? 0.33579 0.33089 0.32505 -0.00352 0.01678  0.00922  84  TYR A CG  
1286 C CD1 . TYR A 84  ? 0.35238 0.34923 0.34122 0.00017  0.01579  0.01040  84  TYR A CD1 
1287 C CD2 . TYR A 84  ? 0.37362 0.36891 0.36141 -0.00733 0.01390  0.00825  84  TYR A CD2 
1288 C CE1 . TYR A 84  ? 0.34201 0.34022 0.32848 -0.00012 0.01221  0.01047  84  TYR A CE1 
1289 C CE2 . TYR A 84  ? 0.40511 0.40153 0.39047 -0.00762 0.01010  0.00850  84  TYR A CE2 
1290 C CZ  . TYR A 84  ? 0.47096 0.46858 0.45541 -0.00411 0.00937  0.00955  84  TYR A CZ  
1291 O OH  . TYR A 84  ? 0.47132 0.46992 0.45286 -0.00482 0.00576  0.00967  84  TYR A OH  
1301 N N   . MET A 85  ? 0.33488 0.32839 0.32710 -0.00189 0.02841  0.01003  85  MET A N   
1302 C CA  . MET A 85  ? 0.35759 0.35286 0.34887 -0.00079 0.02989  0.01057  85  MET A CA  
1303 C C   . MET A 85  ? 0.37982 0.37481 0.37202 0.00385  0.03428  0.01238  85  MET A C   
1304 O O   . MET A 85  ? 0.36335 0.36159 0.35455 0.00679  0.03466  0.01378  85  MET A O   
1305 C CB  . MET A 85  ? 0.41327 0.40762 0.40469 -0.00454 0.03099  0.00889  85  MET A CB  
1306 C CG  . MET A 85  ? 0.40612 0.40323 0.39624 -0.00850 0.02666  0.00772  85  MET A CG  
1307 S SD  . MET A 85  ? 0.43639 0.43777 0.42333 -0.00805 0.02213  0.00865  85  MET A SD  
1308 C CE  . MET A 85  ? 0.41321 0.41347 0.39955 -0.00825 0.01774  0.00882  85  MET A CE  
1318 N N   . SER A 86  ? 0.38564 0.37704 0.37954 0.00441  0.03781  0.01249  86  SER A N   
1319 C CA  . SER A 86  ? 0.44521 0.43593 0.44012 0.00876  0.04203  0.01445  86  SER A CA  
1320 C C   . SER A 86  ? 0.38898 0.38378 0.38464 0.01258  0.04061  0.01636  86  SER A C   
1321 O O   . SER A 86  ? 0.40537 0.40287 0.40120 0.01634  0.04278  0.01819  86  SER A O   
1322 C CB  . SER A 86  ? 0.50924 0.49513 0.50550 0.00814  0.04546  0.01429  86  SER A CB  
1323 O OG  . SER A 86  ? 0.72217 0.70439 0.71786 0.00518  0.04787  0.01262  86  SER A OG  
1329 N N   . ALA A 87  ? 0.37605 0.37192 0.37218 0.01177  0.03701  0.01593  87  ALA A N   
1330 C CA  . ALA A 87  ? 0.34140 0.34167 0.33854 0.01526  0.03540  0.01741  87  ALA A CA  
1331 C C   . ALA A 87  ? 0.35778 0.36222 0.35301 0.01585  0.03326  0.01766  87  ALA A C   
1332 O O   . ALA A 87  ? 0.35166 0.36055 0.34762 0.01942  0.03436  0.01936  87  ALA A O   
1333 C CB  . ALA A 87  ? 0.31744 0.31779 0.31502 0.01428  0.03175  0.01657  87  ALA A CB  
1339 N N   . LEU A 88  ? 0.32569 0.32932 0.31840 0.01214  0.03024  0.01604  88  LEU A N   
1340 C CA  . LEU A 88  ? 0.34992 0.35746 0.34004 0.01191  0.02773  0.01618  88  LEU A CA  
1341 C C   . LEU A 88  ? 0.35198 0.36283 0.34125 0.01442  0.03128  0.01763  88  LEU A C   
1342 O O   . LEU A 88  ? 0.37577 0.39172 0.36357 0.01614  0.03066  0.01865  88  LEU A O   
1343 C CB  . LEU A 88  ? 0.32779 0.33370 0.31540 0.00706  0.02402  0.01433  88  LEU A CB  
1344 C CG  . LEU A 88  ? 0.34314 0.35264 0.32725 0.00573  0.02080  0.01432  88  LEU A CG  
1345 C CD1 . LEU A 88  ? 0.35530 0.36669 0.33884 0.00731  0.01802  0.01475  88  LEU A CD1 
1346 C CD2 . LEU A 88  ? 0.38017 0.38792 0.36236 0.00063  0.01733  0.01266  88  LEU A CD2 
1358 N N   . ASN A 89  ? 0.35514 0.36337 0.34500 0.01470  0.03514  0.01770  89  ASN A N   
1359 C CA  . ASN A 89  ? 0.39874 0.41008 0.38738 0.01767  0.03871  0.01916  89  ASN A CA  
1360 C C   . ASN A 89  ? 0.41875 0.43437 0.40910 0.02264  0.04113  0.02161  89  ASN A C   
1361 O O   . ASN A 89  ? 0.44841 0.46921 0.43711 0.02527  0.04300  0.02308  89  ASN A O   
1362 C CB  . ASN A 89  ? 0.43741 0.44421 0.42658 0.01769  0.04274  0.01879  89  ASN A CB  
1363 C CG  . ASN A 89  ? 0.51319 0.52298 0.49953 0.01910  0.04481  0.01928  89  ASN A CG  
1364 O OD1 . ASN A 89  ? 0.49324 0.50730 0.47660 0.01722  0.04187  0.01870  89  ASN A OD1 
1365 N ND2 . ASN A 89  ? 0.58012 0.58791 0.56701 0.02255  0.04981  0.02047  89  ASN A ND2 
1372 N N   . HIS A 90  ? 0.36980 0.38424 0.36344 0.02398  0.04114  0.02213  90  HIS A N   
1373 C CA  . HIS A 90  ? 0.37775 0.39737 0.37390 0.02844  0.04293  0.02441  90  HIS A CA  
1374 C C   . HIS A 90  ? 0.34093 0.36576 0.33675 0.02825  0.03890  0.02414  90  HIS A C   
1375 O O   . HIS A 90  ? 0.37558 0.40721 0.37137 0.03096  0.03994  0.02565  90  HIS A O   
1376 C CB  . HIS A 90  ? 0.39729 0.41402 0.39733 0.03003  0.04483  0.02521  90  HIS A CB  
1377 C CG  . HIS A 90  ? 0.44020 0.45153 0.44056 0.03061  0.04934  0.02575  90  HIS A CG  
1378 N ND1 . HIS A 90  ? 0.49600 0.50891 0.49744 0.03487  0.05415  0.02824  90  HIS A ND1 
1379 C CD2 . HIS A 90  ? 0.52231 0.52659 0.52194 0.02743  0.04995  0.02411  90  HIS A CD2 
1380 C CE1 . HIS A 90  ? 0.71809 0.72422 0.71913 0.03434  0.05741  0.02802  90  HIS A CE1 
1381 N NE2 . HIS A 90  ? 0.56839 0.56940 0.56839 0.02969  0.05499  0.02543  90  HIS A NE2 
1389 N N   . THR A 91  ? 0.34555 0.36746 0.34106 0.02520  0.03449  0.02225  91  THR A N   
1390 C CA  . THR A 91  ? 0.35144 0.37739 0.34677 0.02544  0.03079  0.02192  91  THR A CA  
1391 C C   . THR A 91  ? 0.34293 0.37243 0.33412 0.02388  0.02900  0.02160  91  THR A C   
1392 O O   . THR A 91  ? 0.33395 0.36836 0.32480 0.02485  0.02731  0.02183  91  THR A O   
1393 C CB  . THR A 91  ? 0.30305 0.32472 0.29834 0.02288  0.02639  0.01999  91  THR A CB  
1394 O OG1 . THR A 91  ? 0.34188 0.35903 0.33376 0.01843  0.02392  0.01822  91  THR A OG1 
1395 C CG2 . THR A 91  ? 0.29657 0.31546 0.29519 0.02396  0.02791  0.02023  91  THR A CG2 
1403 N N   . LYS A 92  ? 0.33926 0.36684 0.32714 0.02126  0.02917  0.02098  92  LYS A N   
1404 C CA  . LYS A 92  ? 0.35455 0.38651 0.33799 0.01967  0.02752  0.02090  92  LYS A CA  
1405 C C   . LYS A 92  ? 0.39373 0.43363 0.37706 0.02357  0.03124  0.02309  92  LYS A C   
1406 O O   . LYS A 92  ? 0.39979 0.44500 0.37939 0.02261  0.02993  0.02323  92  LYS A O   
1407 C CB  . LYS A 92  ? 0.42262 0.45189 0.40275 0.01601  0.02667  0.01979  92  LYS A CB  
1408 C CG  . LYS A 92  ? 0.50854 0.53824 0.48905 0.01812  0.03146  0.02080  92  LYS A CG  
1409 C CD  . LYS A 92  ? 0.55422 0.58124 0.53221 0.01422  0.03016  0.01924  92  LYS A CD  
1410 C CE  . LYS A 92  ? 0.57249 0.60075 0.54995 0.01676  0.03480  0.02016  92  LYS A CE  
1411 N NZ  . LYS A 92  ? 0.56148 0.58813 0.53691 0.01308  0.03346  0.01846  92  LYS A NZ  
1425 N N   . LYS A 93  ? 0.39015 0.43133 0.37729 0.02784  0.03585  0.02491  93  LYS A N   
1426 C CA  . LYS A 93  ? 0.45869 0.50809 0.44641 0.03209  0.03983  0.02734  93  LYS A CA  
1427 C C   . LYS A 93  ? 0.41689 0.47135 0.40890 0.03497  0.04002  0.02837  93  LYS A C   
1428 O O   . LYS A 93  ? 0.42832 0.49112 0.42132 0.03839  0.04314  0.03043  93  LYS A O   
1429 C CB  . LYS A 93  ? 0.47339 0.52150 0.46248 0.03538  0.04519  0.02906  93  LYS A CB  
1430 C CG  . LYS A 93  ? 0.51132 0.55489 0.49665 0.03294  0.04530  0.02789  93  LYS A CG  
1431 C CD  . LYS A 93  ? 0.72115 0.76143 0.70792 0.03614  0.05047  0.02921  93  LYS A CD  
1432 C CE  . LYS A 93  ? 1.02612 1.06126 1.00976 0.03327  0.05008  0.02745  93  LYS A CE  
1433 N NZ  . LYS A 93  ? 1.20301 1.23149 1.18866 0.03509  0.05420  0.02779  93  LYS A NZ  
1447 N N   . TRP A 94  ? 0.35039 0.40084 0.34509 0.03387  0.03689  0.02706  94  TRP A N   
1448 C CA  . TRP A 94  ? 0.33543 0.39138 0.33410 0.03632  0.03625  0.02764  94  TRP A CA  
1449 C C   . TRP A 94  ? 0.39751 0.45901 0.39305 0.03485  0.03352  0.02683  94  TRP A C   
1450 O O   . TRP A 94  ? 0.37483 0.43389 0.36502 0.03111  0.03087  0.02542  94  TRP A O   
1451 C CB  . TRP A 94  ? 0.30627 0.35663 0.30764 0.03537  0.03306  0.02618  94  TRP A CB  
1452 C CG  . TRP A 94  ? 0.32085 0.36686 0.32557 0.03676  0.03567  0.02704  94  TRP A CG  
1453 C CD1 . TRP A 94  ? 0.35955 0.40505 0.36532 0.03888  0.04065  0.02896  94  TRP A CD1 
1454 C CD2 . TRP A 94  ? 0.32321 0.36415 0.32981 0.03573  0.03341  0.02589  94  TRP A CD2 
1455 N NE1 . TRP A 94  ? 0.36142 0.40158 0.36971 0.03897  0.04160  0.02905  94  TRP A NE1 
1456 C CE2 . TRP A 94  ? 0.32929 0.36719 0.33811 0.03701  0.03724  0.02723  94  TRP A CE2 
1457 C CE3 . TRP A 94  ? 0.32560 0.36452 0.33188 0.03403  0.02858  0.02392  94  TRP A CE3 
1458 C CZ2 . TRP A 94  ? 0.30708 0.34060 0.31757 0.03617  0.03639  0.02664  94  TRP A CZ2 
1459 C CZ3 . TRP A 94  ? 0.31256 0.34768 0.32060 0.03372  0.02778  0.02343  94  TRP A CZ3 
1460 C CH2 . TRP A 94  ? 0.29230 0.32502 0.30235 0.03456  0.03166  0.02477  94  TRP A CH2 
1471 N N   . LYS A 95  ? 0.34421 0.41343 0.34321 0.03755  0.03404  0.02766  95  LYS A N   
1472 C CA  . LYS A 95  ? 0.37969 0.45423 0.37622 0.03615  0.03150  0.02666  95  LYS A CA  
1473 C C   . LYS A 95  ? 0.36010 0.43210 0.35880 0.03558  0.02702  0.02471  95  LYS A C   
1474 O O   . LYS A 95  ? 0.34722 0.41904 0.35120 0.03810  0.02727  0.02509  95  LYS A O   
1475 C CB  . LYS A 95  ? 0.38617 0.47299 0.38497 0.03963  0.03560  0.02888  95  LYS A CB  
1476 C CG  . LYS A 95  ? 0.48498 0.57602 0.48094 0.04081  0.04021  0.03098  95  LYS A CG  
1477 C CD  . LYS A 95  ? 0.51229 0.59933 0.50049 0.03641  0.03796  0.02960  95  LYS A CD  
1478 C CE  . LYS A 95  ? 0.63766 0.73143 0.62224 0.03785  0.04228  0.03163  95  LYS A CE  
1479 N NZ  . LYS A 95  ? 1.05758 1.15878 1.04707 0.04350  0.04813  0.03467  95  LYS A NZ  
1493 N N   . TYR A 96  ? 0.34520 0.41557 0.33946 0.03234  0.02288  0.02268  96  TYR A N   
1494 C CA  . TYR A 96  ? 0.30674 0.37316 0.30154 0.03152  0.01805  0.02047  96  TYR A CA  
1495 C C   . TYR A 96  ? 0.33858 0.41181 0.33236 0.03142  0.01681  0.01970  96  TYR A C   
1496 O O   . TYR A 96  ? 0.39095 0.46072 0.37903 0.02779  0.01342  0.01798  96  TYR A O   
1497 C CB  . TYR A 96  ? 0.33479 0.39030 0.32468 0.02731  0.01381  0.01850  96  TYR A CB  
1498 C CG  . TYR A 96  ? 0.30742 0.35726 0.29856 0.02719  0.01548  0.01913  96  TYR A CG  
1499 C CD1 . TYR A 96  ? 0.30657 0.35372 0.30203 0.02918  0.01533  0.01907  96  TYR A CD1 
1500 C CD2 . TYR A 96  ? 0.33539 0.38331 0.32338 0.02512  0.01735  0.01976  96  TYR A CD2 
1501 C CE1 . TYR A 96  ? 0.32943 0.37154 0.32577 0.02870  0.01715  0.01954  96  TYR A CE1 
1502 C CE2 . TYR A 96  ? 0.32612 0.36891 0.31543 0.02492  0.01909  0.02010  96  TYR A CE2 
1503 C CZ  . TYR A 96  ? 0.33569 0.37545 0.32911 0.02658  0.01912  0.01998  96  TYR A CZ  
1504 O OH  . TYR A 96  ? 0.32765 0.36242 0.32210 0.02604  0.02107  0.02021  96  TYR A OH  
1514 N N   . PRO A 97  ? 0.35044 0.43361 0.34970 0.03518  0.01950  0.02094  97  PRO A N   
1515 C CA  . PRO A 97  ? 0.35756 0.44832 0.35618 0.03496  0.01877  0.02009  97  PRO A CA  
1516 C C   . PRO A 97  ? 0.37529 0.46130 0.37357 0.03415  0.01343  0.01729  97  PRO A C   
1517 O O   . PRO A 97  ? 0.36706 0.44815 0.36830 0.03564  0.01121  0.01659  97  PRO A O   
1518 C CB  . PRO A 97  ? 0.38917 0.49253 0.39511 0.03963  0.02348  0.02244  97  PRO A CB  
1519 C CG  . PRO A 97  ? 0.33959 0.43956 0.35098 0.04244  0.02409  0.02345  97  PRO A CG  
1520 C CD  . PRO A 97  ? 0.36175 0.45019 0.36818 0.03961  0.02338  0.02320  97  PRO A CD  
1528 N N   . GLN A 98  ? 0.35400 0.44160 0.34809 0.03174  0.01142  0.01567  98  GLN A N   
1529 C CA  . GLN A 98  ? 0.36209 0.44653 0.35581 0.03150  0.00675  0.01296  98  GLN A CA  
1530 C C   . GLN A 98  ? 0.33624 0.43232 0.33754 0.03573  0.00842  0.01324  98  GLN A C   
1531 O O   . GLN A 98  ? 0.38498 0.49190 0.38764 0.03621  0.01175  0.01419  98  GLN A O   
1532 C CB  . GLN A 98  ? 0.35815 0.43938 0.34403 0.02696  0.00413  0.01110  98  GLN A CB  
1533 C CG  . GLN A 98  ? 0.40696 0.47683 0.38548 0.02247  0.00163  0.01069  98  GLN A CG  
1534 C CD  . GLN A 98  ? 0.44976 0.50841 0.42820 0.02261  -0.00259 0.00930  98  GLN A CD  
1535 O OE1 . GLN A 98  ? 0.45505 0.51043 0.43349 0.02344  -0.00621 0.00725  98  GLN A OE1 
1536 N NE2 . GLN A 98  ? 0.40695 0.46009 0.38519 0.02191  -0.00202 0.01035  98  GLN A NE2 
1545 N N   . VAL A 99  ? 0.34934 0.44430 0.35558 0.03875  0.00618  0.01250  99  VAL A N   
1546 C CA  . VAL A 99  ? 0.33612 0.44270 0.35021 0.04284  0.00718  0.01270  99  VAL A CA  
1547 C C   . VAL A 99  ? 0.35962 0.46279 0.37311 0.04327  0.00180  0.00948  99  VAL A C   
1548 O O   . VAL A 99  ? 0.37826 0.47217 0.39014 0.04347  -0.00192 0.00830  99  VAL A O   
1549 C CB  . VAL A 99  ? 0.30845 0.41922 0.32985 0.04667  0.00972  0.01513  99  VAL A CB  
1550 C CG1 . VAL A 99  ? 0.33667 0.46114 0.36663 0.05071  0.01058  0.01546  99  VAL A CG1 
1551 C CG2 . VAL A 99  ? 0.30230 0.41455 0.32351 0.04642  0.01496  0.01820  99  VAL A CG2 
1561 N N   . ASN A 100 ? 0.36044 0.47153 0.37514 0.04355  0.00156  0.00805  100 ASN A N   
1562 C CA  . ASN A 100 ? 0.38222 0.49028 0.39574 0.04396  -0.00341 0.00471  100 ASN A CA  
1563 C C   . ASN A 100 ? 0.44316 0.53491 0.44793 0.04076  -0.00810 0.00269  100 ASN A C   
1564 O O   . ASN A 100 ? 0.41179 0.49747 0.41596 0.04231  -0.01252 0.00070  100 ASN A O   
1565 C CB  . ASN A 100 ? 0.42934 0.54333 0.45066 0.04881  -0.00502 0.00445  100 ASN A CB  
1566 C CG  . ASN A 100 ? 0.48824 0.60403 0.50990 0.05004  -0.00909 0.00109  100 ASN A CG  
1567 O OD1 . ASN A 100 ? 0.46097 0.58238 0.48194 0.04869  -0.00823 -0.00015 100 ASN A OD1 
1568 N ND2 . ASN A 100 ? 0.52053 0.63155 0.54270 0.05252  -0.01354 -0.00051 100 ASN A ND2 
1575 N N   . GLY A 101 ? 0.43080 0.51621 0.42875 0.03639  -0.00717 0.00329  101 GLY A N   
1576 C CA  . GLY A 101 ? 0.46895 0.53986 0.45844 0.03273  -0.01136 0.00163  101 GLY A CA  
1577 C C   . GLY A 101 ? 0.46878 0.53034 0.45723 0.03269  -0.01261 0.00253  101 GLY A C   
1578 O O   . GLY A 101 ? 0.44932 0.49928 0.43140 0.02998  -0.01625 0.00125  101 GLY A O   
1582 N N   . LEU A 102 ? 0.34790 0.41429 0.34236 0.03546  -0.00962 0.00471  102 LEU A N   
1583 C CA  . LEU A 102 ? 0.35787 0.41653 0.35179 0.03535  -0.01026 0.00555  102 LEU A CA  
1584 C C   . LEU A 102 ? 0.38775 0.44836 0.38259 0.03417  -0.00560 0.00825  102 LEU A C   
1585 O O   . LEU A 102 ? 0.35309 0.42331 0.35151 0.03540  -0.00139 0.00999  102 LEU A O   
1586 C CB  . LEU A 102 ? 0.34640 0.40809 0.34619 0.03975  -0.01126 0.00552  102 LEU A CB  
1587 C CG  . LEU A 102 ? 0.42408 0.48506 0.42365 0.04199  -0.01597 0.00282  102 LEU A CG  
1588 C CD1 . LEU A 102 ? 0.47292 0.53914 0.47850 0.04637  -0.01661 0.00318  102 LEU A CD1 
1589 C CD2 . LEU A 102 ? 0.49863 0.54658 0.49042 0.03946  -0.02051 0.00081  102 LEU A CD2 
1601 N N   . THR A 103 ? 0.32635 0.37812 0.31805 0.03197  -0.00625 0.00861  103 THR A N   
1602 C CA  . THR A 103 ? 0.29821 0.35114 0.29099 0.03125  -0.00199 0.01094  103 THR A CA  
1603 C C   . THR A 103 ? 0.31132 0.36925 0.31109 0.03517  0.00071  0.01254  103 THR A C   
1604 O O   . THR A 103 ? 0.29987 0.35396 0.30090 0.03636  -0.00147 0.01187  103 THR A O   
1605 C CB  . THR A 103 ? 0.33702 0.37954 0.32459 0.02744  -0.00363 0.01059  103 THR A CB  
1606 O OG1 . THR A 103 ? 0.34646 0.38408 0.32747 0.02372  -0.00684 0.00909  103 THR A OG1 
1607 C CG2 . THR A 103 ? 0.31837 0.36233 0.30646 0.02648  0.00072  0.01268  103 THR A CG2 
1615 N N   . SER A 104 ? 0.29529 0.36210 0.29929 0.03717  0.00544  0.01475  104 SER A N   
1616 C CA  . SER A 104 ? 0.28346 0.35474 0.29372 0.04047  0.00856  0.01675  104 SER A CA  
1617 C C   . SER A 104 ? 0.29239 0.36114 0.30164 0.03934  0.01271  0.01877  104 SER A C   
1618 O O   . SER A 104 ? 0.31947 0.38254 0.32323 0.03593  0.01241  0.01831  104 SER A O   
1619 C CB  . SER A 104 ? 0.32961 0.41360 0.34628 0.04421  0.01079  0.01791  104 SER A CB  
1620 O OG  . SER A 104 ? 0.29932 0.38703 0.32209 0.04735  0.01261  0.01961  104 SER A OG  
1626 N N   . ILE A 105 ? 0.30570 0.37858 0.32017 0.04218  0.01643  0.02099  105 ILE A N   
1627 C CA  . ILE A 105 ? 0.28470 0.35541 0.29861 0.04182  0.02079  0.02297  105 ILE A CA  
1628 C C   . ILE A 105 ? 0.30329 0.38418 0.32277 0.04570  0.02567  0.02580  105 ILE A C   
1629 O O   . ILE A 105 ? 0.31205 0.39810 0.33730 0.04866  0.02598  0.02670  105 ILE A O   
1630 C CB  . ILE A 105 ? 0.30468 0.36719 0.31854 0.04090  0.02068  0.02289  105 ILE A CB  
1631 C CG1 . ILE A 105 ? 0.28807 0.34242 0.29808 0.03803  0.01558  0.02025  105 ILE A CG1 
1632 C CG2 . ILE A 105 ? 0.30324 0.36163 0.31469 0.03950  0.02443  0.02411  105 ILE A CG2 
1633 C CD1 . ILE A 105 ? 0.32238 0.37020 0.33253 0.03708  0.01576  0.02018  105 ILE A CD1 
1645 N N   . LYS A 106 ? 0.27875 0.36305 0.29644 0.04578  0.02941  0.02734  106 LYS A N   
1646 C CA  . LYS A 106 ? 0.35087 0.44412 0.37341 0.04965  0.03472  0.03046  106 LYS A CA  
1647 C C   . LYS A 106 ? 0.34767 0.43625 0.37300 0.05113  0.03721  0.03210  106 LYS A C   
1648 O O   . LYS A 106 ? 0.34680 0.42554 0.36851 0.04873  0.03682  0.03130  106 LYS A O   
1649 C CB  . LYS A 106 ? 0.35973 0.45672 0.37843 0.04935  0.03822  0.03172  106 LYS A CB  
1650 C CG  . LYS A 106 ? 0.38482 0.49189 0.40803 0.05371  0.04406  0.03517  106 LYS A CG  
1651 C CD  . LYS A 106 ? 0.49869 0.61067 0.51711 0.05344  0.04720  0.03624  106 LYS A CD  
1652 C CE  . LYS A 106 ? 0.59137 0.71254 0.61369 0.05818  0.05352  0.04001  106 LYS A CE  
1653 N NZ  . LYS A 106 ? 0.91933 1.03274 0.94022 0.05924  0.05659  0.04149  106 LYS A NZ  
1667 N N   . TRP A 107 ? 0.30548 0.40143 0.33732 0.05489  0.03988  0.03443  107 TRP A N   
1668 C CA  . TRP A 107 ? 0.32819 0.41942 0.36256 0.05595  0.04179  0.03591  107 TRP A CA  
1669 C C   . TRP A 107 ? 0.36398 0.44897 0.39489 0.05561  0.04598  0.03726  107 TRP A C   
1670 O O   . TRP A 107 ? 0.35968 0.44956 0.38971 0.05733  0.04973  0.03900  107 TRP A O   
1671 C CB  . TRP A 107 ? 0.33079 0.43193 0.37285 0.06008  0.04419  0.03865  107 TRP A CB  
1672 C CG  . TRP A 107 ? 0.35611 0.45136 0.39998 0.06042  0.04544  0.03992  107 TRP A CG  
1673 C CD1 . TRP A 107 ? 0.37145 0.46382 0.41670 0.05939  0.04197  0.03875  107 TRP A CD1 
1674 C CD2 . TRP A 107 ? 0.35979 0.45088 0.40343 0.06162  0.05047  0.04245  107 TRP A CD2 
1675 N NE1 . TRP A 107 ? 0.40565 0.49258 0.45146 0.05945  0.04455  0.04040  107 TRP A NE1 
1676 C CE2 . TRP A 107 ? 0.37950 0.46500 0.42444 0.06084  0.04979  0.04264  107 TRP A CE2 
1677 C CE3 . TRP A 107 ? 0.45832 0.54982 0.50031 0.06335  0.05548  0.04454  107 TRP A CE3 
1678 C CZ2 . TRP A 107 ? 0.45507 0.53471 0.49981 0.06147  0.05399  0.04476  107 TRP A CZ2 
1679 C CZ3 . TRP A 107 ? 0.50232 0.58797 0.54427 0.06451  0.05963  0.04668  107 TRP A CZ3 
1680 C CH2 . TRP A 107 ? 0.44891 0.52824 0.49220 0.06340  0.05887  0.04671  107 TRP A CH2 
1691 N N   . ALA A 108 ? 0.35785 0.43257 0.38681 0.05356  0.04549  0.03645  108 ALA A N   
1692 C CA  . ALA A 108 ? 0.37821 0.44584 0.40433 0.05319  0.04931  0.03742  108 ALA A CA  
1693 C C   . ALA A 108 ? 0.36741 0.42581 0.39325 0.05099  0.04818  0.03640  108 ALA A C   
1694 O O   . ALA A 108 ? 0.38816 0.44421 0.41351 0.04866  0.04377  0.03421  108 ALA A O   
1695 C CB  . ALA A 108 ? 0.45536 0.51938 0.47526 0.05056  0.04878  0.03586  108 ALA A CB  
1701 N N   . ASP A 109 ? 0.42854 0.48187 0.45437 0.05176  0.05231  0.03799  109 ASP A N   
1702 C CA  . ASP A 109 ? 0.38052 0.42407 0.40466 0.04877  0.05178  0.03670  109 ASP A CA  
1703 C C   . ASP A 109 ? 0.39107 0.43576 0.41765 0.04779  0.04802  0.03580  109 ASP A C   
1704 O O   . ASP A 109 ? 0.37124 0.41001 0.39512 0.04427  0.04504  0.03343  109 ASP A O   
1705 C CB  . ASP A 109 ? 0.38775 0.42362 0.40636 0.04464  0.04999  0.03389  109 ASP A CB  
1706 C CG  . ASP A 109 ? 0.44849 0.48315 0.46406 0.04535  0.05337  0.03453  109 ASP A CG  
1707 O OD1 . ASP A 109 ? 0.48561 0.51825 0.50185 0.04763  0.05804  0.03654  109 ASP A OD1 
1708 O OD2 . ASP A 109 ? 0.44653 0.48177 0.45860 0.04344  0.05121  0.03294  109 ASP A OD2 
1713 N N   . ASN A 110 ? 0.42764 0.48085 0.45942 0.05102  0.04819  0.03779  110 ASN A N   
1714 C CA  . ASN A 110 ? 0.40373 0.45945 0.43812 0.05066  0.04482  0.03730  110 ASN A CA  
1715 C C   . ASN A 110 ? 0.31416 0.36878 0.34582 0.04807  0.03915  0.03401  110 ASN A C   
1716 O O   . ASN A 110 ? 0.37483 0.42650 0.40539 0.04610  0.03638  0.03264  110 ASN A O   
1717 C CB  . ASN A 110 ? 0.44490 0.49372 0.47860 0.04902  0.04662  0.03793  110 ASN A CB  
1718 C CG  . ASN A 110 ? 0.67321 0.72182 0.70922 0.05165  0.05225  0.04130  110 ASN A CG  
1719 O OD1 . ASN A 110 ? 0.51782 0.57481 0.55809 0.05551  0.05421  0.04379  110 ASN A OD1 
1720 N ND2 . ASN A 110 ? 0.56242 0.60149 0.59554 0.04957  0.05505  0.04138  110 ASN A ND2 
1727 N N   . ASN A 111 ? 0.33858 0.39604 0.36890 0.04817  0.03738  0.03283  111 ASN A N   
1728 C CA  . ASN A 111 ? 0.31712 0.37170 0.34389 0.04552  0.03233  0.02976  111 ASN A CA  
1729 C C   . ASN A 111 ? 0.31002 0.37239 0.33955 0.04735  0.02819  0.02893  111 ASN A C   
1730 O O   . ASN A 111 ? 0.29171 0.35235 0.31820 0.04580  0.02415  0.02654  111 ASN A O   
1731 C CB  . ASN A 111 ? 0.36256 0.41387 0.38491 0.04358  0.03228  0.02857  111 ASN A CB  
1732 C CG  . ASN A 111 ? 0.32612 0.38593 0.35013 0.04610  0.03348  0.02971  111 ASN A CG  
1733 O OD1 . ASN A 111 ? 0.32631 0.39492 0.35534 0.04943  0.03439  0.03133  111 ASN A OD1 
1734 N ND2 . ASN A 111 ? 0.31537 0.37340 0.33512 0.04430  0.03338  0.02885  111 ASN A ND2 
1741 N N   . SER A 112 ? 0.31685 0.38762 0.35201 0.05055  0.02885  0.03075  112 SER A N   
1742 C CA  . SER A 112 ? 0.28923 0.36816 0.32720 0.05241  0.02479  0.02967  112 SER A CA  
1743 C C   . SER A 112 ? 0.29528 0.37011 0.33018 0.05066  0.01959  0.02701  112 SER A C   
1744 O O   . SER A 112 ? 0.28168 0.35886 0.31578 0.05107  0.01556  0.02500  112 SER A O   
1745 C CB  . SER A 112 ? 0.29216 0.38218 0.33741 0.05612  0.02628  0.03218  112 SER A CB  
1746 O OG  . SER A 112 ? 0.30172 0.39071 0.34824 0.05595  0.02587  0.03298  112 SER A OG  
1752 N N   . TYR A 113 ? 0.29748 0.36617 0.33019 0.04870  0.01965  0.02688  113 TYR A N   
1753 C CA  . TYR A 113 ? 0.26358 0.32896 0.29276 0.04715  0.01493  0.02444  113 TYR A CA  
1754 C C   . TYR A 113 ? 0.34387 0.40232 0.36767 0.04468  0.01247  0.02198  113 TYR A C   
1755 O O   . TYR A 113 ? 0.28289 0.34116 0.30452 0.04475  0.00790  0.01990  113 TYR A O   
1756 C CB  . TYR A 113 ? 0.28522 0.34590 0.31263 0.04506  0.01604  0.02487  113 TYR A CB  
1757 C CG  . TYR A 113 ? 0.27369 0.32401 0.29649 0.04121  0.01853  0.02431  113 TYR A CG  
1758 C CD1 . TYR A 113 ? 0.33244 0.37979 0.35612 0.04081  0.02359  0.02610  113 TYR A CD1 
1759 C CD2 . TYR A 113 ? 0.29185 0.33592 0.30961 0.03812  0.01595  0.02206  113 TYR A CD2 
1760 C CE1 . TYR A 113 ? 0.35725 0.39568 0.37703 0.03735  0.02584  0.02539  113 TYR A CE1 
1761 C CE2 . TYR A 113 ? 0.28985 0.32556 0.30409 0.03443  0.01834  0.02150  113 TYR A CE2 
1762 C CZ  . TYR A 113 ? 0.33009 0.36311 0.34548 0.03403  0.02318  0.02306  113 TYR A CZ  
1763 O OH  . TYR A 113 ? 0.34249 0.36780 0.35470 0.03049  0.02550  0.02231  113 TYR A OH  
1773 N N   . LEU A 114 ? 0.30901 0.36200 0.33047 0.04260  0.01530  0.02224  114 LEU A N   
1774 C CA  . LEU A 114 ? 0.27946 0.32638 0.29591 0.03993  0.01288  0.02015  114 LEU A CA  
1775 C C   . LEU A 114 ? 0.31849 0.37010 0.33530 0.04147  0.01049  0.01933  114 LEU A C   
1776 O O   . LEU A 114 ? 0.28240 0.33053 0.29549 0.04015  0.00652  0.01721  114 LEU A O   
1777 C CB  . LEU A 114 ? 0.30108 0.34211 0.31511 0.03729  0.01641  0.02069  114 LEU A CB  
1778 C CG  . LEU A 114 ? 0.35608 0.39088 0.36868 0.03483  0.01849  0.02080  114 LEU A CG  
1779 C CD1 . LEU A 114 ? 0.35506 0.38582 0.36642 0.03321  0.02261  0.02161  114 LEU A CD1 
1780 C CD2 . LEU A 114 ? 0.30355 0.33295 0.31207 0.03192  0.01475  0.01852  114 LEU A CD2 
1792 N N   . ALA A 115 ? 0.27842 0.33798 0.29955 0.04416  0.01305  0.02103  115 ALA A N   
1793 C CA  . ALA A 115 ? 0.29228 0.35744 0.31401 0.04546  0.01118  0.02021  115 ALA A CA  
1794 C C   . ALA A 115 ? 0.26427 0.33171 0.28646 0.04693  0.00615  0.01824  115 ALA A C   
1795 O O   . ALA A 115 ? 0.27640 0.34158 0.29523 0.04606  0.00269  0.01615  115 ALA A O   
1796 C CB  . ALA A 115 ? 0.32212 0.39729 0.34927 0.04842  0.01516  0.02260  115 ALA A CB  
1802 N N   . THR A 116 ? 0.29500 0.36714 0.32106 0.04925  0.00555  0.01889  116 THR A N   
1803 C CA  . THR A 116 ? 0.28282 0.35839 0.30929 0.05118  0.00063  0.01696  116 THR A CA  
1804 C C   . THR A 116 ? 0.29974 0.36595 0.31991 0.04900  -0.00324 0.01472  116 THR A C   
1805 O O   . THR A 116 ? 0.30294 0.36844 0.32081 0.04977  -0.00751 0.01255  116 THR A O   
1806 C CB  . THR A 116 ? 0.31418 0.39926 0.34668 0.05442  0.00063  0.01830  116 THR A CB  
1807 O OG1 . THR A 116 ? 0.33135 0.42043 0.36400 0.05657  -0.00450 0.01617  116 THR A OG1 
1808 C CG2 . THR A 116 ? 0.36259 0.44422 0.39451 0.05325  0.00218  0.01960  116 THR A CG2 
1816 N N   . ALA A 117 ? 0.27951 0.33839 0.29664 0.04623  -0.00165 0.01517  117 ALA A N   
1817 C CA  . ALA A 117 ? 0.29426 0.34465 0.30540 0.04385  -0.00483 0.01323  117 ALA A CA  
1818 C C   . ALA A 117 ? 0.29106 0.33596 0.29799 0.04196  -0.00674 0.01169  117 ALA A C   
1819 O O   . ALA A 117 ? 0.28650 0.32779 0.28966 0.04197  -0.01101 0.00972  117 ALA A O   
1820 C CB  . ALA A 117 ? 0.30593 0.35037 0.31512 0.04077  -0.00203 0.01405  117 ALA A CB  
1826 N N   . LEU A 118 ? 0.26638 0.31041 0.27337 0.04024  -0.00366 0.01264  118 LEU A N   
1827 C CA  . LEU A 118 ? 0.29855 0.33772 0.30107 0.03784  -0.00541 0.01137  118 LEU A CA  
1828 C C   . LEU A 118 ? 0.30268 0.34569 0.30537 0.03998  -0.00863 0.00993  118 LEU A C   
1829 O O   . LEU A 118 ? 0.29524 0.33266 0.29320 0.03864  -0.01231 0.00806  118 LEU A O   
1830 C CB  . LEU A 118 ? 0.25405 0.29354 0.25667 0.03593  -0.00128 0.01286  118 LEU A CB  
1831 C CG  . LEU A 118 ? 0.30224 0.33881 0.30044 0.03325  -0.00243 0.01202  118 LEU A CG  
1832 C CD1 . LEU A 118 ? 0.35160 0.37878 0.34418 0.02989  -0.00598 0.01040  118 LEU A CD1 
1833 C CD2 . LEU A 118 ? 0.32550 0.36414 0.32396 0.03193  0.00203  0.01378  118 LEU A CD2 
1845 N N   . LEU A 119 ? 0.29924 0.35190 0.30742 0.04325  -0.00720 0.01077  119 LEU A N   
1846 C CA  . LEU A 119 ? 0.26874 0.32600 0.27764 0.04530  -0.01007 0.00918  119 LEU A CA  
1847 C C   . LEU A 119 ? 0.27719 0.33162 0.28397 0.04695  -0.01512 0.00706  119 LEU A C   
1848 O O   . LEU A 119 ? 0.32474 0.37650 0.32828 0.04709  -0.01869 0.00494  119 LEU A O   
1849 C CB  . LEU A 119 ? 0.30641 0.37615 0.32266 0.04865  -0.00738 0.01066  119 LEU A CB  
1850 C CG  . LEU A 119 ? 0.29532 0.36913 0.31334 0.04766  -0.00235 0.01275  119 LEU A CG  
1851 C CD1 . LEU A 119 ? 0.30672 0.39272 0.33279 0.05121  0.00104  0.01501  119 LEU A CD1 
1852 C CD2 . LEU A 119 ? 0.31728 0.39131 0.33203 0.04600  -0.00317 0.01143  119 LEU A CD2 
1864 N N   . THR A 120 ? 0.27907 0.33423 0.28727 0.04829  -0.01542 0.00762  120 THR A N   
1865 C CA  . THR A 120 ? 0.30464 0.35823 0.31047 0.05027  -0.02008 0.00579  120 THR A CA  
1866 C C   . THR A 120 ? 0.29741 0.33974 0.29586 0.04768  -0.02299 0.00416  120 THR A C   
1867 O O   . THR A 120 ? 0.32302 0.36288 0.31830 0.04923  -0.02724 0.00210  120 THR A O   
1868 C CB  . THR A 120 ? 0.30700 0.36388 0.31500 0.05146  -0.01931 0.00700  120 THR A CB  
1869 O OG1 . THR A 120 ? 0.32570 0.39362 0.34074 0.05417  -0.01727 0.00854  120 THR A OG1 
1870 C CG2 . THR A 120 ? 0.34391 0.39938 0.34841 0.05342  -0.02403 0.00522  120 THR A CG2 
1878 N N   . LEU A 121 ? 0.29734 0.33285 0.29300 0.04379  -0.02079 0.00508  121 LEU A N   
1879 C CA  . LEU A 121 ? 0.33063 0.35614 0.31977 0.04110  -0.02346 0.00384  121 LEU A CA  
1880 C C   . LEU A 121 ? 0.36547 0.38723 0.35114 0.04046  -0.02620 0.00225  121 LEU A C   
1881 O O   . LEU A 121 ? 0.36275 0.37767 0.34332 0.04021  -0.03002 0.00072  121 LEU A O   
1882 C CB  . LEU A 121 ? 0.30634 0.32680 0.29404 0.03679  -0.02037 0.00512  121 LEU A CB  
1883 C CG  . LEU A 121 ? 0.34078 0.36197 0.32997 0.03631  -0.01805 0.00625  121 LEU A CG  
1884 C CD1 . LEU A 121 ? 0.33779 0.35532 0.32661 0.03226  -0.01442 0.00741  121 LEU A CD1 
1885 C CD2 . LEU A 121 ? 0.34274 0.36014 0.32795 0.03669  -0.02137 0.00510  121 LEU A CD2 
1897 N N   . GLN A 122 ? 0.35004 0.37600 0.33796 0.03996  -0.02413 0.00269  122 GLN A N   
1898 C CA  . GLN A 122 ? 0.34455 0.36764 0.32895 0.03889  -0.02639 0.00116  122 GLN A CA  
1899 C C   . GLN A 122 ? 0.39907 0.42479 0.38383 0.04274  -0.03006 -0.00092 122 GLN A C   
1900 O O   . GLN A 122 ? 0.41804 0.44089 0.39954 0.04191  -0.03212 -0.00250 122 GLN A O   
1901 C CB  . GLN A 122 ? 0.33762 0.36615 0.32431 0.03727  -0.02260 0.00237  122 GLN A CB  
1902 C CG  . GLN A 122 ? 0.34761 0.37269 0.33277 0.03336  -0.01950 0.00409  122 GLN A CG  
1903 C CD  . GLN A 122 ? 0.31898 0.35135 0.30705 0.03281  -0.01511 0.00570  122 GLN A CD  
1904 O OE1 . GLN A 122 ? 0.35448 0.38706 0.33957 0.03067  -0.01516 0.00529  122 GLN A OE1 
1905 N NE2 . GLN A 122 ? 0.30583 0.34441 0.29935 0.03478  -0.01123 0.00762  122 GLN A NE2 
1914 N N   . GLN A 123 ? 0.34480 0.37588 0.33301 0.04676  -0.03110 -0.00107 123 GLN A N   
1915 C CA  . GLN A 123 ? 0.37883 0.41325 0.36754 0.05081  -0.03486 -0.00320 123 GLN A CA  
1916 C C   . GLN A 123 ? 0.41968 0.44977 0.40478 0.05323  -0.03882 -0.00437 123 GLN A C   
1917 O O   . GLN A 123 ? 0.41996 0.45274 0.40501 0.05707  -0.04229 -0.00628 123 GLN A O   
1918 C CB  . GLN A 123 ? 0.37645 0.42442 0.37323 0.05426  -0.03299 -0.00249 123 GLN A CB  
1919 C CG  . GLN A 123 ? 0.37732 0.43120 0.37784 0.05257  -0.02896 -0.00130 123 GLN A CG  
1920 C CD  . GLN A 123 ? 0.40241 0.47009 0.41145 0.05581  -0.02659 -0.00002 123 GLN A CD  
1921 O OE1 . GLN A 123 ? 0.37757 0.45271 0.38996 0.05930  -0.02891 -0.00148 123 GLN A OE1 
1922 N NE2 . GLN A 123 ? 0.37016 0.44161 0.38293 0.05480  -0.02200 0.00274  123 GLN A NE2 
1931 N N   . ILE A 124 ? 0.39417 0.41832 0.37619 0.05123  -0.03835 -0.00336 124 ILE A N   
1932 C CA  . ILE A 124 ? 0.42868 0.44912 0.40662 0.05334  -0.04174 -0.00425 124 ILE A CA  
1933 C C   . ILE A 124 ? 0.49347 0.50205 0.46465 0.04980  -0.04287 -0.00439 124 ILE A C   
1934 O O   . ILE A 124 ? 0.42673 0.43133 0.39735 0.04537  -0.04036 -0.00326 124 ILE A O   
1935 C CB  . ILE A 124 ? 0.38400 0.41100 0.36507 0.05467  -0.04004 -0.00277 124 ILE A CB  
1936 C CG1 . ILE A 124 ? 0.39705 0.42185 0.37910 0.05027  -0.03559 -0.00061 124 ILE A CG1 
1937 C CG2 . ILE A 124 ? 0.41944 0.45866 0.40732 0.05818  -0.03938 -0.00250 124 ILE A CG2 
1938 C CD1 . ILE A 124 ? 0.42746 0.45754 0.41169 0.05085  -0.03372 0.00079  124 ILE A CD1 
1950 N N   . GLU A 125 ? 0.41965 0.42307 0.38565 0.05197  -0.04681 -0.00574 125 GLU A N   
1951 C CA  . GLU A 125 ? 0.41652 0.40912 0.37614 0.04909  -0.04826 -0.00575 125 GLU A CA  
1952 C C   . GLU A 125 ? 0.44070 0.43375 0.40045 0.04710  -0.04593 -0.00404 125 GLU A C   
1953 O O   . GLU A 125 ? 0.45910 0.45580 0.41833 0.04999  -0.04680 -0.00405 125 GLU A O   
1954 C CB  . GLU A 125 ? 0.53054 0.51754 0.48441 0.05266  -0.05320 -0.00773 125 GLU A CB  
1955 C CG  . GLU A 125 ? 0.62077 0.59593 0.56790 0.04966  -0.05497 -0.00768 125 GLU A CG  
1956 C CD  . GLU A 125 ? 0.87293 0.84251 0.81398 0.05380  -0.05953 -0.00922 125 GLU A CD  
1957 O OE1 . GLU A 125 ? 0.81308 0.78406 0.75372 0.05796  -0.06220 -0.01117 125 GLU A OE1 
1958 O OE2 . GLU A 125 ? 1.09462 1.05882 1.03137 0.05302  -0.06033 -0.00846 125 GLU A OE2 
1965 N N   . LEU A 126 ? 0.41885 0.40861 0.37899 0.04208  -0.04304 -0.00269 126 LEU A N   
1966 C CA  . LEU A 126 ? 0.39470 0.38533 0.35561 0.03958  -0.04025 -0.00119 126 LEU A CA  
1967 C C   . LEU A 126 ? 0.47225 0.45594 0.43096 0.03420  -0.03924 -0.00046 126 LEU A C   
1968 O O   . LEU A 126 ? 0.48174 0.46450 0.44167 0.03160  -0.03793 -0.00018 126 LEU A O   
1969 C CB  . LEU A 126 ? 0.43653 0.43565 0.40366 0.03959  -0.03606 0.00010  126 LEU A CB  
1970 C CG  . LEU A 126 ? 0.45538 0.45620 0.42305 0.03773  -0.03338 0.00128  126 LEU A CG  
1971 C CD1 . LEU A 126 ? 0.48900 0.49355 0.45472 0.04142  -0.03551 0.00076  126 LEU A CD1 
1972 C CD2 . LEU A 126 ? 0.40665 0.41289 0.37977 0.03633  -0.02875 0.00273  126 LEU A CD2 
1984 N N   . LYS A 127 ? 0.41986 0.39988 0.37553 0.03249  -0.03968 -0.00006 127 LYS A N   
1985 C CA  . LYS A 127 ? 0.43129 0.40587 0.38529 0.02729  -0.03893 0.00071  127 LYS A CA  
1986 C C   . LYS A 127 ? 0.41959 0.39782 0.37625 0.02474  -0.03520 0.00188  127 LYS A C   
1987 O O   . LYS A 127 ? 0.43349 0.41476 0.38971 0.02658  -0.03495 0.00194  127 LYS A O   
1988 C CB  . LYS A 127 ? 0.47743 0.44422 0.42543 0.02719  -0.04293 0.00016  127 LYS A CB  
1989 C CG  . LYS A 127 ? 0.71672 0.67893 0.66308 0.02193  -0.04256 0.00114  127 LYS A CG  
1990 C CD  . LYS A 127 ? 1.18201 1.13860 1.12636 0.01849  -0.04407 0.00106  127 LYS A CD  
1991 C CE  . LYS A 127 ? 1.02350 0.98043 0.96958 0.01266  -0.04176 0.00226  127 LYS A CE  
1992 N NZ  . LYS A 127 ? 0.70379 0.66067 0.65039 0.01001  -0.04116 0.00232  127 LYS A NZ  
2006 N N   . PHE A 128 ? 0.37385 0.35214 0.33294 0.02050  -0.03228 0.00273  128 PHE A N   
2007 C CA  . PHE A 128 ? 0.35593 0.33742 0.31777 0.01780  -0.02843 0.00362  128 PHE A CA  
2008 C C   . PHE A 128 ? 0.37025 0.34820 0.32950 0.01434  -0.02922 0.00384  128 PHE A C   
2009 O O   . PHE A 128 ? 0.40730 0.37982 0.36330 0.01279  -0.03219 0.00368  128 PHE A O   
2010 C CB  . PHE A 128 ? 0.33256 0.31607 0.29820 0.01520  -0.02482 0.00436  128 PHE A CB  
2011 C CG  . PHE A 128 ? 0.34057 0.32929 0.30984 0.01845  -0.02286 0.00460  128 PHE A CG  
2012 C CD1 . PHE A 128 ? 0.34275 0.33644 0.31452 0.02057  -0.02074 0.00495  128 PHE A CD1 
2013 C CD2 . PHE A 128 ? 0.33569 0.32491 0.30575 0.01924  -0.02317 0.00458  128 PHE A CD2 
2014 C CE1 . PHE A 128 ? 0.35623 0.35529 0.33173 0.02362  -0.01910 0.00540  128 PHE A CE1 
2015 C CE2 . PHE A 128 ? 0.36637 0.36146 0.34035 0.02236  -0.02120 0.00499  128 PHE A CE2 
2016 C CZ  . PHE A 128 ? 0.35278 0.35266 0.32964 0.02459  -0.01927 0.00546  128 PHE A CZ  
2026 N N   . ASN A 129 ? 0.34687 0.32831 0.30770 0.01284  -0.02635 0.00427  129 ASN A N   
2027 C CA  . ASN A 129 ? 0.36075 0.34072 0.31987 0.00962  -0.02658 0.00453  129 ASN A CA  
2028 C C   . ASN A 129 ? 0.36862 0.34852 0.33041 0.00428  -0.02406 0.00501  129 ASN A C   
2029 O O   . ASN A 129 ? 0.39553 0.37211 0.35572 0.00126  -0.02601 0.00522  129 ASN A O   
2030 C CB  . ASN A 129 ? 0.43698 0.42162 0.39571 0.01085  -0.02499 0.00457  129 ASN A CB  
2031 C CG  . ASN A 129 ? 0.66006 0.64429 0.61452 0.01563  -0.02855 0.00412  129 ASN A CG  
2032 O OD1 . ASN A 129 ? 0.57387 0.55282 0.52489 0.01698  -0.03238 0.00384  129 ASN A OD1 
2033 N ND2 . ASN A 129 ? 0.60011 0.58992 0.55433 0.01814  -0.02734 0.00405  129 ASN A ND2 
2040 N N   . PRO A 130 ? 0.36135 0.34484 0.32705 0.00299  -0.01994 0.00522  130 PRO A N   
2041 C CA  . PRO A 130 ? 0.34431 0.32800 0.31238 -0.00183 -0.01767 0.00549  130 PRO A CA  
2042 C C   . PRO A 130 ? 0.34302 0.32345 0.31007 -0.00305 -0.01989 0.00563  130 PRO A C   
2043 O O   . PRO A 130 ? 0.32330 0.30335 0.29026 -0.00040 -0.02036 0.00562  130 PRO A O   
2044 C CB  . PRO A 130 ? 0.34821 0.33560 0.32005 -0.00159 -0.01295 0.00564  130 PRO A CB  
2045 C CG  . PRO A 130 ? 0.38336 0.37326 0.35475 0.00219  -0.01258 0.00555  130 PRO A CG  
2046 C CD  . PRO A 130 ? 0.35451 0.34201 0.32264 0.00583  -0.01718 0.00528  130 PRO A CD  
2054 N N   . PRO A 131 ? 0.33318 0.31203 0.29948 -0.00724 -0.02124 0.00582  131 PRO A N   
2055 C CA  . PRO A 131 ? 0.34751 0.32414 0.31247 -0.00912 -0.02316 0.00603  131 PRO A CA  
2056 C C   . PRO A 131 ? 0.32646 0.30580 0.29381 -0.00849 -0.02012 0.00620  131 PRO A C   
2057 O O   . PRO A 131 ? 0.33928 0.31754 0.30491 -0.00783 -0.02155 0.00632  131 PRO A O   
2058 C CB  . PRO A 131 ? 0.35659 0.33344 0.32172 -0.01432 -0.02400 0.00632  131 PRO A CB  
2059 C CG  . PRO A 131 ? 0.37566 0.35261 0.34038 -0.01414 -0.02452 0.00629  131 PRO A CG  
2060 C CD  . PRO A 131 ? 0.36818 0.34784 0.33454 -0.01048 -0.02142 0.00592  131 PRO A CD  
2068 N N   . ALA A 132 ? 0.30996 0.29290 0.28101 -0.00868 -0.01577 0.00626  132 ALA A N   
2069 C CA  . ALA A 132 ? 0.29582 0.28121 0.26904 -0.00765 -0.01259 0.00663  132 ALA A CA  
2070 C C   . ALA A 132 ? 0.31755 0.30321 0.29038 -0.00307 -0.01301 0.00683  132 ALA A C   
2071 O O   . ALA A 132 ? 0.31101 0.29788 0.28369 -0.00238 -0.01254 0.00724  132 ALA A O   
2072 C CB  . ALA A 132 ? 0.31291 0.30104 0.28978 -0.00803 -0.00783 0.00662  132 ALA A CB  
2078 N N   . LEU A 133 ? 0.30793 0.29343 0.28064 0.00011  -0.01381 0.00654  133 LEU A N   
2079 C CA  . LEU A 133 ? 0.32085 0.30768 0.29381 0.00455  -0.01438 0.00660  133 LEU A CA  
2080 C C   . LEU A 133 ? 0.31607 0.29980 0.28537 0.00504  -0.01869 0.00613  133 LEU A C   
2081 O O   . LEU A 133 ? 0.33874 0.32407 0.30824 0.00701  -0.01874 0.00622  133 LEU A O   
2082 C CB  . LEU A 133 ? 0.32234 0.31086 0.29614 0.00775  -0.01418 0.00636  133 LEU A CB  
2083 C CG  . LEU A 133 ? 0.29962 0.29165 0.27693 0.00798  -0.00967 0.00691  133 LEU A CG  
2084 C CD1 . LEU A 133 ? 0.32692 0.32102 0.30400 0.01046  -0.01005 0.00667  133 LEU A CD1 
2085 C CD2 . LEU A 133 ? 0.31354 0.30856 0.29386 0.01001  -0.00688 0.00777  133 LEU A CD2 
2097 N N   . GLN A 134 ? 0.31540 0.29476 0.28124 0.00316  -0.02218 0.00566  134 GLN A N   
2098 C CA  . GLN A 134 ? 0.36469 0.33987 0.32638 0.00299  -0.02630 0.00520  134 GLN A CA  
2099 C C   . GLN A 134 ? 0.38033 0.35638 0.34141 0.00041  -0.02574 0.00561  134 GLN A C   
2100 O O   . GLN A 134 ? 0.35389 0.32998 0.31342 0.00182  -0.02687 0.00534  134 GLN A O   
2101 C CB  . GLN A 134 ? 0.36750 0.33758 0.32560 0.00058  -0.02973 0.00501  134 GLN A CB  
2102 C CG  . GLN A 134 ? 0.38575 0.35493 0.34303 0.00351  -0.03091 0.00462  134 GLN A CG  
2103 C CD  . GLN A 134 ? 0.51467 0.47968 0.46884 0.00091  -0.03361 0.00481  134 GLN A CD  
2104 O OE1 . GLN A 134 ? 0.60731 0.56960 0.55985 -0.00307 -0.03518 0.00519  134 GLN A OE1 
2105 N NE2 . GLN A 134 ? 0.56063 0.52582 0.51390 0.00315  -0.03416 0.00468  134 GLN A NE2 
2114 N N   . ASP A 135 ? 0.34799 0.32520 0.30994 -0.00356 -0.02413 0.00618  135 ASP A N   
2115 C CA  . ASP A 135 ? 0.37924 0.35797 0.33986 -0.00633 -0.02386 0.00663  135 ASP A CA  
2116 C C   . ASP A 135 ? 0.32313 0.30697 0.28628 -0.00344 -0.02032 0.00709  135 ASP A C   
2117 O O   . ASP A 135 ? 0.36516 0.35042 0.32619 -0.00355 -0.02086 0.00722  135 ASP A O   
2118 C CB  . ASP A 135 ? 0.35552 0.33562 0.31714 -0.01071 -0.02270 0.00705  135 ASP A CB  
2119 C CG  . ASP A 135 ? 0.46655 0.44279 0.42582 -0.01428 -0.02629 0.00690  135 ASP A CG  
2120 O OD1 . ASP A 135 ? 0.42605 0.39750 0.38176 -0.01377 -0.03005 0.00659  135 ASP A OD1 
2121 O OD2 . ASP A 135 ? 0.39944 0.37767 0.36061 -0.01758 -0.02523 0.00710  135 ASP A OD2 
2126 N N   . ALA A 136 ? 0.30842 0.29542 0.27595 -0.00112 -0.01649 0.00745  136 ALA A N   
2127 C CA  . ALA A 136 ? 0.30846 0.30054 0.27878 0.00165  -0.01277 0.00822  136 ALA A CA  
2128 C C   . ALA A 136 ? 0.30158 0.29519 0.27214 0.00565  -0.01378 0.00799  136 ALA A C   
2129 O O   . ALA A 136 ? 0.30893 0.30683 0.28017 0.00712  -0.01210 0.00857  136 ALA A O   
2130 C CB  . ALA A 136 ? 0.28883 0.28304 0.26350 0.00289  -0.00851 0.00874  136 ALA A CB  
2136 N N   . TYR A 137 ? 0.30277 0.29367 0.27282 0.00758  -0.01645 0.00713  137 TYR A N   
2137 C CA  . TYR A 137 ? 0.29500 0.28785 0.26551 0.01151  -0.01774 0.00664  137 TYR A CA  
2138 C C   . TYR A 137 ? 0.33615 0.32729 0.30255 0.01016  -0.02059 0.00602  137 TYR A C   
2139 O O   . TYR A 137 ? 0.35470 0.35000 0.32204 0.01235  -0.01995 0.00598  137 TYR A O   
2140 C CB  . TYR A 137 ? 0.29955 0.29014 0.26989 0.01401  -0.02019 0.00576  137 TYR A CB  
2141 C CG  . TYR A 137 ? 0.32561 0.31919 0.29699 0.01837  -0.02158 0.00510  137 TYR A CG  
2142 C CD1 . TYR A 137 ? 0.34554 0.34619 0.32143 0.02113  -0.01849 0.00589  137 TYR A CD1 
2143 C CD2 . TYR A 137 ? 0.40053 0.39014 0.36845 0.01977  -0.02595 0.00370  137 TYR A CD2 
2144 C CE1 . TYR A 137 ? 0.32355 0.32824 0.30110 0.02500  -0.01977 0.00525  137 TYR A CE1 
2145 C CE2 . TYR A 137 ? 0.40193 0.39495 0.37111 0.02388  -0.02729 0.00285  137 TYR A CE2 
2146 C CZ  . TYR A 137 ? 0.41886 0.41986 0.39310 0.02632  -0.02421 0.00361  137 TYR A CZ  
2147 O OH  . TYR A 137 ? 0.43118 0.43690 0.40741 0.03028  -0.02553 0.00274  137 TYR A OH  
2157 N N   . TYR A 138 ? 0.35861 0.34400 0.32039 0.00630  -0.02366 0.00559  138 TYR A N   
2158 C CA  . TYR A 138 ? 0.40283 0.38611 0.35987 0.00403  -0.02628 0.00511  138 TYR A CA  
2159 C C   . TYR A 138 ? 0.38090 0.37035 0.33850 0.00299  -0.02321 0.00602  138 TYR A C   
2160 O O   . TYR A 138 ? 0.39207 0.38406 0.34818 0.00368  -0.02349 0.00568  138 TYR A O   
2161 C CB  . TYR A 138 ? 0.43960 0.41622 0.39198 -0.00056 -0.02968 0.00494  138 TYR A CB  
2162 C CG  . TYR A 138 ? 0.43594 0.40937 0.38250 -0.00370 -0.03279 0.00450  138 TYR A CG  
2163 C CD1 . TYR A 138 ? 0.59830 0.56617 0.54114 -0.00259 -0.03649 0.00326  138 TYR A CD1 
2164 C CD2 . TYR A 138 ? 0.52476 0.50066 0.46906 -0.00792 -0.03211 0.00529  138 TYR A CD2 
2165 C CE1 . TYR A 138 ? 0.72000 0.68428 0.65693 -0.00591 -0.03927 0.00280  138 TYR A CE1 
2166 C CE2 . TYR A 138 ? 0.67915 0.65242 0.61745 -0.01133 -0.03500 0.00494  138 TYR A CE2 
2167 C CZ  . TYR A 138 ? 0.75358 0.72073 0.68819 -0.01050 -0.03851 0.00369  138 TYR A CZ  
2168 O OH  . TYR A 138 ? 1.00242 0.96638 0.93053 -0.01434 -0.04130 0.00330  138 TYR A OH  
2178 N N   . ARG A 139 ? 0.33934 0.33176 0.29896 0.00144  -0.02007 0.00715  139 ARG A N   
2179 C CA  . ARG A 139 ? 0.34850 0.34743 0.30852 0.00109  -0.01677 0.00820  139 ARG A CA  
2180 C C   . ARG A 139 ? 0.35089 0.35622 0.31526 0.00591  -0.01356 0.00869  139 ARG A C   
2181 O O   . ARG A 139 ? 0.38343 0.39420 0.34702 0.00633  -0.01210 0.00915  139 ARG A O   
2182 C CB  . ARG A 139 ? 0.35922 0.35979 0.32083 -0.00077 -0.01397 0.00918  139 ARG A CB  
2183 C CG  . ARG A 139 ? 0.43149 0.42759 0.38954 -0.00581 -0.01697 0.00884  139 ARG A CG  
2184 C CD  . ARG A 139 ? 0.51777 0.51728 0.47705 -0.00780 -0.01412 0.00966  139 ARG A CD  
2185 N NE  . ARG A 139 ? 0.84261 0.84844 0.80051 -0.00746 -0.01170 0.01058  139 ARG A NE  
2186 C CZ  . ARG A 139 ? 0.83730 0.84765 0.79663 -0.00726 -0.00812 0.01147  139 ARG A CZ  
2187 N NH1 . ARG A 139 ? 0.75867 0.76763 0.72102 -0.00776 -0.00649 0.01140  139 ARG A NH1 
2188 N NH2 . ARG A 139 ? 0.84359 0.86023 0.80102 -0.00653 -0.00601 0.01241  139 ARG A NH2 
2202 N N   . ALA A 140 ? 0.31346 0.31904 0.28245 0.00941  -0.01233 0.00872  140 ALA A N   
2203 C CA  . ALA A 140 ? 0.30372 0.31600 0.27748 0.01396  -0.00943 0.00938  140 ALA A CA  
2204 C C   . ALA A 140 ? 0.31386 0.32807 0.28652 0.01555  -0.01174 0.00836  140 ALA A C   
2205 O O   . ALA A 140 ? 0.33036 0.35197 0.30535 0.01768  -0.00929 0.00903  140 ALA A O   
2206 C CB  . ALA A 140 ? 0.32274 0.33461 0.30088 0.01685  -0.00846 0.00951  140 ALA A CB  
2212 N N   . ARG A 141 ? 0.32644 0.33425 0.29558 0.01465  -0.01634 0.00672  141 ARG A N   
2213 C CA  . ARG A 141 ? 0.39429 0.40280 0.36165 0.01581  -0.01884 0.00538  141 ARG A CA  
2214 C C   . ARG A 141 ? 0.49369 0.50481 0.45725 0.01280  -0.01830 0.00553  141 ARG A C   
2215 O O   . ARG A 141 ? 0.44855 0.46458 0.41249 0.01421  -0.01803 0.00497  141 ARG A O   
2216 C CB  . ARG A 141 ? 0.44493 0.44460 0.40816 0.01517  -0.02392 0.00364  141 ARG A CB  
2217 C CG  . ARG A 141 ? 0.44081 0.43971 0.40723 0.01909  -0.02492 0.00315  141 ARG A CG  
2218 C CD  . ARG A 141 ? 0.53503 0.52488 0.49668 0.01828  -0.02956 0.00180  141 ARG A CD  
2219 N NE  . ARG A 141 ? 0.61844 0.60572 0.57665 0.01907  -0.03288 0.00010  141 ARG A NE  
2220 C CZ  . ARG A 141 ? 1.05283 1.03196 1.00464 0.01599  -0.03638 -0.00081 141 ARG A CZ  
2221 N NH1 . ARG A 141 ? 0.78740 0.76061 0.73581 0.01193  -0.03738 -0.00010 141 ARG A NH1 
2222 N NH2 . ARG A 141 ? 0.77436 0.75137 0.72318 0.01687  -0.03898 -0.00250 141 ARG A NH2 
2236 N N   . ALA A 142 ? 0.43112 0.43966 0.39081 0.00847  -0.01825 0.00621  142 ALA A N   
2237 C CA  . ALA A 142 ? 0.49062 0.50268 0.44608 0.00524  -0.01754 0.00660  142 ALA A CA  
2238 C C   . ALA A 142 ? 0.47818 0.50045 0.43729 0.00718  -0.01224 0.00835  142 ALA A C   
2239 O O   . ALA A 142 ? 0.56959 0.59696 0.52542 0.00519  -0.01102 0.00881  142 ALA A O   
2240 C CB  . ALA A 142 ? 0.47533 0.48181 0.42531 -0.00012 -0.01975 0.00679  142 ALA A CB  
2246 N N   . GLY A 143 ? 0.44195 0.46737 0.40730 0.01093  -0.00902 0.00942  143 GLY A N   
2247 C CA  . GLY A 143 ? 0.42909 0.46384 0.39838 0.01356  -0.00381 0.01128  143 GLY A CA  
2248 C C   . GLY A 143 ? 0.42429 0.45915 0.39468 0.01311  -0.00067 0.01282  143 GLY A C   
2249 O O   . GLY A 143 ? 0.47338 0.51531 0.44698 0.01574  0.00389  0.01454  143 GLY A O   
2253 N N   A GLU A 144 ? 0.36773 0.39527 0.33559 0.00992  -0.00286 0.01227  144 GLU A N   
2254 N N   B GLU A 144 ? 0.36707 0.39462 0.33497 0.00995  -0.00283 0.01228  144 GLU A N   
2255 C CA  A GLU A 144 ? 0.40871 0.43593 0.37745 0.00912  -0.00018 0.01334  144 GLU A CA  
2256 C CA  B GLU A 144 ? 0.40805 0.43544 0.37687 0.00920  -0.00007 0.01338  144 GLU A CA  
2257 C C   A GLU A 144 ? 0.36767 0.39003 0.34060 0.01068  -0.00002 0.01305  144 GLU A C   
2258 C C   B GLU A 144 ? 0.36643 0.38889 0.33937 0.01067  0.00008  0.01308  144 GLU A C   
2259 O O   A GLU A 144 ? 0.36877 0.38474 0.34011 0.00795  -0.00267 0.01209  144 GLU A O   
2260 O O   B GLU A 144 ? 0.36776 0.38391 0.33910 0.00788  -0.00247 0.01216  144 GLU A O   
2261 C CB  A GLU A 144 ? 0.44911 0.47320 0.41199 0.00385  -0.00273 0.01290  144 GLU A CB  
2262 C CB  B GLU A 144 ? 0.45284 0.47743 0.41580 0.00400  -0.00246 0.01299  144 GLU A CB  
2263 C CG  A GLU A 144 ? 0.51940 0.54958 0.47741 0.00191  -0.00230 0.01348  144 GLU A CG  
2264 C CG  B GLU A 144 ? 0.51763 0.54882 0.47616 0.00249  -0.00165 0.01367  144 GLU A CG  
2265 C CD  A GLU A 144 ? 0.71552 0.74604 0.67035 0.00109  -0.00509 0.01248  144 GLU A CD  
2266 C CD  B GLU A 144 ? 0.62110 0.65013 0.57328 -0.00304 -0.00476 0.01326  144 GLU A CD  
2267 O OE1 A GLU A 144 ? 0.48577 0.50902 0.43778 -0.00143 -0.00966 0.01102  144 GLU A OE1 
2268 O OE1 B GLU A 144 ? 0.72680 0.74943 0.67859 -0.00566 -0.00741 0.01254  144 GLU A OE1 
2269 O OE2 A GLU A 144 ? 0.79896 0.83721 0.75400 0.00297  -0.00255 0.01316  144 GLU A OE2 
2270 O OE2 B GLU A 144 ? 0.88469 0.91920 0.83220 -0.00490 -0.00457 0.01373  144 GLU A OE2 
2283 N N   . ALA A 145 ? 0.32861 0.35470 0.30687 0.01497  0.00321  0.01399  145 ALA A N   
2284 C CA  . ALA A 145 ? 0.31763 0.34021 0.29954 0.01665  0.00313  0.01367  145 ALA A CA  
2285 C C   . ALA A 145 ? 0.31833 0.33972 0.30259 0.01667  0.00679  0.01461  145 ALA A C   
2286 O O   . ALA A 145 ? 0.29477 0.31393 0.28189 0.01789  0.00729  0.01449  145 ALA A O   
2287 C CB  . ALA A 145 ? 0.34097 0.36839 0.32726 0.02108  0.00380  0.01401  145 ALA A CB  
2294 N N   . ALA A 146 ? 0.33753 0.36028 0.32021 0.01521  0.00925  0.01542  146 ALA A N   
2295 C CA  . ALA A 146 ? 0.33290 0.35445 0.31786 0.01565  0.01312  0.01622  146 ALA A CA  
2296 C C   . ALA A 146 ? 0.32611 0.34112 0.31108 0.01294  0.01148  0.01491  146 ALA A C   
2297 O O   . ALA A 146 ? 0.28816 0.30155 0.27614 0.01411  0.01391  0.01518  146 ALA A O   
2298 C CB  . ALA A 146 ? 0.34196 0.36613 0.32445 0.01451  0.01546  0.01703  146 ALA A CB  
2304 N N   . ASN A 147 ? 0.34123 0.35275 0.32270 0.00904  0.00759  0.01357  147 ASN A N   
2305 C CA  . ASN A 147 ? 0.30566 0.31215 0.28738 0.00639  0.00641  0.01246  147 ASN A CA  
2306 C C   . ASN A 147 ? 0.31092 0.31562 0.29454 0.00831  0.00515  0.01198  147 ASN A C   
2307 O O   . ASN A 147 ? 0.29453 0.29728 0.28002 0.00800  0.00668  0.01175  147 ASN A O   
2308 C CB  . ASN A 147 ? 0.35074 0.35467 0.32859 0.00192  0.00242  0.01142  147 ASN A CB  
2309 C CG  . ASN A 147 ? 0.38032 0.38608 0.35679 -0.00066 0.00392  0.01169  147 ASN A CG  
2310 O OD1 . ASN A 147 ? 0.52085 0.52528 0.49869 -0.00254 0.00548  0.01126  147 ASN A OD1 
2311 N ND2 . ASN A 147 ? 0.43677 0.44635 0.41067 -0.00047 0.00384  0.01238  147 ASN A ND2 
2318 N N   . PHE A 148 ? 0.29612 0.30192 0.27904 0.01028  0.00240  0.01176  148 PHE A N   
2319 C CA  . PHE A 148 ? 0.27962 0.28471 0.26406 0.01258  0.00090  0.01127  148 PHE A CA  
2320 C C   . PHE A 148 ? 0.29285 0.30096 0.28161 0.01563  0.00485  0.01238  148 PHE A C   
2321 O O   . PHE A 148 ? 0.29376 0.30038 0.28359 0.01570  0.00511  0.01207  148 PHE A O   
2322 C CB  . PHE A 148 ? 0.26871 0.27514 0.25185 0.01456  -0.00251 0.01074  148 PHE A CB  
2323 C CG  . PHE A 148 ? 0.31972 0.32552 0.30363 0.01694  -0.00489 0.00996  148 PHE A CG  
2324 C CD1 . PHE A 148 ? 0.30907 0.31008 0.29047 0.01519  -0.00780 0.00886  148 PHE A CD1 
2325 C CD2 . PHE A 148 ? 0.33396 0.34485 0.32113 0.02109  -0.00423 0.01042  148 PHE A CD2 
2326 C CE1 . PHE A 148 ? 0.32841 0.32953 0.30990 0.01775  -0.01004 0.00818  148 PHE A CE1 
2327 C CE2 . PHE A 148 ? 0.33636 0.34760 0.32398 0.02348  -0.00676 0.00963  148 PHE A CE2 
2328 C CZ  . PHE A 148 ? 0.33115 0.33741 0.31563 0.02190  -0.00962 0.00850  148 PHE A CZ  
2338 N N   . CYS A 149 ? 0.32579 0.33847 0.31681 0.01805  0.00808  0.01382  149 CYS A N   
2339 C CA  . CYS A 149 ? 0.30603 0.32143 0.30116 0.02093  0.01188  0.01518  149 CYS A CA  
2340 C C   . CYS A 149 ? 0.33093 0.34246 0.32636 0.01879  0.01489  0.01525  149 CYS A C   
2341 O O   . CYS A 149 ? 0.27092 0.28198 0.26828 0.01957  0.01629  0.01551  149 CYS A O   
2342 C CB  . CYS A 149 ? 0.30765 0.32891 0.30503 0.02390  0.01502  0.01695  149 CYS A CB  
2343 S SG  . CYS A 149 ? 0.33241 0.35980 0.33082 0.02686  0.01214  0.01682  149 CYS A SG  
2349 N N   . ALA A 150 ? 0.29834 0.30746 0.29173 0.01593  0.01588  0.01493  150 ALA A N   
2350 C CA  . ALA A 150 ? 0.27749 0.28302 0.27122 0.01366  0.01870  0.01465  150 ALA A CA  
2351 C C   . ALA A 150 ? 0.29666 0.29888 0.28953 0.01107  0.01646  0.01318  150 ALA A C   
2352 O O   . ALA A 150 ? 0.30462 0.30507 0.29862 0.01022  0.01897  0.01309  150 ALA A O   
2353 C CB  . ALA A 150 ? 0.31934 0.32398 0.31111 0.01117  0.01969  0.01439  150 ALA A CB  
2359 N N   . LEU A 151 ? 0.30170 0.30312 0.29227 0.00979  0.01189  0.01208  151 LEU A N   
2360 C CA  . LEU A 151 ? 0.29472 0.29385 0.28424 0.00790  0.00983  0.01090  151 LEU A CA  
2361 C C   . LEU A 151 ? 0.32944 0.33048 0.32047 0.01078  0.01004  0.01127  151 LEU A C   
2362 O O   . LEU A 151 ? 0.31031 0.31044 0.30131 0.00939  0.01111  0.01085  151 LEU A O   
2363 C CB  . LEU A 151 ? 0.27933 0.27685 0.26574 0.00633  0.00486  0.00987  151 LEU A CB  
2364 C CG  . LEU A 151 ? 0.30180 0.29747 0.28640 0.00225  0.00403  0.00932  151 LEU A CG  
2365 C CD1 . LEU A 151 ? 0.36460 0.35858 0.34584 0.00115  -0.00105 0.00870  151 LEU A CD1 
2366 C CD2 . LEU A 151 ? 0.31954 0.31373 0.30478 -0.00132 0.00572  0.00856  151 LEU A CD2 
2378 N N   . ILE A 152 ? 0.30410 0.30856 0.29641 0.01461  0.00901  0.01203  152 ILE A N   
2379 C CA  . ILE A 152 ? 0.28679 0.29425 0.28084 0.01739  0.00906  0.01248  152 ILE A CA  
2380 C C   . ILE A 152 ? 0.28496 0.29218 0.28098 0.01680  0.01366  0.01341  152 ILE A C   
2381 O O   . ILE A 152 ? 0.29264 0.30002 0.28828 0.01616  0.01394  0.01316  152 ILE A O   
2382 C CB  . ILE A 152 ? 0.32472 0.33719 0.32098 0.02161  0.00797  0.01332  152 ILE A CB  
2383 C CG1 . ILE A 152 ? 0.40381 0.41592 0.39764 0.02204  0.00336  0.01216  152 ILE A CG1 
2384 C CG2 . ILE A 152 ? 0.34813 0.36479 0.34663 0.02437  0.00798  0.01392  152 ILE A CG2 
2385 C CD1 . ILE A 152 ? 0.48317 0.50078 0.47935 0.02582  0.00258  0.01274  152 ILE A CD1 
2397 N N   . LEU A 153 ? 0.28999 0.29695 0.28772 0.01712  0.01740  0.01454  153 LEU A N   
2398 C CA  . LEU A 153 ? 0.29586 0.30153 0.29517 0.01671  0.02204  0.01549  153 LEU A CA  
2399 C C   . LEU A 153 ? 0.32868 0.33014 0.32596 0.01241  0.02298  0.01411  153 LEU A C   
2400 O O   . LEU A 153 ? 0.33199 0.33297 0.32937 0.01155  0.02482  0.01421  153 LEU A O   
2401 C CB  . LEU A 153 ? 0.29455 0.30007 0.29524 0.01788  0.02567  0.01679  153 LEU A CB  
2402 C CG  . LEU A 153 ? 0.29635 0.30735 0.29982 0.02236  0.02615  0.01863  153 LEU A CG  
2403 C CD1 . LEU A 153 ? 0.32030 0.33203 0.32381 0.02333  0.02869  0.01962  153 LEU A CD1 
2404 C CD2 . LEU A 153 ? 0.35175 0.36484 0.35817 0.02465  0.02869  0.02028  153 LEU A CD2 
2416 N N   . ALA A 154 ? 0.29382 0.29284 0.28920 0.00940  0.02163  0.01279  154 ALA A N   
2417 C CA  . ALA A 154 ? 0.28952 0.28568 0.28353 0.00512  0.02266  0.01141  154 ALA A CA  
2418 C C   . ALA A 154 ? 0.26718 0.26460 0.25965 0.00435  0.02038  0.01066  154 ALA A C   
2419 O O   . ALA A 154 ? 0.35874 0.35553 0.35073 0.00212  0.02273  0.01026  154 ALA A O   
2420 C CB  . ALA A 154 ? 0.31800 0.31264 0.31073 0.00217  0.02107  0.01030  154 ALA A CB  
2426 N N   . TYR A 155 ? 0.28222 0.28151 0.27343 0.00608  0.01588  0.01039  155 TYR A N   
2427 C CA  . TYR A 155 ? 0.29430 0.29523 0.28343 0.00584  0.01347  0.00970  155 TYR A CA  
2428 C C   . TYR A 155 ? 0.40422 0.40814 0.39412 0.00783  0.01500  0.01057  155 TYR A C   
2429 O O   . TYR A 155 ? 0.35941 0.36464 0.34745 0.00622  0.01530  0.01009  155 TYR A O   
2430 C CB  . TYR A 155 ? 0.28758 0.28942 0.27503 0.00804  0.00833  0.00928  155 TYR A CB  
2431 C CG  . TYR A 155 ? 0.29184 0.29087 0.27727 0.00527  0.00594  0.00828  155 TYR A CG  
2432 C CD1 . TYR A 155 ? 0.32329 0.32172 0.30691 0.00194  0.00574  0.00737  155 TYR A CD1 
2433 C CD2 . TYR A 155 ? 0.29210 0.28971 0.27732 0.00581  0.00387  0.00835  155 TYR A CD2 
2434 C CE1 . TYR A 155 ? 0.30153 0.29792 0.28368 -0.00064 0.00339  0.00670  155 TYR A CE1 
2435 C CE2 . TYR A 155 ? 0.27747 0.27261 0.26068 0.00299  0.00141  0.00762  155 TYR A CE2 
2436 C CZ  . TYR A 155 ? 0.27813 0.27266 0.26005 -0.00012 0.00110  0.00686  155 TYR A CZ  
2437 O OH  . TYR A 155 ? 0.31187 0.30441 0.29216 -0.00290 -0.00150 0.00639  155 TYR A OH  
2447 N N   . CYS A 156 ? 0.33840 0.34419 0.33093 0.01121  0.01594  0.01197  156 CYS A N   
2448 C CA  . CYS A 156 ? 0.33728 0.34651 0.33096 0.01308  0.01722  0.01309  156 CYS A CA  
2449 C C   . CYS A 156 ? 0.42696 0.43370 0.42137 0.01076  0.02235  0.01377  156 CYS A C   
2450 O O   . CYS A 156 ? 0.40581 0.41498 0.40083 0.01168  0.02364  0.01483  156 CYS A O   
2451 C CB  . CYS A 156 ? 0.34265 0.35594 0.33945 0.01772  0.01613  0.01447  156 CYS A CB  
2452 S SG  . CYS A 156 ? 0.36702 0.38365 0.36280 0.02078  0.01007  0.01351  156 CYS A SG  
2458 N N   . ASN A 157 ? 0.34474 0.34678 0.33897 0.00776  0.02517  0.01315  157 ASN A N   
2459 C CA  . ASN A 157 ? 0.35955 0.35817 0.35428 0.00566  0.03025  0.01358  157 ASN A CA  
2460 C C   . ASN A 157 ? 0.44346 0.44289 0.44101 0.00919  0.03259  0.01577  157 ASN A C   
2461 O O   . ASN A 157 ? 0.40305 0.40177 0.40076 0.00875  0.03550  0.01674  157 ASN A O   
2462 C CB  . ASN A 157 ? 0.49751 0.49639 0.48970 0.00230  0.03135  0.01280  157 ASN A CB  
2463 C CG  . ASN A 157 ? 0.79224 0.78872 0.78251 -0.00233 0.03203  0.01084  157 ASN A CG  
2464 O OD1 . ASN A 157 ? 0.57175 0.57071 0.56001 -0.00350 0.02902  0.00977  157 ASN A OD1 
2465 N ND2 . ASN A 157 ? 0.55413 0.54613 0.54509 -0.00489 0.03607  0.01035  157 ASN A ND2 
2472 N N   . LYS A 158 ? 0.36176 0.36295 0.36141 0.01256  0.03144  0.01665  158 LYS A N   
2473 C CA  . LYS A 158 ? 0.35790 0.36069 0.36063 0.01620  0.03390  0.01890  158 LYS A CA  
2474 C C   . LYS A 158 ? 0.40225 0.40191 0.40546 0.01646  0.03653  0.01915  158 LYS A C   
2475 O O   . LYS A 158 ? 0.41109 0.41023 0.41305 0.01540  0.03449  0.01790  158 LYS A O   
2476 C CB  . LYS A 158 ? 0.39817 0.40765 0.40314 0.02032  0.03048  0.01986  158 LYS A CB  
2477 C CG  . LYS A 158 ? 0.47008 0.48390 0.47493 0.02093  0.02803  0.01995  158 LYS A CG  
2478 C CD  . LYS A 158 ? 0.57341 0.58812 0.58007 0.02162  0.03136  0.02196  158 LYS A CD  
2479 C CE  . LYS A 158 ? 0.63895 0.65896 0.64507 0.02193  0.02869  0.02209  158 LYS A CE  
2480 N NZ  . LYS A 158 ? 0.70208 0.71897 0.70372 0.01753  0.02865  0.02040  158 LYS A NZ  
2494 N N   . THR A 159 ? 0.39026 0.38793 0.39489 0.01784  0.04096  0.02080  159 THR A N   
2495 C CA  . THR A 159 ? 0.41372 0.40963 0.41861 0.01905  0.04346  0.02133  159 THR A CA  
2496 C C   . THR A 159 ? 0.38664 0.38845 0.39420 0.02381  0.04312  0.02340  159 THR A C   
2497 O O   . THR A 159 ? 0.40919 0.41581 0.41924 0.02638  0.04216  0.02480  159 THR A O   
2498 C CB  . THR A 159 ? 0.48992 0.48005 0.49445 0.01837  0.04878  0.02198  159 THR A CB  
2499 O OG1 . THR A 159 ? 0.52049 0.51163 0.52703 0.02080  0.05098  0.02426  159 THR A OG1 
2500 C CG2 . THR A 159 ? 0.59555 0.58041 0.59752 0.01325  0.04943  0.01966  159 THR A CG2 
2508 N N   . VAL A 160 ? 0.39010 0.39240 0.39712 0.02488  0.04395  0.02358  160 VAL A N   
2509 C CA  . VAL A 160 ? 0.38912 0.39754 0.39844 0.02928  0.04463  0.02570  160 VAL A CA  
2510 C C   . VAL A 160 ? 0.44707 0.45629 0.45932 0.03240  0.04869  0.02837  160 VAL A C   
2511 O O   . VAL A 160 ? 0.47393 0.47747 0.48537 0.03184  0.05268  0.02890  160 VAL A O   
2512 C CB  . VAL A 160 ? 0.42455 0.43314 0.43189 0.02959  0.04573  0.02559  160 VAL A CB  
2513 C CG1 . VAL A 160 ? 0.46461 0.47991 0.47405 0.03421  0.04769  0.02809  160 VAL A CG1 
2514 C CG2 . VAL A 160 ? 0.41658 0.42551 0.42129 0.02660  0.04112  0.02331  160 VAL A CG2 
2524 N N   . GLY A 161 ? 0.43549 0.45184 0.45125 0.03565  0.04766  0.03007  161 GLY A N   
2525 C CA  . GLY A 161 ? 0.42450 0.44311 0.44368 0.03877  0.05105  0.03295  161 GLY A CA  
2526 C C   . GLY A 161 ? 0.46668 0.48500 0.48706 0.03758  0.04991  0.03311  161 GLY A C   
2527 O O   . GLY A 161 ? 0.48668 0.50918 0.51061 0.04027  0.05146  0.03563  161 GLY A O   
2531 N N   . GLU A 162 ? 0.43477 0.44911 0.45220 0.03360  0.04721  0.03063  162 GLU A N   
2532 C CA  . GLU A 162 ? 0.44386 0.45823 0.46130 0.03196  0.04607  0.03059  162 GLU A CA  
2533 C C   . GLU A 162 ? 0.44826 0.47174 0.46853 0.03423  0.04173  0.03089  162 GLU A C   
2534 O O   . GLU A 162 ? 0.43917 0.46634 0.45953 0.03511  0.03831  0.02963  162 GLU A O   
2535 C CB  . GLU A 162 ? 0.45657 0.46476 0.46960 0.02702  0.04481  0.02778  162 GLU A CB  
2536 C CG  . GLU A 162 ? 0.63191 0.64011 0.64367 0.02463  0.04385  0.02749  162 GLU A CG  
2537 C CD  . GLU A 162 ? 0.66021 0.66182 0.66758 0.01947  0.04439  0.02505  162 GLU A CD  
2538 O OE1 . GLU A 162 ? 0.51664 0.51397 0.52242 0.01777  0.04506  0.02346  162 GLU A OE1 
2539 O OE2 . GLU A 162 ? 0.75643 0.75794 0.76193 0.01696  0.04416  0.02474  162 GLU A OE2 
2546 N N   . LEU A 163 ? 0.45395 0.48113 0.47637 0.03508  0.04176  0.03250  163 LEU A N   
2547 C CA  . LEU A 163 ? 0.45793 0.49462 0.48327 0.03734  0.03750  0.03272  163 LEU A CA  
2548 C C   . LEU A 163 ? 0.44549 0.48177 0.46722 0.03492  0.03273  0.02978  163 LEU A C   
2549 O O   . LEU A 163 ? 0.48548 0.51600 0.50308 0.03113  0.03296  0.02838  163 LEU A O   
2550 C CB  . LEU A 163 ? 0.50465 0.54557 0.53268 0.03824  0.03842  0.03510  163 LEU A CB  
2551 C CG  . LEU A 163 ? 0.97844 1.02001 1.01029 0.04097  0.04328  0.03847  163 LEU A CG  
2552 C CD1 . LEU A 163 ? 0.77096 0.82089 0.80718 0.04293  0.04258  0.04104  163 LEU A CD1 
2553 C CD2 . LEU A 163 ? 0.84969 0.89461 0.88437 0.04448  0.04466  0.03926  163 LEU A CD2 
2565 N N   . GLY A 164 ? 0.38312 0.42559 0.40625 0.03714  0.02858  0.02883  164 GLY A N   
2566 C CA  . GLY A 164 ? 0.32006 0.36251 0.33976 0.03565  0.02383  0.02622  164 GLY A CA  
2567 C C   . GLY A 164 ? 0.36719 0.41915 0.38939 0.03862  0.01952  0.02625  164 GLY A C   
2568 O O   . GLY A 164 ? 0.35869 0.41813 0.38596 0.04209  0.01963  0.02789  164 GLY A O   
2572 N N   . ASP A 165 ? 0.32654 0.37881 0.34514 0.03733  0.01573  0.02439  165 ASP A N   
2573 C CA  . ASP A 165 ? 0.31636 0.37734 0.33616 0.04009  0.01092  0.02383  165 ASP A CA  
2574 C C   . ASP A 165 ? 0.34064 0.40046 0.35808 0.04090  0.00686  0.02136  165 ASP A C   
2575 O O   . ASP A 165 ? 0.30203 0.35457 0.31475 0.03812  0.00648  0.01970  165 ASP A O   
2576 C CB  . ASP A 165 ? 0.33019 0.39286 0.34679 0.03827  0.00962  0.02367  165 ASP A CB  
2577 C CG  . ASP A 165 ? 0.44260 0.51471 0.45971 0.04121  0.00435  0.02294  165 ASP A CG  
2578 O OD1 . ASP A 165 ? 0.49513 0.57618 0.51711 0.04400  0.00362  0.02456  165 ASP A OD1 
2579 O OD2 . ASP A 165 ? 0.37675 0.44770 0.38931 0.04082  0.00087  0.02078  165 ASP A OD2 
2584 N N   . VAL A 166 ? 0.28385 0.35099 0.30467 0.04463  0.00386  0.02112  166 VAL A N   
2585 C CA  . VAL A 166 ? 0.27352 0.33890 0.29203 0.04548  0.00017  0.01881  166 VAL A CA  
2586 C C   . VAL A 166 ? 0.26480 0.32855 0.27797 0.04481  -0.00394 0.01678  166 VAL A C   
2587 O O   . VAL A 166 ? 0.29220 0.34923 0.30094 0.04322  -0.00547 0.01503  166 VAL A O   
2588 C CB  . VAL A 166 ? 0.30985 0.38395 0.33335 0.04954  -0.00184 0.01890  166 VAL A CB  
2589 C CG1 . VAL A 166 ? 0.35796 0.43073 0.37834 0.05062  -0.00657 0.01624  166 VAL A CG1 
2590 C CG2 . VAL A 166 ? 0.30283 0.37700 0.32999 0.04976  0.00228  0.02048  166 VAL A CG2 
2600 N N   . ARG A 167 ? 0.28622 0.35646 0.29944 0.04600  -0.00581 0.01710  167 ARG A N   
2601 C CA  . ARG A 167 ? 0.27368 0.34349 0.28133 0.04579  -0.00965 0.01529  167 ARG A CA  
2602 C C   . ARG A 167 ? 0.28847 0.34932 0.29082 0.04129  -0.00743 0.01476  167 ARG A C   
2603 O O   . ARG A 167 ? 0.29910 0.35559 0.29679 0.04058  -0.00977 0.01300  167 ARG A O   
2604 C CB  . ARG A 167 ? 0.30556 0.38482 0.31379 0.04744  -0.01161 0.01600  167 ARG A CB  
2605 C CG  . ARG A 167 ? 0.31454 0.39550 0.31694 0.04827  -0.01604 0.01415  167 ARG A CG  
2606 C CD  . ARG A 167 ? 0.36301 0.44839 0.36250 0.04650  -0.01565 0.01503  167 ARG A CD  
2607 N NE  . ARG A 167 ? 0.42262 0.49976 0.41815 0.04150  -0.01169 0.01523  167 ARG A NE  
2608 C CZ  . ARG A 167 ? 0.41298 0.48566 0.40241 0.03952  -0.01243 0.01376  167 ARG A CZ  
2609 N NH1 . ARG A 167 ? 0.39398 0.46906 0.37975 0.04227  -0.01704 0.01210  167 ARG A NH1 
2610 N NH2 . ARG A 167 ? 0.47748 0.54312 0.46456 0.03478  -0.00834 0.01395  167 ARG A NH2 
2624 N N   . GLU A 168 ? 0.29336 0.35142 0.29652 0.03824  -0.00278 0.01628  168 GLU A N   
2625 C CA  . GLU A 168 ? 0.30319 0.35345 0.30196 0.03368  -0.00023 0.01568  168 GLU A CA  
2626 C C   . GLU A 168 ? 0.29901 0.34160 0.29680 0.03227  0.00023  0.01460  168 GLU A C   
2627 O O   . GLU A 168 ? 0.30633 0.34418 0.29981 0.02977  -0.00050 0.01323  168 GLU A O   
2628 C CB  . GLU A 168 ? 0.32577 0.37446 0.32595 0.03094  0.00480  0.01746  168 GLU A CB  
2629 C CG  . GLU A 168 ? 0.35479 0.39669 0.35064 0.02600  0.00762  0.01670  168 GLU A CG  
2630 C CD  . GLU A 168 ? 0.49181 0.53737 0.48312 0.02432  0.00638  0.01621  168 GLU A CD  
2631 O OE1 . GLU A 168 ? 0.36135 0.41471 0.35239 0.02726  0.00274  0.01633  168 GLU A OE1 
2632 O OE2 . GLU A 168 ? 0.44583 0.48706 0.43370 0.01997  0.00907  0.01562  168 GLU A OE2 
2639 N N   . THR A 169 ? 0.26818 0.31019 0.26981 0.03371  0.00144  0.01529  169 THR A N   
2640 C CA  . THR A 169 ? 0.29798 0.33366 0.29844 0.03230  0.00158  0.01437  169 THR A CA  
2641 C C   . THR A 169 ? 0.30226 0.33692 0.29935 0.03338  -0.00335 0.01244  169 THR A C   
2642 O O   . THR A 169 ? 0.30111 0.32969 0.29469 0.03075  -0.00394 0.01133  169 THR A O   
2643 C CB  . THR A 169 ? 0.27780 0.31504 0.28270 0.03409  0.00365  0.01563  169 THR A CB  
2644 O OG1 . THR A 169 ? 0.32333 0.36060 0.33089 0.03327  0.00845  0.01756  169 THR A OG1 
2645 C CG2 . THR A 169 ? 0.30516 0.33685 0.30841 0.03246  0.00369  0.01480  169 THR A CG2 
2653 N N   . MET A 170 ? 0.28280 0.32341 0.28092 0.03727  -0.00698 0.01202  170 MET A N   
2654 C CA  . MET A 170 ? 0.33718 0.37630 0.33162 0.03871  -0.01175 0.01012  170 MET A CA  
2655 C C   . MET A 170 ? 0.33830 0.37497 0.32749 0.03692  -0.01302 0.00924  170 MET A C   
2656 O O   . MET A 170 ? 0.32386 0.35537 0.30905 0.03604  -0.01528 0.00796  170 MET A O   
2657 C CB  . MET A 170 ? 0.30407 0.35092 0.30079 0.04348  -0.01529 0.00971  170 MET A CB  
2658 C CG  . MET A 170 ? 0.30882 0.35958 0.31088 0.04558  -0.01441 0.01037  170 MET A CG  
2659 S SD  . MET A 170 ? 0.36834 0.41194 0.36948 0.04348  -0.01339 0.00987  170 MET A SD  
2660 C CE  . MET A 170 ? 0.33925 0.37912 0.33533 0.04493  -0.01922 0.00728  170 MET A CE  
2670 N N   A SER A 171 ? 0.31126 0.35188 0.30013 0.03621  -0.01152 0.01001  171 SER A N   
2671 N N   B SER A 171 ? 0.30755 0.34819 0.29643 0.03622  -0.01153 0.01001  171 SER A N   
2672 C CA  A SER A 171 ? 0.28764 0.32725 0.27126 0.03435  -0.01231 0.00926  171 SER A CA  
2673 C CA  B SER A 171 ? 0.28341 0.32306 0.26706 0.03436  -0.01230 0.00927  171 SER A CA  
2674 C C   A SER A 171 ? 0.34514 0.37692 0.32662 0.02984  -0.00996 0.00887  171 SER A C   
2675 C C   B SER A 171 ? 0.34932 0.38115 0.33081 0.02985  -0.00995 0.00888  171 SER A C   
2676 O O   A SER A 171 ? 0.33509 0.36420 0.31234 0.02902  -0.01197 0.00781  171 SER A O   
2677 O O   B SER A 171 ? 0.33470 0.36390 0.31194 0.02902  -0.01195 0.00782  171 SER A O   
2678 C CB  A SER A 171 ? 0.37335 0.41878 0.35679 0.03356  -0.01051 0.01028  171 SER A CB  
2679 C CB  B SER A 171 ? 0.37671 0.42218 0.36030 0.03357  -0.01044 0.01031  171 SER A CB  
2680 O OG  A SER A 171 ? 0.37641 0.41875 0.36173 0.02972  -0.00538 0.01143  171 SER A OG  
2681 O OG  B SER A 171 ? 0.39559 0.44125 0.37375 0.03163  -0.01092 0.00961  171 SER A OG  
2692 N N   . TYR A 172 ? 0.31621 0.34465 0.30068 0.02708  -0.00578 0.00976  172 TYR A N   
2693 C CA  . TYR A 172 ? 0.32396 0.34580 0.30701 0.02284  -0.00371 0.00930  172 TYR A CA  
2694 C C   . TYR A 172 ? 0.35647 0.37400 0.33816 0.02331  -0.00683 0.00834  172 TYR A C   
2695 O O   . TYR A 172 ? 0.37178 0.38557 0.35040 0.02087  -0.00772 0.00754  172 TYR A O   
2696 C CB  . TYR A 172 ? 0.36101 0.38050 0.34755 0.02055  0.00110  0.01038  172 TYR A CB  
2697 C CG  . TYR A 172 ? 0.36345 0.38357 0.34988 0.01775  0.00508  0.01097  172 TYR A CG  
2698 C CD1 . TYR A 172 ? 0.46059 0.47753 0.44456 0.01333  0.00710  0.01019  172 TYR A CD1 
2699 C CD2 . TYR A 172 ? 0.44044 0.46438 0.42932 0.01921  0.00699  0.01235  172 TYR A CD2 
2700 C CE1 . TYR A 172 ? 0.45906 0.47629 0.44263 0.01034  0.01100  0.01053  172 TYR A CE1 
2701 C CE2 . TYR A 172 ? 0.49540 0.51914 0.48359 0.01623  0.01071  0.01289  172 TYR A CE2 
2702 C CZ  . TYR A 172 ? 0.49947 0.51961 0.48482 0.01174  0.01277  0.01186  172 TYR A CZ  
2703 O OH  . TYR A 172 ? 0.43567 0.45535 0.42001 0.00840  0.01667  0.01218  172 TYR A OH  
2714 N N   . LEU A 173 ? 0.31459 0.33278 0.29860 0.02611  -0.00829 0.00849  173 LEU A N   
2715 C CA  . LEU A 173 ? 0.35328 0.36724 0.33546 0.02633  -0.01136 0.00756  173 LEU A CA  
2716 C C   . LEU A 173 ? 0.34037 0.35346 0.31804 0.02785  -0.01574 0.00633  173 LEU A C   
2717 O O   . LEU A 173 ? 0.36109 0.36894 0.33563 0.02592  -0.01740 0.00566  173 LEU A O   
2718 C CB  . LEU A 173 ? 0.35043 0.36672 0.33567 0.02926  -0.01208 0.00784  173 LEU A CB  
2719 C CG  . LEU A 173 ? 0.42045 0.43702 0.40950 0.02788  -0.00778 0.00917  173 LEU A CG  
2720 C CD1 . LEU A 173 ? 0.50489 0.52612 0.49727 0.03129  -0.00824 0.00963  173 LEU A CD1 
2721 C CD2 . LEU A 173 ? 0.58465 0.59527 0.57189 0.02395  -0.00676 0.00894  173 LEU A CD2 
2733 N N   . PHE A 174 ? 0.33229 0.35082 0.30941 0.03134  -0.01764 0.00614  174 PHE A N   
2734 C CA  . PHE A 174 ? 0.34912 0.36746 0.32151 0.03352  -0.02177 0.00502  174 PHE A CA  
2735 C C   . PHE A 174 ? 0.37980 0.39626 0.34852 0.03034  -0.02070 0.00499  174 PHE A C   
2736 O O   . PHE A 174 ? 0.37584 0.38940 0.34028 0.03091  -0.02359 0.00424  174 PHE A O   
2737 C CB  . PHE A 174 ? 0.36169 0.38773 0.33436 0.03804  -0.02392 0.00487  174 PHE A CB  
2738 C CG  . PHE A 174 ? 0.37355 0.40268 0.34978 0.04173  -0.02573 0.00461  174 PHE A CG  
2739 C CD1 . PHE A 174 ? 0.39038 0.41486 0.36777 0.04138  -0.02625 0.00420  174 PHE A CD1 
2740 C CD2 . PHE A 174 ? 0.37337 0.41104 0.35175 0.04536  -0.02694 0.00478  174 PHE A CD2 
2741 C CE1 . PHE A 174 ? 0.40712 0.43555 0.38793 0.04455  -0.02755 0.00390  174 PHE A CE1 
2742 C CE2 . PHE A 174 ? 0.42792 0.46980 0.41020 0.04873  -0.02852 0.00450  174 PHE A CE2 
2743 C CZ  . PHE A 174 ? 0.38509 0.42237 0.36864 0.04831  -0.02866 0.00401  174 PHE A CZ  
2753 N N   . GLN A 175 ? 0.35771 0.37600 0.32793 0.02704  -0.01650 0.00581  175 GLN A N   
2754 C CA  . GLN A 175 ? 0.40225 0.41955 0.36948 0.02344  -0.01491 0.00570  175 GLN A CA  
2755 C C   . GLN A 175 ? 0.40180 0.41250 0.36830 0.02034  -0.01517 0.00537  175 GLN A C   
2756 O O   . GLN A 175 ? 0.41294 0.42282 0.37641 0.01839  -0.01547 0.00511  175 GLN A O   
2757 C CB  . GLN A 175 ? 0.38247 0.40227 0.35174 0.01997  -0.00997 0.00646  175 GLN A CB  
2758 C CG  . GLN A 175 ? 0.53570 0.56264 0.50444 0.02192  -0.00962 0.00693  175 GLN A CG  
2759 C CD  . GLN A 175 ? 0.96913 1.00042 0.93257 0.02235  -0.01119 0.00648  175 GLN A CD  
2760 O OE1 . GLN A 175 ? 0.95324 0.98222 0.91342 0.02204  -0.01295 0.00585  175 GLN A OE1 
2761 N NE2 . GLN A 175 ? 0.99563 1.03372 0.95793 0.02307  -0.01057 0.00694  175 GLN A NE2 
2770 N N   . HIS A 176 ? 0.33639 0.34319 0.30561 0.01973  -0.01500 0.00549  176 HIS A N   
2771 C CA  . HIS A 176 ? 0.40302 0.40413 0.37163 0.01665  -0.01558 0.00528  176 HIS A CA  
2772 C C   . HIS A 176 ? 0.37041 0.36764 0.33664 0.01915  -0.02017 0.00469  176 HIS A C   
2773 O O   . HIS A 176 ? 0.36017 0.35286 0.32639 0.01695  -0.02087 0.00466  176 HIS A O   
2774 C CB  . HIS A 176 ? 0.35639 0.35616 0.32889 0.01375  -0.01205 0.00584  176 HIS A CB  
2775 C CG  . HIS A 176 ? 0.44128 0.44325 0.41568 0.01069  -0.00741 0.00622  176 HIS A CG  
2776 N ND1 . HIS A 176 ? 0.54275 0.54363 0.51655 0.00632  -0.00570 0.00594  176 HIS A ND1 
2777 C CD2 . HIS A 176 ? 0.40331 0.40852 0.38010 0.01124  -0.00413 0.00683  176 HIS A CD2 
2778 C CE1 . HIS A 176 ? 0.37253 0.37556 0.34812 0.00424  -0.00144 0.00615  176 HIS A CE1 
2779 N NE2 . HIS A 176 ? 0.50230 0.50750 0.47947 0.00713  -0.00044 0.00676  176 HIS A NE2 
2787 N N   . ALA A 177 ? 0.40128 0.39193 0.35251 0.06838  -0.03085 -0.01846 177 ALA A N   
2788 C CA  . ALA A 177 ? 0.35073 0.35414 0.31858 0.06850  -0.02943 -0.01767 177 ALA A CA  
2789 C C   . ALA A 177 ? 0.40571 0.41341 0.38422 0.06413  -0.03358 -0.01739 177 ALA A C   
2790 O O   . ALA A 177 ? 0.37659 0.37813 0.35090 0.06025  -0.03764 -0.01797 177 ALA A O   
2791 C CB  . ALA A 177 ? 0.34865 0.36031 0.32616 0.06746  -0.02701 -0.01989 177 ALA A CB  
2797 N N   . ASN A 178 ? 0.37959 0.39802 0.37301 0.06462  -0.03261 -0.01602 178 ASN A N   
2798 C CA  . ASN A 178 ? 0.35265 0.37678 0.35921 0.06025  -0.03586 -0.01503 178 ASN A CA  
2799 C C   . ASN A 178 ? 0.36164 0.39298 0.38255 0.05591  -0.03594 -0.01804 178 ASN A C   
2800 O O   . ASN A 178 ? 0.38049 0.42223 0.41520 0.05662  -0.03333 -0.01918 178 ASN A O   
2801 C CB  . ASN A 178 ? 0.42594 0.45898 0.44363 0.06291  -0.03482 -0.01167 178 ASN A CB  
2802 C CG  . ASN A 178 ? 0.74589 0.78518 0.77799 0.05798  -0.03803 -0.00975 178 ASN A CG  
2803 O OD1 . ASN A 178 ? 0.54558 0.58379 0.58224 0.05235  -0.04042 -0.01118 178 ASN A OD1 
2804 N ND2 . ASN A 178 ? 0.77538 0.82186 0.81609 0.06009  -0.03793 -0.00584 178 ASN A ND2 
2811 N N   . LEU A 179 ? 0.36062 0.38634 0.37863 0.05146  -0.03906 -0.01917 179 LEU A N   
2812 C CA  . LEU A 179 ? 0.36673 0.39817 0.39738 0.04731  -0.03924 -0.02158 179 LEU A CA  
2813 C C   . LEU A 179 ? 0.37812 0.40978 0.41847 0.04174  -0.04286 -0.01945 179 LEU A C   
2814 O O   . LEU A 179 ? 0.37606 0.40795 0.42277 0.03782  -0.04408 -0.02046 179 LEU A O   
2815 C CB  . LEU A 179 ? 0.38972 0.41524 0.41046 0.04726  -0.03942 -0.02394 179 LEU A CB  
2816 C CG  . LEU A 179 ? 0.40075 0.42845 0.41575 0.05164  -0.03524 -0.02570 179 LEU A CG  
2817 C CD1 . LEU A 179 ? 0.51086 0.53275 0.51647 0.05136  -0.03590 -0.02703 179 LEU A CD1 
2818 C CD2 . LEU A 179 ? 0.39028 0.43078 0.42006 0.05172  -0.03185 -0.02785 179 LEU A CD2 
2830 N N   . ASP A 180 ? 0.36912 0.40096 0.41104 0.04131  -0.04452 -0.01585 180 ASP A N   
2831 C CA  . ASP A 180 ? 0.43360 0.46507 0.48392 0.03550  -0.04816 -0.01258 180 ASP A CA  
2832 C C   . ASP A 180 ? 0.44032 0.48306 0.51380 0.03168  -0.04650 -0.01297 180 ASP A C   
2833 O O   . ASP A 180 ? 0.52448 0.56630 0.60631 0.02609  -0.04896 -0.01046 180 ASP A O   
2834 C CB  . ASP A 180 ? 0.46451 0.49574 0.51203 0.03607  -0.04992 -0.00825 180 ASP A CB  
2835 C CG  . ASP A 180 ? 0.63415 0.65191 0.65828 0.03788  -0.05267 -0.00760 180 ASP A CG  
2836 O OD1 . ASP A 180 ? 0.59906 0.60728 0.61061 0.03807  -0.05373 -0.01014 180 ASP A OD1 
2837 O OD2 . ASP A 180 ? 0.66909 0.68642 0.68814 0.03924  -0.05366 -0.00451 180 ASP A OD2 
2842 N N   . SER A 181 ? 0.46702 0.51990 0.55118 0.03439  -0.04233 -0.01588 181 SER A N   
2843 C CA  . SER A 181 ? 0.46866 0.53202 0.57440 0.03103  -0.04015 -0.01749 181 SER A CA  
2844 C C   . SER A 181 ? 0.55248 0.61429 0.65806 0.02918  -0.03921 -0.02140 181 SER A C   
2845 O O   . SER A 181 ? 0.51063 0.58042 0.63301 0.02639  -0.03699 -0.02338 181 SER A O   
2846 C CB  . SER A 181 ? 0.45993 0.53491 0.57744 0.03481  -0.03639 -0.01931 181 SER A CB  
2847 O OG  . SER A 181 ? 0.56282 0.64225 0.68662 0.03603  -0.03716 -0.01490 181 SER A OG  
2853 N N   . CYS A 182 ? 0.38675 0.43921 0.47485 0.03074  -0.04066 -0.02248 182 CYS A N   
2854 C CA  . CYS A 182 ? 0.36686 0.41935 0.45470 0.02989  -0.03965 -0.02581 182 CYS A CA  
2855 C C   . CYS A 182 ? 0.36616 0.41206 0.45563 0.02514  -0.04310 -0.02314 182 CYS A C   
2856 O O   . CYS A 182 ? 0.40290 0.43869 0.48171 0.02417  -0.04727 -0.01959 182 CYS A O   
2857 C CB  . CYS A 182 ? 0.34215 0.38985 0.41278 0.03431  -0.03906 -0.02784 182 CYS A CB  
2858 S SG  . CYS A 182 ? 0.36954 0.42543 0.44001 0.03955  -0.03444 -0.03050 182 CYS A SG  
2864 N N   . LYS A 183 ? 0.33416 0.38546 0.43684 0.02225  -0.04135 -0.02471 183 LYS A N   
2865 C CA  . LYS A 183 ? 0.32444 0.37012 0.43135 0.01780  -0.04413 -0.02142 183 LYS A CA  
2866 C C   . LYS A 183 ? 0.37610 0.42470 0.48570 0.01806  -0.04218 -0.02455 183 LYS A C   
2867 O O   . LYS A 183 ? 0.39299 0.45134 0.50969 0.01935  -0.03783 -0.02932 183 LYS A O   
2868 C CB  . LYS A 183 ? 0.36856 0.41828 0.49405 0.01259  -0.04380 -0.01798 183 LYS A CB  
2869 C CG  . LYS A 183 ? 0.49053 0.53320 0.62053 0.00771  -0.04677 -0.01317 183 LYS A CG  
2870 C CD  . LYS A 183 ? 0.63153 0.67639 0.77839 0.00191  -0.04713 -0.00779 183 LYS A CD  
2871 C CE  . LYS A 183 ? 0.84544 0.90123 1.01404 -0.00044 -0.04177 -0.01017 183 LYS A CE  
2872 N NZ  . LYS A 183 ? 0.87845 0.93473 1.06490 -0.00710 -0.04211 -0.00366 183 LYS A NZ  
2886 N N   . ARG A 184 ? 0.37459 0.41492 0.47852 0.01695  -0.04565 -0.02165 184 ARG A N   
2887 C CA  . ARG A 184 ? 0.35093 0.39375 0.45736 0.01742  -0.04442 -0.02338 184 ARG A CA  
2888 C C   . ARG A 184 ? 0.40520 0.44108 0.51805 0.01343  -0.04764 -0.01783 184 ARG A C   
2889 O O   . ARG A 184 ? 0.40745 0.43290 0.51336 0.01201  -0.05268 -0.01282 184 ARG A O   
2890 C CB  . ARG A 184 ? 0.31876 0.35894 0.40990 0.02185  -0.04558 -0.02500 184 ARG A CB  
2891 C CG  . ARG A 184 ? 0.34538 0.38765 0.43875 0.02244  -0.04547 -0.02518 184 ARG A CG  
2892 C CD  . ARG A 184 ? 0.37566 0.41955 0.45735 0.02682  -0.04523 -0.02735 184 ARG A CD  
2893 N NE  . ARG A 184 ? 0.32514 0.38040 0.40863 0.02864  -0.04004 -0.03270 184 ARG A NE  
2894 C CZ  . ARG A 184 ? 0.38695 0.44606 0.46210 0.03201  -0.03850 -0.03478 184 ARG A CZ  
2895 N NH1 . ARG A 184 ? 0.35268 0.40595 0.41781 0.03418  -0.04131 -0.03243 184 ARG A NH1 
2896 N NH2 . ARG A 184 ? 0.34423 0.41341 0.42200 0.03300  -0.03404 -0.03901 184 ARG A NH2 
2910 N N   . VAL A 185 ? 0.38505 0.42632 0.51101 0.01153  -0.04474 -0.01846 185 VAL A N   
2911 C CA  . VAL A 185 ? 0.36898 0.40369 0.50187 0.00819  -0.04726 -0.01255 185 VAL A CA  
2912 C C   . VAL A 185 ? 0.41205 0.44959 0.54414 0.01088  -0.04620 -0.01410 185 VAL A C   
2913 O O   . VAL A 185 ? 0.39614 0.44427 0.53367 0.01222  -0.04112 -0.01968 185 VAL A O   
2914 C CB  . VAL A 185 ? 0.36539 0.40339 0.51719 0.00295  -0.04441 -0.01032 185 VAL A CB  
2915 C CG1 . VAL A 185 ? 0.43581 0.46566 0.59461 -0.00056 -0.04706 -0.00285 185 VAL A CG1 
2916 C CG2 . VAL A 185 ? 0.44332 0.48086 0.59748 0.00044  -0.04538 -0.00837 185 VAL A CG2 
2926 N N   . LEU A 186 ? 0.41125 0.43987 0.53669 0.01178  -0.05121 -0.00910 186 LEU A N   
2927 C CA  . LEU A 186 ? 0.37139 0.40247 0.49668 0.01469  -0.05118 -0.00894 186 LEU A CA  
2928 C C   . LEU A 186 ? 0.44556 0.46984 0.58035 0.01203  -0.05360 -0.00160 186 LEU A C   
2929 O O   . LEU A 186 ? 0.48363 0.49814 0.62054 0.00827  -0.05735 0.00452  186 LEU A O   
2930 C CB  . LEU A 186 ? 0.45679 0.48420 0.56733 0.01908  -0.05515 -0.00884 186 LEU A CB  
2931 C CG  . LEU A 186 ? 0.46935 0.50167 0.56928 0.02197  -0.05305 -0.01473 186 LEU A CG  
2932 C CD1 . LEU A 186 ? 0.52538 0.55109 0.61159 0.02532  -0.05742 -0.01328 186 LEU A CD1 
2933 C CD2 . LEU A 186 ? 0.47926 0.52582 0.58365 0.02387  -0.04702 -0.02087 186 LEU A CD2 
2945 N N   . ASN A 187 ? 0.40229 0.43206 0.54299 0.01396  -0.05139 -0.00175 187 ASN A N   
2946 C CA  . ASN A 187 ? 0.46401 0.48742 0.61324 0.01267  -0.05365 0.00590  187 ASN A CA  
2947 C C   . ASN A 187 ? 0.54352 0.56892 0.68826 0.01782  -0.05595 0.00731  187 ASN A C   
2948 O O   . ASN A 187 ? 0.47410 0.51095 0.61635 0.02130  -0.05236 0.00136  187 ASN A O   
2949 C CB  . ASN A 187 ? 0.47544 0.50448 0.64059 0.00960  -0.04754 0.00527  187 ASN A CB  
2950 C CG  . ASN A 187 ? 0.56787 0.58769 0.74321 0.00688  -0.04978 0.01484  187 ASN A CG  
2951 O OD1 . ASN A 187 ? 0.53976 0.54773 0.71119 0.00578  -0.05636 0.02240  187 ASN A OD1 
2952 N ND2 . ASN A 187 ? 0.59669 0.62150 0.78526 0.00569  -0.04424 0.01478  187 ASN A ND2 
2959 N N   . VAL A 188 ? 0.49792 0.51264 0.64231 0.01821  -0.06221 0.01566  188 VAL A N   
2960 C CA  . VAL A 188 ? 0.40462 0.42082 0.54761 0.02320  -0.06522 0.01877  188 VAL A CA  
2961 C C   . VAL A 188 ? 0.48814 0.50023 0.64370 0.02244  -0.06589 0.02686  188 VAL A C   
2962 O O   . VAL A 188 ? 0.54333 0.54341 0.70316 0.01854  -0.06940 0.03414  188 VAL A O   
2963 C CB  . VAL A 188 ? 0.59002 0.59691 0.72164 0.02527  -0.07274 0.02187  188 VAL A CB  
2964 C CG1 . VAL A 188 ? 0.61819 0.62841 0.75116 0.03073  -0.07573 0.02536  188 VAL A CG1 
2965 C CG2 . VAL A 188 ? 0.57505 0.58477 0.69420 0.02591  -0.07153 0.01441  188 VAL A CG2 
2975 N N   . VAL A 189 ? 0.46095 0.48315 0.62257 0.02605  -0.06244 0.02606  189 VAL A N   
2976 C CA  . VAL A 189 ? 0.51472 0.53507 0.68914 0.02587  -0.06128 0.03293  189 VAL A CA  
2977 C C   . VAL A 189 ? 0.51309 0.53503 0.68827 0.03184  -0.06561 0.03867  189 VAL A C   
2978 O O   . VAL A 189 ? 0.50493 0.53970 0.67717 0.03634  -0.06361 0.03390  189 VAL A O   
2979 C CB  . VAL A 189 ? 0.58287 0.61489 0.76558 0.02478  -0.05225 0.02667  189 VAL A CB  
2980 C CG1 . VAL A 189 ? 0.72177 0.75186 0.91743 0.02519  -0.05045 0.03391  189 VAL A CG1 
2981 C CG2 . VAL A 189 ? 0.55469 0.58574 0.73900 0.01907  -0.04827 0.02147  189 VAL A CG2 
2991 N N   . CYS A 190 ? 0.55162 0.55999 0.72174 0.02863  -0.06726 0.04636  190 CYS A N   
2992 C CA  . CYS A 190 ? 0.52660 0.53451 0.68830 0.03051  -0.06632 0.04927  190 CYS A CA  
2993 C C   . CYS A 190 ? 0.57613 0.58028 0.74369 0.02753  -0.06232 0.05464  190 CYS A C   
2994 O O   . CYS A 190 ? 0.59253 0.58764 0.76453 0.02157  -0.06240 0.05858  190 CYS A O   
2995 C CB  . CYS A 190 ? 0.51232 0.50974 0.66094 0.02878  -0.07091 0.05124  190 CYS A CB  
2996 S SG  . CYS A 190 ? 0.48985 0.48823 0.63034 0.03113  -0.06897 0.05379  190 CYS A SG  
3001 N N   . ASP A 191 ? 0.53747 0.54958 0.70496 0.03142  -0.05868 0.05475  191 ASP A N   
3002 C CA  . ASP A 191 ? 0.57825 0.58735 0.75066 0.02906  -0.05479 0.05961  191 ASP A CA  
3003 C C   . ASP A 191 ? 0.67303 0.67041 0.83906 0.02364  -0.05681 0.06450  191 ASP A C   
3004 O O   . ASP A 191 ? 0.65608 0.64948 0.82824 0.01891  -0.05454 0.06850  191 ASP A O   
3005 C CB  . ASP A 191 ? 0.65937 0.67901 0.83009 0.03471  -0.05135 0.05859  191 ASP A CB  
3006 C CG  . ASP A 191 ? 0.86869 0.90389 1.04821 0.03930  -0.04797 0.05296  191 ASP A CG  
3007 O OD1 . ASP A 191 ? 0.86106 0.89791 1.05325 0.03755  -0.04452 0.05226  191 ASP A OD1 
3008 O OD2 . ASP A 191 ? 0.70527 0.75256 0.87977 0.04423  -0.04813 0.04851  191 ASP A OD2 
3013 N N   . THR A 192 ? 0.54488 0.53864 0.69964 0.02429  -0.06063 0.06357  192 THR A N   
3014 C CA  . THR A 192 ? 0.58007 0.56519 0.72957 0.01953  -0.06258 0.06664  192 THR A CA  
3015 C C   . THR A 192 ? 0.63132 0.60917 0.78225 0.01378  -0.06608 0.06735  192 THR A C   
3016 O O   . THR A 192 ? 0.66429 0.63913 0.81997 0.00830  -0.06541 0.07052  192 THR A O   
3017 C CB  . THR A 192 ? 0.57197 0.55690 0.71035 0.02288  -0.06454 0.06506  192 THR A CB  
3018 O OG1 . THR A 192 ? 0.54465 0.53654 0.68573 0.02640  -0.06211 0.06614  192 THR A OG1 
3019 C CG2 . THR A 192 ? 0.66492 0.64220 0.80547 0.01650  -0.06923 0.06879  192 THR A CG2 
3027 N N   . CYS A 193 ? 0.53942 0.51581 0.68649 0.01513  -0.06975 0.06422  193 CYS A N   
3028 C CA  . CYS A 193 ? 0.68187 0.65059 0.82688 0.01011  -0.07400 0.06472  193 CYS A CA  
3029 C C   . CYS A 193 ? 0.72291 0.69167 0.87808 0.00675  -0.07322 0.06519  193 CYS A C   
3030 O O   . CYS A 193 ? 0.66865 0.63201 0.82268 0.00219  -0.07636 0.06604  193 CYS A O   
3031 C CB  . CYS A 193 ? 0.61042 0.57651 0.74533 0.01308  -0.07866 0.06116  193 CYS A CB  
3032 S SG  . CYS A 193 ? 0.56430 0.53243 0.68971 0.01781  -0.07861 0.06004  193 CYS A SG  
3037 N N   . GLY A 194 ? 0.62810 0.60341 0.79373 0.00898  -0.06888 0.06449  194 GLY A N   
3038 C CA  . GLY A 194 ? 0.58331 0.55923 0.76111 0.00582  -0.06705 0.06470  194 GLY A CA  
3039 C C   . GLY A 194 ? 0.73651 0.71436 0.91493 0.00914  -0.06955 0.05968  194 GLY A C   
3040 O O   . GLY A 194 ? 0.72946 0.71354 0.90243 0.01551  -0.07096 0.05500  194 GLY A O   
3044 N N   . GLN A 195 ? 0.57068 0.54543 0.75607 0.00489  -0.06985 0.06012  195 GLN A N   
3045 C CA  . GLN A 195 ? 0.63464 0.61437 0.82158 0.00725  -0.07012 0.05352  195 GLN A CA  
3046 C C   . GLN A 195 ? 0.58196 0.55283 0.75823 0.00414  -0.07598 0.05415  195 GLN A C   
3047 O O   . GLN A 195 ? 0.58584 0.54784 0.76163 -0.00204 -0.07827 0.06032  195 GLN A O   
3048 C CB  . GLN A 195 ? 0.63486 0.62152 0.83363 0.00283  -0.06160 0.04958  195 GLN A CB  
3049 C CG  . GLN A 195 ? 0.80962 0.80597 1.01792 0.00556  -0.05468 0.04702  195 GLN A CG  
3050 C CD  . GLN A 195 ? 0.78364 0.78837 1.00182 0.00165  -0.04602 0.04037  195 GLN A CD  
3051 O OE1 . GLN A 195 ? 0.69867 0.70826 0.91275 -0.00023 -0.04427 0.03312  195 GLN A OE1 
3052 N NE2 . GLN A 195 ? 0.90163 0.90812 1.13357 0.00064  -0.04043 0.04290  195 GLN A NE2 
3061 N N   . GLN A 196 ? 0.60970 0.58649 0.77345 0.00664  -0.07559 0.04528  196 GLN A N   
3062 C CA  . GLN A 196 ? 0.52554 0.49518 0.67764 0.00439  -0.08029 0.04453  196 GLN A CA  
3063 C C   . GLN A 196 ? 0.58091 0.56100 0.72777 0.00468  -0.07476 0.03409  196 GLN A C   
3064 O O   . GLN A 196 ? 0.54328 0.53245 0.68390 0.00954  -0.07208 0.02688  196 GLN A O   
3065 C CB  . GLN A 196 ? 0.65403 0.61655 0.79350 0.00859  -0.08782 0.04633  196 GLN A CB  
3066 C CG  . GLN A 196 ? 0.64153 0.59510 0.76792 0.00630  -0.09302 0.04586  196 GLN A CG  
3067 C CD  . GLN A 196 ? 0.89145 0.83428 1.02277 -0.00072 -0.09653 0.05396  196 GLN A CD  
3068 O OE1 . GLN A 196 ? 0.90814 0.84623 1.03856 -0.00432 -0.09754 0.05893  196 GLN A OE1 
3069 N NE2 . GLN A 196 ? 1.01156 0.95753 1.14369 -0.00511 -0.09319 0.05105  196 GLN A NE2 
3078 N N   . GLN A 197 ? 0.52423 0.50351 0.67466 -0.00051 -0.07313 0.03400  197 GLN A N   
3079 C CA  . GLN A 197 ? 0.54162 0.53007 0.68843 -0.00032 -0.06848 0.02535  197 GLN A CA  
3080 C C   . GLN A 197 ? 0.62052 0.60261 0.75170 0.00012  -0.07343 0.02435  197 GLN A C   
3081 O O   . GLN A 197 ? 0.61780 0.58826 0.74475 -0.00267 -0.07976 0.03099  197 GLN A O   
3082 C CB  . GLN A 197 ? 0.58996 0.58303 0.75199 -0.00585 -0.06345 0.02590  197 GLN A CB  
3083 C CG  . GLN A 197 ? 0.56920 0.57174 0.72979 -0.00570 -0.05913 0.01803  197 GLN A CG  
3084 C CD  . GLN A 197 ? 0.58880 0.59617 0.76680 -0.01132 -0.05470 0.01948  197 GLN A CD  
3085 O OE1 . GLN A 197 ? 0.60306 0.61734 0.79499 -0.01227 -0.04892 0.01766  197 GLN A OE1 
3086 N NE2 . GLN A 197 ? 0.58689 0.59106 0.76488 -0.01517 -0.05727 0.02293  197 GLN A NE2 
3095 N N   . THR A 198 ? 0.55374 0.54328 0.67607 0.00363  -0.07048 0.01618  198 THR A N   
3096 C CA  . THR A 198 ? 0.46699 0.45140 0.57443 0.00448  -0.07388 0.01445  198 THR A CA  
3097 C C   . THR A 198 ? 0.52609 0.52030 0.63340 0.00506  -0.06844 0.00768  198 THR A C   
3098 O O   . THR A 198 ? 0.49037 0.49572 0.60402 0.00697  -0.06260 0.00224  198 THR A O   
3099 C CB  . THR A 198 ? 0.72654 0.70722 0.81964 0.00981  -0.07730 0.01250  198 THR A CB  
3100 O OG1 . THR A 198 ? 0.75136 0.74370 0.84365 0.01429  -0.07191 0.00551  198 THR A OG1 
3101 C CG2 . THR A 198 ? 0.69406 0.66701 0.78957 0.01030  -0.08249 0.01908  198 THR A CG2 
3109 N N   . THR A 199 ? 0.50069 0.49076 0.60093 0.00345  -0.07061 0.00834  199 THR A N   
3110 C CA  . THR A 199 ? 0.50236 0.50073 0.60226 0.00437  -0.06635 0.00321  199 THR A CA  
3111 C C   . THR A 199 ? 0.57295 0.56693 0.65406 0.00854  -0.06842 0.00015  199 THR A C   
3112 O O   . THR A 199 ? 0.51873 0.50161 0.58881 0.00783  -0.07406 0.00358  199 THR A O   
3113 C CB  . THR A 199 ? 0.53830 0.53752 0.64875 -0.00113 -0.06635 0.00737  199 THR A CB  
3114 O OG1 . THR A 199 ? 0.56702 0.57065 0.69644 -0.00505 -0.06345 0.01011  199 THR A OG1 
3115 C CG2 . THR A 199 ? 0.58790 0.59613 0.69896 0.00044  -0.06245 0.00283  199 THR A CG2 
3123 N N   . LEU A 200 ? 0.49626 0.49863 0.57402 0.01274  -0.06379 -0.00614 200 LEU A N   
3124 C CA  . LEU A 200 ? 0.42483 0.42437 0.48625 0.01707  -0.06418 -0.00928 200 LEU A CA  
3125 C C   . LEU A 200 ? 0.46850 0.47481 0.53110 0.01795  -0.06047 -0.01190 200 LEU A C   
3126 O O   . LEU A 200 ? 0.42176 0.43820 0.49815 0.01684  -0.05629 -0.01359 200 LEU A O   
3127 C CB  . LEU A 200 ? 0.41060 0.41424 0.46718 0.02171  -0.06190 -0.01334 200 LEU A CB  
3128 C CG  . LEU A 200 ? 0.43760 0.43742 0.49591 0.02169  -0.06503 -0.01065 200 LEU A CG  
3129 C CD1 . LEU A 200 ? 0.48158 0.48949 0.53861 0.02594  -0.06176 -0.01455 200 LEU A CD1 
3130 C CD2 . LEU A 200 ? 0.60180 0.58780 0.64910 0.02128  -0.07176 -0.00658 200 LEU A CD2 
3142 N N   . LYS A 201 ? 0.42666 0.42735 0.47521 0.02019  -0.06198 -0.01215 201 LYS A N   
3143 C CA  . LYS A 201 ? 0.37809 0.38432 0.42706 0.02161  -0.05910 -0.01345 201 LYS A CA  
3144 C C   . LYS A 201 ? 0.45220 0.45628 0.48569 0.02718  -0.05741 -0.01667 201 LYS A C   
3145 O O   . LYS A 201 ? 0.44245 0.43805 0.46287 0.02901  -0.05970 -0.01699 201 LYS A O   
3146 C CB  . LYS A 201 ? 0.47459 0.47636 0.52394 0.01784  -0.06264 -0.00863 201 LYS A CB  
3147 C CG  . LYS A 201 ? 0.60882 0.61240 0.67475 0.01164  -0.06412 -0.00420 201 LYS A CG  
3148 C CD  . LYS A 201 ? 0.70488 0.72168 0.78990 0.01019  -0.05946 -0.00477 201 LYS A CD  
3149 C CE  . LYS A 201 ? 0.91468 0.93280 1.00655 0.00614  -0.06138 0.00054  201 LYS A CE  
3150 N NZ  . LYS A 201 ? 1.07125 1.08494 1.17271 -0.00065 -0.06471 0.00672  201 LYS A NZ  
3164 N N   . GLY A 202 ? 0.38538 0.39738 0.42171 0.02991  -0.05322 -0.01870 202 GLY A N   
3165 C CA  . GLY A 202 ? 0.41279 0.42214 0.43500 0.03509  -0.05128 -0.02053 202 GLY A CA  
3166 C C   . GLY A 202 ? 0.40089 0.41135 0.41851 0.03792  -0.04903 -0.02359 202 GLY A C   
3167 O O   . GLY A 202 ? 0.37848 0.39772 0.40672 0.03735  -0.04651 -0.02567 202 GLY A O   
3171 N N   . VAL A 203 ? 0.40711 0.40906 0.40919 0.04085  -0.04977 -0.02381 203 VAL A N   
3172 C CA  . VAL A 203 ? 0.37140 0.37563 0.36995 0.04364  -0.04713 -0.02601 203 VAL A CA  
3173 C C   . VAL A 203 ? 0.39420 0.40110 0.40065 0.04121  -0.04891 -0.02618 203 VAL A C   
3174 O O   . VAL A 203 ? 0.35953 0.37513 0.37167 0.04219  -0.04583 -0.02809 203 VAL A O   
3175 C CB  . VAL A 203 ? 0.52915 0.52309 0.51094 0.04679  -0.04758 -0.02580 203 VAL A CB  
3176 C CG1 . VAL A 203 ? 0.75517 0.73668 0.72847 0.04467  -0.05338 -0.02398 203 VAL A CG1 
3177 C CG2 . VAL A 203 ? 0.44628 0.44308 0.42677 0.04885  -0.04530 -0.02712 203 VAL A CG2 
3187 N N   A GLU A 204 ? 0.36575 0.36548 0.37292 0.03801  -0.05397 -0.02370 204 GLU A N   
3188 N N   B GLU A 204 ? 0.36461 0.36424 0.37168 0.03801  -0.05400 -0.02368 204 GLU A N   
3189 C CA  A GLU A 204 ? 0.38590 0.38762 0.40115 0.03614  -0.05586 -0.02289 204 GLU A CA  
3190 C CA  B GLU A 204 ? 0.39002 0.39137 0.40526 0.03599  -0.05606 -0.02275 204 GLU A CA  
3191 C C   A GLU A 204 ? 0.38797 0.40108 0.41914 0.03401  -0.05289 -0.02401 204 GLU A C   
3192 C C   B GLU A 204 ? 0.38829 0.40131 0.41937 0.03401  -0.05291 -0.02399 204 GLU A C   
3193 O O   A GLU A 204 ? 0.38616 0.40376 0.42456 0.03341  -0.05278 -0.02408 204 GLU A O   
3194 O O   B GLU A 204 ? 0.38779 0.40545 0.42592 0.03353  -0.05270 -0.02416 204 GLU A O   
3195 C CB  A GLU A 204 ? 0.45553 0.44610 0.46849 0.03309  -0.06225 -0.01901 204 GLU A CB  
3196 C CB  B GLU A 204 ? 0.45239 0.44268 0.46567 0.03271  -0.06240 -0.01879 204 GLU A CB  
3197 C CG  A GLU A 204 ? 0.53829 0.51757 0.53691 0.03506  -0.06586 -0.01839 204 GLU A CG  
3198 C CG  B GLU A 204 ? 0.63597 0.61433 0.63464 0.03443  -0.06635 -0.01798 204 GLU A CG  
3199 C CD  A GLU A 204 ? 0.70921 0.68006 0.69480 0.03555  -0.06682 -0.01847 204 GLU A CD  
3200 C CD  B GLU A 204 ? 0.59416 0.56232 0.59284 0.03110  -0.07327 -0.01376 204 GLU A CD  
3201 O OE1 A GLU A 204 ? 0.48942 0.46316 0.47820 0.03401  -0.06558 -0.01795 204 GLU A OE1 
3202 O OE1 B GLU A 204 ? 0.55630 0.52017 0.55637 0.02731  -0.07600 -0.01097 204 GLU A OE1 
3203 O OE2 A GLU A 204 ? 0.64325 0.60485 0.61602 0.03752  -0.06883 -0.01894 204 GLU A OE2 
3204 O OE2 B GLU A 204 ? 0.76320 0.72811 0.76144 0.03221  -0.07610 -0.01268 204 GLU A OE2 
3217 N N   . ALA A 205 ? 0.33486 0.35302 0.37231 0.03301  -0.05043 -0.02482 205 ALA A N   
3218 C CA  . ALA A 205 ? 0.32026 0.34939 0.37348 0.03102  -0.04715 -0.02662 205 ALA A CA  
3219 C C   . ALA A 205 ? 0.31582 0.35558 0.37090 0.03384  -0.04219 -0.03089 205 ALA A C   
3220 O O   . ALA A 205 ? 0.35446 0.40340 0.42139 0.03237  -0.03949 -0.03319 205 ALA A O   
3221 C CB  . ALA A 205 ? 0.41103 0.44273 0.47284 0.02879  -0.04645 -0.02566 205 ALA A CB  
3227 N N   . VAL A 206 ? 0.30818 0.34696 0.35215 0.03758  -0.04072 -0.03183 206 VAL A N   
3228 C CA  . VAL A 206 ? 0.30288 0.35188 0.34885 0.03976  -0.03609 -0.03502 206 VAL A CA  
3229 C C   . VAL A 206 ? 0.32979 0.37982 0.36933 0.04166  -0.03564 -0.03512 206 VAL A C   
3230 O O   . VAL A 206 ? 0.35127 0.41072 0.39301 0.04281  -0.03196 -0.03722 206 VAL A O   
3231 C CB  . VAL A 206 ? 0.29482 0.34496 0.33694 0.04250  -0.03344 -0.03540 206 VAL A CB  
3232 C CG1 . VAL A 206 ? 0.31277 0.36482 0.36451 0.04079  -0.03363 -0.03506 206 VAL A CG1 
3233 C CG2 . VAL A 206 ? 0.31777 0.35763 0.34433 0.04550  -0.03457 -0.03309 206 VAL A CG2 
3243 N N   . MET A 207 ? 0.34185 0.38325 0.37460 0.04185  -0.03936 -0.03265 207 MET A N   
3244 C CA  . MET A 207 ? 0.31192 0.35478 0.34018 0.04382  -0.03913 -0.03212 207 MET A CA  
3245 C C   . MET A 207 ? 0.40322 0.44726 0.43819 0.04229  -0.04211 -0.03073 207 MET A C   
3246 O O   . MET A 207 ? 0.37903 0.41561 0.41591 0.04024  -0.04613 -0.02863 207 MET A O   
3247 C CB  . MET A 207 ? 0.31442 0.34611 0.32922 0.04617  -0.04080 -0.03026 207 MET A CB  
3248 C CG  . MET A 207 ? 0.36934 0.40052 0.37686 0.04868  -0.03693 -0.03092 207 MET A CG  
3249 S SD  . MET A 207 ? 0.45182 0.46943 0.44337 0.05150  -0.03805 -0.02911 207 MET A SD  
3250 C CE  . MET A 207 ? 0.43120 0.45704 0.42532 0.05295  -0.03523 -0.02863 207 MET A CE  
3260 N N   . TYR A 208 ? 0.32349 0.37733 0.36259 0.04327  -0.04015 -0.03126 208 TYR A N   
3261 C CA  . TYR A 208 ? 0.29725 0.35308 0.34271 0.04282  -0.04289 -0.02919 208 TYR A CA  
3262 C C   . TYR A 208 ? 0.31818 0.38088 0.36270 0.04529  -0.04181 -0.02815 208 TYR A C   
3263 O O   . TYR A 208 ? 0.35173 0.42414 0.39628 0.04607  -0.03740 -0.02995 208 TYR A O   
3264 C CB  . TYR A 208 ? 0.29721 0.36221 0.35463 0.04064  -0.04114 -0.03083 208 TYR A CB  
3265 C CG  . TYR A 208 ? 0.31167 0.37734 0.37521 0.04076  -0.04422 -0.02762 208 TYR A CG  
3266 C CD1 . TYR A 208 ? 0.37964 0.43364 0.44369 0.03959  -0.04937 -0.02372 208 TYR A CD1 
3267 C CD2 . TYR A 208 ? 0.31115 0.38919 0.37990 0.04222  -0.04229 -0.02772 208 TYR A CD2 
3268 C CE1 . TYR A 208 ? 0.38662 0.44054 0.45668 0.04021  -0.05256 -0.01983 208 TYR A CE1 
3269 C CE2 . TYR A 208 ? 0.31807 0.39715 0.39313 0.04305  -0.04531 -0.02399 208 TYR A CE2 
3270 C CZ  . TYR A 208 ? 0.36265 0.42918 0.43847 0.04222  -0.05049 -0.01994 208 TYR A CZ  
3271 O OH  . TYR A 208 ? 0.40563 0.47229 0.48838 0.04341  -0.05391 -0.01528 208 TYR A OH  
3281 N N   . MET A 209 ? 0.31736 0.37531 0.36204 0.04638  -0.04601 -0.02472 209 MET A N   
3282 C CA  . MET A 209 ? 0.31544 0.38016 0.36157 0.04877  -0.04562 -0.02279 209 MET A CA  
3283 C C   . MET A 209 ? 0.47375 0.54659 0.53098 0.04899  -0.04750 -0.02041 209 MET A C   
3284 O O   . MET A 209 ? 0.35778 0.42253 0.41751 0.04880  -0.05246 -0.01745 209 MET A O   
3285 C CB  . MET A 209 ? 0.32457 0.37710 0.36253 0.05047  -0.04908 -0.02056 209 MET A CB  
3286 C CG  . MET A 209 ? 0.51390 0.57225 0.55660 0.05285  -0.05009 -0.01752 209 MET A CG  
3287 S SD  . MET A 209 ? 0.50511 0.58018 0.55080 0.05379  -0.04317 -0.01822 209 MET A SD  
3288 C CE  . MET A 209 ? 0.67166 0.73704 0.70406 0.05413  -0.03975 -0.02019 209 MET A CE  
3298 N N   . GLY A 210 ? 0.33025 0.41914 0.39421 0.04941  -0.04363 -0.02123 210 GLY A N   
3299 C CA  . GLY A 210 ? 0.32797 0.42630 0.40250 0.05033  -0.04503 -0.01852 210 GLY A CA  
3300 C C   . GLY A 210 ? 0.35979 0.47517 0.44086 0.04943  -0.04015 -0.02115 210 GLY A C   
3301 O O   . GLY A 210 ? 0.38172 0.50946 0.47079 0.05081  -0.03993 -0.01883 210 GLY A O   
3305 N N   . THR A 211 ? 0.32024 0.43680 0.39852 0.04717  -0.03644 -0.02591 211 THR A N   
3306 C CA  . THR A 211 ? 0.32660 0.45889 0.40972 0.04595  -0.03170 -0.02927 211 THR A CA  
3307 C C   . THR A 211 ? 0.33618 0.46883 0.41328 0.04449  -0.02789 -0.03331 211 THR A C   
3308 O O   . THR A 211 ? 0.29007 0.41066 0.36141 0.04399  -0.02871 -0.03442 211 THR A O   
3309 C CB  . THR A 211 ? 0.41755 0.55287 0.50821 0.04444  -0.03123 -0.03123 211 THR A CB  
3310 O OG1 . THR A 211 ? 0.36871 0.52006 0.46315 0.04328  -0.02655 -0.03502 211 THR A OG1 
3311 C CG2 . THR A 211 ? 0.43244 0.55578 0.52142 0.04224  -0.03166 -0.03373 211 THR A CG2 
3319 N N   . LEU A 212 ? 0.27640 0.42343 0.35526 0.04389  -0.02392 -0.03491 212 LEU A N   
3320 C CA  . LEU A 212 ? 0.28667 0.43567 0.36122 0.04255  -0.02030 -0.03820 212 LEU A CA  
3321 C C   . LEU A 212 ? 0.31900 0.47101 0.39750 0.04025  -0.01830 -0.04364 212 LEU A C   
3322 O O   . LEU A 212 ? 0.31259 0.46295 0.38835 0.03937  -0.01627 -0.04641 212 LEU A O   
3323 C CB  . LEU A 212 ? 0.32701 0.49009 0.40198 0.04236  -0.01702 -0.03688 212 LEU A CB  
3324 C CG  . LEU A 212 ? 0.31363 0.47596 0.38639 0.04429  -0.01776 -0.03142 212 LEU A CG  
3325 C CD1 . LEU A 212 ? 0.26912 0.44760 0.34472 0.04320  -0.01406 -0.02970 212 LEU A CD1 
3326 C CD2 . LEU A 212 ? 0.28514 0.43169 0.34883 0.04549  -0.01841 -0.03049 212 LEU A CD2 
3338 N N   . SER A 213 ? 0.34463 0.50110 0.43027 0.03945  -0.01869 -0.04498 213 SER A N   
3339 C CA  . SER A 213 ? 0.32098 0.48300 0.41194 0.03707  -0.01593 -0.05061 213 SER A CA  
3340 C C   . SER A 213 ? 0.31023 0.45978 0.40365 0.03603  -0.01738 -0.05194 213 SER A C   
3341 O O   . SER A 213 ? 0.31721 0.45966 0.41361 0.03634  -0.02017 -0.04909 213 SER A O   
3342 C CB  . SER A 213 ? 0.38071 0.55502 0.47849 0.03676  -0.01479 -0.05132 213 SER A CB  
3343 O OG  . SER A 213 ? 0.35056 0.52854 0.45361 0.03442  -0.01201 -0.05714 213 SER A OG  
3349 N N   . TYR A 214 ? 0.30275 0.45041 0.39618 0.03467  -0.01551 -0.05573 214 TYR A N   
3350 C CA  . TYR A 214 ? 0.35956 0.49789 0.45782 0.03320  -0.01638 -0.05686 214 TYR A CA  
3351 C C   . TYR A 214 ? 0.38928 0.53230 0.49754 0.03119  -0.01474 -0.05960 214 TYR A C   
3352 O O   . TYR A 214 ? 0.34305 0.47787 0.45636 0.03020  -0.01644 -0.05754 214 TYR A O   
3353 C CB  . TYR A 214 ? 0.33268 0.47025 0.43073 0.03261  -0.01459 -0.05999 214 TYR A CB  
3354 C CG  . TYR A 214 ? 0.33149 0.45923 0.43397 0.03153  -0.01590 -0.05966 214 TYR A CG  
3355 C CD1 . TYR A 214 ? 0.32373 0.44006 0.42493 0.03152  -0.01955 -0.05509 214 TYR A CD1 
3356 C CD2 . TYR A 214 ? 0.33475 0.46528 0.44335 0.03043  -0.01369 -0.06348 214 TYR A CD2 
3357 C CE1 . TYR A 214 ? 0.33652 0.44520 0.44226 0.03005  -0.02073 -0.05413 214 TYR A CE1 
3358 C CE2 . TYR A 214 ? 0.38388 0.50738 0.49832 0.02937  -0.01476 -0.06256 214 TYR A CE2 
3359 C CZ  . TYR A 214 ? 0.32999 0.44279 0.44278 0.02901  -0.01820 -0.05772 214 TYR A CZ  
3360 O OH  . TYR A 214 ? 0.37208 0.47892 0.49121 0.02747  -0.01932 -0.05611 214 TYR A OH  
3370 N N   . GLU A 215 ? 0.33357 0.48973 0.44482 0.03037  -0.01129 -0.06400 215 GLU A N   
3371 C CA  . GLU A 215 ? 0.35160 0.51239 0.47187 0.02867  -0.00911 -0.06692 215 GLU A CA  
3372 C C   . GLU A 215 ? 0.36180 0.51908 0.48361 0.03008  -0.01165 -0.06143 215 GLU A C   
3373 O O   . GLU A 215 ? 0.41688 0.56919 0.54620 0.02888  -0.01153 -0.06066 215 GLU A O   
3374 C CB  . GLU A 215 ? 0.47386 0.64992 0.59518 0.02769  -0.00517 -0.07264 215 GLU A CB  
3375 C CG  . GLU A 215 ? 0.88227 1.06142 1.00962 0.02508  -0.00178 -0.07986 215 GLU A CG  
3376 C CD  . GLU A 215 ? 0.75782 0.93071 0.89595 0.02314  -0.00062 -0.08145 215 GLU A CD  
3377 O OE1 . GLU A 215 ? 0.90601 1.07688 1.04777 0.02330  -0.00085 -0.07877 215 GLU A OE1 
3378 O OE2 . GLU A 215 ? 0.94996 1.12027 1.09404 0.02147  0.00061  -0.08482 215 GLU A OE2 
3385 N N   . GLN A 216 ? 0.35275 0.51252 0.46873 0.03264  -0.01398 -0.05698 216 GLN A N   
3386 C CA  . GLN A 216 ? 0.36907 0.52572 0.48762 0.03452  -0.01698 -0.05112 216 GLN A CA  
3387 C C   . GLN A 216 ? 0.36427 0.50423 0.48312 0.03432  -0.02107 -0.04645 216 GLN A C   
3388 O O   . GLN A 216 ? 0.38657 0.52147 0.51129 0.03440  -0.02275 -0.04266 216 GLN A O   
3389 C CB  . GLN A 216 ? 0.38271 0.54629 0.49661 0.03737  -0.01875 -0.04710 216 GLN A CB  
3390 C CG  . GLN A 216 ? 0.52292 0.68735 0.64179 0.03985  -0.02152 -0.04119 216 GLN A CG  
3391 C CD  . GLN A 216 ? 0.62981 0.80344 0.75661 0.03937  -0.01838 -0.04330 216 GLN A CD  
3392 O OE1 . GLN A 216 ? 0.57728 0.76585 0.70463 0.03898  -0.01474 -0.04717 216 GLN A OE1 
3393 N NE2 . GLN A 216 ? 0.63390 0.79847 0.76681 0.03927  -0.01969 -0.04044 216 GLN A NE2 
3402 N N   . PHE A 217 ? 0.32838 0.45967 0.44085 0.03405  -0.02278 -0.04616 217 PHE A N   
3403 C CA  . PHE A 217 ? 0.31499 0.43093 0.42684 0.03331  -0.02671 -0.04203 217 PHE A CA  
3404 C C   . PHE A 217 ? 0.34037 0.45273 0.46202 0.03010  -0.02505 -0.04335 217 PHE A C   
3405 O O   . PHE A 217 ? 0.37596 0.47834 0.50138 0.02908  -0.02803 -0.03842 217 PHE A O   
3406 C CB  . PHE A 217 ? 0.29755 0.40748 0.40033 0.03376  -0.02778 -0.04250 217 PHE A CB  
3407 C CG  . PHE A 217 ? 0.31560 0.41032 0.41443 0.03345  -0.03243 -0.03793 217 PHE A CG  
3408 C CD1 . PHE A 217 ? 0.39096 0.47821 0.48759 0.03482  -0.03713 -0.03229 217 PHE A CD1 
3409 C CD2 . PHE A 217 ? 0.40263 0.49116 0.49962 0.03196  -0.03230 -0.03917 217 PHE A CD2 
3410 C CE1 . PHE A 217 ? 0.46147 0.53456 0.55335 0.03417  -0.04170 -0.02839 217 PHE A CE1 
3411 C CE2 . PHE A 217 ? 0.37311 0.44847 0.46556 0.03141  -0.03659 -0.03504 217 PHE A CE2 
3412 C CZ  . PHE A 217 ? 0.44388 0.51121 0.53323 0.03229  -0.04132 -0.02988 217 PHE A CZ  
3422 N N   . LYS A 218 ? 0.37437 0.49502 0.50124 0.02825  -0.02025 -0.04968 218 LYS A N   
3423 C CA  . LYS A 218 ? 0.38024 0.49892 0.51861 0.02501  -0.01783 -0.05128 218 LYS A CA  
3424 C C   . LYS A 218 ? 0.44840 0.56977 0.59428 0.02489  -0.01654 -0.04960 218 LYS A C   
3425 O O   . LYS A 218 ? 0.44666 0.56145 0.60162 0.02257  -0.01629 -0.04691 218 LYS A O   
3426 C CB  . LYS A 218 ? 0.40481 0.53210 0.54762 0.02329  -0.01307 -0.05894 218 LYS A CB  
3427 C CG  . LYS A 218 ? 0.37367 0.49797 0.51224 0.02333  -0.01389 -0.06012 218 LYS A CG  
3428 C CD  . LYS A 218 ? 0.38972 0.52463 0.53239 0.02245  -0.00949 -0.06761 218 LYS A CD  
3429 C CE  . LYS A 218 ? 0.44473 0.57709 0.58615 0.02270  -0.01004 -0.06833 218 LYS A CE  
3430 N NZ  . LYS A 218 ? 0.46937 0.61207 0.61525 0.02214  -0.00631 -0.07518 218 LYS A NZ  
3444 N N   . LYS A 219 ? 0.41469 0.54616 0.55767 0.02731  -0.01548 -0.05064 219 LYS A N   
3445 C CA  . LYS A 219 ? 0.42936 0.56437 0.57919 0.02794  -0.01412 -0.04867 219 LYS A CA  
3446 C C   . LYS A 219 ? 0.50143 0.62623 0.65130 0.02978  -0.01942 -0.03949 219 LYS A C   
3447 O O   . LYS A 219 ? 0.52080 0.64061 0.67896 0.02903  -0.01928 -0.03553 219 LYS A O   
3448 C CB  . LYS A 219 ? 0.47774 0.62831 0.62459 0.03008  -0.01156 -0.05216 219 LYS A CB  
3449 C CG  . LYS A 219 ? 0.54054 0.70210 0.68961 0.02787  -0.00588 -0.06128 219 LYS A CG  
3450 C CD  . LYS A 219 ? 0.81713 0.99424 0.96464 0.02958  -0.00342 -0.06358 219 LYS A CD  
3451 C CE  . LYS A 219 ? 0.82750 1.01669 0.97343 0.02752  0.00106  -0.07261 219 LYS A CE  
3452 N NZ  . LYS A 219 ? 1.13317 1.31731 1.27822 0.02523  0.00145  -0.07676 219 LYS A NZ  
3466 N N   . GLY A 220 ? 0.43796 0.55940 0.57912 0.03219  -0.02403 -0.03588 220 GLY A N   
3467 C CA  . GLY A 220 ? 0.52625 0.63876 0.66700 0.03434  -0.02966 -0.02747 220 GLY A CA  
3468 C C   . GLY A 220 ? 0.49554 0.61473 0.63028 0.03834  -0.03220 -0.02531 220 GLY A C   
3469 O O   . GLY A 220 ? 0.47542 0.60911 0.61095 0.03997  -0.02915 -0.02804 220 GLY A O   
3473 N N   . VAL A 221 ? 0.44532 0.55451 0.57457 0.03971  -0.03771 -0.02037 221 VAL A N   
3474 C CA  . VAL A 221 ? 0.46916 0.58312 0.59472 0.04350  -0.04065 -0.01718 221 VAL A CA  
3475 C C   . VAL A 221 ? 0.62189 0.72683 0.75178 0.04564  -0.04657 -0.00872 221 VAL A C   
3476 O O   . VAL A 221 ? 0.53915 0.62948 0.66932 0.04370  -0.04994 -0.00527 221 VAL A O   
3477 C CB  . VAL A 221 ? 0.49143 0.60164 0.60644 0.04357  -0.04178 -0.01917 221 VAL A CB  
3478 C CG1 . VAL A 221 ? 0.56133 0.68013 0.67284 0.04170  -0.03624 -0.02659 221 VAL A CG1 
3479 C CG2 . VAL A 221 ? 0.49848 0.59093 0.60867 0.04194  -0.04611 -0.01663 221 VAL A CG2 
3489 N N   . ASP A 222 ? 0.48698 0.60126 0.62115 0.04955  -0.04797 -0.00488 222 ASP A N   
3490 C CA  . ASP A 222 ? 0.58707 0.69410 0.72660 0.05239  -0.05405 0.00376  222 ASP A CA  
3491 C C   . ASP A 222 ? 0.64990 0.74706 0.78244 0.05347  -0.05961 0.00632  222 ASP A C   
3492 O O   . ASP A 222 ? 0.57344 0.67768 0.70116 0.05479  -0.05865 0.00376  222 ASP A O   
3493 C CB  . ASP A 222 ? 0.58339 0.70574 0.73182 0.05663  -0.05342 0.00726  222 ASP A CB  
3494 C CG  . ASP A 222 ? 0.88677 1.01850 1.04145 0.05574  -0.04777 0.00455  222 ASP A CG  
3495 O OD1 . ASP A 222 ? 0.75975 0.88199 0.91567 0.05245  -0.04618 0.00336  222 ASP A OD1 
3496 O OD2 . ASP A 222 ? 1.10830 1.25651 1.26636 0.05782  -0.04449 0.00398  222 ASP A OD2 
3501 N N   . ILE A 223 ? 0.48782 0.56836 0.61985 0.05257  -0.06523 0.01144  223 ILE A N   
3502 C CA  . ILE A 223 ? 0.42758 0.49720 0.55302 0.05359  -0.07116 0.01410  223 ILE A CA  
3503 C C   . ILE A 223 ? 0.57214 0.63100 0.69633 0.05321  -0.07307 0.02220  223 ILE A C   
3504 O O   . ILE A 223 ? 0.54401 0.60002 0.67242 0.05184  -0.07142 0.02566  223 ILE A O   
3505 C CB  . ILE A 223 ? 0.58746 0.64326 0.70203 0.04945  -0.07169 0.01056  223 ILE A CB  
3506 C CG1 . ILE A 223 ? 0.58441 0.62748 0.70242 0.04591  -0.07400 0.01441  223 ILE A CG1 
3507 C CG2 . ILE A 223 ? 0.71335 0.77775 0.82215 0.04759  -0.06486 0.00225  223 ILE A CG2 
3508 C CD1 . ILE A 223 ? 0.59938 0.63067 0.70837 0.04160  -0.07447 0.01164  223 ILE A CD1 
3520 N N   . PRO A 224 ? 0.69375 0.74595 0.81037 0.05374  -0.07501 0.02452  224 PRO A N   
3521 C CA  . PRO A 224 ? 0.61615 0.65743 0.72908 0.05242  -0.07541 0.03034  224 PRO A CA  
3522 C C   . PRO A 224 ? 0.52310 0.54722 0.63437 0.04821  -0.07950 0.03266  224 PRO A C   
3523 O O   . PRO A 224 ? 0.56943 0.58581 0.67762 0.04671  -0.08384 0.03036  224 PRO A O   
3524 C CB  . PRO A 224 ? 0.64449 0.68435 0.75140 0.05387  -0.07651 0.03054  224 PRO A CB  
3525 C CG  . PRO A 224 ? 0.77762 0.82802 0.88513 0.05601  -0.07626 0.02559  224 PRO A CG  
3526 C CD  . PRO A 224 ? 0.75076 0.80442 0.86230 0.05534  -0.07689 0.02120  224 PRO A CD  
3534 N N   . CYS A 225 ? 0.48446 0.50312 0.59751 0.04615  -0.07790 0.03718  225 CYS A N   
3535 C CA  . CYS A 225 ? 0.40523 0.40794 0.51640 0.04118  -0.08111 0.04056  225 CYS A CA  
3536 C C   . CYS A 225 ? 0.47461 0.46872 0.57899 0.04000  -0.08277 0.04304  225 CYS A C   
3537 O O   . CYS A 225 ? 0.47432 0.47474 0.57739 0.04297  -0.08022 0.04338  225 CYS A O   
3538 C CB  . CYS A 225 ? 0.44392 0.44548 0.56199 0.03869  -0.07821 0.04400  225 CYS A CB  
3539 S SG  . CYS A 225 ? 0.49632 0.48079 0.61404 0.03128  -0.08154 0.04825  225 CYS A SG  
3544 N N   . THR A 226 ? 0.54889 0.52929 0.64951 0.03542  -0.08703 0.04464  226 THR A N   
3545 C CA  . THR A 226 ? 0.53992 0.51255 0.63519 0.03380  -0.08907 0.04634  226 THR A CA  
3546 C C   . THR A 226 ? 0.59643 0.57155 0.69444 0.03358  -0.08506 0.04969  226 THR A C   
3547 O O   . THR A 226 ? 0.56800 0.54261 0.66331 0.03455  -0.08497 0.05023  226 THR A O   
3548 C CB  . THR A 226 ? 0.63763 0.59633 0.72867 0.02834  -0.09438 0.04740  226 THR A CB  
3549 O OG1 . THR A 226 ? 0.92268 0.87514 1.01031 0.02634  -0.09609 0.04914  226 THR A OG1 
3550 C CG2 . THR A 226 ? 0.64884 0.60450 0.74526 0.02373  -0.09348 0.05027  226 THR A CG2 
3558 N N   . CYS A 227 ? 0.52320 0.50116 0.62678 0.03250  -0.08174 0.05174  227 CYS A N   
3559 C CA  . CYS A 227 ? 0.50302 0.48269 0.61032 0.03194  -0.07904 0.05491  227 CYS A CA  
3560 C C   . CYS A 227 ? 0.44670 0.43745 0.55642 0.03698  -0.07643 0.05414  227 CYS A C   
3561 O O   . CYS A 227 ? 0.50782 0.49929 0.62411 0.03569  -0.07657 0.05751  227 CYS A O   
3562 C CB  . CYS A 227 ? 0.46933 0.44850 0.58267 0.02904  -0.07649 0.05744  227 CYS A CB  
3563 S SG  . CYS A 227 ? 0.44651 0.43795 0.56441 0.03387  -0.07184 0.05520  227 CYS A SG  
3568 N N   . GLY A 228 ? 0.40373 0.40410 0.50906 0.04228  -0.07412 0.05001  228 GLY A N   
3569 C CA  . GLY A 228 ? 0.39197 0.40468 0.49955 0.04683  -0.07165 0.04896  228 GLY A CA  
3570 C C   . GLY A 228 ? 0.37879 0.40409 0.48830 0.05041  -0.06709 0.04689  228 GLY A C   
3571 O O   . GLY A 228 ? 0.36684 0.40484 0.47658 0.05450  -0.06496 0.04451  228 GLY A O   
3575 N N   . ARG A 229 ? 0.38433 0.40653 0.49825 0.04804  -0.06651 0.04810  229 ARG A N   
3576 C CA  . ARG A 229 ? 0.38296 0.41658 0.50298 0.05031  -0.06366 0.04622  229 ARG A CA  
3577 C C   . ARG A 229 ? 0.48263 0.52360 0.60518 0.05135  -0.06499 0.04195  229 ARG A C   
3578 O O   . ARG A 229 ? 0.43083 0.46533 0.55019 0.04985  -0.06864 0.04091  229 ARG A O   
3579 C CB  . ARG A 229 ? 0.47699 0.50428 0.60329 0.04679  -0.06277 0.04907  229 ARG A CB  
3580 C CG  . ARG A 229 ? 0.47619 0.49802 0.60124 0.04552  -0.06081 0.05303  229 ARG A CG  
3581 C CD  . ARG A 229 ? 0.49550 0.51156 0.62807 0.04140  -0.05951 0.05620  229 ARG A CD  
3582 N NE  . ARG A 229 ? 0.50543 0.53154 0.64639 0.04360  -0.05673 0.05435  229 ARG A NE  
3583 C CZ  . ARG A 229 ? 0.65281 0.68958 0.79545 0.04764  -0.05328 0.05338  229 ARG A CZ  
3584 N NH1 . ARG A 229 ? 0.51229 0.55030 0.64854 0.04996  -0.05240 0.05420  229 ARG A NH1 
3585 N NH2 . ARG A 229 ? 0.62057 0.66740 0.77211 0.04925  -0.05058 0.05105  229 ARG A NH2 
3599 N N   . ARG A 230 ? 0.43491 0.48960 0.56370 0.05359  -0.06207 0.03900  230 ARG A N   
3600 C CA  . ARG A 230 ? 0.50554 0.56949 0.63855 0.05408  -0.06261 0.03389  230 ARG A CA  
3601 C C   . ARG A 230 ? 0.52931 0.58838 0.67068 0.05093  -0.06322 0.03323  230 ARG A C   
3602 O O   . ARG A 230 ? 0.57279 0.63674 0.72128 0.05104  -0.05971 0.03382  230 ARG A O   
3603 C CB  . ARG A 230 ? 0.60369 0.68810 0.73905 0.05781  -0.05851 0.03002  230 ARG A CB  
3604 C CG  . ARG A 230 ? 0.70479 0.79456 0.83282 0.06077  -0.05770 0.03045  230 ARG A CG  
3605 C CD  . ARG A 230 ? 0.74006 0.82794 0.86409 0.06043  -0.06016 0.02936  230 ARG A CD  
3606 N NE  . ARG A 230 ? 1.06453 1.15852 1.18340 0.06315  -0.05875 0.02959  230 ARG A NE  
3607 C CZ  . ARG A 230 ? 0.95219 1.03987 1.06627 0.06422  -0.05880 0.03206  230 ARG A CZ  
3608 N NH1 . ARG A 230 ? 0.77480 0.84968 0.88782 0.06249  -0.05982 0.03557  230 ARG A NH1 
3609 N NH2 . ARG A 230 ? 0.50371 0.59801 0.61453 0.06671  -0.05775 0.03061  230 ARG A NH2 
3623 N N   . ALA A 231 ? 0.48914 0.53894 0.62996 0.04827  -0.06734 0.03195  231 ALA A N   
3624 C CA  . ALA A 231 ? 0.61722 0.66307 0.76654 0.04518  -0.06798 0.03068  231 ALA A CA  
3625 C C   . ALA A 231 ? 0.71339 0.77405 0.86624 0.04595  -0.06439 0.02168  231 ALA A C   
3626 O O   . ALA A 231 ? 0.54490 0.61633 0.69280 0.04854  -0.06313 0.01731  231 ALA A O   
3627 C CB  . ALA A 231 ? 0.51752 0.54656 0.66145 0.04147  -0.07346 0.03297  231 ALA A CB  
3633 N N   . THR A 232 ? 0.52931 0.58861 0.68450 0.04155  -0.05948 0.01794  232 THR A N   
3634 C CA  . THR A 232 ? 0.48504 0.55471 0.63653 0.03964  -0.05275 0.00802  232 THR A CA  
3635 C C   . THR A 232 ? 0.49790 0.55772 0.64280 0.03534  -0.05339 0.00510  232 THR A C   
3636 O O   . THR A 232 ? 0.47494 0.52373 0.62407 0.03160  -0.05471 0.00890  232 THR A O   
3637 C CB  . THR A 232 ? 0.58079 0.65858 0.74161 0.03825  -0.04603 0.00516  232 THR A CB  
3638 O OG1 . THR A 232 ? 0.65569 0.74397 0.82197 0.04266  -0.04523 0.00782  232 THR A OG1 
3639 C CG2 . THR A 232 ? 0.61886 0.70660 0.77620 0.03601  -0.03965 -0.00528 232 THR A CG2 
3647 N N   . LYS A 233 ? 0.43417 0.49825 0.56936 0.03590  -0.05246 -0.00085 233 LYS A N   
3648 C CA  . LYS A 233 ? 0.46074 0.51810 0.58937 0.03260  -0.05227 -0.00432 233 LYS A CA  
3649 C C   . LYS A 233 ? 0.43089 0.49952 0.56079 0.03113  -0.04527 -0.01271 233 LYS A C   
3650 O O   . LYS A 233 ? 0.43579 0.51690 0.56372 0.03354  -0.04209 -0.01713 233 LYS A O   
3651 C CB  . LYS A 233 ? 0.46451 0.51696 0.58096 0.03461  -0.05639 -0.00434 233 LYS A CB  
3652 C CG  . LYS A 233 ? 0.56715 0.61561 0.67563 0.03226  -0.05520 -0.00880 233 LYS A CG  
3653 C CD  . LYS A 233 ? 0.60895 0.65237 0.70513 0.03461  -0.05864 -0.00882 233 LYS A CD  
3654 C CE  . LYS A 233 ? 0.62424 0.65168 0.71616 0.03332  -0.06544 -0.00308 233 LYS A CE  
3655 N NZ  . LYS A 233 ? 0.60453 0.62642 0.68433 0.03568  -0.06859 -0.00356 233 LYS A NZ  
3669 N N   . TYR A 234 ? 0.41348 0.47843 0.54768 0.02705  -0.04301 -0.01455 234 TYR A N   
3670 C CA  . TYR A 234 ? 0.41681 0.49201 0.55355 0.02568  -0.03679 -0.02245 234 TYR A CA  
3671 C C   . TYR A 234 ? 0.44461 0.51399 0.58108 0.02238  -0.03664 -0.02389 234 TYR A C   
3672 O O   . TYR A 234 ? 0.43170 0.48974 0.56876 0.02007  -0.04046 -0.01855 234 TYR A O   
3673 C CB  . TYR A 234 ? 0.47155 0.55434 0.62019 0.02450  -0.03180 -0.02432 234 TYR A CB  
3674 C CG  . TYR A 234 ? 0.46187 0.53646 0.62182 0.02049  -0.03139 -0.02016 234 TYR A CG  
3675 C CD1 . TYR A 234 ? 0.48691 0.56110 0.65335 0.01648  -0.02829 -0.02333 234 TYR A CD1 
3676 C CD2 . TYR A 234 ? 0.45403 0.52145 0.61944 0.02067  -0.03419 -0.01222 234 TYR A CD2 
3677 C CE1 . TYR A 234 ? 0.49147 0.55899 0.67010 0.01228  -0.02752 -0.01881 234 TYR A CE1 
3678 C CE2 . TYR A 234 ? 0.51246 0.57204 0.68905 0.01655  -0.03358 -0.00736 234 TYR A CE2 
3679 C CZ  . TYR A 234 ? 0.55116 0.61106 0.73453 0.01213  -0.03006 -0.01070 234 TYR A CZ  
3680 O OH  . TYR A 234 ? 0.59261 0.64553 0.78892 0.00750  -0.02906 -0.00519 234 TYR A OH  
3690 N N   . LEU A 235 ? 0.39023 0.46820 0.52596 0.02226  -0.03238 -0.03084 235 LEU A N   
3691 C CA  . LEU A 235 ? 0.35217 0.42735 0.48825 0.02005  -0.03185 -0.03259 235 LEU A CA  
3692 C C   . LEU A 235 ? 0.39979 0.47559 0.55107 0.01574  -0.02869 -0.03281 235 LEU A C   
3693 O O   . LEU A 235 ? 0.42901 0.51393 0.58900 0.01502  -0.02364 -0.03762 235 LEU A O   
3694 C CB  . LEU A 235 ? 0.37307 0.45746 0.50351 0.02209  -0.02871 -0.03918 235 LEU A CB  
3695 C CG  . LEU A 235 ? 0.34851 0.43186 0.47950 0.02091  -0.02795 -0.04106 235 LEU A CG  
3696 C CD1 . LEU A 235 ? 0.34784 0.41939 0.47051 0.02099  -0.03293 -0.03586 235 LEU A CD1 
3697 C CD2 . LEU A 235 ? 0.29707 0.38951 0.42249 0.02345  -0.02503 -0.04666 235 LEU A CD2 
3709 N N   . VAL A 236 ? 0.42017 0.48673 0.57506 0.01265  -0.03148 -0.02763 236 VAL A N   
3710 C CA  . VAL A 236 ? 0.42239 0.48953 0.59361 0.00798  -0.02848 -0.02666 236 VAL A CA  
3711 C C   . VAL A 236 ? 0.46097 0.53466 0.63718 0.00692  -0.02546 -0.03157 236 VAL A C   
3712 O O   . VAL A 236 ? 0.43302 0.51447 0.62277 0.00488  -0.02039 -0.03570 236 VAL A O   
3713 C CB  . VAL A 236 ? 0.45922 0.51410 0.63378 0.00448  -0.03303 -0.01748 236 VAL A CB  
3714 C CG1 . VAL A 236 ? 0.48133 0.53757 0.67428 -0.00092 -0.02963 -0.01570 236 VAL A CG1 
3715 C CG2 . VAL A 236 ? 0.41123 0.45974 0.58380 0.00558  -0.03597 -0.01192 236 VAL A CG2 
3725 N N   . GLN A 237 ? 0.39557 0.46617 0.56151 0.00850  -0.02853 -0.03101 237 GLN A N   
3726 C CA  . GLN A 237 ? 0.34863 0.42460 0.51975 0.00794  -0.02653 -0.03395 237 GLN A CA  
3727 C C   . GLN A 237 ? 0.41055 0.48485 0.56544 0.01203  -0.02900 -0.03505 237 GLN A C   
3728 O O   . GLN A 237 ? 0.36812 0.43339 0.50995 0.01342  -0.03352 -0.03111 237 GLN A O   
3729 C CB  . GLN A 237 ? 0.42311 0.49500 0.60604 0.00329  -0.02775 -0.02829 237 GLN A CB  
3730 C CG  . GLN A 237 ? 0.62755 0.70542 0.81642 0.00321  -0.02643 -0.03005 237 GLN A CG  
3731 C CD  . GLN A 237 ? 0.94549 1.02303 1.15112 -0.00208 -0.02642 -0.02462 237 GLN A CD  
3732 O OE1 . GLN A 237 ? 0.77303 0.84191 0.97898 -0.00543 -0.02973 -0.01755 237 GLN A OE1 
3733 N NE2 . GLN A 237 ? 1.16172 1.24907 1.38228 -0.00300 -0.02289 -0.02736 237 GLN A NE2 
3742 N N   . GLN A 238 ? 0.36687 0.44952 0.52328 0.01392  -0.02597 -0.04017 238 GLN A N   
3743 C CA  . GLN A 238 ? 0.31541 0.39718 0.45783 0.01800  -0.02730 -0.04112 238 GLN A CA  
3744 C C   . GLN A 238 ? 0.38345 0.47066 0.53384 0.01818  -0.02562 -0.04233 238 GLN A C   
3745 O O   . GLN A 238 ? 0.39352 0.49002 0.55769 0.01709  -0.02182 -0.04642 238 GLN A O   
3746 C CB  . GLN A 238 ? 0.34153 0.42900 0.47542 0.02139  -0.02526 -0.04580 238 GLN A CB  
3747 C CG  . GLN A 238 ? 0.30892 0.39414 0.42796 0.02549  -0.02644 -0.04561 238 GLN A CG  
3748 C CD  . GLN A 238 ? 0.33582 0.40976 0.44085 0.02672  -0.03090 -0.04090 238 GLN A CD  
3749 O OE1 . GLN A 238 ? 0.34086 0.41035 0.44537 0.02544  -0.03309 -0.03852 238 GLN A OE1 
3750 N NE2 . GLN A 238 ? 0.30116 0.37025 0.39518 0.02940  -0.03224 -0.03944 238 GLN A NE2 
3759 N N   . GLU A 239 ? 0.32286 0.40454 0.46499 0.01976  -0.02847 -0.03878 239 GLU A N   
3760 C CA  . GLU A 239 ? 0.30315 0.39015 0.45143 0.02112  -0.02732 -0.03900 239 GLU A CA  
3761 C C   . GLU A 239 ? 0.31572 0.39835 0.44618 0.02603  -0.02873 -0.03840 239 GLU A C   
3762 O O   . GLU A 239 ? 0.31527 0.38877 0.43459 0.02654  -0.03220 -0.03420 239 GLU A O   
3763 C CB  . GLU A 239 ? 0.38054 0.46586 0.53950 0.01762  -0.02917 -0.03379 239 GLU A CB  
3764 C CG  . GLU A 239 ? 0.65357 0.74155 0.83054 0.01216  -0.02777 -0.03279 239 GLU A CG  
3765 C CD  . GLU A 239 ? 0.77028 0.87059 0.96700 0.01125  -0.02305 -0.03723 239 GLU A CD  
3766 O OE1 . GLU A 239 ? 0.75649 0.86322 0.95655 0.01411  -0.02206 -0.03871 239 GLU A OE1 
3767 O OE2 . GLU A 239 ? 0.87747 0.98085 1.08640 0.00792  -0.02029 -0.03925 239 GLU A OE2 
3774 N N   . SER A 240 ? 0.30408 0.39271 0.43164 0.02940  -0.02599 -0.04237 240 SER A N   
3775 C CA  . SER A 240 ? 0.27560 0.36059 0.38779 0.03408  -0.02640 -0.04144 240 SER A CA  
3776 C C   . SER A 240 ? 0.26967 0.36393 0.38531 0.03662  -0.02284 -0.04544 240 SER A C   
3777 O O   . SER A 240 ? 0.29960 0.40187 0.42565 0.03465  -0.02048 -0.04971 240 SER A O   
3778 C CB  . SER A 240 ? 0.35641 0.43264 0.45167 0.03508  -0.02842 -0.04028 240 SER A CB  
3779 O OG  . SER A 240 ? 0.30494 0.38599 0.40146 0.03428  -0.02670 -0.04365 240 SER A OG  
3785 N N   . PRO A 241 ? 0.27301 0.36602 0.38005 0.04090  -0.02239 -0.04390 241 PRO A N   
3786 C CA  . PRO A 241 ? 0.27283 0.37400 0.38291 0.04321  -0.01940 -0.04674 241 PRO A CA  
3787 C C   . PRO A 241 ? 0.27179 0.37356 0.37140 0.04377  -0.01804 -0.04866 241 PRO A C   
3788 O O   . PRO A 241 ? 0.27719 0.38649 0.37972 0.04463  -0.01565 -0.05118 241 PRO A O   
3789 C CB  . PRO A 241 ? 0.31556 0.41416 0.42108 0.04774  -0.01960 -0.04276 241 PRO A CB  
3790 C CG  . PRO A 241 ? 0.33481 0.42208 0.42725 0.04841  -0.02231 -0.03858 241 PRO A CG  
3791 C CD  . PRO A 241 ? 0.31632 0.40065 0.41212 0.04367  -0.02452 -0.03914 241 PRO A CD  
3799 N N   . PHE A 242 ? 0.27514 0.36956 0.36312 0.04335  -0.01968 -0.04702 242 PHE A N   
3800 C CA  . PHE A 242 ? 0.26829 0.36448 0.34825 0.04358  -0.01854 -0.04815 242 PHE A CA  
3801 C C   . PHE A 242 ? 0.25932 0.34922 0.33439 0.04175  -0.02113 -0.04697 242 PHE A C   
3802 O O   . PHE A 242 ? 0.26911 0.35136 0.34378 0.04072  -0.02397 -0.04464 242 PHE A O   
3803 C CB  . PHE A 242 ? 0.27453 0.36766 0.34244 0.04741  -0.01732 -0.04528 242 PHE A CB  
3804 C CG  . PHE A 242 ? 0.21297 0.29408 0.26882 0.04949  -0.01945 -0.04112 242 PHE A CG  
3805 C CD1 . PHE A 242 ? 0.27385 0.34899 0.32011 0.04925  -0.02084 -0.03989 242 PHE A CD1 
3806 C CD2 . PHE A 242 ? 0.26917 0.34544 0.32389 0.05176  -0.02013 -0.03851 242 PHE A CD2 
3807 C CE1 . PHE A 242 ? 0.28929 0.35306 0.32434 0.05096  -0.02284 -0.03677 242 PHE A CE1 
3808 C CE2 . PHE A 242 ? 0.25443 0.31966 0.29723 0.05347  -0.02202 -0.03522 242 PHE A CE2 
3809 C CZ  . PHE A 242 ? 0.29752 0.35600 0.33005 0.05295  -0.02338 -0.03466 242 PHE A CZ  
3819 N N   . VAL A 243 ? 0.25478 0.34844 0.32675 0.04129  -0.02036 -0.04810 243 VAL A N   
3820 C CA  . VAL A 243 ? 0.24824 0.33576 0.31416 0.04077  -0.02303 -0.04593 243 VAL A CA  
3821 C C   . VAL A 243 ? 0.26492 0.35474 0.32220 0.04279  -0.02173 -0.04486 243 VAL A C   
3822 O O   . VAL A 243 ? 0.28151 0.38036 0.34036 0.04318  -0.01859 -0.04653 243 VAL A O   
3823 C CB  . VAL A 243 ? 0.28489 0.37620 0.36021 0.03766  -0.02372 -0.04761 243 VAL A CB  
3824 C CG1 . VAL A 243 ? 0.30817 0.39686 0.39334 0.03512  -0.02473 -0.04773 243 VAL A CG1 
3825 C CG2 . VAL A 243 ? 0.31814 0.42236 0.39974 0.03680  -0.02028 -0.05172 243 VAL A CG2 
3835 N N   . MET A 244 ? 0.24999 0.33193 0.29904 0.04379  -0.02421 -0.04181 244 MET A N   
3836 C CA  . MET A 244 ? 0.24467 0.32868 0.28722 0.04549  -0.02310 -0.04006 244 MET A CA  
3837 C C   . MET A 244 ? 0.26172 0.34671 0.30665 0.04457  -0.02558 -0.03907 244 MET A C   
3838 O O   . MET A 244 ? 0.28745 0.36294 0.33044 0.04427  -0.02947 -0.03724 244 MET A O   
3839 C CB  . MET A 244 ? 0.29338 0.36683 0.32428 0.04824  -0.02343 -0.03701 244 MET A CB  
3840 C CG  . MET A 244 ? 0.28214 0.35582 0.30724 0.04976  -0.02255 -0.03453 244 MET A CG  
3841 S SD  . MET A 244 ? 0.32744 0.38586 0.33875 0.05271  -0.02329 -0.03152 244 MET A SD  
3842 C CE  . MET A 244 ? 0.35601 0.41910 0.36499 0.05405  -0.02022 -0.02882 244 MET A CE  
3852 N N   . MET A 245 ? 0.25814 0.35497 0.30765 0.04414  -0.02352 -0.03983 245 MET A N   
3853 C CA  . MET A 245 ? 0.25874 0.35940 0.31228 0.04384  -0.02544 -0.03841 245 MET A CA  
3854 C C   . MET A 245 ? 0.27708 0.38081 0.32652 0.04571  -0.02472 -0.03530 245 MET A C   
3855 O O   . MET A 245 ? 0.30358 0.41539 0.35218 0.04591  -0.02104 -0.03539 245 MET A O   
3856 C CB  . MET A 245 ? 0.30883 0.42235 0.37216 0.04188  -0.02346 -0.04150 245 MET A CB  
3857 C CG  . MET A 245 ? 0.31460 0.42666 0.38358 0.03981  -0.02286 -0.04506 245 MET A CG  
3858 S SD  . MET A 245 ? 0.31272 0.41324 0.38561 0.03846  -0.02723 -0.04304 245 MET A SD  
3859 C CE  . MET A 245 ? 0.28067 0.38528 0.35690 0.03927  -0.02934 -0.03999 245 MET A CE  
3869 N N   . SER A 246 ? 0.25812 0.35552 0.30593 0.04693  -0.02826 -0.03214 246 SER A N   
3870 C CA  . SER A 246 ? 0.28545 0.38497 0.33073 0.04875  -0.02762 -0.02890 246 SER A CA  
3871 C C   . SER A 246 ? 0.29139 0.39663 0.34399 0.04937  -0.03034 -0.02623 246 SER A C   
3872 O O   . SER A 246 ? 0.29892 0.40076 0.35558 0.04894  -0.03388 -0.02601 246 SER A O   
3873 C CB  . SER A 246 ? 0.35006 0.43447 0.38502 0.05046  -0.02915 -0.02728 246 SER A CB  
3874 O OG  . SER A 246 ? 0.32780 0.40712 0.35645 0.05045  -0.02675 -0.02908 246 SER A OG  
3880 N N   . ALA A 247 ? 0.29220 0.40667 0.34758 0.05043  -0.02855 -0.02345 247 ALA A N   
3881 C CA  . ALA A 247 ? 0.29641 0.41791 0.36022 0.05166  -0.03110 -0.01999 247 ALA A CA  
3882 C C   . ALA A 247 ? 0.30278 0.43015 0.36794 0.05294  -0.02906 -0.01640 247 ALA A C   
3883 O O   . ALA A 247 ? 0.34326 0.47305 0.40435 0.05228  -0.02468 -0.01664 247 ALA A O   
3884 C CB  . ALA A 247 ? 0.32717 0.46423 0.40057 0.05054  -0.02991 -0.02090 247 ALA A CB  
3890 N N   . PRO A 248 ? 0.29230 0.42245 0.36441 0.05479  -0.03203 -0.01246 248 PRO A N   
3891 C CA  . PRO A 248 ? 0.30685 0.44618 0.38389 0.05566  -0.02945 -0.00857 248 PRO A CA  
3892 C C   . PRO A 248 ? 0.35069 0.50894 0.43327 0.05370  -0.02422 -0.00817 248 PRO A C   
3893 O O   . PRO A 248 ? 0.31269 0.48105 0.39954 0.05246  -0.02388 -0.01004 248 PRO A O   
3894 C CB  . PRO A 248 ? 0.33358 0.47647 0.42109 0.05799  -0.03412 -0.00446 248 PRO A CB  
3895 C CG  . PRO A 248 ? 0.38782 0.51525 0.47081 0.05858  -0.03974 -0.00609 248 PRO A CG  
3896 C CD  . PRO A 248 ? 0.35275 0.47895 0.43035 0.05618  -0.03776 -0.01066 248 PRO A CD  
3904 N N   . PRO A 249 ? 0.28391 0.44768 0.36683 0.05310  -0.01986 -0.00553 249 PRO A N   
3905 C CA  . PRO A 249 ? 0.28019 0.46098 0.36706 0.05050  -0.01484 -0.00486 249 PRO A CA  
3906 C C   . PRO A 249 ? 0.33099 0.53161 0.43046 0.05009  -0.01549 -0.00289 249 PRO A C   
3907 O O   . PRO A 249 ? 0.36010 0.56291 0.46729 0.05088  -0.01733 0.00137  249 PRO A O   
3908 C CB  . PRO A 249 ? 0.32562 0.50821 0.41324 0.05019  -0.01071 -0.00034 249 PRO A CB  
3909 C CG  . PRO A 249 ? 0.39770 0.56286 0.47994 0.05271  -0.01300 0.00010  249 PRO A CG  
3910 C CD  . PRO A 249 ? 0.30983 0.46306 0.38873 0.05447  -0.01911 -0.00316 249 PRO A CD  
3918 N N   . ALA A 250 ? 0.33207 0.54265 0.43162 0.04779  -0.01356 -0.00599 250 ALA A N   
3919 C CA  . ALA A 250 ? 0.37036 0.58772 0.47415 0.04447  -0.01268 -0.00431 250 ALA A CA  
3920 C C   . ALA A 250 ? 0.35840 0.58480 0.45883 0.04066  -0.00864 -0.00694 250 ALA A C   
3921 O O   . ALA A 250 ? 0.32981 0.55778 0.42664 0.04128  -0.00785 -0.01178 250 ALA A O   
3922 C CB  . ALA A 250 ? 0.37237 0.58522 0.47839 0.04616  -0.01682 -0.00622 250 ALA A CB  
3928 N N   . GLN A 251 ? 0.36001 0.59164 0.46162 0.03685  -0.00642 -0.00391 251 GLN A N   
3929 C CA  . GLN A 251 ? 0.34267 0.58264 0.44053 0.03317  -0.00336 -0.00640 251 GLN A CA  
3930 C C   . GLN A 251 ? 0.32854 0.57020 0.42478 0.03409  -0.00452 -0.01373 251 GLN A C   
3931 O O   . GLN A 251 ? 0.36249 0.60182 0.46135 0.03572  -0.00694 -0.01516 251 GLN A O   
3932 C CB  . GLN A 251 ? 0.43732 0.68185 0.53642 0.02987  -0.00204 -0.00254 251 GLN A CB  
3933 C CG  . GLN A 251 ? 0.50981 0.75363 0.61040 0.02770  -0.00002 0.00396  251 GLN A CG  
3934 C CD  . GLN A 251 ? 0.51091 0.75693 0.60784 0.02573  0.00294  0.00463  251 GLN A CD  
3935 O OE1 . GLN A 251 ? 0.56899 0.82076 0.66163 0.02348  0.00438  0.00159  251 GLN A OE1 
3936 N NE2 . GLN A 251 ? 0.61485 0.85596 0.71385 0.02665  0.00389  0.00867  251 GLN A NE2 
3945 N N   . TYR A 252 ? 0.33610 0.58124 0.42879 0.03286  -0.00261 -0.01818 252 TYR A N   
3946 C CA  . TYR A 252 ? 0.31541 0.56082 0.40771 0.03371  -0.00343 -0.02593 252 TYR A CA  
3947 C C   . TYR A 252 ? 0.35707 0.60887 0.44597 0.03036  -0.00041 -0.02966 252 TYR A C   
3948 O O   . TYR A 252 ? 0.34519 0.59788 0.43171 0.02915  0.00161  -0.02680 252 TYR A O   
3949 C CB  . TYR A 252 ? 0.30245 0.53539 0.39336 0.03743  -0.00597 -0.02809 252 TYR A CB  
3950 C CG  . TYR A 252 ? 0.28669 0.50991 0.37476 0.03718  -0.00701 -0.03468 252 TYR A CG  
3951 C CD1 . TYR A 252 ? 0.37196 0.59305 0.46416 0.03841  -0.00950 -0.03631 252 TYR A CD1 
3952 C CD2 . TYR A 252 ? 0.32170 0.53774 0.40428 0.03582  -0.00550 -0.03859 252 TYR A CD2 
3953 C CE1 . TYR A 252 ? 0.41200 0.62427 0.50319 0.03778  -0.01001 -0.04172 252 TYR A CE1 
3954 C CE2 . TYR A 252 ? 0.33728 0.54508 0.41939 0.03550  -0.00633 -0.04423 252 TYR A CE2 
3955 C CZ  . TYR A 252 ? 0.43225 0.63832 0.51884 0.03623  -0.00837 -0.04581 252 TYR A CZ  
3956 O OH  . TYR A 252 ? 0.43801 0.63644 0.52576 0.03547  -0.00871 -0.05081 252 TYR A OH  
3966 N N   . GLU A 253 ? 0.35095 0.60680 0.44004 0.02884  -0.00007 -0.03584 253 GLU A N   
3967 C CA  . GLU A 253 ? 0.35574 0.61763 0.44207 0.02547  0.00234  -0.04008 253 GLU A CA  
3968 C C   . GLU A 253 ? 0.44357 0.69895 0.53025 0.02702  0.00207  -0.04630 253 GLU A C   
3969 O O   . GLU A 253 ? 0.42060 0.66720 0.50818 0.02839  0.00045  -0.05044 253 GLU A O   
3970 C CB  . GLU A 253 ? 0.49620 0.76585 0.58207 0.02264  0.00316  -0.04366 253 GLU A CB  
3971 C CG  . GLU A 253 ? 0.52339 0.79862 0.60716 0.01942  0.00503  -0.04983 253 GLU A CG  
3972 C CD  . GLU A 253 ? 0.85080 1.13621 0.93185 0.01570  0.00620  -0.05086 253 GLU A CD  
3973 O OE1 . GLU A 253 ? 0.75097 1.03864 0.83283 0.01634  0.00564  -0.04908 253 GLU A OE1 
3974 O OE2 . GLU A 253 ? 0.85893 1.15015 0.93716 0.01232  0.00752  -0.05327 253 GLU A OE2 
3981 N N   . LEU A 254 ? 0.37475 0.62615 0.45718 0.02598  0.00345  -0.04521 254 LEU A N   
3982 C CA  . LEU A 254 ? 0.40324 0.64146 0.48229 0.02650  0.00311  -0.04942 254 LEU A CA  
3983 C C   . LEU A 254 ? 0.41760 0.66492 0.49821 0.02325  0.00471  -0.05543 254 LEU A C   
3984 O O   . LEU A 254 ? 0.43548 0.69338 0.51548 0.02057  0.00647  -0.05346 254 LEU A O   
3985 C CB  . LEU A 254 ? 0.37425 0.60215 0.44815 0.02795  0.00359  -0.04417 254 LEU A CB  
3986 C CG  . LEU A 254 ? 0.36242 0.57759 0.43342 0.03138  0.00191  -0.03954 254 LEU A CG  
3987 C CD1 . LEU A 254 ? 0.28824 0.49582 0.35409 0.03249  0.00348  -0.03387 254 LEU A CD1 
3988 C CD2 . LEU A 254 ? 0.36280 0.56402 0.43293 0.03357  -0.00083 -0.04339 254 LEU A CD2 
4000 N N   . LYS A 255 ? 0.42194 0.66502 0.50512 0.02321  0.00414  -0.06248 255 LYS A N   
4001 C CA  . LYS A 255 ? 0.49190 0.74299 0.57749 0.02020  0.00559  -0.06939 255 LYS A CA  
4002 C C   . LYS A 255 ? 0.44420 0.68548 0.52939 0.02066  0.00534  -0.07137 255 LYS A C   
4003 O O   . LYS A 255 ? 0.39249 0.62053 0.47861 0.02314  0.00399  -0.07195 255 LYS A O   
4004 C CB  . LYS A 255 ? 0.55025 0.80408 0.64075 0.01967  0.00578  -0.07616 255 LYS A CB  
4005 C CG  . LYS A 255 ? 0.79272 1.05836 0.88476 0.01944  0.00615  -0.07450 255 LYS A CG  
4006 C CD  . LYS A 255 ? 1.03359 1.31196 1.12144 0.01593  0.00748  -0.07220 255 LYS A CD  
4007 C CE  . LYS A 255 ? 1.08938 1.37562 1.17714 0.01247  0.00903  -0.07986 255 LYS A CE  
4008 N NZ  . LYS A 255 ? 1.13767 1.43469 1.22020 0.00936  0.00956  -0.07664 255 LYS A NZ  
4022 N N   . HIS A 256 ? 0.45617 0.70463 0.54065 0.01823  0.00646  -0.07193 256 HIS A N   
4023 C CA  . HIS A 256 ? 0.42250 0.66337 0.50780 0.01889  0.00606  -0.07303 256 HIS A CA  
4024 C C   . HIS A 256 ? 0.45062 0.68522 0.54224 0.01961  0.00542  -0.08050 256 HIS A C   
4025 O O   . HIS A 256 ? 0.44751 0.68897 0.54339 0.01749  0.00628  -0.08739 256 HIS A O   
4026 C CB  . HIS A 256 ? 0.46650 0.71845 0.55141 0.01538  0.00709  -0.07354 256 HIS A CB  
4027 C CG  . HIS A 256 ? 0.51557 0.76165 0.60314 0.01596  0.00638  -0.07523 256 HIS A CG  
4028 N ND1 . HIS A 256 ? 0.56949 0.82136 0.66216 0.01351  0.00639  -0.08307 256 HIS A ND1 
4029 C CD2 . HIS A 256 ? 0.50800 0.74320 0.59455 0.01902  0.00560  -0.06992 256 HIS A CD2 
4030 C CE1 . HIS A 256 ? 0.66198 0.90715 0.75762 0.01509  0.00533  -0.08222 256 HIS A CE1 
4031 N NE2 . HIS A 256 ? 0.55111 0.78625 0.64301 0.01859  0.00487  -0.07404 256 HIS A NE2 
4039 N N   . GLY A 257 ? 0.41937 0.64129 0.51217 0.02260  0.00419  -0.07874 257 GLY A N   
4040 C CA  . GLY A 257 ? 0.47014 0.68655 0.57091 0.02318  0.00366  -0.08455 257 GLY A CA  
4041 C C   . GLY A 257 ? 0.44095 0.65041 0.54424 0.02431  0.00296  -0.08553 257 GLY A C   
4042 O O   . GLY A 257 ? 0.44986 0.65527 0.56127 0.02432  0.00284  -0.08982 257 GLY A O   
4046 N N   . THR A 258 ? 0.34493 0.55319 0.44270 0.02511  0.00244  -0.08126 258 THR A N   
4047 C CA  . THR A 258 ? 0.34152 0.54341 0.44166 0.02593  0.00140  -0.08149 258 THR A CA  
4048 C C   . THR A 258 ? 0.36539 0.55421 0.46055 0.02902  -0.00086 -0.07507 258 THR A C   
4049 O O   . THR A 258 ? 0.32122 0.50330 0.41758 0.02970  -0.00235 -0.07411 258 THR A O   
4050 C CB  . THR A 258 ? 0.40449 0.61517 0.50360 0.02471  0.00207  -0.08173 258 THR A CB  
4051 O OG1 . THR A 258 ? 0.44994 0.66286 0.54196 0.02583  0.00149  -0.07513 258 THR A OG1 
4052 C CG2 . THR A 258 ? 0.45862 0.68310 0.56129 0.02151  0.00452  -0.08835 258 THR A CG2 
4060 N N   . PHE A 259 ? 0.30654 0.49140 0.39599 0.03081  -0.00110 -0.07050 259 PHE A N   
4061 C CA  . PHE A 259 ? 0.29422 0.46675 0.37748 0.03383  -0.00287 -0.06460 259 PHE A CA  
4062 C C   . PHE A 259 ? 0.30784 0.47621 0.38830 0.03574  -0.00238 -0.06167 259 PHE A C   
4063 O O   . PHE A 259 ? 0.31116 0.48681 0.39379 0.03464  -0.00091 -0.06305 259 PHE A O   
4064 C CB  . PHE A 259 ? 0.29295 0.46646 0.36973 0.03444  -0.00324 -0.05973 259 PHE A CB  
4065 C CG  . PHE A 259 ? 0.28426 0.46580 0.35709 0.03388  -0.00124 -0.05627 259 PHE A CG  
4066 C CD1 . PHE A 259 ? 0.28978 0.48589 0.36576 0.03088  0.00054  -0.05897 259 PHE A CD1 
4067 C CD2 . PHE A 259 ? 0.27425 0.44896 0.34045 0.03606  -0.00089 -0.05011 259 PHE A CD2 
4068 C CE1 . PHE A 259 ? 0.31983 0.52393 0.39296 0.02972  0.00234  -0.05494 259 PHE A CE1 
4069 C CE2 . PHE A 259 ? 0.31113 0.49307 0.37500 0.03512  0.00132  -0.04605 259 PHE A CE2 
4070 C CZ  . PHE A 259 ? 0.29760 0.49464 0.36523 0.03173  0.00282  -0.04817 259 PHE A CZ  
4080 N N   . THR A 260 ? 0.21772 0.37413 0.29313 0.03871  -0.00371 -0.05725 260 THR A N   
4081 C CA  . THR A 260 ? 0.22131 0.37274 0.29337 0.04130  -0.00309 -0.05331 260 THR A CA  
4082 C C   . THR A 260 ? 0.23826 0.38988 0.30189 0.04215  -0.00149 -0.04733 260 THR A C   
4083 O O   . THR A 260 ? 0.27350 0.43033 0.33707 0.04179  0.00032  -0.04529 260 THR A O   
4084 C CB  . THR A 260 ? 0.27983 0.41874 0.35053 0.04421  -0.00497 -0.05138 260 THR A CB  
4085 O OG1 . THR A 260 ? 0.29990 0.43984 0.38057 0.04289  -0.00611 -0.05622 260 THR A OG1 
4086 C CG2 . THR A 260 ? 0.31565 0.44968 0.38334 0.04751  -0.00416 -0.04694 260 THR A CG2 
4094 N N   . CYS A 261 ? 0.26404 0.40965 0.32128 0.04321  -0.00215 -0.04403 261 CYS A N   
4095 C CA  . CYS A 261 ? 0.22959 0.37538 0.28041 0.04387  -0.00024 -0.03811 261 CYS A CA  
4096 C C   . CYS A 261 ? 0.25914 0.40277 0.30713 0.04385  -0.00150 -0.03689 261 CYS A C   
4097 O O   . CYS A 261 ? 0.25296 0.39280 0.30265 0.04377  -0.00411 -0.03990 261 CYS A O   
4098 C CB  . CYS A 261 ? 0.20232 0.33756 0.24707 0.04733  0.00086  -0.03297 261 CYS A CB  
4099 S SG  . CYS A 261 ? 0.26221 0.38082 0.30144 0.05090  -0.00179 -0.03272 261 CYS A SG  
4105 N N   . ALA A 262 ? 0.25333 0.39963 0.29815 0.04384  0.00037  -0.03192 262 ALA A N   
4106 C CA  . ALA A 262 ? 0.24873 0.39500 0.29290 0.04389  -0.00085 -0.03035 262 ALA A CA  
4107 C C   . ALA A 262 ? 0.24243 0.38591 0.28212 0.04510  0.00153  -0.02387 262 ALA A C   
4108 O O   . ALA A 262 ? 0.25064 0.39513 0.28868 0.04514  0.00464  -0.02020 262 ALA A O   
4109 C CB  . ALA A 262 ? 0.29448 0.45596 0.34592 0.04096  -0.00100 -0.03263 262 ALA A CB  
4115 N N   . SER A 263 ? 0.24109 0.38081 0.27965 0.04608  0.00008  -0.02215 263 SER A N   
4116 C CA  . SER A 263 ? 0.24126 0.37938 0.27764 0.04696  0.00250  -0.01627 263 SER A CA  
4117 C C   . SER A 263 ? 0.23212 0.38353 0.27634 0.04518  0.00235  -0.01443 263 SER A C   
4118 O O   . SER A 263 ? 0.25284 0.40728 0.30101 0.04498  -0.00097 -0.01734 263 SER A O   
4119 C CB  . SER A 263 ? 0.27312 0.39407 0.30144 0.05014  0.00105  -0.01539 263 SER A CB  
4120 O OG  . SER A 263 ? 0.33064 0.44065 0.35198 0.05212  0.00179  -0.01584 263 SER A OG  
4126 N N   . GLU A 264 ? 0.26259 0.42224 0.30992 0.04394  0.00608  -0.00889 264 GLU A N   
4127 C CA  . GLU A 264 ? 0.29202 0.46679 0.34858 0.04215  0.00666  -0.00564 264 GLU A CA  
4128 C C   . GLU A 264 ? 0.31766 0.48709 0.37441 0.04366  0.00844  -0.00007 264 GLU A C   
4129 O O   . GLU A 264 ? 0.29129 0.45300 0.34314 0.04429  0.01193  0.00344  264 GLU A O   
4130 C CB  . GLU A 264 ? 0.31140 0.50328 0.37358 0.03843  0.00989  -0.00337 264 GLU A CB  
4131 C CG  . GLU A 264 ? 0.31538 0.52534 0.38819 0.03618  0.01131  0.00157  264 GLU A CG  
4132 C CD  . GLU A 264 ? 0.37981 0.60449 0.45671 0.03211  0.01528  0.00579  264 GLU A CD  
4133 O OE1 . GLU A 264 ? 0.35651 0.57828 0.43263 0.03151  0.01909  0.01198  264 GLU A OE1 
4134 O OE2 . GLU A 264 ? 0.44828 0.68724 0.52910 0.02936  0.01467  0.00313  264 GLU A OE2 
4141 N N   . TYR A 265 ? 0.26743 0.44070 0.33044 0.04443  0.00613  0.00091  265 TYR A N   
4142 C CA  . TYR A 265 ? 0.26817 0.43779 0.33367 0.04576  0.00766  0.00586  265 TYR A CA  
4143 C C   . TYR A 265 ? 0.27335 0.46309 0.35322 0.04375  0.00900  0.01094  265 TYR A C   
4144 O O   . TYR A 265 ? 0.30448 0.50356 0.39158 0.04394  0.00546  0.00954  265 TYR A O   
4145 C CB  . TYR A 265 ? 0.28012 0.43434 0.34093 0.04902  0.00306  0.00292  265 TYR A CB  
4146 C CG  . TYR A 265 ? 0.28481 0.43389 0.34792 0.05052  0.00452  0.00714  265 TYR A CG  
4147 C CD1 . TYR A 265 ? 0.29855 0.43424 0.35322 0.05167  0.00826  0.00885  265 TYR A CD1 
4148 C CD2 . TYR A 265 ? 0.33238 0.49003 0.40687 0.05104  0.00231  0.00954  265 TYR A CD2 
4149 C CE1 . TYR A 265 ? 0.31765 0.44839 0.37479 0.05290  0.01012  0.01224  265 TYR A CE1 
4150 C CE2 . TYR A 265 ? 0.38756 0.54084 0.46563 0.05235  0.00372  0.01311  265 TYR A CE2 
4151 C CZ  . TYR A 265 ? 0.33981 0.47922 0.40888 0.05314  0.00774  0.01409  265 TYR A CZ  
4152 O OH  . TYR A 265 ? 0.45899 0.59356 0.53182 0.05435  0.00962  0.01717  265 TYR A OH  
4162 N N   . THR A 266 ? 0.28459 0.48106 0.36935 0.04192  0.01420  0.01746  266 THR A N   
4163 C CA  . THR A 266 ? 0.29256 0.50905 0.39261 0.03969  0.01624  0.02375  266 THR A CA  
4164 C C   . THR A 266 ? 0.34233 0.55256 0.44713 0.04162  0.01755  0.02795  266 THR A C   
4165 O O   . THR A 266 ? 0.38789 0.58616 0.48690 0.04208  0.02146  0.03032  266 THR A O   
4166 C CB  . THR A 266 ? 0.30605 0.52579 0.40459 0.03375  0.02038  0.02784  266 THR A CB  
4167 O OG1 . THR A 266 ? 0.37334 0.59810 0.46712 0.03248  0.01907  0.02322  266 THR A OG1 
4168 C CG2 . THR A 266 ? 0.41747 0.63801 0.52098 0.02838  0.02016  0.03181  266 THR A CG2 
4176 N N   . GLY A 267 ? 0.38678 0.59758 0.49856 0.04128  0.01397  0.02816  267 GLY A N   
4177 C CA  . GLY A 267 ? 0.42708 0.63271 0.54502 0.04302  0.01474  0.03153  267 GLY A CA  
4178 C C   . GLY A 267 ? 0.45351 0.65590 0.57537 0.04668  0.00846  0.02861  267 GLY A C   
4179 O O   . GLY A 267 ? 0.46400 0.66807 0.58575 0.04549  0.00411  0.02556  267 GLY A O   
4183 N N   . ASN A 268 ? 0.42966 0.62436 0.55360 0.05085  0.00794  0.02945  268 ASN A N   
4184 C CA  . ASN A 268 ? 0.45588 0.64481 0.58315 0.05416  0.00134  0.02717  268 ASN A CA  
4185 C C   . ASN A 268 ? 0.54736 0.70996 0.65872 0.05663  -0.00057 0.02226  268 ASN A C   
4186 O O   . ASN A 268 ? 0.54411 0.69391 0.64176 0.05611  0.00305  0.02036  268 ASN A O   
4187 C CB  . ASN A 268 ? 0.44891 0.63877 0.58786 0.05067  0.00140  0.03053  268 ASN A CB  
4188 C CG  . ASN A 268 ? 0.53728 0.72573 0.68038 0.04994  0.00740  0.03479  268 ASN A CG  
4189 O OD1 . ASN A 268 ? 0.54214 0.72401 0.68304 0.05519  0.00889  0.03512  268 ASN A OD1 
4190 N ND2 . ASN A 268 ? 0.72581 0.91708 0.87250 0.04339  0.01096  0.03757  268 ASN A ND2 
4197 N N   . TYR A 269 ? 0.53702 0.69166 0.65048 0.05942  -0.00647 0.02057  269 TYR A N   
4198 C CA  . TYR A 269 ? 0.64272 0.77268 0.74023 0.06149  -0.00950 0.01538  269 TYR A CA  
4199 C C   . TYR A 269 ? 0.67265 0.79112 0.76461 0.06173  -0.00402 0.01623  269 TYR A C   
4200 O O   . TYR A 269 ? 0.62412 0.72200 0.69995 0.06309  -0.00516 0.01173  269 TYR A O   
4201 C CB  . TYR A 269 ? 0.76699 0.89189 0.86949 0.06411  -0.01739 0.01426  269 TYR A CB  
4202 C CG  . TYR A 269 ? 0.92996 1.05998 1.04773 0.06556  -0.01732 0.01841  269 TYR A CG  
4203 C CD1 . TYR A 269 ? 0.67237 0.82596 0.81106 0.06478  -0.01461 0.02487  269 TYR A CD1 
4204 C CD2 . TYR A 269 ? 0.69227 0.80430 0.80438 0.06762  -0.02010 0.01590  269 TYR A CD2 
4205 C CE1 . TYR A 269 ? 0.78434 0.94403 0.93954 0.06615  -0.01446 0.02909  269 TYR A CE1 
4206 C CE2 . TYR A 269 ? 0.70262 0.81947 0.83015 0.06900  -0.02009 0.01940  269 TYR A CE2 
4207 C CZ  . TYR A 269 ? 0.83990 0.98096 0.98984 0.06834  -0.01720 0.02618  269 TYR A CZ  
4208 O OH  . TYR A 269 ? 0.69471 0.84206 0.86249 0.06974  -0.01707 0.03010  269 TYR A OH  
4218 N N   . GLN A 270 ? 0.48701 0.61828 0.59200 0.06034  0.00213  0.02214  270 GLN A N   
4219 C CA  . GLN A 270 ? 0.56009 0.68061 0.66119 0.06050  0.00819  0.02356  270 GLN A CA  
4220 C C   . GLN A 270 ? 0.73902 0.86239 0.83569 0.05808  0.01620  0.02685  270 GLN A C   
4221 O O   . GLN A 270 ? 0.57540 0.68369 0.66131 0.05879  0.02076  0.02639  270 GLN A O   
4222 C CB  . GLN A 270 ? 0.63936 0.77008 0.76028 0.06076  0.00981  0.02862  270 GLN A CB  
4223 C CG  . GLN A 270 ? 0.98287 1.10584 1.10693 0.06379  0.00209  0.02543  270 GLN A CG  
4224 C CD  . GLN A 270 ? 0.94957 1.07754 1.09108 0.06454  0.00417  0.02942  270 GLN A CD  
4225 O OE1 . GLN A 270 ? 0.90545 1.01620 1.04072 0.06643  0.00317  0.02601  270 GLN A OE1 
4226 N NE2 . GLN A 270 ? 0.77652 0.92872 0.94068 0.06292  0.00706  0.03669  270 GLN A NE2 
4235 N N   . SER A 271 ? 0.55327 0.69533 0.65788 0.05530  0.01798  0.03040  271 SER A N   
4236 C CA  . SER A 271 ? 0.52659 0.67292 0.62917 0.05261  0.02531  0.03474  271 SER A CA  
4237 C C   . SER A 271 ? 0.51449 0.67358 0.61645 0.05039  0.02373  0.03407  271 SER A C   
4238 O O   . SER A 271 ? 0.44976 0.62693 0.56421 0.04917  0.02087  0.03537  271 SER A O   
4239 C CB  . SER A 271 ? 0.62848 0.78935 0.74909 0.05012  0.03205  0.04342  271 SER A CB  
4240 O OG  . SER A 271 ? 0.67765 0.86157 0.81514 0.04730  0.03040  0.04717  271 SER A OG  
4246 N N   . GLY A 272 ? 0.45498 0.54927 0.41855 0.06060  -0.03872 0.03099  272 GLY A N   
4247 C CA  . GLY A 272 ? 0.45843 0.56204 0.42605 0.05588  -0.03882 0.02876  272 GLY A CA  
4248 C C   . GLY A 272 ? 0.43812 0.53908 0.40538 0.05791  -0.03583 0.03164  272 GLY A C   
4249 O O   . GLY A 272 ? 0.47578 0.57001 0.44111 0.06183  -0.03343 0.03697  272 GLY A O   
4253 N N   . HIS A 273 ? 0.37600 0.48222 0.34533 0.05523  -0.03592 0.02797  273 HIS A N   
4254 C CA  . HIS A 273 ? 0.32297 0.42805 0.29244 0.05683  -0.03343 0.03018  273 HIS A CA  
4255 C C   . HIS A 273 ? 0.34169 0.45005 0.31259 0.05506  -0.03425 0.02348  273 HIS A C   
4256 O O   . HIS A 273 ? 0.32195 0.43884 0.29628 0.04956  -0.03578 0.01935  273 HIS A O   
4257 C CB  . HIS A 273 ? 0.35356 0.46756 0.32757 0.05247  -0.03143 0.03713  273 HIS A CB  
4258 C CG  . HIS A 273 ? 0.36632 0.47854 0.34004 0.05454  -0.02888 0.04048  273 HIS A CG  
4259 N ND1 . HIS A 273 ? 0.40290 0.50538 0.37334 0.06045  -0.02678 0.04560  273 HIS A ND1 
4260 C CD2 . HIS A 273 ? 0.43161 0.55047 0.40787 0.05152  -0.02809 0.03943  273 HIS A CD2 
4261 C CE1 . HIS A 273 ? 0.40862 0.51180 0.37951 0.06126  -0.02508 0.04769  273 HIS A CE1 
4262 N NE2 . HIS A 273 ? 0.35839 0.47150 0.33276 0.05595  -0.02583 0.04406  273 HIS A NE2 
4271 N N   . TYR A 274 ? 0.31185 0.41361 0.28061 0.05961  -0.03316 0.02247  274 TYR A N   
4272 C CA  . TYR A 274 ? 0.30693 0.41148 0.27801 0.05849  -0.03348 0.01663  274 TYR A CA  
4273 C C   . TYR A 274 ? 0.32855 0.44024 0.30303 0.05614  -0.03125 0.01934  274 TYR A C   
4274 O O   . TYR A 274 ? 0.31573 0.42492 0.28883 0.05869  -0.02937 0.02567  274 TYR A O   
4275 C CB  . TYR A 274 ? 0.29550 0.38890 0.26290 0.06488  -0.03398 0.01369  274 TYR A CB  
4276 C CG  . TYR A 274 ? 0.26399 0.35151 0.22898 0.06606  -0.03648 0.00871  274 TYR A CG  
4277 C CD1 . TYR A 274 ? 0.28037 0.37196 0.24879 0.06274  -0.03806 0.00216  274 TYR A CD1 
4278 C CD2 . TYR A 274 ? 0.31557 0.39290 0.27485 0.07052  -0.03706 0.01068  274 TYR A CD2 
4279 C CE1 . TYR A 274 ? 0.29636 0.38192 0.26254 0.06390  -0.04038 -0.00182 274 TYR A CE1 
4280 C CE2 . TYR A 274 ? 0.34026 0.41159 0.29677 0.07163  -0.03939 0.00650  274 TYR A CE2 
4281 C CZ  . TYR A 274 ? 0.35092 0.42629 0.31085 0.06841  -0.04114 0.00053  274 TYR A CZ  
4282 O OH  . TYR A 274 ? 0.34362 0.41258 0.30079 0.06948  -0.04347 -0.00296 274 TYR A OH  
4292 N N   . LYS A 275 ? 0.30006 0.42019 0.27897 0.05130  -0.03133 0.01449  275 LYS A N   
4293 C CA  . LYS A 275 ? 0.30946 0.43550 0.29138 0.04955  -0.02930 0.01550  275 LYS A CA  
4294 C C   . LYS A 275 ? 0.30783 0.43336 0.29227 0.05049  -0.02963 0.00834  275 LYS A C   
4295 O O   . LYS A 275 ? 0.31167 0.43539 0.29686 0.05001  -0.03136 0.00252  275 LYS A O   
4296 C CB  . LYS A 275 ? 0.30085 0.43993 0.28692 0.04106  -0.02840 0.01721  275 LYS A CB  
4297 C CG  . LYS A 275 ? 0.35168 0.49282 0.33694 0.03940  -0.02780 0.02523  275 LYS A CG  
4298 C CD  . LYS A 275 ? 0.37457 0.52935 0.36433 0.03027  -0.02694 0.02731  275 LYS A CD  
4299 C CE  . LYS A 275 ? 0.44261 0.60004 0.43283 0.02801  -0.02673 0.03539  275 LYS A CE  
4300 N NZ  . LYS A 275 ? 0.54629 0.71772 0.54127 0.01806  -0.02669 0.03657  275 LYS A NZ  
4314 N N   . HIS A 276 ? 0.28974 0.41774 0.27622 0.05130  -0.02790 0.00906  276 HIS A N   
4315 C CA  . HIS A 276 ? 0.27850 0.40679 0.26867 0.05244  -0.02782 0.00307  276 HIS A CA  
4316 C C   . HIS A 276 ? 0.32642 0.46660 0.32216 0.04557  -0.02606 0.00069  276 HIS A C   
4317 O O   . HIS A 276 ? 0.32738 0.47307 0.32299 0.04299  -0.02441 0.00570  276 HIS A O   
4318 C CB  . HIS A 276 ? 0.26406 0.38499 0.25222 0.05987  -0.02733 0.00579  276 HIS A CB  
4319 C CG  . HIS A 276 ? 0.27685 0.39821 0.26968 0.06148  -0.02745 0.00011  276 HIS A CG  
4320 N ND1 . HIS A 276 ? 0.27271 0.38705 0.26574 0.06496  -0.02925 -0.00413 276 HIS A ND1 
4321 C CD2 . HIS A 276 ? 0.28312 0.41140 0.28120 0.05982  -0.02595 -0.00183 276 HIS A CD2 
4322 C CE1 . HIS A 276 ? 0.25742 0.37474 0.25641 0.06525  -0.02889 -0.00841 276 HIS A CE1 
4323 N NE2 . HIS A 276 ? 0.28396 0.40975 0.28614 0.06233  -0.02684 -0.00731 276 HIS A NE2 
4331 N N   . ILE A 277 ? 0.27963 0.42366 0.28040 0.04229  -0.02622 -0.00670 277 ILE A N   
4332 C CA  . ILE A 277 ? 0.29510 0.44992 0.30160 0.03580  -0.02411 -0.00987 277 ILE A CA  
4333 C C   . ILE A 277 ? 0.30226 0.45613 0.31374 0.03864  -0.02340 -0.01472 277 ILE A C   
4334 O O   . ILE A 277 ? 0.28895 0.43752 0.30228 0.04121  -0.02482 -0.01933 277 ILE A O   
4335 C CB  . ILE A 277 ? 0.34348 0.50559 0.35288 0.02775  -0.02436 -0.01448 277 ILE A CB  
4336 C CG1 . ILE A 277 ? 0.41082 0.57505 0.41620 0.02484  -0.02525 -0.00912 277 ILE A CG1 
4337 C CG2 . ILE A 277 ? 0.33721 0.51047 0.35249 0.02049  -0.02167 -0.01801 277 ILE A CG2 
4338 C CD1 . ILE A 277 ? 0.44672 0.60395 0.44879 0.02753  -0.02801 -0.00972 277 ILE A CD1 
4350 N N   . THR A 278 ? 0.29384 0.45299 0.30785 0.03811  -0.02125 -0.01335 278 THR A N   
4351 C CA  . THR A 278 ? 0.28428 0.44410 0.30420 0.04054  -0.02039 -0.01765 278 THR A CA  
4352 C C   . THR A 278 ? 0.30285 0.47414 0.32901 0.03309  -0.01754 -0.02139 278 THR A C   
4353 O O   . THR A 278 ? 0.30295 0.48086 0.32730 0.02832  -0.01594 -0.01778 278 THR A O   
4354 C CB  . THR A 278 ? 0.29618 0.45040 0.31339 0.04843  -0.02066 -0.01256 278 THR A CB  
4355 O OG1 . THR A 278 ? 0.34747 0.50376 0.37146 0.05049  -0.01996 -0.01666 278 THR A OG1 
4356 C CG2 . THR A 278 ? 0.33827 0.49602 0.35158 0.04740  -0.01918 -0.00541 278 THR A CG2 
4364 N N   . SER A 279 ? 0.28487 0.45864 0.31869 0.03136  -0.01677 -0.02864 279 SER A N   
4365 C CA  . SER A 279 ? 0.30230 0.48666 0.34295 0.02391  -0.01364 -0.03334 279 SER A CA  
4366 C C   . SER A 279 ? 0.35823 0.54496 0.40362 0.02733  -0.01201 -0.03345 279 SER A C   
4367 O O   . SER A 279 ? 0.34914 0.53288 0.40027 0.03148  -0.01255 -0.03706 279 SER A O   
4368 C CB  . SER A 279 ? 0.34032 0.52643 0.38751 0.01919  -0.01330 -0.04133 279 SER A CB  
4369 O OG  . SER A 279 ? 0.37377 0.56997 0.42804 0.01184  -0.00975 -0.04617 279 SER A OG  
4375 N N   . LYS A 280 ? 0.38809 0.58044 0.43137 0.02545  -0.01013 -0.02918 280 LYS A N   
4376 C CA  . LYS A 280 ? 0.30375 0.49917 0.35097 0.02850  -0.00858 -0.02866 280 LYS A CA  
4377 C C   . LYS A 280 ? 0.33936 0.54619 0.39072 0.01984  -0.00482 -0.03127 280 LYS A C   
4378 O O   . LYS A 280 ? 0.39229 0.60414 0.44927 0.01309  -0.00312 -0.03795 280 LYS A O   
4379 C CB  . LYS A 280 ? 0.32067 0.51076 0.36063 0.03549  -0.00999 -0.02010 280 LYS A CB  
4380 C CG  . LYS A 280 ? 0.34658 0.52517 0.38109 0.04294  -0.01336 -0.01710 280 LYS A CG  
4381 C CD  . LYS A 280 ? 0.38609 0.55986 0.42616 0.04855  -0.01491 -0.02173 280 LYS A CD  
4382 C CE  . LYS A 280 ? 0.61279 0.78825 0.65697 0.05367  -0.01447 -0.02085 280 LYS A CE  
4383 N NZ  . LYS A 280 ? 0.60879 0.77843 0.65740 0.05998  -0.01670 -0.02364 280 LYS A NZ  
4397 N N   . GLU A 281 ? 0.36922 0.58002 0.41779 0.01967  -0.00339 -0.02602 281 GLU A N   
4398 C CA  . GLU A 281 ? 0.39643 0.61806 0.44763 0.01062  0.00030  -0.02777 281 GLU A CA  
4399 C C   . GLU A 281 ? 0.42046 0.64610 0.46772 0.00174  0.00077  -0.02709 281 GLU A C   
4400 O O   . GLU A 281 ? 0.44208 0.67677 0.49269 -0.00749 0.00380  -0.03095 281 GLU A O   
4401 C CB  . GLU A 281 ? 0.39062 0.61469 0.43867 0.01284  0.00136  -0.02118 281 GLU A CB  
4402 C CG  . GLU A 281 ? 0.56838 0.78703 0.60656 0.01606  -0.00073 -0.01123 281 GLU A CG  
4403 C CD  . GLU A 281 ? 0.57142 0.78020 0.60682 0.02767  -0.00353 -0.00688 281 GLU A CD  
4404 O OE1 . GLU A 281 ? 0.36720 0.57100 0.40670 0.03303  -0.00516 -0.01167 281 GLU A OE1 
4405 O OE2 . GLU A 281 ? 0.49268 0.69873 0.52205 0.03118  -0.00404 0.00146  281 GLU A OE2 
4412 N N   . THR A 282 ? 0.40473 0.62419 0.44515 0.00419  -0.00209 -0.02207 282 THR A N   
4413 C CA  . THR A 282 ? 0.39085 0.61311 0.42848 -0.00300 -0.00258 -0.02191 282 THR A CA  
4414 C C   . THR A 282 ? 0.41046 0.62274 0.44428 0.00330  -0.00626 -0.02049 282 THR A C   
4415 O O   . THR A 282 ? 0.36240 0.56650 0.39649 0.01190  -0.00795 -0.02082 282 THR A O   
4416 C CB  . THR A 282 ? 0.45486 0.68320 0.48750 -0.00882 -0.00142 -0.01451 282 THR A CB  
4417 O OG1 . THR A 282 ? 0.46867 0.70171 0.50019 -0.01703 -0.00180 -0.01517 282 THR A OG1 
4418 C CG2 . THR A 282 ? 0.39718 0.61837 0.42320 -0.00133 -0.00335 -0.00491 282 THR A CG2 
4426 N N   . LEU A 283 ? 0.36547 0.57869 0.39601 -0.00121 -0.00755 -0.01905 283 LEU A N   
4427 C CA  . LEU A 283 ? 0.34279 0.54695 0.36919 0.00428  -0.01091 -0.01714 283 LEU A CA  
4428 C C   . LEU A 283 ? 0.34872 0.54848 0.36833 0.00860  -0.01203 -0.00734 283 LEU A C   
4429 O O   . LEU A 283 ? 0.36603 0.57166 0.38340 0.00299  -0.01124 -0.00204 283 LEU A O   
4430 C CB  . LEU A 283 ? 0.37037 0.57779 0.39722 -0.00232 -0.01193 -0.02056 283 LEU A CB  
4431 C CG  . LEU A 283 ? 0.41486 0.62501 0.44838 -0.00627 -0.01102 -0.03024 283 LEU A CG  
4432 C CD1 . LEU A 283 ? 0.46728 0.68097 0.50049 -0.01291 -0.01225 -0.03268 283 LEU A CD1 
4433 C CD2 . LEU A 283 ? 0.44263 0.64342 0.47842 0.00186  -0.01249 -0.03392 283 LEU A CD2 
4445 N N   . TYR A 284 ? 0.30752 0.49708 0.32431 0.01817  -0.01372 -0.00482 284 TYR A N   
4446 C CA  . TYR A 284 ? 0.29946 0.48310 0.31013 0.02321  -0.01464 0.00414  284 TYR A CA  
4447 C C   . TYR A 284 ? 0.32136 0.49709 0.32837 0.02663  -0.01723 0.00509  284 TYR A C   
4448 O O   . TYR A 284 ? 0.32978 0.49934 0.33760 0.03069  -0.01881 -0.00001 284 TYR A O   
4449 C CB  . TYR A 284 ? 0.33012 0.50772 0.33993 0.03162  -0.01449 0.00661  284 TYR A CB  
4450 C CG  . TYR A 284 ? 0.31987 0.50492 0.33227 0.02892  -0.01200 0.00756  284 TYR A CG  
4451 C CD1 . TYR A 284 ? 0.39456 0.58511 0.40442 0.02419  -0.01049 0.01451  284 TYR A CD1 
4452 C CD2 . TYR A 284 ? 0.35753 0.54449 0.37537 0.03074  -0.01111 0.00171  284 TYR A CD2 
4453 C CE1 . TYR A 284 ? 0.36774 0.56503 0.37945 0.02145  -0.00818 0.01560  284 TYR A CE1 
4454 C CE2 . TYR A 284 ? 0.37020 0.56426 0.39051 0.02827  -0.00872 0.00248  284 TYR A CE2 
4455 C CZ  . TYR A 284 ? 0.35656 0.55554 0.37331 0.02365  -0.00728 0.00941  284 TYR A CZ  
4456 O OH  . TYR A 284 ? 0.39266 0.59847 0.41128 0.02104  -0.00490 0.01046  284 TYR A OH  
4466 N N   . CYS A 285 ? 0.33483 0.51065 0.33811 0.02500  -0.01763 0.01193  285 CYS A N   
4467 C CA  . CYS A 285 ? 0.31019 0.47858 0.30997 0.02842  -0.01985 0.01355  285 CYS A CA  
4468 C C   . CYS A 285 ? 0.33510 0.49494 0.33021 0.03570  -0.01979 0.02144  285 CYS A C   
4469 O O   . CYS A 285 ? 0.31409 0.47691 0.30807 0.03379  -0.01845 0.02887  285 CYS A O   
4470 C CB  . CYS A 285 ? 0.38800 0.56342 0.38834 0.02076  -0.02043 0.01480  285 CYS A CB  
4471 S SG  . CYS A 285 ? 0.42822 0.59535 0.42455 0.02487  -0.02296 0.01790  285 CYS A SG  
4477 N N   . ILE A 286 ? 0.31573 0.46504 0.30844 0.04376  -0.02104 0.01994  286 ILE A N   
4478 C CA  . ILE A 286 ? 0.29626 0.43628 0.28446 0.05115  -0.02091 0.02657  286 ILE A CA  
4479 C C   . ILE A 286 ? 0.32725 0.46024 0.31179 0.05330  -0.02223 0.02877  286 ILE A C   
4480 O O   . ILE A 286 ? 0.30699 0.43568 0.29098 0.05484  -0.02399 0.02341  286 ILE A O   
4481 C CB  . ILE A 286 ? 0.29178 0.42489 0.27977 0.05860  -0.02135 0.02366  286 ILE A CB  
4482 C CG1 . ILE A 286 ? 0.30947 0.45020 0.30187 0.05658  -0.01996 0.02141  286 ILE A CG1 
4483 C CG2 . ILE A 286 ? 0.29811 0.42105 0.28105 0.06618  -0.02122 0.03043  286 ILE A CG2 
4484 C CD1 . ILE A 286 ? 0.33979 0.47595 0.33403 0.06294  -0.02068 0.01741  286 ILE A CD1 
4496 N N   . ASP A 287 ? 0.31387 0.44579 0.29627 0.05317  -0.02128 0.03686  287 ASP A N   
4497 C CA  . ASP A 287 ? 0.35153 0.47731 0.33109 0.05503  -0.02202 0.03994  287 ASP A CA  
4498 C C   . ASP A 287 ? 0.30629 0.42232 0.28203 0.06194  -0.02075 0.04684  287 ASP A C   
4499 O O   . ASP A 287 ? 0.34085 0.45840 0.31679 0.06049  -0.01912 0.05478  287 ASP A O   
4500 C CB  . ASP A 287 ? 0.38282 0.51762 0.36500 0.04738  -0.02184 0.04354  287 ASP A CB  
4501 C CG  . ASP A 287 ? 0.44101 0.57080 0.42144 0.04879  -0.02278 0.04584  287 ASP A CG  
4502 O OD1 . ASP A 287 ? 0.37507 0.49393 0.35160 0.05551  -0.02343 0.04436  287 ASP A OD1 
4503 O OD2 . ASP A 287 ? 0.43070 0.56792 0.41393 0.04287  -0.02282 0.04938  287 ASP A OD2 
4508 N N   . GLY A 288 ? 0.31304 0.41916 0.28563 0.06905  -0.02146 0.04400  288 GLY A N   
4509 C CA  . GLY A 288 ? 0.32636 0.42299 0.29529 0.07580  -0.02020 0.04983  288 GLY A CA  
4510 C C   . GLY A 288 ? 0.29061 0.39127 0.26096 0.07585  -0.01870 0.05410  288 GLY A C   
4511 O O   . GLY A 288 ? 0.31163 0.41562 0.28386 0.07640  -0.01919 0.04976  288 GLY A O   
4515 N N   . ALA A 289 ? 0.32399 0.42422 0.29376 0.07533  -0.01680 0.06295  289 ALA A N   
4516 C CA  . ALA A 289 ? 0.31216 0.41606 0.28287 0.07493  -0.01529 0.06850  289 ALA A CA  
4517 C C   . ALA A 289 ? 0.34729 0.46463 0.32221 0.06614  -0.01484 0.06865  289 ALA A C   
4518 O O   . ALA A 289 ? 0.37216 0.49374 0.34791 0.06503  -0.01371 0.07228  289 ALA A O   
4519 C CB  . ALA A 289 ? 0.35968 0.45713 0.32836 0.07760  -0.01327 0.07866  289 ALA A CB  
4525 N N   . LEU A 290 ? 0.32560 0.44964 0.30298 0.05973  -0.01566 0.06526  290 LEU A N   
4526 C CA  . LEU A 290 ? 0.32107 0.45808 0.30238 0.05042  -0.01513 0.06589  290 LEU A CA  
4527 C C   . LEU A 290 ? 0.34000 0.48362 0.32369 0.04769  -0.01585 0.05695  290 LEU A C   
4528 O O   . LEU A 290 ? 0.34089 0.48054 0.32434 0.05110  -0.01732 0.04928  290 LEU A O   
4529 C CB  . LEU A 290 ? 0.40847 0.55028 0.39187 0.04443  -0.01580 0.06669  290 LEU A CB  
4530 C CG  . LEU A 290 ? 0.58738 0.72283 0.56970 0.04684  -0.01504 0.07471  290 LEU A CG  
4531 C CD1 . LEU A 290 ? 0.63237 0.77483 0.61808 0.04015  -0.01588 0.07545  290 LEU A CD1 
4532 C CD2 . LEU A 290 ? 0.56040 0.69549 0.54282 0.04695  -0.01277 0.08476  290 LEU A CD2 
4544 N N   . LEU A 291 ? 0.31515 0.46910 0.30152 0.04098  -0.01460 0.05819  291 LEU A N   
4545 C CA  . LEU A 291 ? 0.32637 0.48751 0.31580 0.03745  -0.01461 0.05003  291 LEU A CA  
4546 C C   . LEU A 291 ? 0.31519 0.48936 0.30790 0.02645  -0.01361 0.05045  291 LEU A C   
4547 O O   . LEU A 291 ? 0.33540 0.51404 0.32798 0.02245  -0.01219 0.05834  291 LEU A O   
4548 C CB  . LEU A 291 ? 0.37867 0.53791 0.36771 0.04229  -0.01369 0.05019  291 LEU A CB  
4549 C CG  . LEU A 291 ? 0.33564 0.50275 0.32875 0.03875  -0.01307 0.04257  291 LEU A CG  
4550 C CD1 . LEU A 291 ? 0.33952 0.50426 0.33491 0.04064  -0.01461 0.03287  291 LEU A CD1 
4551 C CD2 . LEU A 291 ? 0.36567 0.53160 0.35844 0.04346  -0.01208 0.04493  291 LEU A CD2 
4563 N N   . THR A 292 ? 0.31789 0.49802 0.31362 0.02135  -0.01432 0.04216  292 THR A N   
4564 C CA  . THR A 292 ? 0.33481 0.52779 0.33395 0.01051  -0.01326 0.04065  292 THR A CA  
4565 C C   . THR A 292 ? 0.34872 0.54565 0.35120 0.00861  -0.01280 0.03046  292 THR A C   
4566 O O   . THR A 292 ? 0.34756 0.53762 0.35029 0.01505  -0.01382 0.02461  292 THR A O   
4567 C CB  . THR A 292 ? 0.37646 0.57417 0.37684 0.00430  -0.01460 0.04130  292 THR A CB  
4568 O OG1 . THR A 292 ? 0.38462 0.57701 0.38498 0.00785  -0.01673 0.03411  292 THR A OG1 
4569 C CG2 . THR A 292 ? 0.44783 0.64264 0.44642 0.00546  -0.01472 0.05164  292 THR A CG2 
4577 N N   . LYS A 293 ? 0.37980 0.58802 0.38529 -0.00075 -0.01107 0.02849  293 LYS A N   
4578 C CA  . LYS A 293 ? 0.36860 0.58138 0.37820 -0.00362 -0.01001 0.01887  293 LYS A CA  
4579 C C   . LYS A 293 ? 0.40408 0.62743 0.41678 -0.01469 -0.00958 0.01470  293 LYS A C   
4580 O O   . LYS A 293 ? 0.39938 0.62905 0.41136 -0.02147 -0.00959 0.02021  293 LYS A O   
4581 C CB  . LYS A 293 ? 0.36539 0.58124 0.37600 -0.00337 -0.00751 0.01953  293 LYS A CB  
4582 C CG  . LYS A 293 ? 0.41097 0.63782 0.42194 -0.01339 -0.00521 0.02368  293 LYS A CG  
4583 C CD  . LYS A 293 ? 0.56894 0.79829 0.58046 -0.01260 -0.00278 0.02453  293 LYS A CD  
4584 C CE  . LYS A 293 ? 0.63617 0.87717 0.64809 -0.02395 -0.00027 0.02763  293 LYS A CE  
4585 N NZ  . LYS A 293 ? 0.81796 1.06288 0.83136 -0.02458 0.00244  0.02593  293 LYS A NZ  
4599 N N   . SER A 294 ? 0.43498 0.66045 0.45168 -0.01678 -0.00916 0.00502  294 SER A N   
4600 C CA  . SER A 294 ? 0.43894 0.67459 0.45893 -0.02758 -0.00843 0.00013  294 SER A CA  
4601 C C   . SER A 294 ? 0.43373 0.67143 0.45891 -0.02925 -0.00666 -0.01004 294 SER A C   
4602 O O   . SER A 294 ? 0.45001 0.68043 0.47660 -0.02151 -0.00690 -0.01364 294 SER A O   
4603 C CB  . SER A 294 ? 0.48805 0.72249 0.50714 -0.02871 -0.01139 -0.00004 294 SER A CB  
4604 O OG  . SER A 294 ? 0.47720 0.70206 0.49629 -0.02094 -0.01340 -0.00513 294 SER A OG  
4610 N N   . SER A 295 ? 0.45649 0.70456 0.48504 -0.03989 -0.00468 -0.01449 295 SER A N   
4611 C CA  . SER A 295 ? 0.48695 0.73737 0.52139 -0.04242 -0.00250 -0.02439 295 SER A CA  
4612 C C   . SER A 295 ? 0.53027 0.77672 0.56691 -0.04145 -0.00466 -0.03101 295 SER A C   
4613 O O   . SER A 295 ? 0.56826 0.81163 0.60963 -0.03903 -0.00381 -0.03824 295 SER A O   
4614 C CB  . SER A 295 ? 0.58516 0.84798 0.62238 -0.05447 0.00107  -0.02682 295 SER A CB  
4615 O OG  . SER A 295 ? 0.67490 0.94450 0.71023 -0.06278 -0.00005 -0.02397 295 SER A OG  
4621 N N   . GLU A 296 ? 0.50055 0.74698 0.53420 -0.04317 -0.00753 -0.02829 296 GLU A N   
4622 C CA  . GLU A 296 ? 0.53752 0.77929 0.57207 -0.04141 -0.01021 -0.03323 296 GLU A CA  
4623 C C   . GLU A 296 ? 0.51827 0.75171 0.54741 -0.03380 -0.01396 -0.02693 296 GLU A C   
4624 O O   . GLU A 296 ? 0.51844 0.75215 0.54377 -0.03256 -0.01437 -0.01869 296 GLU A O   
4625 C CB  . GLU A 296 ? 0.69721 0.94846 0.73414 -0.05226 -0.01010 -0.03726 296 GLU A CB  
4626 C CG  . GLU A 296 ? 0.93509 1.19042 0.97838 -0.05793 -0.00716 -0.04694 296 GLU A CG  
4627 C CD  . GLU A 296 ? 1.08677 1.35115 1.13268 -0.06516 -0.00265 -0.04773 296 GLU A CD  
4628 O OE1 . GLU A 296 ? 1.22279 1.49116 1.26517 -0.06685 -0.00208 -0.04043 296 GLU A OE1 
4629 O OE2 . GLU A 296 ? 1.20332 1.47074 1.25504 -0.06936 0.00048  -0.05553 296 GLU A OE2 
4636 N N   . TYR A 297 ? 0.52415 0.74998 0.55313 -0.02891 -0.01654 -0.03064 297 TYR A N   
4637 C CA  . TYR A 297 ? 0.45237 0.66998 0.47624 -0.02187 -0.01989 -0.02532 297 TYR A CA  
4638 C C   . TYR A 297 ? 0.53799 0.75294 0.56211 -0.02216 -0.02277 -0.02976 297 TYR A C   
4639 O O   . TYR A 297 ? 0.50150 0.71369 0.52891 -0.02173 -0.02264 -0.03692 297 TYR A O   
4640 C CB  . TYR A 297 ? 0.47048 0.67690 0.49185 -0.01117 -0.02021 -0.02307 297 TYR A CB  
4641 C CG  . TYR A 297 ? 0.40474 0.60405 0.42034 -0.00496 -0.02260 -0.01569 297 TYR A CG  
4642 C CD1 . TYR A 297 ? 0.44752 0.63951 0.46068 -0.00081 -0.02563 -0.01670 297 TYR A CD1 
4643 C CD2 . TYR A 297 ? 0.57928 0.77933 0.59209 -0.00370 -0.02163 -0.00753 297 TYR A CD2 
4644 C CE1 . TYR A 297 ? 0.42315 0.60888 0.43141 0.00444  -0.02739 -0.01016 297 TYR A CE1 
4645 C CE2 . TYR A 297 ? 0.54304 0.73665 0.55136 0.00154  -0.02332 -0.00077 297 TYR A CE2 
4646 C CZ  . TYR A 297 ? 0.54692 0.73349 0.55307 0.00556  -0.02608 -0.00228 297 TYR A CZ  
4647 O OH  . TYR A 297 ? 0.49801 0.67828 0.50004 0.01054  -0.02730 0.00438  297 TYR A OH  
4657 N N   . LYS A 298 ? 0.46808 0.68391 0.48915 -0.02284 -0.02536 -0.02518 298 LYS A N   
4658 C CA  . LYS A 298 ? 0.44540 0.65807 0.46575 -0.02206 -0.02864 -0.02808 298 LYS A CA  
4659 C C   . LYS A 298 ? 0.50409 0.71040 0.51943 -0.01583 -0.03123 -0.02109 298 LYS A C   
4660 O O   . LYS A 298 ? 0.49733 0.70779 0.51145 -0.01737 -0.03083 -0.01399 298 LYS A O   
4661 C CB  . LYS A 298 ? 0.48513 0.70919 0.50871 -0.03232 -0.02906 -0.03108 298 LYS A CB  
4662 C CG  . LYS A 298 ? 0.88565 1.10726 0.90905 -0.03208 -0.03253 -0.03491 298 LYS A CG  
4663 C CD  . LYS A 298 ? 0.86625 1.09961 0.89379 -0.04288 -0.03245 -0.03941 298 LYS A CD  
4664 C CE  . LYS A 298 ? 0.91689 1.15146 0.94362 -0.04402 -0.03667 -0.03974 298 LYS A CE  
4665 N NZ  . LYS A 298 ? 1.02378 1.25220 1.04605 -0.03692 -0.03978 -0.03311 298 LYS A NZ  
4679 N N   . GLY A 299 ? 0.47668 0.67274 0.48938 -0.00895 -0.03362 -0.02284 299 GLY A N   
4680 C CA  . GLY A 299 ? 0.46959 0.65872 0.47755 -0.00281 -0.03579 -0.01693 299 GLY A CA  
4681 C C   . GLY A 299 ? 0.41297 0.59160 0.41826 0.00324  -0.03843 -0.02042 299 GLY A C   
4682 O O   . GLY A 299 ? 0.41558 0.59247 0.42308 0.00249  -0.03871 -0.02714 299 GLY A O   
4686 N N   . PRO A 300 ? 0.40695 0.57842 0.40764 0.00899  -0.04031 -0.01571 300 PRO A N   
4687 C CA  . PRO A 300 ? 0.39150 0.55221 0.38863 0.01493  -0.04290 -0.01821 300 PRO A CA  
4688 C C   . PRO A 300 ? 0.39005 0.53987 0.38504 0.02190  -0.04187 -0.01947 300 PRO A C   
4689 O O   . PRO A 300 ? 0.40455 0.54589 0.39511 0.02838  -0.04179 -0.01523 300 PRO A O   
4690 C CB  . PRO A 300 ? 0.48285 0.64143 0.47635 0.01760  -0.04464 -0.01203 300 PRO A CB  
4691 C CG  . PRO A 300 ? 0.42502 0.58793 0.41915 0.01670  -0.04220 -0.00537 300 PRO A CG  
4692 C CD  . PRO A 300 ? 0.48008 0.65361 0.47908 0.00952  -0.04001 -0.00754 300 PRO A CD  
4700 N N   . ILE A 301 ? 0.36313 0.51335 0.36186 0.02029  -0.04101 -0.02552 301 ILE A N   
4701 C CA  . ILE A 301 ? 0.32932 0.47132 0.32791 0.02580  -0.03996 -0.02705 301 ILE A CA  
4702 C C   . ILE A 301 ? 0.35241 0.48319 0.34740 0.03101  -0.04257 -0.02867 301 ILE A C   
4703 O O   . ILE A 301 ? 0.34139 0.47202 0.33656 0.02885  -0.04475 -0.03181 301 ILE A O   
4704 C CB  . ILE A 301 ? 0.36641 0.51439 0.37190 0.02139  -0.03771 -0.03271 301 ILE A CB  
4705 C CG1 . ILE A 301 ? 0.38443 0.54396 0.39283 0.01537  -0.03514 -0.03093 301 ILE A CG1 
4706 C CG2 . ILE A 301 ? 0.38776 0.52853 0.39448 0.02689  -0.03668 -0.03399 301 ILE A CG2 
4707 C CD1 . ILE A 301 ? 0.40069 0.55948 0.40546 0.01869  -0.03402 -0.02348 301 ILE A CD1 
4719 N N   . THR A 302 ? 0.31797 0.43917 0.30950 0.03778  -0.04240 -0.02637 302 THR A N   
4720 C CA  . THR A 302 ? 0.38775 0.49768 0.37544 0.04268  -0.04462 -0.02739 302 THR A CA  
4721 C C   . THR A 302 ? 0.30342 0.40806 0.29408 0.04535  -0.04399 -0.03050 302 THR A C   
4722 O O   . THR A 302 ? 0.32407 0.42144 0.31381 0.04710  -0.04588 -0.03280 302 THR A O   
4723 C CB  . THR A 302 ? 0.42891 0.53081 0.40908 0.04836  -0.04536 -0.02155 302 THR A CB  
4724 O OG1 . THR A 302 ? 0.35688 0.45728 0.33628 0.05173  -0.04311 -0.01787 302 THR A OG1 
4725 C CG2 . THR A 302 ? 0.51701 0.62401 0.49529 0.04592  -0.04611 -0.01815 302 THR A CG2 
4733 N N   . ASP A 303 ? 0.29669 0.40491 0.29118 0.04562  -0.04154 -0.03035 303 ASP A N   
4734 C CA  . ASP A 303 ? 0.31852 0.42259 0.31685 0.04827  -0.04105 -0.03291 303 ASP A CA  
4735 C C   . ASP A 303 ? 0.33638 0.44982 0.34222 0.04485  -0.03823 -0.03518 303 ASP A C   
4736 O O   . ASP A 303 ? 0.32598 0.44519 0.33100 0.04386  -0.03654 -0.03204 303 ASP A O   
4737 C CB  . ASP A 303 ? 0.34565 0.44066 0.33866 0.05526  -0.04135 -0.02859 303 ASP A CB  
4738 C CG  . ASP A 303 ? 0.36478 0.45048 0.34949 0.05867  -0.04357 -0.02565 303 ASP A CG  
4739 O OD1 . ASP A 303 ? 0.36049 0.43954 0.34422 0.05953  -0.04557 -0.02789 303 ASP A OD1 
4740 O OD2 . ASP A 303 ? 0.39158 0.47678 0.37107 0.06021  -0.04317 -0.02090 303 ASP A OD2 
4745 N N   . VAL A 304 ? 0.32180 0.43653 0.33513 0.04313  -0.03760 -0.04023 304 VAL A N   
4746 C CA  . VAL A 304 ? 0.27024 0.39347 0.29154 0.04014  -0.03471 -0.04288 304 VAL A CA  
4747 C C   . VAL A 304 ? 0.26918 0.38856 0.29629 0.04343  -0.03455 -0.04496 304 VAL A C   
4748 O O   . VAL A 304 ? 0.29507 0.40911 0.32455 0.04372  -0.03607 -0.04756 304 VAL A O   
4749 C CB  . VAL A 304 ? 0.28610 0.41829 0.31356 0.03222  -0.03328 -0.04807 304 VAL A CB  
4750 C CG1 . VAL A 304 ? 0.32063 0.46190 0.35582 0.02892  -0.02982 -0.05050 304 VAL A CG1 
4751 C CG2 . VAL A 304 ? 0.33970 0.47607 0.36199 0.02848  -0.03400 -0.04612 304 VAL A CG2 
4761 N N   . PHE A 305 ? 0.27711 0.39997 0.30732 0.04537  -0.03273 -0.04378 305 PHE A N   
4762 C CA  . PHE A 305 ? 0.26214 0.38314 0.29890 0.04851  -0.03253 -0.04528 305 PHE A CA  
4763 C C   . PHE A 305 ? 0.29196 0.42285 0.33965 0.04379  -0.02956 -0.04998 305 PHE A C   
4764 O O   . PHE A 305 ? 0.27591 0.41491 0.32405 0.04027  -0.02727 -0.04993 305 PHE A O   
4765 C CB  . PHE A 305 ? 0.25740 0.37461 0.28951 0.05502  -0.03292 -0.04014 305 PHE A CB  
4766 C CG  . PHE A 305 ? 0.24838 0.35508 0.27053 0.05984  -0.03543 -0.03585 305 PHE A CG  
4767 C CD1 . PHE A 305 ? 0.30333 0.40883 0.31703 0.05964  -0.03569 -0.03214 305 PHE A CD1 
4768 C CD2 . PHE A 305 ? 0.30849 0.40684 0.33021 0.06402  -0.03742 -0.03552 305 PHE A CD2 
4769 C CE1 . PHE A 305 ? 0.35104 0.44709 0.35612 0.06376  -0.03758 -0.02843 305 PHE A CE1 
4770 C CE2 . PHE A 305 ? 0.30866 0.39719 0.32084 0.06794  -0.03940 -0.03177 305 PHE A CE2 
4771 C CZ  . PHE A 305 ? 0.27626 0.36355 0.28020 0.06792  -0.03934 -0.02841 305 PHE A CZ  
4781 N N   . TYR A 306 ? 0.27382 0.40406 0.33060 0.04336  -0.02947 -0.05386 306 TYR A N   
4782 C CA  . TYR A 306 ? 0.27022 0.40920 0.33907 0.03878  -0.02642 -0.05892 306 TYR A CA  
4783 C C   . TYR A 306 ? 0.32488 0.46316 0.40188 0.04269  -0.02649 -0.05922 306 TYR A C   
4784 O O   . TYR A 306 ? 0.28836 0.41866 0.36390 0.04698  -0.02917 -0.05734 306 TYR A O   
4785 C CB  . TYR A 306 ? 0.28492 0.42480 0.35987 0.03289  -0.02586 -0.06418 306 TYR A CB  
4786 C CG  . TYR A 306 ? 0.26669 0.40765 0.33501 0.02857  -0.02617 -0.06456 306 TYR A CG  
4787 C CD1 . TYR A 306 ? 0.28715 0.42003 0.34636 0.03079  -0.02944 -0.06190 306 TYR A CD1 
4788 C CD2 . TYR A 306 ? 0.32396 0.47448 0.39558 0.02192  -0.02318 -0.06771 306 TYR A CD2 
4789 C CE1 . TYR A 306 ? 0.30728 0.44189 0.36120 0.02694  -0.03000 -0.06218 306 TYR A CE1 
4790 C CE2 . TYR A 306 ? 0.37352 0.52590 0.43980 0.01756  -0.02368 -0.06808 306 TYR A CE2 
4791 C CZ  . TYR A 306 ? 0.34970 0.49442 0.40745 0.02015  -0.02719 -0.06532 306 TYR A CZ  
4792 O OH  . TYR A 306 ? 0.34251 0.48996 0.39576 0.01577  -0.02791 -0.06569 306 TYR A OH  
4802 N N   . LYS A 307 ? 0.31244 0.45949 0.39857 0.04076  -0.02355 -0.06172 307 LYS A N   
4803 C CA  . LYS A 307 ? 0.30148 0.44963 0.39789 0.04365  -0.02347 -0.06269 307 LYS A CA  
4804 C C   . LYS A 307 ? 0.32886 0.47650 0.43645 0.03999  -0.02312 -0.06732 307 LYS A C   
4805 O O   . LYS A 307 ? 0.31116 0.46113 0.42158 0.03400  -0.02143 -0.07120 307 LYS A O   
4806 C CB  . LYS A 307 ? 0.38800 0.54617 0.49120 0.04282  -0.02033 -0.06387 307 LYS A CB  
4807 C CG  . LYS A 307 ? 0.53665 0.69453 0.63148 0.04823  -0.02111 -0.05842 307 LYS A CG  
4808 C CD  . LYS A 307 ? 0.92109 1.08938 1.01974 0.04554  -0.01761 -0.05941 307 LYS A CD  
4809 C CE  . LYS A 307 ? 1.03820 1.20618 1.12464 0.04743  -0.01777 -0.05380 307 LYS A CE  
4810 N NZ  . LYS A 307 ? 0.70481 0.87567 0.78550 0.04095  -0.01626 -0.05434 307 LYS A NZ  
4824 N N   . GLU A 308 ? 0.24003 0.38458 0.35433 0.04343  -0.02476 -0.06664 308 GLU A N   
4825 C CA  . GLU A 308 ? 0.22127 0.36545 0.34784 0.04006  -0.02440 -0.07024 308 GLU A CA  
4826 C C   . GLU A 308 ? 0.27969 0.42637 0.41751 0.04326  -0.02483 -0.06971 308 GLU A C   
4827 O O   . GLU A 308 ? 0.24870 0.39525 0.38260 0.04876  -0.02626 -0.06619 308 GLU A O   
4828 C CB  . GLU A 308 ? 0.31246 0.44617 0.43221 0.04019  -0.02755 -0.06873 308 GLU A CB  
4829 C CG  . GLU A 308 ? 0.28678 0.41910 0.41832 0.03600  -0.02720 -0.07192 308 GLU A CG  
4830 C CD  . GLU A 308 ? 0.42189 0.56245 0.56388 0.02907  -0.02292 -0.07771 308 GLU A CD  
4831 O OE1 . GLU A 308 ? 0.33699 0.47644 0.47393 0.02510  -0.02234 -0.07962 308 GLU A OE1 
4832 O OE2 . GLU A 308 ? 0.32783 0.47630 0.48315 0.02756  -0.02007 -0.08037 308 GLU A OE2 
4839 N N   A ASN A 309 ? 0.28312 0.43280 0.43596 0.03946  -0.02338 -0.07330 309 ASN A N   
4840 N N   B ASN A 309 ? 0.28034 0.42955 0.43287 0.03961  -0.02357 -0.07313 309 ASN A N   
4841 C CA  A ASN A 309 ? 0.29366 0.44497 0.45874 0.04186  -0.02443 -0.07252 309 ASN A CA  
4842 C CA  B ASN A 309 ? 0.29251 0.44311 0.45698 0.04209  -0.02472 -0.07224 309 ASN A CA  
4843 C C   A ASN A 309 ? 0.28957 0.43643 0.46346 0.03831  -0.02520 -0.07373 309 ASN A C   
4844 C C   B ASN A 309 ? 0.28977 0.43632 0.46351 0.03830  -0.02529 -0.07367 309 ASN A C   
4845 O O   A ASN A 309 ? 0.28237 0.42104 0.45224 0.04092  -0.02887 -0.07015 309 ASN A O   
4846 O O   B ASN A 309 ? 0.28374 0.42203 0.45362 0.04071  -0.02892 -0.07019 309 ASN A O   
4847 C CB  A ASN A 309 ? 0.32327 0.48331 0.49878 0.04006  -0.02064 -0.07439 309 ASN A CB  
4848 C CB  B ASN A 309 ? 0.31620 0.47582 0.49100 0.04070  -0.02112 -0.07406 309 ASN A CB  
4849 C CG  A ASN A 309 ? 0.47102 0.63789 0.65130 0.03335  -0.01578 -0.07961 309 ASN A CG  
4850 C CG  B ASN A 309 ? 0.42972 0.58304 0.60634 0.04180  -0.02178 -0.06920 309 ASN A CG  
4851 O OD1 A ASN A 309 ? 0.31873 0.48610 0.50540 0.02833  -0.01443 -0.08354 309 ASN A OD1 
4852 O OD1 B ASN A 309 ? 0.50163 0.64934 0.68065 0.04258  -0.02451 -0.06723 309 ASN A OD1 
4853 N ND2 A ASN A 309 ? 0.44463 0.61599 0.62131 0.03293  -0.01306 -0.07929 309 ASN A ND2 
4854 N ND2 B ASN A 309 ? 0.60455 0.75896 0.77977 0.04155  -0.01937 -0.06698 309 ASN A ND2 
4867 N N   . SER A 310 ? 0.25715 0.40903 0.44269 0.03203  -0.02161 -0.07859 310 SER A N   
4868 C CA  . SER A 310 ? 0.22896 0.37669 0.42349 0.02788  -0.02178 -0.07981 310 SER A CA  
4869 C C   . SER A 310 ? 0.33700 0.48656 0.53268 0.02143  -0.01833 -0.08457 310 SER A C   
4870 O O   . SER A 310 ? 0.38280 0.54136 0.58508 0.01809  -0.01409 -0.08873 310 SER A O   
4871 C CB  . SER A 310 ? 0.33659 0.48312 0.54252 0.02549  -0.01990 -0.07823 310 SER A CB  
4872 O OG  . SER A 310 ? 0.45510 0.59684 0.66923 0.02123  -0.01987 -0.07869 310 SER A OG  
4879 N N   . TYR A 311 ? 0.33924 0.48033 0.52821 0.01959  -0.02015 -0.08393 311 TYR A N   
4880 C CA  . TYR A 311 ? 0.43107 0.57301 0.62062 0.01350  -0.01741 -0.08824 311 TYR A CA  
4881 C C   . TYR A 311 ? 0.41735 0.55286 0.61466 0.01013  -0.01815 -0.08842 311 TYR A C   
4882 O O   . TYR A 311 ? 0.31851 0.44500 0.51032 0.01309  -0.02228 -0.08402 311 TYR A O   
4883 C CB  . TYR A 311 ? 0.31402 0.45234 0.48478 0.01448  -0.01903 -0.08720 311 TYR A CB  
4884 C CG  . TYR A 311 ? 0.39580 0.53354 0.56653 0.00839  -0.01729 -0.09105 311 TYR A CG  
4885 C CD1 . TYR A 311 ? 0.43899 0.58575 0.61596 0.00269  -0.01254 -0.09639 311 TYR A CD1 
4886 C CD2 . TYR A 311 ? 0.31273 0.44094 0.47737 0.00810  -0.02033 -0.08940 311 TYR A CD2 
4887 C CE1 . TYR A 311 ? 0.45076 0.59710 0.62805 -0.00324 -0.01092 -0.10014 311 TYR A CE1 
4888 C CE2 . TYR A 311 ? 0.31970 0.44737 0.48458 0.00267  -0.01896 -0.09291 311 TYR A CE2 
4889 C CZ  . TYR A 311 ? 0.42263 0.55948 0.59397 -0.00303 -0.01425 -0.09837 311 TYR A CZ  
4890 O OH  . TYR A 311 ? 0.41947 0.55594 0.59110 -0.00866 -0.01290 -0.10201 311 TYR A OH  
4900 N N   . THR A 312 ? 0.33666 0.47664 0.54682 0.00368  -0.01395 -0.09338 312 THR A N   
4901 C CA  . THR A 312 ? 0.41394 0.54778 0.63152 -0.00032 -0.01410 -0.09380 312 THR A CA  
4902 C C   . THR A 312 ? 0.36523 0.50102 0.58319 -0.00650 -0.01070 -0.09900 312 THR A C   
4903 O O   . THR A 312 ? 0.43229 0.57739 0.65728 -0.01028 -0.00597 -0.10387 312 THR A O   
4904 C CB  . THR A 312 ? 0.48181 0.61577 0.71594 -0.00227 -0.01187 -0.09293 312 THR A CB  
4905 O OG1 . THR A 312 ? 0.49008 0.62246 0.72371 0.00314  -0.01551 -0.08796 312 THR A OG1 
4906 C CG2 . THR A 312 ? 0.52059 0.64628 0.76053 -0.00656 -0.01159 -0.09229 312 THR A CG2 
4914 N N   . THR A 313 ? 0.39398 0.52112 0.60403 -0.00762 -0.01315 -0.09796 313 THR A N   
4915 C CA  . THR A 313 ? 0.41697 0.54546 0.62659 -0.01342 -0.01047 -0.10271 313 THR A CA  
4916 C C   . THR A 313 ? 0.51589 0.64761 0.74456 -0.01975 -0.00518 -0.10685 313 THR A C   
4917 O O   . THR A 313 ? 0.42987 0.55496 0.66529 -0.01906 -0.00480 -0.10324 313 THR A O   
4918 C CB  . THR A 313 ? 0.49395 0.61182 0.69116 -0.01266 -0.01473 -0.10015 313 THR A CB  
4919 O OG1 . THR A 313 ? 0.56016 0.68023 0.75531 -0.01792 -0.01254 -0.10476 313 THR A OG1 
4920 C CG2 . THR A 313 ? 0.51334 0.62278 0.71891 -0.01318 -0.01643 -0.09727 313 THR A CG2 
4928 N N   . THR A 314 ? 0.69057 0.82446 0.91648 -0.02440 -0.00027 -0.11082 314 THR A N   
4929 C CA  . THR A 314 ? 0.76810 0.89639 0.99873 -0.02840 0.00575  -0.11156 314 THR A CA  
4930 C C   . THR A 314 ? 0.90919 1.03123 1.13850 -0.03227 0.00634  -0.11297 314 THR A C   
4931 O O   . THR A 314 ? 0.95035 1.06737 1.18323 -0.03509 0.01114  -0.11340 314 THR A O   
4932 C CB  . THR A 314 ? 0.79867 0.93264 1.02680 -0.03073 0.01116  -0.11477 314 THR A CB  
4933 O OG1 . THR A 314 ? 0.85594 0.99597 1.07574 -0.03320 0.01090  -0.11836 314 THR A OG1 
4934 C CG2 . THR A 314 ? 0.95441 1.09316 1.18351 -0.02682 0.01087  -0.11274 314 THR A CG2 
4942 N N   . ILE A 315 ? 0.68330 0.80572 0.90643 -0.03211 0.00136  -0.11367 315 ILE A N   
4943 C CA  . ILE A 315 ? 0.91111 1.02751 1.13049 -0.03557 0.00128  -0.11490 315 ILE A CA  
4944 C C   . ILE A 315 ? 0.77346 0.88054 0.99535 -0.03378 -0.00361 -0.11092 315 ILE A C   
4945 O O   . ILE A 315 ? 0.65387 0.76121 0.87699 -0.02992 -0.00871 -0.10826 315 ILE A O   
4946 C CB  . ILE A 315 ? 1.02216 1.14458 1.23053 -0.03710 -0.00089 -0.11831 315 ILE A CB  
4947 C CG1 . ILE A 315 ? 0.98087 1.11075 1.18687 -0.04012 0.00493  -0.12165 315 ILE A CG1 
4948 C CG2 . ILE A 315 ? 1.14312 1.25878 1.34556 -0.03932 -0.00306 -0.11865 315 ILE A CG2 
4949 C CD1 . ILE A 315 ? 1.03627 1.17569 1.23342 -0.03958 0.00227  -0.12325 315 ILE A CD1 
4961 N N   . LYS A 316 ? 0.80535 0.90417 1.02832 -0.03631 -0.00183 -0.11000 316 LYS A N   
4962 C CA  . LYS A 316 ? 0.78461 0.87353 1.00893 -0.03511 -0.00620 -0.10570 316 LYS A CA  
4963 C C   . LYS A 316 ? 1.06868 1.15545 1.28235 -0.03443 -0.01301 -0.10662 316 LYS A C   
4964 O O   . LYS A 316 ? 1.00220 1.09427 1.20750 -0.03582 -0.01308 -0.11053 316 LYS A O   
4965 C CB  . LYS A 316 ? 0.69386 0.77498 0.92254 -0.03759 -0.00165 -0.10385 316 LYS A CB  
4968 N N   . PRO A 317 ? 0.92928 1.00610 1.13867 -0.03123 -0.01848 -0.10134 317 PRO A N   
4969 C CA  . PRO A 317 ? 0.92419 0.99457 1.11340 -0.02686 -0.02424 -0.09826 317 PRO A CA  
4970 C C   . PRO A 317 ? 1.25402 1.32443 1.43787 -0.03040 -0.02413 -0.10218 317 PRO A C   
4971 O O   . PRO A 317 ? 0.97242 1.04604 1.14254 -0.02857 -0.02618 -0.10310 317 PRO A O   
4972 C CB  . PRO A 317 ? 0.94956 1.00773 1.13692 -0.02380 -0.02867 -0.09137 317 PRO A CB  
4973 C CG  . PRO A 317 ? 0.92205 0.98244 1.12521 -0.02459 -0.02613 -0.08983 317 PRO A CG  
4974 C CD  . PRO A 317 ? 0.86562 0.93590 1.08558 -0.03067 -0.01938 -0.09648 317 PRO A CD  
4982 N N   . VAL A 318 ? 1.03197 1.09892 1.22671 -0.03557 -0.02187 -0.10428 318 VAL A N   
4983 C CA  . VAL A 318 ? 1.09685 1.16216 1.28348 -0.03780 -0.02127 -0.10608 318 VAL A CA  
4984 C C   . VAL A 318 ? 1.08174 1.15821 1.26452 -0.04022 -0.01739 -0.11110 318 VAL A C   
4985 O O   . VAL A 318 ? 0.98862 1.06647 1.16127 -0.04115 -0.01903 -0.11280 318 VAL A O   
4986 C CB  . VAL A 318 ? 0.83758 0.89539 1.03022 -0.04007 -0.01679 -0.10320 318 VAL A CB  
4989 N N   . THR A 319 ? 1.01338 1.09776 1.20353 -0.04119 -0.01230 -0.11297 319 THR A N   
4990 C CA  . THR A 319 ? 1.06974 1.16426 1.25590 -0.04369 -0.00850 -0.11715 319 THR A CA  
4991 C C   . THR A 319 ? 1.13094 1.23224 1.30732 -0.04153 -0.01392 -0.11860 319 THR A C   
4992 O O   . THR A 319 ? 1.08899 1.19595 1.25685 -0.04350 -0.01339 -0.12077 319 THR A O   
4993 C CB  . THR A 319 ? 0.84965 0.94944 1.04557 -0.04489 -0.00166 -0.11832 319 THR A CB  
4996 N N   . HIS A 320 ? 1.09129 1.18922 1.26360 -0.03554 -0.01816 -0.11410 320 HIS A N   
4997 C CA  . HIS A 320 ? 1.01305 1.11219 1.16868 -0.03008 -0.02229 -0.11072 320 HIS A CA  
4998 C C   . HIS A 320 ? 1.06467 1.15822 1.20730 -0.02890 -0.02716 -0.10915 320 HIS A C   
4999 O O   . HIS A 320 ? 1.05871 1.15733 1.19112 -0.02878 -0.02861 -0.10979 320 HIS A O   
5000 C CB  . HIS A 320 ? 0.99536 1.08877 1.14671 -0.02300 -0.02549 -0.10455 320 HIS A CB  
5001 C CG  . HIS A 320 ? 1.05921 1.15875 1.22150 -0.02300 -0.02166 -0.10538 320 HIS A CG  
5002 N ND1 . HIS A 320 ? 0.87407 0.98309 1.03423 -0.02249 -0.01954 -0.10686 320 HIS A ND1 
5003 C CD2 . HIS A 320 ? 0.94121 1.03906 1.11748 -0.02373 -0.01959 -0.10486 320 HIS A CD2 
5004 C CE1 . HIS A 320 ? 0.71349 0.82619 0.88569 -0.02247 -0.01643 -0.10732 320 HIS A CE1 
5005 N NE2 . HIS A 320 ? 0.91460 1.02095 1.09711 -0.02331 -0.01642 -0.10618 320 HIS A NE2 
5013 N N   . HIS A 321 ? 1.12273 1.20584 1.26572 -0.02810 -0.02993 -0.10677 321 HIS A N   
5014 C CA  . HIS A 321 ? 1.14043 1.21749 1.27072 -0.02611 -0.03512 -0.10465 321 HIS A CA  
5015 C C   . HIS A 321 ? 1.19467 1.27915 1.32369 -0.03157 -0.03382 -0.11000 321 HIS A C   
5016 O O   . HIS A 321 ? 1.19583 1.28155 1.31246 -0.02977 -0.03761 -0.10891 321 HIS A O   
5017 C CB  . HIS A 321 ? 1.14679 1.21156 1.27992 -0.02533 -0.03756 -0.10149 321 HIS A CB  
5018 C CG  . HIS A 321 ? 1.15432 1.21089 1.27268 -0.02102 -0.04389 -0.09733 321 HIS A CG  
5019 N ND1 . HIS A 321 ? 1.12758 1.18368 1.23151 -0.01521 -0.04790 -0.09350 321 HIS A ND1 
5020 C CD2 . HIS A 321 ? 1.08001 1.12857 1.19606 -0.02163 -0.04683 -0.09633 321 HIS A CD2 
5021 C CE1 . HIS A 321 ? 1.01903 1.06752 1.11259 -0.01246 -0.05296 -0.09047 321 HIS A CE1 
5022 N NE2 . HIS A 321 ? 1.03657 1.08032 1.13689 -0.01612 -0.05261 -0.09202 321 HIS A NE2 
5030 N N   . HIS A 322 ? 1.26697 1.35682 1.40916 -0.03857 -0.02838 -0.11582 322 HIS A N   
5031 C CA  . HIS A 322 ? 1.37117 1.46465 1.50880 -0.04259 -0.02526 -0.11735 322 HIS A CA  
5032 C C   . HIS A 322 ? 1.36512 1.47056 1.50125 -0.04543 -0.02125 -0.12002 322 HIS A C   
5033 O O   . HIS A 322 ? 1.33709 1.44610 1.46751 -0.04846 -0.01936 -0.12057 322 HIS A O   
5034 C CB  . HIS A 322 ? 1.46602 1.55402 1.61197 -0.04600 -0.01968 -0.11716 322 HIS A CB  
5035 C CG  . HIS A 322 ? 1.48174 1.55771 1.63003 -0.04381 -0.02284 -0.11374 322 HIS A CG  
5036 N ND1 . HIS A 322 ? 1.54922 1.61885 1.69070 -0.03930 -0.03054 -0.11119 322 HIS A ND1 
5037 C CD2 . HIS A 322 ? 1.43842 1.50723 1.59450 -0.04534 -0.01935 -0.11196 322 HIS A CD2 
5038 C CE1 . HIS A 322 ? 1.42174 1.48055 1.56685 -0.03852 -0.03165 -0.10788 322 HIS A CE1 
5039 N NE2 . HIS A 322 ? 1.36885 1.42725 1.52300 -0.04219 -0.02486 -0.10809 322 HIS A NE2 
5047 N N   . HIS A 323 ? 1.21305 1.32464 1.35406 -0.04449 -0.02005 -0.12125 323 HIS A N   
5048 C CA  . HIS A 323 ? 1.33754 1.46002 1.47821 -0.04740 -0.01559 -0.12343 323 HIS A CA  
5049 C C   . HIS A 323 ? 1.19695 1.32470 1.33469 -0.04327 -0.01897 -0.12238 323 HIS A C   
5050 O O   . HIS A 323 ? 1.10948 1.23920 1.25422 -0.04190 -0.01606 -0.12204 323 HIS A O   
5051 C CB  . HIS A 323 ? 1.37970 1.50334 1.53136 -0.05104 -0.00748 -0.12543 323 HIS A CB  
5052 C CG  . HIS A 323 ? 1.53246 1.64870 1.68736 -0.05345 -0.00432 -0.12527 323 HIS A CG  
5053 N ND1 . HIS A 323 ? 1.40693 1.52432 1.55619 -0.05699 -0.00203 -0.12608 323 HIS A ND1 
5054 C CD2 . HIS A 323 ? 1.47689 1.58449 1.63992 -0.05265 -0.00328 -0.12386 323 HIS A CD2 
5055 C CE1 . HIS A 323 ? 1.42098 1.53095 1.57467 -0.05804 0.00026  -0.12554 323 HIS A CE1 
5056 N NE2 . HIS A 323 ? 1.55122 1.65509 1.71319 -0.05550 -0.00037 -0.12403 323 HIS A NE2 
5064 N N   . HIS A 324 ? 1.22743 1.35417 1.35094 -0.03919 -0.02398 -0.11844 324 HIS A N   
5065 C CA  . HIS A 324 ? 1.12533 1.25292 1.24031 -0.03309 -0.02601 -0.11353 324 HIS A CA  
5066 C C   . HIS A 324 ? 0.92458 1.05949 1.02883 -0.03414 -0.02789 -0.11279 324 HIS A C   
5067 O O   . HIS A 324 ? 0.82159 0.96367 0.92349 -0.03392 -0.02633 -0.11181 324 HIS A O   
5068 C CB  . HIS A 324 ? 0.86555 0.98120 0.97410 -0.02520 -0.03086 -0.10749 324 HIS A CB  
5069 C CG  . HIS A 324 ? 1.05447 1.16368 1.15297 -0.02320 -0.03613 -0.10518 324 HIS A CG  
5070 N ND1 . HIS A 324 ? 1.15544 1.25471 1.25588 -0.02245 -0.03829 -0.10439 324 HIS A ND1 
5071 C CD2 . HIS A 324 ? 1.07498 1.18639 1.16180 -0.02174 -0.03975 -0.10318 324 HIS A CD2 
5072 C CE1 . HIS A 324 ? 1.24441 1.33998 1.33428 -0.02040 -0.04309 -0.10222 324 HIS A CE1 
5073 N NE2 . HIS A 324 ? 1.32532 1.42840 1.40716 -0.01994 -0.04405 -0.10155 324 HIS A NE2 
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